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<description>Nature Chemical Biology is a monthly multidisciplinary journal providing an international forum for the timely publication of significant new research at the interface between chemistry and biology. Published in hard copy and online, Nature Chemical Biology is a medium for rapid publication and for the exchange of ideas between scientists in both the chemical and the life sciences.</description>
<link>http://www.nature.com/nchembio/current_issue/</link>
<dc:publisher>Nature Publishing Group</dc:publisher>
<dc:language>en</dc:language>
<dc:rights>&#169; 2008 Nature Publishing Group</dc:rights>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:issn>1552-4450</prism:issn>
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<title>Nature Chemical Biology</title>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-v">
<title>In this issue</title>
<link>http://dx.doi.org/10.1038/nchembio0908-v</link>
<description/>
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<p>
<b>In this issue</b>
</p>
<p>Nature Chemical Biology 4, v (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-v">doi:10.1038/nchembio0908-v</a>
</p>
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<dc:title>In this issue</dc:title>
<dc:identifier>doi:10.1038/nchembio0908-v</dc:identifier>
<dc:source>Nature Chemical Biology 4, v (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>In This Issue</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-509">
<title>The bottom line</title>
<link>http://dx.doi.org/10.1038/nchembio0908-509</link>
<description>Enhanced funding support and increased engagement of chemical biologists in the funding process are essential for the advancement of the field.</description>
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<p>
<b>The bottom line</b>
</p>
<p>Nature Chemical Biology 4, 509 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-509">doi:10.1038/nchembio0908-509</a>
</p>
<p>Enhanced funding support and increased engagement of chemical biologists in the funding process are essential for the advancement of the field.</p>
]]></content:encoded>
<dc:title>The bottom line</dc:title>
<dc:identifier>doi:10.1038/nchembio0908-509</dc:identifier>
<dc:source>Nature Chemical Biology 4, 509 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>Editorial</prism:section>
<prism:startingPage>509</prism:startingPage>
<prism:endingPage>509</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-511">
<title>Chemical biology at the US National Science Foundation</title>
<link>http://dx.doi.org/10.1038/nchembio0908-511</link>
<description>Chemical biology continues to grow and blur the theoretical and empirical boundaries between chemistry and biology. Federal funding agencies, including the US National Science Foundation, will be essential to support the development of interdisciplinary research fields.</description>
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<p>
<b>Chemical biology at the US National Science Foundation</b>
</p>
<p>Nature Chemical Biology 4, 511 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-511">doi:10.1038/nchembio0908-511</a>
</p>
<p>Authors: Wilfredo Col&#243;n, Parag Chitnis, James P Collins, Janice Hicks, Tony Chan
&amp; Joanne S Tornow</p>
<p>Chemical biology continues to grow and blur the theoretical and empirical boundaries between chemistry and biology. Federal funding agencies, including the US National Science Foundation, will be essential to support the development of interdisciplinary research fields.</p>
]]></content:encoded>
<dc:title>Chemical biology at the US National Science Foundation</dc:title>
<dc:creator>Wilfredo Col&#243;n</dc:creator>
<dc:creator>Parag Chitnis</dc:creator>
<dc:creator>James P Collins</dc:creator>
<dc:creator>Janice Hicks</dc:creator>
<dc:creator>Tony Chan</dc:creator>
<dc:creator>Joanne S Tornow</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-511</dc:identifier>
<dc:source>Nature Chemical Biology 4, 511 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>Commentary</prism:section>
<prism:startingPage>511</prism:startingPage>
<prism:endingPage>514</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-515">
<title>Chemical biology in China takes on signal transduction</title>
<link>http://dx.doi.org/10.1038/nchembio0908-515</link>
<description>Funding support for chemical biology is essential for its growth around the world. A new funding initiative from the National Natural Science Foundation of China provides a model of a targeted funding program in the area of signal transduction.</description>
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<p>
<b>Chemical biology in China takes on signal transduction</b>
</p>
<p>Nature Chemical Biology 4, 515 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-515">doi:10.1038/nchembio0908-515</a>
</p>
<p>Authors: Hualiang Jiang, Jiarui Wu, Lihe Zhang, Wenping Liang, Feixue Gao, Canping Du, Xuelian Feng
&amp; Yongjun Chen</p>
<p>Funding support for chemical biology is essential for its growth around the world. A new funding initiative from the National Natural Science Foundation of China provides a model of a targeted funding program in the area of signal transduction.</p>
]]></content:encoded>
<dc:title>Chemical biology in China takes on signal transduction</dc:title>
<dc:creator>Hualiang Jiang</dc:creator>
<dc:creator>Jiarui Wu</dc:creator>
<dc:creator>Lihe Zhang</dc:creator>
<dc:creator>Wenping Liang</dc:creator>
<dc:creator>Feixue Gao</dc:creator>
<dc:creator>Canping Du</dc:creator>
<dc:creator>Xuelian Feng</dc:creator>
<dc:creator>Yongjun Chen</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-515</dc:identifier>
<dc:source>Nature Chemical Biology 4, 515 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-519">
<title>Foundation funding and chemical biology</title>
<link>http://dx.doi.org/10.1038/nchembio0908-519</link>
<description>An emerging generation of scientists trained at the interface of chemistry and biology is providing new tools and insights into the workings of biological systems. Private foundations represent an important funding option for scientists at this interface.</description>
<content:encoded><![CDATA[

<p>
<b>Foundation funding and chemical biology</b>
</p>
<p>Nature Chemical Biology 4, 519 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-519">doi:10.1038/nchembio0908-519</a>
</p>
<p>Author: Victoria McGovern</p>
<p>An emerging generation of scientists trained at the interface of chemistry and biology is providing new tools and insights into the workings of biological systems. Private foundations represent an important funding option for scientists at this interface.</p>
]]></content:encoded>
<dc:title>Foundation funding and chemical biology</dc:title>
<dc:creator>Victoria McGovern</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-519</dc:identifier>
<dc:source>Nature Chemical Biology 4, 519 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
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<title>ERA-Chemistry</title>
<link>http://dx.doi.org/10.1038/nchembio0908-523</link>
<description>European Research Area (ERA)-Chemistry is a network of funding agencies that supports international collaborative approaches to chemical research and facilitates the flow of ideas from scientists to funding institutions.</description>
<content:encoded><![CDATA[

<p>
<b>ERA-Chemistry</b>
</p>
<p>Nature Chemical Biology 4, 523 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-523">doi:10.1038/nchembio0908-523</a>
</p>
<p>Author: Amy Donner</p>
<p>European Research Area (ERA)-Chemistry is a network of funding agencies that supports international collaborative approaches to chemical research and facilitates the flow of ideas from scientists to funding institutions.</p>
]]></content:encoded>
<dc:title>ERA-Chemistry</dc:title>
<dc:creator>Amy Donner</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-523</dc:identifier>
<dc:source>Nature Chemical Biology 4, 523 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>Elements</prism:section>
<prism:startingPage>523</prism:startingPage>
<prism:endingPage>523</prism:endingPage>
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<title>From yeast to alkaloids</title>
<link>http://dx.doi.org/10.1038/nchembio0908-524</link>
<description>Alkaloids, which include caffeine and morphine, are a large class of pharmacologically active plant compounds that are often difficult to chemically synthesize. Incorporation of benzylisoquinoline alkaloid pathways in yeast will facilitate the production of natural and non-natural alkaloids.</description>
<content:encoded><![CDATA[

<p>
<b>From yeast to alkaloids</b>
</p>
<p>Nature Chemical Biology 4, 524 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-524">doi:10.1038/nchembio0908-524</a>
</p>
<p>Author: Jay Keasling</p>
<p>Alkaloids, which include caffeine and morphine, are a large class of pharmacologically active plant compounds that are often difficult to chemically synthesize. Incorporation of benzylisoquinoline alkaloid pathways in yeast will facilitate the production of natural and non-natural alkaloids.</p>
]]></content:encoded>
<dc:title>From yeast to alkaloids</dc:title>
<dc:creator>Jay Keasling</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-524</dc:identifier>
<dc:source>Nature Chemical Biology 4, 524 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>524</prism:startingPage>
<prism:endingPage>525</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-525">
<title>Unexpected N-terminal editing: a cysteine protease that cuts and pastes</title>
<link>http://dx.doi.org/10.1038/nchembio0908-525</link>
<description>N-terminal modification is a mechanism for regulation of protein activity, localization and degradation. A proteomic approach using &#946;-lactone activity-based probes has identified a cysteine protease with N-terminal transpeptidase activity.</description>
<content:encoded><![CDATA[

<p>
<b>Unexpected N-terminal editing: a cysteine protease that cuts and pastes</b>
</p>
<p>Nature Chemical Biology 4, 525 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-525">doi:10.1038/nchembio0908-525</a>
</p>
<p>Author: Isaac Carrico</p>
<p>N-terminal modification is a mechanism for regulation of protein activity, localization and degradation. A proteomic approach using &#946;-lactone activity-based probes has identified a cysteine protease with N-terminal transpeptidase activity.</p>
]]></content:encoded>
<dc:title>Unexpected N-terminal editing: a cysteine protease that cuts and pastes</dc:title>
<dc:creator>Isaac Carrico</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-525</dc:identifier>
<dc:source>Nature Chemical Biology 4, 525 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>525</prism:startingPage>
<prism:endingPage>526</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-527">
<title>Cross-dressing proteins by olefin metathesis</title>
<link>http://dx.doi.org/10.1038/nchembio0908-527</link>
<description>Chemists have established numerous methods for performing protein conjugations, but metathesis catalysts have largely remained absent from this toolkit. Evidence that proteins bearing allylsulfides undergo cross-metathesis with chosen alkenes in aqueous conditions will allow chemists to harness the power of metathesis catalysts for modifying biomolecules and other water-soluble compounds.</description>
<content:encoded><![CDATA[

<p>
<b>Cross-dressing proteins by olefin metathesis</b>
</p>
<p>Nature Chemical Biology 4, 527 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-527">doi:10.1038/nchembio0908-527</a>
</p>
<p>Authors: Kent Kirshenbaum
&amp; Paramjit S Arora</p>
<p>Chemists have established numerous methods for performing protein conjugations, but metathesis catalysts have largely remained absent from this toolkit. Evidence that proteins bearing allylsulfides undergo cross-metathesis with chosen alkenes in aqueous conditions will allow chemists to harness the power of metathesis catalysts for modifying biomolecules and other water-soluble compounds.</p>
]]></content:encoded>
<dc:title>Cross-dressing proteins by olefin metathesis</dc:title>
<dc:creator>Kent Kirshenbaum</dc:creator>
<dc:creator>Paramjit S Arora</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-527</dc:identifier>
<dc:source>Nature Chemical Biology 4, 527 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>527</prism:startingPage>
<prism:endingPage>528</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-528">
<title>20S ways to apoptosis</title>
<link>http://dx.doi.org/10.1038/nchembio0908-528</link>
<description>Chemical inhibitors of the proteasome have received substantial attention owing to the success of bortezomib in the treatment of multiple myeloma. A recent whole-cell screen identified the proteasome inhibitor argyrin A and suggests a new role for p27Kip-1 in regulating apoptosis.</description>
<content:encoded><![CDATA[

<p>
<b>20S ways to apoptosis</b>
</p>
<p>Nature Chemical Biology 4, 528 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-528">doi:10.1038/nchembio0908-528</a>
</p>
<p>Author: David J McConkey</p>
<p>Chemical inhibitors of the proteasome have received substantial attention owing to the success of bortezomib in the treatment of multiple myeloma. A recent whole-cell screen identified the proteasome inhibitor argyrin A and suggests a new role for p27Kip-1 in regulating apoptosis.</p>
]]></content:encoded>
<dc:title>20S ways to apoptosis</dc:title>
<dc:creator>David J McConkey</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-528</dc:identifier>
<dc:source>Nature Chemical Biology 4, 528 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>528</prism:startingPage>
<prism:endingPage>529</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-529">
<title>Chloroplast SRP takes another road</title>
<link>http://dx.doi.org/10.1038/nchembio0908-529</link>
<description>The signal recognition particle (SRP), a ribonucleoprotein complex that is conserved across all organisms, is essential for cotranslational insertion of proteins into membranes. A three-dimensional structure of cpSRP43 provides insights into how plants have adapted the SRP for post-translational targeting of membrane proteins.</description>
<content:encoded><![CDATA[

<p>
<b>Chloroplast SRP takes another road</b>
</p>
<p>Nature Chemical Biology 4, 529 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-529">doi:10.1038/nchembio0908-529</a>
</p>
<p>Author: Laurent Nussaume</p>
<p>The signal recognition particle (SRP), a ribonucleoprotein complex that is conserved across all organisms, is essential for cotranslational insertion of proteins into membranes. A three-dimensional structure of cpSRP43 provides insights into how plants have adapted the SRP for post-translational targeting of membrane proteins.</p>
]]></content:encoded>
<dc:title>Chloroplast SRP takes another road</dc:title>
<dc:creator>Laurent Nussaume</dc:creator>
<dc:identifier>doi:10.1038/nchembio0908-529</dc:identifier>
<dc:source>Nature Chemical Biology 4, 529 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>529</prism:startingPage>
<prism:endingPage>531</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nchembio0908-533">
<title>Research highlights</title>
<link>http://dx.doi.org/10.1038/nchembio0908-533</link>
<description/>
<content:encoded><![CDATA[

<p>
<b>Research highlights</b>
</p>
<p>Nature Chemical Biology 4, 533 (2008). <a href="http://dx.doi.org/10.1038/nchembio0908-533">doi:10.1038/nchembio0908-533</a>
</p>
]]></content:encoded>
<dc:title>Research highlights</dc:title>
<dc:identifier>doi:10.1038/nchembio0908-533</dc:identifier>
<dc:source>Nature Chemical Biology 4, 533 (2008)</dc:source>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>News and Views</prism:section>
<prism:startingPage>533</prism:startingPage>
<prism:endingPage>533</prism:endingPage>
</item>
<item rdf:about="http://dx.doi.org/10.1038/nchembio.107">
<title>Biomimetic synthesis of the IDO inhibitors exiguamine A and B</title>
<link>http://dx.doi.org/10.1038/nchembio.107</link>
<description>Biomimetic synthesis is an attempt to assemble natural products along biosynthetic lines without recourse to the full enzymatic machinery of nature. We exemplify this with a total synthesis of exiguamine A and the newly isolated natural product exiguamine B. The most noteworthy feature of this work is an oxidative endgame drawing from the complex chemistry of catecholamines, which allows for ready access to a new class of nanomolar indoleamine-2,3-dioxygenase inhibitors.</description>
<content:encoded><![CDATA[

<p>
<b>Biomimetic synthesis of the IDO inhibitors exiguamine A and B</b>
</p>
<p>Nature Chemical Biology 4, 535 (2008). <a href="http://dx.doi.org/10.1038/nchembio.107">doi:10.1038/nchembio.107</a>
</p>
<p>Authors: Matthew Volgraf, Jean-Philip Lumb, Harry C Brastianos, Gavin Carr, Marco K W Chung, Martin M&#252;nzel, A Grant Mauk, Raymond J Andersen
&amp; Dirk Trauner</p>
<p>Biomimetic synthesis is an attempt to assemble natural products along biosynthetic lines without recourse to the full enzymatic machinery of nature. We exemplify this with a total synthesis of exiguamine A and the newly isolated natural product exiguamine B. The most noteworthy feature of this work is an oxidative endgame drawing from the complex chemistry of catecholamines, which allows for ready access to a new class of nanomolar indoleamine-2,3-dioxygenase inhibitors.</p>
]]></content:encoded>
<dc:title>Biomimetic synthesis of the IDO inhibitors exiguamine A and B</dc:title>
<dc:creator>Matthew Volgraf</dc:creator>
<dc:creator>Jean-Philip Lumb</dc:creator>
<dc:creator>Harry C Brastianos</dc:creator>
<dc:creator>Gavin Carr</dc:creator>
<dc:creator>Marco K W Chung</dc:creator>
<dc:creator>Martin M&#252;nzel</dc:creator>
<dc:creator>A Grant Mauk</dc:creator>
<dc:creator>Raymond J Andersen</dc:creator>
<dc:creator>Dirk Trauner</dc:creator>
<dc:identifier>doi:10.1038/nchembio.107</dc:identifier>
<dc:source>Nature Chemical Biology 4, 535 (2008)</dc:source>
<dc:date>2008-08-01</dc:date>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:publicationDate>2008-08-01</prism:publicationDate>
<prism:volume>4</prism:volume>
<prism:number>9</prism:number>
<prism:section>Brief Communication</prism:section>
<prism:startingPage>535</prism:startingPage>
<prism:endingPage>537</prism:endingPage>
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<item rdf:about="http://dx.doi.org/10.1038/nchembio.103">
<title>Raft nanodomains contribute to Akt/PKB plasma membrane recruitment and activation</title>
<link>http://dx.doi.org/10.1038/nchembio.103</link>
<description/>
<content:encoded><![CDATA[

<p>
<b>Raft nanodomains contribute to Akt/PKB plasma membrane recruitment and activation</b>
</p>
<p>Nature Chemical Biology 4, 538 (2008). <a href="http://dx.doi.org/10.1038/nchembio.103">doi:10.1038/nchembio.103</a>
</p>
<p>Authors: R&#233;mi Lasserre, Xiao-Jun Guo, Fabien Conchonaud, Yannick Hamon, Omar Hawchar, Anne-Marie Bernard, Sa&#239;di M'Homa Soudja, Pierre-Fran&#231;ois Lenne, Herv&#233; Rigneault, Daniel Olive, Georges Bismuth, Jacques A Nun&#232;s, Bernard Payrastre, Didier Marguet
&amp; Hai-Tao He</p>
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<dc:creator>Fabien Conchonaud</dc:creator>
<dc:creator>Yannick Hamon</dc:creator>
<dc:creator>Omar Hawchar</dc:creator>
<dc:creator>Anne-Marie Bernard</dc:creator>
<dc:creator>Sa&#239;di M'Homa Soudja</dc:creator>
<dc:creator>Pierre-Fran&#231;ois Lenne</dc:creator>
<dc:creator>Herv&#233; Rigneault</dc:creator>
<dc:creator>Daniel Olive</dc:creator>
<dc:creator>Georges Bismuth</dc:creator>
<dc:creator>Jacques A Nun&#232;s</dc:creator>
<dc:creator>Bernard Payrastre</dc:creator>
<dc:creator>Didier Marguet</dc:creator>
<dc:creator>Hai-Tao He</dc:creator>
<dc:identifier>doi:10.1038/nchembio.103</dc:identifier>
<dc:source>Nature Chemical Biology 4, 538 (2008)</dc:source>
<dc:date>2008-07-20</dc:date>
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<title>Cytosporone B is an agonist for nuclear orphan receptor Nur77</title>
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<p>
<b>Cytosporone B is an agonist for nuclear orphan receptor Nur77</b>
</p>
<p>Nature Chemical Biology 4, 548 (2008). <a href="http://dx.doi.org/10.1038/nchembio.106">doi:10.1038/nchembio.106</a>
</p>
<p>Authors: Yanyan Zhan, Xiping Du, Hangzi Chen, Jingjing Liu, Bixing Zhao, Danhong Huang, Guideng Li, Qingyan Xu, Mingqing Zhang, Bart C Weimer, Dong Chen, Zhe Cheng, Lianru Zhang, Qinxi Li, Shaowei Li, Zhonghui Zheng, Siyang Song, Yaojian Huang, Zhiyun Ye, Wenjin Su, Sheng-Cai Lin, Yuemao Shen
&amp; Qiao Wu</p>
]]></content:encoded>
<dc:title>Cytosporone B is an agonist for nuclear orphan receptor Nur77</dc:title>
<dc:creator>Yanyan Zhan</dc:creator>
<dc:creator>Xiping Du</dc:creator>
<dc:creator>Hangzi Chen</dc:creator>
<dc:creator>Jingjing Liu</dc:creator>
<dc:creator>Bixing Zhao</dc:creator>
<dc:creator>Danhong Huang</dc:creator>
<dc:creator>Guideng Li</dc:creator>
<dc:creator>Qingyan Xu</dc:creator>
<dc:creator>Mingqing Zhang</dc:creator>
<dc:creator>Bart C Weimer</dc:creator>
<dc:creator>Dong Chen</dc:creator>
<dc:creator>Zhe Cheng</dc:creator>
<dc:creator>Lianru Zhang</dc:creator>
<dc:creator>Qinxi Li</dc:creator>
<dc:creator>Shaowei Li</dc:creator>
<dc:creator>Zhonghui Zheng</dc:creator>
<dc:creator>Siyang Song</dc:creator>
<dc:creator>Yaojian Huang</dc:creator>
<dc:creator>Zhiyun Ye</dc:creator>
<dc:creator>Wenjin Su</dc:creator>
<dc:creator>Sheng-Cai Lin</dc:creator>
<dc:creator>Yuemao Shen</dc:creator>
<dc:creator>Qiao Wu</dc:creator>
<dc:identifier>doi:10.1038/nchembio.106</dc:identifier>
<dc:source>Nature Chemical Biology 4, 548 (2008)</dc:source>
<dc:date>2008-08-10</dc:date>
<prism:publicationName>Nature Chemical Biology</prism:publicationName>
<prism:publicationDate>2008-08-10</prism:publicationDate>
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<title>&#946;-Lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana</title>
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<p>
<b>&#946;-Lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana</b>
</p>
<p>Nature Chemical Biology 4, 557 (2008). <a href="http://dx.doi.org/10.1038/nchembio.104">doi:10.1038/nchembio.104</a>
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<p>Authors: Zheming Wang, Christian Gu, Tom Colby, Takayuki Shindo, Rengarajan Balamurugan, Herbert Waldmann, Markus Kaiser
&amp; Renier A L van der Hoorn</p>
]]></content:encoded>
<dc:title>&#946;-Lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana</dc:title>
<dc:creator>Zheming Wang</dc:creator>
<dc:creator>Christian Gu</dc:creator>
<dc:creator>Tom Colby</dc:creator>
<dc:creator>Takayuki Shindo</dc:creator>
<dc:creator>Rengarajan Balamurugan</dc:creator>
<dc:creator>Herbert Waldmann</dc:creator>
<dc:creator>Markus Kaiser</dc:creator>
<dc:creator>Renier A L van der Hoorn</dc:creator>
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<dc:source>Nature Chemical Biology 4, 557 (2008)</dc:source>
<dc:date>2008-07-27</dc:date>
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<p>
<b>Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae</b>
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<p>Nature Chemical Biology 4, 564 (2008). <a href="http://dx.doi.org/10.1038/nchembio.105">doi:10.1038/nchembio.105</a>
</p>
<p>Authors: Kristy M Hawkins
&amp; Christina D Smolke</p>
]]></content:encoded>
<dc:title>Production of benzylisoquinoline alkaloids in Saccharomyces cerevisiae</dc:title>
<dc:creator>Kristy M Hawkins</dc:creator>
<dc:creator>Christina D Smolke</dc:creator>
<dc:identifier>doi:10.1038/nchembio.105</dc:identifier>
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