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<title>Biotech bailout?</title>
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<description>A rescue of some sort will be needed to save a large subset of the US biotechnology industry.</description>
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<p>
<b>Biotech bailout?</b>
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<p>Nature Immunology 10, 667 (2009). <a href="http://dx.doi.org/10.1038/ni0709-667">doi:10.1038/ni0709-667</a>
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<p>A rescue of some sort will be needed to save a large subset of the US biotechnology industry.</p>
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<b>NKT cells turn ten</b>
</p>
<p>Nature Immunology 10, 669 (2009). <a href="http://dx.doi.org/10.1038/ni0709-669">doi:10.1038/ni0709-669</a>
</p>
<p>Authors: Peter D Burrows, Mitchell Kronenberg &amp; Masaru Taniguchi</p>
<p>It has been 10 years since the first workshop on natural killer T cells helped to launch a growth phase for this field of research.</p>
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<dc:title>NKT cells turn ten</dc:title>
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<description>The US National Institute of Allergy and Infectious Diseases convened a workshop of malaria investigators and immunologists to foster collaborations and attract more immunologists into malaria research. Discussions highlighted research gaps and underscored the incomplete understanding of basic immune mechanisms that contribute to the pathogenesis of or protection against malaria.</description>
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<p>
<b>NIAID workshop on immunity to malaria: addressing immunological challenges</b>
</p>
<p>Nature Immunology 10, 673 (2009). <a href="http://dx.doi.org/10.1038/ni0709-673">doi:10.1038/ni0709-673</a>
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<p>Authors: Alison Deckhut Augustine, B Fenton Hall, Wolfgang W Leitner, Annie X Mo, Tonu M Wali &amp; Anthony S Fauci</p>
<p>The US National Institute of Allergy and Infectious Diseases convened a workshop of malaria investigators and immunologists to foster collaborations and attract more immunologists into malaria research. Discussions highlighted research gaps and underscored the incomplete understanding of basic immune mechanisms that contribute to the pathogenesis of or protection against malaria.</p>
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<dc:title>NIAID workshop on immunity to malaria: addressing immunological challenges</dc:title>
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<dc:creator>B Fenton Hall</dc:creator>
<dc:creator>Wolfgang W Leitner</dc:creator>
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<dc:source>Nature Immunology 10, 673 (2009)</dc:source>
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<description>Dendritic cells are best known as antigen-presenting cells that initiate adaptive immune responses. Three new papers suggest that basophils initiate allergen- and helminth-driven CD4+ T helper type 2 responses by functioning as antigen-presenting cells in draining lymph nodes.</description>
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<p>
<b>Basophils trump dendritic cells as APCs for TH2 responses</b>
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<p>Nature Immunology 10, 679 (2009). <a href="http://dx.doi.org/10.1038/ni0709-679">doi:10.1038/ni0709-679</a>
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<p>Author: Thomas A Wynn</p>
<p>Dendritic cells are best known as antigen-presenting cells that initiate adaptive immune responses. Three new papers suggest that basophils initiate allergen- and helminth-driven CD4+ T helper type 2 responses by functioning as antigen-presenting cells in draining lymph nodes.</p>
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<dc:title>Basophils trump dendritic cells as APCs for TH2 responses</dc:title>
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<p>
<b>CSF-1R, DAP12 and &#946;-catenin: a m&#233;nage &#224; trois</b>
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<p>Nature Immunology 10, 681 (2009). <a href="http://dx.doi.org/10.1038/ni0709-681">doi:10.1038/ni0709-681</a>
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<p>Authors: Daniel W McVicar &amp; Giorgio Trinchieri</p>
<p>DAP12-coupled receptors influence signals emanating from Toll-like receptors, integrins and receptors for cytokines and growth factors. New findings indicate that DAP12 also facilitates the ability of CSF-1R, the receptor for M-CSF, to induce the stabilization and nuclear translocation of &#946;-catenin.</p>
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<description>Deficiency in acid sphingomyelinase causes lysosomal storage of sphingomyelin, mediates resistance to stress-induced apoptosis and alters susceptibility to certain infections. New work links acid sphingomyelinase to the granule exocytosis of cytotoxic T cells.</description>
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<p>
<b>ASMase: the tailor of cytotoxic T cell granule exocytosis</b>
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<p>Nature Immunology 10, 683 (2009). <a href="http://dx.doi.org/10.1038/ni0709-683">doi:10.1038/ni0709-683</a>
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<p>Author: Christian Bogdan</p>
<p>Deficiency in acid sphingomyelinase causes lysosomal storage of sphingomyelin, mediates resistance to stress-induced apoptosis and alters susceptibility to certain infections. New work links acid sphingomyelinase to the granule exocytosis of cytotoxic T cells.</p>
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<dc:title>ASMase: the tailor of cytotoxic T cell granule exocytosis</dc:title>
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<title>A novel modifier of regulatory T cells</title>
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<description>The receptor for the lipid mediator sphingosine 1-phosphate is critical for T cell trafficking. New data show that signaling mediated by this receptor critically controls the development, maintenance and suppressive activity of natural regulatory T cells that express the transcription factor Foxp3.</description>
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<p>
<b>A novel modifier of regulatory T cells</b>
</p>
<p>Nature Immunology 10, 685 (2009). <a href="http://dx.doi.org/10.1038/ni0709-685">doi:10.1038/ni0709-685</a>
</p>
<p>Authors: Naganari Ohkura &amp; Shimon Sakaguchi</p>
<p>The receptor for the lipid mediator sphingosine 1-phosphate is critical for T cell trafficking. New data show that signaling mediated by this receptor critically controls the development, maintenance and suppressive activity of natural regulatory T cells that express the transcription factor Foxp3.</p>
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<dc:title>A novel modifier of regulatory T cells</dc:title>
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<p>
<b>Research Highlights</b>
</p>
<p>Nature Immunology 10, 687 (2009). <a href="http://dx.doi.org/10.1038/ni0709-687">doi:10.1038/ni0709-687</a>
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<dc:title>Research Highlights</dc:title>
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<title>Foxp3+ regulatory T cells: differentiation, specification, subphenotypes</title>
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<description/>
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<p>
<b>Foxp3+ regulatory T cells: differentiation, specification, subphenotypes</b>
</p>
<p>Nature Immunology 10, 689 (2009). <a href="http://dx.doi.org/10.1038/ni.1760">doi:10.1038/ni.1760</a>
</p>
<p>Authors: Markus Feuerer, Jonathan A Hill, Diane Mathis &amp; Christophe Benoist</p>
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<dc:title>Foxp3+ regulatory T cells: differentiation, specification, subphenotypes</dc:title>
<dc:creator>Markus Feuerer</dc:creator>
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<dc:creator>Christophe Benoist</dc:creator>
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<dc:source>Nature Immunology 10, 689 (2009)</dc:source>
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<title>MHC class II&#8211;dependent basophil&#8211;CD4+ T cell interactions promote TH2 cytokine&#8211;dependent immunity</title>
<link>http://dx.doi.org/10.1038/ni.1740</link>
<description>Basophils act as effector cells in immunoglobulin E&#8211;mediated hypersensitivity responses. Artis, Nakanishi and Medzhitov and their colleagues report that basophils present antigen and induce T helper type 2 responses to helminths, allergens and immunoglobulin E immune complexes.</description>
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<p>
<b>MHC class II&#8211;dependent basophil&#8211;CD4+ T cell interactions promote TH2 cytokine&#8211;dependent immunity</b>
</p>
<p>Nature Immunology 10, 697 (2009). <a href="http://dx.doi.org/10.1038/ni.1740">doi:10.1038/ni.1740</a>
</p>
<p>Authors: Jacqueline G Perrigoue, Steven A Saenz, Mark C Siracusa, Eric J Allenspach, Betsy C Taylor, Paul R Giacomin, Meera G Nair, Yurong Du, Colby Zaph, Nico van Rooijen, Michael R Comeau, Edward J Pearce, Terri M Laufer &amp; David Artis</p>
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<dc:title>MHC class II&#8211;dependent basophil&#8211;CD4+ T cell interactions promote TH2 cytokine&#8211;dependent immunity</dc:title>
<dc:creator>Jacqueline G Perrigoue</dc:creator>
<dc:creator>Steven A Saenz</dc:creator>
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<dc:creator>Paul R Giacomin</dc:creator>
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<dc:creator>Michael R Comeau</dc:creator>
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<dc:creator>David Artis</dc:creator>
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<dc:source>Nature Immunology 10, 697 (2009)</dc:source>
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<title>Basophils contribute to TH2-IgE responses in vivo via IL-4 production and presentation of peptide&#8211;MHC class II complexes to CD4+ T cells</title>
<link>http://dx.doi.org/10.1038/ni.1737</link>
<description>Basophils act as effector cells in immunoglobulin E&#8211;mediated hypersensitivity responses. Artis, Nakanishi and Medzhitov and their colleagues report that basophils present antigen and induce T helper type 2 responses to helminths, allergens and immunoglobulin E immune complexes.</description>
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<p>
<b>Basophils contribute to TH2-IgE responses in vivo via IL-4 production and presentation of peptide&#8211;MHC class II complexes to CD4+ T cells</b>
</p>
<p>Nature Immunology 10, 706 (2009). <a href="http://dx.doi.org/10.1038/ni.1737">doi:10.1038/ni.1737</a>
</p>
<p>Authors: Tomohiro Yoshimoto, Koubun Yasuda, Hidehisa Tanaka, Masakiyo Nakahira, Yasutomo Imai, Yoshihiro Fujimori &amp; Kenji Nakanishi</p>
]]></content:encoded>
<dc:title>Basophils contribute to TH2-IgE responses in vivo via IL-4 production and presentation of peptide&#8211;MHC class II complexes to CD4+ T cells</dc:title>
<dc:creator>Tomohiro Yoshimoto</dc:creator>
<dc:creator>Koubun Yasuda</dc:creator>
<dc:creator>Hidehisa Tanaka</dc:creator>
<dc:creator>Masakiyo Nakahira</dc:creator>
<dc:creator>Yasutomo Imai</dc:creator>
<dc:creator>Yoshihiro Fujimori</dc:creator>
<dc:creator>Kenji Nakanishi</dc:creator>
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<dc:source>Nature Immunology 10, 706 (2009)</dc:source>
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<title>Basophils function as antigen-presenting cells for an allergen-induced T helper type 2 response</title>
<link>http://dx.doi.org/10.1038/ni.1738</link>
<description>Basophils act as effector cells in immunoglobulin E&#8211;mediated hypersensitivity responses. Artis, Nakanishi and Medzhitov and their colleagues report that basophils present antigen and induce T helper type 2 responses to helminths, allergens and immunoglobulin E immune complexes.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Basophils function as antigen-presenting cells for an allergen-induced T helper type 2 response</b>
</p>
<p>Nature Immunology 10, 713 (2009). <a href="http://dx.doi.org/10.1038/ni.1738">doi:10.1038/ni.1738</a>
</p>
<p>Authors: Caroline L Sokol, Ngoc-Quynh Chu, Shuang Yu, Simone A Nish, Terri M Laufer &amp; Ruslan Medzhitov</p>
]]></content:encoded>
<dc:title>Basophils function as antigen-presenting cells for an allergen-induced T helper type 2 response</dc:title>
<dc:creator>Caroline L Sokol</dc:creator>
<dc:creator>Ngoc-Quynh Chu</dc:creator>
<dc:creator>Shuang Yu</dc:creator>
<dc:creator>Simone A Nish</dc:creator>
<dc:creator>Terri M Laufer</dc:creator>
<dc:creator>Ruslan Medzhitov</dc:creator>
<dc:identifier>doi:10.1038/ni.1738</dc:identifier>
<dc:source>Nature Immunology 10, 713 (2009)</dc:source>
<dc:date>2009-05-24</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-05-24</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
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<prism:endingPage>720</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1756">
<title>Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor</title>
<link>http://dx.doi.org/10.1038/ni.1756</link>
<description>Complement forms an ancient innate immune defense. Gros and colleagues provide new insight into the interactions between complement convertase C3b and its regulator factor H and with the staphylococcal inhibitor SCIN.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor</b>
</p>
<p>Nature Immunology 10, 721 (2009). <a href="http://dx.doi.org/10.1038/ni.1756">doi:10.1038/ni.1756</a>
</p>
<p>Authors: Suzan H M Rooijakkers, Jin Wu, Maartje Ruyken, Robert  van Domselaar, Karel L Planken, Apostolia Tzekou, Daniel Ricklin, John D Lambris, Bert J C Janssen, Jos A G van Strijp &amp; Piet Gros</p>
]]></content:encoded>
<dc:title>Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor</dc:title>
<dc:creator>Suzan H M Rooijakkers</dc:creator>
<dc:creator>Jin Wu</dc:creator>
<dc:creator>Maartje Ruyken</dc:creator>
<dc:creator>Robert  van Domselaar</dc:creator>
<dc:creator>Karel L Planken</dc:creator>
<dc:creator>Apostolia Tzekou</dc:creator>
<dc:creator>Daniel Ricklin</dc:creator>
<dc:creator>John D Lambris</dc:creator>
<dc:creator>Bert J C Janssen</dc:creator>
<dc:creator>Jos A G van Strijp</dc:creator>
<dc:creator>Piet Gros</dc:creator>
<dc:identifier>doi:10.1038/ni.1756</dc:identifier>
<dc:source>Nature Immunology 10, 721 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
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<prism:endingPage>727</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/ni.1755">
<title>Structure of complement fragment C3b&#8211;factor H and implications for host protection by complement regulators</title>
<link>http://dx.doi.org/10.1038/ni.1755</link>
<description>Complement forms an ancient innate immune defense. Gros and colleagues provide new insight into the interactions between complement convertase C3b and its regulator factor H and with the staphylococcal inhibitor SCIN.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Structure of complement fragment C3b&#8211;factor H and implications for host protection by complement regulators</b>
</p>
<p>Nature Immunology 10, 728 (2009). <a href="http://dx.doi.org/10.1038/ni.1755">doi:10.1038/ni.1755</a>
</p>
<p>Authors: Jin Wu, You-Qiang Wu, Daniel Ricklin, Bert J C Janssen, John D Lambris &amp; Piet Gros</p>
]]></content:encoded>
<dc:title>Structure of complement fragment C3b&#8211;factor H and implications for host protection by complement regulators</dc:title>
<dc:creator>Jin Wu</dc:creator>
<dc:creator>You-Qiang Wu</dc:creator>
<dc:creator>Daniel Ricklin</dc:creator>
<dc:creator>Bert J C Janssen</dc:creator>
<dc:creator>John D Lambris</dc:creator>
<dc:creator>Piet Gros</dc:creator>
<dc:identifier>doi:10.1038/ni.1755</dc:identifier>
<dc:source>Nature Immunology 10, 728 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>728</prism:startingPage>
<prism:endingPage>733</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/ni.1744">
<title>Macrophage colony-stimulating factor induces the proliferation and survival of macrophages via a pathway involving DAP12 and &#946;-catenin</title>
<link>http://dx.doi.org/10.1038/ni.1744</link>
<description>Macrophage colony-stimulating factor (M-CSF) induces the proliferation of mononuclear phagocytes, and DAP12 is needed for their function. Colonna and colleagues show that DAP12 is also needed for M-CSF-induced stabilization of &#946;-catenin.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Macrophage colony-stimulating factor induces the proliferation and survival of macrophages via a pathway involving DAP12 and &#946;-catenin</b>
</p>
<p>Nature Immunology 10, 734 (2009). <a href="http://dx.doi.org/10.1038/ni.1744">doi:10.1038/ni.1744</a>
</p>
<p>Authors: Karel Otero, Isaiah R Turnbull, Pietro Luigi Poliani, William Vermi, Elisa Cerutti, Taiki Aoshi, Ilaria Tassi, Toshiyuki Takai, Samuel L Stanley, Mark Miller, Andrey S Shaw &amp; Marco Colonna</p>
]]></content:encoded>
<dc:title>Macrophage colony-stimulating factor induces the proliferation and survival of macrophages via a pathway involving DAP12 and &#946;-catenin</dc:title>
<dc:creator>Karel Otero</dc:creator>
<dc:creator>Isaiah R Turnbull</dc:creator>
<dc:creator>Pietro Luigi Poliani</dc:creator>
<dc:creator>William Vermi</dc:creator>
<dc:creator>Elisa Cerutti</dc:creator>
<dc:creator>Taiki Aoshi</dc:creator>
<dc:creator>Ilaria Tassi</dc:creator>
<dc:creator>Toshiyuki Takai</dc:creator>
<dc:creator>Samuel L Stanley</dc:creator>
<dc:creator>Mark Miller</dc:creator>
<dc:creator>Andrey S Shaw</dc:creator>
<dc:creator>Marco Colonna</dc:creator>
<dc:identifier>doi:10.1038/ni.1744</dc:identifier>
<dc:source>Nature Immunology 10, 734 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>734</prism:startingPage>
<prism:endingPage>743</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1742">
<title>The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon</title>
<link>http://dx.doi.org/10.1038/ni.1742</link>
<description>E3 ubiquitin ligases are critical for innate and adaptive immunity. Cao and colleagues show that the E3 ubiquitin ligase Nrdp inhibits the production of proinflammatory cytokines while promoting the release of interferon-&#946; in Toll-like receptor&#8211;triggered macrophages.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon</b>
</p>
<p>Nature Immunology 10, 744 (2009). <a href="http://dx.doi.org/10.1038/ni.1742">doi:10.1038/ni.1742</a>
</p>
<p>Authors: Chen Wang, Taoyong Chen, Jia Zhang, Mingjin Yang, Nan Li, Xiongfei Xu &amp; Xuetao Cao</p>
]]></content:encoded>
<dc:title>The E3 ubiquitin ligase Nrdp1 'preferentially' promotes TLR-mediated production of type I interferon</dc:title>
<dc:creator>Chen Wang</dc:creator>
<dc:creator>Taoyong Chen</dc:creator>
<dc:creator>Jia Zhang</dc:creator>
<dc:creator>Mingjin Yang</dc:creator>
<dc:creator>Nan Li</dc:creator>
<dc:creator>Xiongfei Xu</dc:creator>
<dc:creator>Xuetao Cao</dc:creator>
<dc:identifier>doi:10.1038/ni.1742</dc:identifier>
<dc:source>Nature Immunology 10, 744 (2009)</dc:source>
<dc:date>2009-05-31</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-05-31</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>744</prism:startingPage>
<prism:endingPage>752</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1750">
<title>Immunological synapse formation inhibits, via NF-&#954;B and FOXO1, the apoptosis of dendritic cells</title>
<link>http://dx.doi.org/10.1038/ni.1750</link>
<description>Immunological synapses (IS) involving surface receptors form between dendritic cells (DC) and T cells.  Rodriguez-Fernandez and colleagues show that IS-induced signals activate Akt and NF-&#954;B and suppress Foxo1 to promote DC survival.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Immunological synapse formation inhibits, via NF-&#954;B and FOXO1, the apoptosis of dendritic cells</b>
</p>
<p>Nature Immunology 10, 753 (2009). <a href="http://dx.doi.org/10.1038/ni.1750">doi:10.1038/ni.1750</a>
</p>
<p>Authors: Lorena Riol-Blanco, Cristina Delgado-Mart&#237;n, Noelia S&#225;nchez-S&#225;nchez, Luis M Alonso-C, Mar&#237;a Dolores Guti&#233;rrez-L&#243;pez, Gloria Mart&#237;nez del Hoyo, Joaqu&#237;n Navarro, Francisco S&#225;nchez-Madrid, Carlos Caba&#241;as, Paloma S&#225;nchez-Mateos &amp; Jos&#233; Luis Rodr&#237;guez-Fern&#225;ndez</p>
]]></content:encoded>
<dc:title>Immunological synapse formation inhibits, via NF-&#954;B and FOXO1, the apoptosis of dendritic cells</dc:title>
<dc:creator>Lorena Riol-Blanco</dc:creator>
<dc:creator>Cristina Delgado-Mart&#237;n</dc:creator>
<dc:creator>Noelia S&#225;nchez-S&#225;nchez</dc:creator>
<dc:creator>Luis M Alonso-C</dc:creator>
<dc:creator>Mar&#237;a Dolores Guti&#233;rrez-L&#243;pez</dc:creator>
<dc:creator>Gloria Mart&#237;nez del Hoyo</dc:creator>
<dc:creator>Joaqu&#237;n Navarro</dc:creator>
<dc:creator>Francisco S&#225;nchez-Madrid</dc:creator>
<dc:creator>Carlos Caba&#241;as</dc:creator>
<dc:creator>Paloma S&#225;nchez-Mateos</dc:creator>
<dc:creator>Jos&#233; Luis Rodr&#237;guez-Fern&#225;ndez</dc:creator>
<dc:identifier>doi:10.1038/ni.1750</dc:identifier>
<dc:source>Nature Immunology 10, 753 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>753</prism:startingPage>
<prism:endingPage>760</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1757">
<title>Acid sphingomyelinase is a key regulator of cytotoxic granule secretion by primary T lymphocytes</title>
<link>http://dx.doi.org/10.1038/ni.1757</link>
<description>Granules containing perforin and granzymes are secreted from cytotoxic T lymphocytes. Kr&#246;nke and co-workers find that acid sphingomyelase is needed for granule shrinkage just before exocytosis in this process.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Acid sphingomyelinase is a key regulator of cytotoxic granule secretion by primary T lymphocytes</b>
</p>
<p>Nature Immunology 10, 761 (2009). <a href="http://dx.doi.org/10.1038/ni.1757">doi:10.1038/ni.1757</a>
</p>
<p>Authors: Jasmin Herz, Julian Pardo, Hamid Kashkar, Michael Schramm, Elza Kuzmenkina, Erik Bos, Katja Wiegmann, Reinhard Wallich, Peter J Peters, Stefan Herzig, Elmon Schmelzer, Martin Kr&#246;nke, Markus M Simon &amp; Olaf Uterm&#246;hlen</p>
]]></content:encoded>
<dc:title>Acid sphingomyelinase is a key regulator of cytotoxic granule secretion by primary T lymphocytes</dc:title>
<dc:creator>Jasmin Herz</dc:creator>
<dc:creator>Julian Pardo</dc:creator>
<dc:creator>Hamid Kashkar</dc:creator>
<dc:creator>Michael Schramm</dc:creator>
<dc:creator>Elza Kuzmenkina</dc:creator>
<dc:creator>Erik Bos</dc:creator>
<dc:creator>Katja Wiegmann</dc:creator>
<dc:creator>Reinhard Wallich</dc:creator>
<dc:creator>Peter J Peters</dc:creator>
<dc:creator>Stefan Herzig</dc:creator>
<dc:creator>Elmon Schmelzer</dc:creator>
<dc:creator>Martin Kr&#246;nke</dc:creator>
<dc:creator>Markus M Simon</dc:creator>
<dc:creator>Olaf Uterm&#246;hlen</dc:creator>
<dc:identifier>doi:10.1038/ni.1757</dc:identifier>
<dc:source>Nature Immunology 10, 761 (2009)</dc:source>
<dc:date>2009-06-14</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-14</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>761</prism:startingPage>
<prism:endingPage>768</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1743">
<title>The receptor S1P1 overrides regulatory T cell&#8211;mediated immune suppression through Akt-mTOR</title>
<link>http://dx.doi.org/10.1038/ni.1743</link>
<description>Regulatory T cells (Treg cells) are necessary for maintaining peripheral tolerance. Chi and colleagues show that the receptor S1P1 negatively regulates thymic Treg cell production and blocks Treg  cell activity via an Akt-mTor pathway.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>The receptor S1P1 overrides regulatory T cell&#8211;mediated immune suppression through Akt-mTOR</b>
</p>
<p>Nature Immunology 10, 769 (2009). <a href="http://dx.doi.org/10.1038/ni.1743">doi:10.1038/ni.1743</a>
</p>
<p>Authors: Guangwei Liu, Samir Burns, Gonghua Huang, Kelli Boyd, Richard L Proia, Richard A Flavell &amp; Hongbo Chi</p>
]]></content:encoded>
<dc:title>The receptor S1P1 overrides regulatory T cell&#8211;mediated immune suppression through Akt-mTOR</dc:title>
<dc:creator>Guangwei Liu</dc:creator>
<dc:creator>Samir Burns</dc:creator>
<dc:creator>Gonghua Huang</dc:creator>
<dc:creator>Kelli Boyd</dc:creator>
<dc:creator>Richard L Proia</dc:creator>
<dc:creator>Richard A Flavell</dc:creator>
<dc:creator>Hongbo Chi</dc:creator>
<dc:identifier>doi:10.1038/ni.1743</dc:identifier>
<dc:source>Nature Immunology 10, 769 (2009)</dc:source>
<dc:date>2009-05-31</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-05-31</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>769</prism:startingPage>
<prism:endingPage>777</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1741">
<title>Interleukin 17 acts in synergy with B cell&#8211;activating factor to influence B cell biology and the pathophysiology of systemic lupus erythematosus</title>
<link>http://dx.doi.org/10.1038/ni.1741</link>
<description>How interleukin 17 influences B cell biology is unclear. Bonnefoy-B&#233;rard and colleagues find that interleukin 17 alone or in combination with B cell&#8211;activating factor controls the survival, proliferation of human B cells and their differentiation into immunoglobulin-secreting cells.</description>
<content:encoded><![CDATA[
<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Interleukin 17 acts in synergy with B cell&#8211;activating factor to influence B cell biology and the pathophysiology of systemic lupus erythematosus</b>
</p>
<p>Nature Immunology 10, 778 (2009). <a href="http://dx.doi.org/10.1038/ni.1741">doi:10.1038/ni.1741</a>
</p>
<p>Authors: Agn&#232;s Doreau, Alexandre Belot, J&#233;r&#233;my Bastid, Benjamin Riche, Marie-Claude Trescol-Biemont, Bruno Ranchin, Nicole Fabien, Pierre Cochat, Claire Pouteil-Noble, Pierre Trolliet, Isabelle Durieu, Jacques Tebib, Berhouz Kassai, St&#233;phane Ansieau, Alain Puisieux, Jean-Fran&#231;ois Eliaou &amp; Nathalie Bonnefoy-B&#233;rard</p>
]]></content:encoded>
<dc:title>Interleukin 17 acts in synergy with B cell&#8211;activating factor to influence B cell biology and the pathophysiology of systemic lupus erythematosus</dc:title>
<dc:creator>Agn&#232;s Doreau</dc:creator>
<dc:creator>Alexandre Belot</dc:creator>
<dc:creator>J&#233;r&#233;my Bastid</dc:creator>
<dc:creator>Benjamin Riche</dc:creator>
<dc:creator>Marie-Claude Trescol-Biemont</dc:creator>
<dc:creator>Bruno Ranchin</dc:creator>
<dc:creator>Nicole Fabien</dc:creator>
<dc:creator>Pierre Cochat</dc:creator>
<dc:creator>Claire Pouteil-Noble</dc:creator>
<dc:creator>Pierre Trolliet</dc:creator>
<dc:creator>Isabelle Durieu</dc:creator>
<dc:creator>Jacques Tebib</dc:creator>
<dc:creator>Berhouz Kassai</dc:creator>
<dc:creator>St&#233;phane Ansieau</dc:creator>
<dc:creator>Alain Puisieux</dc:creator>
<dc:creator>Jean-Fran&#231;ois Eliaou</dc:creator>
<dc:creator>Nathalie Bonnefoy-B&#233;rard</dc:creator>
<dc:identifier>doi:10.1038/ni.1741</dc:identifier>
<dc:source>Nature Immunology 10, 778 (2009)</dc:source>
<dc:date>2009-05-31</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-05-31</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>778</prism:startingPage>
<prism:endingPage>785</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/ni.1745">
<title>Immune complex relay by subcapsular sinus macrophages and noncognate B cells drives antibody affinity maturation</title>
<link>http://dx.doi.org/10.1038/ni.1745</link>
<description>Immune complexes are captured from lymph by subcapsular macrophages. Cyster and colleagues show that an intricate relay shuttles antigen into germinal centers to drive affinity maturation.</description>
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<div><a href="http://ad.doubleclick.net/adj/ni.nature.com/rss;sz=728x90"><img src="http://ad.doubleclick.net/ad/ni.nature.com/rss;sz=728x90" alt="Advertisement" style="border:0" /></a></div>
<p>
<b>Immune complex relay by subcapsular sinus macrophages and noncognate B cells drives antibody affinity maturation</b>
</p>
<p>Nature Immunology 10, 786 (2009). <a href="http://dx.doi.org/10.1038/ni.1745">doi:10.1038/ni.1745</a>
</p>
<p>Authors: Tri Giang Phan, Jesse A Green, Elizabeth E Gray, Ying Xu &amp; Jason G Cyster</p>
]]></content:encoded>
<dc:title>Immune complex relay by subcapsular sinus macrophages and noncognate B cells drives antibody affinity maturation</dc:title>
<dc:creator>Tri Giang Phan</dc:creator>
<dc:creator>Jesse A Green</dc:creator>
<dc:creator>Elizabeth E Gray</dc:creator>
<dc:creator>Ying Xu</dc:creator>
<dc:creator>Jason G Cyster</dc:creator>
<dc:identifier>doi:10.1038/ni.1745</dc:identifier>
<dc:source>Nature Immunology 10, 786 (2009)</dc:source>
<dc:date>2009-06-07</dc:date>
<prism:publicationName>Nature Immunology</prism:publicationName>
<prism:publicationDate>2009-06-07</prism:publicationDate>
<prism:volume>10</prism:volume>
<prism:number>7</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>786</prism:startingPage>
<prism:endingPage>793</prism:endingPage>
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