Enzymatic activity of the SARS coronavirus main proteinase dimer.
Identifieur interne : 002257 ( PubMed/Corpus ); précédent : 002256; suivant : 002258Enzymatic activity of the SARS coronavirus main proteinase dimer.
Auteurs : Vito Graziano ; William J. Mcgrath ; Ann Marie Degruccio ; John J. Dunn ; Walter F. MangelSource :
- FEBS letters [ 0014-5793 ] ; 2006.
English descriptors
- KwdEn :
- Cloning, Molecular, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (isolation & purification), Cysteine Endopeptidases (metabolism), Dimerization, Gene Expression, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Osmolar Concentration, Peptides (chemistry), Peptides (metabolism), Protein Structure, Quaternary, SARS Virus (enzymology), Sensitivity and Specificity, Substrate Specificity, Temperature.
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Peptides.
- chemical , genetics : Cysteine Endopeptidases.
- chemical , isolation & purification : Cysteine Endopeptidases.
- chemical , metabolism : Cysteine Endopeptidases, Peptides.
- enzymology : SARS Virus.
- Cloning, Molecular, Dimerization, Gene Expression, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Osmolar Concentration, Protein Structure, Quaternary, Sensitivity and Specificity, Substrate Specificity, Temperature.
Abstract
The enzymatic activity of the SARS coronavirus main proteinase dimer was characterized by a sensitive, quantitative assay. The new, fluorogenic substrate, (Ala-Arg-Leu-Gln-NH)(2)-Rhodamine, contained a severe acute respiratory syndrome coronavirus (SARS CoV) main proteinase consensus cleavage sequence and Rhodamine 110, one of the most detectable compounds known, as the reporter group. The gene for the enzyme was cloned in the absence of purification tags, expressed in Escherichia coli and the enzyme purified. Enzyme activity from the SARS CoV main proteinase dimer could readily be detected at low pM concentrations. The enzyme exhibited a high K(m), and is unusually sensitive to ionic strength and reducing agents.
DOI: 10.1016/j.febslet.2006.04.004
PubMed: 16647061
Links to Exploration step
pubmed:16647061Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Enzymatic activity of the SARS coronavirus main proteinase dimer.</title><author><name sortKey="Graziano, Vito" sort="Graziano, Vito" uniqKey="Graziano V" first="Vito" last="Graziano">Vito Graziano</name><affiliation><nlm:affiliation>Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Mcgrath, William J" sort="Mcgrath, William J" uniqKey="Mcgrath W" first="William J" last="Mcgrath">William J. Mcgrath</name></author><author><name sortKey="Degruccio, Ann Marie" sort="Degruccio, Ann Marie" uniqKey="Degruccio A" first="Ann Marie" last="Degruccio">Ann Marie Degruccio</name></author><author><name sortKey="Dunn, John J" sort="Dunn, John J" uniqKey="Dunn J" first="John J" last="Dunn">John J. Dunn</name></author><author><name sortKey="Mangel, Walter F" sort="Mangel, Walter F" uniqKey="Mangel W" first="Walter F" last="Mangel">Walter F. Mangel</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16647061</idno><idno type="pmid">16647061</idno><idno type="doi">10.1016/j.febslet.2006.04.004</idno><idno type="wicri:Area/PubMed/Corpus">002257</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002257</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Enzymatic activity of the SARS coronavirus main proteinase dimer.</title><author><name sortKey="Graziano, Vito" sort="Graziano, Vito" uniqKey="Graziano V" first="Vito" last="Graziano">Vito Graziano</name><affiliation><nlm:affiliation>Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Mcgrath, William J" sort="Mcgrath, William J" uniqKey="Mcgrath W" first="William J" last="Mcgrath">William J. Mcgrath</name></author><author><name sortKey="Degruccio, Ann Marie" sort="Degruccio, Ann Marie" uniqKey="Degruccio A" first="Ann Marie" last="Degruccio">Ann Marie Degruccio</name></author><author><name sortKey="Dunn, John J" sort="Dunn, John J" uniqKey="Dunn J" first="John J" last="Dunn">John J. Dunn</name></author><author><name sortKey="Mangel, Walter F" sort="Mangel, Walter F" uniqKey="Mangel W" first="Walter F" last="Mangel">Walter F. Mangel</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cloning, Molecular</term><term>Cysteine Endopeptidases (chemistry)</term><term>Cysteine Endopeptidases (genetics)</term><term>Cysteine Endopeptidases (isolation & purification)</term><term>Cysteine Endopeptidases (metabolism)</term><term>Dimerization</term><term>Gene Expression</term><term>Hydrogen-Ion Concentration</term><term>Hydrolysis</term><term>Kinetics</term><term>Osmolar Concentration</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Protein Structure, Quaternary</term><term>SARS Virus (enzymology)</term><term>Sensitivity and Specificity</term><term>Substrate Specificity</term><term>Temperature</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Cysteine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Dimerization</term><term>Gene Expression</term><term>Hydrogen-Ion Concentration</term><term>Hydrolysis</term><term>Kinetics</term><term>Osmolar Concentration</term><term>Protein Structure, Quaternary</term><term>Sensitivity and Specificity</term><term>Substrate Specificity</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The enzymatic activity of the SARS coronavirus main proteinase dimer was characterized by a sensitive, quantitative assay. The new, fluorogenic substrate, (Ala-Arg-Leu-Gln-NH)(2)-Rhodamine, contained a severe acute respiratory syndrome coronavirus (SARS CoV) main proteinase consensus cleavage sequence and Rhodamine 110, one of the most detectable compounds known, as the reporter group. The gene for the enzyme was cloned in the absence of purification tags, expressed in Escherichia coli and the enzyme purified. Enzyme activity from the SARS CoV main proteinase dimer could readily be detected at low pM concentrations. The enzyme exhibited a high K(m), and is unusually sensitive to ionic strength and reducing agents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16647061</PMID><DateCompleted><Year>2006</Year><Month>07</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>580</Volume><Issue>11</Issue><PubDate><Year>2006</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett.</ISOAbbreviation></Journal><ArticleTitle>Enzymatic activity of the SARS coronavirus main proteinase dimer.</ArticleTitle><Pagination><MedlinePgn>2577-83</MedlinePgn></Pagination><Abstract><AbstractText>The enzymatic activity of the SARS coronavirus main proteinase dimer was characterized by a sensitive, quantitative assay. The new, fluorogenic substrate, (Ala-Arg-Leu-Gln-NH)(2)-Rhodamine, contained a severe acute respiratory syndrome coronavirus (SARS CoV) main proteinase consensus cleavage sequence and Rhodamine 110, one of the most detectable compounds known, as the reporter group. The gene for the enzyme was cloned in the absence of purification tags, expressed in Escherichia coli and the enzyme purified. Enzyme activity from the SARS CoV main proteinase dimer could readily be detected at low pM concentrations. The enzyme exhibited a high K(m), and is unusually sensitive to ionic strength and reducing agents.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Graziano</LastName><ForeName>Vito</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McGrath</LastName><ForeName>William J</ForeName><Initials>WJ</Initials></Author><Author ValidYN="Y"><LastName>DeGruccio</LastName><ForeName>Ann Marie</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Dunn</LastName><ForeName>John J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Mangel</LastName><ForeName>Walter F</ForeName><Initials>WF</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R56 AI041599</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI056480</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AI041599</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>AI41599</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>U01 AI056480</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>04</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009994" MajorTopicYN="N">Osmolar Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012680" MajorTopicYN="N">Sensitivity and Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>12</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>03</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>04</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>5</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>7</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>5</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16647061</ArticleId><ArticleId IdType="pii">S0014-5793(06)00423-6</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2006.04.004</ArticleId><ArticleId IdType="pmc">PMC7094300</ArticleId></ArticleIdList><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>J Gen Virol. 2002 Mar;83(Pt 3):595-599</Citation><ArticleIdList><ArticleId IdType="pubmed">11842254</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1996 Mar 1;217(1):131-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8599197</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2003 Aug 29;331(5):991-1004</Citation><ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem J. 1983 Nov 1;215(2):253-60</Citation><ArticleIdList><ArticleId IdType="pubmed">6228222</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2000 Sep 22;481(3):289-92</Citation><ArticleIdList><ArticleId IdType="pubmed">11007981</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>EMBO J. 2002 Jul 1;21(13):3213-24</Citation><ArticleIdList><ArticleId IdType="pubmed">12093723</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biophys J. 1999 May;76(5):2587-99</Citation><ArticleIdList><ArticleId IdType="pubmed">10233073</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2002 Sep 6;277(36):33170-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12095981</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2004 Jun 11;318(4):862-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15147951</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>EMBO J. 1999 Oct 15;18(20):5463-75</Citation><ArticleIdList><ArticleId IdType="pubmed">10523291</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>Biochemistry. 2004 Apr 20;43(15):4568-74</Citation><ArticleIdList><ArticleId IdType="pubmed">15078103</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem J. 1983 Feb 1;209(2):299-307</Citation><ArticleIdList><ArticleId IdType="pubmed">6342611</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Bioorg Med Chem Lett. 1999 Nov 15;9(22):3231-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10576694</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>Anal Chem. 1993 Sep 1;65(17):2352-9</Citation><ArticleIdList><ArticleId IdType="pubmed">8238930</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2006 May 15;580(11):2577-83</Citation><ArticleIdList><ArticleId IdType="pubmed">16647061</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biomol Screen. 2002 Dec;7(6):531-40</Citation><ArticleIdList><ArticleId IdType="pubmed">14599351</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2005 Jul 22;333(1):194-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15950190</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 1997 May;71(5):3992-7</Citation><ArticleIdList><ArticleId IdType="pubmed">9094676</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>Acta Pharmacol Sin. 2005 Jan;26(1):99-106</Citation><ArticleIdList><ArticleId IdType="pubmed">15659121</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1995 Apr 1;208(1):1-8</Citation><ArticleIdList><ArticleId IdType="pubmed">11831690</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jun 4;279(23):24765-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15037623</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2005 Apr 15;329(3):934-40</Citation><ArticleIdList><ArticleId IdType="pubmed">15752746</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Nov 30;43(47):14958-70</Citation><ArticleIdList><ArticleId IdType="pubmed">15554703</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>Biochem Pharmacol. 2000 Sep 15;60(6):759-69</Citation><ArticleIdList><ArticleId IdType="pubmed">10930530</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proteins. 2003 Aug 1;52(2):236-53</Citation><ArticleIdList><ArticleId IdType="pubmed">12833547</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 1993 Jan 21;361(6409):274-5</Citation><ArticleIdList><ArticleId IdType="pubmed">8423855</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2004 Sep 10;574(1-3):116-20</Citation><ArticleIdList><ArticleId IdType="pubmed">15358550</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochim Biophys Acta. 1984 Jul 17;788(1):74-86</Citation><ArticleIdList><ArticleId IdType="pubmed">6204689</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>Protein Expr Purif. 2005 May;41(1):207-34</Citation><ArticleIdList><ArticleId IdType="pubmed">15915565</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2005 Jun 17;331(4):1554-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15883050</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002257 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 002257 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:16647061
|texte= Enzymatic activity of the SARS coronavirus main proteinase dimer.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:16647061" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |