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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-7-11
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pubmed:databankReference |
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pubmed:abstractText |
Annexin V, an abundant anticoagulant protein, has been proposed to exert its effects by self-assembling into highly ordered arrays on phospholipid membranes to form a protective anti-thrombotic shield at the cell surface. The protein exhibits very high-affinity calcium-dependent interactions with acidic phospholipid membranes, as well as specific binding to glycosaminoglycans (GAGs) such as heparin and heparan sulfate, a major component of cell surface proteoglycans. At present, there is no structural information to elucidate this interaction or the role it may play in annexin V function at the cell surface.
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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:month |
Jan
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
57-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11342135-Animals,
pubmed-meshheading:11342135-Annexin A5,
pubmed-meshheading:11342135-Binding Sites,
pubmed-meshheading:11342135-Biotinylation,
pubmed-meshheading:11342135-Calcium,
pubmed-meshheading:11342135-Cell Membrane,
pubmed-meshheading:11342135-Crystallography, X-Ray,
pubmed-meshheading:11342135-Electrons,
pubmed-meshheading:11342135-Heparin,
pubmed-meshheading:11342135-Kinetics,
pubmed-meshheading:11342135-Liposomes,
pubmed-meshheading:11342135-Models, Chemical,
pubmed-meshheading:11342135-Models, Molecular,
pubmed-meshheading:11342135-Mutagenesis, Site-Directed,
pubmed-meshheading:11342135-Mutation,
pubmed-meshheading:11342135-Oligosaccharides,
pubmed-meshheading:11342135-Phospholipids,
pubmed-meshheading:11342135-Rats,
pubmed-meshheading:11342135-Recombinant Proteins,
pubmed-meshheading:11342135-Streptavidin,
pubmed-meshheading:11342135-Surface Plasmon Resonance,
pubmed-meshheading:11342135-Swine,
pubmed-meshheading:11342135-Thermodynamics,
pubmed-meshheading:11342135-Time Factors
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pubmed:year |
2001
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pubmed:articleTitle |
Annexin V--heparin oligosaccharide complex suggests heparan sulfate--mediated assembly on cell surfaces.
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pubmed:affiliation |
Division of Medicinal and Natural Products Chemistry, Department of Chemistry, University of Iowa, Iowa City, IA 52242, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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