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        <title>Biology of the Cell 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 'Biology of the Cell' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Biology+of+the+Cell&t=Biology+of+the+Cell&s=Search&f=source]]></link>
        <lastBuildDate>Tue, 07 Feb 2012 08:48:51 +0100</lastBuildDate>
        <item>
            <title>Contents: biology of the cell. 2/2012.</title>
            <link>http://www.medworm.com/index.php?rid=5659176&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22296452%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22296452 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659176</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Cover picture.</title>
            <link>http://www.medworm.com/index.php?rid=5659175&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22296453%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22296453 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659175</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659175</guid>        </item>
        <item>
            <title>Retinal pigment epithelial cells use a MerTK-dependent mechanism to limit the phagocytic particle binding activity of αvβ5 integrin.</title>
            <link>http://www.medworm.com/index.php?rid=5659177&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22289110%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Expressing β5-GFP is sufficient to reverse phagocytic deficiencies of RPE cells derived from β5(-/-) mice indicating that these cells do not irreversibly lose other components of the phagocytic machinery. RPE cells expressing the engulfment receptor MerTK control POS binding by limiting activity of endogenous αvβ5 and αvβ5-GFP integrins although they reside at the apical, phagocytic surface. In contrast, RPE cells permanently or transiently losing MerTK expression lack this regulatory mechanism and bind excess POS via surface αvβ5 receptors. Taken together, these data reveal a novel feedback mechanism that restricts binding of POS to surface avb5 integrin receptors in RPE cells.
    PMID: 22289110 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659177</comments>
            <pubDate>Mon, 30 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659177</guid>        </item>
        <item>
            <title>The transcriptional activity of coactivator AIB1 is regulated by the SUMO E3 ligase PIAS1.</title>
            <link>http://www.medworm.com/index.php?rid=5659178&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22283414%26dopt%3DAbstract</link>
            <description>Authors: Li S, Yang C, Hong Y, Bi H, Zhao F, Liu Y, Ao X, Pang P, Xing X, Chang AK, Xiao L, Zhang Y, Wu H
    Abstract
    Amplified in breast cancer 1 (AIB1) is a transcriptional coactivator of nuclear receptors and other transcription factors. It is required for animal growth and reproductive development, and has also been implicated in breast carcinogenesis. Although AIB1 is known to be covalently modified by SUMO-1, which serves to regulate its stability and transcriptional activity, the exact SUMO E3 ligase involved in its sumoylation has not been determined. Here we show that one member of the PIAS family, PIAS1, co-immunoprecipitated with AIB1 in extract prepared from breast cancer cells (MCF-7), and that over-expression of PIAS1 together with AIB1 in MCF-7 cells led to increased su...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659178</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659178</guid>        </item>
        <item>
            <title>The Dynamic Cytoskeleton of the Developing Male Germ Cell.</title>
            <link>http://www.medworm.com/index.php?rid=5659179&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22276751%26dopt%3DAbstract</link>
            <description>Authors: Sperry AO
    Abstract
    Mammalian spermatogenesis is characterized by dramatic cellular change to transform the non-polar spermatogonium into the highly polarized, functional spermatozoon. The acquisition of cell polarity is a requisite step for formation of viable sperm. The polarity of the spermatozoon is clearly demonstrated by the acrosome at the apical pole of the cell and the flagellum at the opposite end. Spermatogenesis consists of three basic phases: mitosis, meiosis, and spermiogenesis. The final phase represents the period of greatest cellular change where cell-type specific organelles such as the acrosome and the flagellum form, the nucleus migrates to the plasma membrane and elongates, chromatin condenses, and residual cytoplasm is removed. An important feature of ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659179</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659179</guid>        </item>
        <item>
            <title>The unfolded protein response at the crossroads of cellular life and death during ER stress.</title>
            <link>http://www.medworm.com/index.php?rid=5659180&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22268789%26dopt%3DAbstract</link>
            <description>Authors: Jäger R, Bertrand MJ, Gorman AM, Vandenabeele P, Samali A
    Abstract
    One of the early cellular responses to endoplasmic reticulum (ER) stress is the activation of the unfolded protein response (UPR). ER stress and the UPR are both implicated in numerous human diseases and pathologies. In spite of this, our knowledge of the molecular mechanisms that regulate cell fate following ER stress is limited. The UPR is initiated by three ER transmembrane receptors, PERK, ATF6, and IRE1. These proteins sense the accumulation of unfolded proteins and their activation triggers specific adaptive responses to resolve the stress. Intriguingly, the very same receptors can initiate signaling pathways that lead to apoptosis when the attempts to resolve the ER stress fail. In this review we de...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5659180</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5659180</guid>        </item>
        <item>
            <title>Emerging roles for ubiquitin in adenovirus cell entry.</title>
            <link>http://www.medworm.com/index.php?rid=5623478&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22251092%26dopt%3DAbstract</link>
            <description>Authors: Marvin SA, Wiethoff CM
    Abstract
    Adenovirus relies on numerous interactions between viral and host cell proteins to efficiently enter cells. Undoubtedly, post-translational modifications of host and cellular proteins can impact the efficiency of this cell entry process. Ubiquitylation, once simply thought of as a modification targeting proteins for proteasomal degradation, is now known to regulate protein trafficking within cells, protein-protein interactions, and cell signaling pathways. Accumulating evidence suggests that protein ubiquitylation can influence all stages of the life cycle of other viruses such as cell entry, replication, and egress. Until recently the influence of ubiquitylation has only been documented during adenovirus replication. This review highlights ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5623478</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5623478</guid>        </item>
        <item>
            <title>NKCC2 trafficking and activity: the role of interacting proteins.</title>
            <link>http://www.medworm.com/index.php?rid=5560891&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22211456%26dopt%3DAbstract</link>
            <description>Authors: Carmosino M, Procino G, Svelto M
    Abstract
    The central role of Na+-K+-2Cl- cotrasporter type 2 (NKCC2) in the vectorial transepithelial salt reabsorption in thick ascending limb cells from Henle's loop in the kidney is evidenced by the effects of loop diuretics, the pharmacological inhibitors of NKCC2, that are among the most powerful antihypertensive drugs available to date. Moreover, genetic mutations of the NKCC2 encoding gene resulting in impaired apical targeting and function of NKCC2 transporter, give rice to a pathological phenotype known as Type I Bartter's syndrome, characterized by a severe volume depletion, hypokalemia and metabolic alkalosis with high prenatal mortality. On the other hand, excessive NKCC2 activity has been linked with inherited hypertension in h...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560891</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560891</guid>        </item>
        <item>
            <title>A Role for Microtubules in Endothelial Cell Protrusion in 3D Matrices.</title>
            <link>http://www.medworm.com/index.php?rid=5560890&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22211516%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Our results show that MT depolymerization is particularly disruptive when cells interact with pliable 3D matrices, suggesting a role for microtubules and the Rho pathway in the fine-tuning of contractile and adhesive forces necessary to sustain cell motility in vivo.
    PMID: 22211516 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560890</comments>
            <pubDate>Mon, 02 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560890</guid>        </item>
        <item>
            <title>Masthead.</title>
            <link>http://www.medworm.com/index.php?rid=5560889&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22214190%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22214190 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560889</comments>
            <pubDate>Sun, 01 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560889</guid>        </item>
        <item>
            <title>Cover picture.</title>
            <link>http://www.medworm.com/index.php?rid=5560888&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22214191%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22214191 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5560888</comments>
            <pubDate>Sun, 01 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5560888</guid>        </item>
        <item>
            <title>Clathrin-mediated endocytosis regulates occludin, and not focal adhesion, distribution during epithelial wound healing.</title>
            <link>http://www.medworm.com/index.php?rid=5535562&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187938%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Thus, these studies have evaluated mechanistic roles for dynamin-dependant, clathrin-mediated and caveolar endocytosis during epithelial wound healing, and have provided contrasting observations between analyses of cell motility in fibroblast models and epithelial cells. In conclusion these studies have identified a novel mechanism for regulation of occludin during wound healing.
    PMID: 22187938 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535562</comments>
            <pubDate>Mon, 19 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535562</guid>        </item>
        <item>
            <title>Multi-Color Direct STORM with Red Emitting Carbocyanines.</title>
            <link>http://www.medworm.com/index.php?rid=5535561&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187967%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: SD-dSTORM presents a significant advance towards user-friendly single molecule localization-based super-resolution microscopy combining advantages of state-of-the-art methodologies to perform fast, reliable and efficient multi-color dSTORM.
    PMID: 22187967 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535561</comments>
            <pubDate>Mon, 19 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535561</guid>        </item>
        <item>
            <title>HIV-1, Ubiquitin and Ubiquitin-like proteins: the dialectic interactions of a virus with a sophisticated network of post-translational modifications.</title>
            <link>http://www.medworm.com/index.php?rid=5535555&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188301%26dopt%3DAbstract</link>
            <description>Authors: Biard-Piechaczyk M, Borel S, Espert L, de Bettignies G, Coux O
    Abstract
    The modification of intracellular proteins by Ubiquitin and Ubiquitin-like proteins is a central mechanism for regulating and fine-tuning all cellular processes. Indeed, these modifications are widely used to control the stability, activity and localization of many key proteins and therefore they are instrumental in regulating cellular functions as diverse as protein degradation, cell signalling, vesicle trafficking and immune response. It is thus no surprise that pathogens in general, and viruses in particular, have developed multiple strategies to either counteract or exploit the complex mechanisms mediated by the Ubiquitin and Ubiquitin-like protein conjugation pathways. The aim of this review is to...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535555</comments>
            <pubDate>Mon, 19 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535555</guid>        </item>
        <item>
            <title>Rab11 is phosphorylated by classical and novel Protein Kinase C isoenzymes upon sustained phorbol ester activation.</title>
            <link>http://www.medworm.com/index.php?rid=5535560&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188018%26dopt%3DAbstract</link>
            <description>This report shows for the first time that Rab11 is differentially phosphorylated by distinct PKC isoenzymes and that this post-translational modification might be a regulatory mechanism of intracellular trafficking.
    PMID: 22188018 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535560</comments>
            <pubDate>Wed, 07 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535560</guid>        </item>
        <item>
            <title>Histone modifications in herpesvirus infections.</title>
            <link>http://www.medworm.com/index.php?rid=5535559&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188068%26dopt%3DAbstract</link>
            <description>Authors: Van Opdenbosch N, Favoreel H, Van de Walle GR
    Abstract
    In eukaryotic cells, gene expression is not only regulated by transcription factors but also by several epigenetic mechanisms including post-translational modifications of histone proteins. There are numerous histone modifications described to date and methylation, acetylation, ubiquitination and phosphorylation are amongst the best studied. In parallel, certain viruses interact with the very same regulatory mechanisms, hereby manipulating the normal epigenetic landscape of the host cell, to fit their own replication needs. This review concentrates on herpesviruses specifically and how they interfere with the histone-modifying enzymes to regulate their replication cycles. Herpesviruses vary greatly with respect to the ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535559</comments>
            <pubDate>Wed, 07 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535559</guid>        </item>
        <item>
            <title>TI-VAMP/VAMP7 is the snare of secretory lysosomes contributing to ATP secretion from astrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5535558&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188132%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Given that sustained ATP release from glia upon injury greatly contribute to secondary brain damage and cathepsin B plays a critical role in glioma dissemination, TI-VAMP silencing can represent a novel strategy to control lysosome fusion in pathological conditions.
    PMID: 22188132 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535558</comments>
            <pubDate>Wed, 07 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535558</guid>        </item>
        <item>
            <title>Rab30 is required for the morphological integrity of the Golgi.</title>
            <link>http://www.medworm.com/index.php?rid=5535557&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188167%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: Taken together, these data illustrate that Rab30 primarily localises to the Golgi apparatus and is required for the structural integrity of this organelle.
    PMID: 22188167 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535557</comments>
            <pubDate>Mon, 05 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535557</guid>        </item>
        <item>
            <title>Regulation of the nucleocytoplasmic trafficking of viral and cellular proteins by ubiquitin and small ubiquitin-related modifiers (SUMOs).</title>
            <link>http://www.medworm.com/index.php?rid=5535556&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22188262%26dopt%3DAbstract</link>
            <description>Authors: Wang YE, Pernet O, Lee B
    Abstract
    The nucleocytoplasmic trafficking of many cellular proteins is regulated by nuclear import/export signals as well as post-translational modifications such as the covalent conjugation of ubiquitin and the small ubiquitin-related modifiers (SUMOs). Ubiquitination and SUMOylation are rapid and reversible ways to modulate the intracellular localization and function of the substrate proteins. These pathways have been co-opted by some viruses, which depend on the host cell machinery to transport their proteins in and out of the nucleus. In this review, we will summarize our current knowledge on the ubiquitin/SUMO-regulated nuclear/subnuclear trafficking of cellular proteins and describe examples of viral exploitation of these pathways.
    PMID:...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5535556</comments>
            <pubDate>Mon, 05 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5535556</guid>        </item>
        <item>
            <title>Defining the role of TRIP6 in cell physiology and cancer.</title>
            <link>http://www.medworm.com/index.php?rid=5421933&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22054418%26dopt%3DAbstract</link>
            <description>Authors: Willier S, Butt E, Richter GH, Burdach S, Grunewald TG
    Abstract
    Integrating signals from the ECM (extracellular matrix) via the cell surface into the nucleus is an essential feature of multicellular life and often malfunctions in cancer. To date many signal transducers known as shuttle proteins have been identified that act as both: a cytoskeletal and a signalling protein. Here, we highlight the interesting member of the Zyxin family TRIP6 [thyroid receptor interactor protein 6; also designated ZRP-1 (zyxin-related protein 1)] and review current literature to define its role in cell physiology and cancer. TRIP6 is a versatile scaffolding protein at FAs (focal adhesions) involved in cytoskeletal organization, coordinated cell migration and tissue invasion. Via its LIM and T...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421933</comments>
            <pubDate>Sat, 19 Nov 2011 02:42:21 +0100</pubDate>
            <guid isPermaLink="false">5421933</guid>        </item>
        <item>
            <title>Jumping the barrier: VE-cadherin, VEGF and other angiogenic modifiers in cancer.</title>
            <link>http://www.medworm.com/index.php?rid=5421932&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22054419%26dopt%3DAbstract</link>
            <description>Authors: Le Guelte A, Dwyer J, Gavard J
    Abstract
    The endothelial barrier controls the passage of fluids, nutrients and cells through the vascular wall. This physiological function is closely related to developmental and adult angiogenesis, blood pressure control, as well as immune responses. Moreover, cancer progression is frequently characterized by disorganized and leaky blood vessels. In this context, vascular permeability drives tumour-induced angiogenesis, blood flow disturbances, inflammatory cell infiltration and tumour cell extravasation. Although various molecules have been implicated, the vascular endothelial adhesion molecule, VE-cadherin (vascular endothelial cadherin), has emerged as a critical player involved in maintaining endothelial barrier integrity and homoeostas...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5421932</comments>
            <pubDate>Sat, 19 Nov 2011 02:42:11 +0100</pubDate>
            <guid isPermaLink="false">5421932</guid>        </item>
        <item>
            <title>The Golgi apparatus in the endomembrane-rich gastric parietal cells exist as functional stable mini-stacks dispersed throughout the cytoplasm.</title>
            <link>http://www.medworm.com/index.php?rid=5219299&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21899517%26dopt%3DAbstract</link>
            <description>Conclusions: These data indicate that the unusual organisation of individual Golgi stacks dispersed throughout the cytoplasm of these terminally differentiated cells is likely to be a developmentally regulated event.
    PMID: 21899517 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5219299</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5219299</guid>        </item>
        <item>
            <title>The Golgi apparatus in the endomembrane-rich gastric parietal cells exist as functional stable mini-stacks dispersed throughout the cytoplasm</title>
            <link>http://www.medworm.com/index.php?rid=5205539&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110074</link>
            <description>Conclusions: These data indicate that the unusual organisation of individual Golgi stacks dispersed throughout the cytoplasm of these terminally differentiated cells is likely to be a developmentally regulated event. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5205539</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5205539</guid>        </item>
        <item>
            <title>The future is cold: cryo-preparation methods for transmission electron microscopy of cells.</title>
            <link>http://www.medworm.com/index.php?rid=5104198&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21812762%26dopt%3DAbstract</link>
            <description>Authors: Hurbain I, Sachse M
    Our knowledge of the organization of the cell is linked, to a great extent, to light and electron microscopy. Choosing either photons or electrons for imaging has many consequences on the image obtained, as well as on the experiment required in order to generate the image. One apparent effect on the experimental side is in the sample preparation, which can be quite elaborate for electron microscopy. In recent years, rapid freezing, cryo-preparation and cryo-electron microscopy have been more widely used because they introduce fewer artefacts during preparation when compared with chemical fixation and room temperature processing. In addition, cryo-electron microscopy allows the visualization of the hydrated specimens. In the present review, we give an introd...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104198</comments>
            <pubDate>Mon, 08 Aug 2011 00:00:11 +0100</pubDate>
            <guid isPermaLink="false">5104198</guid>        </item>
        <item>
            <title>Vascular cell lines expressing SSAO/VAP-1: a new experimental tool to study its involvement in vascular diseases</title>
            <link>http://www.medworm.com/index.php?rid=5095583&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110049</link>
            <description>Conclusions: Our results endorse the use of these cellular models for the in-depth study of the currently poorly understood functions of SSAO/VAP-1, its involvement in the above-mentioned pathologies, as well as for evaluating potential compounds that could modulate its activity for therapeutic purposes. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5095583</comments>
            <pubDate>Thu, 04 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5095583</guid>        </item>
        <item>
            <title>Efficient In Vitro Myogenic Reprogramming of Human Primary Mesenchymal Stem Cells And Endothelial Cells By Myf5.</title>
            <link>http://www.medworm.com/index.php?rid=5104199&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21810080%26dopt%3DAbstract</link>
            <description>Conclusions. Our procedure could be used for developing new research protocols in the prospect of using these cells as therapeutic agents.
    PMID: 21810080 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5104199</comments>
            <pubDate>Mon, 01 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5104199</guid>        </item>
        <item>
            <title>Efficient In Vitro Myogenic Reprogramming of Human Primary Mesenchymal Stem Cells And Endothelial Cells By Myf5</title>
            <link>http://www.medworm.com/index.php?rid=5095584&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100112</link>
            <description>Conclusions. Our procedure could be used for developing new research protocols in the prospect of using these cells as therapeutic agents. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5095584</comments>
            <pubDate>Mon, 01 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5095584</guid>        </item>
        <item>
            <title>The proteome of cytosolic lipid droplets isolated from differentiated Caco-2/TC7 enterocytes reveals cell-specific characteristics</title>
            <link>http://www.medworm.com/index.php?rid=5069213&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110024</link>
            <description>Conclusions. We report for the first time the protein endowment of Caco-2/TC7 enterocyte CLD. Our results suggest that their formation and mobilization may participate to the control of enterocyte TRL secretion in a cell-specific manner. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5069213</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5069213</guid>        </item>
        <item>
            <title>{alpha}v integrin processing interferes with the crosstalk between {alpha}v{beta}5/{beta}6 and {alpha}2{beta}1 integrins</title>
            <link>http://www.medworm.com/index.php?rid=5069212&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100147</link>
            <description>Conclusions: The increase in cell migration observed upon convertases inhibition appears to be due to the up-activation of beta1 integrins and to their location in larger focal adhesion structures. The endoproteolytic cleavage of av subunits is necessary for alphavbeta5/beta6 integrin to control alpha2beta1 function and could thus play an essential role in colon cancer cell migration (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5069212</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5069212</guid>        </item>
        <item>
            <title>Pes1 and ppan function during Xenopus laevis pronephros development</title>
            <link>http://www.medworm.com/index.php?rid=5050100&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110032</link>
            <description>Conclusion. These data demonstrate that pes1 and ppan are required for Xenopus pronephros development and indicate that their function in the pronephros is independent of their role in ribosome biosynthesis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5050100</comments>
            <pubDate>Mon, 18 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5050100</guid>        </item>
        <item>
            <title>Remodelling of the endoplasmic reticulum during store-operated calcium entry.</title>
            <link>http://www.medworm.com/index.php?rid=5009199&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21736554%26dopt%3DAbstract</link>
            <description>Authors: Shen WW, Frieden M, Demaurex N
    SOCE (store-operated calcium entry) is a ubiquitous cellular mechanism linking the calcium depletion of the ER (endoplasmic reticulum) to the activation of PM (plasma membrane) Ca2+-permeable channels. The activation of SOCE channels favours the entry of extracellular Ca2+ into the cytosol, thereby promoting the refilling of the depleted ER Ca2+ stores as well as the generation of long-lasting calcium signals. The molecules that govern SOCE activation comprise ER Ca2+ sensors [STIM1 (stromal interaction molecule 1) and STIM2], PM Ca2+-permeable channels {Orai and TRPC [TRP (transient receptor potential) canonical]} and regulatory Ca2+-sensitive cytosolic proteins {CRACR2 [CRAC (Ca2+ release-activated Ca2+ current) regulator 2]}. Upon Ca2+ depleti...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009199</comments>
            <pubDate>Sat, 09 Jul 2011 13:30:20 +0100</pubDate>
            <guid isPermaLink="false">5009199</guid>        </item>
        <item>
            <title>Histone demethylases in chromatin cross-talks.</title>
            <link>http://www.medworm.com/index.php?rid=5009198&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21736555%26dopt%3DAbstract</link>
            <description>Authors: Verrier L, Vandromme M, Trouche D
    The 'histone code' hypothesis states that chromatin-based regulation of nuclear processes such as transcription is brought about by the combination of distinct modifications (histone marks) at specific loci. Its correct establishment involves chromatin cross-talks, ensuring an ordered and concerted deposition/removal of a particular set of modifications that act together to give the correct transcriptional outcome. Histone methylation on lysine residues can negatively or positively impact on gene transcription, depending on the residue and on its degree of methylation. Thanks to this complexity and given the number of chromatin 'readers' that can recognize methylated lysine residues, histone methylation plays a very special role in specifying ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009198</comments>
            <pubDate>Sat, 09 Jul 2011 13:30:15 +0100</pubDate>
            <guid isPermaLink="false">5009198</guid>        </item>
        <item>
            <title>Fibroblasts share mesenchymal phenotypes with stem cells, but lack their differentiation and colony-forming potential.</title>
            <link>http://www.medworm.com/index.php?rid=5009197&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21736556%26dopt%3DAbstract</link>
            <description>Authors: Alt E, Yan Y, Gehmert S, Song YH, Altman A, Gehmert S, Vykoukal D, Bai X
    
    PMID: 21736556 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009197</comments>
            <pubDate>Sat, 09 Jul 2011 13:30:11 +0100</pubDate>
            <guid isPermaLink="false">5009197</guid>        </item>
        <item>
            <title>Intraflagellar transport proteins in ciliogenesis of photoreceptor cells.</title>
            <link>http://www.medworm.com/index.php?rid=5009201&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21732910%26dopt%3DAbstract</link>
            <description>Conclusions. Our data conclusively provide evidence for the participation of IFT proteins in photoreceptor cell ciliogenesis, including the formation of the ciliary vesicle and the elongation of the primary cilium. In advanced stages of ciliogenesis the ciliary localization of IFT proteins indicate a role in IFT as is seen in mature cilia. A prominent accumulation of IFT proteins in the periciliary cytoplasm at the base of the cilia in these stages most probably resembles a reserve pool of IFT molecules for further delivery into the growing ciliary shaft and their subsequent function in IFT. Nevertheless, the cytoplasmic localization of IFT proteins in the absence of a ciliary shaft in early stages of ciliogenesis may indicate roles of IFT proteins beyond their well-established function fo...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009201</comments>
            <pubDate>Tue, 05 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009201</guid>        </item>
        <item>
            <title>Characterization of a novel angiogenic model based on stable, fluorescently labeled endothelial cell lines amenable to scale-up for high content screening.</title>
            <link>http://www.medworm.com/index.php?rid=5009200&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21732911%26dopt%3DAbstract</link>
            <description>Conclusions. HMEC-based lines retain most of the angiogenic features of primary endothelial cells, yet possess long-term stability and ease of culture, making them intriguing candidates for large-scale primary HC and HT screening (of ~10,000-1,000,000 molecules). Furthermore, inclusion of EMCs demonstrates the feasibility of using epicardial-derived cells, which normally contribute to smooth muscle, to model large vessel formation. In summary, the immortalized fluorescent HMEC and EMC lines and straightforward culture conditions will enable assay development for HCS of angiogenesis.
    PMID: 21732911 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5009200</comments>
            <pubDate>Tue, 05 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5009200</guid>        </item>
        <item>
            <title>Intraflagellar transport proteins in ciliogenesis of photoreceptor cells</title>
            <link>http://www.medworm.com/index.php?rid=5007769&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110034</link>
            <description>Conclusions. Our data conclusively provide evidence for the participation of IFT proteins in photoreceptor cell ciliogenesis, including the formation of the ciliary vesicle and the elongation of the primary cilium. In advanced stages of ciliogenesis the ciliary localization of IFT proteins indicate a role in IFT as is seen in mature cilia. A prominent accumulation of IFT proteins in the periciliary cytoplasm at the base of the cilia in these stages most probably resembles a reserve pool of IFT molecules for further delivery into the growing ciliary shaft and their subsequent function in IFT. Nevertheless, the cytoplasmic localization of IFT proteins in the absence of a ciliary shaft in early stages of ciliogenesis may indicate roles of IFT proteins beyond their well-established function fo...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5007769</comments>
            <pubDate>Tue, 05 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5007769</guid>        </item>
        <item>
            <title>Characterization of a novel angiogenic model based on stable, fluorescently labeled endothelial cell lines amenable to scale-up for high content screening</title>
            <link>http://www.medworm.com/index.php?rid=5007768&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100146</link>
            <description>Conclusions. HMEC-based lines retain most of the angiogenic features of primary endothelial cells, yet possess long-term stability and ease of culture, making them intriguing candidates for large-scale primary HC and HT screening (of ~10,000-1,000,000 molecules). Furthermore, inclusion of EMCs demonstrates the feasibility of using epicardial-derived cells, which normally contribute to smooth muscle, to model large vessel formation. In summary, the immortalized fluorescent HMEC and EMC lines and straightforward culture conditions will enable assay development for HCS of angiogenesis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5007768</comments>
            <pubDate>Tue, 05 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5007768</guid>        </item>
        <item>
            <title>The site of RanGTP generation can act as an organizational cue for mitotic microtubules.</title>
            <link>http://www.medworm.com/index.php?rid=4962510&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21692748%26dopt%3DAbstract</link>
            <description>Conclusions These data suggest that the site of RanGTP generation in a mitotic somatic cell can generate critical spatial information that specifies where microtubules grow toward and where microtubules are organized. As RanGTP is normally generated on chromosomes these data suggest that RanGTP may play an important role in specifying that spindle assembly occurs around chromosomes.
    PMID: 21692748 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962510</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962510</guid>        </item>
        <item>
            <title>The site of RanGTP generation can act as an organizational cue for mitotic microtubules</title>
            <link>http://www.medworm.com/index.php?rid=4959843&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100135</link>
            <description>Conclusions
 These data suggest that the site of RanGTP generation in a mitotic somatic cell can generate critical spatial information that specifies where microtubules grow toward and where microtubules are organized. As RanGTP is normally generated on chromosomes these data suggest that RanGTP may play an important role in specifying that spindle assembly occurs around chromosomes. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959843</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959843</guid>        </item>
        <item>
            <title>Adipose Stem Cells Originate from Perivascular Cells.</title>
            <link>http://www.medworm.com/index.php?rid=4962511&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21679159%26dopt%3DAbstract</link>
            <description>In this study, we aimed to investigate the origins of adipose stem cells. Smooth muscle actin alpha (α-SMA) is one of the markers of pericytes. We harvested adipose stromal cells from α-SMA-GFP transgenic mice and sorted them into GFP positive and negative cells by FACS. Multilineage differentiation tests were applied to examine the pluripotent ability of the α-SMA-GFP positive and negative cells. Immunofluorescent staining for α-SMA and PDGF-Rβ were applied to identify the α-SMA-GFP positive cells. Then α-SMA-GFP positive cells were loaded on a collagen-fibronectin gel with endothelial cells to test their vascularization ability both in vitro and in vivo. Results show that in the adipose tissue, all of the α-SMA-GFP positive cells congregate around the blood vessels. Only the α-S...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4962511</comments>
            <pubDate>Wed, 15 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4962511</guid>        </item>
        <item>
            <title>Adipose Stem Cells Originate from  Perivascular Cells</title>
            <link>http://www.medworm.com/index.php?rid=4933604&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110033</link>
            <description>In this study, we aimed to investigate the origins of adipose stem cells. Smooth muscle actin alpha (&amp;#x03B1;-SMA) is one of the markers of pericytes. We harvested adipose stromal cells from &amp;#x03B1;-SMA-GFP transgenic mice and sorted them into GFP positive and negative cells by FACS. Multilineage differentiation tests were applied to examine the pluripotent ability of the &amp;#x03B1;-SMA-GFP positive and negative cells. Immunofluorescent staining for &amp;#x03B1;-SMA and PDGF-R&amp;#x03B2; were applied to identify the &amp;#x03B1;-SMA-GFP positive cells. Then &amp;#x03B1;-SMA-GFP positive cells were loaded on a collagen-fibronectin gel with endothelial cells to test their vascularization ability both in vitro and in vivo. Results show that in the adipose tissue, all of the &amp;#x03B1;-SMA-GFP positive cells co...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4933604</comments>
            <pubDate>Wed, 15 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4933604</guid>        </item>
        <item>
            <title>Acute changes in temperature or oxygen availability induce ROS fluctuations in Daphnia magna linked with fluctuations of reduced and oxidized glutathione, catalase activity, and gene (hemoglobin) expression.</title>
            <link>http://www.medworm.com/index.php?rid=4866050&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21592090%26dopt%3DAbstract</link>
            <description>Conclusion. ROS-dependent signaling was affected by changes in temperature or oxygen availability. Feedback interactions between ROS and the glutathione redox system, possibly driven by elevated mitochondrial ROS production, likely contributed to the appearance of the ROS and GSH fluctuations upon acute environmental change. Fluctuating ROS levels, which encode for the magnitude of environmental change, could be a way to transfer information on ROS production to subsequent processes (gene expression) while avoiding too-high and damaging ROS levels.
    PMID: 21592090 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4866050</comments>
            <pubDate>Wed, 18 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4866050</guid>        </item>
        <item>
            <title>Acute changes in temperature or oxygen availability induce ROS fluctuations in Daphnia magna linked with fluctuations of reduced and oxidized glutathione, catalase activity, and gene (hemoglobin) expression</title>
            <link>http://www.medworm.com/index.php?rid=4841102&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100145</link>
            <description>Conclusion. ROS-dependent signaling was affected by changes in temperature or oxygen availability. Feedback interactions between ROS and the glutathione redox system, possibly driven by elevated mitochondrial ROS production, likely contributed to the appearance of the ROS and GSH fluctuations upon acute environmental change. Fluctuating ROS levels, which encode for the magnitude of environmental change, could be a way to transfer information on ROS production to subsequent processes (gene expression) while avoiding too-high and damaging ROS levels. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4841102</comments>
            <pubDate>Wed, 18 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4841102</guid>        </item>
        <item>
            <title>Role of sulfatide in vaccinia virus infection.</title>
            <link>http://www.medworm.com/index.php?rid=4814456&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21554243%26dopt%3DAbstract</link>
            <description>Conclusions: Together the data suggest that sulfatide could play a role as an alternate receptor for VACV-WR and probably other Orthopoxviruses.
    PMID: 21554243 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814456</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814456</guid>        </item>
        <item>
            <title>Role of sulfatide in vaccinia virus infection</title>
            <link>http://www.medworm.com/index.php?rid=4802094&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110012</link>
            <description>Conclusions: Together the data suggest that sulfatide could play a role as an alternate receptor for VACV-WR and probably other Orthopoxviruses. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4802094</comments>
            <pubDate>Sun, 08 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4802094</guid>        </item>
        <item>
            <title>Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi.</title>
            <link>http://www.medworm.com/index.php?rid=4814457&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21545355%26dopt%3DAbstract</link>
            <description>Conclusions. We show that syntaxin 17 has a tyrosine based motif which is required for its incorporation into COPII vesicles, exit from the ER, and localization to the ERGIC. Our results suggest that syntaxin 17 cycles between the ER and ERGIC through classical trafficking pathways involving COPII and COPI vesicles which requires its unique C-terminal tail. We also show that syntaxin 17 is essential for maintaining the architecture of ERGIC and Golgi.
    PMID: 21545355 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814457</comments>
            <pubDate>Wed, 04 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814457</guid>        </item>
        <item>
            <title>Syntaxin 17 cycles between the ER and ERGIC and is required to maintain the architecture of ERGIC and Golgi</title>
            <link>http://www.medworm.com/index.php?rid=4788900&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110006</link>
            <description>Conclusions. We show that syntaxin 17 has a tyrosine based motif which is required for its incorporation into COPII vesicles, exit from the ER, and localization to the ERGIC. Our results suggest that syntaxin 17 cycles between the ER and ERGIC through classical trafficking pathways involving COPII and COPI vesicles which requires its unique C-terminal tail. We also show that syntaxin 17 is essential for maintaining the architecture of ERGIC and Golgi. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4788900</comments>
            <pubDate>Wed, 04 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4788900</guid>        </item>
        <item>
            <title>Rabs and other small GTPases in ciliary transport.</title>
            <link>http://www.medworm.com/index.php?rid=4814460&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21488838%26dopt%3DAbstract</link>
            <description>Authors: Lim YS, Chua CE, Tang BL
    The non-motile primary cilium is a single, microtubule-based hair-like projection that emanates from most, if not all, non-dividing mammalian cells. Enriched in a variety of signalling receptors and accessories, the cilium mediates crucial sensory and regulatory functions during development and postnatal tissue homoeostasis. Maintenance of ciliary morphology and function requires continuous IFT (intraflagellar transport), and recent findings have shed light on some molecular details of how ciliogenesis is dependent on targeted exocytic membrane trafficking from the Golgi. The ARL [Arf (ADP ribosylation factor)-related] small GTPase Arf4 functions in TGN (trans-Golgi network) sorting of cilia-targeted rhodopsin into carrier vesicles, while Arl6 (Arf-lik...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814460</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814460</guid>        </item>
        <item>
            <title>The birth and life of lipid droplets: learning from the hepatitis C virus.</title>
            <link>http://www.medworm.com/index.php?rid=4814459&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21488839%26dopt%3DAbstract</link>
            <description>Authors: Roingeard P, Depla M
    LDs (lipid droplets) are probably the least well-characterized cellular organelles. Having long been considered simple lipid storage depots, they are now considered to be dynamic organelles involved in many biological processes. However, most of the mechanisms driving LDs biogenesis, growth and intracellular movement remain largely unknown. As for other cellular mechanisms deciphered through the study of viral models, HCV (hepatitis C virus) is an original and relevant model for investigations of the birth and life of these organelles. Recent studies in this model have raised the hypothesis that the HCV core protein induces the redistribution of LDs through the regression and regeneration of these organelles in specific intracellular domains.
    PMID: 214...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814459</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814459</guid>        </item>
        <item>
            <title>Agrin triggers the clustering of raft-associated acetylcholine receptors through actin-cytoskeleton reorganization.</title>
            <link>http://www.medworm.com/index.php?rid=4814458&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21524273%26dopt%3DAbstract</link>
            <description>Conclusions: The present observations support the notion that membrane rafts are involved in AChR clustering by promoting local actin cytoskeleton reorganization through the recruitment of effectors of the agrin/MuSK signaling cascade. These mechanisms are believed to play important role in vivo in the formation of the NMJ.
    PMID: 21524273 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4814458</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4814458</guid>        </item>
        <item>
            <title>Agrin triggers the clustering of raft-associated acetylcholine receptors through actin-cytoskeleton reorganization</title>
            <link>http://www.medworm.com/index.php?rid=4758574&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20110018</link>
            <description>Conclusions: The present observations support the notion that membrane rafts are involved in AChR clustering by promoting local actin cytoskeleton reorganization through the recruitment of effectors of the agrin/MuSK signaling cascade. These mechanisms are believed to play important role in vivo in the formation of the NMJ. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4758574</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4758574</guid>        </item>
        <item>
            <title>Ciliary beat co-ordination by calcium.</title>
            <link>http://www.medworm.com/index.php?rid=4652620&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21401526%26dopt%3DAbstract</link>
            <description>This article gives an overview of the complex effects of calcium on the beating of motile cilia in the airways.
    PMID: 21401526 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4652620</comments>
            <pubDate>Wed, 30 Mar 2011 04:30:09 +0100</pubDate>
            <guid isPermaLink="false">4652620</guid>        </item>
        <item>
            <title>Mouse 3T3 fibroblasts under the influence of fibroblasts isolated from stroma of human basal cell carcinoma acquire properties of multipotent stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=4583625&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21355851%26dopt%3DAbstract</link>
            <description>Conclusions: Our observations indicate the pro-stem cell activity of cancer-associated fibroblasts and underline the role of epithelial-mesenchymal interaction in tumor biology.
    PMID: 21355851 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583625</comments>
            <pubDate>Mon, 28 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583625</guid>        </item>
        <item>
            <title>Mouse 3T3 fibroblasts under the influence of fibroblasts isolated from stroma of human basal cell carcinoma acquire properties of multipotent stem cells</title>
            <link>http://www.medworm.com/index.php?rid=4531977&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100113</link>
            <description>Conclusions: Our observations indicate the pro-stem cell activity of cancer-associated fibroblasts and underline the role of epithelial-mesenchymal interaction in tumor biology. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4531977</comments>
            <pubDate>Mon, 28 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4531977</guid>        </item>
        <item>
            <title>Fibroblasts share mesenchymal phenotypes with stem cells, but lack their differentiation and colony forming potential.</title>
            <link>http://www.medworm.com/index.php?rid=4583626&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21332447%26dopt%3DAbstract</link>
            <description>Conclusions. These findings suggest that (1) so called commercially available fibroblast preparations from skin (hSDFs) consist of a significant number of cells with differentiation potential aside from terminally differentiated fibroblasts; (2) colony-forming capacity and differentiation potential are specific important properties that discriminate mesenchymal stem cells from fibroblasts (WI38) while conventional stem cell properties such as plastic adherence and the expression of CD44, CD90 and CD105 are unspecific for stem cells.
    PMID: 21332447 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583626</comments>
            <pubDate>Fri, 18 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583626</guid>        </item>
        <item>
            <title>Fibroblasts share mesenchymal phenotypes with stem cells, but lack their differentiation and colony forming potential</title>
            <link>http://www.medworm.com/index.php?rid=4494838&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100117</link>
            <description>Conclusions. These findings suggest that (1) so called commercially available fibroblast preparations from skin (hSDFs) consist of a significant number of cells with differentiation potential aside from terminally differentiated fibroblasts; (2) colony-forming capacity and differentiation potential are specific important properties that discriminate mesenchymal stem cells from fibroblasts (WI38) while conventional stem cell properties such as plastic adherence and the expression of CD44, CD90 and CD105 are unspecific for stem cells. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4494838</comments>
            <pubDate>Fri, 18 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4494838</guid>        </item>
        <item>
            <title>Dentinogenic capacity: immature root papilla stem cells vs. mature root pulp stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=4583627&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21323645%26dopt%3DAbstract</link>
            <description>Conclusion iRPSCs presented a stronger dentinogenesis but weaker osteogenesis than mRPSCs, suggesting that the dentinogenic competence of root mesenchymal stem cells decreases while their osteogenic potential increases following the maturation of tooth root.
    PMID: 21323645 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4583627</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4583627</guid>        </item>
        <item>
            <title>Dentinogenic capacity: immature root papilla stem cells vs. mature root pulp stem cells</title>
            <link>http://www.medworm.com/index.php?rid=4489460&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100134</link>
            <description>Conclusion
iRPSCs presented a stronger dentinogenesis but weaker osteogenesis than mRPSCs, suggesting that the dentinogenic competence of root mesenchymal stem cells decreases while their osteogenic potential increases following the maturation of tooth root. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4489460</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4489460</guid>        </item>
        <item>
            <title>Dysregulation of axonal transport and motorneuron diseases.</title>
            <link>http://www.medworm.com/index.php?rid=4411892&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21250942%26dopt%3DAbstract</link>
            <description>Authors: Sau D, Rusmini P, Crippa V, Onesto E, Bolzoni E, Ratti A, Poletti A
    MNDs (motorneuron diseases) are neurodegenerative disorders in which motorneurons located in the motor cortex, in the brainstem and in the spinal cord are affected. These diseases in their inherited or sporadic forms are mainly characterized by motor dysfunctions, occasionally associated with cognitive and behavioural alterations. Although these diseases show high variability in onset, progression and clinical symptoms, they share common pathological features, and motorneuronal loss invariably leads to muscle weakness and atrophy. One of the most relevant aspect of these disorders is the occurrence of defects in axonal transport, which have been postulated to be either a direct cause, or a consequence, of moto...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411892</comments>
            <pubDate>Sat, 29 Jan 2011 08:45:05 +0100</pubDate>
            <guid isPermaLink="false">4411892</guid>        </item>
        <item>
            <title>ARAP1 association with CIN85 affects epidermal growth factor receptor endocytic trafficking</title>
            <link>http://www.medworm.com/index.php?rid=4411410&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100154</link>
            <description>Conclusions: ARAP1 interaction with CIN85 regulates endocytic trafficking of the EGFR and affects ubiquitination of EGFR. We propose a model in which the ARAP1/CIN85 complex drives exit of EGF-EGFR-Cbl complex from a pre-early endosome into a pathway distinct from the early endosome/lysosome pathway. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411410</comments>
            <pubDate>Fri, 28 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411410</guid>        </item>
        <item>
            <title>Yeast water channels: an overview of orthodox aquaporins.</title>
            <link>http://www.medworm.com/index.php?rid=4279842&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21143194%26dopt%3DAbstract</link>
            <description>Authors: Soveral G, Prista C, Moura TF, Loureiro-Dias MC
    In yeast, the presence of orthodox aquaporins has been first recognized in Saccharomyces cerevisiae, in which two genes (AQY1 and AQY2) were shown to be related to mammal and plant water channels. The present review summarizes the putative orthodox aquaporin protein sequences found in available genomes of yeast and filamentous fungi. Among the 28 yeast genomes sequenced, most species present only one orthodox aquaporin, and no aquaporins were found in eight yeast species. Alignment of amino acid sequences reveals a very diverse group. Similarity values vary from 99% among species within the Saccharomyces genus to 34% between ScAqy1 and the aquaporin from Debaryomyces hansenii. All of the fungal aquaporins possess the known charac...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4279842</comments>
            <pubDate>Thu, 09 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4279842</guid>        </item>
        <item>
            <title>Effects of naturally occurring G103D point mutation of AQP5 on its water permeability, trafficking, and cellular localization in the submandibular gland of rats.</title>
            <link>http://www.medworm.com/index.php?rid=4252304&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21138418%26dopt%3DAbstract</link>
            <description>Conclusion. Replacement of highly conserved hydrophobic 103Gly with strongly hydrophilic 103Asp in rat AQP5, though it did not affect water permeability, may possibly have resulted in less efficient membrane trafficking and increased lysosomal degradation, leading to its lower expression in the apical membrane of the acinar cells in the SMG.
    PMID: 21138418 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252304</comments>
            <pubDate>Wed, 08 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252304</guid>        </item>
        <item>
            <title>Effects of naturally occurring G103D point mutation of AQP5 on its water permeability, trafficking, and cellular localization in the submandibular gland of rats</title>
            <link>http://www.medworm.com/index.php?rid=4241537&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100086</link>
            <description>Conclusion. Replacement of highly conserved hydrophobic 103Gly with strongly hydrophilic 103Asp in rat AQP5, though it did not affect water permeability, may possibly have resulted in less efficient membrane trafficking and increased lysosomal degradation, leading to its lower expression in the apical membrane of the acinar cells in the SMG. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4241537</comments>
            <pubDate>Wed, 08 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4241537</guid>        </item>
        <item>
            <title>Nuclear Spectrin-like proteins are structural actin binding proteins in plants</title>
            <link>http://www.medworm.com/index.php?rid=4213681&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100083</link>
            <description>Conclusions. These results reveal that the plant nucleus contains suggest that spectrin-like proteins s that are structural nuclear components and function as actin binding proteins. Their intranuclear distribution suggests that plant nuclear spectrin-like proteins could be involved in multiple nuclear functions. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4213681</comments>
            <pubDate>Tue, 30 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4213681</guid>        </item>
        <item>
            <title>CDC25B associates with a centrin 2-containing complex and is involved in maintaining centrosome integrity</title>
            <link>http://www.medworm.com/index.php?rid=4196835&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100111</link>
            <description>Conclusions. Our data therefore suggest that CDC25B associates with a centrin 2-containing multiprotein complex in the cytoplasm, which targets it to the centrosome, where it plays a role in maintaining the centrosome levels of centrin 2 and a number of other centrosome components. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4196835</comments>
            <pubDate>Tue, 23 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4196835</guid>        </item>
        <item>
            <title>How ubiquitination and autophagy participate in the regulation of the cell response to bacterial infection.</title>
            <link>http://www.medworm.com/index.php?rid=4187250&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21077843%26dopt%3DAbstract</link>
            <description>Authors: Dupont N, Temime-Smaali N, Lafont F
    Bacterial infection relies on the micro-organism's ability to orchestrate the host's cell signalling such that the immune response is not activated. Conversely, the host cell has dedicated signalling pathways for coping with intrusions by pathogens. The autophagy of foreign micro-organisms (known as xenophagy) has emerged as one of the most powerful of these pathways, although the triggering mode remains largely unknown. In the present paper, we discuss the role that certain post-translational modifications (primarily ubiquitination) may play in the activation of xenophagy and how some bacteria have evolved mechanisms to subvert or hijack this process. In particular, we address the role played by P62/SQSTM1 (sequestosome 1). Finally, we disc...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187250</comments>
            <pubDate>Sun, 21 Nov 2010 01:50:20 +0100</pubDate>
            <guid isPermaLink="false">4187250</guid>        </item>
        <item>
            <title>Non-coding RNAs and their epigenetic regulatory mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=4187249&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21077844%26dopt%3DAbstract</link>
            <description>Authors: Zhou H, Hu H, Lai M
    It is widely accepted that ncRNAs (non-coding RNAs), as opposed to protein-coding RNAs, represent the majority of human transcripts; and the regulatory roles of many of these ncRNAs have been elucidated over the past decade. One important role so far recognized for ncRNAs is their participation in the epigenetic regulation of genes. Indeed, it is becoming increasingly apparent that most epigenetic mechanisms of gene expression are controlled by ncRNAs. In this review, the different types of ncRNA that are strongly linked to epigenetic regulation are characterized and their possible mechanisms discussed.
    PMID: 21077844 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4187249</comments>
            <pubDate>Sun, 21 Nov 2010 01:50:09 +0100</pubDate>
            <guid isPermaLink="false">4187249</guid>        </item>
        <item>
            <title>TPA up-regulates the transcription of Axl by AP-1 transcription factor binding to TRE sequences via the MAPK cascade in leukaemia cells</title>
            <link>http://www.medworm.com/index.php?rid=4118291&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100094</link>
            <description>Conclusions: Taken together our data suggests that TPA-induced Axl gene expression in leukemia cells is mediated by AP-1 motifs and 5xTGCGTG repeats within the promoter region -660/-580, and through the PKC/ERK1/2/AP-1 or PKC/p-38/AP-1 signalling axis (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4118291</comments>
            <pubDate>Mon, 25 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4118291</guid>        </item>
        <item>
            <title>TPA up-regulates the transcription of Axl by AP-1 transcription factor binding to TRE sequences via the MAPK cascade in leukaemia cells.</title>
            <link>http://www.medworm.com/index.php?rid=4108365&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20977427%26dopt%3DAbstract</link>
            <description>Conclusions: Taken together our data suggests that TPA-induced Axl gene expression in leukemia cells is mediated by AP-1 motifs and 5xTGCGTG repeats within the promoter region -660/-580, and through the PKC/ERK1/2/AP-1 or PKC/p-38/AP-1 signalling axis.
    PMID: 20977427 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4108365</comments>
            <pubDate>Mon, 25 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4108365</guid>        </item>
        <item>
            <title>Expression of ctBP family protein isoforms in breast cancer and their role in chemoresistance</title>
            <link>http://www.medworm.com/index.php?rid=4097455&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100067</link>
            <description>Conclusions. These studies support recent evidence that CtBP family proteins represent potential targets for therapeutic strategies for the treatment of cancer in general, and breast cancer in particular (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4097455</comments>
            <pubDate>Thu, 21 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4097455</guid>        </item>
        <item>
            <title>Expression of ctBP family protein isoforms in breast cancer and their role in chemoresistance.</title>
            <link>http://www.medworm.com/index.php?rid=4089077&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20964627%26dopt%3DAbstract</link>
            <description>Conclusions. These studies support recent evidence that CtBP family proteins represent potential targets for therapeutic strategies for the treatment of cancer in general, and breast cancer in particular.
    PMID: 20964627 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4089077</comments>
            <pubDate>Thu, 21 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4089077</guid>        </item>
        <item>
            <title>A comparison of primary oesophageal squamous epithelial cells with HET-1A in organotypic culture.</title>
            <link>http://www.medworm.com/index.php?rid=3982282&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20843300%26dopt%3DAbstract</link>
            <description>Conclusion Studies of epithelial carcinogenesis will benefit from culture systems which allow the manipulation of the stromal and epithelial layers independently. We have developed an organotypic culture using primary oesophageal squamous cells and fibroblasts in which a stratified epithelium with a proliferative basal layer that stains strongly for ÎNp63 develops. This model will be suitable for the study of the molecular events in the development of Barrett's oesophagus. The most commonly used normal oesophageal squamous cell line, HET-1A, does not have the characteristics of normal oesophageal squamous cells, and should not be used in models of the normal oesophageal epithelium. Until more representative cell lines are available, future studies in oesophageal cancer will be reliant o...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3982282</comments>
            <pubDate>Tue, 14 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3982282</guid>        </item>
        <item>
            <title>A comparison of primary oesophageal squamous epithelial cells with HET-1A in organotypic culture</title>
            <link>http://www.medworm.com/index.php?rid=3972722&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100071</link>
            <description>Conclusion
Studies of epithelial carcinogenesis will benefit from culture systems which allow the manipulation of the stromal and epithelial layers independently. We have developed an organotypic culture using primary oesophageal squamous cells and fibroblasts in which a stratified epithelium with a proliferative basal layer that stains strongly for &amp;#x0394;Np63 develops. This model will be suitable for the study of the molecular events in the development of Barrett&amp;#x2019;s oesophagus. The most commonly used normal oesophageal squamous cell line, HET-1A, does not have the characteristics of normal oesophageal squamous cells, and should not be used in models of the normal oesophageal epithelium. Until more representative cell lines are available, future studies in oesophageal cancer will ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3972722</comments>
            <pubDate>Tue, 14 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3972722</guid>        </item>
        <item>
            <title>Reverse genetics in eukaryotes.</title>
            <link>http://www.medworm.com/index.php?rid=3934863&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20812916%26dopt%3DAbstract</link>
            <description>Authors: Hardy S, Legagneux V, Audic Y, Paillard L
    Reverse genetics consists in the modification of the activity of a target gene to analyse the phenotypic consequences. Four main approaches are used towards this goal and will be explained in this review. Two of them are centred on genome alterations. Mutations produced by random chemical or insertional mutagenesis can be screened to recover only mutants in a specific gene of interest. Alternatively, these alterations may be specifically targeted on a gene of interest by HR (homologous recombination). The other two approaches are centred on mRNA. RNA interference is a powerful method to reduce the level of gene products, while MO (morpholino) antisense oligonucleotides alter mRNA metabolism or translation. Some model species, such as D...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3934863</comments>
            <pubDate>Sun, 05 Sep 2010 15:09:03 +0100</pubDate>
            <guid isPermaLink="false">3934863</guid>        </item>
        <item>
            <title>CEMOVIS on a pathogen: analysis of Bacillus anthracis spores.</title>
            <link>http://www.medworm.com/index.php?rid=3912288&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20795943%26dopt%3DAbstract</link>
            <description>In this study we describe the morphology of dormant spores using cryoelectron microscopy of vitrified sections (CEMOVIS). Biosafety measures do not permit freezing of native spores of B. anthracis without chemical fixation. To study the influence of aldehyde fixation on the ultrastructure of the spore we chose to analyse spores of the closely related non pathogen B. cereus T. For none of the investigated structures we could find a difference in morphology induced by aldehyde fixation compared to the native preparations for CEMOVIS. This result legitimises to work with aldehyde fixed spores from B. anthracis. Using CEMOVIS we describe here two new structures present in the spore: A rectangular structure, which connects the BclA filaments with the basal layer of the exosporium and a repetiti...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3912288</comments>
            <pubDate>Wed, 25 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3912288</guid>        </item>
        <item>
            <title>CEMOVIS on a pathogen: analysis of Bacillus anthracis spores</title>
            <link>http://www.medworm.com/index.php?rid=3907454&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100080</link>
            <description>In this study we describe the morphology of dormant spores using cryoelectron microscopy of vitrified sections (CEMOVIS). Biosafety measures do not permit freezing of native spores of B. anthracis without chemical fixation. To study the influence of aldehyde fixation on the ultrastructure of the spore we chose to analyse spores of the closely related non pathogen B. cereus T. For none of the investigated structures we could find a difference in morphology induced by aldehyde fixation compared to the native preparations for CEMOVIS. This result legitimises to work with aldehyde fixed spores from B. anthracis. Using CEMOVIS we describe here two new structures present in the spore: A rectangular structure, which connects the BclA filaments with the basal layer of the exosporium and a repetiti...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3907454</comments>
            <pubDate>Wed, 25 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3907454</guid>        </item>
        <item>
            <title>Golgi apparatus fragmentation as a mechanism responsible for uniform delivery of uroplakins to the apical plasma membrane of uroepithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3912289&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20735355%26dopt%3DAbstract</link>
            <description>Conclusions. The fragmentation of the GA and its spreading to the cell periphery is one of the key events, which promote the uniform delivery of uroplakins over the entire APM of differentiating UCs and thus have a major importance in the final proper formation and maintenance of the blood-urine barrier.
    PMID: 20735355 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3912289</comments>
            <pubDate>Mon, 23 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3912289</guid>        </item>
        <item>
            <title>Golgi apparatus fragmentation as a mechanism responsible for uniform delivery of uroplakins to the apical plasma membrane of uroepithelial cells</title>
            <link>http://www.medworm.com/index.php?rid=3899232&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100024</link>
            <description>Conclusions. The fragmentation of the GA and its spreading to the cell periphery is one of the key events, which promote the uniform delivery of uroplakins over the entire APM of differentiating UCs and thus have a major importance in the final proper formation and maintenance of the blood-urine barrier. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3899232</comments>
            <pubDate>Mon, 23 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3899232</guid>        </item>
        <item>
            <title>Spatial organization of the transforming MHC class II compartment.</title>
            <link>http://www.medworm.com/index.php?rid=3885795&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20712599%26dopt%3DAbstract</link>
            <description>Conclusions: Our data indicate that MIICs have the capacity to fuse together, whereby the cytoskeleton possibly provides a scaffold for the MIIC shape change and directionality. MIIC-like intermediates may represent MHC class II carriers.
    PMID: 20712599 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3885795</comments>
            <pubDate>Sun, 15 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3885795</guid>        </item>
        <item>
            <title>Spatial organization of the transforming MHC class II compartment</title>
            <link>http://www.medworm.com/index.php?rid=3872375&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100046</link>
            <description>Conclusions: Our data indicate that MIICs have the capacity to fuse together, whereby the cytoskeleton possibly provides a scaffold for the MIIC shape change and directionality. MIIC-like intermediates may represent MHC class II carriers. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3872375</comments>
            <pubDate>Sun, 15 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3872375</guid>        </item>
        <item>
            <title>Transcriptional control of genes involved in ciliogenesis: a first step in making cilia.</title>
            <link>http://www.medworm.com/index.php?rid=3855661&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20690903%26dopt%3DAbstract</link>
            <description>Authors: Thomas J, MorlÃ© L, Soulavie F, LaurenÃ§on A, Sagnol S, Durand B
    Cilia and flagella have essential functions in a wide range of organisms. Cilia assembly is dynamic during development and different types of cilia are found in multicellular organisms. How this dynamic and specific assembly is regulated remains an important question in cilia biology. In metazoans, the regulation of the overall expression level of key components necessary for cilia assembly or function is an important way to achieve ciliogenesis control. The FOXJ1 (forkhead box J1) and RFX (regulatory factor X) family of transcription factors have been shown to be important players in controlling ciliary gene expression. They fulfill a complementary and synergistic function by regulating specific and common t...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3855661</comments>
            <pubDate>Thu, 12 Aug 2010 01:12:03 +0100</pubDate>
            <guid isPermaLink="false">3855661</guid>        </item>
        <item>
            <title>Tackling the pathogenesis of RNA nuclear retention in myotonic dystrophy.</title>
            <link>http://www.medworm.com/index.php?rid=3855660&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20690904%26dopt%3DAbstract</link>
            <description>Authors: Mastroyiannopoulos NP, Shammas C, Phylactou LA
    DM1 (myotonic dystrophy type I) is a common form of muscular dystrophy that affects mainly adults. It is a disease that belongs to the group of defective RNA export diseases, since a major part of the pathogenic mechanism of the disease is the retention of the mutant transcripts in the cell nucleus. The presence of an expanded CUG trinucleotide repeat in the 3'-UTR (3'-untranslated region) of the DMPK (myotonic dystrophy protein kinase) gene causes the attraction of RNA-binding proteins by the nuclear-located mutant transcripts. As a result of the occupation of the RNA-binding proteins, there is defective mis-splicing of several cellular transcripts. This is believed to be a major pathogenic mechanism of the disease and any attemp...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3855660</comments>
            <pubDate>Thu, 12 Aug 2010 01:12:03 +0100</pubDate>
            <guid isPermaLink="false">3855660</guid>        </item>
        <item>
            <title>Tissue-type plasminogen activator induces plasmin-dependent proteolysis of intracellular neuronal nitric oxide synthase.</title>
            <link>http://www.medworm.com/index.php?rid=3767371&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20636282%26dopt%3DAbstract</link>
            <description>Conclusion: Altogether, these data provide a new function of tPA in the central nervous system, which likely contributes to its pleiotropic functions.
    PMID: 20636282 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3767371</comments>
            <pubDate>Thu, 15 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3767371</guid>        </item>
        <item>
            <title>Tissue-type plasminogen activator induces plasmin-dependent proteolysis of intracellular neuronal nitric oxide synthase</title>
            <link>http://www.medworm.com/index.php?rid=3761306&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100072</link>
            <description>Conclusion: Altogether, these data provide a new function of tPA in the central nervous system, which likely contributes to its pleiotropic functions. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3761306</comments>
            <pubDate>Thu, 15 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3761306</guid>        </item>
        <item>
            <title>Inhibition of GSK3beta enhances both adhesive and signaling activities of beta-catenin in mouse embryonic stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=3761845&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20626347%26dopt%3DAbstract</link>
            <description>Conclusion.Our data suggest that inhibition of GSK3beta activity in mESCs enhances both the beta-catenin/E-cadherin mediated adhesion and the Tcf/beta-catenin-dependent transcription, but does not activate transcription in majority of the examined genes involved in epithelial-mesenchymal transition and cell cycle progression.
    PMID: 20626347 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3761845</comments>
            <pubDate>Tue, 13 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3761845</guid>        </item>
        <item>
            <title>Inhibition of GSK3{beta} enhances both adhesive and signaling activities of {beta}-catenin in mouse embryonic stem cells</title>
            <link>http://www.medworm.com/index.php?rid=3753614&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100016</link>
            <description>Conclusion.Our data suggest that inhibition of GSK3&amp;#x03B2; activity in mESCs enhances both the &amp;#x03B2;-catenin/E-cadherin mediated adhesion and the Tcf/&amp;#x03B2;-catenin-dependent transcription, but does not activate transcription in majority of the examined genes involved in epithelial-mesenchymal transition and cell cycle progression. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3753614</comments>
            <pubDate>Tue, 13 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3753614</guid>        </item>
        <item>
            <title>Versatility in the acquisition of energy and carbon sources by the Apicomplexa.</title>
            <link>http://www.medworm.com/index.php?rid=3722252&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20586726%26dopt%3DAbstract</link>
            <description>Authors: Polonais V, Soldati-Favre D
    Members of the phylum Apicomplexa are motile and rapidly dividing intracellular parasites, able to occupy a large spectrum of niches by infecting diverse hosts and invading various cell types. As obligate intracellular parasites, most apicomplexans only survive for a short period extracellularly, and, during this time, have a high energy demand to power gliding motility and invasion into new host cells. Similarly, these fast-replicating intracellular parasites are critically dependent on host-cell nutrients as energy and carbon sources, noticeably for the extensive membrane biogenesis imposed during growth and division. To access host-cell metabolites, the apicomplexans Toxoplasma gondii and Plasmodium falciparum have evolved strategies that exquisi...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3722252</comments>
            <pubDate>Sat, 03 Jul 2010 14:09:02 +0100</pubDate>
            <guid isPermaLink="false">3722252</guid>        </item>
        <item>
            <title>Bimolecular fluorescence complementation analysis of eukaryotic fusion products.</title>
            <link>http://www.medworm.com/index.php?rid=3722251&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20590528%26dopt%3DAbstract</link>
            <description>Conclusions: These results support the possibility that chromosomal instability characteristic of tumor cells may be incurred as a consequence of cell fusion and suggest the role of cell fusion in carcinogenesis may have been masked to this point for lack of an inducible method to track cell fusion. In sum, the BiFC-based approach described here allows for comprehensive studies of the mechanism and biological impact of cell fusion in nature.
    PMID: 20590528 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3722251</comments>
            <pubDate>Wed, 30 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3722251</guid>        </item>
        <item>
            <title>Bimolecular fluorescence complementation analysis of eukaryotic fusion products</title>
            <link>http://www.medworm.com/index.php?rid=3718212&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100033</link>
            <description>Conclusions: These results support the possibility that chromosomal instability characteristic of tumor cells may be incurred as a consequence of cell fusion and suggest the role of cell fusion in carcinogenesis may have been masked to this point for lack of an inducible method to track cell fusion. In sum, the BiFC-based approach described here allows for comprehensive studies of the mechanism and biological impact of cell fusion in nature. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3718212</comments>
            <pubDate>Wed, 30 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3718212</guid>        </item>
        <item>
            <title>Sodium fluoride induces podosome formation in endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3610638&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20504277%26dopt%3DAbstract</link>
            <description>Conclusions. Taken together, our findings establish NaF as a novel inducer of podosomes in endothelial cells, in vitro.
    PMID: 20504277 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3610638</comments>
            <pubDate>Tue, 25 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3610638</guid>        </item>
        <item>
            <title>Sodium fluoride induces podosome formation in endothelial cells</title>
            <link>http://www.medworm.com/index.php?rid=3599264&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100030</link>
            <description>Conclusions. Taken together, our findings establish NaF as a novel inducer of podosomes in endothelial cells, in vitro. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3599264</comments>
            <pubDate>Tue, 25 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3599264</guid>        </item>
        <item>
            <title>Munc18 and Munc13 Regulate Early Neurite Outgrowth.</title>
            <link>http://www.medworm.com/index.php?rid=3600268&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20497124%26dopt%3DAbstract</link>
            <description>Conclusion: These data suggest that the inability of vesicle fusion in the growth cone affects outgrowth during the initial phases when outgrowth speed is high, but not during/after synaptogenesis. Overall, outgrowth speed is probably not rate limiting during neuronal network formation at least in vitro. In addition, Munc18, but not Munc13, regulates growth cone filopodia, potentially via its previously observed effect on filamentous actin.
    PMID: 20497124 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3600268</comments>
            <pubDate>Tue, 18 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3600268</guid>        </item>
        <item>
            <title>Munc18 and Munc13 Regulate Early Neurite Outgrowth</title>
            <link>http://www.medworm.com/index.php?rid=3577191&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100036</link>
            <description>Conclusion: These data suggest that the inability of vesicle fusion in the growth cone affects outgrowth during the initial phases when outgrowth speed is high, but not during/after synaptogenesis. Overall, outgrowth speed is probably not rate limiting during neuronal network formation at least in vitro. In addition, Munc18, but not Munc13, regulates growth cone filopodia, potentially via its previously observed effect on filamentous actin. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3577191</comments>
            <pubDate>Tue, 18 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3577191</guid>        </item>
        <item>
            <title>Visualizing protein interactions involved in the formation of the 42S RNP storage particle of Xenopus oocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3508640&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20415665%26dopt%3DAbstract</link>
            <description>Conclusions. The microscopic approach described allows visualization of protein-protein interactions involved in the assembly of 42S storage particles. In particular the transfection assay using COS-7 cells provides a rapid screening test that should facilitate identification of critical residues and structural determinants that enable the proteins of the 42S storage particle to interact with each other and to establish distinct higher-order RNP complexes.
    PMID: 20415665 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3508640</comments>
            <pubDate>Sun, 25 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3508640</guid>        </item>
        <item>
            <title>Solute transporters and aquaporins are impaired in celiac disease.</title>
            <link>http://www.medworm.com/index.php?rid=3508639&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20415666%26dopt%3DAbstract</link>
            <description>Conclusions: Our results indicate that the main routes for water and solute absorption are deficient in celiac disease and may play a role in malabsorption symptoms onset.
    PMID: 20415666 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3508639</comments>
            <pubDate>Sun, 25 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3508639</guid>        </item>
        <item>
            <title>Visualizing protein interactions involved in the formation of the 42S RNP storage particle of Xenopus oocytes</title>
            <link>http://www.medworm.com/index.php?rid=3504760&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100034</link>
            <description>Conclusions. The microscopic approach described allows visualization of protein-protein interactions involved in the assembly of 42S storage particles. In particular the transfection assay using COS-7 cells provides a rapid screening test that should facilitate identification of critical residues and structural determinants that enable the proteins of the 42S storage particle to interact with each other and to establish distinct higher-order RNP complexes. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3504760</comments>
            <pubDate>Sun, 25 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3504760</guid>        </item>
        <item>
            <title>Solute transporters and aquaporins are impaired in celiac disease</title>
            <link>http://www.medworm.com/index.php?rid=3504759&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100023</link>
            <description>Conclusions: Our results indicate that the main routes for water and solute absorption are deficient in celiac disease and may play a role in malabsorption symptoms onset. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3504759</comments>
            <pubDate>Sun, 25 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3504759</guid>        </item>
        <item>
            <title>Direct modifications of Rho proteins: deconstructing GTPase regulation.</title>
            <link>http://www.medworm.com/index.php?rid=3457220&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20377524%26dopt%3DAbstract</link>
            <description>Authors: Visvikis O, Maddugoda MP, Lemichez E
    Small GTPases of the Rho protein family are master regulators of the actin cytoskeleton and are targeted by potent virulence factors of several pathogenic bacteria. Their dysfunctional regulation can lead to severe human pathologies. Both host and bacterial factors can activate or inactivate Rho proteins by direct post-translational modifications: such as deamidation and transglutamination for activation, or ADP-ribosylation, glucosylation, adenylylation and phosphorylation for inactivation. We review and compare these unconventional ways in which both host cells and bacterial pathogens regulate Rho proteins.
    PMID: 20377524 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3457220</comments>
            <pubDate>Sun, 11 Apr 2010 04:54:03 +0100</pubDate>
            <guid isPermaLink="false">3457220</guid>        </item>
        <item>
            <title>Host-cell lipid rafts: a safe door for micro-organisms?</title>
            <link>http://www.medworm.com/index.php?rid=3457219&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20377525%26dopt%3DAbstract</link>
            <description>Authors: Vieira FS, Corr&amp;#xEA;a G, Einicker-Lamas M, Coutinho-Silva R
    The lipid raft hypothesis proposed that these microdomains are small (10-200 nM), highly dynamic and enriched in cholesterol, glycosphingolipids and signalling phospholipids, which compartmentalize cellular processes. These membrane regions play crucial roles in signal transduction, phagocytosis and secretion, as well as pathogen adhesion/interaction. Throughout evolution, many pathogens have developed mechanisms to escape from the host immune system, some of which are based on the host membrane microdomain machinery. Thus lipid rafts might be exploited by pathogens as signalling and entry platforms. In this review, we summarize the role of lipid rafts as players in the overall invasion process used by different path...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3457219</comments>
            <pubDate>Sun, 11 Apr 2010 04:54:03 +0100</pubDate>
            <guid isPermaLink="false">3457219</guid>        </item>
        <item>
            <title>MAP kinases ERK1/2 activation by cell swelling in turbot hepatocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3457218&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20377528%26dopt%3DAbstract</link>
            <description>Conclusions. In turbot hepatocytes, hypo-osmotic swelling but not hyper-osmotic shrinkage induced the activation of ERK1/2. However these proteins do not seem to be involved in RVD process. Their hypo-osmotic-induced activation is partially due to cascades of signalling events triggered by the binding of released ATP on purinergic P2 receptors and requires the presence of calcium.
    PMID: 20377528 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3457218</comments>
            <pubDate>Thu, 08 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3457218</guid>        </item>
        <item>
            <title>Relationships between plasma membrane microdomains and HIV-1 assembly.</title>
            <link>http://www.medworm.com/index.php?rid=3435309&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20356318%26dopt%3DAbstract</link>
            <description>Authors: Ono A
    Advances in cell biology and biophysics revealed that cellular membranes consist of multiple microdomains with specific sets of components such as lipid rafts and TEMs (tetraspanin-enriched microdomains). An increasing number of enveloped viruses have been shown to utilize these microdomains during their assembly. Among them, association of HIV-1 (HIV type 1) and other retroviruses with lipid rafts and TEMs within the PM (plasma membrane) is well documented. In this review, I describe our current knowledge on interrelationships between PM microdomain organization and the HIV-1 particle assembly process. Microdomain association during virus particle assembly may also modulate subsequent virus spread. Potential roles played by microdomains will be discussed with regard to ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3435309</comments>
            <pubDate>Sat, 03 Apr 2010 16:56:02 +0100</pubDate>
            <guid isPermaLink="false">3435309</guid>        </item>
        <item>
            <title>ESCRT &amp; Co.</title>
            <link>http://www.medworm.com/index.php?rid=3362873&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20222872%26dopt%3DAbstract</link>
            <description>In conclusion, the discovery of novel interactors has and will extend our knowledge of the biological roles of ESCRTs.
    PMID: 20222872 [PubMed - in process] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362873</comments>
            <pubDate>Sun, 14 Mar 2010 03:50:04 +0100</pubDate>
            <guid isPermaLink="false">3362873</guid>        </item>
        <item>
            <title>Calcium and polyphosphate-containing acidocalcisomes in chicken egg yolk.</title>
            <link>http://www.medworm.com/index.php?rid=3331336&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20196772%26dopt%3DAbstract</link>
            <description>Conclusions. The data presented in the present study identify a novel organelle in chicken egg yolk composed of acidic vesicles with morphology, physiology, and composition similar to those of acidocalcisomes, within larger acidic vacuoles. The elemental composition of these acidocalcisomes is proportionally similar to the elemental composition of the yolk suggesting that most of these elements are located in these organelles, which might be an important storage compartment in eggs.
    PMID: 20196772 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3331336</comments>
            <pubDate>Wed, 03 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3331336</guid>        </item>
        <item>
            <title>Calcium and polyphosphate-containing acidocalcisomes in chicken egg yolk</title>
            <link>http://www.medworm.com/index.php?rid=3326788&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100011</link>
            <description>Conclusions. The data presented in the present study identify a novel organelle in chicken egg yolk composed of acidic vesicles with morphology, physiology, and composition similar to those of acidocalcisomes, within larger acidic vacuoles. The elemental composition of these acidocalcisomes is proportionally similar to the elemental composition of the yolk suggesting that most of these elements are located in these organelles, which might be an important storage compartment in eggs. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3326788</comments>
            <pubDate>Wed, 03 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3326788</guid>        </item>
        <item>
            <title>Influence of MT7 toxin on the oligomerization state of the M1 muscarinic receptor.</title>
            <link>http://www.medworm.com/index.php?rid=3303375&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20170475%26dopt%3DAbstract</link>
            <description>Conclusion. Our results suggest that MT7 toxin binds to a dimeric form of hM1 receptor, favouring the stability of this receptor state at the cellular level, probably by inducing some conformational rearrangements of the pre-existing muscarinic receptor homodimers.
    PMID: 20170475 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3303375</comments>
            <pubDate>Mon, 22 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3303375</guid>        </item>
        <item>
            <title>Influence of MT7 toxin on the oligomerization state of the M1 muscarinic receptor</title>
            <link>http://www.medworm.com/index.php?rid=3294462&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090171</link>
            <description>Conclusion. Our results suggest that MT7 toxin binds to a dimeric form of hM1 receptor, favouring the stability of this receptor state at the cellular level, probably by inducing some conformational rearrangements of the pre-existing muscarinic receptor homodimers. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3294462</comments>
            <pubDate>Mon, 22 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3294462</guid>        </item>
        <item>
            <title>Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes.</title>
            <link>http://www.medworm.com/index.php?rid=3270060&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20146669%26dopt%3DAbstract</link>
            <description>Authors: Lanyon-Hogg T, Warriner SL, Baker A
    Peroxisomes are a family of organelles which have many unusual features. They can arise de novo from the endoplasmic reticulum by a still poorly characterized process, yet possess a unique machinery for the import of their matrix proteins. As peroxisomes lack DNA, their function, which is highly variable and dependent on developmental and/or environmental conditions, is determined by the post-translational import of specific metabolic enzymes in folded or oligomeric states. The two classes of matrix targeting signals for peroxisomal proteins [PTS1 (peroxisomal targeting signal 1) and PTS2] are recognized by cytosolic receptors [PEX5 (peroxin 5) and PEX7 respectively] which escort their cargo proteins to, or possibly across, the peroxisome me...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3270060</comments>
            <pubDate>Sun, 14 Feb 2010 01:28:03 +0100</pubDate>
            <guid isPermaLink="false">3270060</guid>        </item>
        <item>
            <title>Chemistry-based protein modification strategy for endocytic pathway analysis.</title>
            <link>http://www.medworm.com/index.php?rid=3213260&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20100171%26dopt%3DAbstract</link>
            <description>Conclusions. Our vectorial concept proposes a new chemical approach for traffic-based profiling of proteins that may prove to be applicable to the analysis of diverse endocytic pathways.
    PMID: 20100171 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3213260</comments>
            <pubDate>Mon, 25 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3213260</guid>        </item>
        <item>
            <title>Chemistry-based protein modification strategy for endocytic pathway analysis</title>
            <link>http://www.medworm.com/index.php?rid=3204697&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20100008</link>
            <description>Conclusions. Our vectorial concept proposes a new chemical approach for traffic-based profiling of proteins that may prove to be applicable to the analysis of diverse endocytic pathways. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3204697</comments>
            <pubDate>Mon, 25 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3204697</guid>        </item>
        <item>
            <title>Intranuclear sphingomyelin is associated with transcriptionally active chromatin and plays a role in nuclear integrity.</title>
            <link>http://www.medworm.com/index.php?rid=3213261&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20095965%26dopt%3DAbstract</link>
            <description>Conclusions. Our observations, supported by biochemical data, provide evidence for the involvement of sphingomyelin in important nuclear functions. They bring additional information pointing out the perichromatin region as an essential functional nuclear domain. Furthermore, they suggest a role for sphingomyelin in the internal nuclear architecture.
    PMID: 20095965 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3213261</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3213261</guid>        </item>
        <item>
            <title>Intranuclear sphingomyelin is associated with transcriptionally active chromatin and plays a role in nuclear integrity</title>
            <link>http://www.medworm.com/index.php?rid=3200359&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090139</link>
            <description>Conclusions. Our observations, supported by biochemical data, provide evidence for the involvement of sphingomyelin in important nuclear functions. They bring additional information pointing out the perichromatin region as an essential functional nuclear domain. Furthermore, they suggest a role for sphingomyelin in the internal nuclear architecture. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3200359</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3200359</guid>        </item>
        <item>
            <title>Intracellular aggregation of human stefin B; confocal and electron microscopy study.</title>
            <link>http://www.medworm.com/index.php?rid=3189551&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20078424%26dopt%3DAbstract</link>
            <description>Conclusions: We have shown that endogenous stefin B aggregates within cells, and that aggregation is increased upon protein over-expression or proteasome inhibition. From confocal and TEM analyses we conclude that aggregates of stefin B show some of the molecular characteristics of aggresomes and may be eliminated from the cell by autophagy. Intracellular stefin B aggregation shows a negative correlation with cell survival.
    PMID: 20078424 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3189551</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3189551</guid>        </item>
        <item>
            <title>Intracellular aggregation of human stefin B; confocal and electron microscopy study</title>
            <link>http://www.medworm.com/index.php?rid=3175729&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090163</link>
            <description>Conclusions: We have shown that endogenous stefin B aggregates within cells, and that aggregation is increased upon protein over-expression or proteasome inhibition. From confocal and TEM analyses we conclude that aggregates of stefin B show some of the molecular characteristics of aggresomes and may be eliminated from the cell by autophagy. Intracellular stefin B aggregation shows a negative correlation with cell survival. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3175729</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3175729</guid>        </item>
        <item>
            <title>Developmental and cellular functions of the ESCRT machinery in pluricellular organisms.</title>
            <link>http://www.medworm.com/index.php?rid=3164636&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20059450%26dopt%3DAbstract</link>
            <description>Authors: Michelet X, Djeddi A, Legouis R
    ESCRTs (endosomal sorting complexes required for transport) were first discovered in yeast and are known to be required in the biogenesis of the MVB (multivesicular body). Most ESCRT research has been carried out in vitro using models such as yeast and mammalian cells in culture. The role of the ESCRTs genes in endosome maturation is conserved from yeast to mammals, but little is known about their function during development in multicellular organisms. Since ESCRTs play a leading role in regulating some cell signalling pathways by addressing receptors to the lysosome, it appears important to monitor ESCRT functions in multicellular models. The present review summarizes recent research on the developmental and cellular functions of the ESCRT in C...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164636</comments>
            <pubDate>Wed, 13 Jan 2010 08:32:02 +0100</pubDate>
            <guid isPermaLink="false">3164636</guid>        </item>
        <item>
            <title>EYA1 Mutations Associated With Branchio-Oto-Renal Syndrome Result In Defective Otic Development in Xenopus laevis</title>
            <link>http://www.medworm.com/index.php?rid=3044478&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090098</link>
            <description>Branchio-Oto-Renal (BOR) syndrome is a dominant disorder most commonly caused by mutations in the EYA1 gene. Symptoms commonly include deafness and renal anomalies. We have used the embryos of the frog Xenopus laevis as an animal model for early ear development to examine the effects of different EYA1 mutations. Four eya1 mRNAs encoding proteins correlated with congenital anomalies in human were injected into early stage embryos. We show that expression of mutations associated with BOR, even in the presence of normal levels of endogenous eya1 mRNA, leads to morphologically abnormal ear development as measured by overall otic vesicle size, establishment of sensory tissue and ear otic innervation patterns. The molecular consequences of mutant eya1 expression were assessed by quantitative PCR...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3044478</comments>
            <pubDate>Tue, 01 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3044478</guid>        </item>
        <item>
            <title>Localisation of translation initiation factors to talin/{beta}3-integrin-enriched adhesion complexes in spreading and migrating mammalian cells</title>
            <link>http://www.medworm.com/index.php?rid=3012215&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090141</link>
            <description>Conclusions Taken together, these findings demonstrate that repression, complex post-transcriptional regulation and modulation of mRNA stability could potentially be taking place along the distal edge of migrating lamellipodia. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3012215</comments>
            <pubDate>Fri, 20 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3012215</guid>        </item>
        <item>
            <title>Polarized traffic towards the cell surface: how to find the route.</title>
            <link>http://www.medworm.com/index.php?rid=3004147&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19909237%26dopt%3DAbstract</link>
            <description>Authors: Carmosino M, Valenti G, Caplan M, Svelto M
    Polarity is the structural and functional hallmark of epithelia. The apical plasma membrane, facing the organism's exterior (the lumen of the gut, renal tubule and glandular duct), differs in many important respects from the basolateral plasma membrane that is apposed to the interior of the organism. The generation and maintenance of epithelial polarity require a highly specialized subcellular machinery to bring proteins to their appropriate sites of action. This is a dynamic process involving the interpretation of sorting signals, vectorial delivery mechanisms, membrane-specific fusion and retention processes. Here, we will provide a review of the field, highlighting recent advances within a historically relevant context.
    PMID: 1...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3004147</comments>
            <pubDate>Wed, 18 Nov 2009 17:46:05 +0100</pubDate>
            <guid isPermaLink="false">3004147</guid>        </item>
        <item>
            <title>The GIT/PIX complexes regulate the chemotactic response of rat basophilic leukemia cells</title>
            <link>http://www.medworm.com/index.php?rid=2992604&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090074</link>
            <description>Conclusions. Our results show that endogenous GIT complexes are involved in the regulation of chemoattractant-induced cell motility and receptor trafficking, and support previous findings indicating an important function of the GIT complexes in the regulation of different G protein-coupled receptors. Our data also indicate that endogenous GIT1 and GIT2 regulate distinct subsets of agonist-induced responses, and suggest a possible functional link between the control of receptor trafficking and the regulation of cell motility by GIT proteins. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2992604</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2992604</guid>        </item>
        <item>
            <title>Members of the CIP4 family of proteins participate in the regulation of platelet-derived growth factor receptor-{beta}-dependent actin reorganization and migration</title>
            <link>http://www.medworm.com/index.php?rid=2984660&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090033</link>
            <description>Conclusions
Our findings shows that CIP4-like proteins induced membrane tubulation downstream of Cdc42 and that they have important roles in PDGF-dependent actin reorganization and cell migration by regulating internalization and activity of the PDGFR&amp;#x03B2;. Moreover, the data suggest an important role for the CIP4-like proteins in the regulation of the activity of the PDGF &amp;#x03B2;-receptor. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2984660</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2984660</guid>        </item>
        <item>
            <title>Modulation of tumorigenesis and estrogen receptor-{alpha} expression by cell culture condition in a stem cell-derived breast epithelial cell line</title>
            <link>http://www.medworm.com/index.php?rid=2973799&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090132</link>
            <description>Conclusion. Estrogen responsive cell line with ER&amp;#x03B1; and CD44&amp;#x002B;/CD24-/low expression can be derived from breast epithelial stem cells. The tumorigenicity and estrogen response of these cells could depend on cell culture condition. The findings of this study have implications in regard to the origins of 1) ER&amp;#x03B1;-positive breast cancers, 2) CD44&amp;#x002B;/CD24-/low breast tumor stem cells and 3) metastatic ability of breast cancer. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2973799</comments>
            <pubDate>Mon, 09 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2973799</guid>        </item>
        <item>
            <title>TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal complex in the testis</title>
            <link>http://www.medworm.com/index.php?rid=2958717&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090091</link>
            <description>Conclusion: We demonstrate here that TLRR interacts with PP1, particularly the testis specific isoform, PP1&amp;#x03B3;2. Immunoaffinity purification confirms that TLRR is associated with the spermatid cytoskeleton. In addition, proteins involved in protein stability are part of the TLRR complex. These results support our hypothesis that TLRR links signaling molecules to the spermatid cytoskeleton in order to regulate important substrates involved in spermatid transformation. The translocation of TLRR from manchette to the centrosome region suggests a possible role for this protein in tail formation. Our finding that TLRR is associated with microtubules in cultured cells suggests that TLRR may play a common role in modulating the cytoskeleton in other cell types besides male germ cells. (Sourc...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2958717</comments>
            <pubDate>Wed, 04 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2958717</guid>        </item>
        <item>
            <title>Focal adhesion kinase-dependent regulation of adhesive force involves vinculin recruitment to focal adhesions</title>
            <link>http://www.medworm.com/index.php?rid=2950596&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090104</link>
            <description>Conclusions. We demonstrate that FAK reduces steady-state adhesion strength by modulating vinculin recruitment to focal adhesions. These findings provide insights into the role of FAK in mechanical interactions between a cell and the extracellular matrix. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2950596</comments>
            <pubDate>Mon, 02 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2950596</guid>        </item>
        <item>
            <title>Role of lipid metabolism in hepatitis C virus assembly and entry.</title>
            <link>http://www.medworm.com/index.php?rid=2935729&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19857204%26dopt%3DAbstract</link>
            <description>Authors: Popescu CI, Dubuisson J
    HCV (hepatitis C virus) represents a major global health problem. A consistent body of evidence has been accumulating, suggesting a peculiar overlap between the HCV life cycle and lipid metabolism. This association becomes evident both for the clinical symptoms of HCV infection and the molecular mechanisms underlying the morphogenesis and entry process of this virus. The HCV core-lipid droplets association seems to be central to the HCV morphogenesis process. Moreover, the biogenesis pathway of very-low-density lipoproteins has been shown to be involved in HCV morphogenesis with MTP (microsomal triacylglycerol transfer protein), ApoB (apolipoprotein B) and ApoE (apolipoprotein E) as essential elements in the production of infectious HCV particles. HCV i...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935729</comments>
            <pubDate>Thu, 29 Oct 2009 09:08:05 +0100</pubDate>
            <guid isPermaLink="false">2935729</guid>        </item>
        <item>
            <title>Adrenomedullin is expressed during rodent dental tissue development and promotes cell growth and mineralisation</title>
            <link>http://www.medworm.com/index.php?rid=2894345&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090122</link>
            <description>Conclusions: During oral and dental development ADM initially localises to epithelial tissue whilst during later stages is present in mineralised secreting cells, including odontoblasts. ADM may regulate proliferation and mineralisation processes during development whilst in adulthood, it may be important in maintaining dental tissue homeostasis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2894345</comments>
            <pubDate>Tue, 13 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2894345</guid>        </item>
        <item>
            <title>Precise and rapid mapping protocol for Correlative Light and Electron Microscopy of small invertebrate organisms</title>
            <link>http://www.medworm.com/index.php?rid=2807452&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090096</link>
            <description>Conclusions: We believe that this technique will contribute to correlative studies in multicellular models, and will facilitate the time-demanding procedure of specimen preparation for any kind of TEM. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2807452</comments>
            <pubDate>Thu, 17 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2807452</guid>        </item>
        <item>
            <title>Secretory phospholipase A promotes MMP-9-mediated cell death by degrading type I collagen via the Erk pathway at an early stage of chondrogenesis</title>
            <link>http://www.medworm.com/index.php?rid=2807451&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090073</link>
            <description>Conclusions:
Taken together, our results suggest that elevated levels of sPLA2 secreted by wing bud mesenchymal cells promote type I collagen degradation by MMP-9 in a manner typical of receptor mediation and that these events lead to apoptotic cell death. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2807451</comments>
            <pubDate>Thu, 17 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2807451</guid>        </item>
        <item>
            <title>Recent development of the mononuclear phagocyte system: in memory of Metchnikoff and Ehrlich on the 100th Anniversary of the 1908 Nobel Prize in Physiology or Medicine.</title>
            <link>http://www.medworm.com/index.php?rid=2789383&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19743965%26dopt%3DAbstract</link>
            <description>Authors: Chang ZL
    Monocytes/macrophages are critical for both immunity and homoeostasis. They are the outposts of the immune system in detecting invading pathogens or foreign antigens for homoeostatic clearance and antigen processing for the initiation and effector stages of both innate and adaptive immunity. In addition, monocytes/macrophages often function as control switches for immune system balance between pro- and anti-inflammatory reactions. In the beginning of this article, I would like to briefly introduce the achievements of Metchnikoff and Ehrlich in immunology, including Metchnikoff's cell theory, since they have both greatly influenced the advancement of modern immunology. Additionally, I will honour the 100th anniversary of the 1908 Nobel Prize in Physiology or Medicine. ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2789383</comments>
            <pubDate>Sun, 13 Sep 2009 03:02:06 +0100</pubDate>
            <guid isPermaLink="false">2789383</guid>        </item>
        <item>
            <title>Class I Rab11-Family Interacting Proteins are binding targets for the Rab14 GTPase</title>
            <link>http://www.medworm.com/index.php?rid=2729960&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090068</link>
            <description>Conclusion
The data presented here, which identifies the class I FIPs as the first putative effector proteins for the Rab14 GTPase, indicates greater complexity in the Rab-binding specificity of the class I FIP proteins. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2729960</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2729960</guid>        </item>
        <item>
            <title>The S-phase checkpoint: targeting the replication fork.</title>
            <link>http://www.medworm.com/index.php?rid=2713521&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19686094%26dopt%3DAbstract</link>
            <description>Authors: Segurado M, Tercero JA
    The S-phase checkpoint is a surveillance mechanism, mediated by the protein kinases Mec1 and Rad53 in the budding yeast Saccharomyces cerevisiae (ATR and Chk2 in human cells, respectively) that responds to DNA damage and replication perturbations by co-ordinating a global cellular response necessary to maintain genome integrity. A key aspect of this response is the stabilization of DNA replication forks, which is critical for cell survival. A defective checkpoint causes irreversible replication-fork collapse and leads to genomic instability, a hallmark of cancer cells. Although the precise mechanisms by which Mec1/Rad53 maintain functional replication forks are currently unclear, our knowledge about this checkpoint function has significantly increased du...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2713521</comments>
            <pubDate>Thu, 20 Aug 2009 06:06:05 +0100</pubDate>
            <guid isPermaLink="false">2713521</guid>        </item>
        <item>
            <title>A novel protein, sperm head and tail associated protein (SHTAP) interacts with cysteine rich secretory protein 2 (CRISP2) during spermatogenesis in the mouse</title>
            <link>http://www.medworm.com/index.php?rid=2708928&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090099</link>
            <description>Conclusions. This study is the first report of the identification, annotation, and expression analysis of the mouse Shtap gene. The redistribution observed during sperm capacitation raises the possibility that SHTAP and the SHTAP-CRISP2 complex play a role in the attainment of sperm functional competence. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2708928</comments>
            <pubDate>Mon, 17 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2708928</guid>        </item>
        <item>
            <title>Interleukin-1{beta} increases gap junctional communication among synovial fibroblasts via the extracellular signal regulated kinase pathway</title>
            <link>http://www.medworm.com/index.php?rid=2674160&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090056</link>
            <description>Conclusions. These data show that interleukin-1&amp;#x03B2; acts through the extracellular signal regulated kinase signaling cascade to alter the expression and function of connexin43 in synovial fibroblasts. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2674160</comments>
            <pubDate>Wed, 05 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2674160</guid>        </item>
        <item>
            <title>Stem/progenitor cells in liver injury repair and regeneration.</title>
            <link>http://www.medworm.com/index.php?rid=2661084&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19642968%26dopt%3DAbstract</link>
            <description>Authors: Zhao Q, Ren H, Zhu D, Han Z
    Morbidity and mortality from cirrhosis is increasing rapidly in the world. Currently, orthotopic liver transplantation is the only definitive therapeutic option. However, its clinical use is limited, because of poor long-term graft survival, donor organ shortage and high costs associated with the procedure. Stem cell replacement strategies are therefore being investigated as an attractive alternative approach to liver repair and regeneration. In this review we discuss recent preclinical and clinical investigations that explore the therapeutic potential of stem cells in repair of liver injuries. Several types of stem cells. including embryonic stem cells, haematopoietic stem cells and mesenchymal stem cells, can be induced to differentiate into hepat...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2661084</comments>
            <pubDate>Sat, 01 Aug 2009 19:14:05 +0100</pubDate>
            <guid isPermaLink="false">2661084</guid>        </item>
        <item>
            <title>Plasma membrane and nuclear envelope integrity during the blebbing stage of apoptosis: a time-lapse study</title>
            <link>http://www.medworm.com/index.php?rid=2641240&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090077</link>
            <description>Conclusions. These results show that the functional integrity of the nuclear envelope and plasma membrane may be conserved until the end of the execution phase of apoptosis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2641240</comments>
            <pubDate>Sun, 26 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2641240</guid>        </item>
        <item>
            <title>Newly-formed E-cadherin contacts do not activate Cdc42 or induce filopodia protrusion in human keratinocytes</title>
            <link>http://www.medworm.com/index.php?rid=2580064&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090048</link>
            <description>Conclusion: We conclude that Cdc42 does not participate in the early events that initiate stable cadherin adhesion in keratinocytes. Yet, it is feasible that Cdc42 may be activated at later time points or by other receptors. Cdc42 can then participate in additional functions during polarization such as Golgi re-positioning or baso-lateral trafficking. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2580064</comments>
            <pubDate>Mon, 06 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2580064</guid>        </item>
        <item>
            <title>The p24 family and selective transport processes at the ER-Golgi interface.</title>
            <link>http://www.medworm.com/index.php?rid=2563027&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19566487%26dopt%3DAbstract</link>
            <description>Authors: Strating JR, Martens GJ
    The secretory pathway is of vital importance for eukaryotic cells and has a pivotal role in the synthesis, sorting, processing and secretion of a large variety of bioactive molecules involved in intercellular communication. One of the key processes in the secretory pathway concerns the transport of cargo proteins from the ER (endoplasmic reticulum) to the Golgi. Type-I transmembrane proteins of approximately 24 kDa are abundantly present in the membranes of the early secretory pathway, and bind the COPI and COPII coat complexes that cover vesicles travelling between the membranes. These p24 proteins are thought to play an important role in the selective transport processes at the ER-Golgi interface, although their exact functioning is still obscure. One...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2563027</comments>
            <pubDate>Fri, 03 Jul 2009 07:04:05 +0100</pubDate>
            <guid isPermaLink="false">2563027</guid>        </item>
        <item>
            <title>Signal transducer and activator of transcription 3 regulates adipocyte differentiation via peroxisome proliferator-activated receptor {gamma}</title>
            <link>http://www.medworm.com/index.php?rid=2555985&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090070</link>
            <description>Conclusions. These data indicate that STAT3 functions as a critical factor for adipogenesis via a mechanism involving the PPAR&amp;#x03B3; activation pathway. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2555985</comments>
            <pubDate>Mon, 29 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2555985</guid>        </item>
        <item>
            <title>Structure-function relationships in telomerase genes.</title>
            <link>http://www.medworm.com/index.php?rid=2527279&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19419346%26dopt%3DAbstract</link>
            <description>Authors: S&amp;#xFD;korov&amp;#xE1; E, Fajkus J
    The TERT (telomerase reverse transcriptase) subunit of telomerase is an intensively studied macromolecule due to its key importance in maintaining genome integrity and role in cellular aging and cancer. In an effort to provide an up-to-date overview of the topic, we discuss the structure of TERT genes, their alternative splicing products and their functions. Nucleotide databases contain more than 90 full-length cDNA sequences of telomerase protein subunits. Numerous in silico, in vitro and in vivo experimental techniques have revealed a great deal of structural and functional data describing particular features of the telomerase subunit in various model organisms. We explore whether particular findings are generally applicable to telomerases or s...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527279</comments>
            <pubDate>Sat, 27 Jun 2009 11:53:26 +0100</pubDate>
            <guid isPermaLink="false">2527279</guid>        </item>
        <item>
            <title>Integrin alpha8beta1 regulates adhesion, migration and proliferation of human intestinal crypt cells via a predominant RhoA/ROCK dependent mechanism.</title>
            <link>http://www.medworm.com/index.php?rid=2527268&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527220%26dopt%3DAbstract</link>
            <description>Conclusions: Integrin alpha8beta1 is expressed in epithelial cells. In intestinal crypt cells, alpha8beta1 is closely involved in the regulation of adhesion, migration and cell proliferation via a predominant RhoA/ROCK dependent mechanism. These results suggest an important role for this integrin in intestinal crypt cell homeostasis.
    PMID: 19527220 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527268</comments>
            <pubDate>Sun, 14 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527268</guid>        </item>
        <item>
            <title>Integrin {alpha}8{beta}1 regulates adhesion, migration and proliferation of human intestinal crypt cells via a predominant RhoA/ROCK dependent mechanism</title>
            <link>http://www.medworm.com/index.php?rid=2508634&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090060</link>
            <description>Conclusions: Integrin &amp;#x03B1;8&amp;#x03B2;1 is expressed in epithelial cells. In intestinal crypt cells, &amp;#x03B1;8&amp;#x03B2;1 is closely involved in the regulation of adhesion, migration and cell proliferation via a predominant RhoA/ROCK dependent mechanism. These results suggest an important role for this integrin in intestinal crypt cell homeostasis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2508634</comments>
            <pubDate>Sun, 14 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2508634</guid>        </item>
        <item>
            <title>Inhibiting Crm1 causes the formation of excess acentriolar spindle poles containing NuMA and B23, but does not affect centrosome numbers.</title>
            <link>http://www.medworm.com/index.php?rid=2527270&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19522705%26dopt%3DAbstract</link>
            <description>Conclusion: Inhibition of Crm1 in early metaphase favors the formation of supplementary acentriolar spindle poles. B23 and NUMA are present at these poles that ultimately focus around the centrosome. Inhibition of Crm1 at metaphase has no effect on the control of centrosome numbers.
    PMID: 19522705 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527270</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527270</guid>        </item>
        <item>
            <title>Inhibiting Crm1 causes the formation of excess acentriolar spindle poles containing NuMA and B23, but does not affect centrosome numbers</title>
            <link>http://www.medworm.com/index.php?rid=2508635&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080218</link>
            <description>Conclusion: Inhibition of Crm1 in early metaphase favors the formation of supplementary acentriolar spindle poles. B23 and NUMA are present at these poles that ultimately focus around the centrosome. Inhibition of Crm1 at metaphase has no effect on the control of centrosome numbers. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2508635</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2508635</guid>        </item>
        <item>
            <title>Altering PI3K-Akt signaling in zebrafish embryos affects Pten phosphorylation and gastrulation.</title>
            <link>http://www.medworm.com/index.php?rid=2527271&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19515017%26dopt%3DAbstract</link>
            <description>Conclusions. These data suggest that Ptena454 regulation is correlated to changes in phospho-Akt levels. We propose a model by which homeostasis in rapidly dividing and migrating embryonic cells depends on a counterbalance between pro-survival signaling employing CK2 and Gsk-3 and the pro-apoptotic activity of Ptena454.
    PMID: 19515017 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527271</comments>
            <pubDate>Tue, 09 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527271</guid>        </item>
        <item>
            <title>Wnt5 is required for notochord cell intercalation in the ascidian Halocynthia roretzi</title>
            <link>http://www.medworm.com/index.php?rid=2463698&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090042</link>
            <description>Conclusion. The present study highlights the role of Wnt5&amp;#x03B1; signal in notochord convergent extension movements in ascidian embryos. Our results raise the novel possibility that Wnt5&amp;#x03B1; functions in a cell-autonomous manner in activation of the Wnt/PCP pathway to polarize the protrusive activity that drives convergent extension. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2463698</comments>
            <pubDate>Mon, 08 Jun 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2463698</guid>        </item>
        <item>
            <title>Wnt5 is required for notochord cell intercalation in the ascidian Halocynthia roretzi.</title>
            <link>http://www.medworm.com/index.php?rid=2527273&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19505288%26dopt%3DAbstract</link>
            <description>Conclusion. The present study highlights the role of Wnt5alpha signal in notochord convergent extension movements in ascidian embryos. Our results raise the novel possibility that Wnt5alpha functions in a cell-autonomous manner in activation of the Wnt/PCP pathway to polarize the protrusive activity that drives convergent extension.
    PMID: 19505288 [PubMed - as supplied by publisher] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527273</comments>
            <pubDate>Sun, 07 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527273</guid>        </item>
        <item>
            <title>The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation.</title>
            <link>http://www.medworm.com/index.php?rid=2527283&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19356152%26dopt%3DAbstract</link>
            <description>Authors: Lankat-Buttgereit B, G&amp;#xF6;ke R
    Pdcd4 (programmed cell death 4) has been known as a tumour suppressor gene and potential target for anticancer therapies for several years. Initially, Pdcd4 was identified as a gene that is up-regulated during apoptosis, but its precise role still remains to be defined. However, there is increasing evidence that Pdcd4 levels influence transcription, as well as translation, modulate different signal transduction pathways and might act as a tumour suppressor. Interestingly, recent data suggest that Pdcd4 function may depend on cell type and/or genetic background. This review summarizes the current knowledge regarding the function and regulation of Pdcd4.
    PMID: 19356152 [PubMed - indexed for MEDLINE] (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527283</comments>
            <pubDate>Sun, 31 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527283</guid>        </item>
        <item>
            <title>Production of reactive oxygen species, impairment of photosynthetic function and dynamic changes of mitochondria are early events in cadmium induced cell death in Arabidopsis thaliana</title>
            <link>http://www.medworm.com/index.php?rid=2423500&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090015</link>
            <description>The effects of Cd on the morphology and function of the chloroplast and mitochondria, as well as on the production and localization of reactive oxygen species (ROS) were studied at the single-cell level in Arabidopsis. Results demonstrated that the morphology of chloroplast changed after Cd treatment, and photochemical efficiency dramatically declined prior to obvious morphological distortion in the chloroplast. A quick burst of ROS was detected after Cd treatment. The ROS appeared first in the mitochondria and subsequently in the chloroplast. Simultaneously, the mitochondria clumped irregularly around the chloroplasts or aggregated in the cytoplasm, and the movement of mitochondria was concomitantly blocked. Furthermore, ROS production could be decreased after pre-treatment with ascorbic ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2423500</comments>
            <pubDate>Tue, 19 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2423500</guid>        </item>
        <item>
            <title>Production of reactive oxygen species, impairment of photosynthetic function and dynamic changes of mitochondria are early events in cadmium induced cell death in Arabidopsis thaliana.</title>
            <link>http://www.medworm.com/index.php?rid=2527275&amp;cid=s_34549_171_f&amp;fid=34549&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19453296%26dopt%3DAbstract</link>
            <description>Authors: Bi Y, Chen W, Zhang W, Zhou Q, Yuan L, Xing D
    The effects of Cd on the morphology and function of the chloroplast and mitochondria, as well as on the production and localization of reactive oxygen species (ROS) were studied at the single-cell level in Arabidopsis. Results demonstrated that the morphology of chloroplast changed after Cd treatment, and photochemical efficiency dramatically declined prior to obvious morphological distortion in the chloroplast. A quick burst of ROS was detected after Cd treatment. The ROS appeared first in the mitochondria and subsequently in the chloroplast. Simultaneously, the mitochondria clumped irregularly around the chloroplasts or aggregated in the cytoplasm, and the movement of mitochondria was concomitantly blocked. Furthermore, ROS produ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527275</comments>
            <pubDate>Mon, 18 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527275</guid>        </item>
        <item>
            <title>The ESCRT-III protein CeVPS-32 is enriched in domains distinct from CeVPS-27 and CeVPS-23 at the endosomal membrane of epithelial cells</title>
            <link>http://www.medworm.com/index.php?rid=2416197&amp;cid=s_34549_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090025</link>
            <description>Within the endocytic pathway, the Endosomal Sorting Complex Required for Transport (ESCRT) machinery is essential for the biogenesis of MultiVesicular Bodies (MVB). In yeast, ESCRTs are recruited at the endosomal membrane and involved in cargo sorting into intralumenal vesicles of the MVB. Here, we characterize the ESCRT-III protein CeVPS-32 in the nematode C. elegans and its interactions with CeVPS-27, CeVPS-23 and CeVPS-4. In contrast to other CevpsE genes, depletion of Cevps-32 is embryonic lethal with severe defects in the remodelling of epithelial cell shape during organogenesis. Furthermore, Cevps-32 animals display an accumulation of enlarged early endosomes in epithelial cells and an accumulation of autophagosomes. CeVPS-32 protein is enriched in epithelial tissues and in residual ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2416197</comments>
            <pubDate>Tue, 12 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2416197</guid>        </item>
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