Linked Life Data

17127442

Source:http://linkedlifedata.com/resource/pubmed/id/17127442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-11-27
pubmed:abstractText
Platelets function physiologically in mediating hemostasis, but are also associated with many pathological conditions, such as thrombosis, which can lead to myocardial infarction and/or stroke. Therefore, the study of platelet regulation and signaling has been of great interest and is necessary for generating effective anti-platelet therapeutics. One platelet signaling molecule of particular interest is the integrin alphaIIb beta3, which binds Fg and mediates platelet cross-linking. The integrin itself as well as cytoplasmic proteins that interact with alphaIIb beta3 have become potential targets for anti-platelet therapies. One such protein that has been shown to directly regulate alphaIIb beta3 function is calcium- and integrin-binding protein 1 (CIB1). CIB1 has been implicated in alphaIIb beta3 activation and outside-in signaling through the integrin. By increasing our understanding of CIB1 and other proteins that like it, associate with integrin alphaIIb beta3, and the signaling events that result from those interactions, we may bring ourselves closer to more effective therapies. In the present work, we explore known cytoplasmic binding partners of the integrin alphaIIb beta3 and their effect on alphaIIb beta3, focusing on CIB1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1093-4715
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2038-49
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Cytoplasmic binding partners of the platelet integrin alphaIIb beta3.
pubmed:affiliation
Delaware Biotechnology Institute, Newark, DE, USA.
pubmed:publicationType
Journal Article, Review