Lebetin peptides: Potent platelet aggregation inhibitors

Haemostasis

Volumn 31, Issue 3-6, 2001, Pages 207-210

  Marrakchi, N ^a   Mabrouk, K ^b   Regaya, I ^a   Sarray, S ^a   Fathallah, M ^b   Rochat, H ^b   El Ayeb, M ^a  

^a PASTEUR INSTITUTE OF TUNIS   (Tunisia)

^b CNRS   (France)

Author keywords

Antiplatelet aggregation; Lebetin peptides; Snake venom; Thrombocytopenia

Indexed keywords

ANTIGEN; ANTITHROMBOCYTIC AGENT; LYSINE; POLYMER; PROTEIN LEBETIN; UNCLASSIFIED DRUG; LEBETIN 1; LEBETIN 2; VIPER VENOM;

ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SYNTHESIS; THROMBOCYTE AGGREGATION; ANIMAL; CHEMISTRY; DRUG EFFECT; ISOLATION AND PURIFICATION; REVIEW; STRUCTURE ACTIVITY RELATION; THROMBOCYTE; THROMBOCYTOPENIA;

ANIMALS; BLOOD PLATELETS; HUMANS; PLATELET AGGREGATION INHIBITORS; STRUCTURE-ACTIVITY RELATIONSHIP; THROMBOCYTOPENIA; VIPER VENOMS;

EID: 0035742611     PISSN: 03010147     EISSN: None     Source Type: Journal    
DOI: 10.1159/000048064     Document Type: Article

References (7)

1. Biochemical mechanism of platelet activation
2. Binding of the snake venom derived proteins applagin and echistatin to the arginine-glycine-aspartic acid recognition sites of platelet glycoprotein IIb/IIIa complex receptor function
3. Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors
4. 3integrins
5. 5integrins in an RGD-independent manner
6. 1 integrin
7. Novel antiplatelet aggregation polypeptides from Vipera lebetina venom: Isolation and characterization