Title : Identification of a small molecule that modulates platelet glycoprotein Ib-von Willebrand factor interaction.

Pub. Date : 2012 Mar 16

PMID : 22232560






4 Functional Relationships(s)
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1 A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation. Ristocetin glycoprotein Ib platelet subunit alpha Homo sapiens
2 A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation. Ristocetin glycoprotein Ib platelet subunit alpha Homo sapiens
3 A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation. Ristocetin glycoprotein Ib platelet subunit alpha Homo sapiens
4 A selection of compounds showing good in silico docking scores into the predicted pockets was retained for testing their in vitro effect on VWF-GPIbalpha complex formation, by which we identified a compound that surprisingly stimulated the VWF-GPIbalpha binding in a ristocetin cofactor ELISA and increased platelet adhesion in whole blood to collagen under arterial shear rate but in contrast inhibited ristocetin-induced platelet aggregation. Ristocetin glycoprotein Ib platelet subunit alpha Homo sapiens