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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Activation and maturation of SARS-CoV main protease</title><author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author><author><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21533772</idno><idno type="pmc">4875205</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4875205</idno><idno type="RBID">PMC:4875205</idno><idno type="doi">10.1007/s13238-011-1034-1</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000169</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000169</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Activation and maturation of SARS-CoV main protease</title><author><name sortKey="Xia, Bin" sort="Xia, Bin" uniqKey="Xia B" first="Bin" last="Xia">Bin Xia</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author><author><name sortKey="Kang, Xue" sort="Kang, Xue" uniqKey="Kang X" first="Xue" last="Kang">Xue Kang</name><affiliation><nlm:aff id="Aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">Protein & Cell</title><idno type="ISSN">1674-800X</idno><idno type="eISSN">1674-8018</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M<sup>pro</sup>) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M<sup>pro</sup> is first auto-cleaved out of polyproteins. The monomeric form of M<sup>pro</sup> is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M<sup>pro</sup> over the past years.</p></div></front></TEI><pmc article-type="review-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Protein Cell</journal-id><journal-id journal-id-type="iso-abbrev">Protein Cell</journal-id><journal-title-group><journal-title>Protein & Cell</journal-title></journal-title-group><issn pub-type="ppub">1674-800X</issn><issn pub-type="epub">1674-8018</issn><publisher><publisher-name>Higher Education Press</publisher-name><publisher-loc>Beijing</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21533772</article-id><article-id pub-id-type="pmc">4875205</article-id><article-id pub-id-type="publisher-id">1034</article-id><article-id pub-id-type="doi">10.1007/s13238-011-1034-1</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Activation and maturation of SARS-CoV main protease</article-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Xia</surname><given-names>Bin</given-names></name><address><email>binxia@pku.edu.cn</email></address><xref ref-type="aff" rid="Aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Kang</surname><given-names>Xue</given-names></name><xref ref-type="aff" rid="Aff1"></xref></contrib><aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.11135.37</institution-id><institution-id institution-id-type="ISNI">0000000122569319</institution-id><institution>Beijing Nuclear Magnetic Resonance Center, College of Chemistry and Molecular Engineering, and School of Life Sciences,</institution><institution>Peking University,</institution></institution-wrap>Beijing, 100871 China</aff></contrib-group><pub-date pub-type="epub"><day>28</day><month>4</month><year>2011</year></pub-date><pub-date pub-type="ppub"><month>4</month><year>2011</year></pub-date><volume>2</volume><issue>4</issue><fpage>282</fpage><lpage>290</lpage><history><date date-type="received"><day>21</day><month>3</month><year>2011</year></date><date date-type="accepted"><day>7</day><month>4</month><year>2011</year></date></history><permissions><copyright-statement>© Higher Education Press and Springer-Verlag Berlin Heidelberg 2011</copyright-statement></permissions><abstract id="Abs1"><p>The worldwide outbreak of the severe acute respiratory syndrome (SARS) in 2003 was due to the transmission of SARS coronavirus (SARS-CoV). The main protease (M<sup>pro</sup>) of SARS-CoV is essential for the viral life cycle, and is considered to be an attractive target of anti-SARS drug development. As a key enzyme for proteolytic processing of viral polyproteins to produce functional non-structure proteins, M<sup>pro</sup> is first auto-cleaved out of polyproteins. The monomeric form of M<sup>pro</sup> is enzymatically inactive, and it is activated through homo-dimerization which is strongly affected by extra residues to both ends of the mature enzyme. This review provides a summary of the related literatures on the study of the quaternary structure, activation, and self-maturation of M<sup>pro</sup> over the past years.</p></abstract><kwd-group xml:lang="en"><title>Keywords</title><kwd>severe acute respiratory syndrome</kwd><kwd>M<sup>pro</sup></kwd><kwd>structure</kwd><kwd>dimerization</kwd></kwd-group><custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name><meta-value>© HEP and Springer 2011</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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