360791-67-9Relevant academic research and scientific papers
Development of serine protease inhibitors displaying a multicentered short (<2.3 ?) hydrogen bond binding mode: Inhibitors of urokinase-type plasminogen activator and factor Xa
Verner,Katz,Spencer,Allen,Hataye,Hruzewicz,Hui,Kolesnikov,Li,Luong,Martelli,Radika,Rai,She,Shrader,Sprengeler,Trapp,Wang,Young,Mackman
, p. 2753 - 2771 (2007/10/03)
Novel scaffolds that bind to serine proteases through a unique network of short hydrogen bonds to the catalytic Ser195 have been developed. The resulting potent serine protease inhibitors were designed from lead molecule 2-(2-hydroxyphenyl)1H-benzoimidazo
Derivatives of 5-amidine indole as inhibitors of thrombin catalytic activity
Iwanowicz, Edwin J.,Lau, Wan F.,Lin, James,Roberts, Daniel G. M.,Seiler, Steven M.
, p. 1339 - 1344 (2007/10/03)
Substituted 5-amidine indoles were constructed based upon a computational analysis of putative modes of binding to thrombin utilizing coordinates from the crystal structure of BMS-183,507-α-thrombin complex. These analogs display competitive kinetics for
