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<dc:rights>© 2012 Nature Publishing Group</dc:rights>
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                     <title>Enlightening the impact of immunogenic cell death in photodynamic cancer therapy</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/LPc52Xra7Ug/emboj.2012.2</link>
<description>Enlightening the impact of immunogenic cell death in photodynamic cancer therapyThis feature highlights novel molecular pathways underlying the cell surface presentation of calreticulin and ATP secretion, critical damage-associated molecular patterns (DAMPs) that trigger immunogenic cell death.</description>
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<p>
<b>Enlightening the impact of immunogenic cell death in photodynamic cancer therapy</b>
</p>
<p>The EMBO Journal 31, 1055 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2012.2">doi:10.1038/emboj.2012.2</a>
</p>
<p>Authors: Lorenzo Galluzzi, Oliver Kepp &amp; Guido Kroemer</p>
<p>EMBO J315, 1062&#8211;1079 (2012); published online 17 January 2012In this issue of The EMBO Journal, Garg et al (2012) delineate a signalling pathway that leads to calreticulin (CRT) exposure and ATP release by cancer cells that succumb to photodynamic therapy (PTD), thereby providing fresh insights into the molecular regulation of immunogenic cell death (ICD).</p>
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<dc:title>Enlightening the impact of immunogenic cell death in photodynamic cancer therapy</dc:title>
<dc:creator>Lorenzo Galluzzi</dc:creator>
<dc:creator>Oliver Kepp</dc:creator>
<dc:creator>Guido Kroemer</dc:creator>
<dc:identifier>doi:10.1038/emboj.2012.2</dc:identifier>
<dc:source>The EMBO Journal 31, 1055 (2012)</dc:source>
<dc:date>2012-01-17</dc:date>
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<prism:section>Have you seen?</prism:section>
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                     <title>B-type lamins and their elusive roles in metazoan cell proliferation and senescence</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/p0N7f9Cw8bQ/emboj.2012.39</link>
<description>B-type lamins and their elusive roles in metazoan cell proliferation and senescenceRecent papers question the traditional role of B-type lamins in DNA replication and transcription, but highlight an entirely novel yet fundamental role for lamin B1 in cell proliferation and cellular senescence.</description>
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<p>
<b>B-type lamins and their elusive roles in metazoan cell proliferation and senescence</b>
</p>
<p>The EMBO Journal 31, 1058 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2012.39">doi:10.1038/emboj.2012.39</a>
</p>
<p>Author: Christopher J Hutchison</p>
<p>EMBO J315, 1080&#8211;1094 (2012); published online 13 January 2012Have you seen the recent papers that question the traditional role of B-type lamins in DNA replication and transcription, but highlight an entirely novel yet fundamental role for lamin B1 (LB1) in cell proliferation and cellular senescence?</p>
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<dc:title>B-type lamins and their elusive roles in metazoan cell proliferation and senescence</dc:title>
<dc:creator>Christopher J Hutchison</dc:creator>
<dc:identifier>doi:10.1038/emboj.2012.39</dc:identifier>
<dc:source>The EMBO Journal 31, 1058 (2012)</dc:source>
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<prism:section>Have you seen?</prism:section>
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                     <title>To be or not to be a stem cell: dissection of cellular and molecular components of haematopoietic stem cell niches</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/-tCLf5SfFP4/emboj.2012.29</link>
<description>To be or not to be a stem cell: dissection of cellular and molecular components of haematopoietic stem cell nichesGenetic ablation of stem cell factor (SCF) facilitates the identification of cellular population(s) that constitute the haematopoietic stem cell (HSC) niche.</description>
<content:encoded><![CDATA[

<p>
<b>To be or not to be a stem cell: dissection of cellular and molecular components of haematopoietic stem cell niches</b>
</p>
<p>The EMBO Journal 31, 1060 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2012.29">doi:10.1038/emboj.2012.29</a>
</p>
<p>Authors: John M Perry &amp; Linheng Li</p>
<p>Nature4817382, 457&#8211;462 (2012); published online 25 January 2012Recent studies have identified multiple cell types that regulate haematopoietic stem cells (HSCs); however, proof that a specific cell type produces a specific factor important for HSC function and maintenance is largely lacking. Ding et al (2012) reported recently that conditional deletion of stem cell factor (SCF) in Leptin receptor (Lepr) expressing perivascular cells or endothelial and haematopoietic cells resulted in significant reductions in number but less profound reduction in function of HSCs. Although the long-term fate of HSCs in these models is largely unexplored and an underlying mechanism for reduction in HSCs not yet reported, these findings further implicate the vascular niche in the functional maintenance of HSCs in vivo and also raise intriguing questions for future studies in this field.</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/-tCLf5SfFP4" height="1" width="1"/>]]></content:encoded>
<dc:title>To be or not to be a stem cell: dissection of cellular and molecular components of haematopoietic stem cell niches</dc:title>
<dc:creator>John M Perry</dc:creator>
<dc:creator>Linheng Li</dc:creator>
<dc:identifier>doi:10.1038/emboj.2012.29</dc:identifier>
<dc:source>The EMBO Journal 31, 1060 (2012)</dc:source>
<dc:date>2012-02-10</dc:date>
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<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Have you seen?</prism:section>
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<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2012.29</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.497">
                     <title>A novel pathway combining calreticulin exposure and ATP secretion in immunogenic cancer cell death</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/gLSI1tvEFvs/emboj.2011.497</link>
<description>A novel pathway combining calreticulin exposure and ATP secretion in immunogenic cancer cell deathUnravelling molecular mechanisms that trigger immunogenic apoptosis of cancer cells could improve therapeutic intervention. Here, photo-oxidative ER stress increases presentation of ‘eat me’ (surface-exposed calreticulin) and ‘find me’ (ATP secretion) signals via a novel, PERK-dependent pathway.</description>
<content:encoded><![CDATA[

<p>
<b>A novel pathway combining calreticulin exposure and ATP secretion in immunogenic cancer cell death</b>
</p>
<p>The EMBO Journal 31, 1062 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.497">doi:10.1038/emboj.2011.497</a>
</p>
<p>Authors: Abhishek D Garg, Dmitri V Krysko, Tom Verfaillie, Agnieszka Kaczmarek, Gabriela B Ferreira, Thierry Marysael, Noemi Rubio, Malgorzata Firczuk, Chantal Mathieu, Anton J M Roebroek, Wim Annaert, Jakub Golab, Peter de Witte, Peter Vandenabeele &amp; Patrizia Agostinis</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/gLSI1tvEFvs" height="1" width="1"/>]]></content:encoded>
<dc:title>A novel pathway combining calreticulin exposure and ATP secretion in immunogenic cancer cell death</dc:title>
<dc:creator>Abhishek D Garg</dc:creator>
<dc:creator>Dmitri V Krysko</dc:creator>
<dc:creator>Tom Verfaillie</dc:creator>
<dc:creator>Agnieszka Kaczmarek</dc:creator>
<dc:creator>Gabriela B Ferreira</dc:creator>
<dc:creator>Thierry Marysael</dc:creator>
<dc:creator>Noemi Rubio</dc:creator>
<dc:creator>Malgorzata Firczuk</dc:creator>
<dc:creator>Chantal Mathieu</dc:creator>
<dc:creator>Anton J M Roebroek</dc:creator>
<dc:creator>Wim Annaert</dc:creator>
<dc:creator>Jakub Golab</dc:creator>
<dc:creator>Peter de Witte</dc:creator>
<dc:creator>Peter Vandenabeele</dc:creator>
<dc:creator>Patrizia Agostinis</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.497</dc:identifier>
<dc:source>The EMBO Journal 31, 1062 (2012)</dc:source>
<dc:date>2012-01-17</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-17</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.497</prism:doi>
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<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.492">
                     <title>Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/vGQHtJm4wN4/emboj.2011.492</link>
<description>Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulationAltered lamin B1 levels are found to induce cellular senescence as well as abnormal nuclear morphology, a marker of both physiological and premature ageing in animals. Lamin B1 accumulation is induced by oxidative stress and p38 kinase, providing links with two other key factors in ageing and senescence.</description>
<content:encoded><![CDATA[

<p>
<b>Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation</b>
</p>
<p>The EMBO Journal 31, 1080 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.492">doi:10.1038/emboj.2011.492</a>
</p>
<p>Authors: Aurelia Barascu, Catherine Le Chalony, Ga&#235;lle Pennarun, Diane Genet, Naima Imam, Bernard Lopez &amp; Pascale Bertrand</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/vGQHtJm4wN4" height="1" width="1"/>]]></content:encoded>
<dc:title>Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation</dc:title>
<dc:creator>Aurelia Barascu</dc:creator>
<dc:creator>Catherine Le Chalony</dc:creator>
<dc:creator>Gaëlle Pennarun</dc:creator>
<dc:creator>Diane Genet</dc:creator>
<dc:creator>Naima Imam</dc:creator>
<dc:creator>Bernard Lopez</dc:creator>
<dc:creator>Pascale Bertrand</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.492</dc:identifier>
<dc:source>The EMBO Journal 31, 1080 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.492</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.492</prism:url>
<prism:volume>31</prism:volume>
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<prism:startingPage>1080</prism:startingPage>
<prism:endingPage>1094</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/emboj.2012.32">
                     <title>A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/ftrVT5YmZXs/emboj.2012.32</link>
<description>A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEBUnder basal conditions TFEB, a master regulator of lysosomal biogenesis, is sequestered in the cytosol due to mTORC1-dependent phosphorylation at the lysosomal membrane. Nutrient starvation or lysosomal dysfunction inhibit mTORC1 activity and induce nuclear translocation of TFEB inducing target gene expression.</description>
<content:encoded><![CDATA[

<p>
<b>A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB</b>
</p>
<p>The EMBO Journal 31, 1095 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2012.32">doi:10.1038/emboj.2012.32</a>
</p>
<p>Authors: Carmine Settembre, Roberto Zoncu, Diego L Medina, Francesco Vetrini, Serkan Erdin, SerpilUckac Erdin, Tuong Huynh, Mathieu Ferron, Gerard Karsenty, Michel C Vellard, Valeria Facchinetti, David M Sabatini &amp; Andrea Ballabio</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/ftrVT5YmZXs" height="1" width="1"/>]]></content:encoded>
<dc:title>A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB</dc:title>
<dc:creator>Carmine Settembre</dc:creator>
<dc:creator>Roberto Zoncu</dc:creator>
<dc:creator>Diego L Medina</dc:creator>
<dc:creator>Francesco Vetrini</dc:creator>
<dc:creator>Serkan Erdin</dc:creator>
<dc:creator>SerpilUckac Erdin</dc:creator>
<dc:creator>Tuong Huynh</dc:creator>
<dc:creator>Mathieu Ferron</dc:creator>
<dc:creator>Gerard Karsenty</dc:creator>
<dc:creator>Michel C Vellard</dc:creator>
<dc:creator>Valeria Facchinetti</dc:creator>
<dc:creator>David M Sabatini</dc:creator>
<dc:creator>Andrea Ballabio</dc:creator>
<dc:identifier>doi:10.1038/emboj.2012.32</dc:identifier>
<dc:source>The EMBO Journal 31, 1095 (2012)</dc:source>
<dc:date>2012-02-17</dc:date>
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<prism:publicationDate>2012-02-17</prism:publicationDate>
<prism:doi>10.1038/emboj.2012.32</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2012.32</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.487">
                     <title>A molecular mechanism that links Hippo signalling to the inhibition of Wnt/β-catenin signalling</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/HsFZKY4es4k/emboj.2011.487</link>
<description>A molecular mechanism that links Hippo signalling to the inhibition of Wnt/β-catenin signallingThe Hippo pathway effector YAZ is found to bind β-catenin and prevents its nuclear translocation. The resulting downregulation of Wnt signal transduction provides a new example for intersection of Hippo and Wnt signalling, two key regulatory pathways in animal development</description>
<content:encoded><![CDATA[

<p>
<b>A molecular mechanism that links Hippo signalling to the inhibition of Wnt/&#946;-catenin signalling</b>
</p>
<p>The EMBO Journal 31, 1109 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.487">doi:10.1038/emboj.2011.487</a>
</p>
<p>Authors: Masamichi Imajo, Koichi Miyatake, Akira Iimura, Atsumu Miyamoto &amp; Eisuke Nishida</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/HsFZKY4es4k" height="1" width="1"/>]]></content:encoded>
<dc:title>A molecular mechanism that links Hippo signalling to the inhibition of Wnt/β-catenin signalling</dc:title>
<dc:creator>Masamichi Imajo</dc:creator>
<dc:creator>Koichi Miyatake</dc:creator>
<dc:creator>Akira Iimura</dc:creator>
<dc:creator>Atsumu Miyamoto</dc:creator>
<dc:creator>Eisuke Nishida</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.487</dc:identifier>
<dc:source>The EMBO Journal 31, 1109 (2012)</dc:source>
<dc:date>2012-01-10</dc:date>
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<prism:publicationDate>2012-01-10</prism:publicationDate>
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<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.495">
                     <title>STIM1 is required for attenuation of PMCA-mediated Ca2+ clearance during T-cell activation</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/pjzBGwNmrF0/emboj.2011.495</link>
<description>STIM1 is required for attenuation of PMCA-mediated CaThe ER Ca2+ sensor STIM1 and the plasma membrane Ca2+ pump, ATPase, PMCA, are recruited to the immunological synapse upon T-cell stimulation where STIM1 binds to and inhibits PMCA function to regulate cytosolic Ca2+ concentration.</description>
<content:encoded><![CDATA[

<p>
<b>STIM1 is required for attenuation of PMCA-mediated Ca2&#43; clearance during T-cell activation</b>
</p>
<p>The EMBO Journal 31, 1123 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.495">doi:10.1038/emboj.2011.495</a>
</p>
<p>Authors: Michael F Ritchie, Elsie Samakai &amp; Jonathan Soboloff</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/pjzBGwNmrF0" height="1" width="1"/>]]></content:encoded>
<dc:title>STIM1 is required for attenuation of PMCA-mediated Ca2+ clearance during T-cell activation</dc:title>
<dc:creator>Michael F Ritchie</dc:creator>
<dc:creator>Elsie Samakai</dc:creator>
<dc:creator>Jonathan Soboloff</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.495</dc:identifier>
<dc:source>The EMBO Journal 31, 1123 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.495</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.495</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1123</prism:startingPage>
<prism:endingPage>1133</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.495</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.478">
                     <title>Akt-dependent Skp2 mRNA translation is required for exiting contact inhibition, oncogenesis, and adipogenesis</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/ZDGvUikSltE/emboj.2011.478</link>
<description>Akt-dependent Skp2 mRNA translation is required for exiting contact inhibition, oncogenesis, and adipogenesisNogueira et al identify a novel, translational component of AKT to regulate Skp2 level. General significance comes from two distinct biological systems, escape from contact inhibition/oncogenic transformation and adipocyte differentiation.</description>
<content:encoded><![CDATA[

<p>
<b>Akt-dependent Skp2 mRNA translation is required for exiting contact inhibition, oncogenesis, and adipogenesis</b>
</p>
<p>The EMBO Journal 31, 1134 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.478">doi:10.1038/emboj.2011.478</a>
</p>
<p>Authors: Veronique Nogueira, Deepa Sundararajan, Jennifer M Kwan, Xiao-ding Peng, Neha Sarvepalli, Nahum Sonenberg &amp; Nissim Hay</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/ZDGvUikSltE" height="1" width="1"/>]]></content:encoded>
<dc:title>Akt-dependent Skp2 mRNA translation is required for exiting contact inhibition, oncogenesis, and adipogenesis</dc:title>
<dc:creator>Veronique Nogueira</dc:creator>
<dc:creator>Deepa Sundararajan</dc:creator>
<dc:creator>Jennifer M Kwan</dc:creator>
<dc:creator>Xiao-ding Peng</dc:creator>
<dc:creator>Neha Sarvepalli</dc:creator>
<dc:creator>Nahum Sonenberg</dc:creator>
<dc:creator>Nissim Hay</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.478</dc:identifier>
<dc:source>The EMBO Journal 31, 1134 (2012)</dc:source>
<dc:date>2012-02-03</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-02-03</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.478</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.478</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1134</prism:startingPage>
<prism:endingPage>1146</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.478</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.480">
                     <title>Ablation of Rassf2 induces bone defects and subsequent haematopoietic anomalies in mice</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/STY_S2NqUlE/emboj.2011.480</link>
<description>Ablation of Rassf2 induces bone defects and subsequent haematopoietic anomalies in miceThe Ras-binding protein RASSF2 has poorly defined functions in cell-cycle control and apoptosis, and has been linked to Hippo signalling. Loss of Rassf2 in vivo disrupts osteoblast differentiation via NF-κB pathway deregulation, with consequent effects on bone formation and haematopoietic development.</description>
<content:encoded><![CDATA[

<p>
<b>Ablation of Rassf2 induces bone defects and subsequent haematopoietic anomalies in mice</b>
</p>
<p>The EMBO Journal 31, 1147 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.480">doi:10.1038/emboj.2011.480</a>
</p>
<p>Authors: Hoogeun Song, Hyunsoo Kim, Kyunghee Lee, Da-Hye Lee, Tae-Shin Kim, Ji Yun Song, Dongjun Lee, Dongwook Choi, Chang-Yong Ko, Han-Sung Kim, Hong-In Shin, Juhyun Choi, Heedong Park, Chankyu Park, Daewon Jeong &amp; Dae-Sik Lim</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/STY_S2NqUlE" height="1" width="1"/>]]></content:encoded>
<dc:title>Ablation of Rassf2 induces bone defects and subsequent haematopoietic anomalies in mice</dc:title>
<dc:creator>Hoogeun Song</dc:creator>
<dc:creator>Hyunsoo Kim</dc:creator>
<dc:creator>Kyunghee Lee</dc:creator>
<dc:creator>Da-Hye Lee</dc:creator>
<dc:creator>Tae-Shin Kim</dc:creator>
<dc:creator>Ji Yun Song</dc:creator>
<dc:creator>Dongjun Lee</dc:creator>
<dc:creator>Dongwook Choi</dc:creator>
<dc:creator>Chang-Yong Ko</dc:creator>
<dc:creator>Han-Sung Kim</dc:creator>
<dc:creator>Hong-In Shin</dc:creator>
<dc:creator>Juhyun Choi</dc:creator>
<dc:creator>Heedong Park</dc:creator>
<dc:creator>Chankyu Park</dc:creator>
<dc:creator>Daewon Jeong</dc:creator>
<dc:creator>Dae-Sik Lim</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.480</dc:identifier>
<dc:source>The EMBO Journal 31, 1147 (2012)</dc:source>
<dc:date>2012-01-06</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-06</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.480</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.480</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1147</prism:startingPage>
<prism:endingPage>1159</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.480</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.490">
                     <title>APRIN is a cell cycle specific BRCA2-interacting protein required for genome integrity and a predictor of outcome after chemotherapy in breast cancer</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/X3dN7g8r_UA/emboj.2011.490</link>
<description>APRIN is a cell cycle specific BRCA2-interacting protein required for genome integrity and a predictor of outcome after chemotherapy in breast cancerProteomic profiling identifies APRIN/PDS5B, a human homologue of the yeast cohesin factor Pds5, as a BRCA2-associated protein required for efficient homologous recombination mediated by this tumour suppressor. BRCA2 cancer mutations disrupt this interaction, and APRIN expression correlates with clinical parameters in breast cancer.</description>
<content:encoded><![CDATA[

<p>
<b>APRIN is a cell cycle specific BRCA2-interacting protein required for genome integrity and a predictor of outcome after chemotherapy in breast cancer</b>
</p>
<p>The EMBO Journal 31, 1160 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.490">doi:10.1038/emboj.2011.490</a>
</p>
<p>Authors: Rachel Brough, Ilirjana Bajrami, Radost Vatcheva, Rachael Natrajan, Jorge S Reis-Filho, Christopher J Lord &amp; Alan Ashworth</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/X3dN7g8r_UA" height="1" width="1"/>]]></content:encoded>
<dc:title>APRIN is a cell cycle specific BRCA2-interacting protein required for genome integrity and a predictor of outcome after chemotherapy in breast cancer</dc:title>
<dc:creator>Rachel Brough</dc:creator>
<dc:creator>Ilirjana Bajrami</dc:creator>
<dc:creator>Radost Vatcheva</dc:creator>
<dc:creator>Rachael Natrajan</dc:creator>
<dc:creator>Jorge S Reis-Filho</dc:creator>
<dc:creator>Christopher J Lord</dc:creator>
<dc:creator>Alan Ashworth</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.490</dc:identifier>
<dc:source>The EMBO Journal 31, 1160 (2012)</dc:source>
<dc:date>2012-01-31</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-31</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.490</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.490</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1160</prism:startingPage>
<prism:endingPage>1176</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.490</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.493">
                     <title>ATR maintains select progenitors during nervous system development</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/iClX0Pr4Meg/emboj.2011.493</link>
<description>ATR maintains select progenitors during nervous system developmentATR kinase acts as a safeguard against replication stress, and hypomorphic mutations result in the neurodevelopmental disorder Seckel syndrome. Conditional ATR deletion in developing neurons reveals a selective role in maintenance of only a subset of neuronal progenitors, which may be distinct from ATR's canonical DNA damage-response roles.</description>
<content:encoded><![CDATA[

<p>
<b>ATR maintains select progenitors during nervous system development</b>
</p>
<p>The EMBO Journal 31, 1177 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.493">doi:10.1038/emboj.2011.493</a>
</p>
<p>Authors: Youngsoo Lee, Erin RP Shull, Pierre-Olivier Frappart, Sachin Katyal, Vanessa Enriquez-Rios, Jingfeng Zhao, Helen R Russell, Eric J Brown &amp; Peter J McKinnon</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/iClX0Pr4Meg" height="1" width="1"/>]]></content:encoded>
<dc:title>ATR maintains select progenitors during nervous system development</dc:title>
<dc:creator>Youngsoo Lee</dc:creator>
<dc:creator>Erin RP Shull</dc:creator>
<dc:creator>Pierre-Olivier Frappart</dc:creator>
<dc:creator>Sachin Katyal</dc:creator>
<dc:creator>Vanessa Enriquez-Rios</dc:creator>
<dc:creator>Jingfeng Zhao</dc:creator>
<dc:creator>Helen R Russell</dc:creator>
<dc:creator>Eric J Brown</dc:creator>
<dc:creator>Peter J McKinnon</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.493</dc:identifier>
<dc:source>The EMBO Journal 31, 1177 (2012)</dc:source>
<dc:date>2012-01-20</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-20</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.493</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.493</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1177</prism:startingPage>
<prism:endingPage>1189</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.493</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.486">
                     <title>RP58 controls neuron and astrocyte differentiation by downregulating the expression of Id1–4 genes in the developing cortex</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/zod_sucKm6w/emboj.2011.486</link>
<description>RP58 controls neuron and astrocyte differentiation by downregulating the expression of Neuronal stem cell differentiation during cortical development requires to exit cell cycle and p57 kinase regulation. Here, the transcription factor RP58 is shown to control neuronal differentiation and migration during embryogenesis by repressing all four Id genes, which in turn downregulates p57, thereby restricting astrogenesis.</description>
<content:encoded><![CDATA[

<p>
<b>RP58 controls neuron and astrocyte differentiation by downregulating the expression of Id1&#8211;4 genes in the developing cortex</b>
</p>
<p>The EMBO Journal 31, 1190 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.486">doi:10.1038/emboj.2011.486</a>
</p>
<p>Authors: Shinobu Hirai, Akiko Miwa, Chiaki Ohtaka-Maruyama, Masataka Kasai, Shigeo Okabe, Yutaka Hata &amp; Haruo Okado</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/zod_sucKm6w" height="1" width="1"/>]]></content:encoded>
<dc:title>RP58 controls neuron and astrocyte differentiation by downregulating the expression of Id1–4 genes in the developing cortex</dc:title>
<dc:creator>Shinobu Hirai</dc:creator>
<dc:creator>Akiko Miwa</dc:creator>
<dc:creator>Chiaki Ohtaka-Maruyama</dc:creator>
<dc:creator>Masataka Kasai</dc:creator>
<dc:creator>Shigeo Okabe</dc:creator>
<dc:creator>Yutaka Hata</dc:creator>
<dc:creator>Haruo Okado</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.486</dc:identifier>
<dc:source>The EMBO Journal 31, 1190 (2012)</dc:source>
<dc:date>2012-01-10</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-10</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.486</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.486</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1190</prism:startingPage>
<prism:endingPage>1202</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.486</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.482">
                     <title>CaMKII binding to GluN2B is critical during memory consolidation</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/q2bWxjBM6a4/emboj.2011.482</link>
<description>CaMKII binding to GluN2B is critical during memory consolidationMice expressing a mutant form of the NMDA-type glutamate receptor subunit GluN2B that is deficient in CaMKII binding exhibit impaired hippocampus-dependent memory consolidation, revealing an important functional role for the activity-driven interaction of CaMKII with GluN2B.</description>
<content:encoded><![CDATA[

<p>
<b>CaMKII binding to GluN2B is critical during memory consolidation</b>
</p>
<p>The EMBO Journal 31, 1203 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.482">doi:10.1038/emboj.2011.482</a>
</p>
<p>Authors: Amy R Halt, Robert F Dallapiazza, Yu Zhou, Ivar S Stein, Hai Qian, Scott Juntti, Sonja Wojcik, Nils Brose, Alcino J Silva &amp; Johannes W Hell</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/q2bWxjBM6a4" height="1" width="1"/>]]></content:encoded>
<dc:title>CaMKII binding to GluN2B is critical during memory consolidation</dc:title>
<dc:creator>Amy R Halt</dc:creator>
<dc:creator>Robert F Dallapiazza</dc:creator>
<dc:creator>Yu Zhou</dc:creator>
<dc:creator>Ivar S Stein</dc:creator>
<dc:creator>Hai Qian</dc:creator>
<dc:creator>Scott Juntti</dc:creator>
<dc:creator>Sonja Wojcik</dc:creator>
<dc:creator>Nils Brose</dc:creator>
<dc:creator>Alcino J Silva</dc:creator>
<dc:creator>Johannes W Hell</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.482</dc:identifier>
<dc:source>The EMBO Journal 31, 1203 (2012)</dc:source>
<dc:date>2012-01-10</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-10</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.482</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.482</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1203</prism:startingPage>
<prism:endingPage>1216</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.482</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.488">
                     <title>Raising cytosolic Cl− in cerebellar granule cells affects their excitability and vestibulo-ocular learning</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/YUQFUgDsrrE/emboj.2011.488</link>
<description>Raising cytosolic ClThe cerebellar circuitry underlying motor control and learning consists of granule cells (GCs) and Purkinje cells (PCs). Deletion of the Kcc2 K-Cl cotransporter ablates Cl− extrusion in both cell types. Unexpectedly, a critical role for GC excitability in the consolidation of motor learning is uncovered.</description>
<content:encoded><![CDATA[

<p>
<b>Raising cytosolic Cl&#8722; in cerebellar granule cells affects their excitability and vestibulo-ocular learning</b>
</p>
<p>The EMBO Journal 31, 1217 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.488">doi:10.1038/emboj.2011.488</a>
</p>
<p>Authors: Patricia Seja, Martijn Schonewille, Guillermo Spitzmaul, Aleksandra Badura, Ilse Klein, York Rudhard, William Wisden, Christian A H&#252;bner, Chris I De Zeeuw &amp; Thomas J Jentsch</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/YUQFUgDsrrE" height="1" width="1"/>]]></content:encoded>
<dc:title>Raising cytosolic Cl− in cerebellar granule cells affects their excitability and vestibulo-ocular learning</dc:title>
<dc:creator>Patricia Seja</dc:creator>
<dc:creator>Martijn Schonewille</dc:creator>
<dc:creator>Guillermo Spitzmaul</dc:creator>
<dc:creator>Aleksandra Badura</dc:creator>
<dc:creator>Ilse Klein</dc:creator>
<dc:creator>York Rudhard</dc:creator>
<dc:creator>William Wisden</dc:creator>
<dc:creator>Christian A Hübner</dc:creator>
<dc:creator>Chris I De Zeeuw</dc:creator>
<dc:creator>Thomas J Jentsch</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.488</dc:identifier>
<dc:source>The EMBO Journal 31, 1217 (2012)</dc:source>
<dc:date>2012-01-17</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-17</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.488</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.488</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1217</prism:startingPage>
<prism:endingPage>1230</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.488</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.489">
                     <title>Microvesicles released from microglia stimulate synaptic activity via enhanced sphingolipid metabolism</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/tqqeTOlePIk/emboj.2011.489</link>
<description>Microvesicles released from microglia stimulate synaptic activity via enhanced sphingolipid metabolismMicrovesicles (MVs) shed from microglia stimulate neuronal exocytosis and enhance neurotransmission by inducing sphingolipid metabolism in neurons.</description>
<content:encoded><![CDATA[

<p>
<b>Microvesicles released from microglia stimulate synaptic activity via enhanced sphingolipid metabolism</b>
</p>
<p>The EMBO Journal 31, 1231 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.489">doi:10.1038/emboj.2011.489</a>
</p>
<p>Authors: Flavia Antonucci, Elena Turola, Loredana Riganti, Matteo Caleo, Martina Gabrielli, Cristiana Perrotta, Luisa Novellino, Emilio Clementi, Paola Giussani, Paola Viani, Michela Matteoli &amp; Claudia Verderio</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/tqqeTOlePIk" height="1" width="1"/>]]></content:encoded>
<dc:title>Microvesicles released from microglia stimulate synaptic activity via enhanced sphingolipid metabolism</dc:title>
<dc:creator>Flavia Antonucci</dc:creator>
<dc:creator>Elena Turola</dc:creator>
<dc:creator>Loredana Riganti</dc:creator>
<dc:creator>Matteo Caleo</dc:creator>
<dc:creator>Martina Gabrielli</dc:creator>
<dc:creator>Cristiana Perrotta</dc:creator>
<dc:creator>Luisa Novellino</dc:creator>
<dc:creator>Emilio Clementi</dc:creator>
<dc:creator>Paola Giussani</dc:creator>
<dc:creator>Paola Viani</dc:creator>
<dc:creator>Michela Matteoli</dc:creator>
<dc:creator>Claudia Verderio</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.489</dc:identifier>
<dc:source>The EMBO Journal 31, 1231 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.489</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.489</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1231</prism:startingPage>
<prism:endingPage>1240</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.489</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.471">
                     <title>Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/vm6QogFA8UA/emboj.2011.471</link>
<description>Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linkingTDP-43 is a major constituent of inclusions characteristic of a number of neurodegenerative diseases. Oxidative stress induces reversible intra- and inter-molecular disulphide bond formation at the second RNA-recognition motif impairing the solubility and the RNA processing function of TDP-43.</description>
<content:encoded><![CDATA[

<p>
<b>Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking</b>
</p>
<p>The EMBO Journal 31, 1241 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.471">doi:10.1038/emboj.2011.471</a>
</p>
<p>Authors: Todd J Cohen, Andrew W Hwang, Travis Unger, John Q Trojanowski &amp; Virginia M Y Lee</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/vm6QogFA8UA" height="1" width="1"/>]]></content:encoded>
<dc:title>Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking</dc:title>
<dc:creator>Todd J Cohen</dc:creator>
<dc:creator>Andrew W Hwang</dc:creator>
<dc:creator>Travis Unger</dc:creator>
<dc:creator>John Q Trojanowski</dc:creator>
<dc:creator>Virginia M Y Lee</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.471</dc:identifier>
<dc:source>The EMBO Journal 31, 1241 (2012)</dc:source>
<dc:date>2011-12-23</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2011-12-23</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.471</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.471</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1241</prism:startingPage>
<prism:endingPage>1252</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.471</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.476">
                     <title>Genetic evidence of a redox-dependent systemic wound response via Hayan Protease-Phenoloxidase system in Drosophila</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/JkOQokOen3Q/emboj.2011.476</link>
<description>Genetic evidence of a redox-dependent systemic wound response via Hayan Protease-Phenoloxidase system in Melanin production is a rapid response to wounding in Drosophila. The enzymatic reactions generate reactive oxygen species. ROS-dependent activation of JNK signalling in the nervous system contributes to the systemic wound response and promotes survival upon physical trauma.</description>
<content:encoded><![CDATA[

<p>
<b>Genetic evidence of a redox-dependent systemic wound response via Hayan Protease-Phenoloxidase system in Drosophila</b>
</p>
<p>The EMBO Journal 31, 1253 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.476">doi:10.1038/emboj.2011.476</a>
</p>
<p>Authors: Hyuck-Jin Nam, In-Hwan Jang, Hyejin You, Kyung-Ah Lee &amp; Won-Jae Lee</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/JkOQokOen3Q" height="1" width="1"/>]]></content:encoded>
<dc:title>Genetic evidence of a redox-dependent systemic wound response via Hayan Protease-Phenoloxidase system in Drosophila</dc:title>
<dc:creator>Hyuck-Jin Nam</dc:creator>
<dc:creator>In-Hwan Jang</dc:creator>
<dc:creator>Hyejin You</dc:creator>
<dc:creator>Kyung-Ah Lee</dc:creator>
<dc:creator>Won-Jae Lee</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.476</dc:identifier>
<dc:source>The EMBO Journal 31, 1253 (2012)</dc:source>
<dc:date>2012-01-06</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-06</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.476</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.476</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1253</prism:startingPage>
<prism:endingPage>1265</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.476</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.498">
                     <title>A DR4:tBID axis drives the p53 apoptotic response by promoting oligomerization of poised BAX</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/nZNo2uAD4Jg/emboj.2011.498</link>
<description>A DR4:tBID axis drives the p53 apoptotic response by promoting oligomerization of poised BAXDepending on the context, cells either arrest or undergo apoptosis in response to p53 activation. Key mediators of both pathways are activated irrespective of the fate choice, but apoptotic cells selectively induce the DR4 death receptor pathway, caspase 8-mediated BID cleavage and activation of BAX.</description>
<content:encoded><![CDATA[

<p>
<b>A DR4:tBID axis drives the p53 apoptotic response by promoting oligomerization of poised BAX</b>
</p>
<p>The EMBO Journal 31, 1266 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.498">doi:10.1038/emboj.2011.498</a>
</p>
<p>Authors: Ryan E Henry, Zdenek Andrysik, Ramiro Par&#237;s, Matthew D Galbraith &amp; Joaqu&#237;n M Espinosa</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/nZNo2uAD4Jg" height="1" width="1"/>]]></content:encoded>
<dc:title>A DR4:tBID axis drives the p53 apoptotic response by promoting oligomerization of poised BAX</dc:title>
<dc:creator>Ryan E Henry</dc:creator>
<dc:creator>Zdenek Andrysik</dc:creator>
<dc:creator>Ramiro París</dc:creator>
<dc:creator>Matthew D Galbraith</dc:creator>
<dc:creator>Joaquín M Espinosa</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.498</dc:identifier>
<dc:source>The EMBO Journal 31, 1266 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.498</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.498</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1266</prism:startingPage>
<prism:endingPage>1278</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.498</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.491">
                     <title>Rsk-mediated phosphorylation and 14-3-3ɛ binding of Apaf-1 suppresses cytochrome c-induced apoptosis</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/o-1FyGh-5eM/emboj.2011.491</link>
<description>Rsk-mediated phosphorylation and 14-3-3ɛ binding of Apaf-1 suppresses cytochrome In response to various stimuli, the MAP kinase cascade and its effector kinase Rsk promote cell viability. Rsk phosphorylates Apaf-1 and prevents its interaction with cytochrome c in a 14-3-3ɛ-dependent manner, which results in the inhibition of apoptosome formation.</description>
<content:encoded><![CDATA[

<p>
<b>Rsk-mediated phosphorylation and 14-3-3&#603; binding of Apaf-1 suppresses cytochrome c-induced apoptosis</b>
</p>
<p>The EMBO Journal 31, 1279 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.491">doi:10.1038/emboj.2011.491</a>
</p>
<p>Authors: Jiyeon Kim, Amanda B Parrish, Manabu Kurokawa, Kenkyo Matsuura, Christopher D Freel, Joshua L Andersen, Carrie E Johnson &amp; Sally Kornbluth</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/o-1FyGh-5eM" height="1" width="1"/>]]></content:encoded>
<dc:title>Rsk-mediated phosphorylation and 14-3-3ɛ binding of Apaf-1 suppresses cytochrome c-induced apoptosis</dc:title>
<dc:creator>Jiyeon Kim</dc:creator>
<dc:creator>Amanda B Parrish</dc:creator>
<dc:creator>Manabu Kurokawa</dc:creator>
<dc:creator>Kenkyo Matsuura</dc:creator>
<dc:creator>Christopher D Freel</dc:creator>
<dc:creator>Joshua L Andersen</dc:creator>
<dc:creator>Carrie E Johnson</dc:creator>
<dc:creator>Sally Kornbluth</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.491</dc:identifier>
<dc:source>The EMBO Journal 31, 1279 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.491</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.491</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1279</prism:startingPage>
<prism:endingPage>1292</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.491</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.477">
                     <title>Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assembly</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/aVJxk6bmyTc/emboj.2011.477</link>
<description>Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assemblyRespiratory chain complexes are organized into supercomplexes. Patient cell lines expressing a truncated COX1 subunit point to an m-AAA protease-dependent quality control pathway that clears unstable respiratory complexes that are still capable to assemble into supercomplexes.</description>
<content:encoded><![CDATA[

<p>
<b>Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assembly</b>
</p>
<p>The EMBO Journal 31, 1293 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.477">doi:10.1038/emboj.2011.477</a>
</p>
<p>Authors: Hue-Tran Hornig-Do, Takashi Tatsuta, Angela Buckermann, Maria Bust, Gittan Kollberg, Agnes R&#246;tig, Martin Hellmich, Leo Nijtmans &amp; Rudolf J Wiesner</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/aVJxk6bmyTc" height="1" width="1"/>]]></content:encoded>
<dc:title>Nonsense mutations in the COX1 subunit impair the stability of respiratory chain complexes rather than their assembly</dc:title>
<dc:creator>Hue-Tran Hornig-Do</dc:creator>
<dc:creator>Takashi Tatsuta</dc:creator>
<dc:creator>Angela Buckermann</dc:creator>
<dc:creator>Maria Bust</dc:creator>
<dc:creator>Gittan Kollberg</dc:creator>
<dc:creator>Agnes Rötig</dc:creator>
<dc:creator>Martin Hellmich</dc:creator>
<dc:creator>Leo Nijtmans</dc:creator>
<dc:creator>Rudolf J Wiesner</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.477</dc:identifier>
<dc:source>The EMBO Journal 31, 1293 (2012)</dc:source>
<dc:date>2012-01-17</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-17</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.477</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.477</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1293</prism:startingPage>
<prism:endingPage>1307</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.477</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.496">
                     <title>Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/9cxu55cP1hw/emboj.2011.496</link>
<description>Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherinIn this article, the authors characterize the phosphotyrosine-binding domain of the E3 ubiquitin ligase Hakai. They find that Hakai homodimerizes to form a phosphotyrosine-binding pocket that recognizes Src targets. This represents a novel phosphotyrosine recognition structure, fundamentally different from the previously known SH2 and PTB domains.</description>
<content:encoded><![CDATA[

<p>
<b>Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin</b>
</p>
<p>The EMBO Journal 31, 1308 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.496">doi:10.1038/emboj.2011.496</a>
</p>
<p>Authors: Manjeet Mukherjee, Soah Yee Chow, Permeen Yusoff, J Seetharaman, Cherlyn Ng, Saravanan Sinniah, Xiao Woon Koh, Nur Farehan M Asgar, Dan Li, Daniel Yim, Rebecca A Jackson, Jingxi Yew, Jingru Qian, Audrey Iyu, Yoon Pin Lim, Xingding Zhou, Siu Kwan Sze, Graeme R Guy &amp; J Sivaraman</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/9cxu55cP1hw" height="1" width="1"/>]]></content:encoded>
<dc:title>Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin</dc:title>
<dc:creator>Manjeet Mukherjee</dc:creator>
<dc:creator>Soah Yee Chow</dc:creator>
<dc:creator>Permeen Yusoff</dc:creator>
<dc:creator>J Seetharaman</dc:creator>
<dc:creator>Cherlyn Ng</dc:creator>
<dc:creator>Saravanan Sinniah</dc:creator>
<dc:creator>Xiao Woon Koh</dc:creator>
<dc:creator>Nur Farehan M Asgar</dc:creator>
<dc:creator>Dan Li</dc:creator>
<dc:creator>Daniel Yim</dc:creator>
<dc:creator>Rebecca A Jackson</dc:creator>
<dc:creator>Jingxi Yew</dc:creator>
<dc:creator>Jingru Qian</dc:creator>
<dc:creator>Audrey Iyu</dc:creator>
<dc:creator>Yoon Pin Lim</dc:creator>
<dc:creator>Xingding Zhou</dc:creator>
<dc:creator>Siu Kwan Sze</dc:creator>
<dc:creator>Graeme R Guy</dc:creator>
<dc:creator>J Sivaraman</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.496</dc:identifier>
<dc:source>The EMBO Journal 31, 1308 (2012)</dc:source>
<dc:date>2012-01-17</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-17</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.496</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.496</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1308</prism:startingPage>
<prism:endingPage>1319</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.496</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2011.483">
                     <title>Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/Td-CUI2mqxQ/emboj.2011.483</link>
<description>Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymeraseThe genome of most negative-strand RNA viruses is encased by the nucleoprotein N forming the N-RNA RNP and replicated by the L/P polymerase complex. The authors show for the first time that in vesicular stomatitis virus L protein can initiate de-novo synthesis of naked RNA independently of N or P, although P stimulates L initiation and processivity.</description>
<content:encoded><![CDATA[

<p>
<b>Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase</b>
</p>
<p>The EMBO Journal 31, 1320 (2012).  
            <a href="http://dx.doi.org/10.1038/emboj.2011.483">doi:10.1038/emboj.2011.483</a>
</p>
<p>Authors: Benjamin Morin, Amal A Rahmeh &amp; Sean PJ Whelan</p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/Td-CUI2mqxQ" height="1" width="1"/>]]></content:encoded>
<dc:title>Mechanism of RNA synthesis initiation by the vesicular stomatitis virus polymerase</dc:title>
<dc:creator>Benjamin Morin</dc:creator>
<dc:creator>Amal A Rahmeh</dc:creator>
<dc:creator>Sean PJ Whelan</dc:creator>
<dc:identifier>doi:10.1038/emboj.2011.483</dc:identifier>
<dc:source>The EMBO Journal 31, 1320 (2012)</dc:source>
<dc:date>2012-01-13</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2012-01-13</prism:publicationDate>
<prism:doi>10.1038/emboj.2011.483</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2011.483</prism:url>
<prism:volume>31</prism:volume>
<prism:number>5</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>1320</prism:startingPage>
<prism:endingPage>1329</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2011.483</feedburner:origLink></item>
</rdf:RDF>

