Peptide LSARLAF activates α(IIb)β3 on resting platelets and causes resting platelet aggregate formation without platelet shape change

Thrombosis Research

Volumn 89, Issue 1, 1998, Pages 31-40

  Derrick, Jerry M ^a   Loudon, Robert G ^a   Gartner, T Kent ^a  

^a UNIVERSITY OF MEMPHIS   (United States)

Author keywords

(IIb) 3; Fibrinogen receptor; GPIIb IIIa; Platelet agonist

Indexed keywords

PEPTIDE HORMONE;

ARTICLE; BINDING SITE; CELL ADHESION; CONFORMATIONAL TRANSITION; DRUG RECEPTOR BINDING; HUMAN; HUMAN CELL; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; SCANNING ELECTRON MICROSCOPY; THROMBOCYTE ACTIVATION; THROMBOCYTE ADHESION; THROMBOCYTE AGGLUTINATION; THROMBOCYTE SHAPE;

ADENOSINE DIPHOSPHATE; BLOOD PLATELETS; CELL SIZE; EPINEPHRINE; HUMANS; OLIGOPEPTIDES; PLATELET AGGREGATION; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX; PROTEIN CONFORMATION;

EID: 0031778169     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(97)00289-2     Document Type: Article

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