Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
Identifieur interne : 001B19 ( PubMed/Curation ); précédent : 001B18; suivant : 001B20Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.
Auteurs : Berend Jan Bosch [Pays-Bas] ; Willem Bartelink ; Peter J M. RottierSource :
- Journal of virology [ 1098-5514 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cathepsine L, Cathepsines (métabolisme), Cathepsines (pharmacologie), Cellules Vero, Concentration en ions d'hydrogène, Cysteine endopeptidases (métabolisme), Cysteine endopeptidases (pharmacologie), Facteurs temps, Peptides (métabolisme), Plasmides, Protéines de fusion virale (), Protéines de fusion virale (métabolisme), Protéines à fluorescence verte (métabolisme), Température, Transfection, Trypsine (pharmacologie), Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Cathepsines, Cysteine endopeptidases, Peptides, Protéines de fusion virale, Protéines à fluorescence verte, Virus du SRAS.
- pharmacologie : Cathepsines, Cysteine endopeptidases, Trypsine.
- Animaux, Cathepsine L, Cellules Vero, Concentration en ions d'hydrogène, Facteurs temps, Plasmides, Protéines de fusion virale, Température, Transfection.
English descriptors
- KwdEn :
- Animals, Cathepsin L, Cathepsins (metabolism), Cathepsins (pharmacology), Chlorocebus aethiops, Cysteine Endopeptidases (metabolism), Cysteine Endopeptidases (pharmacology), Green Fluorescent Proteins (metabolism), Hydrogen-Ion Concentration, Peptides (metabolism), Plasmids, SARS Virus (metabolism), Temperature, Time Factors, Transfection, Trypsin (pharmacology), Vero Cells, Viral Fusion Proteins (classification), Viral Fusion Proteins (metabolism).
- MESH :
- chemical , classification : Viral Fusion Proteins.
- chemical , metabolism : Cathepsins, Cysteine Endopeptidases, Green Fluorescent Proteins, Peptides, Viral Fusion Proteins.
- chemical , pharmacology : Cathepsins, Cysteine Endopeptidases, Trypsin.
- chemical : Cathepsin L.
- metabolism : SARS Virus.
- Animals, Chlorocebus aethiops, Hydrogen-Ion Concentration, Plasmids, Temperature, Time Factors, Transfection, Vero Cells.
Abstract
Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.
DOI: 10.1128/JVI.00415-08
PubMed: 18562523
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001B19
Links to Exploration step
pubmed:18562523Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.</title>
<author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Institute of Biomembranes, Utrecht, The Netherlands.</nlm:affiliation>
<country xml:lang="fr">Pays-Bas</country>
<wicri:regionArea>Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Institute of Biomembranes, Utrecht</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Bartelink, Willem" sort="Bartelink, Willem" uniqKey="Bartelink W" first="Willem" last="Bartelink">Willem Bartelink</name>
</author>
<author><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2008">2008</date>
<idno type="RBID">pubmed:18562523</idno>
<idno type="pmid">18562523</idno>
<idno type="doi">10.1128/JVI.00415-08</idno>
<idno type="wicri:Area/PubMed/Corpus">001B19</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001B19</idno>
<idno type="wicri:Area/PubMed/Curation">001B19</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001B19</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.</title>
<author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Institute of Biomembranes, Utrecht, The Netherlands.</nlm:affiliation>
<country xml:lang="fr">Pays-Bas</country>
<wicri:regionArea>Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Institute of Biomembranes, Utrecht</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Bartelink, Willem" sort="Bartelink, Willem" uniqKey="Bartelink W" first="Willem" last="Bartelink">Willem Bartelink</name>
</author>
<author><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name>
</author>
</analytic>
<series><title level="j">Journal of virology</title>
<idno type="eISSN">1098-5514</idno>
<imprint><date when="2008" type="published">2008</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Cathepsin L</term>
<term>Cathepsins (metabolism)</term>
<term>Cathepsins (pharmacology)</term>
<term>Chlorocebus aethiops</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Cysteine Endopeptidases (pharmacology)</term>
<term>Green Fluorescent Proteins (metabolism)</term>
<term>Hydrogen-Ion Concentration</term>
<term>Peptides (metabolism)</term>
<term>Plasmids</term>
<term>SARS Virus (metabolism)</term>
<term>Temperature</term>
<term>Time Factors</term>
<term>Transfection</term>
<term>Trypsin (pharmacology)</term>
<term>Vero Cells</term>
<term>Viral Fusion Proteins (classification)</term>
<term>Viral Fusion Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Cathepsine L</term>
<term>Cathepsines (métabolisme)</term>
<term>Cathepsines (pharmacologie)</term>
<term>Cellules Vero</term>
<term>Concentration en ions d'hydrogène</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Cysteine endopeptidases (pharmacologie)</term>
<term>Facteurs temps</term>
<term>Peptides (métabolisme)</term>
<term>Plasmides</term>
<term>Protéines de fusion virale ()</term>
<term>Protéines de fusion virale (métabolisme)</term>
<term>Protéines à fluorescence verte (métabolisme)</term>
<term>Température</term>
<term>Transfection</term>
<term>Trypsine (pharmacologie)</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsins</term>
<term>Cysteine Endopeptidases</term>
<term>Green Fluorescent Proteins</term>
<term>Peptides</term>
<term>Viral Fusion Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Cathepsins</term>
<term>Cysteine Endopeptidases</term>
<term>Trypsin</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cathepsin L</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cathepsines</term>
<term>Cysteine endopeptidases</term>
<term>Peptides</term>
<term>Protéines de fusion virale</term>
<term>Protéines à fluorescence verte</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Cathepsines</term>
<term>Cysteine endopeptidases</term>
<term>Trypsine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Chlorocebus aethiops</term>
<term>Hydrogen-Ion Concentration</term>
<term>Plasmids</term>
<term>Temperature</term>
<term>Time Factors</term>
<term>Transfection</term>
<term>Vero Cells</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cathepsine L</term>
<term>Cellules Vero</term>
<term>Concentration en ions d'hydrogène</term>
<term>Facteurs temps</term>
<term>Plasmides</term>
<term>Protéines de fusion virale</term>
<term>Température</term>
<term>Transfection</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18562523</PMID>
<DateCompleted><Year>2008</Year>
<Month>09</Month>
<Day>29</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>82</Volume>
<Issue>17</Issue>
<PubDate><Year>2008</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.</ArticleTitle>
<Pagination><MedlinePgn>8887-90</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.00415-08</ELocationID>
<Abstract><AbstractText>Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bosch</LastName>
<ForeName>Berend Jan</ForeName>
<Initials>BJ</Initials>
<AffiliationInfo><Affiliation>Department of Infectious Diseases and Immunology, Virology Division, Faculty of Veterinary Medicine, Utrecht University, Institute of Biomembranes, Utrecht, The Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bartelink</LastName>
<ForeName>Willem</ForeName>
<Initials>W</Initials>
</Author>
<Author ValidYN="Y"><LastName>Rottier</LastName>
<ForeName>Peter J M</ForeName>
<Initials>PJ</Initials>
</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>2008</Year>
<Month>06</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010455">Peptides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014760">Viral Fusion Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>147336-22-9</RegistryNumber>
<NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
<NameOfSubstance UI="D002403">Cathepsins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber>
<NameOfSubstance UI="D014357">Trypsin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
<NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.15</RegistryNumber>
<NameOfSubstance UI="D056668">Cathepsin L</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056668" MajorTopicYN="N">Cathepsin L</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002403" MajorTopicYN="N">Cathepsins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D049452" MajorTopicYN="N">Green Fluorescent Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014709" MajorTopicYN="N">Vero Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014760" MajorTopicYN="N">Viral Fusion Proteins</DescriptorName>
<QualifierName UI="Q000145" MajorTopicYN="Y">classification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year>
<Month>6</Month>
<Day>20</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2008</Year>
<Month>9</Month>
<Day>30</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2008</Year>
<Month>6</Month>
<Day>20</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">18562523</ArticleId>
<ArticleId IdType="pii">JVI.00415-08</ArticleId>
<ArticleId IdType="doi">10.1128/JVI.00415-08</ArticleId>
<ArticleId IdType="pmc">PMC2519682</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 30;102(35):12543-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16116101</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11876-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16081529</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jun;80(12):5768-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16731916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jul;80(14):6794-800</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16809285</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2006 Jul 5;350(2):358-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16519916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2006 Nov 21;103(47):17903-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17093041</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2007;2(10):e1082</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17957264</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2000 Mar 7;1477(1-2):98-111</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10708852</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2000 May 25;271(1):122-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10814577</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Immunol. 2003 Jun;3(6):472-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12776207</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4240-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15010527</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Jun;78(11):6048-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15141003</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Sep 3;321(4):994-1000</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15358126</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1988 Nov;69 ( Pt 11):2785-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3183628</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1990 Dec;71 ( Pt 12):3075-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2177097</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Feb 10;281(6):3198-203</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16339146</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001B19 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 001B19 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= SrasV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:18562523 |texte= Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:18562523" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a SrasV1
![]() | This area was generated with Dilib version V0.6.33. | ![]() |