Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-4-15
pubmed:abstractText
Monoclonal antibodies against cell surface receptors can be useful for the study of structural and biochemical features involved in protein interactions underlying platelet adhesion and aggregation. We report here the characterization of a monoclonal antibody, IID510g52 (hereafter referred to as IID5), which has been selected based on its specific binding properties against the platelet membrane glycoprotein IIIa. Characterization of the reactive epitope, including evolutionary conservation and identification of related IID5 target antigens in tumor cells, suggest that the IID5 epitope is implicated in the ligand-binding function of integrin receptors. Indeed, we show that this MoAb acts as a potent inhibitor of platelet aggregation and cell adhesion. Taken together, these results indicate that such a monoclonal may be a strategic tool for better understanding multiple integrin-mediated adhesive reactions, as well as the determination of interacting recognition sites.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0272-457X
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
741-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
A monoclonal antibody (IID510g52) for the determination of functional domains within integrin cell surface receptors.
pubmed:affiliation
Ludwig Institute for Cancer Research, São Paulo Branch, Brazil.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't