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<title>Boycott everything</title>
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<description>The renewed calls for an academic boycott of Israel (see the Opinion article by Steven Rose in this issue) raise the fundamental question of whether and how this sanction should be applied.Boycotts can be effective when the target is appropriate, when the case is </description>
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<p>
<b>Boycott everything</b>
</p>
<p>EMBO Reports 10, 1183 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.228">doi:10.1038/embor.2009.228</a>
</p>
<p>Author: Howy Jacobs</p>
<p>The renewed calls for an academic boycott of Israel (see the Opinion article by Steven Rose in this issue) raise the fundamental question of whether and how this sanction should be applied.Boycotts can be effective when the target is appropriate, when the case is </p>
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<title>Academic freedom in Israel and Palestine</title>
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<description>Many readers of this journal will, like me, have Israeli colleagues whose research we respect, with whom we have collaborated, and among whom we have friends. Yet, these relationships have been overshadowed by the human rights abuses inflicted against the Palestinians, Israel's flouting of UN </description>
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<p>
<b>Academic freedom in Israel and Palestine</b>
</p>
<p>EMBO Reports 10, 1184 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.229">doi:10.1038/embor.2009.229</a>
</p>
<p>Author: Steven Rose</p>
<p>Many readers of this journal will, like me, have Israeli colleagues whose research we respect, with whom we have collaborated, and among whom we have friends. Yet, these relationships have been overshadowed by the human rights abuses inflicted against the Palestinians, Israel's flouting of UN </p>
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<title>Left is right, right is wrong</title>
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<description>The cover illustration of the August 2009 issue of EMBO reports, although aesthetically pleasing, is unfortunately erroneous and could come as a shock to researchers in the chromatin field. Canonical nucleosomes are indeed left-handed, such as the nucleosomes in the left ‘column’ of chromatin </description>
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<p>
<b>Left is right, right is wrong</b>
</p>
<p>EMBO Reports 10, 1185 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.227">doi:10.1038/embor.2009.227</a>
</p>
<p>Author: Christophe Lavelle</p>
<p>The cover illustration of the August 2009 issue of EMBO reports, although aesthetically pleasing, is unfortunately erroneous and could come as a shock to researchers in the chromatin field. Canonical nucleosomes are indeed left-handed, such as the nucleosomes in the left &#8216;column&#8217; of chromatin </p>
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<dc:creator>Christophe Lavelle</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.227</dc:identifier>
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<title>Is the end in cite?</title>
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<description>Howy Jacobs's light-hearted exploration of where the perverse incentives surrounding the quest for publication in high impact-factor journals might lead paints a gruesome picture. Of course, there is a serious message in his October editorial, and even now many would argue that our fixation with </description>
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<p>
<b>Is the end in cite?</b>
</p>
<p>EMBO Reports 10, 1186 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.235">doi:10.1038/embor.2009.235</a>
</p>
<p>Author: Mark Patterson</p>
<p>Howy Jacobs's light-hearted exploration of where the perverse incentives surrounding the quest for publication in high impact-factor journals might lead paints a gruesome picture. Of course, there is a serious message in his October editorial, and even now many would argue that our fixation with </p>
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<dc:title>Is the end in cite?</dc:title>
<dc:creator>Mark Patterson</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.235</dc:identifier>
<dc:source>EMBO Reports 10, 1186 (2009)</dc:source>
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<title>Genetically modified abominations?</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/b2PkKZpvqyE/embor.2009.230</link>
<description>Widespread opposition to GMOs might have deep-seated cultural causes</description>
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<p>
<b>Genetically modified abominations?</b>
</p>
<p>EMBO Reports 10, 1187 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.230">doi:10.1038/embor.2009.230</a>
</p>
<p>Author: Jakub Kwieci&#324;ski</p>
<p>Widespread opposition to GMOs might have deep-seated cultural causes</p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/b2PkKZpvqyE" height="1" width="1"/>]]></content:encoded>
<dc:title>Genetically modified abominations?</dc:title>
<dc:creator>Jakub Kwieciński</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.230</dc:identifier>
<dc:source>EMBO Reports 10, 1187 (2009)</dc:source>
<dc:date>2009-10-23</dc:date>
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<prism:doi>10.1038/embor.2009.230</prism:doi>
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<prism:startingPage>1187</prism:startingPage>
<prism:endingPage>1190</prism:endingPage>
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<title>Beyond us</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/Ncevw5CjEdg/embor.2009.225</link>
<description>Is a world without humans possible?</description>
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<p>
<b>Beyond us</b>
</p>
<p>EMBO Reports 10, 1191 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.225">doi:10.1038/embor.2009.225</a>
</p>
<p>Author: Valent&#237; Rull</p>
<p>Is a world without humans possible?</p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/Ncevw5CjEdg" height="1" width="1"/>]]></content:encoded>
<dc:title>Beyond us</dc:title>
<dc:creator>Valentí Rull</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.225</dc:identifier>
<dc:source>EMBO Reports 10, 1191 (2009)</dc:source>
<dc:date>2009-10-16</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-16</prism:publicationDate>
<prism:doi>10.1038/embor.2009.225</prism:doi>
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<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
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<prism:startingPage>1191</prism:startingPage>
<prism:endingPage>1195</prism:endingPage>
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<title>Home is where the bench is</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/ktomL70Ne-o/embor.2009.226</link>
<description>International mobility is not restricted to young scientists</description>
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<p>
<b>Home is where the bench is</b>
</p>
<p>EMBO Reports 10, 1196 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.226">doi:10.1038/embor.2009.226</a>
</p>
<p>Author: Howard Wolinsky</p>
<p>International mobility is not restricted to young scientists</p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/ktomL70Ne-o" height="1" width="1"/>]]></content:encoded>
<dc:title>Home is where the bench is</dc:title>
<dc:creator>Howard Wolinsky</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.226</dc:identifier>
<dc:source>EMBO Reports 10, 1196 (2009)</dc:source>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:doi>10.1038/embor.2009.226</prism:doi>
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<prism:volume>10</prism:volume>
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<title>How smart is smart?</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/TFhk1kAYJZw/embor.2009.234</link>
<description>Is human intelligence still evolving?</description>
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<p>
<b>How smart is smart?</b>
</p>
<p>EMBO Reports 10, 1198 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.234">doi:10.1038/embor.2009.234</a>
</p>
<p>Author: Philip Hunter</p>
<p>Is human intelligence still evolving?</p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/TFhk1kAYJZw" height="1" width="1"/>]]></content:encoded>
<dc:title>How smart is smart?</dc:title>
<dc:creator>Philip Hunter</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.234</dc:identifier>
<dc:source>EMBO Reports 10, 1198 (2009)</dc:source>
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<prism:doi>10.1038/embor.2009.234</prism:doi>
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<prism:volume>10</prism:volume>
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<title>Cancer proteomics—an evolving battlefield</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/u73nLGtax6M/embor.2009.222</link>
<description>IntroductionThe first conference of the EMBO Cancer Proteomics series aimed to bring investigators from oncological backgrounds (both basic and clinical) into close contact with equivalent leaders in proteomics approaches, to establish a translational framework by which proteomics can advance our mechanistic understanding of cancer-related </description>
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<p>
<b>Cancer proteomics&#8212;an evolving battlefield</b>
</p>
<p>EMBO Reports 10, 1202 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.222">doi:10.1038/embor.2009.222</a>
</p>
<p>Authors: Ben C. Collins, Thomas Y. K. Lau, Darran P. O'Connor &amp; Hubert Hondermarck</p>
<p>IntroductionThe first conference of the EMBO Cancer Proteomics series aimed to bring investigators from oncological backgrounds (both basic and clinical) into close contact with equivalent leaders in proteomics approaches, to establish a translational framework by which proteomics can advance our mechanistic understanding of cancer-related </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/u73nLGtax6M" height="1" width="1"/>]]></content:encoded>
<dc:title>Cancer proteomics—an evolving battlefield</dc:title>
<dc:creator>Ben C. Collins</dc:creator>
<dc:creator>Thomas Y. K. Lau</dc:creator>
<dc:creator>Darran P. O'Connor</dc:creator>
<dc:creator>Hubert Hondermarck</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.222</dc:identifier>
<dc:source>EMBO Reports 10, 1202 (2009)</dc:source>
<dc:date>2009-10-02</dc:date>
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<prism:doi>10.1038/embor.2009.222</prism:doi>
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<title>Protein quality control—linking the unfolded protein response to disease</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/-NoZacI7g8c/embor.2009.224</link>
<description>See Glossary for abbreviations used in this article.IntroductionThe correct folding of proteins is essential for cellular homeostasis and the prevention of disease. During times of stress or changes in demand for newly synthesized proteins, signalling pathways cooperate with networks of protein-folding and </description>
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<p>
<b>Protein quality control&#8212;linking the unfolded protein response to disease</b>
</p>
<p>EMBO Reports 10, 1206 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.224">doi:10.1038/embor.2009.224</a>
</p>
<p>Authors: Douglas M. Cyr &amp; Daniel N. Hebert</p>
<p>See Glossary for abbreviations used in this article.IntroductionThe correct folding of proteins is essential for cellular homeostasis and the prevention of disease. During times of stress or changes in demand for newly synthesized proteins, signalling pathways cooperate with networks of protein-folding and </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/-NoZacI7g8c" height="1" width="1"/>]]></content:encoded>
<dc:title>Protein quality control—linking the unfolded protein response to disease</dc:title>
<dc:creator>Douglas M. Cyr</dc:creator>
<dc:creator>Daniel N. Hebert</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.224</dc:identifier>
<dc:source>EMBO Reports 10, 1206 (2009)</dc:source>
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<title>V for victory—a V1-ATPase structure revealed</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/wAQtBGakuxg/embor.2009.231</link>
<description>Vacuolar H+-ATPases (V-ATPases) were discovered more than 30 years ago. They are related to the F-ATPases—that is, ATP synthases—but have been refined for proton pumping by the rotary ATPase activity and are responsible for the acidification of intracellular compartments. Acidification is crucial for </description>
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<p>
<b>V for victory&#8212;a V1-ATPase structure revealed</b>
</p>
<p>EMBO Reports 10, 1211 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.231">doi:10.1038/embor.2009.231</a>
</p>
<p>Authors: Thomas Boesen &amp; Poul Nissen</p>
<p>Vacuolar H+-ATPases (V-ATPases) were discovered more than 30 years ago. They are related to the F-ATPases&#8212;that is, ATP synthases&#8212;but have been refined for proton pumping by the rotary ATPase activity and are responsible for the acidification of intracellular compartments. Acidification is crucial for </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/wAQtBGakuxg" height="1" width="1"/>]]></content:encoded>
<dc:title>V for victory—a V1-ATPase structure revealed</dc:title>
<dc:creator>Thomas Boesen</dc:creator>
<dc:creator>Poul Nissen</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.231</dc:identifier>
<dc:source>EMBO Reports 10, 1211 (2009)</dc:source>
<dc:date>2009-10-16</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-16</prism:publicationDate>
<prism:doi>10.1038/embor.2009.231</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.231</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>1211</prism:startingPage>
<prism:endingPage>1212</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.231</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.221">
<title>Modifications of RNA polymerase II are pivotal in regulating gene expression states</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/us_dD5pLRD8/embor.2009.221</link>
<description>The regulation of gene expression programmes is essential for the generation of diverse cell types during development and for adaptation to environmental signals. RNA polymerase II (RNAPII) transcribes genetic information and coordinates the recruitment of accessory proteins that are responsible for the establishment of active </description>
<content:encoded><![CDATA[

<p>
<b>Modifications of RNA polymerase II are pivotal in regulating gene expression states</b>
</p>
<p>EMBO Reports 10, 1213 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.221">doi:10.1038/embor.2009.221</a>
</p>
<p>Authors: Emily Brookes &amp; Ana Pombo</p>
<p>The regulation of gene expression programmes is essential for the generation of diverse cell types during development and for adaptation to environmental signals. RNA polymerase II (RNAPII) transcribes genetic information and coordinates the recruitment of accessory proteins that are responsible for the establishment of active </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/us_dD5pLRD8" height="1" width="1"/>]]></content:encoded>
<dc:title>Modifications of RNA polymerase II are pivotal in regulating gene expression states</dc:title>
<dc:creator>Emily Brookes</dc:creator>
<dc:creator>Ana Pombo</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.221</dc:identifier>
<dc:source>EMBO Reports 10, 1213 (2009)</dc:source>
<dc:date>2009-10-16</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-16</prism:publicationDate>
<prism:doi>10.1038/embor.2009.221</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.221</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>1213</prism:startingPage>
<prism:endingPage>1219</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.221</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.223">
<title>Towards a small animal model for hepatitis C</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/QBD3dDxIVc0/embor.2009.223</link>
<description>Hepatitis C virus (HCV) causes chronic liver disease and affects an estimated 3% of the world's population. Options for the prevention or therapy of HCV infection are limited; there is no vaccine and the nonspecific, interferon-based treatments now in use are frequently ineffective and have </description>
<content:encoded><![CDATA[

<p>
<b>Towards a small animal model for hepatitis C</b>
</p>
<p>EMBO Reports 10, 1220 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.223">doi:10.1038/embor.2009.223</a>
</p>
<p>Authors: Alexander Ploss &amp; Charles M. Rice</p>
<p>Hepatitis C virus (HCV) causes chronic liver disease and affects an estimated 3% of the world's population. Options for the prevention or therapy of HCV infection are limited; there is no vaccine and the nonspecific, interferon-based treatments now in use are frequently ineffective and have </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/QBD3dDxIVc0" height="1" width="1"/>]]></content:encoded>
<dc:title>Towards a small animal model for hepatitis C</dc:title>
<dc:creator>Alexander Ploss</dc:creator>
<dc:creator>Charles M. Rice</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.223</dc:identifier>
<dc:source>EMBO Reports 10, 1220 (2009)</dc:source>
<dc:date>2009-10-16</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-16</prism:publicationDate>
<prism:doi>10.1038/embor.2009.223</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.223</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>1220</prism:startingPage>
<prism:endingPage>1227</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.223</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.202">
<title>Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/i3_Ju3o0YEw/embor.2009.202</link>
<description>V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report </description>
<content:encoded><![CDATA[

<p>
<b>Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase</b>
</p>
<p>EMBO Reports 10, 1228 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.202">doi:10.1038/embor.2009.202</a>
</p>
<p>Authors: Nobutaka Numoto, Yu Hasegawa, Kazuki Takeda &amp; Kunio Miki</p>
<p>V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/i3_Ju3o0YEw" height="1" width="1"/>]]></content:encoded>
<dc:title>Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase</dc:title>
<dc:creator>Nobutaka Numoto</dc:creator>
<dc:creator>Yu Hasegawa</dc:creator>
<dc:creator>Kazuki Takeda</dc:creator>
<dc:creator>Kunio Miki</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.202</dc:identifier>
<dc:source>EMBO Reports 10, 1228 (2009)</dc:source>
<dc:date>2009-09-25</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-09-25</prism:publicationDate>
<prism:doi>10.1038/embor.2009.202</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.202</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1228</prism:startingPage>
<prism:endingPage>1234</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.202</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.218">
<title>Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX–DNMT3–DNMT3L domain</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/rlVS1N1WI7s/embor.2009.218</link>
<description>DNMT3 proteins are de novo DNA methyltransferases that are responsible for the establishment of DNA methylation patterns in mammalian genomes. Here, we have determined the crystal structures of the ATRX–DNMT3–DNMT3L (ADD) domain of DNMT3A in an unliganded form and in a complex with the </description>
<content:encoded><![CDATA[

<p>
<b>Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX&#8211;DNMT3&#8211;DNMT3L domain</b>
</p>
<p>EMBO Reports 10, 1235 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.218">doi:10.1038/embor.2009.218</a>
</p>
<p>Authors: Junji Otani, Toshiyuki Nankumo, Kyohei Arita, Susumu Inamoto, Mariko Ariyoshi &amp; Masahiro Shirakawa</p>
<p>DNMT3 proteins are de novo DNA methyltransferases that are responsible for the establishment of DNA methylation patterns in mammalian genomes. Here, we have determined the crystal structures of the ATRX&#8211;DNMT3&#8211;DNMT3L (ADD) domain of DNMT3A in an unliganded form and in a complex with the </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/rlVS1N1WI7s" height="1" width="1"/>]]></content:encoded>
<dc:title>Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX–DNMT3–DNMT3L domain</dc:title>
<dc:creator>Junji Otani</dc:creator>
<dc:creator>Toshiyuki Nankumo</dc:creator>
<dc:creator>Kyohei Arita</dc:creator>
<dc:creator>Susumu Inamoto</dc:creator>
<dc:creator>Mariko Ariyoshi</dc:creator>
<dc:creator>Masahiro Shirakawa</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.218</dc:identifier>
<dc:source>EMBO Reports 10, 1235 (2009)</dc:source>
<dc:date>2009-10-16</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-16</prism:publicationDate>
<prism:doi>10.1038/embor.2009.218</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.218</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1235</prism:startingPage>
<prism:endingPage>1241</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.218</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.210">
<title>Helicobacter pylori CagA activates NF-κB by targeting TAK1 for TRAF6-mediated Lys 63 ubiquitination</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/osRDsqto69s/embor.2009.210</link>
<description>Helicobacter pylori-initiated chronic gastritis is characterized by the cag pathogenicity island-dependent upregulation of proinflammatory cytokines, which is largely mediated by the transcription factor nuclear factor (NF)-κB. However, the cag pathogenicity island-encoded proteins and cellular signalling molecules that are involved in H. pylori</description>
<content:encoded><![CDATA[

<p>
<b>Helicobacter pylori CagA activates NF-&#954;B by targeting TAK1 for TRAF6-mediated Lys 63 ubiquitination</b>
</p>
<p>EMBO Reports 10, 1242 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.210">doi:10.1038/embor.2009.210</a>
</p>
<p>Authors: Acacia Lamb, Xiao-Dong Yang, Ying-Hung N Tsang, Jiang-Dong Li, Hideaki Higashi, Masanori Hatakeyama, Richard M Peek, Steven R Blanke &amp; Lin-Feng Chen</p>
<p>Helicobacter pylori-initiated chronic gastritis is characterized by the cag pathogenicity island-dependent upregulation of proinflammatory cytokines, which is largely mediated by the transcription factor nuclear factor (NF)-&#954;B. However, the cag pathogenicity island-encoded proteins and cellular signalling molecules that are involved in H. pylori</p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/osRDsqto69s" height="1" width="1"/>]]></content:encoded>
<dc:title>Helicobacter pylori CagA activates NF-κB by targeting TAK1 for TRAF6-mediated Lys 63 ubiquitination</dc:title>
<dc:creator>Acacia Lamb</dc:creator>
<dc:creator>Xiao-Dong Yang</dc:creator>
<dc:creator>Ying-Hung N Tsang</dc:creator>
<dc:creator>Jiang-Dong Li</dc:creator>
<dc:creator>Hideaki Higashi</dc:creator>
<dc:creator>Masanori Hatakeyama</dc:creator>
<dc:creator>Richard M Peek</dc:creator>
<dc:creator>Steven R Blanke</dc:creator>
<dc:creator>Lin-Feng Chen</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.210</dc:identifier>
<dc:source>EMBO Reports 10, 1242 (2009)</dc:source>
<dc:date>2009-10-09</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-09</prism:publicationDate>
<prism:doi>10.1038/embor.2009.210</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.210</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1242</prism:startingPage>
<prism:endingPage>1249</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.210</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.192">
<title>Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/02w_N689EJk/embor.2009.192</link>
<description>Post-translational modification with ubiquitin is one of the most important mechanisms in the regulation of protein stability and function. However, the high reversibility of this modification is the main obstacle for the isolation and characterization of ubiquitylated proteins. To overcome this problem, we have developed </description>
<content:encoded><![CDATA[

<p>
<b>Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities</b>
</p>
<p>EMBO Reports 10, 1250 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.192">doi:10.1038/embor.2009.192</a>
</p>
<p>Authors: Roland Hjerpe, Fabienne Aillet, Fernando Lopitz-Otsoa, Valerie Lang, Patrick England &amp; Manuel S Rodriguez</p>
<p>Post-translational modification with ubiquitin is one of the most important mechanisms in the regulation of protein stability and function. However, the high reversibility of this modification is the main obstacle for the isolation and characterization of ubiquitylated proteins. To overcome this problem, we have developed </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/02w_N689EJk" height="1" width="1"/>]]></content:encoded>
<dc:title>Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities</dc:title>
<dc:creator>Roland Hjerpe</dc:creator>
<dc:creator>Fabienne Aillet</dc:creator>
<dc:creator>Fernando Lopitz-Otsoa</dc:creator>
<dc:creator>Valerie Lang</dc:creator>
<dc:creator>Patrick England</dc:creator>
<dc:creator>Manuel S Rodriguez</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.192</dc:identifier>
<dc:source>EMBO Reports 10, 1250 (2009)</dc:source>
<dc:date>2009-10-02</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-02</prism:publicationDate>
<prism:doi>10.1038/embor.2009.192</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.192</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1250</prism:startingPage>
<prism:endingPage>1258</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.192</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.201">
<title>Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/fIO_iN6RgWk/embor.2009.201</link>
<description>Recent studies have indicated that nuclear protein of 95 kDa (Np95) is essential for maintaining genomic methylation by recruiting DNA methyltransferase (Dnmt) 1 to hemi-methylated sites. Here, we show that Np95 interacts more strongly with regulatory domains of the de novo methyltransferases Dnmt3a and </description>
<content:encoded><![CDATA[

<p>
<b>Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells</b>
</p>
<p>EMBO Reports 10, 1259 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.201">doi:10.1038/embor.2009.201</a>
</p>
<p>Authors: Daniela Meilinger, Karin Fellinger, Sebastian Bultmann, Ulrich Rothbauer, Ian Marc Bonapace, Wolfgang E F Klinkert, Fabio Spada &amp; Heinrich Leonhardt</p>
<p>Recent studies have indicated that nuclear protein of 95 kDa (Np95) is essential for maintaining genomic methylation by recruiting DNA methyltransferase (Dnmt) 1 to hemi-methylated sites. Here, we show that Np95 interacts more strongly with regulatory domains of the de novo methyltransferases Dnmt3a and </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/fIO_iN6RgWk" height="1" width="1"/>]]></content:encoded>
<dc:title>Np95 interacts with de novo DNA methyltransferases, Dnmt3a and Dnmt3b, and mediates epigenetic silencing of the viral CMV promoter in embryonic stem cells</dc:title>
<dc:creator>Daniela Meilinger</dc:creator>
<dc:creator>Karin Fellinger</dc:creator>
<dc:creator>Sebastian Bultmann</dc:creator>
<dc:creator>Ulrich Rothbauer</dc:creator>
<dc:creator>Ian Marc Bonapace</dc:creator>
<dc:creator>Wolfgang E F Klinkert</dc:creator>
<dc:creator>Fabio Spada</dc:creator>
<dc:creator>Heinrich Leonhardt</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.201</dc:identifier>
<dc:source>EMBO Reports 10, 1259 (2009)</dc:source>
<dc:date>2009-10-02</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-02</prism:publicationDate>
<prism:doi>10.1038/embor.2009.201</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.201</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1259</prism:startingPage>
<prism:endingPage>1264</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.201</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.200">
<title>Upf1 stimulates degradation of the product derived from aberrant messenger RNA containing a specific nonsense mutation by the proteasome</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/OPxz8FlNuCg/embor.2009.200</link>
<description>Aberrant messenger RNAs containing a premature termination codon (PTC) are eliminated by the nonsense-mediated mRNA decay (NMD) pathway. Here, we show that a crucial NMD factor, up frameshift 1 protein (Upf1), is required for rapid proteasome-mediated degradation of an aberrant protein (PTC product) derived from </description>
<content:encoded><![CDATA[

<p>
<b>Upf1 stimulates degradation of the product derived from aberrant messenger RNA containing a specific nonsense mutation by the proteasome</b>
</p>
<p>EMBO Reports 10, 1265 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.200">doi:10.1038/embor.2009.200</a>
</p>
<p>Authors: Kazushige Kuroha, Tsuyako Tatematsu &amp; Toshifumi Inada</p>
<p>Aberrant messenger RNAs containing a premature termination codon (PTC) are eliminated by the nonsense-mediated mRNA decay (NMD) pathway. Here, we show that a crucial NMD factor, up frameshift 1 protein (Upf1), is required for rapid proteasome-mediated degradation of an aberrant protein (PTC product) derived from </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/OPxz8FlNuCg" height="1" width="1"/>]]></content:encoded>
<dc:title>Upf1 stimulates degradation of the product derived from aberrant messenger RNA containing a specific nonsense mutation by the proteasome</dc:title>
<dc:creator>Kazushige Kuroha</dc:creator>
<dc:creator>Tsuyako Tatematsu</dc:creator>
<dc:creator>Toshifumi Inada</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.200</dc:identifier>
<dc:source>EMBO Reports 10, 1265 (2009)</dc:source>
<dc:date>2009-10-02</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-10-02</prism:publicationDate>
<prism:doi>10.1038/embor.2009.200</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.200</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1265</prism:startingPage>
<prism:endingPage>1271</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/embor.2009.200</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/embor.2009.197">
<title>RelA/p65 functions to maintain cellular senescence by regulating genomic stability and DNA repair</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/k8xPaFBYKcI/embor.2009.197</link>
<description>Nuclear factor (NF)-κB is a positive regulator of tumour development and progression, but how it functions in normal cells leading to oncogenesis is not clear. As cellular senescence has proven to be an intrinsic tumour suppressor mechanism that cells must overcome to establish deregulated growth, </description>
<content:encoded><![CDATA[

<p>
<b>RelA/p65 functions to maintain cellular senescence by regulating genomic stability and DNA repair</b>
</p>
<p>EMBO Reports 10, 1272 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.197">doi:10.1038/embor.2009.197</a>
</p>
<p>Authors: Jingxin Wang, Naduparambil K Jacob, Katherine J Ladner, Amer Beg, James D Perko, Stephan M Tanner, Sandya Liyanarachchi, Richard Fishel &amp; Denis C Guttridge</p>
<p>Nuclear factor (NF)-&#954;B is a positive regulator of tumour development and progression, but how it functions in normal cells leading to oncogenesis is not clear. As cellular senescence has proven to be an intrinsic tumour suppressor mechanism that cells must overcome to establish deregulated growth, </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/k8xPaFBYKcI" height="1" width="1"/>]]></content:encoded>
<dc:title>RelA/p65 functions to maintain cellular senescence by regulating genomic stability and DNA repair</dc:title>
<dc:creator>Jingxin Wang</dc:creator>
<dc:creator>Naduparambil K Jacob</dc:creator>
<dc:creator>Katherine J Ladner</dc:creator>
<dc:creator>Amer Beg</dc:creator>
<dc:creator>James D Perko</dc:creator>
<dc:creator>Stephan M Tanner</dc:creator>
<dc:creator>Sandya Liyanarachchi</dc:creator>
<dc:creator>Richard Fishel</dc:creator>
<dc:creator>Denis C Guttridge</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.197</dc:identifier>
<dc:source>EMBO Reports 10, 1272 (2009)</dc:source>
<dc:date>2009-09-25</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-09-25</prism:publicationDate>
<prism:doi>10.1038/embor.2009.197</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.197</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Scientific Report</prism:section>
<prism:startingPage>1272</prism:startingPage>
<prism:endingPage>1278</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/embor.2009.220">
<title>The complexity of living: when biology meets theory. Conference on Systems Dynamics of Intracellular Communication</title>
<link>http://feeds.nature.com/~r/embor/rss/current/~3/yiBX3Nnbpks/embor.2009.220</link>
<description>EMBO reports (2009) 10: 953–957. doi:10.1038/embor.2009.195We regret that the above Meeting Report, printed in the September issue of the journal, contained an error in the discussion of N. Kam's (Rehovot, Israel) presentation concerning neuron response to </description>
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<p>
<b>The complexity of living: when biology meets theory. Conference on Systems Dynamics of Intracellular Communication</b>
</p>
<p>EMBO Reports 10, 1279 (2009). <a href="http://dx.doi.org/10.1038/embor.2009.220">doi:10.1038/embor.2009.220</a>
</p>
<p>Author: Sara Salinas &amp; Nir Gov</p>
<p>EMBO reports (2009) 10: 953&#8211;957. doi:10.1038/embor.2009.195We regret that the above Meeting Report, printed in the September issue of the journal, contained an error in the discussion of N. Kam's (Rehovot, Israel) presentation concerning neuron response to </p>
<img src="http://feeds.feedburner.com/~r/embor/rss/current/~4/yiBX3Nnbpks" height="1" width="1"/>]]></content:encoded>
<dc:title>The complexity of living: when biology meets theory. Conference on Systems Dynamics of Intracellular Communication</dc:title>
<dc:creator>Sara Salinas</dc:creator>
<dc:creator>Nir Gov</dc:creator>
<dc:identifier>doi:10.1038/embor.2009.220</dc:identifier>
<dc:source>EMBO Reports 10, 1279 (2009)</dc:source>
<dc:date>2009-09-25</dc:date>
<prism:publicationName>EMBO Reports</prism:publicationName>
<prism:publicationDate>2009-09-25</prism:publicationDate>
<prism:doi>10.1038/embor.2009.220</prism:doi>
<prism:url>http://dx.doi.org/10.1038/embor.2009.220</prism:url>
<prism:volume>10</prism:volume>
<prism:number>11</prism:number>
<prism:section>Review</prism:section>
<prism:startingPage>1279</prism:startingPage>
<prism:endingPage>1279</prism:endingPage>
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