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        <title>European Journal of Cell Biology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'European Journal of Cell Biology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=European+Journal+of+Cell+Biology&t=European+Journal+of+Cell+Biology&s=Search&f=source]]></link>
        <lastBuildDate>Tue, 07 Feb 2012 08:48:57 +0100</lastBuildDate>
        <item>
            <title>δ-Aminolevulinate synthase is required for apical transcellular barrier formation in the skin of the Drosophila larva.</title>
            <link>http://www.medworm.com/index.php?rid=5659165&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22293958%26dopt%3DAbstract</link>
            <description>Authors: Shaik KS, Meyer F, Vázquez AV, Flötenmeyer M, Cerdán ME, Moussian B
    Abstract
    Animals construct a layered skin to prevent dehydration and pathogen entrance. The barrier function of the skin relies on the extensive cross-linking of specialised components. In insects, for instance, epidermal cells produce an apical extracellular cuticle that consists of a network of proteins, chitin and lipids. We have identified mutations in the Drosophila gene coding for the δ-aminolevulinate synthase (Alas) that cause massive water loss. The cuticle of alas mutant larvae detaches from the epidermis and its basal region is frayed suggesting that an Alas dependent pathway is needed to organise the contact between the cuticle and the epidermis and anchor the cuticle to the apical surface ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659165</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659165</guid>        </item>
        <item>
            <title>Protoporphyrin IX-dependent photodynamic production of endogenous ROS stimulates cell proliferation.</title>
            <link>http://www.medworm.com/index.php?rid=5659164&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22293959%26dopt%3DAbstract</link>
            <description>Authors: Blázquez-Castro A, Carrasco E, Calvo MI, Jaén P, Stockert JC, Juarranz A, Sánz-Rodríguez F, Espada J
    Abstract
    Photodynamic therapy using methyl 5-aminolevulinate (MAL) as a precursor of the photosensitizing agent protoporphyrin IX is widely used in clinical practice for the treatment of different pathologies, including cancer. In this therapeutic modality, MAL treatment promotes the forced accumulation of the endogenous photoactive compound protoporphyrin IX in target malignant cells. Subsequent irradiation of treated tissues with an appropriate visible light source induces the production of reactive oxygen species (ROS) that, once accumulated above a critical level, promote cell death. Here we demonstrate that a photodynamic treatment with low MAL concentrations can b...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659164</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659164</guid>        </item>
        <item>
            <title>Models and mechanisms of acute lung injury caused by direct insults.</title>
            <link>http://www.medworm.com/index.php?rid=5659167&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22284832%26dopt%3DAbstract</link>
            <description>Authors: Reiss LK, Uhlig U, Uhlig S
    Abstract
    Acute lung injury (ALI) and its more severe form acute respiratory distress syndrome (ARDS) are life-threatening diseases that are characterized by acute onset, pulmonary inflammation, oedema due to increased vascular permeability and severe hypoxemia. Clinically, ARDS can be divided into ARDS due to direct causes such as pneumonia, aspiration or injurious ventilation, and due to extrapulmonary indirect causes such as sepsis, severe burns or pancreatitis. In order to identify potential therapeutic targets, we asked here whether common molecular mechanisms can be identified that are relevant in different models of the direct form of ALI/ARDS. To this end, we reviewed three widely used models: (a) one based on a biological insult, i.e. ins...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659167</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659167</guid>        </item>
        <item>
            <title>Formation of atypical podosomes in extravillous trophoblasts regulates extracellular matrix degradation.</title>
            <link>http://www.medworm.com/index.php?rid=5659166&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22284833%26dopt%3DAbstract</link>
            <description>In this study these structures have been identified and characterised in extravillous trophoblasts. The role of specialised invasive structures in trophoblasts in the degradation of the extracellular matrix was compared with well characterised podosomes and invadopodia in other invasive cells and the trophoblast specific structures were characterised by using a sensitive matrix degradation assay which enabled visualisation of the structures and their dynamics. We show trophoblasts form actin rich protrusive structures which have the ability to degrade the extracellular matrix during invasion. The degradation ability and dynamics of the structures closely resemble podosomes, but have unique characteristics that have not previously been described in other cell types. The composition of these...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659166</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659166</guid>        </item>
        <item>
            <title>Human DHHC proteins: A spotlight on the hidden player of palmitoylation.</title>
            <link>http://www.medworm.com/index.php?rid=5535484&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178113%26dopt%3DAbstract</link>
            <description>Authors: Korycka J, Lach A, Heger E, Bogusławska DM, Wolny M, Toporkiewicz M, Augoff K, Korzeniewski J, Sikorski AF
    Abstract
    Palmitoylation is one of the most common posttranslational lipid modifications of proteins and we now know quite a lot about it. However, the state of knowledge about the enzymes that catalyze this process is clearly insufficient. This review is focused on 23 human DHHC genes and their products - protein palmitoyltransferases. Here we describe mainly the structure and function of these proteins, but also, to a lesser degree, what the substrates of the enzymes are and whether they are related to various diseases. The main aim of this review was to catalogue existing information concerning the human DHHC family of genes/proteins, making them and their function...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535484</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535484</guid>        </item>
        <item>
            <title>Cyclic stretch induces reorientation of cells in a Src family kinase- and p130Cas-dependent manner.</title>
            <link>http://www.medworm.com/index.php?rid=5535483&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178114%26dopt%3DAbstract</link>
            <description>Authors: Niediek V, Born S, Hampe N, Kirchgeßner N, Merkel R, Hoffmann B
    Abstract
    Recognition of external mechanical signals by cells is an essential process for life. One important mechanical signal experienced by various cell types, e.g. around blood vessels, within the lung epithelia or around the intestine, is cyclic stretch. As a response, many cell types reorient their actin cytoskeleton and main cell axis almost perpendicular to the direction of stretch. Despite the vital necessity of cellular adaptation to cyclic stretch, the underlying mechanosensory signal cascades are far from being understood. Here we show an important function of Src-family kinase activity in cellular reorientation upon cyclic stretch. Deletion of all three family members, namely c-Src, Yes and Fyn (S...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535483</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535483</guid>        </item>
        <item>
            <title>Inflammatory response in human skeletal muscle cells: CXCL10 as a potential therapeutic target.</title>
            <link>http://www.medworm.com/index.php?rid=5535485&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22176919%26dopt%3DAbstract</link>
            <description>In conclusion, we sustain that pharmacological targeting of CXCL10 within muscular cells might contribute to keep in control pro-Th1 polarization of the immune/inflammatory response.
    PMID: 22176919 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535485</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535485</guid>        </item>
        <item>
            <title>Highly effective removal of floxed Blasticidin S resistance cassettes from Dictyostelium discoideum mutants by extrachromosomal expression of Cre.</title>
            <link>http://www.medworm.com/index.php?rid=5513833&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22154549%26dopt%3DAbstract</link>
            <description>Authors: Linkner J, Nordholz B, Junemann A, Winterhoff M, Faix J
    Abstract
    The inactivation of proteins in cells is inevitable to study their physiological role in various cellular processes. In contrast to strategies to alter the amount of active proteins in cells, only a gene knockout guarantees complete removal of the protein of interest. For Dictyostelium discoideum cells, the gene replacement construct typically consists of a Blasticidin S resistance (Bsr) cassette flanked by fragments of the target gene to allow insertion by homologous recombination. More advanced knockout constructs additionally carry loxP sites on both sides of the Bsr cassettes for subsequent removal of the selection marker by transient expression of Cre recombinase, thus allowing generation of multiple kno...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513833</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513833</guid>        </item>
        <item>
            <title>Skeletal muscle-specific variant of nascent polypeptide associated complex alpha (skNAC): Implications for a specific role in mammalian myoblast differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=5513832&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22154550%26dopt%3DAbstract</link>
            <description>Authors: Berger F, Berkholz J, Breustedt T, Ploen D, Munz B
    Abstract
    NAC (nascent polypeptide associated complex) is a heterodimer consisting of an α and a β subunit. skNAC (skeletal and heart muscle-specific form of αNAC) is a variant of αNAC, which is induced in muscle differentiation and regeneration. We show here that skNAC expression is regulated by p38 MAPK, which plays a crucial role in myogenesis. Furthermore, inhibition of skNAC expression in myoblasts via specific siRNAs might lead to disturbed incorporation of myosin heavy chain (MyHC) into sarcomeres, however, it has no inhibitory effect on absolute MyHC protein levels. Taken together, our data suggest that skNAC regulates specific aspects of myogenesis.
    PMID: 22154550 [PubMed - as supplied by publisher] (Source...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513832</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513832</guid>        </item>
        <item>
            <title>Leupeptin enhances cell surface localization of fibroblast growth factor receptor 1 in adult sensory neurons by increased recycling.</title>
            <link>http://www.medworm.com/index.php?rid=5513831&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22169219%26dopt%3DAbstract</link>
            <description>Authors: Hausott B, Vallant N, Hochfilzer M, Mangger S, Irschick R, Haugsten EM, Klimaschewski L
    Abstract
    Fibroblast growth factors (FGFs) act as trophic factors during development and regeneration of the nervous system. FGFs mediate their responses by activation of four types of FGF receptors (FGFR1-4). FGFR1 is expressed in adult sensory neurons of dorsal root ganglia (DRG), and overexpression of FGFR1 enhances FGF-2-induced elongative axon growth in vitro. Ligand-induced activation of FGFR1 is followed by endocytosis and rapid lysosomal degradation. We previously reported that the lysosomal inhibitor leupeptin prevents degradation of FGFR1 and promotes FGF-2-induced elongative axon growth of DRG neurons overexpressing FGFR1. Therefore, we analyzed the effects of leupeptin on int...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513831</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513831</guid>        </item>
        <item>
            <title>The role of TNF and Fas dependent signaling in animal models of inflammatory liver injury and liver cancer.</title>
            <link>http://www.medworm.com/index.php?rid=5513834&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22153863%26dopt%3DAbstract</link>
            <description>In conclusion, our work demonstrates that therapeutic intervention in the TNF-NF-κB-caspase-8 network is technically feasible and could be of potential benefit in inflammatory liver disease.
    PMID: 22153863 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513834</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513834</guid>        </item>
        <item>
            <title>Interleukin-6 signalling: More than Jaks and STATs.</title>
            <link>http://www.medworm.com/index.php?rid=5513836&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138086%26dopt%3DAbstract</link>
            <description>Authors: Eulenfeld R, Dittrich A, Khouri C, Müller PJ, Mütze B, Wolf A, Schaper F
    Abstract
    The hallmark of signalling by many cytokines is the activation of the Janus kinase (Jak)/signal transducer and activator of transcription (STAT) pathway. However, cytokines additionally activate other pathways. In past years we realised that these pathways significantly contribute to the physiological functions of IL-6 and pathophysiological functions in the context of many inflammatory and proliferative diseases. Whereas other articles in this issue of the European Journal of Cell Biology focus on STAT activation and its regulation we here aim to summarise our knowledge and some remaining questions on interleukin-6 (IL-6)-induced STAT-independent pathways as well as the cross-talk with the...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513836</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513836</guid>        </item>
        <item>
            <title>The role of ADAM-mediated shedding in vascular biology.</title>
            <link>http://www.medworm.com/index.php?rid=5513835&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22138087%26dopt%3DAbstract</link>
            <description>Authors: Dreymueller D, Pruessmeyer J, Groth E, Ludwig A
    Abstract
    Within the vasculature the disintegrins and metalloproteinases (ADAMs) 8, 9, 10, 12, 15, 17, 19, 28 and 33 are expressed on endothelial cells, smooth muscle cells and on leukocytes. As surface-expressed proteases they mediate cleavage of vascular surface molecules at an extracellular site close to the membrane. This process is termed shedding and leads to the release of a soluble substrate ectodomain thereby critically modulating the biological function of the substrate. In the vasculature several surface molecules undergo ADAM-mediated shedding including tumour necrosis factor (TNF) α, interleukin (IL) 6 receptor α, L-selectin, vascular endothelial (VE)-cadherin, the transmembrane CX3C-chemokine ligand (CX3CL) 1, ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513835</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513835</guid>        </item>
        <item>
            <title>Conditioned medium from hypoxia-treated adipocytes renders muscle cells insulin resistant.</title>
            <link>http://www.medworm.com/index.php?rid=5380236&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21962636%26dopt%3DAbstract</link>
            <description>Authors: Yu J, Shi L, Wang H, Bilan PJ, Yao Z, Samaan MC, He Q, Klip A, Niu W
    Abstract
    Adipose tissue hypoxia is an early phenotype in obesity, associated with macrophage infiltration and local inflammation. Here we test the hypothesis that adipocytes in culture respond to a hypoxic environment with the release of pro-inflammatory factors that stimulate macrophage migration and cause muscle insulin resistance. 3T3-L1 adipocytes cultured in a 1% O(2) atmosphere responded with a classic hypoxia response by elevating protein expression of HIF-1α. This was associated with elevated mRNA expression and peptide release of cytokines TNFα, IL-6 and the chemokine monocyte chemoattractant protein-1 (MCP-1). The mRNA and protein expression of the anti-inflammatory adipokine adiponectin was r...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380236</comments>
            <pubDate>Mon, 07 Nov 2011 00:05:34 +0100</pubDate>
            <guid isPermaLink="false">5380236</guid>        </item>
        <item>
            <title>Pros and cons of fish skin cells in culture: Long-term full skin and short-term scale cell culture from rainbow trout, Oncorhynchus mykiss.</title>
            <link>http://www.medworm.com/index.php?rid=5380233&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22000680%26dopt%3DAbstract</link>
            <description>Authors: Rakers S, Klinger M, Kruse C, Gebert M
    Abstract
    Here, we report the establishment of a permanent skin cell culture from rainbow trout (Oncorhynchus mykiss). The cells of the fish skin cell culture could be propagated over 60 passages so far. Furthermore, we show for the first time that it is possible to integrate freshly harvested rainbow trout scales into this new fish skin cell culture. We further demonstrated that epithelial cells derived from the scales survived in the artificial micro-environment of surrounding fibroblast-like cells. Also, antibody staining indicated that both cell types proliferated and started to build connections with the other cell type. It seems that it is possible to generate an 'artificial skin' with two different cell types. This could lead to...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380233</comments>
            <pubDate>Mon, 07 Nov 2011 00:04:15 +0100</pubDate>
            <guid isPermaLink="false">5380233</guid>        </item>
        <item>
            <title>Yeast Rsp5 ubiquitin ligase affects the actin cytoskeleton in vivo and in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=5380232&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22000681%26dopt%3DAbstract</link>
            <description>Authors: Kaminska J, Spiess M, Stawiecka-Mirota M, Monkaityte R, Haguenauer-Tsapis R, Urban-Grimal D, Winsor B, Zoladek T
    Abstract
    Yeast Rsp5 ubiquitin ligase is involved in several cellular processes, including endocytosis. Actin patches are sites of endocytosis, a process involving actin assembly and disassembly. Here we show Rsp5 localization in cortical patches and demonstrate its involvement in actin cytoskeleton organization and dynamics. We found that the Rsp5-F1-GFP(2) N-terminal fragment and full length GFP-Rsp5 were recruited to peripheral patches that temporarily co-localized with Abp1-mCherry, a marker of actin patches. Actin cytoskeleton organization was defective in a strain lacking RSP5 or overexpressing RSP5, and this phenotype was accompanied by morphological abnor...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380232</comments>
            <pubDate>Mon, 07 Nov 2011 00:03:48 +0100</pubDate>
            <guid isPermaLink="false">5380232</guid>        </item>
        <item>
            <title>A peptide derived from the CD loop-D helix region of ciliary neurotrophic factor (CNTF) induces neuronal differentiation and survival by binding to the leukemia inhibitory factor (LIF) receptor and common cytokine receptor chain gp130.</title>
            <link>http://www.medworm.com/index.php?rid=5380231&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22000729%26dopt%3DAbstract</link>
            <description>Authors: Rathje M, Pankratova S, Nielsen J, Gotfryd K, Bock E, Berezin V
    Abstract
    Ciliary neurotrophic factor (CNTF) induces neuronal differentiation and promotes the survival of various neuronal cell types by binding to a receptor complex formed by CNTF receptor α (CNTFRα), gp130, and the leukemia inhibitory factor (LIF) receptor (LIFR). The CD loop-D helix region of CNTF has been suggested to be important for the cytokine interaction with LIFR. We designed a peptide, termed cintrofin, that encompasses this region. Surface plasmon resonance analysis demonstrated that cintrofin bound to LIFR and gp130, but not to CNTFRα, with apparent K(D) values of 35nM and 1.1nM, respectively. Cintrofin promoted the survival of cerebellar granule neurons (CGNs), in which cell death was induced...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380231</comments>
            <pubDate>Mon, 07 Nov 2011 00:03:22 +0100</pubDate>
            <guid isPermaLink="false">5380231</guid>        </item>
        <item>
            <title>Expression of keratinocyte biomarkers is governed by environmental biomechanics.</title>
            <link>http://www.medworm.com/index.php?rid=5380230&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22000730%26dopt%3DAbstract</link>
            <description>Authors: Eberwein P, Steinberg T, Schulz S, Zimmermann D, Accardi R, Beck D, Reinhard T, Tomakidi P
    Abstract
    In solid body tissues, environmental biomechanics is indispensable for tissue homeostasis. While characteristics of homeostasis include morphogenesis, proliferation and differentiation, the influences through biomechanics in corneal keratinocytes are poorly understood. Here we show for the first time that corneal keratinocytes, established in a defined biomechanical microenvironment of micropatterned soft pillars, exhibit favoritism of late and terminal differentiation at large pillar patterns of 11μm with matched small 5μm arrays. At 11μm, epithelial cells expressed decreased levels of early differentiation marker cytokeratin 19 (KRT19), which was antagonized by an incre...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380230</comments>
            <pubDate>Mon, 07 Nov 2011 00:02:54 +0100</pubDate>
            <guid isPermaLink="false">5380230</guid>        </item>
        <item>
            <title>Solid-state magic-angle spinning NMR of membrane proteins and protein-ligand interactions.</title>
            <link>http://www.medworm.com/index.php?rid=5380225&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22019511%26dopt%3DAbstract</link>
            <description>We describe the development of the methodology by looking at examples in detail and provide an outlook towards future 'big' projects.
    PMID: 22019511 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380225</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380225</guid>        </item>
        <item>
            <title>Deletion of gp130 in myeloid cells modulates IL-6-release and is associated with more severe liver injury of Con A hepatitis.</title>
            <link>http://www.medworm.com/index.php?rid=5380228&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22018663%26dopt%3DAbstract</link>
            <description>Authors: Lutz HH, Sackett SD, Kroy DC, Gassler N, Trautwein C
    Abstract
    IL-6/gp130 dependent signaling plays an important role in modulating inflammation in acute and chronic diseases. The course of Concanavalin A- (Con A) induced hepatitis can be modulated by different immune-mediated mechanisms. IL-6/gp130-dependent signaling has been shown to be protective in hepatocytes. However, the role of this pathway in myeloid cells has not yet been studied. In our present study we used macrophage/neutrophil-specific gp130 knockout (gp130(ΔLys), KO) animals and analyzed its relevance in modulating Con A-induced hepatitis. Additionally, we performed in vitro studies with gp130(ΔLys)-macrophages. We demonstrate that gp130(ΔLys) animals are more susceptible to Con A-induced hepatitis. This ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380228</comments>
            <pubDate>Thu, 20 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380228</guid>        </item>
        <item>
            <title>Dynamics and non-canonical aspects of JAK/STAT signalling.</title>
            <link>http://www.medworm.com/index.php?rid=5380227&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22018664%26dopt%3DAbstract</link>
            <description>Authors: Mohr A, Chatain N, Domoszlai T, Rinis N, Sommerauer M, Vogt M, Müller-Newen G
    Abstract
    The Janus kinase/signal transducer and activator of transcription (JAK/STAT) pathway directly links ligand-binding to a membrane-bound receptor with the activation of a transcription factor. This signalling module enables the cell to rapidly initiate a transcriptional response to external stimulation. The main components of this evolutionary conserved module are cytokines that specifically bind to cytokine receptors leading to the activation of receptor-associated Janus tyrosine kinases (JAKs). The receptor-bound JAKs activate STAT transcription factors through phosphorylation of a single tyrosine residue. Activated STAT dimers translocate into the nucleus to induce target gene expressi...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380227</comments>
            <pubDate>Thu, 20 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380227</guid>        </item>
        <item>
            <title>Calculating kinetics and pathways of protein-ligand association.</title>
            <link>http://www.medworm.com/index.php?rid=5380226&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22018914%26dopt%3DAbstract</link>
            <description>Authors: Held M, Noé F
    Abstract
    While studies of protein-ligand association have mostly focused on the native complex and its stability (binding affinity), relatively little attention has been paid to the association process that precedes the formation of the complex. Here we review approaches to study the kinetics of association and association mechanisms, i.e. the probability distribution of association pathways. Selected methods are described that allow these properties to be calculated quantitatively from simulation models. We summarize some applications of these methods and finally propose a model mechanism by which proteins may efficiently screen potential ligands for those that can be natively bound.
    PMID: 22018914 [PubMed - as supplied by publisher] (Source: European J...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380226</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380226</guid>        </item>
        <item>
            <title>Role for CD74 and CXCR4 in clathrin-dependent endocytosis of the cytokine MIF.</title>
            <link>http://www.medworm.com/index.php?rid=5380229&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22014447%26dopt%3DAbstract</link>
            <description>Authors: Schwartz V, Krüttgen A, Weis J, Weber C, Ostendorf T, Lue H, Bernhagen J
    Abstract
    Macrophage migration inhibitory factor (MIF) is a pleiotropic cytokine that plays a role in innate and adaptive immunity. Depending on the cellular context and disease state, MIF signaling is mediated by its receptors CXCR2, CXCR4 and/or CD74. Although it is known that MIF is endocytosed, the exact mechanism has remained unknown. In exploring the mechanism of MIF endocytosis with biologically active Alexa(546)MIF, pathway-specific inhibitors (monodansylcadaverine, MDC; chlorpromazine, CPZ; dynasore; dominant-negative dynamin, bafilomycin, nocodazole) and receptor overexpression and blockade approaches, we identified a clathrin/dynamin-dependent endocytosis pathway as the main track for MIF i...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380229</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380229</guid>        </item>
        <item>
            <title>Signaling by IL-31 and functional consequences.</title>
            <link>http://www.medworm.com/index.php?rid=5380234&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21982586%26dopt%3DAbstract</link>
            <description>We describe the current state of knowledge of the involvement of IL-31 in diseases, both in humans and in mouse models. From these studies it is becoming clear that IL-31 plays an important role in the proper functioning of the skin and of airway and intestinal epithelia. The findings available suggest that IL-31 might be an interesting target for directed drug therapy.
    PMID: 21982586 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380234</comments>
            <pubDate>Wed, 05 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380234</guid>        </item>
        <item>
            <title>Cold shock Y-box protein-1 participates in signaling circuits with auto-regulatory activities.</title>
            <link>http://www.medworm.com/index.php?rid=5380235&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21962637%26dopt%3DAbstract</link>
            <description>Authors: Brandt S, Raffetseder U, Djudjaj S, Schreiter A, Kadereit B, Michele M, Pabst M, Zhu C, Mertens PR
    Abstract
    The cold shock protein Y-box (YB) binding-1 is an example of a highly regulated protein with pleiotropic functions. Besides activities as a transcription factor in the nucleus or regulator of translation in the cytoplasm, recent findings indicate extracellular effects and secretion via a non-classical secretion pathway. This review summarizes regulatory pathways in which YB-1 participates, all iterating auto-regulatory loops. Schematics are developed that elucidate the cold shock protein activities in (i) fine-tuning its own expression level following platelet-derived growth factor-B-, thrombin- or interferon-γ-dependent signaling, (ii) as a component of the messeng...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5380235</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5380235</guid>        </item>
        <item>
            <title>Receptor fusion proteins for the inhibition of cytokines.</title>
            <link>http://www.medworm.com/index.php?rid=5281450&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21958554%26dopt%3DAbstract</link>
            <description>Authors: Schwache D, Müller-Newen G
    Abstract
    Cells are exposed to a large variety of cytokines that signal through corresponding cytokine receptors. In healthy tissues or tissues that respond properly to disturbed homeostasis, the cross-talk of a few conserved core signaling pathways downstream of the cytokine receptors is translated into an adequate cellular response. In chronic inflammatory diseases but also in cancer associated inflammation cytokine expression and the downstream signaling networks are dysregulated. Targeted therapies are aimed at the specific interference with dysregulated cytokine signaling. In this article some concepts of pharmacological intervention with cytokine signaling will be reviewed including biologics that target cytokines and cytokine receptors. Re...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281450</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281450</guid>        </item>
        <item>
            <title>Centriolar satellites: Busy orbits around the centrosome.</title>
            <link>http://www.medworm.com/index.php?rid=5281451&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21945726%26dopt%3DAbstract</link>
            <description>Authors: Bärenz F, Mayilo D, Gruss OJ
    Abstract
    Since its first description by Theodor Boveri in 1888, the centrosome has been studied intensely, and it revealed detailed information about its structure, molecular composition and its various functions. The centrosome consists of two centrioles, which generally appear in electron microscopy as barrel-shaped structures usually composed of nine microtubule triplets. An amorphous mass of pericentriolar material surrounds the centrioles and accumulates many proteins important for the integrity and function of centrosomes, such as the γ-tubulin ring complex (γ-TuRC) that mediates microtubule nucleation and capping. In animal somatic cells, the centrosome generally accounts for the major microtubule organizing center, and the duplicated...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281451</comments>
            <pubDate>Fri, 23 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281451</guid>        </item>
        <item>
            <title>Role of cold shock Y-box protein-1 in inflammation, atherosclerosis and organ transplant rejection.</title>
            <link>http://www.medworm.com/index.php?rid=5281452&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21943779%26dopt%3DAbstract</link>
            <description>Authors: Raffetseder U, Liehn EA, Weber C, Mertens PR
    Abstract
    Chemokines (chemoattractant cytokines) are crucial regulators of immune cell extravasation from the bloodstream into inflamed tissue. Dysfunctional regulation and perpetuated chemokine gene expression are linked to progressive chronic inflammatory diseases and, in respect to transplanted organs, may trigger graft rejection. RANTES (regulated upon activation, normal T cell expressed and secreted (also known as CCL5)) is a model chemokine with relevance in numerous inflammatory diseases where the innate immune response predominates. Transcription factor Y-box binding protein-1 (YB-1) serves as a trans-regulator of CCL5 gene transcription in vascular smooth muscle cells and leucocytes. This review provides an update on YB-...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5281452</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5281452</guid>        </item>
        <item>
            <title>MAD1 and its life as a MYC antagonist: An update.</title>
            <link>http://www.medworm.com/index.php?rid=5231731&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21917351%26dopt%3DAbstract</link>
            <description>Authors: Lüscher B
    Abstract
    The MYC/MAX/MAD network is of central importance for controlling cell physiology. The network is compiled of transcriptional regulators that form different heterodimers, which can either activate or repress the expression of target genes. Thus these proteins function as a molecular switch to control gene expression. MAD1, a member of this network, acts as a transcriptional repressor. It interacts with MAX to form the OFF position of the switch, antagonizing MYC/MAX complexes that define the ON position. MAD1 regulates cell proliferation and apoptosis through a number of target genes. In addition recent evidence indicates that the expression and activity of MAD1 are regulated at multiple levels. Here the recent developments are summarized, in comparison ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5231731</comments>
            <pubDate>Mon, 12 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5231731</guid>        </item>
        <item>
            <title>A novel explant outgrowth culture model for mouse pancreatic acinar cells with long-term maintenance of secretory phenotype.</title>
            <link>http://www.medworm.com/index.php?rid=5219281&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21906833%26dopt%3DAbstract</link>
            <description>Authors: Bläuer M, Nordback I, Sand J, Laukkarinen J
    Abstract
    The development of in vitro models able to support the long-term viability and function of acinar cells is critical for exploring pancreatic pathophysiology. Despite considerable efforts, no long-term culture models for non-transformed pancreatic acini exist. Our aim was to develop and validate culture conditions for this purpose. An explant outgrowth culture design was established in which mouse pancreatic explants were cultured at the gas-liquid interphase. An enriched culture medium, pH 7.8, was employed to promote the selective outgrowth of acinar cells and to support their differentiated phenotype. After 7 days, the outgrown primary acinar cells were subcultured and maintained up to an additional 7 days as secondar...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5219281</comments>
            <pubDate>Wed, 07 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5219281</guid>        </item>
        <item>
            <title>The platelet-derived growth factor system in renal disease: An emerging role of endogenous inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=5176757&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21872965%26dopt%3DAbstract</link>
            <description>Authors: van Roeyen CR, Ostendorf T, Floege J
    Abstract
    The platelet-derived growth factor (PDGF) family consists of four isoforms which are secreted as homodimers (PDGF-AA, PDGF-BB, PDGF-CC and PDGF-DD) or heterodimers (PDGF-AB), and two receptor chains (PDGFR-α and -β). All members of the PDGF system are constitutively or inducibly expressed in renal cells and are involved in the regulation of cell proliferation and migration, the accumulation of extracellular matrix proteins and the secretion of pro- and anti-inflammatory mediators. Particular roles have been identified in mediating mesangioproliferative changes, renal interstitial fibrosis and glomerular angiogenesis. Different endogenous inhibitors of PDGF-induced biological responses exist which affect the activation/deactiv...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176757</comments>
            <pubDate>Thu, 25 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176757</guid>        </item>
        <item>
            <title>Binding sites in membrane proteins - Diversity, druggability and prospects.</title>
            <link>http://www.medworm.com/index.php?rid=5176756&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21872966%26dopt%3DAbstract</link>
            <description>Authors: Adams R, Worth CL, Guenther S, Dunkel M, Lehmann R, Preissner R
    Abstract
    The identification of novel drug targets is one of the major challenges in proteomics. Computational methods developed over the last decade have enhanced the process of drug design in both terms of time and quality. The main task is the design of selective compounds, which bind targets more specifically, dependent on the desired mode of action of the particular drug. This makes it necessary to create compounds, which either exhibit their functions on one single protein to exclude undesired cross-reactivity or to use the advantageous effect of less selective drugs that target numerous proteins and therefore exhibit their functions on whole protein classes. Main aspects in the assignment of interactions...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176756</comments>
            <pubDate>Thu, 25 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176756</guid>        </item>
        <item>
            <title>Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast.</title>
            <link>http://www.medworm.com/index.php?rid=5176758&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21872358%26dopt%3DAbstract</link>
            <description>Authors: Murphy ER, Boxberger J, Colvin R, Lee SJ, Zahn G, Loor F, Kim K
    Abstract
    The eisosome protein Pil1 is known to be implicated in the endocytosis of Ste3, but the precise biological function of it during endocytosis is poorly understood. Here, we present data to reveal Pil1's role in receptor-mediated endocytosis. Using live cell imaging, we show that endocytic patches carrying Abp1 and Las17 persisted much longer in PIL1-deficient cells. The loss of Pil1 also greatly affected both the scission efficiency and the frequency of formation of endocytic sites carrying Rvs161- and Rvs167-GFP. Furthermore, the mistargeting of the synaptojanins, Sjl1 and Sjl2, to the cytoplasm in pil1Δ cells suggests that Pil1 is required for the proper recruitment of the synaptojanins to endocytic...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176758</comments>
            <pubDate>Wed, 24 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176758</guid>        </item>
        <item>
            <title>Role and regulation of autophagy in the development of acinar structures formed by bovine BME-UV1 mammary epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5176761&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21868124%26dopt%3DAbstract</link>
            <description>Authors: Sobolewska A, Motyl T, Gajewska M
    Abstract
    Autophagy is a catabolic process providing an alternative energy source for cells under stressful conditions such as starvation, growth factor deprivation or hypoxia. During involution of the bovine mammary gland autophagy is induced in mammary epithelial cells (MECs) as a survival mechanism, and is tightly regulated by hormones and growth factors necessary for gland development. In the present study we adapted the three-dimensional culture model to investigate the role of autophagy during formation of alveoli-like structures by bovine BME-UV1 MECs grown on extracellular matrix (ECM) components. Using confocal microscopy and Western-blot analyses of autophagic and apoptotic markers: LC3, and cleaved caspase-3, we showed that autop...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176761</comments>
            <pubDate>Mon, 22 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176761</guid>        </item>
        <item>
            <title>Yeast ubiquitin ligase Rsp5 contains nuclear localization and export signals.</title>
            <link>http://www.medworm.com/index.php?rid=5176760&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21868125%26dopt%3DAbstract</link>
            <description>Authors: Cholbinski P, Jastrzebska Z, Wysocka-Kapcinska M, Plochocka D, Gornicka A, Hopper AK, Zoladek T
    Abstract
    The Rsp5 ubiquitin ligase regulates numerous cellular processes. Rsp5 is mainly localized to the cytoplasm but nuclear localization was also reported. A potential nuclear export signal was tested for activity by using a GFP(2) reporter. The 687-LIGGIAEIDI-696 sequence located in the Hect domain was identified as a nuclear export signal active in a Crm1-dependent manner, and its importance for the localization of Rsp5 was documented by using fluorescence microscopy and a lacZ-based reporter system. Analysis of the cellular location of other Rsp5 fragments fused with GFP(2) indicated two independent potential nuclear localization signals, both located in the Hect domain. ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176760</comments>
            <pubDate>Mon, 22 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176760</guid>        </item>
        <item>
            <title>A look at tricellulin and its role in tight junction formation and maintenance.</title>
            <link>http://www.medworm.com/index.php?rid=5176759&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21868126%26dopt%3DAbstract</link>
            <description>Authors: Mariano C, Sasaki H, Brites D, Brito MA
    Abstract
    Tight junctions are elaborate networks of transmembrane and cytosolic proteins that regulate epithelial permeability. Tricellulin was the first tight junction protein found at tricellular tight junctions, the specialized structures occurring where three cells meet together. Here, we summarize the current knowledge about tricellulin (marvelD2), a MARVEL domain protein. We address tricellulin location at tricellular junctions, and establish the comparison with the other members of the MARVEL family, occludin (marvelD1) and marvelD3. The structure of tricellulin and its membrane folding, as well as the proposed molecular interactions of tricellulin with other tight junction proteins, together with the interplay between those pr...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5176759</comments>
            <pubDate>Mon, 22 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5176759</guid>        </item>
        <item>
            <title>RNAi knockdown of parafusin inhibits the secretory pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5157522&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21856035%26dopt%3DAbstract</link>
            <description>Authors: Liu L, Wyroba E, Satir BH
    Abstract
    Several glycolytic enzymes and their isoforms have been found to be important in cell signaling unrelated to glycolysis. The involvement of parafusin (PFUS), a member of the phosphoglucomutase (PGM) superfamily with no phosphoglucomutase activity, in Ca(2+)-dependent exocytosis has been controversial. This protein was first described in Paramecium tetraurelia, but is widely found. Earlier work showed that parafusin is a secretory vesicle scaffold component with unusual post-translational modifications (cyclic phosphorylation and phosphoglucosylation) coupled to stages in the exocytic process. Using RNAi, we demonstrate that parafusin synthesis can be reversibly blocked, with minor or no effect on other PGM isoforms. PFUS knockdown produce...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157522</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157522</guid>        </item>
        <item>
            <title>Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator.</title>
            <link>http://www.medworm.com/index.php?rid=5157521&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21856036%26dopt%3DAbstract</link>
            <description>Authors: Fan H, Tansi FL, Weihofen WA, Böttcher C, Hu J, Martinez J, Saenger W, Reutter W
    Abstract
    Dipeptidyl peptidase IV (DPPIV or CD26) is a multifunctional membrane glycoprotein. As an exopeptidase it regulates the activity of a series of biologically important peptides. Through its interaction with specific proteins and peptides, DPPIV is also involved in a wide range of biologically relevant processes such as cell adhesion, T cell activation and apoptosis. In this paper, we review our recent studies on the interactions of DPPIV with adenosine deaminase (ADA) and the transcription transactivator of the human immunodeficiency virus type-1 (HIV-1 Tat) as revealed by three-dimensional structure reconstructed by single particle analysis of cryo-electron microscopy (EM) and crysta...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5157521</comments>
            <pubDate>Tue, 16 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5157521</guid>        </item>
        <item>
            <title>βIII-Tubulin is required for interphase microtubule dynamics in untransformed human mammary epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5141667&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21820201%26dopt%3DAbstract</link>
            <description>Authors: Bouchet BP, Puisieux A, Galmarini CM
    Abstract
    Numerous works have questioned the pertinence of using βII- and/or βIII-tubulin expression as markers of prognosis and/or prediction of breast cancer response to chemotherapy containing microtubule-targeting agents. The rationale of such studies was essentially based on microtubule dynamics analysis using purified tubulin in vitro and cancer cell lines. Nonetheless, the significance of βII- and βIII-tubulin expression in the control of microtubule dynamics in normal mammary epithelium has never been addressed. Here we investigate the expression and the consequences of βII- and/or βIII-tubulin depletion in interphase microtubule dynamics in non-tumor human mammary epithelial cells. We find that both isoforms contribute to ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141667</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141667</guid>        </item>
        <item>
            <title>Actin: From structural plasticity to functional diversity.</title>
            <link>http://www.medworm.com/index.php?rid=5141666&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21820202%26dopt%3DAbstract</link>
            <description>This article addresses the multiple activities of actin. Starting out with the history of actin's discovery, purification and structure, it emphasizes the close relation between structure and function. In this context, we also point to unconventional actin conformations. Their existence in living cells is not yet well documented, however, they seem to play a special role in the supramolecular patterning that underlies some of the physiological functions of actin. Conceivably, such conformations may contribute to actin's diverse activities in the nucleus that are poorly understood so far.
    PMID: 21820202 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141666</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141666</guid>        </item>
        <item>
            <title>Connexin32 can restore hearing in connexin26 deficient mice.</title>
            <link>http://www.medworm.com/index.php?rid=5104170&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21813206%26dopt%3DAbstract</link>
            <description>Authors: Degen J, Schütz M, Dicke N, Strenzke N, Jokwitz M, Moser T, Willecke K
    Functional gap junction channels composed of certain connexin proteins are essential for the function of the cochlea. Homozygous deficiency in the Gjb2 (mice) or GJB2 (human) gene coding for connexin26 (Cx26) in the cochlea leads to hearing impairment in mice and humans, respectively. Here we have studied the functional equivalence of Cx26 and connexin32 (Cx32) isoforms in the cochlea. We analyzed a conditional mouse mutant in which the Gjb2 coding DNA was exchanged by LacZ DNA coding for the reporter protein beta-galactosidase. This allowed us to follow the unrestricted and cell type specific expression of Gjb2 promoter activity. After inner ear specific, Otogelin-Cre recombinase mediated deletion of the ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104170</comments>
            <pubDate>Sun, 31 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104170</guid>        </item>
        <item>
            <title>Activation and molecular recognition of the GPCR rhodopsin - Insights from time-resolved fluorescence depolarisation and single molecule experiments.</title>
            <link>http://www.medworm.com/index.php?rid=5104172&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21803442%26dopt%3DAbstract</link>
            <description>Authors: Kim TY, Schlieter T, Haase S, Alexiev U
    The cytoplasmic surface of the G-protein coupled receptor (GPCR) rhodopsin is a key element in membrane receptor activation, molecular recognition by signalling molecules, and receptor deactivation. Understanding of the coupling between conformational changes in the intramembrane domain and the membrane-exposed surface of the photoreceptor rhodopsin is crucial for the elucidation of the molecular mechanism in GPCR activation. As little is known about protein dynamics, particularly the conformational dynamics of the cytoplasmic surface elements on the nanoseconds timescale, we utilised time-resolved fluorescence anisotropy experiments and site-directed fluorescence labelling to provide information on both, conformational space and motion....</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104172</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104172</guid>        </item>
        <item>
            <title>Dynamic modification of microtubule-dependent transport by effector proteins of intracellular Salmonella enterica.</title>
            <link>http://www.medworm.com/index.php?rid=5104171&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21803443%26dopt%3DAbstract</link>
            <description>Authors: Rajashekar R, Hensel M
    Intracellular Salmonella enterica translocate effector proteins that modify microtubule-dependent transport processes of the host cell and modulate the biogenesis of the Salmonella-containing vacuole (SCV). One functional consequence is the induction of tubular aggregates of endosomal membranes, termed Salmonella-induced filaments or SIFs, and further tubular membrane compartments have recently been described. SIFs are unique, highly dynamic compartments that form by modification of vesicular transport on microtubules. The molecular mechanism of the interference of intracellular Salmonella with host cell vesicular transport is still elusive, but recent studies demonstrate the complexity of pathogenic activities and the intricacy of manipulating host cell...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104171</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104171</guid>        </item>
        <item>
            <title>The priority program Signal Pathways to the Cytoskeleton and Bacterial Pathogenesis (SPP1150).</title>
            <link>http://www.medworm.com/index.php?rid=5104173&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21802769%26dopt%3DAbstract</link>
            <description>Authors: Schmidt G, Aktories K
    
    PMID: 21802769 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104173</comments>
            <pubDate>Wed, 27 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104173</guid>        </item>
        <item>
            <title>Viral functions and immune modulation.</title>
            <link>http://www.medworm.com/index.php?rid=5104174&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21802169%26dopt%3DAbstract</link>
            <description>Authors: Koszinowski U
    
    PMID: 21802169 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104174</comments>
            <pubDate>Tue, 26 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104174</guid>        </item>
        <item>
            <title>Microfluidic tools for quantitative studies of eukaryotic chemotaxis.</title>
            <link>http://www.medworm.com/index.php?rid=5104175&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21783273%26dopt%3DAbstract</link>
            <description>Authors: Beta C, Bodenschatz E
    Over the past decade, microfluidic techniques have been established as a versatile platform to perform live cell experiments under well-controlled conditions. To investigate the directional responses of cells, stable concentration profiles of chemotactic factors can be generated in microfluidic gradient mixers that provide a high degree of spatial control. However, the times for built-up and switching of gradient profiles are in general too slow to resolve the intracellular protein translocation events of directional sensing of eukaryotes. Here, we review an example of a conventional microfluidic gradient mixer as well as the novel flow photolysis technique that achieves an increased temporal resolution by combining the photo-activation of caged compounds...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104175</comments>
            <pubDate>Wed, 20 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104175</guid>        </item>
        <item>
            <title>Comprehensive analysis of TGF-β and BMP receptor interactomes.</title>
            <link>http://www.medworm.com/index.php?rid=5009174&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21715044%26dopt%3DAbstract</link>
            <description>Authors: Poorgholi Belverdi M, Krause C, Guzman A, Knaus P
    An immense number of cellular processes are initiated by cell surface serine/threonine kinase receptors belonging to the TGF-β/BMP family. Subsequent downstream signalling cascades, as well as their crosstalk results in enormous specificity in terms of phenotypic outcome, e.g. proliferation, differentiation, migration or apoptosis. Such signalling diversity is achieved by the ability of receptors to interact with distinct proteins in a spatio-temporal manner. Following the cloning of the TGF-β/BMP receptors a variety of different technologies were applied to identify such interacting proteins. Here we present a comprehensive survey of known interactome analyses, including our own data, on these receptors and discuss advantage...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009174</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009174</guid>        </item>
        <item>
            <title>The cellular basis of chitin synthesis in fungi and insects: Common principles and differences.</title>
            <link>http://www.medworm.com/index.php?rid=5009176&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21700357%26dopt%3DAbstract</link>
            <description>Authors: Merzendorfer H
    Chitin is a polymer of N-acetylglucosamine, which assembles into microfibrils of about 20 sugar chains. These microfibrils serve as a structural component of natural biocomposites found in cell walls and specialized extracellular matrices such as cuticles and peritrophic membranes. Chitin synthesis is performed by a wide range of organisms including fungi and insects. The underlying biosynthetic machinery is highly conserved and involves several enzymes, of which the chitin synthase is the key enzyme. This membrane integral glycosyltransferase catalyzes the polymerization reaction. Most of what we know about chitin synthesis derives from studies of fungal and insect systems. In this review, common principles and differences will be worked out at the levels of ge...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009176</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009176</guid>        </item>
        <item>
            <title>A role for Tctex-1 (DYNLT1) in controlling primary cilium length.</title>
            <link>http://www.medworm.com/index.php?rid=5009175&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21700358%26dopt%3DAbstract</link>
            <description>Authors: Palmer KJ, Maccarthy-Morrogh L, Smyllie N, Stephens DJ
    The microtubule motor complex cytoplasmic dynein is known to be involved in multiple processes including endomembrane organization and trafficking, mitosis, and microtubule organization. The majority of studies of cytoplasmic dynein have focused on the form of the motor that is built around the dynein-1 heavy chain. A second isoform, dynein heavy chain-2, and its specifically associated light intermediate chain, LIC3 (D2LIC), are known to be involved in the formation and function of primary cilia. We have used RNAi in human epithelial cells to define the cytoplasmic dynein subunits that function with dynein heavy chain 2 in primary cilia. We identify the dynein light chain Tctex-1 as a key modulator of cilia length control...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009175</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009175</guid>        </item>
        <item>
            <title>The KdpFABC complex from Escherichia coli: A chimeric K(+) transporter merging ion pumps with ion channels.</title>
            <link>http://www.medworm.com/index.php?rid=4962269&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684627%26dopt%3DAbstract</link>
            <description>Authors: Greie JC
    The KdpFABC complex represents a multi-subunit ATP-driven potassium pump, which is only found in bacteria and archaea. Based on the properties of the ATP-hydrolyzing subunit (KdpB) the transporter has been classified as a type IA P-type ATPase. However, structural and functional properties of the remaining subunits clearly show homologies to members of the potassium channel as well as the ABC transporter family, thus rendering the KdpFABC complex to represent an inimitable chimera of ion pumps and ion channels. Accordingly, this striking juxtaposition entails special features of KdpFABC with respect to typical members of each of the transporter families, involving not only the concepts but also the structures of ion channels and ion pumps. For example, the sites of AT...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962269</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962269</guid>        </item>
        <item>
            <title>Exploring protein import pores of cellular organelles at the single molecule level using the planar lipid bilayer technique.</title>
            <link>http://www.medworm.com/index.php?rid=4962268&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684628%26dopt%3DAbstract</link>
            <description>Authors: Harsman A, Bartsch P, Hemmis B, Krüger V, Wagner R
    Proteins of living cells carry out their specialized functions within various subcellular membranes or aqueous spaces. Approximately half of all the proteins of a typical cell are transported into or across membranes. Targeting and transport to their correct subcellular destinations are essential steps in protein biosynthesis. In eukaryotic cells secretory proteins are transported into the endoplasmic reticulum before they are transported in vesicles to the plasma membrane. Virtually all proteins of the endosymbiotic organelles, chloroplasts and mitochondria, are synthesized on cytosolic ribosomes and posttranslationally imported. Genetic and biochemical techniques led to rather detailed knowledge on the subunit composition o...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962268</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962268</guid>        </item>
        <item>
            <title>Drosophila metalloproteases in development and differentiation: The role of ADAM proteins and their relatives.</title>
            <link>http://www.medworm.com/index.php?rid=4962267&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684629%26dopt%3DAbstract</link>
            <description>Authors: Meyer H, Panz M, Albrecht S, Drechsler M, Wang S, Hüsken M, Lehmacher C, Paululat A
    ADAM metalloproteases are membrane bound glycoproteins that control many biological processes during development and differentiation, mainly by acting as ectodomain sheddases. The Drosophila genome contains five genes that code for classical ADAM proteins which are characterized by a highly conserved domain structure with the respective catalytic domains facing the extracellular space. More than 50 genes encode related proteins such as those that have lost their primary enzymatic activity while retaining, e.g., their adhesive properties. The physiological relevance of many Drosophila ADAMs and their relatives is still unknown, however for others, a striking role during organogenesis and tissue...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962267</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962267</guid>        </item>
        <item>
            <title>Centromere regulation: New players, new rules, new questions.</title>
            <link>http://www.medworm.com/index.php?rid=4962266&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684630%26dopt%3DAbstract</link>
            <description>Authors: Pauleau AL, Erhardt S
    Centromeres support the assembly of the kinetochore on every chromosome and are therefore essential for the proper segregation of sister chromatids during cell division. Centromere identity is regulated epigenetically through the presence of the histone H3 variant CENP-A. CENP-A regulation and incorporation specifically into centromeric nucleosomes are the matter of intensive studies in many different model organisms. Here we briefly review the current knowledge in centromere biology with a focus on Drosophila melanogaster and how these insights lead to new rules and challenges.
    PMID: 21684630 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962266</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962266</guid>        </item>
        <item>
            <title>Transmembrane signal transduction in archaeal phototaxis: The sensory rhodopsin II-transducer complex studied by electron paramagnetic resonance spectroscopy.</title>
            <link>http://www.medworm.com/index.php?rid=4962265&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21684631%26dopt%3DAbstract</link>
            <description>Authors: Klare JP, Bordignon E, Engelhard M, Steinhoff HJ
    Archaeal photoreceptors, together with their cognate transducer proteins, mediate phototaxis by regulating cell motility through two-component signal transduction pathways. This sensory pathway is closely related to the bacterial chemotactic system, which has been studied in detail during the past 40 years. Structural and functional studies applying site-directed spin labelling and electron paramagnetic resonance spectroscopy on the sensory rhodopsin II/transducer (NpSRII/NpHtrII) complex of Natronomonas pharaonis have yielded insights into the structure, the mechanisms of signal perception, the signal transduction across the membrane and provided information about the subsequent information transfer within the transducer protei...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962265</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962265</guid>        </item>
        <item>
            <title>Membrane dynamics and fusion at late endosomes and vacuoles - Rab regulation, multisubunit tethering complexes and SNAREs.</title>
            <link>http://www.medworm.com/index.php?rid=4962270&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21683469%26dopt%3DAbstract</link>
            <description>Authors: Epp N, Rethmeier R, Krämer L, Ungermann C
    Membrane fusion at late endosomes and vacuoles depends on a conserved machinery, which includes Rab GTPases, their binding to tethering complexes and SNAREs. Fusion is initiated by the interaction of Rabs with tethering complexes. At the endosome, the CORVET complex interacts with the Rab5 GTPase Vps21, whereas the homologous HOPS complex binds the Rab7-like Ypt7 at the late endosome and vacuole. Activation of Ypt7 requires the recruitment of the Mon1-Ccz1 complex to the late endosome, which occurs via the CORVET complex. The interaction of Rab and the tethering complex is followed by the assembly of SNAREs, which leads to bilayer mixing. In this review, we will summarize our current knowledge on the mechanisms and regulation of endos...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962270</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962270</guid>        </item>
        <item>
            <title>KtrB, a member of the superfamily of K(+) transporters.</title>
            <link>http://www.medworm.com/index.php?rid=4962271&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21680052%26dopt%3DAbstract</link>
            <description>Authors: Hänelt I, Tholema N, Kröning N, Vor der Brüggen M, Wunnicke D, Bakker EP
    KtrB is the K(+)-translocating subunit of the K(+)-uptake system KtrAB from bacteria. It is a member of the superfamily of K(+)transporters (SKT proteins) with other sub-families occurring in archaea, bacteria, fungi, plants and trypanosomes. SKT proteins may have originated from small K(+) channels by at least two gene duplication and two gene fusion events. They contain four covalently linked M(1)PM(2) domains, in which M(1) and M(2) stand for transmembrane stretches, and P for a P-loop, which folds back from the external medium into the membrane. SKT proteins distinguish themselves in two important aspects from K(+) channels: first, with just one conserved glycine residue in their P-loops they conta...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962271</comments>
            <pubDate>Mon, 13 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962271</guid>        </item>
        <item>
            <title>HLA class I-associated diseases with a suspected autoimmune etiology: HLA-B27 subtypes as a model system.</title>
            <link>http://www.medworm.com/index.php?rid=4962272&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21665321%26dopt%3DAbstract</link>
            <description>Authors: Uchanska-Ziegler B, Loll B, Fabian H, Hee CS, Saenger W, Ziegler A
    Although most autoimmune diseases are connected to major histocompatibility complex (MHC) class II alleles, a small number of these disorders exhibit a variable degree of association with selected MHC class I genes, like certain human HLA-A and HLA-B alleles. The basis for these associations, however, has so far remained elusive. An understanding might be obtained by comparing functional, biochemical, and biophysical properties of alleles that are minimally distinct from each other, but are nevertheless differentially associated to a given disease, like the HLA-B*27:05 and HLA-B*27:09 antigens, which differ only by a single amino acid residue (Asp116His) that is deeply buried within the binding groove. We have ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962272</comments>
            <pubDate>Thu, 09 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962272</guid>        </item>
        <item>
            <title>p21(Cip1) regulates cell-substrate adhesion and interphase microtubule dynamics in untransformed human mammary epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4866045&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561680%26dopt%3DAbstract</link>
            <description>Authors: Bouchet BP, Fauvet F, Grelier G, Galmarini CM, Puisieux A
    Despite its frequent inactivation in human breast cancers, the role of p21(Cip1) (p21) in morphological plasticity of normal mammary epithelial cells is still poorly understood. To address this question, we have investigated the consequences of p21 silencing in two-dimensional (2D) morphogenesis of untransformed human mammary epithelial cells. Here we show that p21 inactivation causes a reduction of 2D cell spreading and suppresses focal adhesion. In order to investigate the cytoskeletal modifications associated with this altered morphology, we have analyzed the microtubule dynamics in interphase p21-depleted cells. Our results demonstrate that interphase microtubule dynamic instability is strongly increased by p21 sile...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866045</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866045</guid>        </item>
        <item>
            <title>Mapping receptor-ligand interactions with synthetic peptide arrays: Exploring the structure and function of membrane receptors.</title>
            <link>http://www.medworm.com/index.php?rid=4866044&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561681%26dopt%3DAbstract</link>
            <description>We present several systematic sets of peptide arrays useful for mapping protein-protein- or receptor-ligand binding sites. Besides a more technical description of the peptide array preparation we discuss in detail the reliability and improvement of mapping protein-protein interactions by synthetic peptide arrays. At least proteomic approaches for mapping protein-protein interactions by peptide arrays are shown especially for the case of protein interaction domains.
    PMID: 21561681 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866044</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866044</guid>        </item>
        <item>
            <title>Properties, functions and evolution of cytokinin receptors.</title>
            <link>http://www.medworm.com/index.php?rid=4866043&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561682%26dopt%3DAbstract</link>
            <description>Authors: Heyl A, Riefler M, Romanov GA, Schmülling T
    The discovery of cytokinin receptors of Arabidopsis thaliana ten years ago was a milestone in plant hormone research. Since then, research has yielded insights into the biochemical properties and functions of these sensor histidine kinases. Their affinities to both trans-zeatin and isopentenyladenine are in the low nM range. Cytokinin ribosides, cis-zeatin and thidiazuron were established as compounds with genuine cytokinin activity and the first cytokinin antagonists were identified. Numerous functions of cytokinin receptors in plant development, as well as in the plant's responses to the environment, have been elucidated and are summarized. Finally, we address the question how the receptors have evolved during plant evolution.
   ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866043</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866043</guid>        </item>
        <item>
            <title>Capturing ER calcium dynamics.</title>
            <link>http://www.medworm.com/index.php?rid=4866042&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561683%26dopt%3DAbstract</link>
            <description>Authors: Jaepel J, Blum R
    The lumen of the endoplasmic reticulum (ER) contributes to the dynamics of Ca(2+) signaling by acting as a source or sink of signal Ca(2+). Despite its relevance for the understanding of the cell biology and pathophysiology of the luminal calcium store, the direct measurement of luminal Ca(2+) release and uptake is still critical when Ca(2+) homeostasis is analyzed in neural cells. For the analysis of Ca(2+)-dependent signaling, synthetic Ca(2+) indicators have become popular. The properties of these indicators allow only limited targeting to subcellular structures such as the ER. Recently, we introduced a new strategy for the targeting of synthetic Ca(2+) indicators to the lumen of the ER. The method, termed Targeted-Esterase-induced Dye loading (TED) is base...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866042</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866042</guid>        </item>
        <item>
            <title>Integrin-mediated uptake of fibronectin-binding bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=4866041&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561684%26dopt%3DAbstract</link>
            <description>Authors: Hoffmann C, Ohlsen K, Hauck CR
    Invasion of mammalian cells via cell adhesion molecules of the integrin family is a common theme in bacterial pathogenesis. Whereas some microorganisms directly bind to integrins, other pathogens such as Staphylococcus aureus indirectly engage these receptors via fibronectin-binding proteins (FnBPs). In this review, we summarize the structure-function relationship of FnBPs and the current view of the role of these proteins during pathogenesis in vivo. A major focus will be on recent findings on the role of cholesterol- and sphingolipid-rich membrane microdomains for integrin-initiated uptake of fibronectin-binding bacteria and the surprising inhibitory function of caveolin-1 in this process. The detailed mechanistic understanding of host cell inv...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866041</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866041</guid>        </item>
        <item>
            <title>Receptor-transporter interactions of canonical ATP-binding cassette import systems in prokaryotes.</title>
            <link>http://www.medworm.com/index.php?rid=4866040&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21561685%26dopt%3DAbstract</link>
            <description>Authors: Schneider E, Eckey V, Weidlich D, Wiesemann N, Vahedi-Faridi A, Thaben P, Saenger W
    ATP-binding cassette (ABC) transport systems mediate the translocation of solutes across biological membranes at the expense of ATP. They share a common modular architecture comprising two pore-forming transmembrane domains and two nucleotide binding domains. In prokaryotes, ABC transporters are involved in the uptake of a large variety of chemicals, including nutrients, osmoprotectants and signal molecules. In pathogenic bacteria, some ABC importers are virulence factors. Canonical ABC import systems require an additional component, a substrate-specific receptor or binding protein for function. Interaction of the liganded receptor with extracytoplasmic loop regions of the transmembrane domains...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866040</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866040</guid>        </item>
        <item>
            <title>l-Selectin - A dynamic regulator of leukocyte migration.</title>
            <link>http://www.medworm.com/index.php?rid=4814235&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21546114%26dopt%3DAbstract</link>
            <description>Authors: Wedepohl S, Beceren-Braun F, Riese S, Buscher K, Enders S, Bernhard G, Kilian K, Blanchard V, Dernedde J, Tauber R
    The leukocytic cell adhesion receptor l-selectin mediates the initial step of the adhesion cascade, the capture and rolling of leukocytes on endothelial cells. This event enables leukocytes to migrate out of the vasculature into surrounding tissues during inflammation and immune surveillance. Distinct domains of l-selectin contribute to proper leukocyte migration. In this review, we discuss the contributions of these domains with respect to l-selectin function: the regulation by serine phosphorylation of the cytoplasmic tail, the role of the transmembrane domain in receptor positioning on the cell surface as well as the N-glycosylation of the extracellular part an...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814235</comments>
            <pubDate>Mon, 02 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814235</guid>        </item>
        <item>
            <title>Functional significance of cleavable signal peptides of G protein-coupled receptors.</title>
            <link>http://www.medworm.com/index.php?rid=4814236&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21543132%26dopt%3DAbstract</link>
            <description>Authors: Schülein R, Westendorf C, Krause G, Rosenthal W
    About 5-10% of the G protein-coupled receptors (GPCRs) contain N-terminal signal peptides that are cleaved off by the signal peptidases of the endoplasmic reticulum (ER) during the translocon-mediated receptor insertion into the ER membrane. The reason as to why only a subset of the GPCRs requires these additional signal peptides was addressed in the past decade only by a limited number of studies. Recent progress suggests that signal peptides of GPCRs do not only serve the classical ER targeting and translocon gating functions as described for the signal peptides of secretory proteins. In the case of GPCRs, uncleaved pseudo signal peptides may regulate receptor expression at the plasma membrane and may also influence G protein ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814236</comments>
            <pubDate>Sun, 01 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814236</guid>        </item>
        <item>
            <title>Ret finger protein 2 enhances ionizing radiation-induced apoptosis via degradation of AKT and MDM2.</title>
            <link>http://www.medworm.com/index.php?rid=4583552&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333377%26dopt%3DAbstract</link>
            <description>Authors: Joo HM, Kim JY, Jeong JB, Seong KM, Nam SY, Yang KH, Kim CS, Kim HS, Jeong M, An S, Jin YW
    Ret finger protein 2 (RFP2), a gene frequently deleted in multiple tumor types, encodes a protein with a RING finger, B-box, and coiled-coil domain that belongs to the RBCC/TRIM protein family. Although RBCC proteins are involved in diverse cellular processes such as apoptosis, proliferation, differentiation, and transcriptional regulation, the biological function of RFP2 has not been well defined. Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. The expression of RFP2, which possesses RING domain-dependent E3 ubiquitin ligase activity, was increased by ionizing radiation dose- and time-dependently, and RFP2 over...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583552</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:46 +0100</pubDate>
            <guid isPermaLink="false">4583552</guid>        </item>
        <item>
            <title>AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes.</title>
            <link>http://www.medworm.com/index.php?rid=4583551&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333378%26dopt%3DAbstract</link>
            <description>Authors: Snyder BN, Cho Y, Qian Y, Coad JE, Flynn DC, Cunnick JM
    The actin-filament associated protein (AFAP) family of adaptor proteins consists of three members: AFAP1, AFAP1L1, and AFAP1L2/XB130 with AFAP1 being the best described as a cSrc binding partner and actin cross-linking protein. A homology search of AFAP1 recently identified AFAP1L1 which has a similar sequence, domain structure and cellular localization; however, based upon sequence variations, AFAP1L1 is hypothesized to have unique functions that are distinct from AFAP1. While AFAP1 has the ability to bind to the SH3 domain of the nonreceptor tyrosine kinase cSrc via an N-terminal SH3 binding motif, it was unable to bind cortactin. However, the SH3 binding motif of AFAP1L1 was more efficient at interacting with the SH3 d...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583551</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:42 +0100</pubDate>
            <guid isPermaLink="false">4583551</guid>        </item>
        <item>
            <title>Glucocorticoid receptor is indispensable for physiological responses to aldosterone in epithelial Na(+) channel induction via the mineralocorticoid receptor in a human colonic cell line.</title>
            <link>http://www.medworm.com/index.php?rid=4583548&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354648%26dopt%3DAbstract</link>
            <description>Authors: Bergann T, Fromm A, Borden SA, Fromm M, Schulzke JD
    The epithelial Na+ channel (ENaC) plays a crucial role in electrogenic Na(+) absorption in the distal colon. ENaC induction via the mineralocorticoid receptor (MR) and the glucocorticoid receptor (GR) is differentially regulated by modulatory components. As most existing epithelial cell lines including colonic epithelial cell lines miss the co-expression of functional GR and MR, signaling on ENaC is only poorly characterized regarding the interplay of glucocorticoids and mineralocorticoids. In the present study, we show that GR expression and activity are indispensable for MR-dependent induction of ENaC-mediated Na(+) transport. Cooperativity of the two receptors has been studied in the highly differentiated, epithelial colon...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583548</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:32 +0100</pubDate>
            <guid isPermaLink="false">4583548</guid>        </item>
        <item>
            <title>Characterisation of the potential SNARE proteins relevant to milk product release by mouse mammary epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4583547&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354649%26dopt%3DAbstract</link>
            <description>Authors: Chat S, Layani S, Mahaut C, Henry C, Chanat E, Truchet S
    Casein micelles and fat globules are essential components of milk and are both secreted at the apical side of mammary epithelial cells during lactation. Milk fat globules are excreted by budding, being enwrapped by the apical plasma membrane, while caseins contained in transport vesicles are released by exocytosis. Nevertheless, the molecular mechanisms governing casein exocytosis are, to date, not fully deciphered. SNARE proteins are known to take part in cellular membrane trafficking and in exocytosis events in many cell types and we therefore attempted to identify those relevant to casein secretion. With this aim, we performed a detailed analysis of their expression by RT-PCR in both whole mouse mammary gland and in p...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583547</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:28 +0100</pubDate>
            <guid isPermaLink="false">4583547</guid>        </item>
        <item>
            <title>A developmental defect in astrocytes inhibits programmed regression of the hyaloid vasculature in the mammalian eye.</title>
            <link>http://www.medworm.com/index.php?rid=4583546&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21354650%26dopt%3DAbstract</link>
            <description>Authors: Zhang C, Asnaghi L, Gongora C, Patek B, Hose S, Ma B, Fard MA, Brako L, Singh K, Goldberg MF, Handa JT, Lo WK, Eberhart CG, Zigler JS, Sinha D
    Previously we reported the novel observation that astrocytes ensheath the persistent hyaloid artery, both in the Nuc1 spontaneous mutant rat, and in human PFV (persistent fetal vasculature) disease (Developmental Dynamics 234:36-47, 2005). We now show that astrocytes isolated from both the optic nerve and retina of Nuc1 rats migrate faster than wild type astrocytes. Aquaporin 4 (AQP4), the major water channel in astrocytes, has been shown to be important in astrocyte migration. We demonstrate that AQP4 expression is elevated in the astrocytes in PFV conditions, and we hypothesize that this causes the cells to migrate abnormally into the...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583546</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:25 +0100</pubDate>
            <guid isPermaLink="false">4583546</guid>        </item>
        <item>
            <title>Membrane palmitoylated proteins regulate trafficking and processing of nectins.</title>
            <link>http://www.medworm.com/index.php?rid=4583545&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21371776%26dopt%3DAbstract</link>
            <description>We report that nectin-1α associates with membrane palmitoylated protein 3 (MPP3), one of the human homologues of a Drosophila tumor suppressor gene, Disc large. Two major forms of MPP3 at 66 and 98kDa were detected, in conjunction with nectin-1α, suggesting that an association between the two may occur in various cell types. Nectin-1α recruits MPP3 to cell-cell contact sites, mediated by a PDZ-binding motif at the carboxyl terminus of nectin-1α. Association with MPP3 increases cell surface expression of nectin-1α and enhances nectin-1α ectodomain shedding, indicating that MPP3 regulates trafficking and processing of nectin-1α. Further study showed that MPP3 interacts with nectin-3α, but not with nectin-2α, showing that the association of nectins with MPP3 is isoform-specific. MPP5...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583545</comments>
            <pubDate>Tue, 15 Mar 2011 16:15:21 +0100</pubDate>
            <guid isPermaLink="false">4583545</guid>        </item>
        <item>
            <title>The importance of being short: The role of rabies virus phosphoprotein isoforms assessed by differential IRES translation initiation.</title>
            <link>http://www.medworm.com/index.php?rid=4583543&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21397980%26dopt%3DAbstract</link>
            <description>Authors: Marschalek A, Drechsel L, Conzelmann KK
    The rabies virus (RV) phosphoprotein P is a multifunctional protein involved in viral RNA synthesis and in counteracting host innate immune responses. We have previously shown that RV P gene expression levels can be regulated by using picornavirus internal ribosome entry site (IRES) elements. Here we exploited a particular feature of the foot-and-mouth disease virus (FMDV) IRES, namely, preferential initiation at a downstream initiation codon, to address the role of N-terminally truncated RV phosphoproteins usually generated in RV-infected cells through ribosomal leaky scanning. Recombinant RVs in which P synthesis was directed by the poliovirus or FMDV IRES produced full-length P (P1) or a truncated form (P2), as the dominant product, r...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583543</comments>
            <pubDate>Fri, 11 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583543</guid>        </item>
        <item>
            <title>Significantly improved rescue of rabies virus from cDNA plasmids.</title>
            <link>http://www.medworm.com/index.php?rid=4583542&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21397981%26dopt%3DAbstract</link>
            <description>Authors: Ghanem A, Kern A, Conzelmann KK
    The rescue of recombinant rabies virus (RV) from cloned cDNA is an inefficient process because it relies on the de novo formation within cells of functional ribonucleoprotein (RNP) complexes from plasmid-expressed viral-like antigenome RNAs and three helper proteins. In the standard RV reverse genetics systems, bacteriophage T7 RNA polymerase drives the transcription of virus antigenome-like RNAs containing three nonviral G residues at the 5'-end and a correct 3'-end generated by the autocatalytic activity of an 85 nucleotides long hepatitis delta virus antigenomic &quot;core&quot; ribozyme (HDVagrz). Here, we show that employing optimized ribozyme sequences significantly improves RV rescue. Substitution of the &quot;core&quot; HDVagrz by a ribozyme with an enhance...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583542</comments>
            <pubDate>Fri, 11 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583542</guid>        </item>
        <item>
            <title>Probing gene function in thymic epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4583544&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21392839%26dopt%3DAbstract</link>
            <description>Authors: Aichinger M, Hinterberger M, Klein L
    Thymic epithelial cells (TECs) provide a highly specialized microenvironment for the generation of a functional and self-tolerant T cell repertoire. Much of our current view of TEC biology is derived from gain- or loss-of-function approaches, which have significantly contributed to our understanding of gene function in TEC development and T cell repertoire selection. Here, we will review transgenic and viral strategies that have been used to manipulate gene expression in TECs, highlight some of the shortcomings of particular currently available tools and provide a brief outline of our own attempts to more rapidly and/or more specifically assess gene function in TECs.
    PMID: 21392839 [PubMed - as supplied by publisher] (Source: European J...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583544</comments>
            <pubDate>Tue, 08 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583544</guid>        </item>
        <item>
            <title>Characterisation of Legionella pneumophila phospholipases and their impact on host cells.</title>
            <link>http://www.medworm.com/index.php?rid=4583549&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21342713%26dopt%3DAbstract</link>
            <description>Authors: Lang C, Flieger A
    Phospholipases are a diverse class of enzymes produced both by eukaryotic hosts and their pathogens. Major insights into action pathways of bacterial phospholipases have been provided during the last years. On the one hand bacterial phospholipases act as potent membrane destructors and on the other hand they manipulate and initiate host signalling paths, such as chemokine expression or the inflammatory cascade. Reaction products of bacterial phospholipases may potentially influence many more host cell processes, such as cell respreading, lamellopodia formation, cell migration and membrane traffic. Phospholipases play a dominant role in the biology of the lung pathogen Legionella pneumophila. So far, 15 different phospholipase A-encoding genes have been identi...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583549</comments>
            <pubDate>Sun, 20 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583549</guid>        </item>
        <item>
            <title>The bottleneck of JNK signaling: Molecular and functional characteristics of MKK4 and MKK7.</title>
            <link>http://www.medworm.com/index.php?rid=4583550&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333379%26dopt%3DAbstract</link>
            <description>Authors: Haeusgen W, Herdegen T, Waetzig V
    The functions of mitogen-activated protein kinases (MKKs) 4 and 7 are typically associated with the c-Jun N-terminal kinase (JNK) signaling pathway. Both MKKs synergistically phosphorylate different JNK isoforms and are therefore involved in numerous physiological (e.g. differentiation and proliferation) and pathological (e.g. apoptosis and tumorigenesis) processes. MKK4 and MKK7 share similar molecular characteristics as well as several upstream activators and scaffold proteins. However, their functions are non-redundant and determined by different stimuli, biochemical interactions and differential tissue distribution. The central question is how two MKKs regulate or affect the multiple actions of their JNK substrates. Similar to JNKs, MKK4 a...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583550</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583550</guid>        </item>
        <item>
            <title>Alterations of pre-mRNA splicing in human inflammatory bowel disease.</title>
            <link>http://www.medworm.com/index.php?rid=4583553&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21324547%26dopt%3DAbstract</link>
            <description>This study demonstrates the potential impact of regulated splicing factors on subsequent regulated intron retention in the pathogenesis of chronic inflammation, exemplified by IBD.
    PMID: 21324547 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583553</comments>
            <pubDate>Mon, 14 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583553</guid>        </item>
        <item>
            <title>Plectin interacts with the rod domain of type III intermediate filament proteins desmin and vimentin.</title>
            <link>http://www.medworm.com/index.php?rid=4476322&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21296452%26dopt%3DAbstract</link>
            <description>This study furthers our knowledge of the interaction between plectin and IF proteins important for maintenance of cytoarchitecture in skeletal muscle. Moreover, binding of plectin to the conserved rod domain of IF proteins could well explain its broad interaction with most types of IFs.
    PMID: 21296452 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476322</comments>
            <pubDate>Fri, 04 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4476322</guid>        </item>
        <item>
            <title>Molecular pathways of platelet factor 4/CXCL4 signaling.</title>
            <link>http://www.medworm.com/index.php?rid=4476323&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21295372%26dopt%3DAbstract</link>
            <description>Authors: Kasper B, Petersen F
    The platelet-derived chemokine CXCL4 takes a specific and unique position within the family of chemotactic cytokines. Today, much attention is directed to CXCL4's capacity to inhibit angiogenesis and to promote innate immune responses, which makes this chemokine an interesting tool and target for potential intervention in tumor growth and inflammation. However, such attempts demand a comprehensive knowledge on the molecular mechanisms and pathways underlying the corresponding cellular functions. At least two structurally different receptors, CXCR3-B and a chondroitin sulfate proteoglycan, are capable of binding CXCL4 and to induce a specific intracellular signaling machinery. While signaling mediated by CXCR3-B involves Gs proteins, elevated cAMP levels, a...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476323</comments>
            <pubDate>Wed, 02 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4476323</guid>        </item>
        <item>
            <title>Regulation of T cell activation by TLR ligands.</title>
            <link>http://www.medworm.com/index.php?rid=4476324&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21292344%26dopt%3DAbstract</link>
            <description>Authors: Oberg HH, Juricke M, Kabelitz D, Wesch D
    Regulatory T cells (Treg) maintain peripheral tolerance and play a critical role in the control of the immune response in infection, tumor defense, organ transplantation and allergy. CD4(+)CD25(high) Treg suppress the proliferation and cytokine production of CD4(+)CD25(-) responder T cells. The suppression requires cell-cell-contact and/or production of inhibitory cytokines like IL-10 or TGF-β. The current knowledge about the regulation of Treg suppressive function is limited. Toll-like receptors (TLR) are widely expressed in the innate immune system. They recognize conserved microbial ligands such as lipopolysaccharide, bacterial lipopeptides or viral and bacterial RNA and DNA. TLR play an essential role in innate immune responses and...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476324</comments>
            <pubDate>Tue, 01 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4476324</guid>        </item>
        <item>
            <title>Cellular prion protein localizes to the nucleus of endocrine and neuronal cells and interacts with structural chromatin components.</title>
            <link>http://www.medworm.com/index.php?rid=4476326&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21277044%26dopt%3DAbstract</link>
            <description>This study reveals new avenues for the elucidation of the physiological function of PrP(C) in endocrine and neuronal cells as well as the molecular mechanisms leading to prion diseases.
    PMID: 21277044 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476326</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4476326</guid>        </item>
        <item>
            <title>Rho proteins of plants - Functional cycle and regulation of cytoskeletal dynamics.</title>
            <link>http://www.medworm.com/index.php?rid=4476325&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21277045%26dopt%3DAbstract</link>
            <description>Authors: Mucha E, Fricke I, Schaefer A, Wittinghofer A, Berken A
    Rho-related ROP proteins are molecular switches that essentially regulate a wide variety of processes. Of central interest is their influence on the plant cytoskeleton by which they affect vital processes like cell division, growth, morphogenesis, and pathogen defense. ROPs switch between GTP- and GDP-bound conformations by strictly regulated nucleotide exchange and GTP-hydrolysis, and only the active GTP-form interacts with downstream effectors to ultimately provoke a biological response. However, the mode of action of the engaged regulators and effectors as well as their upstream and downstream interaction partners have long been largely unknown. As opposed to analogous systems in animals and fungi, plants use specific ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4476325</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4476325</guid>        </item>
        <item>
            <title>Homeodomain-only protein HOP is a novel modulator of late differentiation in keratinocytes.</title>
            <link>http://www.medworm.com/index.php?rid=4411880&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256618%26dopt%3DAbstract</link>
            <description>Authors: Obarzanek-Fojt M, Favre B, Kypriotou M, Ryser S, Huber M, Hohl D
    The homeodomain-only protein (HOP) contains an atypical homeodomain which is unable to bind to DNA due to mutations in residues important for DNA binding. Recently, HOP was reported to regulate proliferation/differentiation homeostasis in different cell types. In the present study, we performed transcriptional profiling of cultured primary human keratinocytes and noted a robust induction of HOP upon calcium-induced cell differentiation. Immunohistochemistry of human skin localized HOP to the granular layer in the epidermis. Overexpression of HOP using a lentiviral vector up-regulated FLG and LOR expression during keratinocyte differentiation. Conversely, decreasing HOP expression using small interfering RNA marke...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411880</comments>
            <pubDate>Thu, 20 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411880</guid>        </item>
        <item>
            <title>Actin regulation in the malaria parasite.</title>
            <link>http://www.medworm.com/index.php?rid=4411879&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256619%26dopt%3DAbstract</link>
            <description>Authors: Sattler JM, Ganter M, Hliscs M, Matuschewski K, Schüler H
    Many intracellular pathogens hijack host cell actin or its regulators for cell-to-cell spreading. In marked contrast, apicomplexan parasites, obligate intracellular, single cell eukaryotes that are phylogenetically older than the last common ancestor of animals and plants, employ their own actin cytoskeleton for active motility through tissues and invasion of host cells. A hallmark of actin-based motility of the malaria parasite is a minimal set of proteins that potentially regulate microfilament dynamics. An intriguing feature of the Plasmodium motor machinery is the virtual absence of elongated filamentous actin in vivo. Despite this unusual actin regulation sporozoites, the transmission stages that are injected into...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411879</comments>
            <pubDate>Thu, 20 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411879</guid>        </item>
        <item>
            <title>Activity modulation of the bacterial Rho GAP YopE: An inspiration for the investigation of mammalian Rho GAPs.</title>
            <link>http://www.medworm.com/index.php?rid=4411882&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21255863%26dopt%3DAbstract</link>
            <description>Authors: Aepfelbacher M, Roppenser B, Hentschke M, Ruckdeschel K
    The Yersinia enterocolitica Rho GTPase Activating Protein (Rho GAP) YopE belongs to a group of bacterial virulence factors that is translocated into infected target cells by a type three secretion system. Structurally and biochemically YopE resembles eukaryotic Rho GAPs which control various cellular functions by modulating the activity of Rho GTP binding proteins. Here we summarise the published information on cellular effects, Rho protein substrates, compartmentalisation and turnover of YopE. A fascinating picture evolves of how this virulence factor integrates in host cellular regulatory mechanisms to fine tune bacterial pathogenicity.
    PMID: 21255863 [PubMed - as supplied by publisher] (Source: European Journal of ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411882</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411882</guid>        </item>
        <item>
            <title>Yersinia enterocolitica outer protein T (YopT).</title>
            <link>http://www.medworm.com/index.php?rid=4411881&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21255864%26dopt%3DAbstract</link>
            <description>Authors: Schmidt G
    Pathogenic Yersinia strains evade the innate immune responses of the host by producing effector proteins (Yersinia outer proteins (Yops)), which are directly injected into mammalian cells by a type III secretion system (TTSS). One of these effector proteins (YopT) disrupts the actin cytoskeleton of the host cell. YopT is a cysteine protease which cleaves Rho proteins directly upstream of the post-translationally modified cysteine. Thereby, it releases the GTPases from the membrane leading to their inactivation. Besides a biochemical characterisation of the molecular mechanism and substrate specificity also delivery into host cells with chaperone binding and guidance to the injection apparatus and the patho-physiological role of YopT have been studied and are summaris...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411881</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411881</guid>        </item>
        <item>
            <title>Role of Abl and Src family kinases in actin-cytoskeletal rearrangements induced by the Helicobacter pylori CagA protein.</title>
            <link>http://www.medworm.com/index.php?rid=4411884&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21247656%26dopt%3DAbstract</link>
            <description>Authors: Tegtmeyer N, Backert S
    The clinical outcome of infections with Helicobacter pylori is determined by a complex interplay of host-pathogen interactions, and persistent infection with this pathogen is the major cause of developing chronic gastritis, peptic ulcers and gastric cancer. Highly virulent strains encode a so-called type IV secretion system which translocates the CagA effector protein into gastric epithelial target cells. Injected CagA becomes tyrosine-phosphorylated on EPIYA sequence motifs by Src and Abl family kinase members. CagA then binds to and activates/inactivates various signalling proteins in a phosphorylation-dependent and phosphorylation-independent manner. In this way injected CagA can act as a master key that evolved during evolution the ability to highjac...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411884</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411884</guid>        </item>
        <item>
            <title>New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin.</title>
            <link>http://www.medworm.com/index.php?rid=4411883&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21247657%26dopt%3DAbstract</link>
            <description>Authors: Barth H, Aktories K
    The C2 toxin from Clostridium botulinum represents the prototype of the family of binary actin-ADP-ribosylating toxins. These toxins covalently transfer ADP-ribose from nicotinamide adenine dinucleotide (NAD(+)) onto arginine-177 of actin in the cytosol of eukaryotic cells resulting in depolymerization of actin filaments and cell rounding. The C2 toxin consists of two non-linked proteins, the enzyme component C2I and the binding and translocation component C2II, which delivers C2I into host cells. The ADP-ribosyltransferase SpvB from Salmonella enterica also modifies actin, but is delivered into the host cell cytosol from intracellular growing Salmonella, most likely via type-III-secretion. We characterized the mode of action of SpvB in comparison to C2 tox...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411883</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411883</guid>        </item>
        <item>
            <title>Structural insights into Met receptor activation.</title>
            <link>http://www.medworm.com/index.php?rid=4411885&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21242015%26dopt%3DAbstract</link>
            <description>Authors: Niemann HH
    The receptor tyrosine kinase Met plays a pivotal role in vertebrate development and tissue regeneration, its deregulation contributes to cancer. Met is also targeted during the infection by the facultative intracellular bacterium Listeria monocytogenes. The mechanistic basis for Met activation by its natural ligand hepatocyte growth factor/scatter factor (HGF/SF) is only beginning to be understood at a structural level. Crystal structures of Met in complex with L. monocytogenes InlB suggest that Met dimerization by this bacterial invasion protein is mediated by a dimer contact of the ligand. Here, I review the structural basis of Met activation by InlB and highlight parallels and differences to the physiological Met ligand HGF/SF and its splice variant NK1.
    PMID...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411885</comments>
            <pubDate>Sat, 15 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411885</guid>        </item>
        <item>
            <title>The &quot;A Disintegrin And Metalloproteases&quot; ADAM10 and ADAM17: Novel drug targets with therapeutic potential?</title>
            <link>http://www.medworm.com/index.php?rid=4346593&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21194787%26dopt%3DAbstract</link>
            <description>The &quot;A Disintegrin And Metalloproteases&quot; ADAM10 and ADAM17: Novel drug targets with therapeutic potential?
    Eur J Cell Biol. 2010 Dec 29;
    Authors: Saftig P, Reiss K
    Proteolytic ectodomain release, a process known as &quot;shedding&quot;, has been recognised as a key mechanism for regulating the function of a diversity of cell surface proteins. A Disintegrin And Metalloproteinases (ADAMs) have emerged as the major proteinase family that mediates ectodomain shedding. Dysregulation of ectodomain shedding is associated with autoimmune and cardiovascular diseases, neurodegeneration, infection, inflammation and cancer. Therefore, ADAMs are increasingly regarded as attractive targets for novel therapies. ADAM10 and its close relative ADAM17 (TNF-alpha converting enzyme (TACE)) have been studied ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4346593</comments>
            <pubDate>Wed, 29 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4346593</guid>        </item>
        <item>
            <title>Wnt signaling in macrophages: Augmenting and inhibiting mycobacteria-induced inflammatory responses.</title>
            <link>http://www.medworm.com/index.php?rid=4346594&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21185106%26dopt%3DAbstract</link>
            <description>Authors: Schaale K, Neumann J, Schneider D, Ehlers S, Reiling N
    Wnt proteins are secreted, palmitoylated glycoproteins with multiple functions in cell proliferation and migration as well as tissue organization. They are best known for their role in embryonic development and tissue homeostasis. In the last years, Wnt signaling was also shown to be involved in the regulation of inflammatory processes: Wnt5a is induced in human macrophages in response to mycobacteria and conserved bacterial structures and contributes to the regulation of pro-inflammatory cytokines via its receptor Frizzled (Fzd) 5. Wnt5a is also induced in other infectious and inflammatory diseases such as tuberculosis, sepsis, psoriasis, rheumatoid arthritis and atherosclerosis. In contrast, Wnt3a, a ligand of Fzd1, is c...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4346594</comments>
            <pubDate>Wed, 22 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4346594</guid>        </item>
        <item>
            <title>Viral Interleukin-6: Structure, pathophysiology and strategies of neutralization.</title>
            <link>http://www.medworm.com/index.php?rid=4346596&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21176991%26dopt%3DAbstract</link>
            <description>Authors: Suthaus J, Adam N, Grötzinger J, Scheller J, Rose-John S
    Viral Interleukin-6 (vIL-6) is encoded by Human herpes virus 8 (HHV8), also known as Kaposi's sarcoma (KS)-associated herpes virus (KSHV). HHV8 infection is found in patients with KS, primary effusion lymphoma (PEL) and plasma cell-type of multicentric Castleman's disease (MCD), with a high incidence observed in HIV infected individuals. vIL-6 shares about 25% identity with its human counterpart. Human IL-6 (hIL-6) binds to the human IL-6 receptor (hIL-6R) and the hIL-6/hIL-6R complex associates with the signaling receptor subunit gp130. Upon dimerization of gp130 intracellular signaling is initiated. All cells in the body express gp130 but only some cell types express the hIL-6R. Human IL-6 does not stimulate cells, wh...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4346596</comments>
            <pubDate>Mon, 20 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4346596</guid>        </item>
        <item>
            <title>Distinct roles of JNK-1 and ERK-2 isoforms in permeability barrier repair and wound healing.</title>
            <link>http://www.medworm.com/index.php?rid=4346595&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21176992%26dopt%3DAbstract</link>
            <description>Authors: Koehler K, Mielke K, Schunck M, Neumann C, Herdegen T, Proksch E
    c-Jun N-terminal kinases (JNKs, also called stress activated protein kinases) and the extra-cellular signal responsive kinases (ERKs) exert different functions in mitogenesis, maturation and differentiation of immune and epithelial cells. We investigated specific functions of individual JNK and ERK isoforms in skin permeability barrier repair and in wound healing. JNK1, but not JNK2 or JNK3, deficient mice revealed a delay in the permeability barrier repair after superficial injury to the skin (tape-stripping) as well as a delay in the healing of full skin thickness wounds. Skin barrier injury induced an increase in epidermal JNK1 enzyme activity in mouse skin in vivo, and JNK1 activity correlated with the degree...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4346595</comments>
            <pubDate>Mon, 20 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4346595</guid>        </item>
        <item>
            <title>Tyrosine phosphorylation of VE-cadherin and claudin-5 is associated with TGF-β1-induced permeability of centrally derived vascular endothelium.</title>
            <link>http://www.medworm.com/index.php?rid=4279762&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21168935%26dopt%3DAbstract</link>
            <description>This study aimed to test the hypothesis that transforming growth factor (TGF)-β1 increases the paracellular permeability of vascular endothelial monolayers through tyrosine phosphorylation of VE-cadherin and claudin-5. Bovine retinal and human brain capillary endothelial cells were grown as monolayers on coated polycarbonate membranes. Paracellular permeability was studied by measuring the equilibration of (14)C-inulin or fluorescence-labelled dextran. Changes in VE-cadherin and claudin-5 expression were studied by immunocytochemistry (ICC) and quantified by cell-based enzyme linked immunosorbent assays (ELISA). Tyrosine phosphorylation of VE-cadherin and claudin-5 was studied by ICC, immunoprecipitation and Western blotting. We found that exposure of endothelial cells to TGF-β1 caused a...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279762</comments>
            <pubDate>Fri, 17 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279762</guid>        </item>
        <item>
            <title>Flanking genes of an essential gene give information about the evolution of metazoa.</title>
            <link>http://www.medworm.com/index.php?rid=4279763&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21163549%26dopt%3DAbstract</link>
            <description>Authors: Zimek A, Weber K
    We collected as much information as possible on new lamin genes and their flanking genes. The number of lamin genes varies from 1 to 4 depending more or less on the phylogenetic position of the species. Strong genome drift is recognised by fewer and unusually placed introns and a change in flanking genes. This applies to the nematode Caenorhabditis elegans, the insect Drosophila melanogaster, the urochordate Ciona intestinalis, the annelid Capitella teleta and the planaria Schmidtea mediterranea. In contrast stable genomes show astonishing conservation of the flanking genes. These are identical in the sea anemone Nematostella vectensis and the cephalochordate Branchiostoma floridae lamin B1 gene. Even in the lamin B1 genes from Xenopus tropicalis and man one o...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279763</comments>
            <pubDate>Tue, 14 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279763</guid>        </item>
        <item>
            <title>Tropomodulins are negative regulators of neurite outgrowth.</title>
            <link>http://www.medworm.com/index.php?rid=4279765&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21146252%26dopt%3DAbstract</link>
            <description>Authors: Fath T, Fischer RS, Dehmelt L, Halpain S, Fowler VM
    Regulation of the actin cytoskeleton is critical for neurite formation. Tropomodulins (Tmods) regulate polymerization at actin filament pointed ends. Previous experiments using a mouse model deficient for the neuron specific isoform Tmod2 suggested a role for Tmods in neuronal function by impacting processes underlying learning and memory. However, the role of Tmods in neuronal function on the cellular level remains unknown. Immunofluorescence localization of the neuronal isoforms Tmod1 and Tmod2 in cultured rat primary hippocampal neurons revealed that Tmod1 is enriched along the proximal part of F-actin bundles in lamellipodia of spreading cells and in growth cones of extending neurites, while Tmod2 appears largely cytoplas...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279765</comments>
            <pubDate>Thu, 09 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279765</guid>        </item>
        <item>
            <title>The complex interplay of NOD-like receptors and the autophagy machinery in the pathophysiology of Crohn disease.</title>
            <link>http://www.medworm.com/index.php?rid=4279764&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21146253%26dopt%3DAbstract</link>
            <description>Authors: Billmann-Born S, Lipinski S, Böck J, Till A, Rosenstiel P, Schreiber S
    Several coding variants of NOD2 and ATG16L1 are associated with increased risk of Crohn disease (CD). NOD2, a cytosolic receptor of the innate immune system activates pro-inflammatory signalling cascades upon recognition of bacterial muramyl dipeptide, but seems also to be involved in antiviral and anti-parasitic defence programs. The CD associated variant L1007fsinsC leads to impaired pro-inflammatory signalling and diminished bacterial clearance. ATG16L1 is a protein essential for autophagosome formation at the phagophore assembly site. The CD associated T300A variant is located in the c-terminal WD40 domain, whose function is still unknown. Basal autophagy is not affected by the T300A variant, but antib...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279764</comments>
            <pubDate>Thu, 09 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279764</guid>        </item>
        <item>
            <title>The soluble Interleukin 6 receptor: Generation and role in inflammation and cancer.</title>
            <link>http://www.medworm.com/index.php?rid=4279766&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21145125%26dopt%3DAbstract</link>
            <description>Authors: Chalaris A, Garbers C, Rabe B, Rose-John S, Scheller J
    Soluble cytokine receptors are frequently found in human serum, most of them possessing antagonistic properties. The Interleukin 6 receptor (IL-6R) is found as a transmembrane protein on hepatocytes and subsets of leukocytes, but soluble isoforms of the IL-6R (sIL-6R) are generated by alternative splicing or by limited proteolysis of the ADisintegrin And Metalloproteinases (ADAM) gene family members ADAM10 and ADAM17. Importantly, the sIL-6R in complex with its ligand Interleukin 6 (IL-6) has agonistic functions and requires cells expressing the signal transducing ß-receptor gp130 but not the membrane-bound IL-6R. We have called this process IL-6 trans-signaling. Naturally occurring isoforms of soluble gp130 (sgp130), whi...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279766</comments>
            <pubDate>Tue, 07 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279766</guid>        </item>
        <item>
            <title>gp130 on macrophages/granulocytes modulates inflammation during experimental tuberculosis.</title>
            <link>http://www.medworm.com/index.php?rid=4279769&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21144615%26dopt%3DAbstract</link>
            <description>Authors: Sodenkamp J, Behrends J, Förster I, Müller W, Ehlers S, Hölscher C
    gp130 is a common receptor chain for cytokines such as interleukin (IL)-27 and IL-6. During experimental tuberculosis (TB), IL-27 prevents optimal antimycobacterial protection and limits the pathological sequelae of chronic inflammation. The anti-inflammatory properties of IL-27 have been attributed mainly to its suppressive effect on T helper (TH) cells. However, because gp130 cytokines also suppress the inflammatory immune response of macrophages, IL-27 may also regulate inflammation by limiting the secretion of pro-inflammatory cytokines. To specifically address the role of gp130 cytokines on macrophages, the outcome of experimental TB was analysed in macrophage/neutrophil-specific gp130-deficient (LysM(c...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279769</comments>
            <pubDate>Mon, 06 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279769</guid>        </item>
        <item>
            <title>Subcellular compartmentalization of TNF receptor-1 and CD95 signaling pathways.</title>
            <link>http://www.medworm.com/index.php?rid=4279768&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21144616%26dopt%3DAbstract</link>
            <description>We report on the regulation of NF-κB signaling by recruitment of the endosomal E3-ubiquitin ligases CARP-2 and CARP-1 during TNF-receptosome trafficking. The biological significance of TNF receptor-1 compartmentalization is demonstrated by the strategy of adenoviruses to impede TNF-R1 internalization and by this preventing host cell apoptosis.
    PMID: 21144616 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279768</comments>
            <pubDate>Mon, 06 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279768</guid>        </item>
        <item>
            <title>The German Collaborative Research Center 415 &quot;Specificity and Pathophysiology of Signal Transduction Pathways&quot;</title>
            <link>http://www.medworm.com/index.php?rid=4279767&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21144617%26dopt%3DAbstract</link>
            <description>The German Collaborative Research Center 415 &quot;Specificity and Pathophysiology of Signal Transduction Pathways&quot;
    Eur J Cell Biol. 2010 Dec 6;
    Authors: Kabelitz D
    
    PMID: 21144617 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279767</comments>
            <pubDate>Mon, 06 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279767</guid>        </item>
        <item>
            <title>Functional implications of lethal toxin-catalysed glucosylation of (H/K/N)Ras and Rac1 in Clostridium sordellii-associated disease.</title>
            <link>http://www.medworm.com/index.php?rid=4252293&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21134703%26dopt%3DAbstract</link>
            <description>Authors: Genth H, Just I
    Clostridium sordellii-based diseases in humans and livestock rely on the activity of the major virulence factors, the single-chain protein toxins TcsL and TcsH, both belonging to the large clostridial glucosylating toxins. TcsL exclusively glucosylates Rho and Ras low molecular weight GTP-binding proteins. TcsL-induced loss of barrier function in epithelial (diarrhoea) and endothelial cells (extravasation of blood fluid) is based on Rac glucosylation whereas induction of apoptosis results from glucosylation of Ras. Intracellular glucosylation of Rac and Ras can be tracked by immunoblot applying the glucosylation-sensitive antibodies Rac1(Mab 102) and Ras(Mab 27H5). Induction of apoptosis especially of phagocytotic cells is crucial for the severity of C. sordell...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252293</comments>
            <pubDate>Sat, 04 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252293</guid>        </item>
        <item>
            <title>The Ras related GTPase Miro is not required for mitochondrial transport in Dictyostelium discoideum.</title>
            <link>http://www.medworm.com/index.php?rid=4252294&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21131095%26dopt%3DAbstract</link>
            <description>Authors: Vlahou G, Eliáš M, von Kleist-Retzow JC, Wiesner RJ, Rivero F
    Ras-related GTPases of the Miro family have been implicated in mitochondrial homeostasis and microtubule-dependent transport. They consist of two GTP-binding domains separated by calcium-binding motifs and of a C-terminal transmembrane domain that targets the protein to the outer mitochondrial membrane. We disrupted the single Miro-encoding gene in Dictyostelium discoideum and observed a substantial growth defect that we attribute to a decreased mitochondrial mass and cellular ATP content. However, mutant cells even showed an increased rate of oxygen consumption, while glucose consumption, mitochondrial transmembrane potential and production of reactive oxygen species were unaltered. Processes characteristic of th...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252294</comments>
            <pubDate>Fri, 03 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252294</guid>        </item>
        <item>
            <title>Actin dynamics at intracellular membranes: The Spir/formin nucleator complex.</title>
            <link>http://www.medworm.com/index.php?rid=4252296&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21129813%26dopt%3DAbstract</link>
            <description>Authors: Kerkhoff E
    The assembly of actin monomers into filaments is a highly regulated basic cellular function. The structural organization of a cell, morphological changes or cell motility is dependent on actin filament dynamics. While within the last decade substantial knowledge has been acquired about actin dynamics at the cell membrane, today only little is known about the actin cytoskeleton and its functions at intracellular endosomal and organelle membranes. The Spir actin nucleators are specifically targeted towards endosomal membranes by a FYVE zinc finger membrane localization domain, and provide an important link to study the role of actin dynamics in the regulation of intracellular membrane transport. Spir proteins are the founding members of a novel class of actin nucleati...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252296</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252296</guid>        </item>
        <item>
            <title>Impact of death receptor signaling on the malignancy of pancreatic ductal adenocarcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=4252295&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21129814%26dopt%3DAbstract</link>
            <description>Authors: Röder C, Trauzold A, Kalthoff H
    Pancreatic ductal adenocarcinoma, PDAC, is a type of tumor with late diagnosis, rapid progression and poor prognosis. It is mostly unresponsive to chemo- and radiation therapy due to a marked resistance against apoptosis induction via both the intrinsic and extrinsic pathway. Accordingly, also activation of death receptors of the TNF-receptor superfamily does not or hardly induces apoptosis in PDAC cells. The reasons for this resistance include expression of multiple inhibitory proteins that block apoptotic signaling at almost every step of the signaling cascade. Moreover and more importantly, death receptors such as CD95/Fas, TRAIL-R1/-R2 and TNF-R1 exhibit marked non-apoptotic functions after ligand binding leading to strong proinflammatory r...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252295</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252295</guid>        </item>
        <item>
            <title>Insights into the molecular regulation of FasL (CD178) biology.</title>
            <link>http://www.medworm.com/index.php?rid=4252298&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21126798%26dopt%3DAbstract</link>
            <description>Authors: Lettau M, Paulsen M, Schmidt H, Janssen O
    Fas ligand (FasL, CD95L, APO-1L, CD178, TNFSF6, APT1LG1) is the key death factor of receptor-triggered programmed cell death in immune cells. FasL/Fas-dependent apoptosis plays a pivotal role in activation-induced cell death, termination of immune responses, elimination of autoreactive cells, cytotoxic effector function of T and NK cells, and the establishment of immune privilege. Deregulation or functional impairment of FasL threatens the maintenance of immune homeostasis and defense and results in severe autoimmunity. In addition, FasL has been implicated as an accessory or costimulatory receptor in T cell activation. The molecular mechanisms underlying this reverse signaling capacity are, however, poorly understood and still controv...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252298</comments>
            <pubDate>Tue, 30 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252298</guid>        </item>
        <item>
            <title>The Notch signaling pathway: Molecular basis of cell context dependency.</title>
            <link>http://www.medworm.com/index.php?rid=4252297&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21126799%26dopt%3DAbstract</link>
            <description>Authors: Schwanbeck R, Martini S, Bernoth K, Just U
    Notch receptor signaling controls cell-fate specification, self-renewal, differentiation, proliferation and apoptosis throughout development and regeneration in all animal species studied to date. Its dysfunction causes several developmental defects and diseases in the adult. A key feature of Notch signaling is its remarkable cell-context dependency. In this review, we summarize the influences of the cellular context that regulate Notch activity and propose a model how the interplay between the cell-intrinsically established chromatin state and the cell-extrinsic signals that modify chromatin may select for Notch target accessibility and activation in different cellular contexts.
    PMID: 21126799 [PubMed - as supplied by publisher] ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252297</comments>
            <pubDate>Tue, 30 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252297</guid>        </item>
        <item>
            <title>Glycine-induced cytoprotection is mediated by ERK1/2 and AKT in renal cells with ATP depletion.</title>
            <link>http://www.medworm.com/index.php?rid=4252299&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21122942%26dopt%3DAbstract</link>
            <description>Authors: Jiang L, Qin X, Zhong X, Liu L, Jiang L, Lu Y, Fan L, He Z, Chen Q
    Glycine receptor (GlyR) activation by glycine protects cells against ATP depletion. However, the underlying mechanisms remain unclear. To define signaling pathways responsible for the GlyR mediated cytoprotection, we examined the phosphorylation status of key kinases signaling pathways in Madin-Darby canine kidney (MDCK) cells. Our results indicated that growing the ATP-depleted MDCK cells in glycine-containing media increased the level of phosphorylated extracellular signal-regulated kinase 1 and 2 (ERK1/2), Ets-like transcription factor-1 (Elk1), AKT, and Forkhead box O-class 1 (FoxO1), decreased the level of phosphorylated p38 mitogen-activated protein kinase, while having little effect on the phosphorylatio...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252299</comments>
            <pubDate>Mon, 29 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252299</guid>        </item>
        <item>
            <title>Role of the immediate early response 3 (IER3) gene in cellular stress response, inflammation and tumorigenesis.</title>
            <link>http://www.medworm.com/index.php?rid=4221765&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21112119%26dopt%3DAbstract</link>
            <description>Authors: Arlt A, Schäfer H
    The expression of the early response gene immediate early response 3 (IER3), formerly known as IEX-1, is induced by a great variety of stimuli, such as growth factors, cytokines, ionizing radiation, viral infection and other types of cellular stress. Being of a rather unique protein structure not sharing any similarity to other vertebrate proteins, IER3 plays a complex and to some extent contradictory role in cell cycle control and apoptosis. As outlined in this review, these effects of IER3 relate to an interference with certain signalling pathways, in particular NF-κB, MAPK/ERK and PI3K/Akt. In addition to numerous functional data relying on cell culture based studies, transgenic and knock-out mouse models revealed an involvement of IER3 expression in imm...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4221765</comments>
            <pubDate>Thu, 25 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4221765</guid>        </item>
        <item>
            <title>S-Adenosylmethionine regulates connexins sub-types expressed by hepatocytes.</title>
            <link>http://www.medworm.com/index.php?rid=4202953&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21093098%26dopt%3DAbstract</link>
            <description>Authors: Yamaji S, Droggiti A, Lu SC, Martinez-Chantar ML, Warner A, Varela-Rey M
    Intercellular communication via GAP Junctions plays an important role in tissue homeostasis, apoptosis, carcinogenesis, cell proliferation and differentiation. Hepatocyte connexins (Cx) 26 and 32 levels are decreased during the de-differentiation process of primary hepatocytes in culture, a situation that is also characterized by a decrease in S-Adenosylmethionine (SAMe) levels. In this current study, we show that SAMe supplementation in cultured hepatocytes every 12h, leads to an up-regulation of Cx26 and 32 mRNA and protein levels and blocks culture-induced Cx43 expression, although it failed to increase Cx26 and 32 membrane localization and GAP junction intracellular communication. SAMe reduced nuclear...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4202953</comments>
            <pubDate>Wed, 17 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4202953</guid>        </item>
        <item>
            <title>Role of Rab1b in COPII dynamics and function.</title>
            <link>http://www.medworm.com/index.php?rid=4202952&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21093099%26dopt%3DAbstract</link>
            <description>In this study, we analyze the involvement of Rab1b in COPII dynamics and function by expressing either the Rab1b negative-mutant (Rab1N121I) or the Rab1b GTP restricted mutant (Rab1Q67L), or performing short interference RNA-based knockdown. We show that Rab1b interacts with the COPII components Sec23, Sec24 and Sec31 and that Rab1b inhibition changes the COPII phenotype. FRAP assays reveal that Rab1b modulates COPII association/dissociation kinetics at the ERES interface. Furthermore, Rab1b inhibition delays cargo sorting at the ER exit sites. We postulate that Rab1b is a key regulatory component of COPII dynamics and function.
    PMID: 21093099 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4202952</comments>
            <pubDate>Wed, 17 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4202952</guid>        </item>
        <item>
            <title>Blebbing dynamics during endothelial cell spreading.</title>
            <link>http://www.medworm.com/index.php?rid=4187247&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21087809%26dopt%3DAbstract</link>
            <description>Authors: Norman L, Sengupta K, Aranda-Espinoza H
    Cell spreading is a critical component of numerous physiological phenomena including cancer metastasis, embryonic development, and mitosis. We have previously illustrated that cellular blebs appear after abrupt cell-substrate detachment and play a critical role in regulating membrane tension; however, the dynamics of bleb-substrate interactions during spreading remains unclear. Here we explore the role of blebs during endothelial cell spreading using chemical and osmotic modifications to either induce or inhibit bleb formation. We track cell-substrate dynamics as well as individual blebs using surface sensitive microscopic techniques. Blebbing cells (both control and chemically induced) exhibit increased lag times prior to fast growth. I...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187247</comments>
            <pubDate>Wed, 17 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4187247</guid>        </item>
        <item>
            <title>Differing contributions of LIMK and ROCK to TGFβ-induced transcription, motility and invasion.</title>
            <link>http://www.medworm.com/index.php?rid=4187248&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21074289%26dopt%3DAbstract</link>
            <description>In this study, we made use of siRNA-mediated knockdown and selective inhibitors to determine the contributions of ROCK and LIMK to TGFβ-induced responses. We find that both ROCK and LIMK are required for TGFβ stimulation of serum-response factor (SRF) transcriptional activity and actin stress fibre formation during EMT. In contrast, although LIMK inhibition had little effect on cell motility in scratch wound and Transwell migration assays, ROCK inhibition actually promoted TGFβ-induced cell motility by helping individual cells to break free from the epithelial sheet. Furthermore, we demonstrate that selective inhibition of LIMK, but not ROCK, effectively blocked TGFβ driven invasion through a layer of matrigel extracellular matrix protein. These results indicate that the roles of LIMK ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187248</comments>
            <pubDate>Wed, 10 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4187248</guid>        </item>
        <item>
            <title>Nef does not inhibit F-actin remodelling and HIV-1 cell-cell transmission at the T lymphocyte virological synapse.</title>
            <link>http://www.medworm.com/index.php?rid=4140023&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21044805%26dopt%3DAbstract</link>
            <description>Authors: Haller C, Tibroni N, Rudolph JM, Grosse R, Fackler OT
    Nef, a HIV-1 pathogenesis factor, elevates virus replication in vivo and thus progression to AIDS by incompletely defined mechanisms. As one of its biological properties, Nef enhances the infectivity of cell-free HIV-1 particles in single round infections, however it fails to provide a significant and amplifying growth advantage for HIV-1 on such virus producing cells. A major difference between HIV-1 cell-free single round infections and virus replication kinetics on T lymphocytes consists in the predominant role of cell-associated virus transmission rather than cell-free infection during multiple round virus replication. HIV-1 cell-to-cell transmission occurs across close cell contacts also referred to as virological syna...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4140023</comments>
            <pubDate>Sun, 31 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4140023</guid>        </item>
        <item>
            <title>The effect of MMP inhibitor GM6001 on early fibroblast-mediated collagen matrix contraction is correlated to a decrease in cell protrusive activity.</title>
            <link>http://www.medworm.com/index.php?rid=4140024&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21040999%26dopt%3DAbstract</link>
            <description>Authors: Martin-Martin B, Tovell V, Dahlmann-Noor AH, Khaw PT, Bailly M
    Although fibroblasts play an essential part during the wound healing response, the mechanisms by which they mediate tissue remodelling and contraction are still unclear. Using live cell and matrix imaging within 3D free-floating fibroblast-populated collagen lattices as a model for tissue contraction, we compared the behaviour of a range of fibroblasts with low and high contraction abilities and analysed the effect of the broad spectrum MMP-inhibitor GM6001 on cell behaviour and matrix contraction. We identified two mechanisms underlying matrix contraction, one via direct cell-mediated contractile activity, the second through matrix degradation. These appear to be linked to cell morphology and regulated by the coll...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4140024</comments>
            <pubDate>Sat, 30 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4140024</guid>        </item>
        <item>
            <title>Differential localization and processing of apoptotic proteins in Malpighian tubules of Drosophila during metamorphosis.</title>
            <link>http://www.medworm.com/index.php?rid=4140027&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21035895%26dopt%3DAbstract</link>
            <description>Authors: Shukla A, Tapadia MG
    Drosophila development proceeds through three larval stages, before it pupates to reach adulthood. During pupation, larval tissues are destructed by programmed cell death and replaced by adult structures. Programmed cell death is a tightly regulated process accomplished by the induction of three closely linked pro-apoptotic genes reaper, hid and grim, ultimately leading to the activation of caspases, DRONC and DRICE and results in cell death. Unlike other larval tissues, Malpighian tubules are unique in not undergoing characteristic ecdysone-induced apoptosis and are carried to the adults. In this paper we show that apoptotic proteins, HID, GRIM, DRONC and DRICE are expressed in the Malpighian tubules, however they are sequestered in the nucleus. Significa...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4140027</comments>
            <pubDate>Fri, 29 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4140027</guid>        </item>
        <item>
            <title>Molecular mechanisms of ultraviolet radiation-induced immunosuppression.</title>
            <link>http://www.medworm.com/index.php?rid=4140026&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21035896%26dopt%3DAbstract</link>
            <description>Authors: Schwarz T, Schwarz A
    Solar ultraviolet radiation (UVR) is well known for its immunosuppressive properties. UVR can suppress immune reactions both in a local and a systemic fashion. One of the major molecular mediators of photoimmunosuppression is UVR-induced DNA damage. In contrast to immunosuppressive drugs, UVR does not act in a general but antigen-specific fashion. This is due to the induction of regulatory T cells. Epidermal Langerhans cells harboring UVR-induced DNA damage appear to be essentially involved in the induction of these cells. Cytokines including interleukin (IL)-12, -18 and -23 exert the capacity to reduce UVR-induced DNA damage via induction of DNA repair. Accordingly, these cytokines prevent UVR-mediated immunosuppression. In contrast to IL-18, IL-12 and IL...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4140026</comments>
            <pubDate>Thu, 28 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4140026</guid>        </item>
        <item>
            <title>The structure of the unliganded extracellular domain of the interleukin-6 signal transducer gp130 in solution.</title>
            <link>http://www.medworm.com/index.php?rid=4140025&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21035897%26dopt%3DAbstract</link>
            <description>Authors: Lorenzen I, Shang W, Perbandt M, Petoukhov MV, Svergun DI, Waetzig GH, Rose-John S, Hilgenfeld R, Grötzinger J
    Interleukin-6 (IL-6) plays an important role in immune responses and signals via two different pathways. When IL-6 binds to its non-signalling membrane-bound receptor (IL-6R), a non-covalent dimer of the ubiquitous interleukin-6 signal transducer gp130 is recruited to initiate intracellular signalling cascades. This so-called classical signalling pathway is restricted to cells expressing the membrane-bound IL-6R, such as hepatocytes and certain leukocytes. In addition, an alternative trans-signalling pathway uses soluble forms of IL-6R (sIL-6R) in complex with IL-6 to activate cells expressing gp130, but not membrane-bound IL-6R. In both cases, a tetrameric or hexame...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4140025</comments>
            <pubDate>Thu, 28 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4140025</guid>        </item>
        <item>
            <title>Migration of epithelial cells on laminins: RhoA antagonizes directionally persistent migration.</title>
            <link>http://www.medworm.com/index.php?rid=4108362&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20971525%26dopt%3DAbstract</link>
            <description>Authors: Zhang Z, Chometon G, Wen T, Qu H, Mauch C, Krieg T, Aumailley M
    Spatial and temporal expression of laminin isoforms is assumed to provide specific local information to neighboring cells. Here, we report the remarkably selective presence of LM-111 at the very tip of hair follicles where LM-332 is absent, suggesting that epithelial cells lining the dermal-epidermal junction at this location may receive different signals from the two laminins. This hypothesis was tested in vitro by characterizing with functional and molecular assays the comportment of keratinocytes exposed to LM-111 and LM-332. The two laminins induced morphologically distinct focal adhesions, and LM-332, but not LM-111, elicited persistent migration of keratinocytes. The different impact on cellular behavior was...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4108362</comments>
            <pubDate>Thu, 21 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4108362</guid>        </item>
        <item>
            <title>Specificities of β(1) integrin signaling in the control of cell adhesion and adhesive strength.</title>
            <link>http://www.medworm.com/index.php?rid=4108361&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20971526%26dopt%3DAbstract</link>
            <description>Authors: Régent M, Planus E, Bouin AP, Bouvard D, Brunner M, Faurobert E, Millon-Frémillon A, Block MR, Albiges-Rizo C
    Cells exert actomyosin contractility and cytoskeleton-dependent force in response to matrix stiffness cues. Cells dynamically adapt to force by modifying their behavior and remodeling their microenvironment. This adaptation is favored by integrin activation switch and their ability to modulate their clustering and the assembly of an intracellular hub in response to force. Indeed integrins are mechanoreceptors and mediate mechanotransduction by transferring forces to specific adhesion proteins into focal adhesions which are sensitive to tension and activate intracellular signals. α(5)β(1) integrin is considered of major importance for the formation of an elaborate m...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4108361</comments>
            <pubDate>Thu, 21 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4108361</guid>        </item>
        <item>
            <title>HDAC6 is required for invadopodia activity and invasion by breast tumor cells.</title>
            <link>http://www.medworm.com/index.php?rid=4108363&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970878%26dopt%3DAbstract</link>
            <description>In this report, we examined the role of the histone deacetylase HDAC6 in invadopodia formation and invasion by breast cancer cells. Using small interfering RNA silencing of protein expression in highly invasive MDA-MB-231 breast adenocarcinoma cells, we show that HDAC6 is required for two-dimensional matrix proteolysis. In addition, we demonstrate that HDAC6 acts as a tubulin and cortactin deacetylase. We also report that the inhibition of HDAC6 by siRNA or treatment with HDAC inhibitor TSA results in a decreased invasion capacity of a three-dimensional type I collagen matrix by MDA-MB-231 cells. These data identify HDAC6 as a critical component of the invasive apparatus of tumor cells, in both two- and three-dimensional matrices.
    PMID: 20970878 [PubMed - as supplied by publisher] (Sou...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4108363</comments>
            <pubDate>Wed, 20 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4108363</guid>        </item>
        <item>
            <title>Glycosaminoglycans inhibit the adherence and the spreading of osteoclasts and their precursors: Role in osteoclastogenesis and bone resorption.</title>
            <link>http://www.medworm.com/index.php?rid=4108364&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970218%26dopt%3DAbstract</link>
            <description>Authors: Baud'huin M, Ruiz-Velasco C, Jego G, Charrier C, Gasiunas N, Gallagher J, Maillasson M, Naggi A, Padrines M, Redini F, Duplomb L, Heymann D
    The bone microenvironment (e.g. glycosaminoglycans (GAGs), growth factors) plays a major role in bone resorption, especially in the formation of osteoclasts which differentiate from the hematopoietic lineage in the presence of RANKL. Previous studies revealed that GAGs may influence osteoclastogenesis, but data are very controversial, some studies showing an inhibitory effect of GAGs on osteoclastic differentiation whereas others demonstrated a stimulatory effect. To clarify their activities, we investigated the effect of 5 families of GAGs in three different models of human/mouse osteoclastogenesis. The present data revealed that heparin ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4108364</comments>
            <pubDate>Tue, 19 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4108364</guid>        </item>
        <item>
            <title>Controlling actin cytoskeletal organization and dynamics during neuronal morphogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=4088979&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20965607%26dopt%3DAbstract</link>
            <description>Authors: Kessels MM, Schwintzer L, Schlobinski D, Qualmann B
    Coordinated functions of the actin cytoskeleton and microtubules, which need to be carefully controlled in time and space, are required for the drastic alterations of neuronal morphology during neuromorphogenesis and neuronal network formation. A key process in neuronal actin dynamics is filament formation by actin nucleators, such as the Arp2/3 complex, formins and the brain-enriched, novel WH2 domain-based nucleators Spire and cordon-bleu (Cobl). We here discuss in detail the currently available data on the roles of these actin nucleators during neuromorphogenesis and highlight how their required control at the plasma membrane may be brought about. The Arp2/3 complex was found to be especially important for proper growth co...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088979</comments>
            <pubDate>Mon, 18 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088979</guid>        </item>
        <item>
            <title>Conditional ablation of integrin alpha-6 in mouse epidermis leads to skin fragility and inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=4088978&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20965608%26dopt%3DAbstract</link>
            <description>Authors: Niculescu C, Ganguli-Indra G, Pfister V, Dupé V, Messaddeq N, De Arcangelis A, Georges-Labouesse E
    Hemidesmosomes (HDs) are essential anchorage junctions which mediate the firm attachment of epithelia to the underlying basement membranes, of which one main component is the integrin α6β4. These specific junctions are also able to trigger signalling pathways, via the recruitment and interactions of signalling molecules with HD components such as the cytoplasmic tail of the β4 integrin or the plakin plectin. HDs must also assemble and disassemble depending on the tissue context for example during tissue remodelling. Alterations of HD components or their loss result in skin blistering disorders known as epidermolysis bullosa. Since mice lacking integrin α6 die at birth with s...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088978</comments>
            <pubDate>Mon, 18 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088978</guid>        </item>
        <item>
            <title>p130Cas promotes invasiveness of three-dimensional ErbB2-transformed mammary acinar structures by enhanced activation of mTOR/p70S6K and Rac1.</title>
            <link>http://www.medworm.com/index.php?rid=4088980&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20961652%26dopt%3DAbstract</link>
            <description>In conclusion, high levels of p130Cas favour progression of ErbB2-transformed cells towards an invasive phenotype.
    PMID: 20961652 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088980</comments>
            <pubDate>Sun, 17 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088980</guid>        </item>
        <item>
            <title>Molecular biology of complex functions of botanical systems.</title>
            <link>http://www.medworm.com/index.php?rid=4088982&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20952092%26dopt%3DAbstract</link>
            <description>Authors: Kück U
    
    PMID: 20952092 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088982</comments>
            <pubDate>Thu, 14 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088982</guid>        </item>
        <item>
            <title>The cortactin-binding domain of WIP is essential for podosome formation and extracellular matrix degradation by murine dendritic cells.</title>
            <link>http://www.medworm.com/index.php?rid=4088981&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20952093%26dopt%3DAbstract</link>
            <description>Authors: Bañón-Rodríguez I, Monypenny J, Ragazzini C, Franco A, Calle Y, Jones GE, Antón IM
    In immature dendritic cells (DCs) podosomes form and turn over behind the leading edge of migrating cells. The Arp2/3 complex activator Wiskott-Aldrich Syndrome Protein (WASP) localises to the actin core of forming podosomes together with WASP-Interacting Protein (WIP). A second weaker Arp2/3 activator, cortactin, is also found at podosomes where it has been proposed to participate in matrix metalloproteinase (MMP) secretion. We have previously shown that WIP(-/-) DCs are unable to make podosomes. WIP binds to cortactin and in this report we address whether WIP regulates cortactin-mediated MMP activity. Using DCs derived from splenic murine precursors, we found that wild-type cells were able...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088981</comments>
            <pubDate>Thu, 14 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088981</guid>        </item>
        <item>
            <title>Dynamics of the cyanobacterial photosynthetic network: Communication and modification of membrane protein complexes.</title>
            <link>http://www.medworm.com/index.php?rid=4088983&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20943284%26dopt%3DAbstract</link>
            <description>Authors: Nowaczyk MM, Sander J, Grasse N, Cormann KU, Rexroth D, Bernát G, Rögner M
    Cyanobacterial photosystem 2 and cytochrome b(6)f complexes have been structurally resolved up to the molecular level while the adjustment of their function in response to environmental and intracellular parameters is based on various modifications of these complexes which have not yet been resolved in detail. This minireview summarizes recent results on two central modifications for each complex: (a) for the cytochrome b(6)f complex the implication of PetP, a new subunit, and of three copies of PetC, the Rieske protein, for the fine-tuning of the photosynthetic electron transport is evaluated; (b) for photosystem 2, the heterogeneity of the D1 subunit and the role of subunit Psb27 is discussed in rel...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088983</comments>
            <pubDate>Sun, 10 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088983</guid>        </item>
        <item>
            <title>Histidine is involved in coupling proton uptake to electron transfer in photosynthetic proteins.</title>
            <link>http://www.medworm.com/index.php?rid=4065759&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20934775%26dopt%3DAbstract</link>
            <description>In this study, we investigated the role of the iron-histidine complex located between Q(A) and Q(B). We used time-resolved fast-scan FTIR spectroscopy to characterize the Rb. sphaeroides L210DN RC mutant marked with isotopically labeled histidine. FTIR marker bands of the intermediate X between 1120cm(-1) and 1050cm(-1) are assigned to histidine vibrations and indicate the protonation of a histidine, most likely HisL190, during the disappearance of the intermediate. Based on these results we propose a novel mechanism of the coupling of electron and proton transfer in photosynthesis.
    PMID: 20934775 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4065759</comments>
            <pubDate>Thu, 07 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4065759</guid>        </item>
        <item>
            <title>Nck1 and Grb2 localization patterns can distinguish invadopodia from podosomes.</title>
            <link>http://www.medworm.com/index.php?rid=4000224&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20850195%26dopt%3DAbstract</link>
            <description>Authors: Oser M, Dovas A, Cox D, Condeelis J
    Invadopodia are matrix-degrading ventral cell surface structures formed in invasive carcinoma cells. Podosomes are matrix-degrading structures formed in normal cell types including macrophages, endothelial cells, and smooth muscle cells that are believed to be related to invadopodia in function. Both invadopodia and podosomes are enriched in proteins that regulate actin polymerization including proteins involved in N-WASp/WASp-dependent Arp2/3-complex activation. However, it is unclear whether invadopodia and podosomes use distinct mediators for N-WASp/WASp-dependent Arp2/3-complex activation. We investigated the localization patterns of the upstream N-WASp/WASp activators Nck1 and Grb2 in invadopodia of metastatic mammary carcinoma cells, p...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4000224</comments>
            <pubDate>Tue, 14 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4000224</guid>        </item>
        <item>
            <title>Structure and function of native and refolded peridinin-chlorophyll-proteins from dinoflagellates.</title>
            <link>http://www.medworm.com/index.php?rid=4000225&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20846743%26dopt%3DAbstract</link>
            <description>Authors: Schulte T, Johanning S, Hofmann E
    Peridinin-chlorophyll a-proteins are a class of light-harvesting proteins only found in photosynthetic dinoflagellates. Due to their exceptional stability they are an excellent model system to study carotenoid to chlorophyll energy transfer. We were able to solve structures of these complexes at near atomic resolution, allowing the detailed discussion of pigment-pigment and pigment-protein interactions. Using a refolding system, we also determined structures of complexes with mutated apoproteins and modified pigment compositions. Here we summarize the current understanding of PCP structures, with an emphasis on how the basic dimeric structure may be modified in the oligomeric state of these complexes.
    PMID: 20846743 [PubMed - as supplied b...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4000225</comments>
            <pubDate>Mon, 13 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4000225</guid>        </item>
        <item>
            <title>The native structure of cytoplasmic dynein at work translocating vesicles in Paramecium.</title>
            <link>http://www.medworm.com/index.php?rid=3973826&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20837374%26dopt%3DAbstract</link>
            <description>Authors: Ishida M, Aihara MS, Allen RD, Fok AK
    In Paramecium multimicronucleatum, the discoidal vesicles, the acidosomes and the 100-nm carrier vesicles are involved in phagosome formation, phagosome acidification and endosomal processing, respectively. Numerous cross bridges link these vesicles to the kinetic side of the microtubules of a cytopharyngeal microtubular ribbon. Vesicles are translocated along these ribbons in a minus-end direction towards the cytopharynx. A monoclonal antibody specific for the light vanadate-photocleaved fragment of the heavy chain of cytoplasmic dynein was used to show that this dynein is located between the discoidal vesicles and the ribbons as well as on the cytosolic surface of the acidosomes and the 100-nm carrier vesicles. This antibody inhibited th...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3973826</comments>
            <pubDate>Fri, 10 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3973826</guid>        </item>
        <item>
            <title>Interactions in the pollen-specific receptor-like kinases-containing signaling network.</title>
            <link>http://www.medworm.com/index.php?rid=3973828&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20832899%26dopt%3DAbstract</link>
            <description>Authors: LÃ¶cke S, Fricke I, Mucha E, Humpert ML, Berken A
    The pollen-specific receptor-like kinases (PRKs) from Solanum lycopersicum, LePRK1 and LePRK2, are believed to be involved in the regulation of pollen germination and pollen tube growth. They appear to be part of a multimeric complex in which the transmembranic LePRKs presumably have a key position in transducing exogenous signals through the plasma membrane. Here, we focused on extra- and intracellular interactions involving the LePRKs. We show in yeast two-hybrid experiments a cross-interaction of putative PRK-ligands, the oligomerization of LePRK2 and a direct contact of LePRKs to activated Rho proteins of plants (ROPs). Moreover, we observed that pollen-specific RopGEFs, which catalyze ROP activation and may be regulated ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3973828</comments>
            <pubDate>Thu, 09 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3973828</guid>        </item>
        <item>
            <title>RIP3 and AtKinesin-13A - A novel interaction linking Rho proteins of plants to microtubules.</title>
            <link>http://www.medworm.com/index.php?rid=3973827&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20832900%26dopt%3DAbstract</link>
            <description>Authors: Mucha E, Hoefle C, HÃ¼ckelhoven R, Berken A
    RIP3 belongs to a group of recently identified proteins, classified as the ICR/RIP family whose members were described to interact with Rho proteins of plants (ROPs). Our in vivo and in vitro data demonstrate that RIP3 is a true ROP effector, interacting specifically with the active form of ROPs. We found that RIP3 has properties and cellular roles different from the previously described RIP family member ICR1/RIP1. We show that RIP3 is localized at microtubules and interacts with the kinesin-13 family member AtKinesin-13A, suggesting a role for RIP3 in microtubule reorganization and a possible function in ROP-regulated polar growth.
    PMID: 20832900 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3973827</comments>
            <pubDate>Wed, 08 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3973827</guid>        </item>
        <item>
            <title>Transparent peer review-An appreciation of the reviewers' contribution to a published article.</title>
            <link>http://www.medworm.com/index.php?rid=3956646&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20813427%26dopt%3DAbstract</link>
            <description>Authors: Linder S, Schliwa M, Werner S, Gebauer D
    
    PMID: 20813427 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3956646</comments>
            <pubDate>Mon, 30 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3956646</guid>        </item>
        <item>
            <title>Macrophage podosomes go 3D.</title>
            <link>http://www.medworm.com/index.php?rid=3916040&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20801545%26dopt%3DAbstract</link>
            <description>In conclusion, human macrophage podosomes go 3D and take the shape of spherical podosome rosettes when the cells perform mesenchymal migration. This work sets the scene for future studies of molecular and cellular processes regulating macrophage trans-migration.
    PMID: 20801545 [PubMed - as supplied by publisher] (Source: European Journal of Cell Biology)</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3916040</comments>
            <pubDate>Thu, 26 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3916040</guid>        </item>
        <item>
            <title>NO (nitric oxide): The ring master.</title>
            <link>http://www.medworm.com/index.php?rid=3916041&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20800929%26dopt%3DAbstract</link>
            <description>Authors: Sinha S, Sridhara SR, Srinivasan S, Muley A, Majumder S, Kuppusamy M, Gupta R, Chatterjee S
    The migration and proliferation of endothelial cells affect the process of angiogenesis or the formation of blood vessels. Endothelial cells interact with each other to form ring-like structures in monolayers and tubular structures in matrigels. However, the transit phase between the individual endothelial cells and fully formed tubular structures is yet to be established. Guided by imaging, Western blot analysis, drug perturbation studies and siRNA studies we validate that endothelial ring structures are the fundamental and monomeric units of capillary tubes and nitric oxide is implicated in their fabrication. Giving input from experimental data, we used bagging classifier and informat...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3916041</comments>
            <pubDate>Wed, 25 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3916041</guid>        </item>
        <item>
            <title>Sordaria macrospora, a model organism to study fungal cellular development.</title>
            <link>http://www.medworm.com/index.php?rid=3916042&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20739093%26dopt%3DAbstract</link>
            <description>Authors: Engh I, Nowrousian M, KÃ¼ck U
    During the development of multicellular eukaryotes, the processes of cellular growth and organogenesis are tightly coordinated. Since the 1940s, filamentous fungi have served as genetic model organisms to decipher basic mechanisms underlying eukaryotic cell differentiation. Here, we focus on Sordaria macrospora, a homothallic ascomycete and important model organism for developmental biology. During its sexual life cycle, S. macrospora forms three-dimensional fruiting bodies, a complex process involving the formation of different cell types. S. macrospora can be used for genetic, biochemical and cellular experimental approaches since diverse tools, including fluorescence microscopy, a marker recycling system and gene libraries, are available. Mor...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3916042</comments>
            <pubDate>Sun, 22 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3916042</guid>        </item>
        <item>
            <title>Tight junctions form a barrier in human epidermis.</title>
            <link>http://www.medworm.com/index.php?rid=3901375&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20732726%26dopt%3DAbstract</link>
            <description>Authors: Kirschner N, Houdek P, Fromm M, Moll I, Brandner JM
    Tight junctions (TJ) are cell-cell junctions that have proved to form a paracellular barrier for solutes and water between cells of epithelia, including the stratum granulosum of the stratified epithelium of the epidermis of newborn mice. In mice lacking claudin-1, a major barrier-forming TJ component, this barrier was abolished. However, the role of TJ in human skin is controversially discussed as unambiguous data were missing so far. Here, we investigated TJ barrier function in healthy human skin as well as in skin samples from psoriatic lesions which are characterized by an altered localization of TJ proteins. We demonstrate for human skin that occludin- and claudin-1-positive sites in the stratum granulosum form a barrier...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901375</comments>
            <pubDate>Fri, 20 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901375</guid>        </item>
        <item>
            <title>The non-redundant role of N-WASP in podosome-mediated matrix degradation in macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=3901374&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20732727%26dopt%3DAbstract</link>
            <description>Authors: Nusblat LM, Dovas A, Cox D
    Wiskott-Aldrich Syndrome Protein (WASP) is a hematopoietic cell-specific regulator of Arp2/3-dependent actin polymerization. Despite the presence of the highly homologous N-WASP (neural-WASP), macrophages from WAS patients are devoid of podosomes, adhesion structures in cells of the monocytic lineage capable of matrix degradation via matrix metalloproteases (MMPs), suggesting that WASP and N-WASP play unique roles in macrophages. To determine whether N-WASP also plays a unique role in macrophage function, N-WASP expression was reduced using silencing RNA in a sub-line of RAW 264.7 macrophages (RAW/LR5). Similar to reduction in WASP levels, cells with reduced N-WASP levels were rounder and less polarized. Interestingly, podosomes still formed when N-W...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901374</comments>
            <pubDate>Fri, 20 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901374</guid>        </item>
        <item>
            <title>PTRF-cavin-1 expression decreases the migration of PC3 prostate cancer cells: Role of matrix metalloprotease 9.</title>
            <link>http://www.medworm.com/index.php?rid=3901373&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20732728%26dopt%3DAbstract</link>
            <description>Authors: Aung CS, Hill MM, Bastiani M, Parton RG, Parat MO
    Caveolae are specialized plasma membrane subdomains with a distinct lipid and protein composition, which play an essential role in cell physiology by performing trafficking and signalling functions. The structure and functions of caveolae have been shown to require caveolin-1, a major protein component of caveolae. Caveolin-1 expression and secretion are increased in metastatic prostate cancer, and caveolin-1 seems to contribute to prostate cancer growth and metastasis. Recently, a cytoplasmic protein named PTRF (Polymerase I and Transcript Release Factor) or cavin-1 was found to be required, in concert with caveolin-1, for the formation and functions of caveolae. Genetic ablation of PTRF results in loss of caveolae while caveo...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901373</comments>
            <pubDate>Fri, 20 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901373</guid>        </item>
        <item>
            <title>Identification of PEX33, a novel component of the peroxisomal docking complex in the filamentous fungus Neurospora crassa.</title>
            <link>http://www.medworm.com/index.php?rid=3901376&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20728240%26dopt%3DAbstract</link>
            <description>In this report we isolated PEX14 complexes of Neurospora crassa. Among the complex constituents, one protein designated as PEX33 possessed homology to PEX14 but only in a short N-terminal domain. The PEX14/PEX33 interaction was verified by means of two-hybrid analysis. Moreover, PEX33 was shown to interact with itself and the PTS1-receptor PEX5. Localization studies demonstrated that PEX33 constitutes a glyoxysomal protein. Growth tests of the pex33 deletion strain revealed a defect of this strain in the biogenesis of glyoxysomes and Woronin bodies. As the function of PEX33 was not redundant to that of PEX14, it is a genuine novel peroxin. Based on our experimental data, the function of PEX33 seems to resemble that of yeast PEX17 despite clear structural differences.
    PMID: 20728240 [Pu...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901376</comments>
            <pubDate>Wed, 18 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901376</guid>        </item>
        <item>
            <title>The carboxyl tail of Cx43 augments p38 mediated cell migration in a gap junction-independent manner.</title>
            <link>http://www.medworm.com/index.php?rid=3901378&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20727616%26dopt%3DAbstract</link>
            <description>Authors: Behrens J, Kameritsch P, Wallner S, Pohl U, Pogoda K
    The expression of connexin 43 (Cx43) has been shown to correlate with an enhanced migration of several cell types such as glioma or neural crest cells, but the mechanism remains unclear. We studied whether Cx43 also affects migration in non-neural cells and whether or not this is related to gap junction formation. Therefore, we analysed the migratory activity of HeLa cells under conditions of controlled connexin (Cx) expression. The expression of Cx43 enhanced their migration significantly as compared to Cx deficient wild-type cells. Expression of only the carboxyl tail of Cx43 (Cx43CT, AA 257-382) without channel forming capacity enhanced migration similarly as the full length protein. In contrast, the expression of the N-t...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901378</comments>
            <pubDate>Tue, 17 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901378</guid>        </item>
        <item>
            <title>Phycobiliproteins in Prochlorococcus marinus: Biosynthesis of pigments and their assembly into proteins.</title>
            <link>http://www.medworm.com/index.php?rid=3901383&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20724022%26dopt%3DAbstract</link>
            <description>Authors: Wiethaus J, Busch AW, Dammeyer T, Frankenberg-Dinkel N
    Prochlorococcus sp. is a very unique and highly abundant class of organisms within the cyanobacteria. Found in the world's oceans Prochlorococcus is very small in size and possesses the smallest genome of a photosynthetic autotroph. Prochlorococcus is characterized by a special chlorophyll antenna for light harvesting and the absence of classical cyanobacterial phycobilisomes. Despite the lack of phycobilisomes Prochlorococcus possesses remnants thereof which is the phycobiliprotein phycoerythrin (PE) encoded in a PE operon as well as genes encoding enzymes of phycobilin biosynthesis. The size of this PE operon varies depending on the light-adapted ecotype. While high-light strains only possess a beta-subunit of PE, low-li...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3901383</comments>
            <pubDate>Mon, 16 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3901383</guid>        </item>
        <item>
            <title>Analysis of the signaling pathways regulating Src-dependent remodeling of the actin cytoskeleton.</title>
            <link>http://www.medworm.com/index.php?rid=3885756&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20719402%26dopt%3DAbstract</link>
            <description>Authors: Winograd-Katz SE, Brunner MC, Mirlas N, Geiger B
    Cell adhesion to the extracellular matrix is mediated by adhesion receptors, mainly integrins, which upon interaction with the extracellular matrix, bind to the actin cytoskeleton via their cytoplasmic domains. This association is mediated by a variety of scaffold and signaling proteins, which control the mechanical and signaling activities of the adhesion site. Upon transformation of fibroblasts with active forms of Src (e.g., v-Src), focal adhesions are disrupted, and transformed into dot-like contacts known as podosomes, and consisting of a central actin core surrounded by an adhesion ring. To clarify the mechanism underlying Src-dependent modulation of the adhesive phenotype, and its influence on podosome organization, we sc...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3885756</comments>
            <pubDate>Mon, 16 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3885756</guid>        </item>
        <item>
            <title>Mutants of the Saccharomyces cerevisiae VPS genes CCZ1 and YPT7 are blocked in different stages of sporulation.</title>
            <link>http://www.medworm.com/index.php?rid=3873261&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20709422%26dopt%3DAbstract</link>
            <description>Authors: Piekarska I, Kucharczyk R, Mickowska B, Rytka J, Rempola B
    The CCZ1 gene is a member of the class B VPS (vacuolar protein sorting) genes and it is engaged in the last stage of delivery of multiple kinds of cargo to the yeast vacuole. In the process of fusion of the multivesicular body (MVB) with the vacuole, Ccz1p forms a complex with Ypt7p. Both genes are non-essential for vegetative growth, but their deletions cause a complete block in spore formation. The results of this study indicate that ccz1Delta cells initiate the meiotic program, properly proceed through premeiotic DNA replication and through the pairing of homologous chromosomes, but fail to progress through the first meiotic divisions and arrest in prophase I with a single nucleus. The mutant cells are defective in ...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3873261</comments>
            <pubDate>Thu, 12 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3873261</guid>        </item>
        <item>
            <title>abLIM3 is a novel component of adherens junctions with actin-binding activity.</title>
            <link>http://www.medworm.com/index.php?rid=3873260&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20709423%26dopt%3DAbstract</link>
            <description>Authors: Matsuda M, Yamashita JK, Tsukita S, Furuse M
    The interactions of adhesion molecules with dense actin filaments via cytoplasmic plaque proteins are crucial for the adhesive function of adherens junctions (AJs) in epithelial and endothelial cells. Using localization-based expression cloning, we identified abLIM3, a member of the actin-binding LIM (abLIM) protein family, as a component of the junctional complex. Immunolocalization studies revealed that abLIM3 was localized at AJs in limited cell types, including hepatocytes, bronchial epithelial cells, mesothelial cells and endothelial cells lining muscular tissues. Deletion mutant analyses in cultured cells showed that the C-terminal dematin-like domain of abLIM3, which bound to actin filaments in vitro, was colocalized with pha...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3873260</comments>
            <pubDate>Thu, 12 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3873260</guid>        </item>
        <item>
            <title>Native type IV collagen induces cell migration through a CD9 and DDR1-dependent pathway in MDA-MB-231 breast cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=3873259&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20709424%26dopt%3DAbstract</link>
            <description>Authors: Castro-Sanchez L, Soto-Guzman A, Navarro-Tito N, Martinez-Orozco R, Salazar EP
    CD9 is a member of the tetraspanin family and is widely expressed in the plasma membrane of several cell types as well as malignant cells. CD9 associates with a number of transmembrane proteins, which facilitates biological processes, including cell signaling, adhesion, migration and proliferation. DDR1 is activated by native type IV collagen and overexpressed in human breast cancer. Type IV collagen is the main component of basement membranes, and may interact with cell surface biomolecules, promoting adhesion and motility. However, the role of DDR1 and type IV collagen in the regulation of CD9-cell surface levels and migration in breast cancer cells has not been studied in detail. We demonstrate h...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3873259</comments>
            <pubDate>Thu, 12 Aug 2010 23:00:00 +0100</pubDate>
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            <title>Component interactions, regulation and mechanisms of chloroplast signal recognition particle-dependent protein transport.</title>
            <link>http://www.medworm.com/index.php?rid=3873258&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20709425%26dopt%3DAbstract</link>
            <description>Authors: Richter CV, Bals T, SchÃ¼nemann D
    The chloroplast proteome comprises nuclear- and plastome-encoded proteins. In order to function correctly these proteins must be transported, either cotranslationally or posttranslationally, to their final destination in the chloroplast. Here the chloroplast signal recognition particle (cpSRP) which is present in two different stromal pools plays an essential role. On the one hand, the conserved 54kDa subunit (cpSRP54) is associated with 70S ribosomes to function in the cotranslational transport of the plastid-encoded thylakoid membrane protein D1. On the other hand, the cpSRP consists of cpSRP54 and a unique 43kDa subunit (cpSRP43) and facilitates the transport of nuclear-encoded light-harvesting chlorophyll-binding proteins (LHCPs), the mo...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3873258</comments>
            <pubDate>Thu, 12 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3873258</guid>        </item>
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            <title>Annexin XIIIb guides raft-dependent and -independent apical traffic in MDCK cells.</title>
            <link>http://www.medworm.com/index.php?rid=3873262&amp;cid=s_35539_171_f&amp;fid=35539&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20708818%26dopt%3DAbstract</link>
            <description>Authors: Astanina K, Delebinski CI, Delacour D, Jacob R
    Epithelial cells are characterized by a polarized organization of their plasma membrane that is divided into apical and basolateral domains. This architecture is maintained by a highly specific cargo sorting machinery that efficiently delivers components to their respective membrane domains. After TGN exit apical cargo is segregated by at least two distinct sorting mechanisms into lipid raft-dependent or lipid raft-independent apical pathways. Annexin XIIIb had been shown to be a member of the lipid raft-dependent trafficking machinery. We now identify this annexin also in raft-independent apical trafficking by mass spectrometry, immunoblotting and confocal microscopy. Annexin XIIIb accumulates in endosomal organelles that are tra...</description>
            <author>European Journal of Cell Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3873262</comments>
            <pubDate>Wed, 11 Aug 2010 23:00:00 +0100</pubDate>
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