Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.
Identifieur interne : 000C78 ( Ncbi/Merge ); précédent : 000C77; suivant : 000C79Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.
Auteurs : Yan G. Fulcher [États-Unis] ; Raghavendar Reddy Sanganna Gari ; Nathan C. Frey ; Fuming Zhang ; Robert J. Linhardt ; Gavin M. King ; Steven R. Van DorenSource :
- ACS chemical biology [ 1554-8937 ] ; 2014.
Descripteurs français
- KwdFr :
- Activation enzymatique, Animaux, Humains, Héparinoïde (pharmacologie), Liaison aux protéines, Matrix metalloproteinase 7 (génétique), Matrix metalloproteinase 7 (métabolisme), Microscopie à force atomique, Modèles biologiques, Muqueuse (métabolisme), Peptide hydrolases (), Peptide hydrolases (métabolisme), Propriétés de surface, Rats, Régulation allostérique, Tumeurs (métabolisme).
- MESH :
- génétique : Matrix metalloproteinase 7.
- métabolisme : Matrix metalloproteinase 7, Muqueuse, Peptide hydrolases, Tumeurs.
- pharmacologie : Héparinoïde.
- Activation enzymatique, Animaux, Humains, Liaison aux protéines, Microscopie à force atomique, Modèles biologiques, Peptide hydrolases, Propriétés de surface, Rats, Régulation allostérique.
English descriptors
- KwdEn :
- Allosteric Regulation, Animals, Enzyme Activation, Heparinoids (pharmacology), Humans, Matrix Metalloproteinase 7 (genetics), Matrix Metalloproteinase 7 (metabolism), Microscopy, Atomic Force, Models, Biological, Mucous Membrane (metabolism), Neoplasms (metabolism), Peptide Hydrolases (drug effects), Peptide Hydrolases (metabolism), Protein Binding, Rats, Surface Properties.
- MESH :
- chemical , drug effects : Peptide Hydrolases.
- chemical , genetics : Matrix Metalloproteinase 7.
- chemical , metabolism : Matrix Metalloproteinase 7, Peptide Hydrolases.
- chemical , pharmacology : Heparinoids.
- metabolism : Mucous Membrane, Neoplasms.
- Allosteric Regulation, Animals, Enzyme Activation, Humans, Microscopy, Atomic Force, Models, Biological, Protein Binding, Rats, Surface Properties.
Abstract
Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces.
DOI: 10.1021/cb400898t
PubMed: 24495220
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001A65
- to stream PubMed, to step Curation: 001A65
- to stream PubMed, to step Checkpoint: 001893
Links to Exploration step
pubmed:24495220Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.</title>
<author><name sortKey="Fulcher, Yan G" sort="Fulcher, Yan G" uniqKey="Fulcher Y" first="Yan G" last="Fulcher">Yan G. Fulcher</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211</wicri:regionArea>
<wicri:noRegion>Missouri 65211</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Sanganna Gari, Raghavendar Reddy" sort="Sanganna Gari, Raghavendar Reddy" uniqKey="Sanganna Gari R" first="Raghavendar Reddy" last="Sanganna Gari">Raghavendar Reddy Sanganna Gari</name>
</author>
<author><name sortKey="Frey, Nathan C" sort="Frey, Nathan C" uniqKey="Frey N" first="Nathan C" last="Frey">Nathan C. Frey</name>
</author>
<author><name sortKey="Zhang, Fuming" sort="Zhang, Fuming" uniqKey="Zhang F" first="Fuming" last="Zhang">Fuming Zhang</name>
</author>
<author><name sortKey="Linhardt, Robert J" sort="Linhardt, Robert J" uniqKey="Linhardt R" first="Robert J" last="Linhardt">Robert J. Linhardt</name>
</author>
<author><name sortKey="King, Gavin M" sort="King, Gavin M" uniqKey="King G" first="Gavin M" last="King">Gavin M. King</name>
</author>
<author><name sortKey="Van Doren, Steven R" sort="Van Doren, Steven R" uniqKey="Van Doren S" first="Steven R" last="Van Doren">Steven R. Van Doren</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2014">2014</date>
<idno type="RBID">pubmed:24495220</idno>
<idno type="pmid">24495220</idno>
<idno type="doi">10.1021/cb400898t</idno>
<idno type="wicri:Area/PubMed/Corpus">001A65</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A65</idno>
<idno type="wicri:Area/PubMed/Curation">001A65</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001A65</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001893</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001893</idno>
<idno type="wicri:Area/Ncbi/Merge">000C78</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.</title>
<author><name sortKey="Fulcher, Yan G" sort="Fulcher, Yan G" uniqKey="Fulcher Y" first="Yan G" last="Fulcher">Yan G. Fulcher</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211, United States.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211</wicri:regionArea>
<wicri:noRegion>Missouri 65211</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Sanganna Gari, Raghavendar Reddy" sort="Sanganna Gari, Raghavendar Reddy" uniqKey="Sanganna Gari R" first="Raghavendar Reddy" last="Sanganna Gari">Raghavendar Reddy Sanganna Gari</name>
</author>
<author><name sortKey="Frey, Nathan C" sort="Frey, Nathan C" uniqKey="Frey N" first="Nathan C" last="Frey">Nathan C. Frey</name>
</author>
<author><name sortKey="Zhang, Fuming" sort="Zhang, Fuming" uniqKey="Zhang F" first="Fuming" last="Zhang">Fuming Zhang</name>
</author>
<author><name sortKey="Linhardt, Robert J" sort="Linhardt, Robert J" uniqKey="Linhardt R" first="Robert J" last="Linhardt">Robert J. Linhardt</name>
</author>
<author><name sortKey="King, Gavin M" sort="King, Gavin M" uniqKey="King G" first="Gavin M" last="King">Gavin M. King</name>
</author>
<author><name sortKey="Van Doren, Steven R" sort="Van Doren, Steven R" uniqKey="Van Doren S" first="Steven R" last="Van Doren">Steven R. Van Doren</name>
</author>
</analytic>
<series><title level="j">ACS chemical biology</title>
<idno type="eISSN">1554-8937</idno>
<imprint><date when="2014" type="published">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation</term>
<term>Animals</term>
<term>Enzyme Activation</term>
<term>Heparinoids (pharmacology)</term>
<term>Humans</term>
<term>Matrix Metalloproteinase 7 (genetics)</term>
<term>Matrix Metalloproteinase 7 (metabolism)</term>
<term>Microscopy, Atomic Force</term>
<term>Models, Biological</term>
<term>Mucous Membrane (metabolism)</term>
<term>Neoplasms (metabolism)</term>
<term>Peptide Hydrolases (drug effects)</term>
<term>Peptide Hydrolases (metabolism)</term>
<term>Protein Binding</term>
<term>Rats</term>
<term>Surface Properties</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique</term>
<term>Animaux</term>
<term>Humains</term>
<term>Héparinoïde (pharmacologie)</term>
<term>Liaison aux protéines</term>
<term>Matrix metalloproteinase 7 (génétique)</term>
<term>Matrix metalloproteinase 7 (métabolisme)</term>
<term>Microscopie à force atomique</term>
<term>Modèles biologiques</term>
<term>Muqueuse (métabolisme)</term>
<term>Peptide hydrolases ()</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Propriétés de surface</term>
<term>Rats</term>
<term>Régulation allostérique</term>
<term>Tumeurs (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Peptide Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Matrix Metalloproteinase 7</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Matrix Metalloproteinase 7</term>
<term>Peptide Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Heparinoids</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Matrix metalloproteinase 7</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mucous Membrane</term>
<term>Neoplasms</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Matrix metalloproteinase 7</term>
<term>Muqueuse</term>
<term>Peptide hydrolases</term>
<term>Tumeurs</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Héparinoïde</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term>
<term>Animals</term>
<term>Enzyme Activation</term>
<term>Humans</term>
<term>Microscopy, Atomic Force</term>
<term>Models, Biological</term>
<term>Protein Binding</term>
<term>Rats</term>
<term>Surface Properties</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Animaux</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Microscopie à force atomique</term>
<term>Modèles biologiques</term>
<term>Peptide hydrolases</term>
<term>Propriétés de surface</term>
<term>Rats</term>
<term>Régulation allostérique</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24495220</PMID>
<DateCompleted><Year>2015</Year>
<Month>07</Month>
<Day>01</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1554-8937</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>9</Volume>
<Issue>4</Issue>
<PubDate><Year>2014</Year>
<Month>Apr</Month>
<Day>18</Day>
</PubDate>
</JournalIssue>
<Title>ACS chemical biology</Title>
<ISOAbbreviation>ACS Chem. Biol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery.</ArticleTitle>
<Pagination><MedlinePgn>957-66</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/cb400898t</ELocationID>
<Abstract><AbstractText>Activation by glycosaminoglycans (GAGs) is an emerging trend among extracellular proteases important in disease. ProMMP-7, the zymogen of a matrix metalloproteinase secreted by mucosal epithelial and tumor cells, is activated at their surfaces by sulfated GAGs, but how? ProMMP-7 is activated in trans by representative heparin oligosaccharides in a length-dependent manner, with a large jump in activation at lengths of 16 monosaccharides. Imaging by atomic force microscopy visualized small complexes of proMMP-7 molecules linked by 8-mer lengths of heparinoids and extended assembles formed with 16-mer lengths of heparin. Complexes of proMMP-7 with polydisperse heparin or heparan sulfate were more diverse. Heparinoids evidently accelerate activation by tethering multiple proMMP-7 molecules together for proteolytic attack among neighbors. Removal of either the prodomain or C-terminal peptide sequence of KRSNSRKK from MMP-7 prevents formation of the long arrays induced by heparin 16-mers or heparan sulfate. The role of the C-terminus in activation assays suggests it contributes to remote, allosteric binding of GAGs. Enhancement of proteolytic velocity of MMP-by GAGs indicates them to be effectors of V-type allostery. GAGs from proteoglycans appear to assemble proMMP-7 molecules for activation, an event preceding its tumorigenic or antibacterial proteolytic activities at cell surfaces. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fulcher</LastName>
<ForeName>Yan G</ForeName>
<Initials>YG</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and ‡Department of Physics and Astronomy, University of Missouri , Columbia, Missouri 65211, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sanganna Gari</LastName>
<ForeName>Raghavendar Reddy</ForeName>
<Initials>RR</Initials>
</Author>
<Author ValidYN="Y"><LastName>Frey</LastName>
<ForeName>Nathan C</ForeName>
<Initials>NC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Fuming</ForeName>
<Initials>F</Initials>
</Author>
<Author ValidYN="Y"><LastName>Linhardt</LastName>
<ForeName>Robert J</ForeName>
<Initials>RJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>King</LastName>
<ForeName>Gavin M</ForeName>
<Initials>GM</Initials>
</Author>
<Author ValidYN="Y"><LastName>Van Doren</LastName>
<ForeName>Steven R</ForeName>
<Initials>SR</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R01 GM057289</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>S10 RR022341</GrantID>
<Acronym>RR</Acronym>
<Agency>NCRR NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01GM057289</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>RR022341</GrantID>
<Acronym>RR</Acronym>
<Agency>NCRR 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="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>02</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>ACS Chem Biol</MedlineTA>
<NlmUniqueID>101282906</NlmUniqueID>
<ISSNLinking>1554-8929</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D006496">Heparinoids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.-</RegistryNumber>
<NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.24.23</RegistryNumber>
<NameOfSubstance UI="D020783">Matrix Metalloproteinase 7</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006496" MajorTopicYN="N">Heparinoids</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020783" MajorTopicYN="N">Matrix Metalloproteinase 7</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018625" MajorTopicYN="N">Microscopy, Atomic Force</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008954" MajorTopicYN="Y">Models, Biological</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009092" MajorTopicYN="N">Mucous Membrane</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009369" MajorTopicYN="N">Neoplasms</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013499" MajorTopicYN="N">Surface Properties</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year>
<Month>2</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2014</Year>
<Month>2</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2015</Year>
<Month>7</Month>
<Day>2</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">24495220</ArticleId>
<ArticleId IdType="doi">10.1021/cb400898t</ArticleId>
<ArticleId IdType="pmc">PMC4063349</ArticleId>
<ArticleId IdType="mid">NIHMS563514</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Biol Chem. 2002 May 3;277(18):16022-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11839746</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 2002 Feb 1;16(3):307-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11825873</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Feb 13;279(7):5470-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14645229</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 2004 May 15;328(2):166-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15113693</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2004 Sep;11(9):857-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15311269</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1982 Jul 10;257(13):7360-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7085630</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1983 Sep;80(18):5460-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6577437</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1991 Apr 5;266(10):6353-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2007588</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 1993 Aug 1;293 ( Pt 3):849-58</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8352752</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 1993 Dec 1;218(2):431-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8269931</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1997 Dec 16;36(50):16019-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9398337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Jan 9;273(2):871-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9422744</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1999 Oct 1;286(5437):113-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10506557</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1999 Sep 14;38(37):12187-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10508424</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2005 Feb 14;579(5):1285-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15710427</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Carcinogenesis. 2006 May;27(5):1113-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16474169</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2006 May 30;45(21):6703-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16716081</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Br J Cancer. 2006 Aug 21;95(4):506-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16880790</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2007 Mar;64(5):610-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17310281</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem J. 2007 May 1;403(3):553-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17217338</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Res. 2007 Jul 15;67(14):6760-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17638887</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 2007 Dec 1;371(1):43-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17706587</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Am Chem Soc. 2007 Nov 7;129(44):13566-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17929919</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Nov 9;282(45):33076-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17726009</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2008 Feb 15;366(3):862-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18086562</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2008 Oct 31;383(1):78-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18692071</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2009;4(8):e6565</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19668337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2009 Oct 9;284(41):27924-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19654318</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2009 Dec;276(24):7343-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19919557</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2010 Jan 22;395(3):504-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19895822</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2011 Jan;278(1):28-45</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21087458</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2010 Dec 31;285(53):41270-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21041295</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS J. 2013 May;280(10):2332-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23421805</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FASEB J. 2013 Jun;27(6):2342-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23493619</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2000 Oct 24;39(42):13068-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11041873</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 Feb 11;275(6):4183-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10660581</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2013 Nov;1830(11):5287-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23891937</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Res. 2001 Jan 15;61(2):577-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11212252</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Anal Biochem. 2001 Jun 1;293(1):38-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11373076</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Res. 2002 Oct 1;62(19):5559-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12359768</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
</list>
<tree><noCountry><name sortKey="Frey, Nathan C" sort="Frey, Nathan C" uniqKey="Frey N" first="Nathan C" last="Frey">Nathan C. Frey</name>
<name sortKey="King, Gavin M" sort="King, Gavin M" uniqKey="King G" first="Gavin M" last="King">Gavin M. King</name>
<name sortKey="Linhardt, Robert J" sort="Linhardt, Robert J" uniqKey="Linhardt R" first="Robert J" last="Linhardt">Robert J. Linhardt</name>
<name sortKey="Sanganna Gari, Raghavendar Reddy" sort="Sanganna Gari, Raghavendar Reddy" uniqKey="Sanganna Gari R" first="Raghavendar Reddy" last="Sanganna Gari">Raghavendar Reddy Sanganna Gari</name>
<name sortKey="Van Doren, Steven R" sort="Van Doren, Steven R" uniqKey="Van Doren S" first="Steven R" last="Van Doren">Steven R. Van Doren</name>
<name sortKey="Zhang, Fuming" sort="Zhang, Fuming" uniqKey="Zhang F" first="Fuming" last="Zhang">Fuming Zhang</name>
</noCountry>
<country name="États-Unis"><noRegion><name sortKey="Fulcher, Yan G" sort="Fulcher, Yan G" uniqKey="Fulcher Y" first="Yan G" last="Fulcher">Yan G. Fulcher</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Ncbi/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000C78 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 000C78 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Ncbi |étape= Merge |type= RBID |clé= pubmed:24495220 |texte= Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i -Sk "pubmed:24495220" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
This area was generated with Dilib version V0.6.33. |