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<pubDate>Thu, 21 Aug 2008 15:14:56 BST</pubDate>


	<title>CiteULike: AlfonsoVicenteSuarez's Smith</title>
	<description>CiteULike: AlfonsoVicenteSuarez's Smith</description>


	<link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/author/Smith</link>
	<dc:publisher>CiteULike.org</dc:publisher>
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	<dc:rights>Copyright &#169; 2004-2008 citeulike.org</dc:rights>
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        <rdf:li rdf:resource="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/2319977"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1379191"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1378963"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1374793"/>
        <rdf:li rdf:resource="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1366434"/>

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<item rdf:about="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/2319977">
    <title>Mesenteric lymph nodes at the center of immune anatomy</title>
    <link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/2319977</link>
    <description>&lt;i&gt;J. Exp. Med., Vol. 203, No. 3. (20 March 2006), pp. 497-500.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;The surface of the intestinal mucosa is constantly assaulted by food antigens and enormous numbers of commensal microbes and their products, which are sampled by dendritic cells (DCs). Recent work shows that the mesenteric lymph nodes (MLNs) are the key site for tolerance induction to food proteins and that they also act as a firewall to prevent live commensal intestinal bacteria from penetrating the systemic immune system. 10.1084/jem.20060227</description>
    <dc:title>Mesenteric lymph nodes at the center of immune anatomy</dc:title>

    <dc:creator>Andrew Macpherson</dc:creator>
    <dc:creator>Karen Smith</dc:creator>
    <dc:identifier>doi:10.1084/jem.20060227</dc:identifier>
    <dc:source>J. Exp. Med., Vol. 203, No. 3. (20 March 2006), pp. 497-500.</dc:source>
    <dc:date>2008-02-01T16:30:17-00:00</dc:date>
    <prism:publicationYear>2006</prism:publicationYear>
    <prism:publicationName>J. Exp. Med.</prism:publicationName>
    <prism:volume>203</prism:volume>
    <prism:number>3</prism:number>
    <prism:startingPage>497</prism:startingPage>
    <prism:endingPage>500</prism:endingPage>
    <prism:category>anatomy-immune</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1379191">
    <title>Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility</title>
    <link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1379191</link>
    <description>&lt;i&gt;Nat Immunol, Vol. 4, No. 12. (December 2003), pp. 1247-1253.&lt;/i&gt;</description>
    <dc:title>Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility</dc:title>

    <dc:creator>Kelly Smith</dc:creator>
    <dc:creator>Erica Andersen-Nissen</dc:creator>
    <dc:creator>Fumitaka Hayashi</dc:creator>
    <dc:creator>Katie Strobe</dc:creator>
    <dc:creator>Molly Bergman</dc:creator>
    <dc:creator>Sara Barrett</dc:creator>
    <dc:creator>Brad Cookson</dc:creator>
    <dc:creator>Alan Aderem</dc:creator>
    <dc:identifier>doi:10.1038/ni1011</dc:identifier>
    <dc:source>Nat Immunol, Vol. 4, No. 12. (December 2003), pp. 1247-1253.</dc:source>
    <dc:date>2007-06-11T19:04:45-00:00</dc:date>
    <prism:publicationYear>2003</prism:publicationYear>
    <prism:publicationName>Nat Immunol</prism:publicationName>
    <prism:volume>4</prism:volume>
    <prism:number>12</prism:number>
    <prism:startingPage>1247</prism:startingPage>
    <prism:endingPage>1253</prism:endingPage>
    <prism:category>tlr5-flagellin</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1378963">
    <title>The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5</title>
    <link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1378963</link>
    <description>&lt;i&gt;Nature, Vol. 410, No. 6832. (26 April 2001), pp. 1099-1103.&lt;/i&gt;</description>
    <dc:title>The innate immune response to bacterial flagellin is mediated by Toll-like receptor 5</dc:title>

    <dc:creator>Fumitaka Hayashi</dc:creator>
    <dc:creator>Kelly Smith</dc:creator>
    <dc:creator>Adrian Ozinsky</dc:creator>
    <dc:creator>Thomas Hawn</dc:creator>
    <dc:creator>Eugene Yi</dc:creator>
    <dc:creator>David Goodlett</dc:creator>
    <dc:creator>Jimmy Eng</dc:creator>
    <dc:creator>Shizuo Akira</dc:creator>
    <dc:creator>David Underhill</dc:creator>
    <dc:creator>Alan Aderem</dc:creator>
    <dc:identifier>doi:10.1038/35074106</dc:identifier>
    <dc:source>Nature, Vol. 410, No. 6832. (26 April 2001), pp. 1099-1103.</dc:source>
    <dc:date>2007-06-11T16:37:08-00:00</dc:date>
    <prism:publicationYear>2001</prism:publicationYear>
    <prism:publicationName>Nature</prism:publicationName>
    <prism:volume>410</prism:volume>
    <prism:number>6832</prism:number>
    <prism:startingPage>1099</prism:startingPage>
    <prism:endingPage>1103</prism:endingPage>
    <prism:category>tlr5-flagellin</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1374793">
    <title>Toll-like receptor-5 and the innate immune response to bacterial flagellin.</title>
    <link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1374793</link>
    <description>&lt;i&gt;Curr Top Microbiol Immunol, Vol. 270 (2002), pp. 93-108.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;The innate immune system identifies the presence of infection by detecting structures that are unique to microbes and that are not expressed in the host. The bacterial flagellum (Latin, a whip) confers motility, on a wide range of bacterial species. Vertebrates, plants, and invertebrates all have evolved flagellar recognition systems that are activated by flagellin, the major component of the bacterial flagellar filament. In mammals, flagellin is recognized by Toll-like receptor-5 and activates defense responses both systemically and at epithelial surfaces. Here, we review the role for Toll-like receptor-5 in mediating the mammalian innate immune response to flagellin, and how this provides for defense against infections caused by many different species of flagellated bacteria.</description>
    <dc:title>Toll-like receptor-5 and the innate immune response to bacterial flagellin.</dc:title>

    <dc:creator>KD Smith</dc:creator>
    <dc:creator>A Ozinsky</dc:creator>
    <dc:source>Curr Top Microbiol Immunol, Vol. 270 (2002), pp. 93-108.</dc:source>
    <dc:date>2007-06-09T23:06:04-00:00</dc:date>
    <prism:publicationYear>2002</prism:publicationYear>
    <prism:publicationName>Curr Top Microbiol Immunol</prism:publicationName>
    <prism:issn>0070-217X</prism:issn>
    <prism:volume>270</prism:volume>
    <prism:startingPage>93</prism:startingPage>
    <prism:endingPage>108</prism:endingPage>
    <prism:category>tlr5-flagellin</prism:category>
</item>



<item rdf:about="http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1366434">
    <title>Molecular interpretation of ERK signal duration by immediate early gene products.</title>
    <link>http://www.citeulike.org/user/AlfonsoVicenteSuarez/article/1366434</link>
    <description>&lt;i&gt;Nat Cell Biol, Vol. 4, No. 8. (August 2002), pp. 556-564.&lt;/i&gt;&lt;br /&gt;&lt;br /&gt;The duration of intracellular signalling is associated with distinct biological responses, but how cells interpret differences in signal duration are unknown. We show that the immediate early gene product c-Fos functions as a sensor for ERK1 (extracellular-signal-regulated kinase 1) and ERK2 signal duration. When ERK activation is transient, its activity declines before the c-Fos protein accumulates, and under these conditions c-Fos is unstable. However, when ERK signalling is sustained, c-Fos is phosphorylated by still-active ERK and RSK (90K-ribosomal S6 kinase). Carboxy-terminal phosphorylation stabilizes c-Fos and primes additional phosphorylation by exposing a docking site for ERK, termed the FXFP (DEF) domain. Mutating the DEF domain disrupts the c-Fos sensor and c-Fos-mediated signalling. Other immediate early gene products that control cell cycle progression, neuronal differentiation and circadium rhythms also contain putative DEF domains, indicating that multiple sensors exist for sustained ERK signalling. Together, our data identify a general mechanism by which cells can interpret differences in ERK activation kinetics.</description>
    <dc:title>Molecular interpretation of ERK signal duration by immediate early gene products.</dc:title>

    <dc:creator>LO Murphy</dc:creator>
    <dc:creator>S Smith</dc:creator>
    <dc:creator>RH Chen</dc:creator>
    <dc:creator>DC Fingar</dc:creator>
    <dc:creator>J Blenis</dc:creator>
    <dc:identifier>doi:10.1038/ncb822</dc:identifier>
    <dc:source>Nat Cell Biol, Vol. 4, No. 8. (August 2002), pp. 556-564.</dc:source>
    <dc:date>2007-06-05T22:04:41-00:00</dc:date>
    <prism:publicationYear>2002</prism:publicationYear>
    <prism:publicationName>Nat Cell Biol</prism:publicationName>
    <prism:issn>1465-7392</prism:issn>
    <prism:volume>4</prism:volume>
    <prism:number>8</prism:number>
    <prism:startingPage>556</prism:startingPage>
    <prism:endingPage>564</prism:endingPage>
    <prism:category>erk-il-10</prism:category>
</item>



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