The tetrapeptide analogue of the cell attachment site of fibronectin inhibits platelet aggregation and fibrinogen binding to activated platelets.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference23 articles.
1. Fibronectins: multifunctional modular glycoproteins.
2. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
3. Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can autoinhibit fibronectin function.
4. Variants of the cell recognition site of fibronectin that retain attachment-promoting activity.
5. Fibrinogen and ADP-induced platelet aggregation
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