Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function.-Reference-Cited by-同舟云学术

Binding of the snake venom-derived proteins applaggin and echistatin to the arginine-glycine-aspartic acid recognition site(s) on platelet glycoprotein IIb.IIIa complex inhibits receptor function.

Published:1990-07 Issue:20 Volume:265 Page:11766-11772
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Savage B,Marzec U M,Chao B H,Harker L A,Maraganore J M,Ruggeri Z M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Agkistrodon piscivorus piscivorus platelet aggregation inhibitor: a potent inhibitor of platelet activation.

2. Chemical synthesis of echistatin, a potent inhibitor of platelet aggregation from Echis carinatus: synthesis and biological activity of selected analogs.

3. Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus.

4. New Perspectives in Cell Adhesion: RGD and Integrins

5. Cytoadhesins, Integrins, and Platelets

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