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Conservation of glutamine-rich transactivation function between yeast and humans 总被引:7,自引:0,他引:7 下载免费PDF全文
Escher D Bodmer-Glavas M Barberis A Schaffner W 《Molecular and cellular biology》2000,20(8):2774-2782
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Aux/IAA proteins contain a potent transcriptional repression domain 总被引:21,自引:0,他引:21
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New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa. For the activators studied, the equilibrium dissociation constant (K(D)) of the interaction with plasma antithrombin varies nearly 53-fold, with the highest affinity of 1.8 microM observed for morin sulfate, while the acceleration in factor Xa inhibition varies 2.6-fold. The results demonstrate that antithrombin binding and activation is a common property of these small sulfated molecules and suggests plausible directions for designing more potent activators. 相似文献