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        <title>Cell Structure and Function 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 'Cell Structure and Function' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Cell+Structure+and+Function&t=Cell+Structure+and+Function&s=Search&f=source]]></link>
        <lastBuildDate>Sat, 20 Mar 2010 16:35:09 +0100</lastBuildDate>
        <item>
            <title>NDP kinase 7 is a conserved microtubule-binding protein preferentially expressed in ciliated cells.</title>
            <link>http://www.medworm.com/index.php?rid=3355117&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20215702%26dopt%3DAbstract</link>
            <description>Authors: Ikeda T
    Nucleoside diphosphate (NDP) kinase is an enzyme that synthesizes the nucleoside triphosphates. In mammals, nine sequences (NDK1-NDK9) have been found with domain(s) homologous to the catalytic domain of NDP kinase, and some of their products have been shown to associate with sperm flagella. The present study examines the localization of NDK7, for which little information has been available. Database analysis showed that the NDK7 gene is present in organisms with cilia and flagella. Western blotting analyses of various mouse tissues consistently indicated that NDK7 is preferentially expressed in tissues with motile cilia as well as in sperm. Immunofluorescence microscopy revealed that this protein is localized along the entire length of the TritonX-100-insoluble fracti...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3355117</comments>
            <pubDate>Wed, 10 Mar 2010 00:00:00 +0100</pubDate>
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            <title>Humanized Gene Replacement in Mice Reveals the Contribution of Cancer Stroma-Derived HB-EGF to Tumor Growth.</title>
            <link>http://www.medworm.com/index.php?rid=3322770&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20190463%26dopt%3DAbstract</link>
            <description>Authors: Ichise T, Adachi S, Ohishi M, Ikawa M, Okabe M, Iwamoto R, Mekada E
    Tumor progression is a complex process that involves the interaction of cancer cells with the cancer-surrounding stromal cells. The cancer stroma influences the cancer cell growth and metastatic potential. The EGF family growth factor HB-EGF is synthesized in cancer cells and plays pivotal roles in oncogenic transformation and tumor progression, but the contribution of HB-EGF expressed in tumor stromal cells to tumor growth remains unclear. In the present study, we found that HB-EGF was expressed in host-derived cancer stromal cells in xenograft and allograft mouse tumor models. CRM197 is a specific inhibitor of human HB-EGF that has no effect on mouse HB-EGF. To elucidate whether host-derived stromal HB-EGF c...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3322770</comments>
            <pubDate>Tue, 02 Mar 2010 21:38:02 +0100</pubDate>
            <guid isPermaLink="false">3322770</guid>        </item>
        <item>
            <title>Unique Post-translational Modifications in Specialized Microtubule Architecture.</title>
            <link>http://www.medworm.com/index.php?rid=3322771&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20190462%26dopt%3DAbstract</link>
            <description>Authors: Ikegami K, Setou M
    Microtubule (MT) plays specialized roles in a wide variety of cellular events, e.g. molecular transport, cell motility, and cell division. Specialized MT architectures, such as bundles, axonemes, and centrioles, underlie the function. The specialized function and highly organized structure depend on interactions with MT-binding proteins. MT-associated proteins (e.g. MAP1, MAP2, and tau), molecular motors (kinesin and dynein), plus-end tracking proteins (e.g. CLIP-170), and MT-severing proteins (e.g. katanin) interact with MTs. How can the MT-binding proteins know temporospatial information to associate with MTs and to properly play their roles? Post-translational modifications (PTMs) including detyrosination, polyglutamylation, and polyglycylation can provid...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3322771</comments>
            <pubDate>Sat, 27 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3322771</guid>        </item>
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            <title>Retraction notice: the RZZ complex and the spindle assembly checkpoint.</title>
            <link>http://www.medworm.com/index.php?rid=3195935&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20086311%26dopt%3DAbstract</link>
            <description>This article has been retracted at the request of the Editor-in-Chief of the Cell Structure and Function. This review article contains a substantial amount of text that had previously appeared in other published articles, including the Elsevier journals Current Biology (Howell et al., Curr. Biol. 2004 Jun 8; 14(11): 953-964), Trends in Cell Biology (Karess, Trends Cell Biol. 2005 Jul; 15(7): 386-392) and Current Opinion in Cell Biology (Yu, Curr. Opin. Cell Biol. 2002 Dec; 14(6): 706-714). In accordance with policies and procedures governing academic publication we concluded that the above-mentioned article published in Cell Struct. Funct. be retracted. We apologize to readers of the journals that this was not detected during the submission and review process.
    PMID: 20086311 [PubMed - ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3195935</comments>
            <pubDate>Fri, 22 Jan 2010 15:08:03 +0100</pubDate>
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            <title>Spermidine regulates insulin synthesis and cytoplasmic Ca(2+) in mouse beta-TC6 insulinoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=2948586&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19875898%26dopt%3DAbstract</link>
            <description>Authors: Ohtani M, Mizuno I, Kojima Y, Ishikawa Y, Sodeno M, Asakura Y, Samejima K, Oka T
    In order to assess the functional role of the polyamines spermidine and spermine in pancreatic beta-cells, we examined the effect of spermidine and spermine synthase inhibitors, trans-4-methylcyclohexylamine (MCHA) and N-(3-aminopropyl)cyclohexylamine (APCHA), on cellular polyamine and insulin contents, insulin secretion, and cytoplasmic Ca(2+) concentration ([Ca(2+)](i)) in mouse insulin-secreting Beta-TC6 cells. The cellular spermidine and spermine contents were reduced 90% and 64% by cultivation of cells in the presence of MCHA and APCHA for 3 days, respectively. Addition of spermidine or spermine reversed the polyamine level reduced by MCHA or APCHA, respectively. Insulin secretion was decreas...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2948586</comments>
            <pubDate>Mon, 02 Nov 2009 00:58:03 +0100</pubDate>
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            <title>Role of VAMP8/endobrevin in Constitutive Exocytotic Pathway in HeLa Cells.</title>
            <link>http://www.medworm.com/index.php?rid=2782718&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19738360%26dopt%3DAbstract</link>
            <description>Authors: Okayama M, Arakawa T, Tanimura A, Mizoguchi I, Tajima Y, Takuma T
    To evaluate the role of VAMP8/endobrevin in constitutive exocytosis, we have examined the exocytotic pathways of VAMP8 and human growth hormone, both GFP-tagged, by total internal reflection fluorescence microscopy (TIRF-M). Human GH-GFP and VAMP8-GFP were similarly expressed in small round vesicles and elongated tubular vesicles in HeLa cells, and were mostly exocytosed at the peripheral area of the cells. VAMP8-GFP gave 2 types of exocytotic images: a burst type and a non-burst type. The burst type showed a sharp transient increase in the peak fluorescence intensity and a much slower decrease in the average intensity in the active windows, where exocytosis took place, as observed in the full-fusion type of exo...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2782718</comments>
            <pubDate>Mon, 07 Sep 2009 23:00:00 +0100</pubDate>
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            <title>Increased motility and invasiveness in tumor cells that survive 10 gy irradiation.</title>
            <link>http://www.medworm.com/index.php?rid=2762348&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19724156%26dopt%3DAbstract</link>
            <description>In this report, we identify molecules responsible for the malignant properties of tumor cells that survive irradiation. These molecules may be important therapeutic targets for the control of repopulated tumors after radiotherapy.
    PMID: 19724156 [PubMed - in process] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2762348</comments>
            <pubDate>Thu, 03 Sep 2009 21:52:03 +0100</pubDate>
            <guid isPermaLink="false">2762348</guid>        </item>
        <item>
            <title>Expression of Prolyl 3-hydroxylase Genes in Embryonic and Adult Mouse Tissues.</title>
            <link>http://www.medworm.com/index.php?rid=2675476&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19652424%26dopt%3DAbstract</link>
            <description>This report characterizes expression of the three prolyl 3-hydroxylase genes in embryonic and adult mice. Overall these data demonstrate tissue specific prolyl 3-hydroxylase gene expression in both fetal and adult tissues indicating a developmental role for prolyl 3-hydroxylase activity.
    PMID: 19652424 [PubMed - as supplied by publisher] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2675476</comments>
            <pubDate>Fri, 31 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2675476</guid>        </item>
        <item>
            <title>Ectopic Calcification is Caused by Elevated Levels of Serum Inorganic Phosphate in Mdx Mice.</title>
            <link>http://www.medworm.com/index.php?rid=2630428&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19622873%26dopt%3DAbstract</link>
            <description>Authors: Kikkawa N, Ohno T, Nagata Y, Shiozuka M, Kogure T, Matsuda R
    Ectopic calcification occurs in the skeletal muscle of mdx mice, a dystrophin-deficient animal model of Duchenne muscular dystrophy. The purpose of this study was to clarify the mechanism of the calcification. The calcified deposits were identified as hydroxyapatite, a crystallized form of calcium phosphate, and the serum inorganic phosphate (Pi) level in the mdx mice was approximately 1.4 times higher than that in the normal B10 mice, suggesting that Pi plays a critical role in the ectopic calcification. When C2C12 mouse myoblasts were cultured under high-Pi conditions, myogenic differentiation was retarded while the expression of osteogenic markers such as osteocalcin and Runx2 were upregulated. This was followed b...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2630428</comments>
            <pubDate>Fri, 17 Jul 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Male germline stem cell division and spermatocyte growth require insulin signaling in Drosophila.</title>
            <link>http://www.medworm.com/index.php?rid=2526265&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19384053%26dopt%3DAbstract</link>
            <description>We examined whether insulin signaling extrinsically induces the greatest cell growth in Drosophila diploid cells and found that spermatocyte growth was affected in mutants. The results indicate that in addition to its function in somatic cells, insulin signaling plays an essential role in cell proliferation and growth during male Drosophila gametogenesis and that sperm production is regulated by hormonal control via insulin-like peptides.
    PMID: 19384053 [PubMed - in process] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2526265</comments>
            <pubDate>Sat, 27 Jun 2009 11:31:04 +0100</pubDate>
            <guid isPermaLink="false">2526265</guid>        </item>
        <item>
            <title>The RZZ complex and the spindle assembly checkpoint.</title>
            <link>http://www.medworm.com/index.php?rid=2526262&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19420794%26dopt%3DAbstract</link>
            <description>Authors: Lu Y, Wang Z, Ge L, Chen N, Liu H
    The conserved protein Rod is found in various organisms. It is localized on the kinetochores or spindle microtubules during cell division. Rod is required for proper chromosome segregation during both mitosis and meiosis. The effects of rod mutations are similar for both equational and reductional divisions, giving rise to anaphases with lagging chromosomes and/or unequal numbers of chromosomes at the two poles. Recent studies have shown that Rod is a significant component of the mitotic checkpoint. It can form the RZZ complex with Zw10 and Zwilch, which plays an important role in maintaining a functional spindle assembly checkpoint.
    PMID: 19420794 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2526262</comments>
            <pubDate>Sat, 27 Jun 2009 11:31:04 +0100</pubDate>
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            <title>TRFH Domain Is Critical for TRF1-Mediated Telomere Stabilization.</title>
            <link>http://www.medworm.com/index.php?rid=2526260&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19521025%26dopt%3DAbstract</link>
            <description>Authors: Okamoto K, Shinkai Y
    Telomere is the nucleoprotein complex essential for genomic integrity of linear chromosomes. Six telomere localizing proteins form a complex named &quot;shelterin/telosome&quot; to cooperatively regulate telomere length and protect chromosomal ends from DNA damage and repair responses. Mouse embryonic stem (ES) cells lacking TRF1, a shelterin component, exhibit a high-incidence of broken or lost telomere FISH signals, supporting a critical role for TRF1 in telomere maintenance. We demonstrate that these abnormal telomere structures are not caused by the inability of TRF1-deficient cells to recruit TIN2 but are due to a specific role for TRF1 at telomeres. Furthermore, we provide evidences that the mTRF1 TRF homology (TRFH) domain is crucial for this abnormal telomer...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2526260</comments>
            <pubDate>Wed, 10 Jun 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Simultaneous Single Cell Stable Expression of 2-4 cDNAs in HeLaS3 Using psiC31 Integrase System.</title>
            <link>http://www.medworm.com/index.php?rid=2301020&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19305101%26dopt%3DAbstract</link>
            <description>Authors: Nishiumi F, Sone T, Kishine H, Thyagarajan B, Kogure T, Miyawaki A, Chesnut JD, Imamoto F
    An important consideration in the design of multigene delivery technology is the availability of suitable vectors to introduce multiple genes stably and stoichiometrically into living cells and co-express these genes efficiently. As a promising system for this purpose, we developed multi-cDNA expression constructs harboring two to three tandemly situated cDNAs in a single plasmid. The utility of this vector system is amplified by combining it with the psiC31 recombinase system which mediates site-specific integration of the genes into naturally occurring chromosomal sequences. By analyzing 55 psiC31-mediated integration events with five different constructs, each carrying one, two or thre...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2301020</comments>
            <pubDate>Fri, 20 Mar 2009 04:00:00 +0100</pubDate>
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        <item>
            <title>Magnetic Separation of Human Podocalyxin-like Protein 1 (hPCLP1)-Positive Cells from Peripheral Blood and Umbilical Cord Blood Using Anti-hPCLP1 Monoclonal Antibody and Protein A Expressed on Bacterial Magnetic Particles.</title>
            <link>http://www.medworm.com/index.php?rid=2275196&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19293534%26dopt%3DAbstract</link>
            <description>In this study, we prepared a novel monoclonal antibody against human PCLP1 (hPCLP1) and attempted to isolate human hematopoietic progenitor cells from umbilical cord blood and peripheral blood using nano-sized bacterial magnetic particles (BacMPs) coupled with the anti-hPCLP1 antibody. Flow cytometric analysis demonstrated that the purity of separated hPCLP1-positive cells from peripheral blood was approximately 95% whereas peripheral blood mononuclear cells contained only 0.1% PCLP1(+) cells. Umbilical cord blood was demonstrated to be a better source for PCLP1(+) cells than peripheral blood. These results suggest that the separation of human PCLP1(+) cells using BacMPs with anti-hPCLP1 were extremely effective and may be useful as a means to prepare human hematopoietic progenitor cells.
...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
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            <pubDate>Tue, 17 Mar 2009 04:00:00 +0100</pubDate>
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        <item>
            <title>Novel Function of Transcription Factor ATF5: Blockade of p53-dependent Apoptosis Induced by Ionizing Irradiation.</title>
            <link>http://www.medworm.com/index.php?rid=2275195&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19293535%26dopt%3DAbstract</link>
            <description>Conclusions: It seems likely that ATF5 is a potent repressor of p53 and elevated expression of ATF5 in a tumor may relate to enhanced malignant phenotypes, such as radioresistance or greater cell motility.
    PMID: 19293535 [PubMed - as supplied by publisher] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2275195</comments>
            <pubDate>Tue, 17 Mar 2009 04:00:00 +0100</pubDate>
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        <item>
            <title>Insufficient Membrane Fusion in Dysferlin-Deficient Muscle Fibers after Heavy-Ion Irradiation.</title>
            <link>http://www.medworm.com/index.php?rid=2192363&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19218742%26dopt%3DAbstract</link>
            <description>In this study we irradiated muscle fibers isolated from skeletal muscle of SJL/J mice with heavy-ion microbeam, and the ultrastructural changes were observed by electron microscopy. The plasma membrane of heavy-ion beam irradiated areas showed irregular protrusions and invaginations. Disruption of sarcomeric structures and the enhancement of autophagy were also observed. In addition, many vesicles of varying size and shape were seen to be accumulated just beneath the plasma membrane. This finding further supports the recent hypothesis that dysferlin functions as a membrane fusion protein in the wound healing system of plasma membrane, and that the defect in dysferlin causes insufficient membrane fusion resulting in accumulation of vesicles.
    PMID: 19218742 [PubMed - as supplied by publi...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2192363</comments>
            <pubDate>Fri, 13 Feb 2009 05:00:00 +0100</pubDate>
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        <item>
            <title>pXBP1(U), a Negative Regulator of the Unfolded Protein Response Activator pXBP1(S), Targets ATF6 but not ATF4 in Proteasome-mediated Degradation.</title>
            <link>http://www.medworm.com/index.php?rid=2081762&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19122331%26dopt%3DAbstract</link>
            <description>In this study, we show that pXBP1(U) targets the active form of ATF6 but not ATF4 for destruction by the proteasome via direct association. This enhanced degradation is mediated by the degradation domain located at the pXBP1(U)-specific C-terminal end. We conclude that pXBP1(U) functions as a negative regulator of the UPR-specific transcription factors ATF6 and pXBP1(S).
    PMID: 19122331 [PubMed - as supplied by publisher] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2081762</comments>
            <pubDate>Thu, 01 Jan 2009 05:00:00 +0100</pubDate>
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        <item>
            <title>Mature Adipocyte-Derived Dedifferentiated Fat Cells Can Trans-Differentiate into Osteoblasts In Vitro and In Vivo only by All-Trans Retinoic Acid.</title>
            <link>http://www.medworm.com/index.php?rid=2048701&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19088398%26dopt%3DAbstract</link>
            <description>Authors: Oki Y, Watanabe S, Endo T, Kano K
    We investigated whether de-differentiated fat (DFAT) cells, a mature adipocyte-derived preadipocyte cell line, can be induced to trans-differentiate into osteoblasts in vitro and in vivo. All-trans retinoic acid (RA) induced expression of osteoblast-specific mRNAs encoding Cbfa1/Runx2, osterix, alkaline phosphatase, osteopontin, parathyroid hormone receptor, and osteocalcin in the DFAT cells, but did not induce the expression of adipocyte-specific mRNAs encoding PPARgamma2, C/EBPalpha, and GLUT4. Moreover, alkaline phosphatase activity was expressed in DFAT cells and the cells underwent mineralization of the bone matrix in vitro. Furthermore, when DFAT cells were transplanted subcutaneously into C57BL/6N mice in diffusion chambers, these cells...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2048701</comments>
            <pubDate>Wed, 17 Dec 2008 05:00:00 +0100</pubDate>
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        <item>
            <title>Mechanical Strain Increases Expression of Type XII Collagen in Murine Osteoblastic MC3T3-E1 Cells.</title>
            <link>http://www.medworm.com/index.php?rid=1926871&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18957791%26dopt%3DAbstract</link>
            <description>Authors: Arai K, Nagashima Y, Takemoto T, Nishiyama T
    In adult mouse, the mRNA corresponding to the alpha1 chain of type XII collagen (alpha 1(XII)) is predominantly detected in the bone. Additionally, murine osteoblastic cells, MC3T3-E1, increased the mRNA level of alpha 1(XII) response to the mechanical strain in the stretch culture system. Cyclic stretch stress resulted in a threefold increase in mRNA level of alpha 1(XII) as compared to the control experiment in MC3T3-E1. Transient transfection assays employing a reporter construct, together with site-directed mutagenesis studies, suggested that the AP-1 binding site in the first exon of mouse alpha 1(XII) gene is important for stretch stress-mediated upregulation of alpha 1(XII) expression. Electrophoretic mobility shift assay and...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1926871</comments>
            <pubDate>Wed, 29 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1926871</guid>        </item>
        <item>
            <title>Suppression of Cardiac Troponin T Induces Reduction of Contractility and Structural Disorganization in Chicken Cardiomyocytes.</title>
            <link>http://www.medworm.com/index.php?rid=1906918&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18948673%26dopt%3DAbstract</link>
            <description>Authors: Toyota N, Takano-Ohmuro H, Yoshida LS, Araki M, Yoshinobu K, Suzuki-Toyota F
    We herein examine the effect of cardiac troponin T (CTnT) suppression in cultured chicken cardiomyocytes derived from embryonic cardiac ventricular muscle. TnT is an important protein participating in regulation of striated muscle contraction, but it is not clear whether TnT contributes to the formation of sarcomere structure in myofibrils. Double-stranded RNA homologous to the nucleotide sequence of CTnT (CTnT-siRNA) was introduced into cultured muscle cells two days after plating. Transfection efficiency was above 80%. Immunoblot analyses suggested that the expression of CTnT progressively falls for the three consecutive days after transfection, but partly reappears on the fourth day. Maximum suppre...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1906918</comments>
            <pubDate>Fri, 24 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1906918</guid>        </item>
        <item>
            <title>Cross-talk-free Fluorescence Cross-Correlation Spectroscopy by the Switching Method.</title>
            <link>http://www.medworm.com/index.php?rid=1896918&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18931453%26dopt%3DAbstract</link>
            <description>In this report, we demonstrate the feasibility of switching FCCS for enzymatic cleavage of proteins in living cells. A fusion protein of two fluorophores (EGFP and mRFP) with a cleavage site of caspase-3 inserted was expressed in HeLa cells, and proteolysis assay was performed during apoptotic cell death. Due to the absence of cross-talk signals, the FCCS measurement with the switching function gave a large change in relative cross-correlation amplitude after protein cleavage. Hence, switching FCCS enables more reliable measurement of molecular interactions than conventional FCCS.
    PMID: 18931453 [PubMed - in process] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1896918</comments>
            <pubDate>Wed, 22 Oct 2008 21:53:54 +0100</pubDate>
            <guid isPermaLink="false">1896918</guid>        </item>
        <item>
            <title>Migratory Localization of Cyclin D2-Cdk4 Complex Suggests a Spatial Regulation of the G1-S Transition.</title>
            <link>http://www.medworm.com/index.php?rid=1845828&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18827403%26dopt%3DAbstract</link>
            <description>Authors: Wang Z, Xie Y, Zhang L, Zhang H, An X, Wang T, Meng A
    The association of the cyclin D-Cdk (DC) complex with retinoblastoma protein (pRb) is required for the G1-S transition of the cell cycle. Cyclin synthesis, nuclear localization and degradation are control mechanisms for the transition, but regulation of the DC complex nuclear import also contributes to the transition. Analysis of the timing of the G1-S transition in mammalian cell lines revealed acceleration with overexpression of cyclin D2 and Cdk4. Immunolocalization assays revealed that cyclin D2 and Cdk4 formed a complex in the cytoplasm and approached the nucleus. They accumulated on the cytosolic surfaces of the nuclear pores and then were arrested at the nuclear membrane before the nucleus reached a critical size. Fi...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1845828</comments>
            <pubDate>Wed, 01 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1845828</guid>        </item>
        <item>
            <title>SYP71, a Plant-specific Qc-SNARE Protein, Reveals Dual Localization to the Plasma Membrane and the Endoplasmic Reticulum in Arabidopsis.</title>
            <link>http://www.medworm.com/index.php?rid=1845827&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18827404%26dopt%3DAbstract</link>
            <description>Authors: Suwastika IN, Uemura T, Shiina T, Sato MH, Takeyasu K
    SNAREs ('Soluble N-ethyl-maleimide sensitive factor attachment protein receptors') play a critical role in the membrane fusion step of the vesicular transport system in eukaryotes. The number of the genes encoding SNARE proteins is estimated to be 64 in Arabidopsis thaliana. This number is much larger than those in other eukaryotes, suggesting a complex membrane trafficking in plants. The Arabidopsis SNAREs, the SYP7 group proteins, SYP71, SYP72, and SYP73, form a plant-specific SNARE subfamily with not-yet-identified functions. We have previously reported that the SYP7 subfamily proteins are predominantly localized to the endoplasmic reticulum in the Arabidopsis suspension cultured cells under transient expression conditio...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1845827</comments>
            <pubDate>Wed, 01 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1845827</guid>        </item>
        <item>
            <title>MicroRNA-206 Is Highly Expressed in Newly Formed Muscle Fibers: Implications Regarding Potential for Muscle Regeneration and Maturation in Muscular Dystrophy.</title>
            <link>http://www.medworm.com/index.php?rid=1845826&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18827405%26dopt%3DAbstract</link>
            <description>Authors: Yuasa K, Hagiwara Y, Ando M, Nakamura A, Takeda S, Hijikata T
    miR-1, miR-133a, and miR-206 are muscle-specific microRNAs expressed in skeletal muscles and have been shown to contribute to muscle development. To gain insight into the pathophysiological roles of these three microRNAs in dystrophin-deficient muscular dystrophy, their expression in the tibialis anterior (TA) muscles of mdx mice and CXMD(J )dogs were evaluated by semiquantitative RT-PCR and in situ hybridization. Their temporal and spatial expression patterns were also analyzed in C2C12 cells during muscle differentiation and in cardiotoxin (CTX)-injured TA muscles to examine how muscle degeneration and regeneration affect their expression. In dystrophic TA muscles of mdx mice, miR-206 expression was significantly ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1845826</comments>
            <pubDate>Wed, 01 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1845826</guid>        </item>
        <item>
            <title>Involvement of a 25 kDa Tetrahymena Ca(2+)-binding Protein in Pronuclear Exchange.</title>
            <link>http://www.medworm.com/index.php?rid=1769831&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18772531%26dopt%3DAbstract</link>
            <description>Authors: Nakagawa T, Fujiu K, Cole ES, Numata O
    The Tetrahymena Ca(2+)-binding protein of 25 kDa (TCBP-25) is a calmodulin family protein containing four EF-hand type calcium-binding domains. TCBP-25 is localized in the whole cell cortex and around both the migratory and stationary pronuclei at the pronuclear exchange stage during conjugation. TCBP-25 is expected to play an important role in conjugation, though its function during sexual reproduction has not been elucidated. According to the localization of this protein and its timing, three possible roles of TCBP-25 are proposed. TCBP-25 may play a role in 1) differentiating the two functional pronuclei from the degenerative post-meiotic nuclei, 2) the process of pronuclear exchange and 3) pronuclear fusion. To test these hypotheses, ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1769831</comments>
            <pubDate>Fri, 05 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1769831</guid>        </item>
        <item>
            <title>A Mercury Arc Lamp-Based Multi-Color Confocal Real Time Imaging System for Cellular Structure and Function.</title>
            <link>http://www.medworm.com/index.php?rid=1690247&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18685226%26dopt%3DAbstract</link>
            <description>Authors: Saito K, Kobayashi K, Tani T, Nagai T
    Multi-point scanning confocal microscopy using a Nipkow disk enables the acquisition of fluorescent images with high spatial and temporal resolutions. Like other single-point scanning confocal systems that use Galvano meter mirrors, a commercially available Nipkow spinning disk confocal unit, Yokogawa CSU10, requires lasers as the excitation light source. The choice of fluorescent dyes is strongly restricted, however, because only a limited number of laser lines can be introduced into a single confocal system. To overcome this problem, we developed an illumination system in which light from a mercury arc lamp is scrambled to make homogeneous light by passing it through a multi-mode optical fiber. This illumination system provides incoheren...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1690247</comments>
            <pubDate>Wed, 06 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1690247</guid>        </item>
        <item>
            <title>The organization of histone H3 modifications as revealed by a panel of specific monoclonal antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=1628481&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18227620%26dopt%3DAbstract</link>
            <description>Authors: Kimura H, Hayashi-Takanaka Y, Goto Y, Takizawa N, Nozaki N
    Histone modifications play critical roles in the epigenetic regulation of gene expression and in the maintenance of genome integrity. Acetylation and methylation of histone H3 are particularly important in gene activation and silencing. We generated and characterized a panel of mouse monoclonal antibodies that specifically recognize different modifications on K4, K9, and K27 residues on histone H3. By using these antibodies for chromatin immunoprecipitation and immunoblotting, we analyzed the relationship between different modifications in nearby nucleosomes in human cells. Within a few nucleosome neighbors, trimethyl-K4 was associated with acetyl-K27, rather than with dimethyl-K4 and acetyl-K9, consistent with their c...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628481</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628481</guid>        </item>
        <item>
            <title>Human RME-8 is involved in membrane trafficking through early endosomes.</title>
            <link>http://www.medworm.com/index.php?rid=1628480&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18256511%26dopt%3DAbstract</link>
            <description>Authors: Fujibayashi A, Taguchi T, Misaki R, Ohtani M, Dohmae N, Takio K, Yamada M, Gu J, Yamakami M, Fukuda M, Waguri S, Uchiyama Y, Yoshimori T, Sekiguchi K
    RME-8 is a DnaJ-domain-containing protein that was first identified in Caenorhabditis elegans as being required for uptake of yolk proteins. RME-8 has also been identified in other species, including flies and mammals, and the phenotypes of their RME-8 mutants suggest the importance of this protein in endocytosis. In the present study, we cloned human RME-8 (hRME-8) and characterized its biochemical properties and functions in endocytic pathways. hRME-8 was found to be a peripheral protein that was tightly associated with the membrane via its N-terminal region. It partially colocalized with several early endosomal markers, but no...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628480</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628480</guid>        </item>
        <item>
            <title>GFP-like proteins stably accumulate in lysosomes.</title>
            <link>http://www.medworm.com/index.php?rid=1628479&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18256512%26dopt%3DAbstract</link>
            <description>In this study, we demonstrate that these structures are not cytosolic aggregates but lysosomes that have accumulated the GFP-like proteins. Our biochemical and immunocytochemical experiments have revealed that certain GFP-like proteins expressed in the cytosol enter lysosomes possibly by an autophagy-related mechanism, but retain their fluorescence because of resistance not only to acidity but also to lysosomal proteases.
    PMID: 18256512 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628479</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628479</guid>        </item>
        <item>
            <title>BDNF increases the phagocytic activity in cultured iris pigment epithelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628478&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18285636%26dopt%3DAbstract</link>
            <description>Authors: Yoshida H, Tomita H, Sugano E, Isago H, Ishiguro S, Tamai M
    To investigate the effect of brain derived neurotrophic factor (BDNF) on the phagocytic activity in iris pigment epithelial (IPE) cells, purified porcine photoreceptor outer segments (POS) were applied to cultured IPE cells for three hours. To measure phagocytic activities, bound and total POS were differentially stained using a double immunofluorescence staining method. BDNF increased the binding of POS in IPE cells in a dose-dependent manner. Ingestion of POS, however, was not affected throughout the concentrations used in this study. To investigate the signal transduction pathways of BDNF, a phosphatidylinositol 3-kinase (PI3K) inhibitor, LY294002, and MAPK/ERK kinase (MEK) inhibitor, PD98059, were used for this st...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628478</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628478</guid>        </item>
        <item>
            <title>Different effects of all-trans-retinoic acid on phorbol ester-stimulated and phytohemagglutinin-stimulated interleukin-2 expression in human T-cell lymphoma HUT-78 cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628476&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18296860%26dopt%3DAbstract</link>
            <description>Authors: Goto S, Okada N, Kaneko A, Isemura M
    In view of the importance of vitamin A in the human immune system and the central role of interleukin-2 (IL-2) in the proliferation of T-lymphocytes, we examined the effects of all-trans-retinoic acid (ATRA) on the protein and gene expression of IL-2 in the human T-cell line HUT-78 when stimulated with either 12-O-tetradecanoylphorbol-13-acetate (TPA) or phytohemagglutinin (PHA). ATRA enhanced the production of IL-2 stimulated by TPA, but suppressed that stimulated by PHA. These findings were consistent with the results of a reverse transcription-polymerase chain reaction and quantitative real-time polymerase chain reaction examining IL-2 gene expression. ATRA augmented the gene expression of PKC-beta1 up-regulated by TPA and restored that ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628476</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628476</guid>        </item>
        <item>
            <title>Phospholipase D is essential for keratocyte-like migration of NBT-II cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628475&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18344600%26dopt%3DAbstract</link>
            <description>Authors: Nagasaki A, Inotsume K, Kanada M, Uyeda TQ
    NBT-II cells on collagen-coated substrates move rapidly and persistently, maintaining a semi-circular shape with a large lamellipodium, in a manner similar to fish keratocytes. The inhibitor of phospholipase D (PLD), n-butanol, completely blocked the migration and disturbed the characteristic localization of actin along the edge of lamellipodia. To investigate the functional difference between the two isozymes of PLD (PLD1 and PLD2), we transfected NBT-II cells with vectors expressing shRNA to deplete PLD1 or PLD2. Depletion of both PLD1 and 2 by RNA interference reduced the velocity of the migration, but depletion of PLD2 inhibited motility more severely than that of PLD1. Furthermore, GFP-PLD2 was localized to the protruding regions...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628475</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:32 +0100</pubDate>
            <guid isPermaLink="false">1628475</guid>        </item>
        <item>
            <title>ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum.</title>
            <link>http://www.medworm.com/index.php?rid=1628474&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18360008%26dopt%3DAbstract</link>
            <description>In this study, we performed a genome-wide search for ATF6alpha-target genes in mice. Only 30 of the 14,729 analyzable genes were identified as specific targets, of which 40% were ER quality control proteins, 20% were ER proteins, while the rest had miscellaneous functions. The negative effects of the absence of PERK on transcriptional induction of ER quality control proteins could be explained by its inhibitory effect on ATF6alpha activation. Further, proteins involved in transport from the ER are not regulated by ATF6alpha, and transport of folded cargo molecules from the ER was not affected by the absence of ATF6alpha. Based on these results, we propose that ATF6 is a transcription factor specialized in the regulation of ER quality control proteins.
    PMID: 18360008 [PubMed - indexed f...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628474</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:31 +0100</pubDate>
            <guid isPermaLink="false">1628474</guid>        </item>
        <item>
            <title>Mechanism of destruction of microtubule structures by 4-hydroxy-2-nonenal.</title>
            <link>http://www.medworm.com/index.php?rid=1628473&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18360009%26dopt%3DAbstract</link>
            <description>In this study we addressed the mechanism. Immunochemical studies revealed that HNE preferentially modified alpha-tubulin in rat primary neuronal cells, PC12 cells, and rat fibroblast cell line 3Y1 cells. This was morphologically associated with the disappearance of microtubule structures in those cells. In a purified rat brain microtubule fraction, HNE modified unpolymerized tubulin and impaired its polymerizability, with a concomitant increase in insolubilized tubulin. Nevertheless, HNE had a marginal effect on the stability of pre-polymerized microtubules. These results suggest that disruption of microtubule assembly as a result of HNE modification of unpolymerized tubulin, rather than destruction of assembled microtubules, is responsible for the disappearance of microtubule structures i...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628473</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:31 +0100</pubDate>
            <guid isPermaLink="false">1628473</guid>        </item>
        <item>
            <title>Recruitment of Tom1L1/Srcasm to endosomes and the midbody by Tsg101.</title>
            <link>http://www.medworm.com/index.php?rid=1628472&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18367816%26dopt%3DAbstract</link>
            <description>Authors: Yanagida-Ishizaki Y, Takei T, Ishizaki R, Imakagura H, Takahashi S, Shin HW, Katoh Y, Nakayama K
    Tom1 (target of Myb 1) and its related proteins (Tom1L1/Srcasm and Tom1L2) constitute a protein family, which share an N-terminal VHS (Vps27, Hrs and STAM) domain and a following GAT (GGA and Tom1) domain. Tom1L1 has potential binding sequences for Tsg101, which is one of key regulators of the multivesicular body (MVB) formation. To obtain a clue to the role of Tom1L1 in the MVB formation, we have characterized the Tom1L1-Tsg101 interaction. We have found that not only the PTAP sequence in the GAT domain but also the PSAP sequence in the C-terminal region of Tom1L1 is responsible for its interaction with the UEV domain of Tsg101 and competes with the HIV-1 Gag protein for the Tsg10...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628472</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:31 +0100</pubDate>
            <guid isPermaLink="false">1628472</guid>        </item>
        <item>
            <title>Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes.</title>
            <link>http://www.medworm.com/index.php?rid=1628470&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18388399%26dopt%3DAbstract</link>
            <description>Authors: Kimura S, Noda T, Yoshimori T
    Autophagy is a membrane trafficking pathway that carries cytosolic components to the lysosome for degradation. During this process, the autophagosome, a double-membraned organelle, is generated de novo, sequesters cytoplasmic proteins and organelles, and delivers them to lysosomes. However, the mechanism by which autophagosomes are targeted to lysosomes has not been determined. Here, we observed the real-time behavior of microtubule-associated protein light chain 3 (LC3), which localizes to autophagosomes, and showed that autophagosomes move in a microtubule- and dynein-dynactin motor complex-dependent manner. After formation, autophagosomes show a rapid vectorial movement in the direction of the centrosome, where lysosomes are usually concentrate...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628470</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:31 +0100</pubDate>
            <guid isPermaLink="false">1628470</guid>        </item>
        <item>
            <title>Ultrastructural study of Rac1 and its effectors beneath the substratum-facing membrane.</title>
            <link>http://www.medworm.com/index.php?rid=1628469&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18497446%26dopt%3DAbstract</link>
            <description>In this study, we examined the molecular organization on the cytoplasmic surface of the substratum-facing plasma membrane, focusing on Rac1 and its effectors, IQGAP1 and Sra-1, by electron microscopy. We employed deep-etch immunoreplica methods to observe the membrane cytoskeletal architecture while determining molecular locations. Beneath the plasma membrane, Rac1 and its effectors showed similar, but distinct, destinations. Rac1 localized on the membrane and associated with the membrane cytoskeleton. IQGAP1 predominantly localized beside actin filaments and occasionally near microtubules together with Rac1. On the other hand, Sra-1 localized at actin filaments, microtubules, and the plasma membrane. Sra-1 colabeled with Rac1 was mainly found at the membrane and actin filaments. These res...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628469</comments>
            <pubDate>Wed, 16 Jul 2008 19:39:31 +0100</pubDate>
            <guid isPermaLink="false">1628469</guid>        </item>
        <item>
            <title>Functional Analysis of alpha5beta1 Integrin and Lipid Rafts in Invasion of Epithelial Cells by Porphyromonas gingivalis using Fluorescent Beads Coated with Bacterial Membrane Vesicle.</title>
            <link>http://www.medworm.com/index.php?rid=1628471&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18388398%26dopt%3DAbstract</link>
            <description>Authors: Tsuda K, Furuta N, Inaba H, Kawai S, Hanada K, Yoshimori T, Amano A
    Porphyromonas gingivalis, a periodontal pathogen, was previously suggested to exploit alpha5beta1 integrin and lipid rafts to invade host cells. However, it is unknown if the functional roles of these host components are divided on the bacterial invasion. In the present study, we analyzed the mechanisms underlying P. gingivalis invasion, using fluorescent beads coated with bacterial membrane vesicles (MV beads). Cholesterol depletion reagents including methyl-beta-cyclodextrin (MbetaCD) drastically inhibited the entry of MV beads into epithelial cells, while they were less effective on bead adhesion to the cells. Bead entry was also abolished in CHO cells deficient in sphingolipids, components of lipid rafts, ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628471</comments>
            <pubDate>Fri, 04 Apr 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628471</guid>        </item>
        <item>
            <title>AMSH, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes.</title>
            <link>http://www.medworm.com/index.php?rid=1628498&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17159328%26dopt%3DAbstract</link>
            <description>Authors: Kyuuma M, Kikuchi K, Kojima K, Sugawara Y, Sato M, Mano N, Goto J, Takeshita T, Yamamoto A, Sugamura K, Tanaka N
    The appropriate sorting of vesicular cargo, including cell-surface proteins, is critical for many cellular functions. Ubiquitinated cargo is targeted to endosomes and digested by lysosomal enzymes. We previously identified AMSH, a deubiquitination enzyme (DUB), to be involved in vesicular transport. Here, we purified an AMSH-binding protein, CHMP3, which is an ESCRT-III subunit. ESCRT-III functions on maturing endosomes, indicating AMSH might also play a role in MVB/late endosomes. Expression of an AMSH mutant lacking CHMP3-binding ability resulted in aberrant endosomes with accumulations of ubiquitinated cargo. Nevertheless, CHMP3-binding capability was not essenti...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628498</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628498</guid>        </item>
        <item>
            <title>Substitution F659G in the Irr1p/Scc3p cohesin influences the cell wall of Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=1628496&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17229992%26dopt%3DAbstract</link>
            <description>Authors: Cena A, Orlowski J, Machula K, Fronk J, Kurlandzka A
    The sister chromatid cohesion complex of Saccharomyces cerevisiae is composed of proteins termed cohesins. The complex forms a ring structure that entraps sister DNAs, probably following replication. The mechanism of cohesion is universal and the proteins participating in this process are evolutionarily highly conserved. We investigated the Irr1p/Scc3p cohesin subunit, an under-studied protein. We show that the presence of a mutated copy of IRR1 gene, encoding the F658G substitution in Irr1p, changes the sensitivity of the heterozygous irr1-1/IRR1 diploid to cell wall-affecting compounds. Microscopic images indicate that chitin distribution in the mutant cell wall is affected, although the biochemical composition of the cell...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628496</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628496</guid>        </item>
        <item>
            <title>Differential Ras activation between caveolae/raft and non-raft microdomains.</title>
            <link>http://www.medworm.com/index.php?rid=1628495&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17314458%26dopt%3DAbstract</link>
            <description>Authors: Fukano T, Sawano A, Ohba Y, Matsuda M, Miyawaki A
    Although the consequences of Ras activation have been studied extensively in the context of oncogenesis, its regulation in physiological modes of signal transduction is not well understood. A fluorescent indicator, Raichu-Ras, was fused to the C-terminal hypervariable regions of H-Ras and K-Ras to create indicators for Ras activation within caveolae/rafts (Raichu-tH) and non-raft domains (Raichu-tK) of the plasma membrane, respectively. Raichu-tH was also found abundantly in endomembranes. To monitor Ras activation with high spatial resolution, it is imperative to observe sectioned images of the signals. We have developed a wide-field fluorescence microscope equipped with a digital micromirror device (DMD) to acquire optically ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628495</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628495</guid>        </item>
        <item>
            <title>Induction of beating by imposed bending or mechanical pulse in demembranated, motionless sea urchin sperm flagella at very low ATP concentrations.</title>
            <link>http://www.medworm.com/index.php?rid=1628494&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17314459%26dopt%3DAbstract</link>
            <description>Authors: Ishikawa R, Shingyoji C
    A basic feature of the movement of eukaryotic flagella is oscillation. Although flagellar oscillation is thought to be regulated by a self-regulatory feedback system including the mechanical signal of bending itself, the mechanism regulating the dynein motile activity to produce oscillation is not well understood. To elucidate the mechanism, we developed a new experimental system which allowed us to analyze the conditions necessary for the induction of oscillation. When a mechanical signal of bending or a pulse was applied by micromanipulation to a demembranated motionless sea urchin sperm flagellar axoneme at very low ATP concentrations (1-3 microM), a localized pair of bends was induced. The bend formation was often followed by further responses inclu...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628494</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628494</guid>        </item>
        <item>
            <title>Heavy ion microbeam irradiation induces ultrastructural changes in isolated single fibers of skeletal muscle.</title>
            <link>http://www.medworm.com/index.php?rid=1628493&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17460350%26dopt%3DAbstract</link>
            <description>Authors: Hino M, Wada S, Tajika Y, Morimura Y, Hamada N, Funayama T, Sakashita T, Kakizaki T, Kobayashi Y, Yorifuji H
    The effects of heavy ion microbeams on muscle fibers isolated from mouse skeletal muscles were examined by electron microscopy. The plasma membranes of heavy ion beam-irradiated areas of muscle fibers showed irregular protrusions and invaginations. In the cytoplasm, an irregular distribution of microfilaments was found near the plasma membrane. Sarcoplasmic reticula in the irradiated regions showed a distended appearance with flocculent material within the lumen. These changes were seen as early as 2 min after irradiation, and persisted until as late as 22 min after irradiation. Many autophagic vacuoles could be seen at 7 min after irradiation. At 22 min, the vacuoles b...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628493</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628493</guid>        </item>
        <item>
            <title>ARMET is a soluble ER protein induced by the unfolded protein response via ERSE-II element.</title>
            <link>http://www.medworm.com/index.php?rid=1628492&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17507765%26dopt%3DAbstract</link>
            <description>Authors: Mizobuchi N, Hoseki J, Kubota H, Toyokuni S, Nozaki J, Naitoh M, Koizumi A, Nagata K
    Arginine rich, mutated in early stage of tumors (ARMET) was first identified as a human gene highly mutated in a variety of cancers. However, little is known about the characteristics of the ARMET protein and its expression. We identified ARMET as a gene upregulated by endoplasmic reticulum (ER) stress. Here, we show that the mouse homologue of ARMET is an 18-kDa soluble ER protein that is mature after cleavage of a signal sequence and has four intramolecular disulfide bonds, including two in CXXC sequences. ER stress stimulated ARMET expression, and the expression patterns of ARMET mRNA and protein in mouse tissues were similar to those of Grp78, an Hsp70-family protein required for quality c...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628492</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628492</guid>        </item>
        <item>
            <title>Quantitative analysis of cortical actin filaments during polar body formation in starfish oocytes.</title>
            <link>http://www.medworm.com/index.php?rid=1628491&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17575411%26dopt%3DAbstract</link>
            <description>Authors: Hamaguchi Y, Numata T, K Satoh S
    Polar body formation is an extremely unequal cell division. In order to understand the mechanism of polar body formation, morphological changes at the animal pole were investigated in living oocytes of the starfish, Asterina pectinifera, and the amounts of cortical actin filaments were quantitatively estimated after staining the maturing oocytes with fluorescently-labeled phallotoxins using a computer and image-processing software. Formation of a bulge, which is presumed to become a polar body, and the anaphase separation of chromosomes occurred simultaneously. When the bulge became large, one group of chromatids moved into the bulge. The dividing furrow then formed and finally a polar body formed. Just at the time of bulge formation, the inten...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628491</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628491</guid>        </item>
        <item>
            <title>Functional domain analysis of human HP1 isoforms in Drosophila.</title>
            <link>http://www.medworm.com/index.php?rid=1628490&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17575412%26dopt%3DAbstract</link>
            <description>Authors: Kato M, Kato Y, Nishida M, Hayakawa T, Haraguchi T, Hiraoka Y, H Inoue Y, Yamaguchi M
    Three subtypes of HP1, a conserved non-histone chromosomal protein enriched in heterochromatin, have been identified in humans, HP1alpha, beta and gamma. In the present study, we utilized a Drosophila system to characterize human HP1 functions. Over-expression of HP1beta in eye imaginal discs caused abnormally patterned eyes, with reduced numbers of ommatidia, and over-expression of HP1gamma in wing imaginal discs caused abnormal wings, in which L4 veins were gapped. These phenotypes were specific to the HP1 subtypes and appear to reflect suppressed gene expression. To determine the molecular domains of HP1 required for each specific phenotype, we constructed a series of chimeric molecules wi...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628490</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628490</guid>        </item>
        <item>
            <title>Role of IRS and PHIP on insulin-induced tyrosine phosphorylation and distribution of IRS proteins.</title>
            <link>http://www.medworm.com/index.php?rid=1628489&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17634669%26dopt%3DAbstract</link>
            <description>Authors: Kaburagi Y, Okochi H, Satoh S, Yamashita R, Hamada K, Ikari K, Yamamoto-Honda R, Terauchi Y, Yasuda K, Noda M
    To analyze the functional differences of the insulin receptor substrate (IRS) family, the N-terminal fragments containing the pleckstrin homology (PH) domains and the phosphotyrosine-binding (PTB) domains of IRS (IRS-N) proteins, as well as intact IRS molecules, were expressed in Cos-1 cells, and insulin-induced tyrosine phosphorylation and subcellular distribution of IRS proteins were analyzed. In contrast to the distinct affinities toward phosphoinositides, these IRS-N fragments non-selectively inhibited insulin-induced tyrosine phosphorylation of IRS-1, IRS-2 and IRS-3, among which IRS3-N was most effective. The mutations of IRS-1 disrupting all the phosphoinositide...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628489</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628489</guid>        </item>
        <item>
            <title>Implication of amphiphysin 1 and dynamin 2 in tubulobulbar complex formation and spermatid release.</title>
            <link>http://www.medworm.com/index.php?rid=1628488&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17785912%26dopt%3DAbstract</link>
            <description>Authors: Kusumi N, Watanabe M, Yamada H, Li SA, Kashiwakura Y, Matsukawa T, Nagai A, Nasu Y, Kumon H, Takei K
    Tubulobulbar complexes (TBCs) are composed of several tubular invaginations formed at the plasma membrane of testicular Sertoli cells. TBCs are transiently formed at the contact region with spermatids at spermatogenic stage VII in rat and mouse, and such TBC formation is prerequisite for spermatid release. Since the characteristic structure of TBCs suggests that the molecules implicated in endocytosis could be involved in TBC formation, we here investigated the localization and physiological roles of endocytic proteins, amphiphysin 1 and dynamin 2, at TBCs. We demonstrated by immunofluorescence that the endocytic proteins were concentrated at TBCs, where they colocalized with c...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628488</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628488</guid>        </item>
        <item>
            <title>A novel function of plant histone H1: microtubule nucleation and continuous plus end association.</title>
            <link>http://www.medworm.com/index.php?rid=1628487&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17917305%26dopt%3DAbstract</link>
            <description>Authors: Hotta T, Haraguchi T, Mizuno K
    In higher plant cells, various microtubular arrays can be seen despite of their lack of structurally defined microtubule-organizing centers (MTOCs) like centrosomes in animal cells. Little is known about the molecular properties of the microtubule-organizing centers in higher plant cells. The nuclear surface contains one of these microtubule-organizing centers and generates microtubules radially toward the cell periphery (radial microtubules). Previously, we reported that histone H1 possessed the microtubule-organizing activity, and it was suggested that histone H1 localized on the nuclear surfaces in Tobacco BY-2 cells (Nakayama, T., Ishii, T., Hotta, T., and Mizuno, K. J. Biol. Chem. (submitted)). Here we show that histone H1 forms ring-shaped ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628487</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628487</guid>        </item>
        <item>
            <title>A Drosophila orthologue of larp protein family is required for multiple processes in male meiosis.</title>
            <link>http://www.medworm.com/index.php?rid=1628486&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17951964%26dopt%3DAbstract</link>
            <description>Authors: Ichihara K, Shimizu H, Taguchi O, Yamaguchi M, Inoue YH
    It is important for the proper execution of cell division in both mitosis and meiosis that the chromosome segregation, cytokinesis, and partition of cell organelles progress in smooth coordination. We show here that the mitochondria inheritance is closely linked with microtubules during meiotic divisions in Drosophila males. They are first clustered in a cell equator at metaphase associated with astral microtubules and then distributed along central spindle microtubules after anaphase. The molecular mechanism for the microtubule-dependent inheritance of mitochondria in male meiosis has not been demonstrated yet. We first isolated mutations for a larp gene that is highly conserved among eukaryotes and showed that these mut...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628486</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628486</guid>        </item>
        <item>
            <title>Psg18 is specifically expressed in follicle-associated epithelium.</title>
            <link>http://www.medworm.com/index.php?rid=1628485&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17984568%26dopt%3DAbstract</link>
            <description>Authors: Kawano K, Ebisawa M, Hase K, Fukuda S, Hijikata A, Kawano S, Date Y, Tsuneda S, Itoh K, Ohno H
    Pregnancy-specific glycoproteins (Psgs) secreted by the placenta regulate the immune system to ensure the survival of the fetal allograft by inducing IL-10, an anti-inflammatory cytokine. However, it is unknown whether Psgs are involved in more general aspects of immune response other than maternal immunity. Here, we report that Psg18 is highly expressed in the follicle-associated epithelium (FAE) overlaying Peyer's patches (PPs). Bioinformatics analysis with Reference Database for Immune Cells (RefDIC) as well as RT-PCR data demonstrated that Psg18 is exclusively expressed in FAE in adult mice, in contrast to other Psg family members that are either not expressed or only slightly ex...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628485</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628485</guid>        </item>
        <item>
            <title>Endothelial cells constituting blood-nerve barrier have highly specialized characteristics as barrier-forming cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628484&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18057801%26dopt%3DAbstract</link>
            <description>Authors: Sano Y, Shimizu F, Nakayama H, Abe M, Maeda T, Ohtsuki S, Terasaki T, Obinata M, Ueda M, Takahashi R, Kanda T
    In autoimmune disorders of the peripheral nervous system (PNS) such as Guillain-Barr&amp;#xE9; syndrome and chronic inflammatory demyelinating polyradiculoneuropathy, breakdown of the blood-nerve barrier (BNB) has been considered as a key step in the disease process. Hence, it is important to know the cellular property of peripheral nerve microvascular endothelial cells (PnMECs) constituting the bulk of BNB. Although many in vitro models of the blood-brain barrier (BBB) have been established, very few in vitro BNB models have been reported so far. We isolated PnMECs from transgenic rats harboring the temperature-sensitive SV40 large T-antigen gene (tsA58 rat) and investiga...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628484</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628484</guid>        </item>
        <item>
            <title>Identification of novel nuclear localization signals of Drosophila myeloid leukemia factor.</title>
            <link>http://www.medworm.com/index.php?rid=1628483&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18159124%26dopt%3DAbstract</link>
            <description>Authors: Sugano W, Yamaguchi M
    Myeloid leukemia factor 1 (MLF1) was first identified as part of a leukemic fusion protein produced by a chromosomal translocation, and MLF family proteins are present in many animals. In mammalian cells, MLF1 has been described as mainly cytoplasmic, but in Drosophila, one of the dMLF isoforms (dMLFA) localized mainly in the nucleus while the other isoform (dMLFB), that appears to be produced by the alternative splicing, displays both nuclear and cytoplasmic localization. To investigate the difference in subcellular localization between MLF family members, we examined the subcellular localization of deletion mutants of dMLFA isoform. The analyses showed that the C-terminal 40 amino acid region of dMLFA is necessary and sufficient for nuclear localization...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628483</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628483</guid>        </item>
        <item>
            <title>Involvement of p120 carboxy-terminal domain in cadherin trafficking.</title>
            <link>http://www.medworm.com/index.php?rid=1628482&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18159125%26dopt%3DAbstract</link>
            <description>Authors: Liu H, Komiya S, Shimizu M, Fukunaga Y, Nagafuchi A
    P120 plays an essential role in cadherin turnover. The molecular mechanism involved, however, remains only partially understood. Here, using a gene trap targeting technique, we replaced the genomic sequence of p120 with HA-tagged p120 cDNA in mouse teratocarcinoma F9 cells. In the p120 knock-in (p120KI) cells, we found that the expression level of p120 was severely reduced and that the expression level of other components of the cadherin-catenin complex was also reduced. The stable expression of various p120 mutants in p120KI cells revealed that the armadillo repeat domain of p120 is sufficient to restore the expression level of E-cadherin. In p120KI cells, internalized E-cadherin was frequently detected as large aggregates. ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628482</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628482</guid>        </item>
        <item>
            <title>Gene expression and distribution of Swi6 in partial aneuploids of the fission yeast Schizosaccharomyces pombe.</title>
            <link>http://www.medworm.com/index.php?rid=1628477&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18285637%26dopt%3DAbstract</link>
            <description>Authors: Chikashige Y, Tsutsumi C, Okamasa K, Yamane M, Nakayama J, Niwa O, Haraguchi T, Hiraoka Y
    Imbalances of gene expression in aneuploids, which contain an abnormal number of chromosomes, cause a variety of growth and developmental defects. Aneuploid cells of the fission yeast Schizosaccharomyces pombe are inviable, or very unstable, during mitotic growth. However, S. pombe haploid cells bearing minichromosomes derived from the chromosome 3 can grow stably as a partial aneuploid. To address biological consequences of aneuploidy, we examined the gene expression profiles of partial aneuploid strains using DNA microarray analysis. The expression of genes in disomic or trisomic cells was found to increase approximately in proportion to their copy number. We also found that some genes ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628477</comments>
            <pubDate>Mon, 01 Jan 2007 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628477</guid>        </item>
        <item>
            <title>ErbB and HB-EGF signaling in heart development and function.</title>
            <link>http://www.medworm.com/index.php?rid=1628513&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16508205%26dopt%3DAbstract</link>
            <description>Authors: Iwamoto R, Mekada E
    The epidermal growth factor (EGF)-ErbB signaling network is composed of multiple ligands of the EGF family and four tyrosine kinase receptors of the ErbB family. In higher vertebrates, these four receptors bind a multitude of ligands. Ligand binding induces the formation of various homo- and heterodimers of ErbB, potentially providing for a high degree of signal diversity. ErbB receptors and their ligands are expressed in a variety of tissues throughout development. Recent advances in gene targeting strategies in mice have revealed that the EGF-ErbB signaling network has fundamental roles in development, proliferation, differentiation, and homeostasis in mammals. The heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of growth fac...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628513</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628513</guid>        </item>
        <item>
            <title>Cytoplasmic domain phosphorylation of heparin-binding EGF-like growth factor.</title>
            <link>http://www.medworm.com/index.php?rid=1628512&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16557002%26dopt%3DAbstract</link>
            <description>Authors: Wang X, Mizushima H, Adachi S, Ohishi M, Iwamoto R, Mekada E
    Heparin-binding EGF-like growth factor (HB-EGF) is synthesized as a transmembrane precursor protein that is anchored to the plasma membrane. The extracellular EGF-like domain acts as a mitogen and motogen upon ectodomain shedding, but the functional roles of the transmembrane and cytoplasmic domains are largely unknown. We demonstrate here that cytoplasmic domain of HB-EGF is phosphorylated by external stimuli, and that the phosphorylation site is involved in HB-EGF-dependent tumorigenesis. Treatment of Vero cells overexpressing human HB-EGF with 12-O-tetradecanoylphorbol-13-acetate (TPA) caused ectodomain shedding of HB-EGF and generated two carboxyl (C)-terminal fragments with distinct electrophoretic mobilities. M...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628512</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628512</guid>        </item>
        <item>
            <title>Deficiency of the Caenorhabditis elegans DNA polymerase eta homologue increases sensitivity to UV radiation during germ-line development.</title>
            <link>http://www.medworm.com/index.php?rid=1628511&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16565574%26dopt%3DAbstract</link>
            <description>Authors: Ohkumo T, Masutani C, Eki T, Hanaoka F
    Defects in the human XPV/POLH gene result in the variant form of the disease xeroderma pigmentosum (XP-V). The gene encodes DNA polymerase eta (Poleta), which catalyzes translesion synthesis (TLS) past UV-induced cyclobutane pyrimidine dimers (CPDs) and other lesions. To further understand the roles of Poleta in multicellular organisms, we analyzed phenotypes caused by suppression of Caenorhabditis elegans POLH (Ce-POLH) by RNA interference (RNAi). F1 and F2 progeny from worms treated by Ce-POLH-specific RNAi grew normally, but F1 eggs laid by worms treated by RNAi against Ce-POLD, which encodes Poldelta did not hatch. These results suggest that Poldelta but not Poleta is essential for C. elegans embryogenesis. Poleta-targeted embryos UV-...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628511</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628511</guid>        </item>
        <item>
            <title>Merkel cell-nerve cell interaction undergoes formation of a synapse-like structure in a primary culture.</title>
            <link>http://www.medworm.com/index.php?rid=1628510&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16648663%26dopt%3DAbstract</link>
            <description>Authors: Shimohira-Yamasaki M, Toda S, Narisawa Y, Sugihara H
    Merkel cells have been assumed to guide nerve fibers to the skin. However, there has been little in vitro evidence that supports this hypothesis, because there is no suitable established culture system of Merkel cells. Here we show that Merkel cells isolated from rat footpad skin were successfully cultured in a monolayer with keratinocytes. Keratinocytes did not affect any structural changes in Merkel cells. When nerve cells (NG108-15 or PC12) were added to the culture system, both nerve fibers and cytoplasmic processes of Merkel cells outgrew and cooperatively organized synapse-like structures at their contact points. Nerve cells promoted Merkel cell survival, compared with keratinocytes only. Merkel cell proliferation was ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628510</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628510</guid>        </item>
        <item>
            <title>X-ray irradiation altered chemosensitivity of a p53-null non-small cell lung cancer cell line.</title>
            <link>http://www.medworm.com/index.php?rid=1628509&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16951535%26dopt%3DAbstract</link>
            <description>Authors: Tsutsumi K, Yasuda M, Nishioka T
    Radiotherapy is an effective approach to treating many types of cancer. Recent progress in radiotherapy technology, such as intensity-modulated radiation therapy (IMRT) and three-dimensional (3D) radiotherapy, allow precise energy transfer to the tumor, which has improved local control rates. However, the emergence of tolerant cells during or after radiotherapy remains problematic. In the present study, we first established a cell population from H1299, the p53-null non-small cell lung cancer cell line, by 10 Gy irradiation using 6 MV X-rays. The radio- and chemosensitivity of this cell population (referred to as H1299-IR) was determined using colony formation analyses and MTS assays. Compared with the parental cell line, the radiosensitivity o...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628509</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628509</guid>        </item>
        <item>
            <title>Identification of Jmjd1a as a STAT3 downstream gene in mES cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628508&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16988490%26dopt%3DAbstract</link>
            <description>Authors: Ko SY, Kang HY, Lee HS, Han SY, Hong SH
    Mouse embryonic stem (mES) cells can be maintained in undifferentiated state in the presence of a cytokine, leukemia inhibitory factor (LIF). Many investigators found that STAT3 activation is important for the maintenance of pluripotency by LIF. However, the downstream pathways of STAT3 activation are still unknown. To look for STAT3-downstream target genes, we performed DD-RT PCR in the presence or absence of LIF. Through further confirmation, we finally selected 8 genes whose expressions were significantly dependent upon the presence of LIF. Among them, Jmjd1a was down-regulated after LIF withdrawal, and it was selected for further investigation. Its expression started to decrease 1 day after the removal of LIF, and disappeared on day ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628508</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628508</guid>        </item>
        <item>
            <title>The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN.</title>
            <link>http://www.medworm.com/index.php?rid=1628507&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17062999%26dopt%3DAbstract</link>
            <description>Authors: Sakane H, Yamamoto T, Tanaka K
    Drs2p, the catalytic subunit of the Cdc50p-Drs2p putative aminophospholipid translocase, has been implicated in conjunction with the Arf1 signaling pathway in the formation of clathrin-coated vesicles (CCVs) from the TGN. Herein, we searched for Arf regulator genes whose mutations were synthetically lethal with cdc50Delta, and identified the Arf GAP gene GCS1. Most of the examined transport pathways in the Cdc50p-depleted gcs1Delta mutant were nearly normal, including endocytic transport to vacuoles, carboxypeptidase Y sorting, and the processing and secretion of invertase. In contrast, this mutant exhibited severe defects in the early endosome-to-TGN transport pathway; proteins that are transported via this pathway, such as the v-SNARE Snc1p, th...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628507</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628507</guid>        </item>
        <item>
            <title>Soluble megalin is accumulated in the lumen of the rat endolymphatic sac.</title>
            <link>http://www.medworm.com/index.php?rid=1628506&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17063000%26dopt%3DAbstract</link>
            <description>Authors: Ishida T, Hatae T, Nishi N, Araki N
    The endolymphatic sac (ES) is believed to play an important role in maintaining homeostasis in the inner ear by the absorption and endocytosis of endolymph. Megalin is a 600-kDa multiligand endocytic receptor expressed in certain types of absorptive epithelia including kidney proximal tubules. We analyzed the immunoreactivity for megalin in rat ES by immunofluorescence, immunogold electron microscopy, and immunoblotting. With immunostaining, the luminal substances of the ES were strongly stained for megalin. Megalin was also localized in luminal macrophage-like cells and both types of epithelial cell (mitochondria-rich cells and ribosome-rich cells). In these cells, the megalin was localized in the lumen of endosomes, but was not membrane as...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628506</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628506</guid>        </item>
        <item>
            <title>Visualization of the post-Golgi trafficking of multiphoton photoactivated transferrin receptors.</title>
            <link>http://www.medworm.com/index.php?rid=1628505&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17072087%26dopt%3DAbstract</link>
            <description>In this report, first, we demonstrated the advantages of photoactivating PA-GFP, a variant of the Aequorea victoria green fluorescent protein (GFP), with multiphoton laser light rather than single-photon laser light, in terms of photoactivation efficiency and spatial resolution. We then applied the multiphoton photoactivation technique to selectively photoactivate the TfR tagged with PA-GFP (PA-GFP-TfR) at the TGN, and monitored the movement of the photoactivated PA-GFP-TfR in live cells. We observed that the PA-GFP-TfR photoactivated at the TGN are transported to the Tfn(+)EEA1(+) endosomal compartments after exiting the TGN. These data support the notion that early endosomes can serve as a sorting station for not only internalized plasma membrane proteins in the endocytic pathway but als...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628505</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628505</guid>        </item>
        <item>
            <title>Mechanical strength of sarcomere structures of skeletal myofibrils studied by submicromanipulation.</title>
            <link>http://www.medworm.com/index.php?rid=1628504&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17110784%26dopt%3DAbstract</link>
            <description>Authors: Kayamori T, Miyake N, Akiyama N, Aimi M, Wakayama J, Kunioka Y, Yamada T
    The mechanical strength of sarcomere structures of skeletal muscle was studied by rupturing single myofibrils of rabbit psoas muscle by submicromanipulation techniques. Microbeads coated with alpha-actinin were attached to the surface of myofibrils immobilized to coverslip. By use of either optical tweezers or atomic force microscope, the attached beads were captured and detached from the myofibrils. During the detachment of the beads, the actin filaments bound specifically to the beads were peeled off from the bulk structures of myofibrils, thus rupturing the peripheral components of the myofibrils bound to the actin filaments. By analyzing the ruptures thus produced in various myofibril preparations, it...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628504</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628504</guid>        </item>
        <item>
            <title>XBP1 is critical to protect cells from endoplasmic reticulum stress: evidence from Site-2 protease-deficient Chinese hamster ovary cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628503&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17110785%26dopt%3DAbstract</link>
            <description>Authors: Yoshida H, Nadanaka S, Sato R, Mori K
    XBP1 is a transcription factor downstream of IRE1, a transmembrane protein in the endoplasmic reticulum (ER) which functions as a sensor and transducer of ER stress. XBP1 mRNA is constitutively expressed at a low level as an intron-containing precursor mRNA (unspliced mRNA), which is subject to IRE1-mediated splicing reaction upon ER stress to produce the active form of XBP1, pXBP1(S). Because the XBP1 promoter carries a perfect ER stress-response element, namely, the cis-acting element responsible for the induction of ER chaperones, and XBP1 mRNA is induced in response to ER stress with a time course similar to that of ER chaperone mRNAs, it is conjectured that transcription factor ATF6, activated immediately upon ER stress, induces the t...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628503</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628503</guid>        </item>
        <item>
            <title>Analysis of ATF6 activation in Site-2 protease-deficient Chinese hamster ovary cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628502&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17110786%26dopt%3DAbstract</link>
            <description>Authors: Nadanaka S, Yoshida H, Sato R, Mori K
    Mammalian transcription factor ATF6 is constitutively synthesized as a type II transmembrane protein embedded in the endoplasmic reticulum (ER). It is activated when unfolded proteins are accumulated in the ER under ER stress through a process called regulated intramembrane proteolysis (Rip), in which ATF6 is transported from the ER to the Golgi apparatus where it undergoes sequential cleavage by Site-1 and Site-2 proteases. The cytosolic transcription factor domain of ATF6 liberated from the Golgi membrane enters the nucleus where it activates transcription of ER-localized molecular chaperones and folding enzymes, leading to the maintenance of the homeostasis of the ER. Here, we analyzed M19 cells, a mutant of Chinese hamster ovary cells ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628502</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628502</guid>        </item>
        <item>
            <title>Reduction of disulfide bridges in the lumenal domain of ATF6 in response to glucose starvation.</title>
            <link>http://www.medworm.com/index.php?rid=1628501&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17130669%26dopt%3DAbstract</link>
            <description>In this study, we evoked ER stress under more physiological conditions, namely, glucose starvation, and analyzed its consequence for ATF6 activation. Glucose starvation activated ATF6 and induced the ER chaperone BiP, albeit weakly. ATF6 was thus dissociated from BiP, transported to the Golgi apparatus, and cleaved. Glucose starvation enhanced the synthesis of ATF6 approximately two-fold, probably via transcriptional induction. Importantly, reduction of disulfide bridges and transport of reduced monomer occurred in response to glucose starvation. We conclude that ER stress-induced reduction of ATF6 represents a general feature of the ATF6 activation process.
    PMID: 17130669 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628501</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628501</guid>        </item>
        <item>
            <title>Effect of 3-methyladenine on the fusion process of macropinosomes in EGF-stimulated A431 cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628500&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17146146%26dopt%3DAbstract</link>
            <description>In this study, we examined the effect of 3-methlyadenine (3-MA), which shows a distinct specificity to the PI3K classes from wortmannin and LY294002, on the macropinosome formation and fusion in EGF-stimulated A431 cells. Unlike wortmannin or LY294002, 3-MA did not inhibit the uptake of fluorescent dextran by macropinocytosis. However, the fusion of macropinosomes was inhibited by 3-MA. By imaging of live-cells expressing fluorescent protein-fused tandem FYVE domains, we found that PtdIns(3)P appeared on the macropinosomal membrane shortly after the closure of macropinocytic cups and remained on macropinosomes even at 60-min age. The production of PtdIns(3)P and the recruitment of EEA1 to macropinosomes were abolished by the 3-MA treatment. Therefore, it is likely that 3-MA impairs recruit...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628500</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628500</guid>        </item>
        <item>
            <title>Dynamic changes in the subcellular localization of Drosophila beta-sarcoglycan during the cell cycle.</title>
            <link>http://www.medworm.com/index.php?rid=1628499&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17159290%26dopt%3DAbstract</link>
            <description>Authors: Hashimoto R, Yamaguchi M
    One of the proposed roles of sarcoglycan is to stabilize dystrophin glycoprotein complexes in muscle sarcolemma. Involvement in signal transduction has also been proposed and abnormalities in some sarcoglycan genes are known to be responsible for muscular dystrophy. While characterization of sarcoglycans in muscle has been performed, little is known about its functions in the non-muscle tissues in which mammalian sarcoglycans are expressed. Here, we investigated temporal and spatial expression patterns of Drosophila beta-sarcoglycan (dScgbeta) during development by immunohistochemistry. In addition to almost ubiquitous expression in various tissues and organs, as seen for its mammalian counterpart, anti-dScgbeta staining data of embryos, eye imaginal d...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628499</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628499</guid>        </item>
        <item>
            <title>Localization of type I myosin and F-actin to the leading edge region of the forespore membrane in Schizosaccharomyces pombe.</title>
            <link>http://www.medworm.com/index.php?rid=1628497&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D17202724%26dopt%3DAbstract</link>
            <description>Authors: Itadani A, Nakamura T, Shimoda C
    Myo1, a heavy chain of type I myosin of the fission yeast Schizosaccharomyces pombe, is essential for sporulation. Here we have analyzed the expression, localization and cellular function of the type I myosin light chain calmodulin, Cam2, encoded by cam2(+). Transcription of cam2(+) was constitutive and markedly enhanced in meiosis. The cam2 null mutant was viable and completed sporulation normally at 28 degrees C, but formed four-spored asci poorly at 34 degrees C. In those sporulation-defective cells, the forespore membrane was formed abnormally. A Cam2-GFP fusion protein accumulated at the cell poles in interphase cells and at the medial septation site in postmitotic cells, colocalizing with Myo1 and F-actin patches. During the mating proces...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628497</comments>
            <pubDate>Sun, 01 Jan 2006 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628497</guid>        </item>
        <item>
            <title>Identification of a neural cell specific variant of microtubule-associated protein 4.</title>
            <link>http://www.medworm.com/index.php?rid=1628530&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840943%26dopt%3DAbstract</link>
            <description>Authors: Matsushima K, Aosaki M, Tokuraku K, Hasan MR, Nakagawa H, Kotani S
    The microtubule-binding domain of MAP4, a ubiquitous microtubule-associated protein, contains a region rich in proline and basic residues (proline-rich region). We searched the bovine adrenal gland for MAP4 isoforms, and identified a novel variant lacking 72 consecutive amino acid residues within the proline-rich region, as compared with the full-length MAP4. The amino acid sequence of the missing region was highly conserved (about 85% identity/similarity) among the corresponding regions of bovine, human, mouse, and rat MAP4, which suggested the functional significance of this region. A comparison of the genomic sequence with the cDNA sequence revealed that the missing region is encoded by a single exon. A MAP4...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628530</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628530</guid>        </item>
        <item>
            <title>Hsp16p is required for thermotolerance in nuclear mRNA export in fission yeast Schizosaccharomyces pombe.</title>
            <link>http://www.medworm.com/index.php?rid=1628529&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840944%26dopt%3DAbstract</link>
            <description>Authors: Yoshida J, Tani T
    Export of mRNA from the nucleus to the cytoplasm is one of the essential steps for eukaryotic gene expression. In the fission yeast Schizosaccharomyces pombe, heat shock stress at 42 degrees C causes block of mRNA export from the nucleus. We now report that saline and ethanol stresses also inhibit nuclear mRNA export, resulting in accumulation of bulk poly (A)+ RNA, as well as a specific mRNA, in the nucleus. Under stressed conditions, an mRNA export receptor Mex67p relocates to the nucleolus from the nuclear periphery and this relocation is closely correlated with inhibition of mRNA export by the stresses. Pretreatment of cells with a mild saline stress induced thermotolerance in mRNA export in a similar manner seen with mild heat pretreatment and protected ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628529</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628529</guid>        </item>
        <item>
            <title>Functional expression of single-chain heterodimeric G-protein-coupled receptors for adenosine and dopamine.</title>
            <link>http://www.medworm.com/index.php?rid=1628528&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840945%26dopt%3DAbstract</link>
            <description>Authors: Kamiya T, Saitoh O, Nakata H
    The direct homo- and heteromeric association between G-protein-coupled receptors (GPCRs), adenosine A2A receptor (A(2A)R) and dopamine D2 receptor (D2R), occurs although little is known about the selectivity of their formation (A(2A)R/A(2A)R vs. A(2A)R/D2R). In order to stimulate the heteromerization of A(2A)R and D2R, we have designed a single-polypeptide-chain heterodimeric A(2A)R/D2R complex by fusing the C-terminus of the A(2A)R via transmembrane (TM) of a type II TM protein with the N-terminus of D2R in tandem. This was successfully expressed on the cell surface as a full-length protein with specific binding to the respective ligands and functional coupling to G-proteins comparable to wild-type receptors, suggesting the possible creation of ph...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628528</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628528</guid>        </item>
        <item>
            <title>Truncation of the projection domain of MAP4 (microtubule-associated protein 4) leads to attenuation of microtubule dynamic instability.</title>
            <link>http://www.medworm.com/index.php?rid=1628527&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840946%26dopt%3DAbstract</link>
            <description>Authors: Permana S, Hisanaga S, Nagatomo Y, Iida J, Hotani H, Itoh TJ
    MAP4, a ubiquitous heat-stable MAP, is composed of an asymmetric structure common to the heat-stable MAPs, consisting of an N-terminal projection (PJ) domain and a C-terminal microtubule (MT)-binding (MTB) domain. Although the MTB domain has been intensively studied, the role of the PJ domain, which protrudes from MT-wall and does not bind to MTs, remains unclear. We investigated the roles of the PJ domain on the dynamic instability of MTs by dark-field microscopy using various PJ domain deletion constructs of human MAP4 (PJ1, PJ2, Na-MTB and KDM-MTB). There was no obvious difference in the dynamic instability between the wtMAP4 and any fragments at 0.1 microM, the minimum concentration required to stabilize MTs. The...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628527</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628527</guid>        </item>
        <item>
            <title>Class-specific binding of two aminoacyl-tRNA synthetases to annexin, a Ca2+- and phospholipid-binding protein.</title>
            <link>http://www.medworm.com/index.php?rid=1628526&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840947%26dopt%3DAbstract</link>
            <description>Authors: Shirakawa T, Nakamura A, Kohama K, Hirakata M, Ogihara S
    Annexins are a family of Ca2+/phospholipid-binding proteins that have diverse functions. To understand the function of annexin in Physarum polycephalum, we searched for its binding proteins. Here we demonstrate the presence of two novel annexin-binding proteins. The homology search of partial amino acid sequences of these two proteins identified them as aminoacyl-tRNA synthetases (ARSs). Furthermore, antibody against aminoacyl-tRNA synthetases cross-reacted with one of two proteins. Our results imply the interaction between intracellular membrane dynamics and protein translation system, and may give a clue to understand the mechanism of some myositis diseases, which have been known to produce autoantibodies against ARSs....</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628526</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628526</guid>        </item>
        <item>
            <title>Protamine-induced epithelial barrier disruption involves rearrangement of cytoskeleton and decreased tight junction-associated protein expression in cultured MDCK strains.</title>
            <link>http://www.medworm.com/index.php?rid=1628525&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15840948%26dopt%3DAbstract</link>
            <description>In conclusion, protamine induces alterations in the epithelial barrier function of MDCK monolayers that may involve the cytoskeleton and TJ-associated proteins. The various actions of protamine on epithelial function may reflect different degrees of interaction of protamine with the plasma membrane and different intracellular processes triggered by this polycation.
    PMID: 15840948 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628525</comments>
            <pubDate>Tue, 01 Feb 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628525</guid>        </item>
        <item>
            <title>1,25-Dihydroxyvitamin D3 suppresses gene expression of eukaryotic translation initiation factor 2 in human promyelocytic leukemia HL-60 cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628524&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15951637%26dopt%3DAbstract</link>
            <description>Authors: Suzuki T, Koyama Y, Ichikawa H, Tsushima K, Abe K, Hayakawa S, Kuruto-Niwa R, Nozawa R, Isemura M
    The physiologically active metabolite of vitamin D(3), 1alpha,25-dihydroxyvitamin D(3) (DVD), is a potent inducer of cell differentiation in human myeloid leukemia cells. In the present study, we examined changes in gene expression during DVD-induced cell differentiation of promyelocytic HL-60 cells employing a DNA microarray technique. The results identified 7 up-regulated and 9 down-regulated genes with a change greater than 1.5-fold after the DVD-treatment for both 2 and 6 days. Seven of these genes were further examined by reverse transcription-polymerase chain reaction (RT-PCR). The results showed that findings obtained from the DNA microarray analysis and RT-PCR are generall...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628524</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628524</guid>        </item>
        <item>
            <title>Microtubule bundle formation and cell death induced by the human CLASP/Orbit N-terminal fragment.</title>
            <link>http://www.medworm.com/index.php?rid=1628523&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16145243%26dopt%3DAbstract</link>
            <description>Authors: Aonuma M, Miyamoto M, Inoue YH, Tamai K, Sakai H, Kamasawa N, Matsukage A
    Previously we have identified the Drosophila orbit gene whose hypomorphic mutations cause abnormal chromosome segregation (Inoue et al., 2000). The orbit encodes Orbit/Mast, a 165-kDa microtubule-associated protein (MAP) with GTP-binding motifs. Two human homologues of the Orbit/Mast, CLASP1 (hOrbit1) and CLASP2 (hOrbit2) have been identified. Using an antibody to CLASP1/hOrbit1 polypeptide, we confirmed that the polypeptide of about 150 kDa associates with microtubule purified from the porcine brain. Thus, we conjectured that CLASP1 may be a human orthologue of the Drosophila Orbit/Mast, and therefore we named it h (human) Orbit1. We constructed the plasmid for expression of a fusion protein of the puta...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628523</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628523</guid>        </item>
        <item>
            <title>A fission yeast SNAP-25 homologue, SpSec9, is essential for cytokinesis and sporulation.</title>
            <link>http://www.medworm.com/index.php?rid=1628522&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16272747%26dopt%3DAbstract</link>
            <description>Authors: Nakamura T, Kashiwazaki J, Shimoda C
    The soluble NSF attachment protein 25 (SNAP-25) is a component of the SNARE complex that is essential for regulated exocytosis in diverse cell types. Here, we identified a fission yeast SNAP-25 homologue, SpSec9. The sec9+ gene was essential for vegetative growth. sec9 mRNA was detected in vegetative cells and further increased during sporulation. This increase during sporulation was dependent on Mei4, a meiosis-specific transcription factor. A sporulation-deficient sec9 mutant was isolated by random PCR mutagenesis (sec9-10). The sec9-10 mutant also exhibited temperature sensitivity for growth and cell division was found to arrest before completion of cell separation at restrictive temperatures. In sec9-10 cells, the forespore membrane was...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628522</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628522</guid>        </item>
        <item>
            <title>Defining the roles of beta-catenin and plakoglobin in cell-cell adhesion: isolation of beta-catenin/plakoglobin-deficient F9 cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628521&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16357441%26dopt%3DAbstract</link>
            <description>Authors: Fukunaga Y, Liu H, Shimizu M, Komiya S, Kawasuji M, Nagafuchi A
    F9 teratocarcinoma cells in which beta-catenin and/or plakoglobin genes are knocked-out were generated and investigated in an effort to define the role of beta-catenin and plakoglobin in cell adhesion. Loss of beta-catenin expression only did not affect cadherin-mediated cell adhesion activity. Loss of both beta-catenin and plakoglobin expression, however, severely affected the strong cell adhesion activity of cadherin. In beta-catenin-deficient cells, the amount of plakoglobin associated with E-cadherin dramatically increased. In beta-catenin/plakoglobin-deficient cells, the level of E-cadherin and alpha-catenin markedly decreased. In these cells, E-cadherin formed large aggregates in cytoplasm and membrane local...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628521</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628521</guid>        </item>
        <item>
            <title>Soluble form of heparin-binding EGF-like growth factor contributes to retinoic acid-induced epidermal hyperplasia.</title>
            <link>http://www.medworm.com/index.php?rid=1628520&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16357442%26dopt%3DAbstract</link>
            <description>Authors: Kimura R, Iwamoto R, Mekada E
    Heparin-binding EGF-like growth factor (HB-EGF), a member of the EGF-family, is thought to be important for keratinocyte functions. HB-EGF is first synthesized as a membrane-anchored form, and its soluble form is released by ectodomain shedding. Here we investigate the role of HB-EGF in epidermal hyperplasia induced by all-trans retinoic acid (tRA) treatment. HB-EGF is normally expressed in epidermis of normal adult mice at very low levels, but topical tRA treatment results in epidermal hyperplasia, concomitant with the strong induction of HB-EGF expression in the suprabasal layer. tRA-induced epidermal hyperplasia was reduced both in the keratinocyte-specific HB-EGF null mice (K5-HB(del/del)) and knock-in mice expressing the uncleavable mutant fo...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628520</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628520</guid>        </item>
        <item>
            <title>A role for fission yeast Rab GTPase Ypt7p in sporulation.</title>
            <link>http://www.medworm.com/index.php?rid=1628519&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16357443%26dopt%3DAbstract</link>
            <description>Authors: Kashiwazaki J, Nakamura T, Iwaki T, Takegawa K, Shimoda C
    Ypt7p, a fission yeast (Schizosaccharomyces pombe) homologue of Rab7 GTPase, mediates fusion of endosomes to vacuoles and homotypic vacuole fusion. Here, we report that Ypt7p plays important roles in sporulation. Most ypt7Delta asci produced less than four spores, which were apparently immature and germinated at low frequency. Furthermore, ypt7Delta cells were defective in development of the forespore membranes. Vacuoles in sporulating cells were found to undergo extensive homotypic vacuole fusion to form a few large compartments occupying the entire cytoplasm of asci. This extensive vacuole fusion depended on Ypt7p.
    PMID: 16357443 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628519</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628519</guid>        </item>
        <item>
            <title>The role of mammalian Staufen on mRNA traffic: a view from its nucleocytoplasmic shuttling function.</title>
            <link>http://www.medworm.com/index.php?rid=1628518&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16377940%26dopt%3DAbstract</link>
            <description>Authors: Miki T, Takano K, Yoneda Y
    The localization of mRNA in neuronal dendrites plays a role in both locally and temporally regulated protein synthesis, which is required for certain forms of synaptic plasticity. RNA granules constitute a dendritic mRNA transport machinery in neurons, which move along microtubules. RNA granules contain densely packed clusters of ribosomes, but lack some factors that are required for translation, suggesting that they are translationally incompetent. Recently some of the components of RNA granules have been identified, and their functions are in the process of being examined, in attempts to better understand the properties of RNA granules. Mammalian Staufen, a double-stranded RNA binding protein, is a component of RNA granules. Staufen is localized in...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628518</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628518</guid>        </item>
        <item>
            <title>Molecular dissection of ARP1 regions required for nuclear migration and cell wall integrity checkpoint functions in Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=1628517&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16415535%26dopt%3DAbstract</link>
            <description>Authors: Igarashi R, Suzuki M, Nogami S, Ohya Y
    The dynactin complex is one of the components required for the regulation of the cell wall integrity checkpoint, which ensures the completion of cell wall remodeling before mitosis. The core of the dynactin complex is a backbone filament composed of monomers of an actin-related protein, Arp1, which is also involved in nuclear migration. To examine the molecular basis for the dual functions of the dynactin core subunit Arp1p in yeast, we constructed 32 mutated arp1 alleles. We assessed the effects of the mutations on cell wall integrity checkpoint and nuclear migration functions and identified four categories of mutants: 1) those showing no change from the wild type; 2) those resulting in a defective cell wall integrity checkpoint but norm...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628517</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628517</guid>        </item>
        <item>
            <title>Phosphorylation of RanGAP1 stabilizes its interaction with Ran and RanBP1.</title>
            <link>http://www.medworm.com/index.php?rid=1628516&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16428860%26dopt%3DAbstract</link>
            <description>Authors: Takeda E, Hieda M, Katahira J, Yoneda Y
    Ran is a nuclear Ras-like GTPase that is required for various nuclear events including the bi-directional transport of proteins and ribonucleoproteins through the nuclear pore complex, spindle formation, and reassembly of the nuclear envelope. One of the key regulators of Ran is RanGAP1, a Ran specific GTPase activating protein. The question of whether a mechanism exists for controlling nucleocytoplasmic transport through the regulation of RanGAP1 activity continues to be debated. Here we show that RanGAP1 is phosphorylated in vivo and in vitro. Serine-358 (358S) was identified as the major phosphorylation site, by MALDI-TOF-MS spectrometry. Site directed mutagenesis at this position abolished the phosphorylation. Experiments using purif...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628516</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628516</guid>        </item>
        <item>
            <title>Molecular dissection of internalization of Porphyromonas gingivalis by cells using fluorescent beads coated with bacterial membrane vesicle.</title>
            <link>http://www.medworm.com/index.php?rid=1628515&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16428861%26dopt%3DAbstract</link>
            <description>Authors: Tsuda K, Amano A, Umebayashi K, Inaba H, Nakagawa I, Nakanishi Y, Yoshimori T
    Porphyromonas gingivalis is one of the causative agents of adult periodontitis, and has been reported to be internalized by nonphagocytic epithelial cells. However, the mechanism for the internalization remains unclear. In the present study, we addressed this issue using fluorescent beads coated with bacterial membrane vesicles (MVs) that retain surface components of P. gingivalis. We established an assay system in which we could easily quantify the bead internalization to cells. MVs-coated beads were internalized by HeLa cells in kinetics similar to that of living bacteria. The internalization depended on dynamin but not clathrin. The beads were internalized through the actin-mediated pathway that i...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628515</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628515</guid>        </item>
        <item>
            <title>Primary cilia of inv/inv mouse renal epithelial cells sense physiological fluid flow: bending of primary cilia and Ca2+ influx.</title>
            <link>http://www.medworm.com/index.php?rid=1628514&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D16474191%26dopt%3DAbstract</link>
            <description>Authors: Shiba D, Takamatsu T, Yokoyama T
    Primary cilia are hypothesized to act as a mechanical sensor to detect renal tubular fluid flow. Anomalous structure of primary cilia and/or impairment of increases in intracellular Ca2+ concentration in response to fluid flow are thought to result in renal cyst formation in conditional kif3a knockout, Tg737 and pkd1/pkd2 mutant mice. The mutant inv/inv mouse develops multiple renal cysts like kif3a, Tg737 and pkd1/pkd2 mutants. Inv proteins have been shown to be localized in the renal primary cilia, but response of inv/inv cilia to fluid stress has not been examined. In the present study, we examined the mechanical response of primary cilia to physiological fluid flow using a video microscope, as well as intracellular Ca2+ increases in renal e...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628514</comments>
            <pubDate>Sat, 01 Jan 2005 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628514</guid>        </item>
        <item>
            <title>Functional characterization of contractile vacuole isolated from Amoeba proteus.</title>
            <link>http://www.medworm.com/index.php?rid=1628533&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15665503%26dopt%3DAbstract</link>
            <description>Authors: Nishihara E, Shimmen T, Sonobe S
    Contractile vacuoles (CVs) released from cells of Amoeba proteus were used to analyze its function in vitro. When CV was transferred to a hypertonic medium, its volume decreased within 10 sec. When it was subsequently returned to its original medium, it quickly started swelling. However, it ruptured before recovering its initial volume. These results suggested that the CV membrane is semi-permeable and that the fluid is collected by the osmotic gradient in vivo. The water permeability of membrane of isolated CV was calculated from the rate of osmotic volume change to be 0.94 microm/sec . OsM. This high value suggested that CV membrane is equipped with water channel. CV contracted (or burst) quickly upon addition of 1 mM ATP. Contraction was ind...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628533</comments>
            <pubDate>Wed, 01 Dec 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628533</guid>        </item>
        <item>
            <title>Immunohistochemical localization of Klotho protein in brain, kidney, and reproductive organs of mice.</title>
            <link>http://www.medworm.com/index.php?rid=1628532&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15665504%26dopt%3DAbstract</link>
            <description>Authors: Li SA, Watanabe M, Yamada H, Nagai A, Kinuta M, Takei K
    Klotho mutant mouse (kl-/-), a mouse model for human aging, exhibits various phenotypes in a wide range of organs including arteriosclerosis, neural degeneration, skin and gonadal atrophy, pulmonary emphysema, calcification of soft tissues, and cognition impairment. Klotho mRNA, however, is expressed only in brain, kidney, reproductive organs, pituitary gland, and parathyroid gland. Therefore it remains to be elucidated how lack of Klotho protein in these limited organs leads to the variety of phenotypes. To shed light on mechanisms by which Klotho protein acts on distant targets, we examined localization of Klotho protein in brain, kidney, and reproductive organs, and analyzed brain and kidney in kl-/- mice searching for...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628532</comments>
            <pubDate>Wed, 01 Dec 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628532</guid>        </item>
        <item>
            <title>Adenosine A2A receptor facilitates calcium-dependent protein secretion through the activation of protein kinase A and phosphatidylinositol-3 kinase in PC12 cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628531&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15665505%26dopt%3DAbstract</link>
            <description>In this study, we found that treatment of PC12 cells with the A(2A)-R agonist CGS21680 promotes calcium-evoked secretion of the fusion protein between neuropeptide Y and modified yellow fluorescence protein (NPY-Venus). CGS21680 treatment of PC12 cells transiently increased the phosphorylation of p38 and JNK MAP kinases and Akt, as well as that of ATF2 and CREB, reaching maximal levels at around 10-15 min of CGS21680 treatment. Importantly, pretreatment of PC12 cells with the PI3K inhibitor LY294002, together with the protein kinase A (PKA) inhibitor KT5720, significantly inhibited CGS21680 enhancement of calcium-dependent NPY-Venus release. Moreover, expression of a dominant-negative form of Akt and the PKA inhibitory polypeptide protein kinase inhibitor (PKI) co-operatively inhibited the...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628531</comments>
            <pubDate>Wed, 01 Dec 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628531</guid>        </item>
        <item>
            <title>Turnover of actin in Chlamydomonas flagella detected by fluorescence recovery after photobleaching (FRAP).</title>
            <link>http://www.medworm.com/index.php?rid=1628535&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15528838%26dopt%3DAbstract</link>
            <description>Authors: Watanabe Y, Hayashi M, Yagi T, Kamiya R
    Recent indirect observations have suggested that various axonemal proteins in cilia and flagella of live cells undergo turnover independently of shortening or elongation of the axoneme. To gain direct evidence, here we examined using a FRAP (fluorescence recovery after photobleaching) technique whether actin, a subunit of inner arm dynein, is being turned over in Chlamydomonas flagella. Fluorescently labeled rabbit actin was introduced by electroporation into the cells of ida5oda1, a double mutant between oda1 lacking outer arm dynein and ida5 lacking several species of inner arm dyneins due to the absence of a conventional-type actin. In actin-loaded cells, flagella became motile and fluorescent due to incorporation of inner-arm dyneins...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628535</comments>
            <pubDate>Tue, 01 Jun 2004 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628535</guid>        </item>
        <item>
            <title>Human amniotic epithelial cells possess hepatocyte-like characteristics and functions.</title>
            <link>http://www.medworm.com/index.php?rid=1628534&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15528839%26dopt%3DAbstract</link>
            <description>Authors: Takashima S, Ise H, Zhao P, Akaike T, Nikaido T
    Hepatocyte transplantation is expected to become a novel method for treatment of liver disease. However, many questions remain regarding this approach, especially concerning donor cells. To evaluate whether human amniotic epithelial cells can be used as a cell source for hepatocyte transplantation, hepatic gene expression and functions of human amniotic epithelial cells were analyzed. Reverse transcription-polymerase chain reaction analysis demonstrated that human amniotic epithelial cells expressed albumin, alpha(1)-antitrypsin, and other hepatocyte-related genes. Cultivated human amniotic epithelial cells demonstrated albumin production, glycogen storage, and albumin secretion consistent with the hepatocyte gene expression prof...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628534</comments>
            <pubDate>Tue, 01 Jun 2004 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628534</guid>        </item>
        <item>
            <title>Abstracts of the 57th Annual Meeting of the Japan Society for Cell Biology. Osaka, Japan, May 26-28, 2004.</title>
            <link>http://www.medworm.com/index.php?rid=1628564&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15185676%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 15185676 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628564</comments>
            <pubDate>Sat, 01 May 2004 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628564</guid>        </item>
        <item>
            <title>Morphological and biochemical characterization of macrophages activated by carrageenan and lipopolysaccharide in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=1628539&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15342962%26dopt%3DAbstract</link>
            <description>In conclusion, our morphological and biochemical data clearly showed that in vivo stimulation with CAR induces a potent inflammatory response in macrophages representing an interesting model to analyze inflammatory responses.
    PMID: 15342962 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628539</comments>
            <pubDate>Thu, 01 Apr 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628539</guid>        </item>
        <item>
            <title>Expression profile of mouse BWF1, a protein with a BEACH domain, WD40 domain and FYVE domain.</title>
            <link>http://www.medworm.com/index.php?rid=1628538&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15342963%26dopt%3DAbstract</link>
            <description>Authors: Chen GY, Muramatsu H, Ichihara-Tanaka K, Muramatsu T
    We isolated a mouse cDNA encoding a protein that contains a BEACH domain, 5 WD40 repeats and a FYVE domain, which we designated as BWF1. The mRNA is approximately 10 kb in size and encodes a protein consisting of 3508 amino acids with a predicted molecular weight of 385 kDa. BWF1 has 45% homology with the Drosophila protein, blue cheese (BCHS). The BWF1 gene consists of 67 exons, which span 270 kb of genomic sequence, and has been mapped to mouse chromosome 5. Northern blot analysis revealed that it was strongly expressed in the liver, moderately in the kidney and testis, and weakly in the brain of adult mice. During the development of the mouse brain, BWF1 mRNA was abundant on embryonic day (E) 14-16; after birth, the level...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628538</comments>
            <pubDate>Thu, 01 Apr 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628538</guid>        </item>
        <item>
            <title>An ultrastructural and biochemical study of foot structure in &quot;catch&quot; smooth muscle cells of a clam.</title>
            <link>http://www.medworm.com/index.php?rid=1628537&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15342964%26dopt%3DAbstract</link>
            <description>Authors: Notsu E, Matsuno A
    The foot structure of molluscan (clam) catch muscle cells was studied from the structural and biochemical standpoints. In vertebrate cross striated muscle cells, foot structures are situated in the interspaces between T-tubules and sarcoplasmic reticula (SRs). By contrast, T-tubules were not observed in clam catch muscle cells, but foot structures were ultrastructurally identified in the interspaces between the SRs and cell membranes. We isolated the SR fraction from muscle cells which contained vesicles with SRs and cell membranes. Foot structures were also observed in the SR fraction by thin sectioning. The size and shape of the foot structure in both intact muscle cells and the SR fractions appeared to be slightly smaller than those of vertebrates. Howeve...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628537</comments>
            <pubDate>Thu, 01 Apr 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628537</guid>        </item>
        <item>
            <title>Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628536&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15342965%26dopt%3DAbstract</link>
            <description>Authors: Uemura T, Ueda T, Ohniwa RL, Nakano A, Takeyasu K, Sato MH
    In all eucaryotic cells, specific vesicle fusion during vesicular transport is mediated by membrane-associated proteins called SNAREs (soluble N-ethyl-maleimide sensitive factor attachment protein receptors). Sequence analysis identified a total of 54 SNARE genes (18 Qa-SNAREs/Syntaxins, 11 Qb-SNAREs, 8 Qc-SNAREs, 14 R-SNAREs/VAMPs and 3 SNAP-25) in the Arabidopsis genome. Almost all of them were ubiquitously expressed through out all tissues examined. A series of transient expression assays using green fluorescent protein (GFP) fused proteins revealed that most of the SNARE proteins were located on specific intracellular compartments: 6 in the endoplasmic reticulum, 9 in the Golgi apparatus, 4 in the trans-Golgi netwo...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628536</comments>
            <pubDate>Thu, 01 Apr 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628536</guid>        </item>
        <item>
            <title>Ybr267w is a new cytoplasmic protein belonging to the mitotic signaling network of Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=1628566&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15107529%26dopt%3DAbstract</link>
            <description>Authors: Iwase M, Toh-e A
    YBR267w designated REI1 (required for isotropic bud growth) was isolated by two-hybrid screening using NIS1 encoding the neck protein as bait. Disruption of REI1 exhibited cold sensitive growth but did not exhibit a morphological defect. However, Deltarei1Deltanap1, Deltarei1Deltacla4 and Deltarei1Deltagin4 double disruptants exhibited an elongated cell morphology, which was suppressed by the disruption of SWE1, indicating that REI1 is a new member of genes belonging to the mitotic signaling network that negatively regulates Swe1 kinase. Deltanap1 cells displayed a lower Gin4 kinase activity and a lower Gin4 protein level, both of which were recovered nearly to a wild type level in Deltarei1Deltanap1 cells. Interaction between Rei1 and Gin4 was suggested from ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628566</comments>
            <pubDate>Sun, 01 Feb 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628566</guid>        </item>
        <item>
            <title>Isolation of desmosomes from the epidermis of Xenopus laevis and immunochemical characterization of the Xenopus desmosomal cadherins.</title>
            <link>http://www.medworm.com/index.php?rid=1628565&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15107530%26dopt%3DAbstract</link>
            <description>Authors: Ohga R, Shida M, Shida H
    Here we report a new method of isolating epidermal desmosomes from Xenopus laevis, and a major constituent of desmosomes designated as Xenopus desmogleins (XDsg). Isolation of desmosomes from Xenopus laevis epidermis was carried out by a two step-incubation with different concentrations of NP-40. After discontinuous sucrose gradient centrifugation at 30,000 g for 60 min, a pure desmosomal fraction was obtained at 30%/40% interface. In the SDS-PAGE of isolated desmosomes, at least 12 bands (XDB1 to XDB12) were observed over a 75 kD region. Among them, three bands (XDB3, XDB7, XDB8; estimated MW 175, 124, and 112 kD respectively) were recognized as glycoproteins based on ConA binding. Monospecific polyclonal antibody against XDB3 cross-reacted with bovin...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628565</comments>
            <pubDate>Sun, 01 Feb 2004 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628565</guid>        </item>
        <item>
            <title>Stimulation of pro-MMP-2 production and activation by native form of extracellular type I collagen in cultured hepatic stellate cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628568&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15004420%26dopt%3DAbstract</link>
            <description>We examined the regulatory role of the native form of type I collagen fibrils in pro-MMP-2 production and activation in cultured HSCs. Gelatin zymography of the conditioned media revealed that pro- and active form of MMP-2 was increased in the HSCs cultured on type I collagen gel but not on type I collagen-coated surface, gelatin-coated surface, type IV collagen-coated surface, or Matrigel, suggesting the importance of the native form of type I collagen fibrils in pro-MMP-2 production and activation. The induction of active MMP-2 by extracellular type I collagen was suppressed by the blocking antibody against integrin beta1 subunits, indicating the involvement of integrin signaling in pro-MMP-2 activation. RT-PCR analysis indicated that MMP-2, membrane type-1 MMP (MT1-MMP) and tissue inhib...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628568</comments>
            <pubDate>Mon, 01 Dec 2003 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628568</guid>        </item>
        <item>
            <title>Dominant negative E2F inhibits progression of the cell cycle after the midblastula transition in Xenopus.</title>
            <link>http://www.medworm.com/index.php?rid=1628567&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15004421%26dopt%3DAbstract</link>
            <description>Authors: Tanaka T, Ono T, Kitamura N, Kato JY
    The cleavage cycle, which is initiated by fertilization, consists of only S and M phases, and the gap phases (G1 and G2) appear after the midblastula transition (MBT) in the African clawed frog, Xenopus laevis. During early development in Xenopus, we examined the E2F activity, which controls transition from the G1 to S phase in the somatic cell cycle. Gel retardation and transactivation assays revealed that, although the E2F protein was constantly present throughout early development, the E2F transactivation activity was induced in a stage-specific manner, that is, low before MBT and rapidly increased after MBT. Introduction of the recombinant dominant negative E2F (dnE2F), but not the control, protein into the 2-cell stage embryos specific...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628567</comments>
            <pubDate>Mon, 01 Dec 2003 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628567</guid>        </item>
        <item>
            <title>Rearrangements of actin cytoskeleton during infection with Escherichia coli O157 in macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=1628563&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216878%26dopt%3DAbstract</link>
            <description>We examined the structural rearrangements of the actin cytoskeleton during the microbial infection process. Macrophage actin filaments were rearranged in the following sequence; 1) disappearance of the actin filament bundles in the cytoplasm, 2) accumulation of actin filaments under the cell surface, and 3) construction of actin networks underlying the endosome membrane. Before infection, actin filaments were distributed under the cell surface and in bundles located in the macrophage cytoplasm. Within 2 min, infection caused a rapid and marked loss of the actin filament bundles that had run parallel to the long axis of the cell. Concomitant with the loss, actin filaments became more markedly distributed under the cell surface. In the formation of the endosome, new networks of actin filamen...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628563</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628563</guid>        </item>
        <item>
            <title>Exocytotic secretion of toxins from macrophages infected with Escherichia coli O157.</title>
            <link>http://www.medworm.com/index.php?rid=1628562&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216879%26dopt%3DAbstract</link>
            <description>This study examined whether macrophages are involved in the development of pathogenicity in Shiga-like toxin (SLT)-producing enterohemorrhagic Escherichia coil (EHEC) O157:H7. Macrophages were infected with the bacteria, after which the macrophage culture medium showed a clear increase in toxicity in rats in vivo as well as in rat aortic endothelial cells in vitro. The increased toxicity resulted mainly from a rapid increase in the concentrations of SLT type I (SLT-I) and type II (SLT-II) and partly from an increase in concentrations of the proinflammatory cytokines, tumor necrosis factor alpha (TNFalpha) and interleukin-1 (IL-1), in the culture medium. Most of the EHEC O157 added to the macrophage culture were quickly incorporated to form phagosomes, which then fused with lysosomes to bec...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628562</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628562</guid>        </item>
        <item>
            <title>Regulatory role of extracellular matrix components in expression of matrix metalloproteinases in cultured hepatic stellate cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628561&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216880%26dopt%3DAbstract</link>
            <description>In this study, we have assessed the effects of several types of substrata on the expression of MMPs in HSC culture. MMP-1 expression was detectable in HSC culture on polystyrene surface and on type I collagen gel by immunofluorescence staining and reverse transcriptase-polymerase chain reaction (RT-PCR). The results from in situ zymography revealed the presence of interstitial collagenase activity around HSCs and along their cellular processes. Although proMMP-2 and proMMP-9 were detectable by gelatin zymography in the conditioned medium from both cultures using type I collagen gel and Matrigel as substratum, an active form of MMP-2 but not of MMP-9 was detected only in the culture using type I collagen as a substratum. Tissue inhibitor of metalloproteinase-2 expression was observed by RT-...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628561</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628561</guid>        </item>
        <item>
            <title>Tubulin: 30 years later. Proceedings of the 42nd National Institute for Basic Biology Conference. February 24-26, 1999, Okazaki, Japan.</title>
            <link>http://www.medworm.com/index.php?rid=1628560&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216881%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 15216881 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628560</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628560</guid>        </item>
        <item>
            <title>Crystallographic structure of tubulin: implications for dynamics and drug binding.</title>
            <link>http://www.medworm.com/index.php?rid=1628559&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216882%26dopt%3DAbstract</link>
            <description>Authors: Downing KH, Nogales E
    The structure of tubulin, recently solved by electron crystallography, has given a first look at the molecular basis for some of the properties of tubulin and microtubules that have been observed over the last decades. We discuss how the structure relates to some of these properties, and how inferences about drug binding sites can explain some of the effects of the drugs on tubulin. Microtubules can form a highly dynamic system that requires careful tuning of the stability and properties of tubulin and its interactions with its many ligands. Understanding these interactions can provide fundamental information on the regulation of the microtubule system.
    PMID: 15216882 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628559</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628559</guid>        </item>
        <item>
            <title>3D electron microscopy of the interaction of kinesin with tubulin.</title>
            <link>http://www.medworm.com/index.php?rid=1628558&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216883%26dopt%3DAbstract</link>
            <description>Authors: Hirose K, L&amp;#xF6;we J, Alonso M, Cross RA, Amos LA
    We have studied the structure of microtubules decorated with kinesin motor domains in different nucleotide states by 3D electron microscopy. Having docked the atomic coordinates of both dimeric ADP.kinesin and tubulin heterodimer into a map of kinesin dimers bound to microtubules in the presence of ADP, we try to predict which regions of the proteins interact in the weakly binding state. When either the presence of 5'-adenylyimidodiphosphate (AMP-PNP) or an absence of nucleotides puts motor domains into a strongly-bound state, the 3D maps show changes in the motor domains which modify their interaction with beta-tubulin. The maps also show differences in beta-tubulin conformation compared with undecorated microtubules or those...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628558</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628558</guid>        </item>
        <item>
            <title>The straight and curved conformation of FtsZ protofilaments-evidence for rapid exchange of GTP into the curved protofilament.</title>
            <link>http://www.medworm.com/index.php?rid=1628557&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216884%26dopt%3DAbstract</link>
            <description>Authors: Lu C, Erickson HP
    Bacterial cell division protein FtsZ assembles into protofilaments, which can adopt a straight or curved conformation, similar to its eukaryotic homolog, tubulin. The straight protofilaments can assemble into sheets with a lattice similar to the microtubule wall. The curved protofilaments can form rings when adsorbed to a lipid monolayer, but in solution they form helices. 4 helices assemble together to make a tube, the characteristic polymer of the curved protofilament. GTP favors the straight conformation, while GDP favors the curved. We show here that addition of EDTA and GTP to tubes causes a rapid transformation to straight protofilament sheets. Apparently when the magnesium is chelated the GDP in the curved protofilaments dissociates rapidly and is repl...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628557</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628557</guid>        </item>
        <item>
            <title>Multiple-color fluorescence imaging of chromosomes and microtubules in living cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628556&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216885%26dopt%3DAbstract</link>
            <description>Authors: Haraguchi T, Ding DQ, Yamamoto A, Kaneda T, Koujin T, Hiraoka Y
    Microscopic observation of fluorescently-stained intracellular molecules within a living cell provides a straightforward approach to understanding their temporal and spatial relationships. However, exposure to the excitation light used to visualize these fluorescently-stained molecules can be toxic to the cells. Here we describe several important considerations in microscope instrumentation and experimental conditions for avoiding the toxicity associated with observing living fluorescently-stained cells. Using a computer-controlled fluorescence microscope system designed for live observation, we recorded time-lapse, multi-color images of chromosomes and microtubules in living human and fission yeast cells. In HeLa...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628556</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628556</guid>        </item>
        <item>
            <title>Microtubule's conformational cap.</title>
            <link>http://www.medworm.com/index.php?rid=1628555&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216886%26dopt%3DAbstract</link>
            <description>Authors: Chr&amp;#xE9;tien D, J&amp;#xE1;inosi I, Taveau JC, Flyvbjerg H
    The molecular mechanisms that allow elongation of the unstable microtubule lattice remain unclear. It is usually thought that the GDP-liganded tubulin lattice is capped by a small layer of GTP- or GDP-Pi-liganded molecules, the so called &quot;GTP-cap&quot;. Here, we point-out that the elastic properties of the microtubule lattice cause a difference in stability between the elongating tubulin sheet and the completed microtubule wall. The implications of our observations for microtubule structure and dynamics are discussed.
    PMID: 15216886 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628555</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628555</guid>        </item>
        <item>
            <title>Effects of purinenucleotide analogues on microtubule assembly.</title>
            <link>http://www.medworm.com/index.php?rid=1628554&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216887%26dopt%3DAbstract</link>
            <description>Authors: Muraoka M, Sakai H
    This minireview summarizes the syntheses of various purinenucleotide analogues and their effects on microtubule (Mt) assembly. 27 analogues were so far synthesized and, together with 3 analogues commercially available (ITP, XTP and dGTP), their effects on Microtubule assembly were investigated. The positions C2, C6, C8, and ribose moiety of purine nucleotides were modified or substituted. It was found that the microenvironments of the purine base and ribose moiety are important for the nucleotides to support Mt assembly. Introduction of amino group into position C2 of ATP, formation of 2-amino ATP, caused Mt assembly substantially. 2-Amino deoxy ATP and deoxy GTP are more potent than GTP in supporting assembly. The introduction of reactive thiol group into C...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628554</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628554</guid>        </item>
        <item>
            <title>GFP chimeras of E-MAP-115 (ensconsin) domains mimic behavior of the endogenous protein in vitro and in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=1628553&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216888%26dopt%3DAbstract</link>
            <description>Authors: Bulinski JC, Gruber D, Faire K, Prasad P, Chang W
    E-MAP-115 (ensconsin) is a microtubule-associated protein (MAP) abundant in carcinoma and other epithelia-derived cells. We expressed chimeras of green fluorescent protein (GFP) conjugated to ensconsin's N-terminal MT-binding domain (EMTB), to study distribution, dynamics, and function of the MAP in living cells. We tested the hypothesis that behavior of expressed GFP-EMTB accurately matched behavior of endogenous ensconsin. Like endogenous MAP, GFP-EMTB was associated with microtubules in living or fixed cells, and microtubule association of either molecule was impervious to extraction with nonionic detergents. In cell lysates both GFP-EMTB and endogenous ensconsin were dissociated from microtubules by identical salt extractio...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628553</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628553</guid>        </item>
        <item>
            <title>Serum-dependent phosphorylation of human MAP4 at Ser696 in cultured mammalian cells.</title>
            <link>http://www.medworm.com/index.php?rid=1628552&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216889%26dopt%3DAbstract</link>
            <description>Authors: Srsen V, Kitazawa H, Sugita M, Murofushi H, Bulinski JC, Kishimoto T, Hisanaga S
    In the previous paper (Ookata et al., (1997) Biochemistry, 36: 249-259), we identified two mitotic cdc2 kinase phosphorylation sites (Ser696 and Ser787) in the proline-rich region of human MAP4. One (Ser696) of them was also phosphorylated during interphase. A protein kinase responsible for interphase phosphorylation of Ser696 could necessarily be distinct from cdc2/cyclin B kinase. To get insights into a physiological role for Ser696 phosphorylation, we searched for a Ser696 kinase and for cellular conditions under which Ser696 is dephosphorylated. Because Ser696 conforms to the MAP kinase phosphorylation consensus motif (PXSP), MAP kinase was tested as a possible kinase phosphorylating Ser696. M...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628552</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628552</guid>        </item>
        <item>
            <title>Modulation of microtubule dynamics by drugs: a paradigm for the actions of cellular regulators.</title>
            <link>http://www.medworm.com/index.php?rid=1628551&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216890%26dopt%3DAbstract</link>
            <description>Authors: Wilson L, Panda D, Jordan MA
    Microtubules are intrinsically dynamic polymers. Two kinds of dynamic behaviors, dynamic instability and treadmilling, are important for microtubule function in cells. Both dynamic behaviors appear to be tightly regulated, but the cellular molecules and the mechanisms responsible for the regulation remain largely unexplored. While microtubule dynamics can be modulated transiently by the interaction of regulatory molecules with soluble tubulin, the microtubule itself is likely to be the primary target of cellular molecules that regulate microtubule dynamics. The antimitotic drugs that modulate microtubule dynamics serve as excellent models for such cellular molecules. Our laboratory has been investigating the interactions of small drug molecules and...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628551</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628551</guid>        </item>
        <item>
            <title>Functional analysis of microtubule-binding domain of bovine MAP4.</title>
            <link>http://www.medworm.com/index.php?rid=1628550&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216891%26dopt%3DAbstract</link>
            <description>Authors: Katsuki M, Tokuraku K, Murofushi H, Kotani S
    Bovine microtubule-associated protein 4 (MAP4) consists of an amino-terminal projection domain and a carboxyl-terminal microtubule-binding domain. The carboxyl-terminal domain of MAP4 is further divided into three subdomains: a region rich in proline and basic residues (Pro-rich region), a region containing four repeats of an assembly-promoting (AP) sequence, which consists of 22 amino acid residues (AP sequence region), and a hydrophobic tail region (Tail region). The subdomain structure of MAP4 microtubule binding domain is similar to those of other MAPs (MAP2 and tau). In order to study the function of each subdomain per se of bovine MAP4 microtubule-binding domain, we purified a series of truncated fragments of MAP4, expressed i...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628550</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628550</guid>        </item>
        <item>
            <title>Stathmin and its phosphoprotein family: general properties, biochemical and functional interaction with tubulin.</title>
            <link>http://www.medworm.com/index.php?rid=1628549&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216892%26dopt%3DAbstract</link>
            <description>Authors: Curmi PA, Gavet O, Charbaut E, Ozon S, Lachkar-Colmerauer S, Manceau V, Siavoshian S, Maucuer A, Sobel A
    Stathmin, also referred to as Op18, is a ubiquitous cytosolic phosphoprotein, proposed to be a small regulatory protein and a relay integrating diverse intracellular signaling pathways involved in the control of cell proliferation, differentiation and activities. It interacts with several putative downstream target and/or partner proteins. One major action of stathmin is to interfere with microtubule dynamics, by inhibiting the formation of microtubules and/or favoring their depolymerization. Stathmin (S) interacts directly with soluble tubulin (T), which results in the formation of a T2S complex which sequesters free tubulin and therefore impedes microtubule formation. How...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628549</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628549</guid>        </item>
        <item>
            <title>Inhibition of microtubule assembly by HPC-1/syntaxin 1A, an exocytosis relating protein.</title>
            <link>http://www.medworm.com/index.php?rid=1628548&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216893%26dopt%3DAbstract</link>
            <description>Authors: Itoh TJ, Fujiwara T, Shibuya T, Akagawa K, Hotani H
    HPC-1/syntaxin 1A (HPC-1), which has been identified as a presynaptic membrane protein, is believed to regulate the synaptic exocytosis as a component of t-SNARE. The distribution of the protein, however, is not restricted to the synaptic terminal, but it has been found to locate on the axonal membrane. When the expression of HPC-1 was suppressed, neurite sprouting was enhanced in cultured neurons. These findings suggest that HPC-1 possesses other functions than the regulation of the membrane fusion in neurotransmitter release. Rather it may also participate in the morphogenesis of neurons through membrane fusion, and possibly through cytoskeleton. HPC-1 has a sequence resemble to the assembly promoting sequence of heat stabl...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628548</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628548</guid>        </item>
        <item>
            <title>Gamma-tubulin at ten: progress and prospects.</title>
            <link>http://www.medworm.com/index.php?rid=1628547&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216894%26dopt%3DAbstract</link>
            <description>Authors: Oakley BR, Akkari YN
    The existence of gamma-tubulin was first reported approximately ten years ago, and it is appropriate to review the progress that has been made in gamma-tubulin research and to discuss some of the unanswered questions about gamma-tubulin function. gamma-Tubulin is ubiquitous in eukaryotes and is generally quite conserved. Two highly divergent gamma-tubulins have been discovered, however, one in Saccharomyces cerevisiae and one in Caenorhabditis elegans. Several organisms have two gamma-tubulin genes. In Drosophila melanogaster, the two gamma-tubulins differ significantly in sequence and expression pattern. In other organisms the two gamma-tubulins are almost identical and expression patterns have not been determined. gamma-Tubulin is located at microtubule ...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628547</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628547</guid>        </item>
        <item>
            <title>One-dimensional diffusion on microtubules of particles coated with cytoplasmic dynein and immunoglobulins.</title>
            <link>http://www.medworm.com/index.php?rid=1628546&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216895%26dopt%3DAbstract</link>
            <description>Authors: Wang Z, Sheetz MP
    We characterized and compared the diffusion of beads coated with proteins such as cytoplasmic dynein, alpha-casein, and some immunoglobulins on microtubules. Such weak binding interactions could be common and convenient for concentrating proteins at the surface of cytoplasmic structures such as microtubules. In studying the motile behavior of anionic latex beads coated with limiting dilutions of cytoplasmic dynein, we observed that in addition to active movement, 20-50% of the beads moved back and forth in a random manner. The random movement was inhibited by depletion of ATP or addition of ADP or AMP-PNP. Mean-square-displacement analysis showed that the movement is a one-dimensional diffusion along the microtubule axis with a diffusion coefficient of 2.16 x...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628546</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628546</guid>        </item>
        <item>
            <title>Regulation of microtubule organization during interphase and M phase.</title>
            <link>http://www.medworm.com/index.php?rid=1628545&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216896%26dopt%3DAbstract</link>
            <description>Authors: Shiina N, Tsukita S
    Microtubule (MT) dynamics and organization change markedly during interphase-M phase transition of the cell cycle. This mini review focuses first on p220, a ubiquitous MT-associated protein of Xenopus. p220 is phosphorylated by p34cdc2 kinase and MAP kinase in M phase, and concomitantly loses its MT-binding and MT-stabilizing activities. A cDNA encoding p220 was cloned, which identified p220 as a Xenopus homolog of MAP4, and p220 was therefore termed XMAP4. To examine the physiological relevance of XMAP4 phosphorylation during mitosis, Xenopus A6 cells were transfected with cDNA encoding wild-type or various XMAP4 mutants fused with a green fluorescent protein (GFP). Mutations of serine and threonine within potential phosphorylation sites for p34cdc2 kinase...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628545</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628545</guid>        </item>
        <item>
            <title>Localization of microtubules during macronuclear division in Tetrahymena and possible involvement of macronuclear microtubules in 'amitotic' chromatin distribution.</title>
            <link>http://www.medworm.com/index.php?rid=1628544&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216897%26dopt%3DAbstract</link>
            <description>Authors: Fujiu K, Numata O
    The ciliated protozoa Tetrahymena contains two nuclei, a micronucleus and a macronucleus. In the vegetatively growing cell, the macronucleus divides amitotic while the micronucleus divides by mitosis. It has been indicated that microtubules are involved in macronuclear division and microtubules are observed to exist in the dividing macronucleus. To clarify the localization and the organization of microtubules in the amitotic dividing macronuclei, we used immunofluorescent staining technique. The microtubules were observed in the cytoplasm and macronucleus. The microtubules were organized and dynamically changed their distribution throughout the macronuclear division. We suggest a possibility that these microtubules are involved in 'amitotic' distribution of c...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628544</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628544</guid>        </item>
        <item>
            <title>Biophysical properties of stable microtubules in neurites revealed by optical techniques.</title>
            <link>http://www.medworm.com/index.php?rid=1628543&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216898%26dopt%3DAbstract</link>
            <description>Authors: Kurachi M, Komiya Y, Tashiro T
    We tested the stability of microtubules in the neurites of cultured dorsal root ganglion cells by dissolving the cytoplasmic membrane with detergent and exposing them to defined extracellular medium under the microscope. Smooth cytoplasmic filaments visualized after membrane removal were suggested to be microtubules by the preservation of all of the filaments in the presence but not in the absence of taxol. They were further confirmed to be microtubules by immunostaining with anti-tubulin antibody. Significant number of microtubules in the established neurites remained longer than 1 hour after membrane removal. To investigate their stabilization mechanism, we transected the exposed microtubules by laser microbeam irradiation and observed their le...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628543</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628543</guid>        </item>
        <item>
            <title>Turnover of tubulin in ciliary outer doublet microtubules.</title>
            <link>http://www.medworm.com/index.php?rid=1628542&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216899%26dopt%3DAbstract</link>
            <description>Authors: Stephens RE
    Previous pulse-chase labeling studies have shown that structural proteins incorporate into fully assembled sea urchin embryonic cilia at rates approaching those of full regeneration. When all background ciliogenesis was suppressed by taxol, the turnover of most proteins, including tubulin, continued. The present study utilized chemical dissection to explore the route of tubulin incorporation in the presence of taxol and also in steady-state cilia from prism stage embryos. Surprisingly, in cilia from untreated embryos, the most heavily labeled tubulin was found in the most stable portion of the doublet microtubles, the junctional protofilaments. With taxol, this preferential incorporation was suppressed, although control-level turnover still took place in the remain...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628542</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628542</guid>        </item>
        <item>
            <title>Loosening of a preprophase band of microtubules in onion (Allium cepa L.) root tip cells by kinase inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=1628541&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15216900%26dopt%3DAbstract</link>
            <description>Authors: Nogami A, Mineyuki Y
    Effects of kinase inhibitors on the preprophase band of microtubules in onion (Allium cepa L.) root tip cells were examined. Bundled microtubules in preprophase bands were dispersed on the cell cortex when onion seedlings were incubated with 2.5-5.0 mM 6-dimethylaminopurine. Fifteen min was enough for the bundled microtubules to disappear. Although many preprophase bands remained when the seedlings were incubated with 60 microM staurosporin, these preprophase band microtubules were loosened and the width of the band became broad. These results sugget that some kinases are involved in the microtubule bundling in the preprophase band development.
    PMID: 15216900 [PubMed - indexed for MEDLINE] (Source: Cell Structure and Function)</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628541</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1628541</guid>        </item>
        <item>
            <title>STOP proteins.</title>
            <link>http://www.medworm.com/index.php?rid=1628540&amp;cid=s_37763_171_f&amp;fid=37763&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D15218867%26dopt%3DAbstract</link>
            <description>Authors: Bosc C, Oenarier E, Andrieux A, Job D
    Microtubules assembled from pure tubulin in vitro are labile, rapidly depolymerized upon exposure to the cold. In contrast, in a number of cell types, cytoplasmic microtubules are stable, resistant to prolonged cold exposure. During the past years, the molecular basis of this microtubule stabilization in cells has been elucidated. Cold stability is due to polymer association with different variants of a calmodulin-regulated protein, STOP protein. The dynamic and hence the physiological consequences of STOP association with microtubules vary in different tissues. In neurons, STOP seems almost permanently associated with microtubules. STOP is apparently a major determinant of microtubule turnover in such cells and is required for normal neur...</description>
            <author>Cell Structure and Function</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1628540</comments>
            <pubDate>Fri, 01 Oct 1999 04:00:00 +0100</pubDate>
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