Fused-ring structure of decahydroisoquinolin as a novel scaffold for SARS 3CL protease inhibitors.
Identifieur interne : 000E73 ( PubMed/Corpus ); précédent : 000E72; suivant : 000E74Fused-ring structure of decahydroisoquinolin as a novel scaffold for SARS 3CL protease inhibitors.
Auteurs : Yasuhiro Shimamoto ; Yasunao Hattori ; Kazuya Kobayashi ; Kenta Teruya ; Akira Sanjoh ; Atsushi Nakagawa ; Eiki Yamashita ; Kenichi AkajiSource :
- Bioorganic & medicinal chemistry [ 1464-3391 ] ; 2015.
English descriptors
- KwdEn :
- Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Chymases (antagonists & inhibitors), Chymases (chemistry), Chymases (metabolism), Crystallography, X-Ray, Humans, Isoquinolines (chemistry), Isoquinolines (pharmacology), Molecular Docking Simulation, Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), SARS Virus (chemistry), SARS Virus (drug effects), SARS Virus (enzymology), Severe Acute Respiratory Syndrome (drug therapy), Severe Acute Respiratory Syndrome (virology).
- MESH :
- chemical , antagonists & inhibitors : Chymases.
- chemical , chemistry : Antiviral Agents, Chymases, Isoquinolines, Protease Inhibitors.
- chemical , metabolism : Chymases.
- chemical , pharmacology : Antiviral Agents, Isoquinolines, Protease Inhibitors.
- chemistry : SARS Virus.
- drug effects : SARS Virus.
- drug therapy : Severe Acute Respiratory Syndrome.
- enzymology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Crystallography, X-Ray, Humans, Molecular Docking Simulation.
Abstract
The design and evaluation of a novel decahydroisoquinolin scaffold as an inhibitor for severe acute respiratory syndrome (SARS) chymotrypsin-like protease (3CL(pro)) are described. Focusing on hydrophobic interactions at the S2 site, the decahydroisoquinolin scaffold was designed by connecting the P2 site cyclohexyl group of the substrate-based inhibitor to the main-chain at the α-nitrogen atom of the P2 position via a methylene linker. Starting from a cyclohexene enantiomer obtained by salt resolution, trans-decahydroisoquinolin derivatives were synthesized. All decahydroisoquinolin inhibitors synthesized showed moderate but clear inhibitory activities for SARS 3CL(pro), which confirmed the fused ring structure of the decahydroisoquinolin functions as a novel scaffold for SARS 3CL(pro) inhibitor. X-ray crystallographic analyses of the SARS 3CL(pro) in a complex with the decahydroisoquinolin inhibitor revealed the expected interactions at the S1 and S2 sites, as well as additional interactions at the N-substituent of the inhibitor.
DOI: 10.1016/j.bmc.2014.12.028
PubMed: 25614110
Links to Exploration step
pubmed:25614110Le document en format XML
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Electronic address: akaji@mb.kyoto-phu.ac.jp.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Bioorganic & medicinal chemistry</title><idno type="eISSN">1464-3391</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (chemistry)</term><term>Antiviral Agents (pharmacology)</term><term>Chymases (antagonists & inhibitors)</term><term>Chymases (chemistry)</term><term>Chymases (metabolism)</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Isoquinolines (chemistry)</term><term>Isoquinolines (pharmacology)</term><term>Molecular Docking Simulation</term><term>Protease Inhibitors (chemistry)</term><term>Protease Inhibitors (pharmacology)</term><term>SARS Virus (chemistry)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (enzymology)</term><term>Severe Acute Respiratory Syndrome (drug therapy)</term><term>Severe Acute Respiratory Syndrome (virology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Chymases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term><term>Chymases</term><term>Isoquinolines</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chymases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Isoquinolines</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Humans</term><term>Molecular Docking Simulation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The design and evaluation of a novel decahydroisoquinolin scaffold as an inhibitor for severe acute respiratory syndrome (SARS) chymotrypsin-like protease (3CL(pro)) are described. Focusing on hydrophobic interactions at the S2 site, the decahydroisoquinolin scaffold was designed by connecting the P2 site cyclohexyl group of the substrate-based inhibitor to the main-chain at the α-nitrogen atom of the P2 position via a methylene linker. Starting from a cyclohexene enantiomer obtained by salt resolution, trans-decahydroisoquinolin derivatives were synthesized. All decahydroisoquinolin inhibitors synthesized showed moderate but clear inhibitory activities for SARS 3CL(pro), which confirmed the fused ring structure of the decahydroisoquinolin functions as a novel scaffold for SARS 3CL(pro) inhibitor. X-ray crystallographic analyses of the SARS 3CL(pro) in a complex with the decahydroisoquinolin inhibitor revealed the expected interactions at the S1 and S2 sites, as well as additional interactions at the N-substituent of the inhibitor. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25614110</PMID><DateCompleted><Year>2015</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1464-3391</ISSN><JournalIssue CitedMedium="Internet"><Volume>23</Volume><Issue>4</Issue><PubDate><Year>2015</Year><Month>Feb</Month><Day>15</Day></PubDate></JournalIssue><Title>Bioorganic & medicinal chemistry</Title><ISOAbbreviation>Bioorg. Med. Chem.</ISOAbbreviation></Journal><ArticleTitle>Fused-ring structure of decahydroisoquinolin as a novel scaffold for SARS 3CL protease inhibitors.</ArticleTitle><Pagination><MedlinePgn>876-90</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bmc.2014.12.028</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0968-0896(14)00876-1</ELocationID><Abstract><AbstractText>The design and evaluation of a novel decahydroisoquinolin scaffold as an inhibitor for severe acute respiratory syndrome (SARS) chymotrypsin-like protease (3CL(pro)) are described. Focusing on hydrophobic interactions at the S2 site, the decahydroisoquinolin scaffold was designed by connecting the P2 site cyclohexyl group of the substrate-based inhibitor to the main-chain at the α-nitrogen atom of the P2 position via a methylene linker. Starting from a cyclohexene enantiomer obtained by salt resolution, trans-decahydroisoquinolin derivatives were synthesized. All decahydroisoquinolin inhibitors synthesized showed moderate but clear inhibitory activities for SARS 3CL(pro), which confirmed the fused ring structure of the decahydroisoquinolin functions as a novel scaffold for SARS 3CL(pro) inhibitor. X-ray crystallographic analyses of the SARS 3CL(pro) in a complex with the decahydroisoquinolin inhibitor revealed the expected interactions at the S1 and S2 sites, as well as additional interactions at the N-substituent of the inhibitor. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shimamoto</LastName><ForeName>Yasuhiro</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hattori</LastName><ForeName>Yasunao</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kobayashi</LastName><ForeName>Kazuya</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Teruya</LastName><ForeName>Kenta</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Sakyo-ku, Kyoto 606-0823, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sanjoh</LastName><ForeName>Akira</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>R&D Center, Protein Wave Co., Nara 631-0006, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakagawa</LastName><ForeName>Atsushi</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamashita</LastName><ForeName>Eiki</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Akaji</LastName><ForeName>Kenichi</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan. Electronic address: akaji@mb.kyoto-phu.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>12</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Bioorg Med Chem</MedlineTA><NlmUniqueID>9413298</NlmUniqueID><ISSNLinking>0968-0896</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007546">Isoquinolines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.39</RegistryNumber><NameOfSubstance UI="D053818">Chymases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053818" MajorTopicYN="N">Chymases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007546" MajorTopicYN="N">Isoquinolines</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000188" MajorTopicYN="N">drug therapy</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Decahydroisoquinolin</Keyword><Keyword MajorTopicYN="N">Hydrophobic interaction</Keyword><Keyword MajorTopicYN="N">Inhibitor</Keyword><Keyword MajorTopicYN="N">SARS 3CL protease</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>11</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>12</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>12</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>10</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25614110</ArticleId><ArticleId IdType="pii">S0968-0896(14)00876-1</ArticleId><ArticleId IdType="doi">10.1016/j.bmc.2014.12.028</ArticleId><ArticleId IdType="pmc">PMC7111320</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):22-5</Citation><ArticleIdList><ArticleId IdType="pubmed">20057045</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem. 2014 Jan 1;22(1):167-77</Citation><ArticleIdList><ArticleId IdType="pubmed">24332657</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Cell. 2013 Apr;4(4):248-50</Citation><ArticleIdList><ArticleId IdType="pubmed">23549610</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Comput Chem. 2004 Oct;25(13):1605-12</Citation><ArticleIdList><ArticleId IdType="pubmed">15264254</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2011 Dec 8;54(23):7962-73</Citation><ArticleIdList><ArticleId IdType="pubmed">22014094</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2013 Jan 24;56(2):534-46</Citation><ArticleIdList><ArticleId IdType="pubmed">23231439</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2006 Feb 9;49(3):1066-79</Citation><ArticleIdList><ArticleId IdType="pubmed">16451072</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem. 2008 Nov 1;16(21):9400-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18845442</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 Jun 13;300(5626):1763-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12746549</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Gen Virol. 2003 Sep;84(Pt 9):2305-2315</Citation><ArticleIdList><ArticleId IdType="pubmed">12917450</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2010 Mar 15;20(6):1873-6</Citation><ArticleIdList><ArticleId IdType="pubmed">20167482</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Org Lett. 2003 Jan 9;5(1):27-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12509882</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):14040-5</Citation><ArticleIdList><ArticleId IdType="pubmed">16169905</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2013 Nov;87(21):11955-62</Citation><ArticleIdList><ArticleId IdType="pubmed">23986593</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Med Chem. 2013 Jul;65:436-47</Citation><ArticleIdList><ArticleId IdType="pubmed">23747811</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem. 2014 Jan 1;22(1):292-302</Citation><ArticleIdList><ArticleId IdType="pubmed">24316352</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):431-40</Citation><ArticleIdList><ArticleId IdType="pubmed">22505263</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42</Citation><ArticleIdList><ArticleId IdType="pubmed">21460441</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jan 16;279(3):1637-42</Citation><ArticleIdList><ArticleId IdType="pubmed">14561748</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem. 2013 Jul 1;21(13):3730-7</Citation><ArticleIdList><ArticleId IdType="pubmed">23647823</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240-55</Citation><ArticleIdList><ArticleId IdType="pubmed">15299926</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2006 Feb 9;49(3):1140-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16451078</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2007 May 1;17(9):2470-3</Citation><ArticleIdList><ArticleId IdType="pubmed">17336519</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2007 Aug 23;50(17):4087-95</Citation><ArticleIdList><ArticleId IdType="pubmed">17663539</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem. 2010 Nov 15;18(22):7849-54</Citation><ArticleIdList><ArticleId IdType="pubmed">20947359</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation><ArticleIdList><ArticleId IdType="pubmed">12690091</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2009 May 15;19(10):2722-7</Citation><ArticleIdList><ArticleId IdType="pubmed">19362479</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation><ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 2007 Nov 1;17(21):5876-80</Citation><ArticleIdList><ArticleId IdType="pubmed">17855091</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation><ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2005 Oct 28;310(5748):676-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16195424</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Med Chem. 2006 May 4;49(9):2845-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16640347</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Med Chem. 2013 Jan;59:1-6</Citation><ArticleIdList><ArticleId IdType="pubmed">23202846</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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|étape= Corpus
|type= RBID
|clé= pubmed:25614110
|texte= Fused-ring structure of decahydroisoquinolin as a novel scaffold for SARS 3CL protease inhibitors.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:25614110" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |