PMID

Data

Article Title

Organization

Synthesis and structure-activity relationships of novel selective factor Xa inhibitors with a tetrahydroisoquinoline ring.

Central Pharmaceutical Research Institute

Efficacious and orally bioavailable thrombin inhibitors based on a 2,5-thienylamidine at the P1 position: discovery of N-carboxymethyl-d-diphenylalanyl-l-prolyl[(5-amidino-2-thienyl)methyl]amide.

Lg Life Sciences

Discovery of 1-[3-(aminomethyl)phenyl]-N-3-fluoro-2'-(methylsulfonyl)-[1,1'-biphenyl]-4-yl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide (DPC423), a highly potent, selective, and orally bioavailable inhibitor of blood coagulation factor Xa.

Dupont Pharmaceuticals

Protease inhibitors: synthesis and QSAR study of novel classes of nonbasic thrombin inhibitors incorporating sulfonylguanidine and O-methylsulfonylisourea moieties at P1.

Universit£

Tetrahydro-isoquinoline-based factor Xa inhibitors.

Boehringer Mannheim

Development of an oxazolopyridine series of dual thrombin/factor Xa inhibitors via structure-guided lead optimization.

Merck Research Laboratories

Chlorothiophenecarboxamides as P1 surrogates of inhibitors of blood coagulation factor Xa.

Merck

Structure-based design of novel potent nonpeptide thrombin inhibitors.

Boehringer Ingelheim Pharma

Exploiting subsite S1 of trypsin-like serine proteases for selectivity: potent and selective inhibitors of urokinase-type plasminogen activator.

Axys Pharmaceuticals

1,2-Benzisothiazol-3-one 1,1-dioxide inhibitors of human mast cell tryptase.

Bristol-Myers Squibb Pharmaceutical Research Institute

Identification and initial structure-activity relationships of a novel class of nonpeptide inhibitors of blood coagulation factor Xa.

Collegeville