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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5963
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pubmed:dateCreated |
1984-6-20
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pubmed:abstractText |
The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronectin and present in at least five other proteins. This tetrapeptide may constitute a cellular recognition determinant common to several proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
309
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30-3
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6325925-Amino Acid Sequence,
pubmed-meshheading:6325925-Animals,
pubmed-meshheading:6325925-Cell Line,
pubmed-meshheading:6325925-Fibronectins,
pubmed-meshheading:6325925-Kidney,
pubmed-meshheading:6325925-Kinetics,
pubmed-meshheading:6325925-Oligopeptides,
pubmed-meshheading:6325925-Protein Conformation,
pubmed-meshheading:6325925-Rats,
pubmed-meshheading:6325925-Receptors, Cell Surface,
pubmed-meshheading:6325925-Receptors, Fibronectin
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pubmed:articleTitle |
Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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