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<pubDate>Sat, 05 Jul 2008 21:38:38 BST</pubDate>


	<title>CiteULike: jyuh's Aihara</title>
	<description>CiteULike: jyuh's Aihara</description>


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<item rdf:about="http://www.citeulike.org/user/jyuh/article/2782600">
    <title>Protein function prediction with high-throughput data.</title>
    <link>http://www.citeulike.org/user/jyuh/article/2782600</link>
    <description>&lt;i&gt;Amino acids (22 April 2008)&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;Protein function prediction is one of the main challenges in post-genomic era. The availability of large amounts of high-throughput data provides an alternative approach to handling this problem from the computational viewpoint. In this review, we provide a comprehensive description of the computational methods that are currently applicable to protein function prediction, especially from the perspective of machine learning. Machine learning techniques can generally be classified as supervised learning, semi-supervised learning and unsupervised learning. By classifying the existing computational methods for protein annotation into these three groups, we are able to present a comprehensive framework on protein annotation based on machine learning techniques. In addition to describing recently developed theoretical methodologies, we also cover representative databases and software tools that are widely utilized in the prediction of protein function.</description>
    <dc:title>Protein function prediction with high-throughput data.</dc:title>

    <dc:creator>Xing-Ming Zhao</dc:creator>
    <dc:creator>Luonan Chen</dc:creator>
    <dc:creator>Kazuyuki Aihara</dc:creator>
    <dc:identifier>doi:10.1007/s00726-008-0077-y</dc:identifier>
    <dc:source>Amino acids (22 April 2008)</dc:source>
    <dc:date>2008-05-10T08:52:29-00:00</dc:date>
    <prism:publicationYear>2008</prism:publicationYear>
    <prism:publicationName>Amino acids</prism:publicationName>
    <prism:issn>1438-2199</prism:issn>
    <prism:category>no-tag</prism:category>
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<item rdf:about="http://www.citeulike.org/user/jyuh/article/2452268">
    <title>Molecular cloning of rat klotho cDNA: markedly decreased expression of klotho by acute inflammatory stress.</title>
    <link>http://www.citeulike.org/user/jyuh/article/2452268</link>
    <description>&lt;i&gt;Biochem Biophys Res Commun, Vol. 251, No. 3. (29 October 1998), pp. 920-925.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;We have recently identified a novel gene, termed klotho, that is involved in the suppression of several aging phenotypes. The gene encodes a membrane protein that shares sequence similarity with the beta-glucosidases of bacteria and plants. In this study, we isolated rat klotho cDNA and examined its tissue distribution in rats. The deduced amino acid sequence of rat Klotho protein was 1014 amino acids in length and 94 and 85% homologous to those of mouse and human Klotho proteins, respectively. Northern blot analysis using the rat klotho cDNA probe identified a single transcript of 5.2 kb in size expressed predominantly in the kidney, while RT-PCR detected low levels of expression also in the brain, lung, intestine, and ovaries. During development, klotho expression in the kidney was markedly augmented after birth. Chromosomal localization of rat klotho was mapped to 12q12. Northern blot analysis showed that expression of klotho was markedly decreased by lipopolysaccharide (LPS) in vivo, suggesting that expression of klotho is affected by acute inflammatory stress. The present study leads to a better understanding of the physiologic and pathophysiologic roles of Klotho.</description>
    <dc:title>Molecular cloning of rat klotho cDNA: markedly decreased expression of klotho by acute inflammatory stress.</dc:title>

    <dc:creator>Y Ohyama</dc:creator>
    <dc:creator>M Kurabayashi</dc:creator>
    <dc:creator>H Masuda</dc:creator>
    <dc:creator>T Nakamura</dc:creator>
    <dc:creator>Y Aihara</dc:creator>
    <dc:creator>T Kaname</dc:creator>
    <dc:creator>T Suga</dc:creator>
    <dc:creator>M Arai</dc:creator>
    <dc:creator>H Aizawa</dc:creator>
    <dc:creator>Y Matsumura</dc:creator>
    <dc:creator>M Kuro-o</dc:creator>
    <dc:creator>Y Nabeshima</dc:creator>
    <dc:creator>R Nagail</dc:creator>
    <dc:source>Biochem Biophys Res Commun, Vol. 251, No. 3. (29 October 1998), pp. 920-925.</dc:source>
    <dc:date>2008-03-01T16:24:38-00:00</dc:date>
    <prism:publicationYear>1998</prism:publicationYear>
    <prism:publicationName>Biochem Biophys Res Commun</prism:publicationName>
    <prism:issn>0006-291X</prism:issn>
    <prism:volume>251</prism:volume>
    <prism:number>3</prism:number>
    <prism:startingPage>920</prism:startingPage>
    <prism:endingPage>925</prism:endingPage>
    <prism:category>no-tag</prism:category>
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