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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, 16 Mar 2010 18:19:24 +0100</lastBuildDate>
        <item>
            <title>ESCRT &amp; Co.</title>
            <link>http://www.medworm.com/index.php?rid=3362873&amp;cid=s_37622_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>
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        <item>
            <title>Calcium and polyphosphate-containing acidocalcisomes in chicken egg yolk.</title>
            <link>http://www.medworm.com/index.php?rid=3331336&amp;cid=s_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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>Altering PI3K-Akt signaling in zebrafish embryos affects Pten phosphorylation and gastrulation.</title>
            <link>http://www.medworm.com/index.php?rid=2508636&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090034</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. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2508636</comments>
            <pubDate>Tue, 09 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2508636</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_37622_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_37622_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_37622_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_37622_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_37622_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_37622_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>
        <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=2527277&amp;cid=s_37622_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%3D19432559%26dopt%3DAbstract</link>
            <description>Authors: Michelet X, Alberti A, Benkemoun L, Roudier N, Lefebvre C, Legouis R
    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 a...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2527277</comments>
            <pubDate>Mon, 11 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527277</guid>        </item>
        <item>
            <title>Cell cycle analysis of fetal germ cells during sex differentiation in mice</title>
            <link>http://www.medworm.com/index.php?rid=2397768&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20090021</link>
            <description>Conclusion: This study has provided a detailed analysis of cell cycle gene expression during fetal germ cell development and identified candidate factors warranting further investigation in order to understand cases of aberrant cell cycle control in these specialised 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=2397768</comments>
            <pubDate>Wed, 06 May 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2397768</guid>        </item>
        <item>
            <title>Cell cycle analysis of fetal germ cells during sex differentiation in mice.</title>
            <link>http://www.medworm.com/index.php?rid=2527281&amp;cid=s_37622_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%3D19419345%26dopt%3DAbstract</link>
            <description>Conclusion: This study has provided a detailed analysis of cell cycle gene expression during fetal germ cell development and identified candidate factors warranting further investigation in order to understand cases of aberrant cell cycle control in these specialised cells.
    PMID: 19419345 [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=2527281</comments>
            <pubDate>Tue, 05 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2527281</guid>        </item>
        <item>
            <title>Distribution, pharmacological characterization and function of the translocator protein (18kDa) in rat small intestine</title>
            <link>http://www.medworm.com/index.php?rid=2367329&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080231</link>
            <description>Conclusions: The functional differences in subpopulations of TSPO in different regions of the intestine could be related to structural organization of mitochondrial protein complexes that mediate the ability of TSPO to modulate either chloride secretion or absorption in the duodenum and ileum, respectively. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2367329</comments>
            <pubDate>Fri, 24 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2367329</guid>        </item>
        <item>
            <title>Emerin-prelamin A interplay in human fibroblasts</title>
            <link>http://www.medworm.com/index.php?rid=2301077&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080175</link>
            <description>Conclusion.
These results indicate that emerin-prelamin A interplay influences nuclear organization. This finding may be relevant to the understanding of laminopathies. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2301077</comments>
            <pubDate>Thu, 26 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2301077</guid>        </item>
        <item>
            <title>Role of 5'- and 3'-untranslated regions of mRNAs in human diseases.</title>
            <link>http://www.medworm.com/index.php?rid=2261486&amp;cid=s_37622_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%3D19275763%26dopt%3DAbstract</link>
            <description>Authors: Chatterjee S, Pal JK
    Protein synthesis is often regulated at the level of initiation of translation, making it a critical step. This regulation occurs by both the cis-regulatory elements, which are located in the 5'- and 3'-UTRs (untranslated regions), and trans-acting factors. A breakdown in this regulation machinery can perturb cellular metabolism, leading to various physiological abnormalities. The highly structured UTRs, along with features such as GC-richness, upstream open reading frames and internal ribosome entry sites, significantly influence the rate of translation of mRNAs. In this review, we discuss how changes in the cis-regulatory sequences of the UTRs, for example, point mutations and truncations, influence expression of specific genes at the level of translatio...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2261486</comments>
            <pubDate>Sat, 14 Mar 2009 16:01:38 +0100</pubDate>
            <guid isPermaLink="false">2261486</guid>        </item>
        <item>
            <title>Cross-talk between the VEGF-A and HGF signalling pathways in endothelial cells</title>
            <link>http://www.medworm.com/index.php?rid=2261268&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080221</link>
            <description>Conclusions. Under angiogenic conditions, combining VEGF-A with HGF can promote neovascularisation by enhancing intracellular signalling and allowing more finely regulated control of the signalling molecules involved in the regulation of the cytoskeleton and cellular migration and morphogenesis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2261268</comments>
            <pubDate>Thu, 12 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2261268</guid>        </item>
        <item>
            <title>Two new miR-16 targets: Caprin-1 and HMGA1, proteins implicated in cell proliferation</title>
            <link>http://www.medworm.com/index.php?rid=2224261&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080213</link>
            <description>Conclusions:
Taken together, our data demonstrated that miR-16 can negatively regulate the two new targets HMGA1 and caprin-1 involved in cell proliferation. In addition, we also showed that the inhibition of cyclin E expression was due, at least in part, to a decrease in its mRNA stability. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2224261</comments>
            <pubDate>Fri, 27 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2224261</guid>        </item>
        <item>
            <title>Ins(1,4,5)P3 receptor type 1 associates with AKAP9 (AKAP450 variant) and protein kinase A type II{beta} in the Golgi apparatus in cerebellar granule cells</title>
            <link>http://www.medworm.com/index.php?rid=2212547&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080184</link>
            <description>Conclusions. Taken together these results suggest that InsP3R1 forms a complex with AKAP450 and PKAII&amp;#x03B2; localised in the Golgi apparatus of cerebellar granule cells. By contrast, the association of InsP3R1 with PKA in Purkinje cells would require a different macromolecular complex. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2212547</comments>
            <pubDate>Tue, 24 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2212547</guid>        </item>
        <item>
            <title>Progesterone induces nano-scale molecular modifications on endometrial epithelial cell surfaces</title>
            <link>http://www.medworm.com/index.php?rid=2212546&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080189</link>
            <description>Conclusions &amp;#x2013; Progesterone treatment induces changes to the cell surface as a result of nanoscale molecular modifications in response to external hormonal treatments. AFM provides the basis for the identification, visualisation and quantification of these cell surface nanoscale changes. Together these findings demonstrate the utility of AFM for use in reproductive science and cancer biology where it could be applied in both in vitro analysis of protein structure-function relationships and clinical diagnosis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2212546</comments>
            <pubDate>Tue, 24 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2212546</guid>        </item>
        <item>
            <title>Histone deacetylases: salesmen and customers in the post-translational modification market.</title>
            <link>http://www.medworm.com/index.php?rid=2182348&amp;cid=s_37622_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%3D19207105%26dopt%3DAbstract</link>
            <description>Authors: Brandl A, Heinzel T, Kr&amp;#xE4;mer OH
    HDACs (histone deacetylases) are enzymes that remove the acetyl moiety from N-epsilon-acetylated lysine residues in histones and non-histone proteins. In recent years, it has turned out that HDACs themselves are also subject to post-translational modification. Such structural alterations can determine the stability, localization, activity and protein-protein interactions of HDACs. This subsequently affects the modification of their substrates and the co-ordination of cellular signalling networks. Intriguingly, physiologically relevant non-histone proteins are increasingly found to be deacetylated by HDACs, and aberrant deacetylase activity contributes to several severe human diseases. Targeting the catalytic activity of these enzymes and the...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2182348</comments>
            <pubDate>Fri, 13 Feb 2009 17:56:27 +0100</pubDate>
            <guid isPermaLink="false">2182348</guid>        </item>
        <item>
            <title>Spatiotemporal activation of caspase-dependent and -independent pathways in staurosporine-induced apoptosis of p53wt and p53mt human cervical carcinoma cells</title>
            <link>http://www.medworm.com/index.php?rid=2184799&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080164</link>
            <description>Conclusions. Our data highlight that staurosporine engages the intrinsic mitochondrial apoptotic pathway via caspase-8 or caspase-9 signalling cascades and via caspase-independent cell death, as well as through p53 activity. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2184799</comments>
            <pubDate>Fri, 13 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2184799</guid>        </item>
        <item>
            <title>The ribonome: a dominant force in co-ordinating gene expression.</title>
            <link>http://www.medworm.com/index.php?rid=2121416&amp;cid=s_37622_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%3D19152504%26dopt%3DAbstract</link>
            <description>Authors: Mansfield KD, Keene JD
    The ribonome is the total cellular complement of RNAs and their regulatory factors functioning dynamically in time and space within ribonucleoprotein complexes. We theorize that the ribonome is an ancient central co-ordinator that has evolved to communicate on multiple levels to the proteome on the one hand (feed-forward), and the transcriptome and RNA processing machinery on the other (feed-back). Furthermore, the ribonome can potentially communicate to other cells horizontally with implications for biological information transfer and for the evolution of both RNA and DNA operating systems. The post-transcriptional RNA operon theory of co-regulated gene expression accounts for the co-ordinated dynamics of RNA-binding proteins within the cellular ribonom...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2121416</comments>
            <pubDate>Thu, 22 Jan 2009 08:27:00 +0100</pubDate>
            <guid isPermaLink="false">2121416</guid>        </item>
        <item>
            <title>The function of ROCO proteins in health and disease.</title>
            <link>http://www.medworm.com/index.php?rid=2121415&amp;cid=s_37622_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%3D19152505%26dopt%3DAbstract</link>
            <description>Authors: Lewis PA
    The ROCO family of multidomain proteins extends across the eukaryotes, and has been implicated in numerous cellular processes. Following the description of mutations causing PD (Parkinson's disease) in a human representative of the ROCO family, LRRK2 (leucine-rich repeat kinase 2), a great deal of research has been carried out into these proteins. This review examines the published data regarding the roles the ROCO proteins are thought to play in cell processes, and how the structure and domain organization of these proteins relates to their function.
    PMID: 19152505 [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=2121415</comments>
            <pubDate>Thu, 22 Jan 2009 08:26:56 +0100</pubDate>
            <guid isPermaLink="false">2121415</guid>        </item>
        <item>
            <title>Evidence for cross-reactivity of JAM-C antibodies: Implications for cellular localization studies</title>
            <link>http://www.medworm.com/index.php?rid=2105410&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080130</link>
            <description>Conclusions. These results demonstrate that a majority of available anti-human JAM-C antibodies cross-react with phosphorylated K8 and suggest that cellular localization studies using these reagents should be interpreted with caution. Of the JAM-C antibodies tested, only mAb PACA4 is monospecific for human JAM-C. Analyses using PACA4 reveal that JAM-C expression is variable in different epithelial cell lines with co-localization at TJs. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2105410</comments>
            <pubDate>Wed, 14 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2105410</guid>        </item>
        <item>
            <title>GFP-targeting allows visualisation of the apicoplast throughout the life cycle of live malaria parasites</title>
            <link>http://www.medworm.com/index.php?rid=2105409&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080202</link>
            <description>In this study, we have generated P. berghei parasites in which GFP is targeted to the apicoplast using the specific targeting sequence of acyl carrier protein (ACP), which has allowed us to visualise this organelle in live Plasmodium parasites. During each phase of asexual reproduction, the apicoplast becomes highly branched, but remains as a single organelle until the completion of nuclear division, whereupon it divides and is rapidly segregated into newly forming daughter cells. We have shown that the antimicrobial agents azithromycin, clindamycin and doxycycline block development of the apicoplast during exo-erythrocytic schizogony in vitro, leading to impaired parasite maturation.
Using a range of powerful live microscopy techniques, we show for the first time the development of a Plas...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2105409</comments>
            <pubDate>Wed, 14 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2105409</guid>        </item>
        <item>
            <title>Actin filaments: key players in the control of asymmetric divisions in mouse oocytes.</title>
            <link>http://www.medworm.com/index.php?rid=2046577&amp;cid=s_37622_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%3D19076067%26dopt%3DAbstract</link>
            <description>Authors: Azoury J, Verlhac MH, Dumont J
    Meiotic maturation is characterized by the succession of two asymmetric divisions each giving rise to a small polar body and a large oocyte. These highly asymmetric divisions are characteristic of meiosis in higher organisms. They allow most of the maternal stores to be retained in the oocyte, a vital property for further embryo development. In mouse oocytes, the asymmetry is ensured by the migration and the anchoring of the division spindle to the cortex in meiosis I and by its anchoring to the cortex in meiosis II. In addition, and subsequent to this off-centre positioning of the spindle, a differentiation of the cortex overhanging the chromosomes takes place and is necessary for the extrusion of small polar bodies. In the present review, we wi...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2046577</comments>
            <pubDate>Thu, 18 Dec 2008 09:49:39 +0100</pubDate>
            <guid isPermaLink="false">2046577</guid>        </item>
        <item>
            <title>Small regulatory non-coding RNAs in bacteria: physiology and mechanistic aspects.</title>
            <link>http://www.medworm.com/index.php?rid=2046576&amp;cid=s_37622_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%3D19076068%26dopt%3DAbstract</link>
            <description>Authors: Repoila F, Darfeuille F
    Regulatory ncRNAs (non-coding RNAs) adjust bacterial physiology in response to environmental cues. ncRNAs can base-pair to mRNAs and change their translation efficiency and/or their stability, or they can bind to proteins and modulate their activity. ncRNAs have been discovered in several species throughout the bacterial kingdom. This review illustrates the diversity of physiological processes and molecular mechanisms where ncRNAs are key regulators.
    PMID: 19076068 [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=2046576</comments>
            <pubDate>Thu, 18 Dec 2008 09:49:34 +0100</pubDate>
            <guid isPermaLink="false">2046576</guid>        </item>
        <item>
            <title>Membrane remodeling during vaccinia virus morphogenesis</title>
            <link>http://www.medworm.com/index.php?rid=2029378&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080176</link>
            <description>Conclusions. The main features observed for the VACV membrane maturation during morphogenesis resemble cellular endomembranes breakdown and reassembly. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2029378</comments>
            <pubDate>Wed, 10 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2029378</guid>        </item>
        <item>
            <title>Spindle assembly defects leading to the formation of a monopolar mitotic apparatus.</title>
            <link>http://www.medworm.com/index.php?rid=2017406&amp;cid=s_37622_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%3D19055485%26dopt%3DAbstract</link>
            <description>Authors: Tillement V, Remy MH, Raynaud-Messina B, Mazzolini L, Haren L, Merdes A
    Mitotic spindle formation in animal cells involves microtubule nucleation from two centrosomes that are positioned at opposite sides of the nucleus. Microtubules are captured by the kinetochores and stabilized. In addition, microtubules can be nucleated independently of the centrosome and stabilized by a gradient of Ran-GTP, surrounding the mitotic chromatin. Complex regulation ensures the formation of a bipolar apparatus, involving motor proteins and controlled polymerization and depolymerization of microtubule ends. The bipolar apparatus is, in turn, responsible for faithful chromosome segregation. During recent years, a variety of experiments has indicated that defects in specific motor proteins, centro...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2017406</comments>
            <pubDate>Sun, 07 Dec 2008 09:27:13 +0100</pubDate>
            <guid isPermaLink="false">2017406</guid>        </item>
        <item>
            <title>Phosphoinositide 3-kinases in cell migration.</title>
            <link>http://www.medworm.com/index.php?rid=2017405&amp;cid=s_37622_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%3D19055486%26dopt%3DAbstract</link>
            <description>Authors: Cain RJ, Ridley AJ
    Cell migration is essential for many biological processes in animals and is a complex highly co-ordinated process that involves cell polarization, actin-driven protrusion and formation and turnover of cell adhesions. The PI3K (phosphoinositide 3-kinase) family of lipid kinases regulate cell migration in many different cell types, both through direct binding of proteins to their lipid products and indirectly through crosstalk with other pathways, such as Rho GTPase signalling. Emerging evidence suggests that the involvement of PI3Ks at different stages of migration varies even within one cell type, and is dependent on the combination of external stimuli, as well as on the signalling status of the cell. In addition, it appears that different PI3K isoforms have...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2017405</comments>
            <pubDate>Sun, 07 Dec 2008 09:27:03 +0100</pubDate>
            <guid isPermaLink="false">2017405</guid>        </item>
        <item>
            <title>MY01, a class XIV myosin, affects developmentally-regulated elimination of the macronucleus during conjugation of Tetrahymena thermophila.</title>
            <link>http://www.medworm.com/index.php?rid=1996158&amp;cid=s_37622_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%3D19032155%26dopt%3DAbstract</link>
            <description>Conclusion. Perturbation of either DNA fragmentation, chromatin condensation or nuclear acidification can lead to blockage of apoptotic-like elimination of the macronucleus in MYO1-knockout conjugants. Consistent with known motor function of myosins and the involvement of Myo1 in vesicle trafficking in Tetrahymena, we argue that Myo1 could specifically affect condensation of chromatin and acidification of the nucleus through direct interaction with chromatin and through Myo1-dependent vesicle trafficking to the nucleus.
    PMID: 19032155 [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=1996158</comments>
            <pubDate>Wed, 26 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1996158</guid>        </item>
        <item>
            <title>MY01, a class XIV myosin, affects developmentally-regulated elimination of the macronucleus during conjugation of Tetrahymena thermophila</title>
            <link>http://www.medworm.com/index.php?rid=1993369&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080198</link>
            <description>Conclusion. Perturbation of either DNA fragmentation, chromatin condensation or nuclear acidification can lead to blockage of apoptotic-like elimination of the macronucleus in MYO1-knockout conjugants. Consistent with known motor function of myosins and the involvement of Myo1 in vesicle trafficking in Tetrahymena, we argue that Myo1 could specifically affect condensation of chromatin and acidification of the nucleus through direct interaction with chromatin and through Myo1-dependent vesicle trafficking to the nucleus. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1993369</comments>
            <pubDate>Wed, 26 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1993369</guid>        </item>
        <item>
            <title>Characterization of MYG1 gene and protein: subcellular distribution and function.</title>
            <link>http://www.medworm.com/index.php?rid=1974846&amp;cid=s_37622_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%3D19014353%26dopt%3DAbstract</link>
            <description>Conclusions. Taken together, we infer that MYG1 is a ubiquitous nucleo-mitochondrial protein, with differential pattern and level of expression during embryonic development. MYG1 expression in normal adult tissues is stable and our data suggest MYG1 involvement in early developmental processes and also in adult stress/illness conditions.
    PMID: 19014353 [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=1974846</comments>
            <pubDate>Tue, 18 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1974846</guid>        </item>
        <item>
            <title>Characterization of MYG1 gene and protein: subcellular distribution and function</title>
            <link>http://www.medworm.com/index.php?rid=1970637&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080086</link>
            <description>Conclusions. Taken together, we infer that MYG1 is a ubiquitous nucleo-mitochondrial protein, with differential pattern and level of expression during embryonic development. MYG1 expression in normal adult tissues is stable and our data suggest MYG1 involvement in early developmental processes and also in adult stress/illness conditions. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1970637</comments>
            <pubDate>Tue, 18 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1970637</guid>        </item>
        <item>
            <title>Extracellular HspBP1 and Hsp72 synergistically activate EGF receptor.</title>
            <link>http://www.medworm.com/index.php?rid=1943259&amp;cid=s_37622_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%3D18986301%26dopt%3DAbstract</link>
            <description>Conclusions. Heat stress and PLC inhibition result in the enhanced secretion of both Hsp72 and HspBP1. In an extracellular environment, the two chaperones interact both physically and functionally leading to the activation of EGFR-ERK1/2 signaling pathway. However, the magnitude of EGFR activation depends on the e-HspBP1/e-Hsp72 ratio in the medium. Extracellular chaperone-mediated activation of EGFR can provide a survival advantage to cells under heat shock and other stresses.
    PMID: 18986301 [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=1943259</comments>
            <pubDate>Wed, 05 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1943259</guid>        </item>
        <item>
            <title>Extracellular HspBP1 and Hsp72 synergistically activate EGF receptor</title>
            <link>http://www.medworm.com/index.php?rid=1935060&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080069</link>
            <description>Conclusions. Heat stress and PLC inhibition result in the enhanced secretion of both Hsp72 and HspBP1. In an extracellular environment, the two chaperones interact both physically and functionally leading to the activation of EGFR-ERK1/2 signaling pathway. However, the magnitude of EGFR activation depends on the e-HspBP1/e-Hsp72 ratio in the medium. Extracellular chaperone-mediated activation of EGFR can provide a survival advantage to cells under heat shock and other stresses. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1935060</comments>
            <pubDate>Wed, 05 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1935060</guid>        </item>
        <item>
            <title>FGF signaling modulates transcriptional repression by Xenopus groucho-related-4.</title>
            <link>http://www.medworm.com/index.php?rid=1938836&amp;cid=s_37622_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%3D18983265%26dopt%3DAbstract</link>
            <description>Conclusions: These data suggest to us a novel molecular mechanism where FGF and Wnt signaling pathways interact at the level of the co-repressor Xgrg4: the weakening of Xgrg4 repression by FGF signaling, combined with the stabilization of beta-catenin by Wnt signals, enhances expression of Wnt target genes.
    PMID: 18983265 [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=1938836</comments>
            <pubDate>Tue, 04 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1938836</guid>        </item>
        <item>
            <title>FGF signaling modulates transcriptional repression by Xenopus groucho-related-4</title>
            <link>http://www.medworm.com/index.php?rid=1931263&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080136</link>
            <description>Conclusions: These data suggest to us a novel molecular mechanism where FGF and Wnt signaling pathways interact at the level of the co-repressor Xgrg4: the weakening of Xgrg4 repression by FGF signaling, combined with the stabilization of &amp;#x03B2;-catenin by Wnt signals, enhances expression of Wnt target genes. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1931263</comments>
            <pubDate>Tue, 04 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1931263</guid>        </item>
        <item>
            <title>Cytoplasmic signalling by the c-Abl tyrosine kinase in normal and cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=1879740&amp;cid=s_37622_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%3D18851712%26dopt%3DAbstract</link>
            <description>Authors: Sirvent A, Benistant C, Roche S
    c-Abl is a non-receptor tyrosine kinase which is localized both in the nucleus and cytoplasm, and is involved in the regulation of cell growth, survival and morphogenesis. Although c-Abl nuclear function has been extensively studied, recent data also indicate an important role in cytoplasmic signalling through mitogenic and adhesive receptors. Here, we review the mechanisms by which growth factors promote cytoplasmic c-Abl activation and signalling and its function in the induction of DNA synthesis, changes in cell morphology and receptor endocytosis. The importance of de-regulated c-Abl cytoplasmic signalling in solid tumours is also discussed.
    PMID: 18851712 [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=1879740</comments>
            <pubDate>Thu, 16 Oct 2008 11:13:58 +0100</pubDate>
            <guid isPermaLink="false">1879740</guid>        </item>
        <item>
            <title>NFAT directly regulates Nkx2-5 transcription during cardiac cell differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=1850890&amp;cid=s_37622_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%3D18828760%26dopt%3DAbstract</link>
            <description>Conclusions. These data suggest that Nkx2-5 is a direct target of NFAT which coordinates with other transcription factors such as GATA4 to regulate Nkx2-5 during cardiogenesis.
    PMID: 18828760 [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=1850890</comments>
            <pubDate>Wed, 01 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1850890</guid>        </item>
        <item>
            <title>NFAT directly regulates Nkx2-5 transcription during cardiac cell differentiation</title>
            <link>http://www.medworm.com/index.php?rid=1841934&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080108</link>
            <description>Conclusions. These data suggest that Nkx2-5 is a direct target of NFAT which coordinates with other transcription factors such as GATA4 to regulate Nkx2-5 during cardiogenesis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1841934</comments>
            <pubDate>Wed, 01 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1841934</guid>        </item>
        <item>
            <title>Characterization of the ubinuclein protein as a new member of the nuclear and adhesion complex components (NaCos)</title>
            <link>http://www.medworm.com/index.php?rid=1838493&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080072</link>
            <description>Conclusions: Ubinuclein mRNA and its corresponding protein are expressed in almost all cell types. Careful analyses have revealed that in most cells ubinuclein occurs in the nucleoplasm, but in cells forming tight junctions it is recruited to the plaque structure of the zonula occludens. This recruitment appears to be dependent on cell density. Hence, ubinuclein is a new NACos (Nuclear and Adhesion Complex components) protein. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1838493</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1838493</guid>        </item>
        <item>
            <title>Discovery of a new RNA containing nuclear structure in UVC-induced apoptotic cells by integrated laser electron microscopy</title>
            <link>http://www.medworm.com/index.php?rid=1838492&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080076</link>
            <description>Conclusions: Because the UV-induced nuclear structure was only found in cells labelled for cleaved caspase-3 it is proposed for an electron microscopic marker for all stages of apoptosis. Such a marker will facilitate especially the screening for early apoptotic cells, which lack the well-known hallmarks of apoptosis within a cell population. It also raises new questions on the mechanisms involved in the UV-induced apoptotic 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=1838492</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1838492</guid>        </item>
        <item>
            <title>Developmental origin of adipocytes: new insights into a pending question.</title>
            <link>http://www.medworm.com/index.php?rid=1802583&amp;cid=s_37622_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%3D18793119%26dopt%3DAbstract</link>
            <description>Authors: Billon N, Monteiro MC, Dani C
    The current epidemic of obesity has caused a surge of interest in the study of adipose tissue formation. Much progress has been made in defining the transcriptional networks controlling the terminal differentiation of preadipocytes into mature adipocytes. However, the mechanisms that direct MSCs (mesenchymal stem cells) down the adipocyte lineage remain largely unknown. Similarly, although adipocytes are generally described to derive from mesoderm, the study of the developmental origin of MSCs and adipose tissues has been largely disregarded until now. Functional variations do exist between different adipose tissues, which suggest possible differences in their developmental origin and might explain why some depots are more associated than other to...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1802583</comments>
            <pubDate>Thu, 18 Sep 2008 11:10:33 +0100</pubDate>
            <guid isPermaLink="false">1802583</guid>        </item>
        <item>
            <title>Geminin is partially localized to centrosome and plays a role in proper centrosome duplication</title>
            <link>http://www.medworm.com/index.php?rid=1803670&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080109</link>
            <description>Conclusions. Our data demonstrate that a fraction of geminin is localized on centrosome, and the centrosomal localization of geminin is Arp1 mediated and dynein/dynactin-dependent. The coiled-coil motif of geminin is required for its targeting to centrosome and inhibition of centrosome duplication. Thus the centrosomal localization of geminin might perform an important role in regulation of proper centrosome duplication. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1803670</comments>
            <pubDate>Thu, 18 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1803670</guid>        </item>
        <item>
            <title>Adiponectin Induces Interleukin-6 Production and Activates STAT3 in Adult Mouse Cardiac Fibroblasts</title>
            <link>http://www.medworm.com/index.php?rid=1799246&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080117</link>
            <description>Conclusions. Adiponectin induces IL-6 production mediated by AdipoR1, not AdipoR2, in adult mouse cardiac fibroblasts, which leads to the stimulation of gp130/JAK signaling pathway and as a result causes STAT3 activation. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1799246</comments>
            <pubDate>Wed, 17 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1799246</guid>        </item>
        <item>
            <title>Role of AQP2 during apoptosis in cortical collecting duct cells</title>
            <link>http://www.medworm.com/index.php?rid=1724394&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080050</link>
            <description>Conclusions: These results let us propose that under apoptotic stimulation Aquaporin-2 would act as a sensor leading to a coordinated activation of specific ionic channels for potassium and chloride efflux resulting in both more rapid cell shrinkage and more rapid achieve of adequate levels of ions necessary to activate the enzymatic apoptotic cascade. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1724394</comments>
            <pubDate>Fri, 22 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1724394</guid>        </item>
        <item>
            <title>Ajuba: a new microtubule-associated protein that interacts with BUBR1 and Aurora B at kinetochores in metaphase</title>
            <link>http://www.medworm.com/index.php?rid=1712041&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080060</link>
            <description>Conclusions. Ajuba is a microtubule-associated protein that collaborates with Aurora
B and BUBR1 at the metaphase-anaphase transition and this may be important to
ensure proper chromosome segregation. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1712041</comments>
            <pubDate>Mon, 18 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1712041</guid>        </item>
        <item>
            <title>Transgenesis procedures in Xenopus.</title>
            <link>http://www.medworm.com/index.php?rid=1704619&amp;cid=s_37622_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%3D18699776%26dopt%3DAbstract</link>
            <description>Authors: Chesneau A, Sachs LM, Chai N, Chen Y, Pasquier LD, Loeber J, Pollet N, Reilly M, Weeks DL, Bronchain OJ
    Stable integration of foreign DNA into the frog genome has been the purpose of several studies aimed at generating transgenic animals or producing mutations of endogenous genes. Inserting DNA into a host genome can be achieved in a number of ways. In Xenopus, different strategies have been developed which exhibit specific molecular and technical features. Although several of these technologies were also applied in various model organizms, the attributes of each method have rarely been experimentally compared. Investigators are thus confronted with a difficult choice to discriminate which method would be best suited for their applications. To gain better understanding, a tran...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1704619</comments>
            <pubDate>Thu, 14 Aug 2008 13:01:15 +0100</pubDate>
            <guid isPermaLink="false">1704619</guid>        </item>
        <item>
            <title>Functional diversity among p24 subfamily members.</title>
            <link>http://www.medworm.com/index.php?rid=1704620&amp;cid=s_37622_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%3D18699773%26dopt%3DAbstract</link>
            <description>Conclusions Our results show that the four upregulated proteins p24alpha3, -beta1, -gamma3 and -delta2 have non-redundant roles in the early secretory pathway, and suggest that each p24 subfamily member provides a proper ER/Golgi subcompartmental microenvironment, together allowing correct secretory protein transport and processing.
    PMID: 18699773 [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=1704620</comments>
            <pubDate>Wed, 13 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1704620</guid>        </item>
        <item>
            <title>Functional diversity among p24 subfamily members</title>
            <link>http://www.medworm.com/index.php?rid=1702716&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080075</link>
            <description>Conclusions
Our results show that the four upregulated proteins p24&amp;#x03B1;3, -&amp;#x03B2;1, -&amp;#x03B3;3 and -&amp;#x03B4;2 have non-redundant roles in the early secretory pathway, and suggest that each p24 subfamily member provides a proper ER/Golgi subcompartmental microenvironment, together allowing correct secretory protein transport and processing. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1702716</comments>
            <pubDate>Wed, 13 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1702716</guid>        </item>
        <item>
            <title>Endosomal lipid accumulation in NPC1 leads to inhibition of PKC, hypophosphorylation of vimentin and Rab9 entrapment.</title>
            <link>http://www.medworm.com/index.php?rid=1688909&amp;cid=s_37622_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%3D18681838%26dopt%3DAbstract</link>
            <description>Conclusions. To further investigate the mechanism by which Rab9 facilitates lipid movement from late endosomes we sought to identify novel Rab9 binding/interacting proteins. Here, we report that Rab9 interacts with the intermediate filament phosphoprotein vimentin and this interaction is altered by lipid accumulation in late endosomes, which results in inhibition of protein kinase C (PKC) and hypophosphorylation of vimentin, leading to late endosome dysfunction. Intermediate filament hyposphorylation, aggregation and entrapment of Rab9 ultimately leads to transport defects and inhibition of lipid egress from late endosomes. These data reveal a previously unappreciated interaction between Rab proteins and intermediate filaments in regulating intracellular lipid transport.
    PMID: 18681838...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1688909</comments>
            <pubDate>Wed, 06 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1688909</guid>        </item>
        <item>
            <title>Endosomal lipid accumulation in NPC1 leads to inhibition of PKC, hypophosphorylation of vimentin and Rab9 entrapment</title>
            <link>http://www.medworm.com/index.php?rid=1684211&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070171</link>
            <description>Conclusions. To further investigate the mechanism by which Rab9 facilitates lipid movement from late endosomes we sought to identify novel Rab9 binding/interacting proteins. Here, we report that Rab9 interacts with the intermediate filament phosphoprotein vimentin and this interaction is altered by lipid accumulation in late endosomes, which results in inhibition of protein kinase C (PKC) and hypophosphorylation of vimentin, leading to late endosome dysfunction. Intermediate filament hyposphorylation, aggregation and entrapment of Rab9 ultimately leads to transport defects and inhibition of lipid egress from late endosomes. These data reveal a previously unappreciated interaction between Rab proteins and intermediate filaments in regulating intracellular lipid transport. (Source: Biology o...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1684211</comments>
            <pubDate>Wed, 06 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1684211</guid>        </item>
        <item>
            <title>Osteoclast differentiation and function in aquaglyceroporin AQP9 null mice</title>
            <link>http://www.medworm.com/index.php?rid=1666291&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080083</link>
            <description>Conclusions: Our data confirm that AQP9 expression rises during osteoclast biogenesis but indicate that AQP9 is not essential for osteoclast function or differentiation under normal physiological conditions. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1666291</comments>
            <pubDate>Wed, 30 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1666291</guid>        </item>
        <item>
            <title>Shifting from clonal to sexual reproduction in aphids: physiological and developmental aspects.</title>
            <link>http://www.medworm.com/index.php?rid=1634779&amp;cid=s_37622_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%3D18627352%26dopt%3DAbstract</link>
            <description>Authors: Le Trionnaire G, Hardie J, Jaubert-Possamai S, Simon JC, Tagu D
    Developmental biology is one of the fastest growing and fascinating research fields in life sciences. Among the wide range of embryonic development, a fundamental difference exists between organisms with sexual or asexual development. Aphids are unusual organisms which display alternative pathways of sexual and asexual development, the orientation of the pathway being determined by environmental conditions. These insects offer an adapted system in which to study developmental plasticity, because a side-by-side comparison of sexual and asexual development can be made in individuals with the same genotype. In this review, we describe the developmental mechanisms that have evolved in aphids for alternative sexual and...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1634779</comments>
            <pubDate>Fri, 18 Jul 2008 09:50:56 +0100</pubDate>
            <guid isPermaLink="false">1634779</guid>        </item>
        <item>
            <title>Viral detection by electron microscopy: past, present and future.</title>
            <link>http://www.medworm.com/index.php?rid=1634778&amp;cid=s_37622_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%3D18627353%26dopt%3DAbstract</link>
            <description>Authors: Roingeard P
    Viruses are very small and most of them can be seen only by TEM (transmission electron microscopy). TEM has therefore made a major contribution to virology, including the discovery of many viruses, the diagnosis of various viral infections and fundamental investigations of virus-host cell interactions. However, TEM has gradually been replaced by more sensitive methods, such as the PCR. In research, new imaging techniques for fluorescence light microscopy have supplanted TEM, making it possible to study live cells and dynamic interactions between viruses and the cellular machinery. Nevertheless, TEM remains essential for certain aspects of virology. It is very useful for the initial identification of unknown viral agents in particular outbreaks, and is recommended b...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1634778</comments>
            <pubDate>Fri, 18 Jul 2008 09:50:53 +0100</pubDate>
            <guid isPermaLink="false">1634778</guid>        </item>
        <item>
            <title>Conditional knockout of nucleolin in DT40 cells reveals the functional redundancy of its RNA binding domains</title>
            <link>http://www.medworm.com/index.php?rid=1635976&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080054</link>
            <description>Conclusions: The function of nucleolin in ribosomal synthesis could account for its effect on cell division and survival, but this vital role does not seem to be linked to sequence specific RNA binding. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1635976</comments>
            <pubDate>Fri, 18 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1635976</guid>        </item>
        <item>
            <title>A novel neuronal calcium sensor family protein, calaxin, is a potential Ca2+-dependent regulator for outer arm dynein of metazoan cilia and flagella.</title>
            <link>http://www.medworm.com/index.php?rid=1630880&amp;cid=s_37622_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%3D18620543%26dopt%3DAbstract</link>
            <description>Conclusions. These results suggest that calaxin is a potential Ca2+-dependent modulator of outer arm dynein in metazoan cilia and flagella.
    PMID: 18620543 [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=1630880</comments>
            <pubDate>Fri, 11 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1630880</guid>        </item>
        <item>
            <title>A novel neuronal calcium sensor family protein, calaxin, is a potential Ca2+-dependent regulator for outer arm dynein of metazoan cilia and flagella</title>
            <link>http://www.medworm.com/index.php?rid=1607734&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080032</link>
            <description>Conclusions. These results suggest that calaxin is a potential Ca2+-dependent modulator of outer arm dynein in metazoan cilia and flagella. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1607734</comments>
            <pubDate>Fri, 11 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1607734</guid>        </item>
        <item>
            <title>Compartmentalized DCC signaling is distinct from DCC localized to lipid rafts.</title>
            <link>http://www.medworm.com/index.php?rid=1615830&amp;cid=s_37622_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%3D18616430%26dopt%3DAbstract</link>
            <description>Conclusions: Together, these results suggest that DCC can be found in raft and non-raft portions of the plasma membrane with early signaling events propagated by non-raft associated DCC.
    PMID: 18616430 [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=1615830</comments>
            <pubDate>Thu, 10 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1615830</guid>        </item>
        <item>
            <title>Compartmentalized DCC signaling is distinct from DCC localized to lipid rafts</title>
            <link>http://www.medworm.com/index.php?rid=1603730&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070108</link>
            <description>Conclusions: Together, these results suggest that DCC can be found in raft and non-raft portions of the plasma membrane with early signaling events propagated by non-raft associated DCC. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1603730</comments>
            <pubDate>Thu, 10 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1603730</guid>        </item>
        <item>
            <title>Dopamine-induced programmed cell death is associated with cytochrome-c release and caspase-3 activation in snail salivary gland cells.</title>
            <link>http://www.medworm.com/index.php?rid=1602867&amp;cid=s_37622_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%3D18601650%26dopt%3DAbstract</link>
            <description>Conclusion. Our results provide evidence for a type of transmitter mediated pathway that regulates PCD of secretory cells through a mitochondrial-caspase-dependent way. The activation of specific molecules, such as K-channels, DA receptors, cytochrome-c, ceramide, Bcl-2 proteins and caspase-3, but not caspase-8, was demonstrated in cells involved in the dopamine induced PCD suggesting that PCD is a physiological way for the release of saliva from SG cells.
    PMID: 18601650 [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=1602867</comments>
            <pubDate>Fri, 04 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1602867</guid>        </item>
        <item>
            <title>Dopamine-induced programmed cell death is associated with cytochrome-c release and caspase-3 activation in snail salivary gland cells</title>
            <link>http://www.medworm.com/index.php?rid=1599748&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070168</link>
            <description>Conclusion. Our results provide evidence for a type of transmitter mediated pathway that regulates PCD of secretory cells through a mitochondrial-caspase-dependent way. The activation of specific molecules, such as K-channels, DA receptors, cytochrome-c, ceramide, Bcl-2 proteins and caspase-3, but not caspase-8, was demonstrated in cells involved in the dopamine induced PCD suggesting that PCD is a physiological way for the release of saliva from SG 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=1599748</comments>
            <pubDate>Fri, 04 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599748</guid>        </item>
        <item>
            <title>Upregulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells</title>
            <link>http://www.medworm.com/index.php?rid=1599750&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080043</link>
            <description>Conclusions. The upregulation of cathepsin B by NF&amp;#x03BA;B, followed by its secretion into the extracellular environment, might be partly responsible for the previously reported invasiveness of the mtDNA-depleted 143B osteosarcoma 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=1599750</comments>
            <pubDate>Thu, 03 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599750</guid>        </item>
        <item>
            <title>Raman microspectrometry sulphur detection and characterisation in the marine ectosymbiotic nematode Eubostrichus dianae (Desmodoridae, Stilbonematidae)</title>
            <link>http://www.medworm.com/index.php?rid=1599749&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080051</link>
            <description>Conclusions
As Raman Spectrometry can be used on living organisms (without preliminary fixation) without sample damages and preserving the molecular structure of the sulphur (denatured during chemical fixation) it represents a very well adapted investigation tool for biologists. This technique permits therefore to detect quickly and easily (in few seconds and on entire living animals) the presence of sulphur compounds in the symbiotic nematode. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599749</comments>
            <pubDate>Thu, 03 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599749</guid>        </item>
        <item>
            <title>Upregulation of cathepsin B expression and enhanced secretion in mitochondrial DNA-depleted osteosarcoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=1581858&amp;cid=s_37622_170_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%3D18598236%26dopt%3DAbstract</link>
            <description>Conclusions. The upregulation of cathepsin B by NFkappaB, followed by its secretion into the extracellular environment, might be partly responsible for the previously reported invasiveness of the mtDNA-depleted 143B osteosarcoma cells.
    PMID: 18598236 [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=1581858</comments>
            <pubDate>Thu, 03 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1581858</guid>        </item>
        <item>
            <title>Raman microspectrometry sulphur detection and characterisation in the marine ectosymbiotic nematode Eubostrichus dianae (Desmodoridae, Stilbonematidae).</title>
            <link>http://www.medworm.com/index.php?rid=1581857&amp;cid=s_37622_170_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%3D18598237%26dopt%3DAbstract</link>
            <description>Conclusions As Raman Spectrometry can be used on living organisms (without preliminary fixation) without sample damages and preserving the molecular structure of the sulphur (denatured during chemical fixation) it represents a very well adapted investigation tool for biologists. This technique permits therefore to detect quickly and easily (in few seconds and on entire living animals) the presence of sulphur compounds in the symbiotic nematode.
    PMID: 18598237 [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=1581857</comments>
            <pubDate>Thu, 03 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1581857</guid>        </item>
        <item>
            <title>Functional analysis of SRY-KRAB interaction in mouse sex determination</title>
            <link>http://www.medworm.com/index.php?rid=1599751&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080061</link>
            <description>Conclusions: Reduced Sox9 expression in KRAB knockdown cells supports a role for KRAB-O and perhaps other KRAB genes in mediating SRY function. Overlapping expression and potential redundancy between members of the large KRAB-O gene cluster may mask any loss of function in vivo, presenting clear challenges for further functional analysis. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599751</comments>
            <pubDate>Mon, 30 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599751</guid>        </item>
        <item>
            <title>Intracellular trafficking of Shiga toxin B-subunit functionalized spherulites</title>
            <link>http://www.medworm.com/index.php?rid=1599752&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080009</link>
            <description>Conclusions. While recognition of Gb3 is the cause of their specific adhesion to cell membranes, STxB-functionalized spherulites do not follow the retrograde transport route. Our data strongly suggest that STxB-spherulites are at least in part disrupted at the plasma membrane, leading to lipid and content targeting to the classical endocytic pathway. It is discussed how these findings influence the development of innovative delivery strategies. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599752</comments>
            <pubDate>Thu, 19 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599752</guid>        </item>
        <item>
            <title>Which in vitro models could be best used to study hepatocyte polarity?</title>
            <link>http://www.medworm.com/index.php?rid=1518576&amp;cid=s_37622_170_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%3D18549352%26dopt%3DAbstract</link>
            <description>Authors: Decaens C, Durand M, Grosse B, Cassio D
    The correct functioning of the liver is ensured by the setting and the maintenance of hepatocyte polarity. The complex polarity of the hepatocyte is characterized by the existence of several basolateral and apical poles per cell. Many in vitro models are available for studying hepatocyte polarity, but which are the more suitable? To answer this question, we aimed to identify criteria which determine the typical hepatocyte polarity. Therefore, we compiled a range of protein markers of membrane domains in rat hepatocytes and investigated their involvement in hepatocytic functions. Then, we focused on the relationship between hepatic functions and the cytoskeleton, Golgi apparatus and endoplasmic reticulum. Subsequently, we compared differe...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1518576</comments>
            <pubDate>Sat, 14 Jun 2008 22:00:05 +0100</pubDate>
            <guid isPermaLink="false">1518576</guid>        </item>
        <item>
            <title>Knockdown of Pdcd4 results in induction of proprotein convertase 1/3 and potent secretion of chromogranin A and secretogranin II in a neuroendocrine cell line</title>
            <link>http://www.medworm.com/index.php?rid=1599753&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080052</link>
            <description>Programmed cell death 4 (Pdcd4) is up-regulated during apoptosis and seems to play an important role as a tumor suppressor. To get further insights into its biological functions we suppressed Pdcd4 expression in the neuroendocrine cell line Bon-1 via siRNA technology. Using this cell line we found that suppression of Pdcd4 resulted in an increased release of chromogranin A (CgA) and secretogranin II (Sg II) accompanied by an up-regulation of intracellular proprotein convertase 1/3 (PC1). The enhanced secretion of CgA and SgII seemed to be mediated by an activation of protein kinase Akt via PI3 kinase. In accordance with this, inhibition of PI3 kinase activity and, thereby, reduced phosphorylation of Akt was shown to enhance Pdcd4 expression. Neither the PKC signal transduction cascade nor ...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599753</comments>
            <pubDate>Thu, 12 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599753</guid>        </item>
        <item>
            <title>Knockdown of Pdcd4 results in induction of proprotein convertase 1/3 and potent secretion of chromogranin A and secretogranin II in a neuroendocrine cell line.</title>
            <link>http://www.medworm.com/index.php?rid=1518577&amp;cid=s_37622_170_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%3D18549351%26dopt%3DAbstract</link>
            <description>Authors: Lankat-Buttgereit B, M&amp;#xFC;ller S, Schmidt H, Parhofer KG, Gress TM, G&amp;#xF6;ke R
    Programmed cell death 4 (Pdcd4) is up-regulated during apoptosis and seems to play an important role as a tumor suppressor. To get further insights into its biological functions we suppressed Pdcd4 expression in the neuroendocrine cell line Bon-1 via siRNA technology. Using this cell line we found that suppression of Pdcd4 resulted in an increased release of chromogranin A (CgA) and secretogranin II (Sg II) accompanied by an up-regulation of intracellular proprotein convertase 1/3 (PC1). The enhanced secretion of CgA and SgII seemed to be mediated by an activation of protein kinase Akt via PI3 kinase. In accordance with this, inhibition of PI3 kinase activity and, thereby, reduced phosphorylation...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1518577</comments>
            <pubDate>Thu, 12 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1518577</guid>        </item>
        <item>
            <title>The 5' - 3' exoribonuclease pacman is required for epithelial sheet sealing in Drosophila and genetically interacts with the phosphatase puckered</title>
            <link>http://www.medworm.com/index.php?rid=1599754&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080049</link>
            <description>Conclusions: 
These results reveal that the 5' &amp;#x2013; 3' exoribonuclease pacman is required for a critical aspect of epithelial sheet sealing in Drosophila. Since these mutations result in specific phenotypes our data suggest that the exoribonuclease Pacman targets a specific subset of mRNAs involved in this process. One of these targets could be a member of the JNK signaling pathway, although it is possible that a parallel pathway may instead be affected. The exoribonuclease pacman is highly conserved in all eukaryotes, therefore it is likely that it is involved in similar morphological processes such as wound healing in human 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=1599754</comments>
            <pubDate>Wed, 11 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599754</guid>        </item>
        <item>
            <title>The 5' - 3' exoribonuclease pacman is required for epithelial sheet sealing in Drosophila and genetically interacts with the phosphatase puckered.</title>
            <link>http://www.medworm.com/index.php?rid=1516363&amp;cid=s_37622_170_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%3D18547166%26dopt%3DAbstract</link>
            <description>Conclusions: These results reveal that the 5' - 3' exoribonuclease pacman is required for a critical aspect of epithelial sheet sealing in Drosophila. Since these mutations result in specific phenotypes our data suggest that the exoribonuclease Pacman targets a specific subset of mRNAs involved in this process. One of these targets could be a member of the JNK signaling pathway, although it is possible that a parallel pathway may instead be affected. The exoribonuclease pacman is highly conserved in all eukaryotes, therefore it is likely that it is involved in similar morphological processes such as wound healing in human cells.
    PMID: 18547166 [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=1516363</comments>
            <pubDate>Wed, 11 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1516363</guid>        </item>
        <item>
            <title>Lys-110 is essential for targeting PCNA to replication and repair foci, and the K110A mutant activates apoptosis</title>
            <link>http://www.medworm.com/index.php?rid=1599755&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070158</link>
            <description>Conclusions: The present study suggests that the regulation of PCNA is intimately connected with that of DNA replication, repair and cell death signals, and raises the possibility that defects in the formation of the PCNA double trimer complex can cause 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=1599755</comments>
            <pubDate>Thu, 22 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599755</guid>        </item>
        <item>
            <title>mRNA journey to the cytoplasm: attire required.</title>
            <link>http://www.medworm.com/index.php?rid=1445855&amp;cid=s_37622_170_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%3D18479253%26dopt%3DAbstract</link>
            <description>Authors: Rougemaille M, Villa T, Gudipati RK, Libri D
    In eukaryotes, copying the genetic information from a DNA template into RNA is not sufficient itself to confer functional competence to the DNA-encoded message. mRNAs have to be processed by enzymes and packaged with proteins within nuclei to generate mRNP (messenger ribonucleoprotein) particles, before these can be exported to the cytoplasm. Processing and packaging factors are believed to interact with the nascent mRNA co-transcriptionally, which protects the highly reactive RNA molecule from a presumably aggressive nuclear environment while providing early commitment to its functional fate. In this review, we will describe the factors that are believed to provide the appropriate 'dress code' to the mRNA and the mechanisms underly...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1445855</comments>
            <pubDate>Fri, 16 May 2008 15:24:56 +0100</pubDate>
            <guid isPermaLink="false">1445855</guid>        </item>
        <item>
            <title>Activation of the small GTPase Rac1 by a specific guanine nucleotide exchange factor suffices to induce glucose uptake into skeletal muscle cells</title>
            <link>http://www.medworm.com/index.php?rid=1599756&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070160</link>
            <description>Conclusions. Collectively, Rac1 activation specifically in membrane ruffles by the guanine nucleotide exchange factor FLJ00068 is sufficient for insulin induction of glucose uptake into skeletal muscle 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=1599756</comments>
            <pubDate>Fri, 16 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599756</guid>        </item>
        <item>
            <title>Repulsive guidance molecule A (RGM A) and its receptor Neogenin during neural and neural crest cell development of Xenopus laevis</title>
            <link>http://www.medworm.com/index.php?rid=1599757&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080023</link>
            <description>Conclusions. These data indicate that RGM A and Neogenin have important functions during early neural development in addition to their role during axonal guidance and synapse formation. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599757</comments>
            <pubDate>Thu, 15 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599757</guid>        </item>
        <item>
            <title>Repulsive guidance molecule A (RGM A) and its receptor Neogenin during neural and neural crest cell development of Xenopus laevis.</title>
            <link>http://www.medworm.com/index.php?rid=1445856&amp;cid=s_37622_170_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%3D18479252%26dopt%3DAbstract</link>
            <description>Conclusions. These data indicate that RGM A and Neogenin have important functions during early neural development in addition to their role during axonal guidance and synapse formation.
    PMID: 18479252 [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=1445856</comments>
            <pubDate>Thu, 15 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1445856</guid>        </item>
        <item>
            <title>The regulation of diacylglycerol production and protein kinase C stimulation during sperm and PLC{zeta}(zeta) mediated mouse egg activation</title>
            <link>http://www.medworm.com/index.php?rid=1599758&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080033</link>
            <description>Conclusions. Our data suggests that over production of diacylglycerol in PLC{zeta} injected eggs can lead to protein kinase C-mediated Ca2+ influx and subsequent overloading of Ca2+ stores. These data suggest that diacylglycerol generation in the plasma membrane of fertilizing mouse eggs is minimized since it can perturb egg Ca2+ homeostasis via excessive Ca2+ influx. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599758</comments>
            <pubDate>Fri, 09 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599758</guid>        </item>
        <item>
            <title>The regulation of diacylglycerol production and protein kinase C stimulation during sperm and PLCzeta(zeta) mediated mouse egg activation.</title>
            <link>http://www.medworm.com/index.php?rid=1439405&amp;cid=s_37622_170_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%3D18471090%26dopt%3DAbstract</link>
            <description>Conclusions. Our data suggests that over production of diacylglycerol in PLCzeta injected eggs can lead to protein kinase C-mediated Ca 2+ influx and subsequent overloading of Ca 2+ stores. These data suggest that diacylglycerol generation in the plasma membrane of fertilizing mouse eggs is minimized since it can perturb egg Ca 2+ homeostasis via excessive Ca 2+ influx.
    PMID: 18471090 [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=1439405</comments>
            <pubDate>Fri, 09 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1439405</guid>        </item>
        <item>
            <title>Supramolecular organization of the yeast F1F{subo}-ATP synthase</title>
            <link>http://www.medworm.com/index.php?rid=1599759&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080022</link>
            <description>Conclusions. Our results shed new light on the supramolecular organization of the F1Fo-ATP synthase and its potential role in mitochondrial morphology. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599759</comments>
            <pubDate>Wed, 30 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599759</guid>        </item>
        <item>
            <title>Palmitoylation of stathmin family proteins domain A controls Golgi vs mitochondrial subcellular targeting</title>
            <link>http://www.medworm.com/index.php?rid=1599760&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070119</link>
            <description>Conclusions. Our results unravel that, upon specific biological conditions, palmitoylation of stathmin proteins might be able to control their targeting to express their functional activities at appropriate subcellular sites. They more generally open new perspectives regarding the role of palmitoylation as a signaling mechanism orienting proteins to their functional subcellular compartments. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599760</comments>
            <pubDate>Mon, 21 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599760</guid>        </item>
        <item>
            <title>Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles</title>
            <link>http://www.medworm.com/index.php?rid=1599761&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080025</link>
            <description>Conclusion: The dissemination of prions in N2a cell culture is mediated through the exosomal 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=1599761</comments>
            <pubDate>Fri, 18 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599761</guid>        </item>
        <item>
            <title>Similarity and diversity in mechanisms of muscle fate induction between ascidian species.</title>
            <link>http://www.medworm.com/index.php?rid=1379284&amp;cid=s_37622_170_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%3D18412545%26dopt%3DAbstract</link>
            <description>Authors: Hudson C, Yasuo H
    Developmental processes can change during evolution at many levels of the ontogeny of an individual. Embryos of solitary ascidians have a largely invariant mode of development, with fixed cleavage patterns and fate maps. Thus the cell lineages and final body plan of the two quite distantly related species considered in this review, Ciona intestinalis and Halocynthia roretzi, are highly similar. However, close comparison of the developmental mechanisms used by these two species provide examples of evolutionary changes and help pinpoint which aspects of development are evolutionarily flexible. Examples of both similarity and diversity are observed in the mechanisms used to generate the full complement of larval muscle. We will describe the changes in muscle-cel...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1379284</comments>
            <pubDate>Thu, 17 Apr 2008 20:11:44 +0100</pubDate>
            <guid isPermaLink="false">1379284</guid>        </item>
        <item>
            <title>Molecular pathogenesis of sialic acid storage diseases: insight gained from four missense mutations and a putative polymorphism of human sialin</title>
            <link>http://www.medworm.com/index.php?rid=1599762&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070166</link>
            <description>Conclusions. The molecular effects of the R57C and G127E mutations strengthen the conclusion that the infantile phenotype is caused by loss-of-function mutations. On the other hand, the milder severity of the heterozygous G409E patient may reflect an incomplete expression of the splicing mutation present on the second allele. In the case of G328E, found in the homozygous state in a clinically heterogeneous family, the apparent severity of the transport phenotype suggests that the genetic or environmental factors underlying this clinical heterogeneity might be protective. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599762</comments>
            <pubDate>Thu, 10 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599762</guid>        </item>
        <item>
            <title>Molecular pathogenesis of sialic acid storage diseases: insight gained from four missense mutations and a putative polymorphism of human sialin.</title>
            <link>http://www.medworm.com/index.php?rid=1366569&amp;cid=s_37622_170_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%3D18399798%26dopt%3DAbstract</link>
            <description>Conclusions. The molecular effects of the R57C and G127E mutations strengthen the conclusion that the infantile phenotype is caused by loss-of-function mutations. On the other hand, the milder severity of the heterozygous G409E patient may reflect an incomplete expression of the splicing mutation present on the second allele. In the case of G328E, found in the homozygous state in a clinically heterogeneous family, the apparent severity of the transport phenotype suggests that the genetic or environmental factors underlying this clinical heterogeneity might be protective.
    PMID: 18399798 [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=1366569</comments>
            <pubDate>Thu, 10 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1366569</guid>        </item>
        <item>
            <title>TGF{beta} regulates cell spreading and hypertrophy through a rac-p38 mediated pathway</title>
            <link>http://www.medworm.com/index.php?rid=1599763&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080021</link>
            <description>Conclusions: The Rac-p38 pathway may have conceptual implications in pathophysiological endothelial cell responses to TGF{beta} such as wound healing or development of atherosclerotic lesions. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599763</comments>
            <pubDate>Fri, 04 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599763</guid>        </item>
        <item>
            <title>TGFbeta regulates cell spreading and hypertrophy through a rac-p38 mediated pathway.</title>
            <link>http://www.medworm.com/index.php?rid=1351916&amp;cid=s_37622_170_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%3D18387002%26dopt%3DAbstract</link>
            <description>Conclusions: The Rac-p38 pathway may have conceptual implications in pathophysiological endothelial cell responses to TGFbeta such as wound healing or development of atherosclerotic lesions.
    PMID: 18387002 [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=1351916</comments>
            <pubDate>Fri, 04 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1351916</guid>        </item>
        <item>
            <title>Cell-penetrating peptides: from molecular mechanisms to therapeutics.</title>
            <link>http://www.medworm.com/index.php?rid=1310903&amp;cid=s_37622_170_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%3D18341479%26dopt%3DAbstract</link>
            <description>Authors: Morris MC, Deshayes S, Heitz F, Divita G
    The recent discovery of new potent therapeutic molecules which do not reach the clinic due to poor delivery and low bioavailability have made the delivery of molecules a keystone in therapeutic development. Several technologies have been designed to improve cellular uptake of therapeutic molecules, including CPPs (cell-penetrating peptides), which represent a new and innovative concept to bypass the problem of bioavailability of drugs. CPPs constitute very promising tools and have been successfully applied for in vivo. Two CPP strategies have been described to date; the first one requires chemical linkage between the drug and the carrier for cellular drug internalization, and the second is based on the formation of stable complexes with...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1310903</comments>
            <pubDate>Tue, 18 Mar 2008 20:37:21 +0100</pubDate>
            <guid isPermaLink="false">1310903</guid>        </item>
        <item>
            <title>S1-1 nuclear domains: characterization and dynamics as a function of transcriptional activity</title>
            <link>http://www.medworm.com/index.php?rid=1599764&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070142</link>
            <description>Conclusions. S1-1 constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, S1-1 nuclear bodies enlarge and decrease in number. They are novel domains different from paraspeckles or IGAZs, despite their similar occurrence adjacent to nuclear speckles. We discuss S1-1 granules in terms of their association with gene expression. In addition, this is the first report of a TIDR-localized protein. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599764</comments>
            <pubDate>Tue, 04 Mar 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599764</guid>        </item>
        <item>
            <title>S1-1 nuclear domains: characterization and dynamics as a function of transcriptional activity.</title>
            <link>http://www.medworm.com/index.php?rid=1280620&amp;cid=s_37622_170_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%3D18315527%26dopt%3DAbstract</link>
            <description>Conclusions. S1-1 constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner. Upon globally reducing RNA polymerase II transcription, S1-1 nuclear bodies enlarge and decrease in number. They are novel domains different from paraspeckles or IGAZs, despite their similar occurrence adjacent to nuclear speckles. We discuss S1-1 granules in terms of their association with gene expression. In addition, this is the first report of a TIDR-localized protein.
    PMID: 18315527 [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=1280620</comments>
            <pubDate>Tue, 04 Mar 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1280620</guid>        </item>
        <item>
            <title>Toxoplasma gondii Hsp20 is a stripe-arranged chaperone like protein associated with the outer leaflet of the inner membrane complex</title>
            <link>http://www.medworm.com/index.php?rid=1599765&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20080004</link>
            <description>Conclusions: Hsp20 showed to be associated to a specialized membranous structure of the parasite, the IMC. This discontinuous striped-arrangement is unique in T. gondii, indicating that the topology of the outer leaflet of the IMC is not homogeneous. (Source: Biology of the Cell)</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599765</comments>
            <pubDate>Mon, 03 Mar 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599765</guid>        </item>
        <item>
            <title>Toxoplasma gondii Hsp20 is a stripe-arranged chaperone like protein associated with the outer leaflet of the inner membrane complex.</title>
            <link>http://www.medworm.com/index.php?rid=1280621&amp;cid=s_37622_170_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%3D18315523%26dopt%3DAbstract</link>
            <description>Conclusions: Hsp20 showed to be associated to a specialized membranous structure of the parasite, the IMC. This discontinuous striped-arrangement is unique in T. gondii, indicating that the topology of the outer leaflet of the IMC is not homogeneous.
    PMID: 18315523 [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=1280621</comments>
            <pubDate>Mon, 03 Mar 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1280621</guid>        </item>
        <item>
            <title>Nuclear localization, DNA binding and restricted expression in neural and germ cells of zebrafish Dmrt3</title>
            <link>http://www.medworm.com/index.php?rid=1599767&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070114</link>
            <description>Conclusion. These results suggest that as a DNA binding protein, zebrafish Dmrt3 may function in the nucleus as a potential transcription factor to exert potential roles in the development of the olfactory placode, the neural tube and germ 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=1599767</comments>
            <pubDate>Tue, 19 Feb 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599767</guid>        </item>
        <item>
            <title>{alpha}v{beta}3 and {alpha}v{beta}5 integrins and their role in muscle precursor cell adhesion</title>
            <link>http://www.medworm.com/index.php?rid=1599766&amp;cid=s_37622_171_f&amp;fid=37622&amp;url=http%3A%2F%2Fwww.biolcell.org%2Fboc%2Fimps%2Frefer.htm%3FMSID%3DBC20070115</link>
            <description>Background Information. Functional adaptation of skeletal muscle is a requirement for different muscle groups (e.g. craniofacial, ocular, limb) to undergo site-specific changes. Such tissue remodelling depends on dynamic interactions between muscle cells and their extracellular matrix, via participation of multifunctional molecules like integrins. In view of data suggesting a role in fundamental muscle biology and muscle development in other systems, this study has focussed on expression and function of {alpha}v integrins, in cultured adult human craniofacial muscle (masseter) precursor cells and myotubes, and the predominantly fibroblastic interstital cell population. 
Results and conclusions. Flow cytometric and immunofluorescence phenotyping show that {alpha}v, {alpha}v{beta}3 and {alph...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1599766</comments>
            <pubDate>Tue, 19 Feb 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1599766</guid>        </item>
        <item>
            <title>Shh and forebrain evolution in the blind cavefish Astyanax mexicanus.</title>
            <link>http://www.medworm.com/index.php?rid=1234535&amp;cid=s_37622_170_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%3D18271755%26dopt%3DAbstract</link>
            <description>Authors: R&amp;#xE9;taux S, Pottin K, Alunni A
    The blind cavefish and its surface counterpart of the teleost species Astyanax mexicanus constitute an excellent model to study the evolution of morphological features. During adaptation to their lives in perpetual darkness, the cave population has lost eyes (and pigmentation), but has gained several constructive traits. Recently, the demonstration that an increase in Shh (Sonic Hedgehog) midline signalling was indirectly responsible for the loss of eyes in cavefish led to new ways to search for possible modifications in the forebrain of these cavefish, as this anterior-most region of the vertebrate central nervous system develops under close control of the powerful Shh morphogen. In this review, we summarize the recent progress in the underst...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1234535</comments>
            <pubDate>Fri, 15 Feb 2008 20:43:26 +0100</pubDate>
            <guid isPermaLink="false">1234535</guid>        </item>
        <item>
            <title>Non-coding RNAs in imprinted gene clusters.</title>
            <link>http://www.medworm.com/index.php?rid=1234534&amp;cid=s_37622_170_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%3D18271756%26dopt%3DAbstract</link>
            <description>Authors: Royo H, Cavaill&amp;#xE9; J
    Imprinted ncRNA (non-coding RNA) genes represent a family of untranslated transcripts that are mono-allelically expressed in a parent-of-origin manner (their expression is restricted to either the maternal or the paternal allele). Although the expression of a few long imprinted ncRNAs act as cis-acting silencers in the epigenetic regulation of chromatin at imprinted gene clusters, many of them fall into the growing class of small regulatory RNAs, namely C/D small nucleolar RNAs, microRNAs and also likely piRNAs (Piwi-interacting RNAs), which are known to act as antisense trans-acting regulators of gene expression (for example, site-specific RNA modifications and RNA-mediated gene silencing). Although their biological functions remain elusive, recent stu...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1234534</comments>
            <pubDate>Fri, 15 Feb 2008 20:43:24 +0100</pubDate>
            <guid isPermaLink="false">1234534</guid>        </item>
        <item>
            <title>Effect of translocator protein (18-kDa) ligand binding on neurotransmitter-induced saliva secretion in rat submandibular glands.</title>
            <link>http://www.medworm.com/index.php?rid=1231751&amp;cid=s_37622_170_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%3D18269350%26dopt%3DAbstract</link>
            <description>Conclusions: High affinity ligand binding to mitochondrial TSPO modulates neurotransmitter-induced salivary secretion by duct and mucous acinar cells of rat sub-mandibular glands.
    PMID: 18269350 [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=1231751</comments>
            <pubDate>Wed, 13 Feb 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1231751</guid>        </item>
        <item>
            <title>microRNAs: small molecules with big roles - C. elegans to human cancer.</title>
            <link>http://www.medworm.com/index.php?rid=1160927&amp;cid=s_37622_170_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%3D18199046%26dopt%3DAbstract</link>
            <description>Authors: Kato M, Slack FJ
    miRNAs (microRNAs) were first discovered as critical regulators of developmental timing events in Caenorhabditis elegans. Subsequent studies have shown that miRNAs and cellular factors necessary for miRNA biogenesis are conserved in many organisms, suggesting the importance of miRNAs during developmental processes. Indeed, mutations in the miRNA-processing pathway induce pleiotropic defects in development, which accompany perturbation of correct expression of target genes. However, control of gene expression in development is not the only function of miRNAs. Recent work has provided new insights into the role of miRNAs in various biological events, including aging and cancer. C. elegans continues to be helpful in facilitating a further understanding of miRNA f...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1160927</comments>
            <pubDate>Fri, 18 Jan 2008 21:51:47 +0100</pubDate>
            <guid isPermaLink="false">1160927</guid>        </item>
        <item>
            <title>Non-coding RNAs regulating the transcriptional machinery.</title>
            <link>http://www.medworm.com/index.php?rid=1160926&amp;cid=s_37622_170_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%3D18199047%26dopt%3DAbstract</link>
            <description>Authors: Barrandon C, Spiluttini B, Bensaude O
    During the past decade, numerous ncRNAs (non-coding RNAs) have been identified as regulators of transcription. This review focuses on a few examples of ncRNAs that directly interact with and regulate components of the transcription machinery. Artificial RNA aptamers have been selected against components of the transcriptional machinery. The bacterial 6S RNA and the eukaryotic B2 RNA directly target RNA polymerases. The 7SK RNA, U1 snRNA (small nuclear RNA) and SRA (steroid receptor RNA activator) RNA bind to and regulate the activity of transcription factors. Xist (X-inactive-specific transcript) and roX (RNA on the X) RNAs are involved in epigenetic regulation of transcription through the recruitment of histone-modifying enzymes.
    PMID...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1160926</comments>
            <pubDate>Fri, 18 Jan 2008 21:51:46 +0100</pubDate>
            <guid isPermaLink="false">1160926</guid>        </item>
        <item>
            <title>A tale of two Paks.</title>
            <link>http://www.medworm.com/index.php?rid=1160925&amp;cid=s_37622_170_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%3D18199048%26dopt%3DAbstract</link>
            <description>Authors: Arias-Romero LE, Chernoff J
    Paks (p21-activated kinases) are effectors for the small GTPases Cdc42 (cell division cycle 42) and Rac that play fundamental roles in a wide range of cellular processes, including cell morphology, motility, survival, gene transcription, apoptosis and hormone signalling. These enzymes are widely expressed in numerous tissues and are activated by extracellular signals through GTPase-dependent and -independent mechanisms. On the basis of structural and biochemical features, the Pak family members have been classified into two groups, comprising three members each. The two Pak groups have generally been considered as two halves of a single entity, but accumulating evidence indicates that this is not so. In this review, we discuss recent advances in our...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1160925</comments>
            <pubDate>Fri, 18 Jan 2008 21:51:44 +0100</pubDate>
            <guid isPermaLink="false">1160925</guid>        </item>
        <item>
            <title>Tethering of proteins to RNAs by bacteriophage proteins.</title>
            <link>http://www.medworm.com/index.php?rid=1160924&amp;cid=s_37622_170_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%3D18199049%26dopt%3DAbstract</link>
            <description>Authors: Keryer-Bibens C, Barreau C, Osborne HB
    Many steps in the control of gene expression are dependent on RNA-binding proteins, most of which are bi-functional, in as much as they both bind to RNA and interact with other protein partners in a functional complex. A powerful approach to study the functional properties of these proteins in vivo, independently of their RNA-binding ability, is to attach or tether them to specifically engineered reporter mRNAs whose fate can be easily followed. Two tethering systems have been mainly used in eukaryotic cells, namely the MS2 coat protein system and the lambda N-B box system. In this review, we firstly describe several studies in which these tethering systems have been used and provide an overview of these applications. We next describe the...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1160924</comments>
            <pubDate>Fri, 18 Jan 2008 21:51:42 +0100</pubDate>
            <guid isPermaLink="false">1160924</guid>        </item>
        <item>
            <title>beta-estradiol rescues Delta-F508CFTR functional expression in human cystic fibrosis airway CFBE41o- cells through the up-regulation of NHERF1.</title>
            <link>http://www.medworm.com/index.php?rid=1146100&amp;cid=s_37622_170_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%3D18184109%26dopt%3DAbstract</link>
            <description>Conclusions. These results demonstrate that beta-estradiol-dependent up-regulation of NHERF1 significantly increases DeltaF508CFTR functional expression in CFBE41o- cells.
    PMID: 18184109 [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=1146100</comments>
            <pubDate>Wed, 09 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1146100</guid>        </item>
        <item>
            <title>Both ERK and JNK pathways are required for PMA-induced MD-2 gene expression during HL-60 cells differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=1142264&amp;cid=s_37622_170_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%3D18181766%26dopt%3DAbstract</link>
            <description>Conclusions. These results suggest that extracellular signal-regulated kinases (ERK) and JNK pathways are involved in PMA-mediated MD-2 gene expression during HL-60 cell differentiation, and the activation of MEK/possible ERK/Elk signal pathway is the mechnism responsible for PMA-induced MD-2 gene expression in differentiated HL-60 cells.
    PMID: 18181766 [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=1142264</comments>
            <pubDate>Tue, 08 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1142264</guid>        </item>
        <item>
            <title>Mercury chloride decreases the water permeability of aquaporin-4-reconstituted proteoliposomes.</title>
            <link>http://www.medworm.com/index.php?rid=1128562&amp;cid=s_37622_170_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%3D18167118%26dopt%3DAbstract</link>
            <description>Conclusions: Our results suggest that mercury inhibits the osmotic water permeability of AQP4 by mechanisms different from those for AQP1 and that AQP4 may be gated by modification of a cysteine residue in cytoplasmic loop D.
    PMID: 18167118 [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=1128562</comments>
            <pubDate>Wed, 02 Jan 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1128562</guid>        </item>
        <item>
            <title>Exploring the complex world of RNA regulation.</title>
            <link>http://www.medworm.com/index.php?rid=1091270&amp;cid=s_37622_170_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%3D18072939%26dopt%3DAbstract</link>
            <description>Authors: Romby P, Wagner EG
    
    PMID: 18072939 [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=1091270</comments>
            <pubDate>Thu, 13 Dec 2007 14:15:44 +0100</pubDate>
            <guid isPermaLink="false">1091270</guid>        </item>
        <item>
            <title>Purine sensing by riboswitches.</title>
            <link>http://www.medworm.com/index.php?rid=1091269&amp;cid=s_37622_170_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%3D18072940%26dopt%3DAbstract</link>
            <description>Authors: Kim JN, Breaker RR
    Structured mRNA elements called riboswitches control gene expression by binding to small metabolites. Over a dozen riboswitch classes have been characterized that target a broad range of molecules and vary widely in size and secondary structure. Four of the known riboswitch classes recognize purines or modified purines. Three of these classes are closely related in conserved sequence and secondary structure, but members of these classes selectively recognize guanine, adenine or 2'-deoxyguanosine. Members of the fourth riboswitch class adopt a distinct structure to form a selective binding pocket for the guanine analogue preQ(1) (7-aminomethyl-7-deazaguanine). All four classes of purine-sensing riboswitches are most likely to recognize their respective metabo...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1091269</comments>
            <pubDate>Thu, 13 Dec 2007 14:15:42 +0100</pubDate>
            <guid isPermaLink="false">1091269</guid>        </item>
        <item>
            <title>RNA silencing movement in plants.</title>
            <link>http://www.medworm.com/index.php?rid=1091268&amp;cid=s_37622_170_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%3D18072941%26dopt%3DAbstract</link>
            <description>Authors: Kalantidis K, Schumacher HT, Alexiadis T, Helm JM
    Higher eukaryotes have developed a mechanism of sequence-specific RNA degradation which is known as RNA silencing. In plants and some animals, similar to the nematode Caenorhabditis elegans, RNA silencing is a non-cell-autonomous event. Hence, silencing initiation in one or a few cells leads progressively to the sequence-specific suppression of homologous sequences in neighbouring cells in an RNA-mediated fashion. Spreading of silencing in plants occurs through plasmodesmata and results from a cell-to-cell movement of a short-range silencing signal, most probably 21-nt siRNAs (short interfering RNAs) that are produced by one of the plant Dicer enzymes. In addition, silencing spreads systemically through the phloem system of the...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1091268</comments>
            <pubDate>Thu, 13 Dec 2007 14:15:38 +0100</pubDate>
            <guid isPermaLink="false">1091268</guid>        </item>
        <item>
            <title>Re-programming of translation following cell stress allows IRES-mediated translation to predominate.</title>
            <link>http://www.medworm.com/index.php?rid=1091267&amp;cid=s_37622_170_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%3D18072942%26dopt%3DAbstract</link>
            <description>Authors: Spriggs KA, Stoneley M, Bushell M, Willis AE
    There is now an overwhelming body of evidence to suggest that internal ribosome entry is required to maintain the expression of specific proteins during patho-physiological situations when cap-dependent translation is compromised, for example, following heat shock or during mitosis, hypoxia, differentiation and apoptosis. Translational profiling has been used by several groups to assess the extent to which alternative mechanisms of translation initiation selectively recruit mRNAs to polysomes during cell stress. The data from these studies have shown that under each condition 3-5% of coding mRNAs remain associated with the polysomes. Importantly, the genes identified in each of these studies do not show a significant amount of overl...</description>
            <author>Biology of the Cell</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1091267</comments>
            <pubDate>Thu, 13 Dec 2007 14:15:37 +0100</pubDate>
            <guid isPermaLink="false">1091267</guid>        </item>
        <item>
            <title>Building up the inactive X chromosome(1).</title>
            <link>http://www.medworm.com/index.php?rid=1091266&amp;cid=s_37622_170_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%3D18072943%26dopt%3DAbstract</link>
            <description>Authors: Matarazzo MR, Cerase A, D'esposito M
    The compensation of the different level of transcripts of X-linked genes in male and female mammals is achieved through X chromosome inactivation, a complex process that differentially regulates the sex chromosomes of female cells. This mechanism has been dissected at evolutionary, genetic and molecular levels: here, we discuss some of the latest examples that illustrate better these intricate connections, focusing particularly on the emerging role of spatial and three-dimensional chromatin arrangements in the building of this special chromosome, the inactive X chromosome.
    PMID: 18072943 [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=1091266</comments>
            <pubDate>Thu, 13 Dec 2007 14:15:35 +0100</pubDate>
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