13 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
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Protease inhibitors: current status and future prospects.

University of Queensland
Design and synthesis of thrombin inhibitors: analogues of MD-805 with reduced stereogenicity and improved potency.

Novartis Horsham Research Centre
Design and structure-activity relationships of potent and selective inhibitors of blood coagulation factor Xa.

Rh£Ne-Poulenc Rorer
Synthesis and structure-activity relationships of potent thrombin inhibitors: piperazides of 3-amidinophenylalanine.

Klinikum Der Friedrich-Schiller-Universit£T Jena
New mechanism-based inactivators of trypsin-like proteinases. Selective inactivation of urokinase by functionalized cyclopeptides incorporating a sulfoniomethyl-substituted m-aminobenzoic acid residue.

Cnrs-Cercoa
Novel thrombin inhibitors incorporating weakly basic heterobicyclic P1-arginine mimetics: optimization via modification of P1 and P3 moieties.

University of Ljubljana
3-Amidinophenylalanine-based inhibitors of urokinase.

UniversitäT Jena
Design of benzamidine-type inhibitors of factor Xa.

Institut FüR Biochemie
Design, synthesis, and evolution of a novel, selective, and orally bioavailable class of thrombin inhibitors: P1-argininal derivatives incorporating P3-P4 lactam sulfonamide moieties.

Corvas International
Potent and selective thrombin inhibitors incorporating the constrained arginine mimic l-3-piperidyl(N-guanidino)alanine at P1.

Corvas International
Active site-directed synthetic thrombin inhibitors: synthesis, in vitro and in vivo activity profile of BMY 44621 and analogs. An examination of the role of the amino group in the D-Phe-Pro-Arg-H series.

Bristol-Myers Squibb Pharmaceutical Research Institute
Nonpeptidic inhibitors of human leukocyte elastase. 2. Design, synthesis, and in vitro activity of a series of 3-amino-6-arylopyridin-2-one trifluoromethyl ketones.

Zeneca Pharmaceuticals Group
SMall Molecule Growth 2001 (SMoG2001): an improved knowledge-based scoring function for protein-ligand interactions.

Harvard University