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<pubDate>Sun, 20 Jul 2008 13:45:24 BST</pubDate>


	<title>CiteULike: jyuh Weis</title>
	<description>CiteULike: jyuh Weis</description>


	<link>http://www.citeulike.org/user/jyuh/author/Weis</link>
	<dc:publisher>CiteULike.org</dc:publisher>
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<item rdf:about="http://www.citeulike.org/user/jyuh/article/2784495">
    <title>Advances in collagen cross-link analysis.</title>
    <link>http://www.citeulike.org/user/jyuh/article/2784495</link>
    <description>&lt;i&gt;Methods (San Diego, Calif.), Vol. 45, No. 1. (May 2008), pp. 65-74.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;The combined application of ion-trap mass spectrometry and peptide-specific antibodies for the isolation and structural analysis of collagen cross-linking domains is illustrated with examples of results from various types of collagen with the emphasis on bone and cartilage. We highlight the potential of such methods to advance knowledge on the importance of post-translational modifications (e.g., degrees of lysine hydroxylation and glycosylation) and preferred intermolecular binding partners for telopeptide and helical cross-linking domains in regulating cross-link type and placement.</description>
    <dc:title>Advances in collagen cross-link analysis.</dc:title>

    <dc:creator>DR Eyre</dc:creator>
    <dc:creator>MA Weis</dc:creator>
    <dc:creator>JJ Wu</dc:creator>
    <dc:identifier>doi:10.1016/j.ymeth.2008.01.002</dc:identifier>
    <dc:source>Methods (San Diego, Calif.), Vol. 45, No. 1. (May 2008), pp. 65-74.</dc:source>
    <dc:date>2008-05-11T14:35:19-00:00</dc:date>
    <prism:publicationYear>2008</prism:publicationYear>
    <prism:publicationName>Methods (San Diego, Calif.)</prism:publicationName>
    <prism:issn>1046-2023</prism:issn>
    <prism:volume>45</prism:volume>
    <prism:number>1</prism:number>
    <prism:startingPage>65</prism:startingPage>
    <prism:endingPage>74</prism:endingPage>
    <prism:category>no-tag</prism:category>
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<item rdf:about="http://www.citeulike.org/user/jyuh/article/952383">
    <title>Re-solving the cadherin-catenin-actin conundrum.</title>
    <link>http://www.citeulike.org/user/jyuh/article/952383</link>
    <description>&lt;i&gt;J Biol Chem (27 September 2006)&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Cadherins are an important family of plasma membrane glyco-proteins that regulate Ca++-dependent cell-cell adhesion in vertebrates and invertebrates. It is generally accepted that strong cell-cell adhesion is mediated through cadherin binding to cytoplasmic proteins and the actin cytoskeleton. The cytoplasmic domain of cadherins binds ss-catenin, which in turn binds a-catenin, a protein structurally related to the actin binding protein vinculin. Alpha-catenin binds and bundles actin filaments, and forms binary complexes with a wide range of cytoplasmic proteins that also have in common the capacity to bind actin filaments. These interactions have been taken as evidence of a linkage of cadherins, through ss-catenin and a-catenin to the actin cytoskeleton. A recent study attempted to reconstitute ternary, quaternary and quinternary complexes between cadherins, catenins, actin binding proteins and actin, but failed to identify cadherin complexes that bound actin filaments. Here we seek to reconcile some of the conundrums that have arisen from these studies, speculate on how the cadherin-catenin complex regulates local actin organization, and identify potential areas of future study.</description>
    <dc:title>Re-solving the cadherin-catenin-actin conundrum.</dc:title>

    <dc:creator>William I Weis</dc:creator>
    <dc:creator>W James Nelson</dc:creator>
    <dc:identifier>doi:10.1074/jbc.R600027200</dc:identifier>
    <dc:source>J Biol Chem (27 September 2006)</dc:source>
    <dc:date>2006-11-20T00:43:25-00:00</dc:date>
    <prism:publicationYear>2006</prism:publicationYear>
    <prism:publicationName>J Biol Chem</prism:publicationName>
    <prism:issn>0021-9258</prism:issn>
    <prism:category>no-tag</prism:category>
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