MersV1, PubMed, Checkpoint, bibRecord, 002822

The properdin-like type I repeats of human thrombospondin contain a cell attachment site.

Identifieur interne : 002822 ( PubMed/Checkpoint ); précédent : 002821; suivant : 002823

The properdin-like type I repeats of human thrombospondin contain a cell attachment site.

Auteurs : C A Prater [États-Unis] ; J. Plotkin ; D. Jaye ; W A Frazier

Source :

The Journal of cell biology [ 0021-9525 ] ; 1991.

RBID : pubmed:1999454

Descripteurs français

KwdFr :
- Adhérence cellulaire, Anticorps monoclonaux, Cellules cancéreuses en culture, Données de séquences moléculaires, Glycoprotéines de membrane plaquettaire (), Glycoprotéines de membrane plaquettaire (génétique), Glycoprotéines de membrane plaquettaire (métabolisme), Humains, Mélanome, Properdine (), Properdine (génétique), Similitude de séquences d'acides nucléiques, Sites de fixation, Séquence d'acides aminés, Séquences répétées d'acides nucléiques, Technique de Western, Test ELISA, Thrombospondines.
MESH :

English descriptors

KwdEn :
- Amino Acid Sequence, Antibodies, Monoclonal, Binding Sites, Blotting, Western, Cell Adhesion, Enzyme-Linked Immunosorbent Assay, Humans, Melanoma, Molecular Sequence Data, Platelet Membrane Glycoproteins (chemistry), Platelet Membrane Glycoproteins (genetics), Platelet Membrane Glycoproteins (metabolism), Properdin (chemistry), Properdin (genetics), Repetitive Sequences, Nucleic Acid, Sequence Homology, Nucleic Acid, Thrombospondins, Tumor Cells, Cultured.
MESH :
- chemical , chemistry : Platelet Membrane Glycoproteins, Properdin.
- chemical , genetics : Platelet Membrane Glycoproteins, Properdin.
- chemical , metabolism : Platelet Membrane Glycoproteins.
- chemical : Antibodies, Monoclonal, Thrombospondins.
- Amino Acid Sequence, Binding Sites, Blotting, Western, Cell Adhesion, Enzyme-Linked Immunosorbent Assay, Humans, Melanoma, Molecular Sequence Data, Repetitive Sequences, Nucleic Acid, Sequence Homology, Nucleic Acid, Tumor Cells, Cultured.

Abstract

Thrombospondin (TS) is a modular adhesive glycoprotein that contains three domains previously implicated in the attachment of cells to TS. These include the amino-terminal heparin-binding domain, the carboxy terminal cell or platelet-binding domain, and an RGDA sequence of TS. We have characterized a mAb against human TS, designated A4.1, which inhibits the attachment of human melanoma cells (G361) to TS. The epitope for A4.1 lies within the amino terminal half of the central stalklike region of TS which is distinct from the three known cell attachment sites. This region of TS is recovered in a 50-kD peptide after chymotryptic digestion of TS in EDTA. It contains the procollagen-like domain of TS as well as three type I repeats of a 60-residue segment homologous to two malarial proteins and the complement proteins properdin, and factors C6 through C9. The purified chymotryptic fragment is an effective attachment factor for G361 cells. A4.1 blocks adhesion to the 50-kD domain, as do some sulfated glycoconjugates. RGD (and RGE) peptides and mAbs against other domains of TS are not inhibitory. Peptides (19 mers) based on the core homology sequence of the three type I repeats of TS are potent attachment factors for these cells, and this adhesion is also inhibited by sulfated glycoconjugates. A polyclonal antibody raised against one of these peptides inhibits adhesion of G361 cells to the peptides, to the 50-kD fragment and to intact TS. Thus a new cell-adhesion site has been identified in TS whose sequence is very similar to the site identified in region II of the circumsporozoite protein of malaria parasites (Rich, K. A., F. W. George IV, J. L. Law, and W. J. Martin. 1990. Science (Wash. DC) 249:1574-1577. Thus there may be a common receptor which binds TS, malarial proteins, and properdin.

DOI: 10.1083/jcb.112.5.1031
PubMed: 1999454

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002A03
to stream PubMed, to step Curation: 002A03

Links to Exploration step

pubmed:1999454

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The properdin-like type I repeats of human thrombospondin contain a cell attachment site.</title>
<author><name sortKey="Prater, C A" sort="Prater, C A" uniqKey="Prater C" first="C A" last="Prater">C A Prater</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Missouri (État)</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Plotkin, J" sort="Plotkin, J" uniqKey="Plotkin J" first="J" last="Plotkin">J. Plotkin</name>
</author>
<author><name sortKey="Jaye, D" sort="Jaye, D" uniqKey="Jaye D" first="D" last="Jaye">D. Jaye</name>
</author>
<author><name sortKey="Frazier, W A" sort="Frazier, W A" uniqKey="Frazier W" first="W A" last="Frazier">W A Frazier</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="1991">1991</date>
<idno type="RBID">pubmed:1999454</idno>
<idno type="pmid">1999454</idno>
<idno type="doi">10.1083/jcb.112.5.1031</idno>
<idno type="wicri:Area/PubMed/Corpus">002A03</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A03</idno>
<idno type="wicri:Area/PubMed/Curation">002A03</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002A03</idno>
<idno type="wicri:Area/PubMed/Checkpoint">002822</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002822</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">The properdin-like type I repeats of human thrombospondin contain a cell attachment site.</title>
<author><name sortKey="Prater, C A" sort="Prater, C A" uniqKey="Prater C" first="C A" last="Prater">C A Prater</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Missouri (État)</region>
</placeName>
<wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis</wicri:cityArea>
</affiliation>
</author>
<author><name sortKey="Plotkin, J" sort="Plotkin, J" uniqKey="Plotkin J" first="J" last="Plotkin">J. Plotkin</name>
</author>
<author><name sortKey="Jaye, D" sort="Jaye, D" uniqKey="Jaye D" first="D" last="Jaye">D. Jaye</name>
</author>
<author><name sortKey="Frazier, W A" sort="Frazier, W A" uniqKey="Frazier W" first="W A" last="Frazier">W A Frazier</name>
</author>
</analytic>
<series><title level="j">The Journal of cell biology</title>
<idno type="ISSN">0021-9525</idno>
<imprint><date when="1991" type="published">1991</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Antibodies, Monoclonal</term>
<term>Binding Sites</term>
<term>Blotting, Western</term>
<term>Cell Adhesion</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Humans</term>
<term>Melanoma</term>
<term>Molecular Sequence Data</term>
<term>Platelet Membrane Glycoproteins (chemistry)</term>
<term>Platelet Membrane Glycoproteins (genetics)</term>
<term>Platelet Membrane Glycoproteins (metabolism)</term>
<term>Properdin (chemistry)</term>
<term>Properdin (genetics)</term>
<term>Repetitive Sequences, Nucleic Acid</term>
<term>Sequence Homology, Nucleic Acid</term>
<term>Thrombospondins</term>
<term>Tumor Cells, Cultured</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Adhérence cellulaire</term>
<term>Anticorps monoclonaux</term>
<term>Cellules cancéreuses en culture</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéines de membrane plaquettaire ()</term>
<term>Glycoprotéines de membrane plaquettaire (génétique)</term>
<term>Glycoprotéines de membrane plaquettaire (métabolisme)</term>
<term>Humains</term>
<term>Mélanome</term>
<term>Properdine ()</term>
<term>Properdine (génétique)</term>
<term>Similitude de séquences d'acides nucléiques</term>
<term>Sites de fixation</term>
<term>Séquence d'acides aminés</term>
<term>Séquences répétées d'acides nucléiques</term>
<term>Technique de Western</term>
<term>Test ELISA</term>
<term>Thrombospondines</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Platelet Membrane Glycoproteins</term>
<term>Properdin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Platelet Membrane Glycoproteins</term>
<term>Properdin</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Platelet Membrane Glycoproteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Thrombospondins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines de membrane plaquettaire</term>
<term>Properdine</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines de membrane plaquettaire</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Binding Sites</term>
<term>Blotting, Western</term>
<term>Cell Adhesion</term>
<term>Enzyme-Linked Immunosorbent Assay</term>
<term>Humans</term>
<term>Melanoma</term>
<term>Molecular Sequence Data</term>
<term>Repetitive Sequences, Nucleic Acid</term>
<term>Sequence Homology, Nucleic Acid</term>
<term>Tumor Cells, Cultured</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Adhérence cellulaire</term>
<term>Anticorps monoclonaux</term>
<term>Cellules cancéreuses en culture</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéines de membrane plaquettaire</term>
<term>Humains</term>
<term>Mélanome</term>
<term>Properdine</term>
<term>Similitude de séquences d'acides nucléiques</term>
<term>Sites de fixation</term>
<term>Séquence d'acides aminés</term>
<term>Séquences répétées d'acides nucléiques</term>
<term>Technique de Western</term>
<term>Test ELISA</term>
<term>Thrombospondines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Thrombospondin (TS) is a modular adhesive glycoprotein that contains three domains previously implicated in the attachment of cells to TS. These include the amino-terminal heparin-binding domain, the carboxy terminal cell or platelet-binding domain, and an RGDA sequence of TS. We have characterized a mAb against human TS, designated A4.1, which inhibits the attachment of human melanoma cells (G361) to TS. The epitope for A4.1 lies within the amino terminal half of the central stalklike region of TS which is distinct from the three known cell attachment sites. This region of TS is recovered in a 50-kD peptide after chymotryptic digestion of TS in EDTA. It contains the procollagen-like domain of TS as well as three type I repeats of a 60-residue segment homologous to two malarial proteins and the complement proteins properdin, and factors C6 through C9. The purified chymotryptic fragment is an effective attachment factor for G361 cells. A4.1 blocks adhesion to the 50-kD domain, as do some sulfated glycoconjugates. RGD (and RGE) peptides and mAbs against other domains of TS are not inhibitory. Peptides (19 mers) based on the core homology sequence of the three type I repeats of TS are potent attachment factors for these cells, and this adhesion is also inhibited by sulfated glycoconjugates. A polyclonal antibody raised against one of these peptides inhibits adhesion of G361 cells to the peptides, to the 50-kD fragment and to intact TS. Thus a new cell-adhesion site has been identified in TS whose sequence is very similar to the site identified in region II of the circumsporozoite protein of malaria parasites (Rich, K. A., F. W. George IV, J. L. Law, and W. J. Martin. 1990. Science (Wash. DC) 249:1574-1577. Thus there may be a common receptor which binds TS, malarial proteins, and properdin.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1999454</PMID>
<DateCompleted><Year>1991</Year>
<Month>04</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>08</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9525</ISSN>
<JournalIssue CitedMedium="Print"><Volume>112</Volume>
<Issue>5</Issue>
<PubDate><Year>1991</Year>
<Month>Mar</Month>
</PubDate>
</JournalIssue>
<Title>The Journal of cell biology</Title>
<ISOAbbreviation>J. Cell Biol.</ISOAbbreviation>
</Journal>
<ArticleTitle>The properdin-like type I repeats of human thrombospondin contain a cell attachment site.</ArticleTitle>
<Pagination><MedlinePgn>1031-40</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Thrombospondin (TS) is a modular adhesive glycoprotein that contains three domains previously implicated in the attachment of cells to TS. These include the amino-terminal heparin-binding domain, the carboxy terminal cell or platelet-binding domain, and an RGDA sequence of TS. We have characterized a mAb against human TS, designated A4.1, which inhibits the attachment of human melanoma cells (G361) to TS. The epitope for A4.1 lies within the amino terminal half of the central stalklike region of TS which is distinct from the three known cell attachment sites. This region of TS is recovered in a 50-kD peptide after chymotryptic digestion of TS in EDTA. It contains the procollagen-like domain of TS as well as three type I repeats of a 60-residue segment homologous to two malarial proteins and the complement proteins properdin, and factors C6 through C9. The purified chymotryptic fragment is an effective attachment factor for G361 cells. A4.1 blocks adhesion to the 50-kD domain, as do some sulfated glycoconjugates. RGD (and RGE) peptides and mAbs against other domains of TS are not inhibitory. Peptides (19 mers) based on the core homology sequence of the three type I repeats of TS are potent attachment factors for these cells, and this adhesion is also inhibited by sulfated glycoconjugates. A polyclonal antibody raised against one of these peptides inhibits adhesion of G361 cells to the peptides, to the 50-kD fragment and to intact TS. Thus a new cell-adhesion site has been identified in TS whose sequence is very similar to the site identified in region II of the circumsporozoite protein of malaria parasites (Rich, K. A., F. W. George IV, J. L. Law, and W. J. Martin. 1990. Science (Wash. DC) 249:1574-1577. Thus there may be a common receptor which binds TS, malarial proteins, and properdin.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Prater</LastName>
<ForeName>C A</ForeName>
<Initials>CA</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Plotkin</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jaye</LastName>
<ForeName>D</ForeName>
<Initials>D</Initials>
</Author>
<Author ValidYN="Y"><LastName>Frazier</LastName>
<ForeName>W A</ForeName>
<Initials>WA</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Cell Biol</MedlineTA>
<NlmUniqueID>0375356</NlmUniqueID>
<ISSNLinking>0021-9525</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010980">Platelet Membrane Glycoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D019699">Thrombospondins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>11016-39-0</RegistryNumber>
<NameOfSubstance UI="D011414">Properdin</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002448" MajorTopicYN="Y">Cell Adhesion</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008545" MajorTopicYN="N">Melanoma</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010980" MajorTopicYN="N">Platelet Membrane Glycoproteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011414" MajorTopicYN="N">Properdin</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012091" MajorTopicYN="N">Repetitive Sequences, Nucleic Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012689" MajorTopicYN="N">Sequence Homology, Nucleic Acid</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019699" MajorTopicYN="N">Thrombospondins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014407" MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year>
<Month>3</Month>
<Day>1</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>1991</Year>
<Month>3</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>1991</Year>
<Month>3</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">1999454</ArticleId>
<ArticleId IdType="pmc">PMC2288870</ArticleId>
<ArticleId IdType="doi">10.1083/jcb.112.5.1031</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>J Cell Biol. 1984 Feb;98(2):646-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6693501</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1990 Sep 28;249(4976):1574-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2120774</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1985 May;82(10):3472-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2582413</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1985 Aug 5;260(16):9405-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3926767</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1985 Sep;101(3):1059-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4030891</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1985 Oct;101(4):1434-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2413043</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1985 Jul 30;24(16):4270-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4052397</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1986 Feb 5;261(4):1962-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2418018</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Exp Cell Res. 1986 Dec;167(2):376-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3770094</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1986 Nov;103(5):1635-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2430973</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1987 Jan;104(1):131-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3793757</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 1987 Jan 23;235(4787):442-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2432664</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Clin Invest. 1987 Apr;79(4):1054-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2435757</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Ann N Y Acad Sci. 1986;485:273-87</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3471148</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1987 May;104(5):1413-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3571333</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1987 Jun 25;262(18):8821-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3597395</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Res. 1987 Aug 1;47(15):4130-3</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3607754</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1987 Aug;105(2):625-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3305519</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1987 Oct;105(4):1603-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2444599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1987 Nov;105(5):2409-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3680388</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1988 Feb;106(2):415-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2448314</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1988 May 5;263(13):6400-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3129423</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Clin Invest. 1988 May;81(5):1537-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2452837</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1988 Jul 25;263(21):10162-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3164720</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1988 Sep 1;335(6185):79-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3045563</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1988 Sep 1;335(6185):82-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3045564</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1988;57:375-413</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2972252</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1988 Dec 15;263(35):19112-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3198614</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1988 Dec;107(6 Pt 1):2351-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2848850</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1988 Dec;107(6 Pt 2):2737-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3204123</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arteriosclerosis. 1989 Jan-Feb;9(1):21-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2463827</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1989 Feb 10;56(3):345-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2464438</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1989 Feb 15;264(5):2885-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2521631</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Clin Invest. 1989 Mar;83(3):994-1001</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2522106</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Clin Exp Metastasis. 1989 May-Jun;7(3):265-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2647330</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Exp Cell Res. 1989 Jun;182(2):473-81</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2470606</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1989 Jun;108(6):2495-505</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2661564</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1989 Jul 14;58(1):95-101</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2473841</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1989 Oct 25;264(30):17971-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2808359</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1989 Oct 25;264(30):18041-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2808363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1990 Feb 15;265(5):2852-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2303431</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1990 Apr;110(4):1275-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2182649</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1990 Aug;111(2):765-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1696271</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1990 Sep;87(17):6624-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1697685</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1984 Aug 25;259(16):10100-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6236212</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Missouri (État)</li>
</region>
</list>
<tree><noCountry><name sortKey="Frazier, W A" sort="Frazier, W A" uniqKey="Frazier W" first="W A" last="Frazier">W A Frazier</name>
<name sortKey="Jaye, D" sort="Jaye, D" uniqKey="Jaye D" first="D" last="Jaye">D. Jaye</name>
<name sortKey="Plotkin, J" sort="Plotkin, J" uniqKey="Plotkin J" first="J" last="Plotkin">J. Plotkin</name>
</noCountry>
<country name="États-Unis"><region name="Missouri (État)"><name sortKey="Prater, C A" sort="Prater, C A" uniqKey="Prater C" first="C A" last="Prater">C A Prater</name>
</region>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Checkpoint

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002822 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 002822 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    MersV1
   |flux=    PubMed
   |étape=   Checkpoint
   |type=    RBID
   |clé=     pubmed:1999454
   |texte=   The properdin-like type I repeats of human thrombospondin contain a cell attachment site.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i   -Sk "pubmed:1999454" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd   \
       | NlmPubMed2Wicri -a MersV1

This area was generated with Dilib version V0.6.33.
Data generation: Mon Apr 20 23:26:43 2020. Site generation: Sat Mar 27 09:06:09 2021

	Serveur d'exploration MERS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration MERS

The properdin-like type I repeats of human thrombospondin contain a cell attachment site.

The properdin-like type I repeats of human thrombospondin contain a cell attachment site.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki