100 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
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Article Title
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Guanidinophenyl-substituted enol lactones as selective, mechanism-based inhibitors of trypsin-like serine proteases.
University of Illinois
Grassystatins A-C from marine cyanobacteria, potent cathepsin E inhibitors that reduce antigen presentation.
University of Florida
Solid-phase synthesis of naphthylamidines as factor VIIa/tissue factor inhibitors.
Berlex Biosciences
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
GRID/CPCA: a new computational tool to design selective ligands.
Boehringer Ingelheim Pharma
Potent thrombin inhibitors that probe the S1 subsite: tripeptide transition state analogues based on a heterocycle-activated carbonyl group.
R. W. Johnson Pharmaceutical Research Institute
Design and synthesis of potent and highly selective thrombin inhibitors.
F. Hoffmann-La Roche
Inhibition studies of some serine and thiol proteinases by new leupeptin analogues.
University of Arkansas
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
Selective inhibition of urokinase by substituted phenylguanidines: quantitative structure-activity relationship analyses.
Abbott Laboratories
Solid-phase synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors.
The Bristol-Myers Squibb Pharmaceutical Research Institute
D-Phe-Pro-Arg type thrombin inhibitors: unexpected selectivity by modification of the P1 moiety.
Basf
Noncovalent tripeptidic thrombin inhibitors incorporating amidrazone, amine and amidine functions at P1.
Life Science R & D, Lgci
Selectivity enhancement induced by substitution of non-natural analogues of arginine and lysine in arginine-based thrombin inhibitors.
Medical University of South Carolina
Synthesis and biological activity of P2–P4 azapeptidomimetic P1-argininal and P1-ketoargininamide derivatives: a novel class of serine protease inhibitors
TBA
Synthesis, evaluation, and crystallographic analysis of L-371,912: A potent and selective active-site thrombin inhibitor
TBA
Kinetic characterization of a peptide inhibitor of trypsin isolated from a synthetic peptide combinatorial library
TBA
Selective 3-amino-2-pyridinone acetamide thrombin inhibitors incorporating weakly basic partially saturated heterobicyclic P1-arginine mimetics.
University of Ljubljana
Synthesis of 2-guanidinyl pyridines and their trypsin inhibition and docking.
University College Dublin
Retro-binding thrombin active site inhibitors: identification of an orally active inhibitor of thrombin catalytic activity.
Bristol-Myers Squibb Pharmaceutical Research Institute
A mechanism-based probe for gp120-Hydrolyzing antibodies.
University of Texas-Houston Medical School
PRO_SELECT: combining structure-based drug design and array-based chemistry for rapid lead discovery. 2. The development of a series of highly potent and selective factor Xa inhibitors.
Protherics Molecular Design
Synthesis and structure-activity relationships of a new class of 1-oxacephem-based human chymase inhibitors.
Shionogi
Design, synthesis, and in vitro biological activity of benzimidazole based factor Xa inhibitors.
Berlex Biosciences
Synthesis, characterization, and structure-activity relationships of amidine-substituted (bis)benzylidene-cycloketone olefin isomers as potent and selective factor Xa inhibitors.
Berlex Biosciences
Non-peptidic phenyl-based thrombin inhibitors: exploring structural requirements of the S1 specificity pocket with amidines.
3-Dimensional Pharmaceuticals
Amidinohydrazones as guanidine bioisosteres: application to a new class of potent, selective and orally bioavailable, non-amide-based small-molecule thrombin inhibitors.
3-Dimensional Pharmaceuticals
Conformations of trypsin-bound amidine inhibitors of blood coagulant factor Xa by double REDOR NMR and MD simulations.
Washington University
Fluorobenzamidrazone thrombin inhibitors: influence of fluorine on enhancing oral absorption.
Biotech Research Institute
Design, synthesis, and activity of 2,6-diphenoxypyridine-derived factor Xa inhibitors.
Berlex Biosciences
Secondary structure peptide mimetics: design, synthesis, and evaluation of beta-strand mimetic thrombin inhibitors.
Molecumetics
Binding Loop Substitutions in the Cyclic Peptide SFTI-1 Generate Potent and Selective Chymase Inhibitors.
The University of Queensland
Novel acylguanidine containing thrombin inhibitors with reduced basicity at the P1 moiety.
Nv Organon Scientific Development Group
N-[2,2-dimethyl-3-(N-(4-cyanobenzoyl)amino)nonanoyl]-L-phenylalanine ethyl ester as a stable ester-type inhibitor of chymotrypsin-like serine proteases: structural requirements for potent inhibition of alpha-chymotrypsin.
Nippon Steel
Structural and functional analyses of benzamidine-based inhibitors in complex with trypsin: implications for the inhibition of factor Xa, tPA, and urokinase.
Institut FüR Biochemie
Highly Potent and Selective Plasmin Inhibitors Based on the Sunflower Trypsin Inhibitor-1 Scaffold Attenuate Fibrinolysis in Plasma.
The University of Queensland
Benzylamine-based selective and orally bioavailable inhibitors of thrombin.
Biotech Research Institute
Design, synthesis, and biological activity of novel purine and bicyclic pyrimidine factor Xa inhibitors.
Berlex Biosciences
Potent and efficacious thienylamidine-incorporated thrombin inhibitors.
Biotech Research Institute
Rational design, synthesis, and X-ray structure of selective noncovalent thrombin inhibitors.
Novartis Pharma
Discovery of N-[2-[5-[Amino(imino)methyl]-2-hydroxyphenoxy]-3, 5-difluoro-6-[3-(4, 5-dihydro-1-methyl-1H-imidazol-2-yl)phenoxy]pyridin-4-yl]-N-methylgl y cine (ZK-807834): a potent, selective, and orally active inhibitor of the blood coagulation enzyme factor Xa.
Berlex Biosciences
(Z,Z)-2,7-Bis(4-amidinobenzylidene)cycloheptan-1-one: identification of a highly active inhibitor of blood coagulation factor Xa.
Berlex Biosciences
Protein-Induced Change in Ligand Protonation during Trypsin and Thrombin Binding: Hint on Differences in Selectivity Determinants of Both Proteins?
Philipps-University Marburg
Assessment of solvation effects on calculated binding affinity differences: trypsin inhibition by flavonoids as a model system for congeneric series.
Universidad De Alcalá
Discovery of a novel, selective, and orally bioavailable class of thrombin inhibitors incorporating aminopyridyl moieties at the P1 position.
Merck Research Laboratories
Iterative Optimization of the Cyclic Peptide SFTI-1 Yields Potent Inhibitors of Neutrophil Proteinase 3.
The University of Queensland
Design of Specific Serine Protease Inhibitors Based on a Versatile Peptide Scaffold: Conversion of a Urokinase Inhibitor to a Plasma Kallikrein Inhibitor.
Aarhus University
Characterization of a class of peptide boronates with neutral P1 side chains as highly selective inhibitors of thrombin.
Thrombosis Research Institute
Structure-activity study of tripeptide thrombin inhibitors using alpha-alkyl amino acids and other conformationally constrained amino acid substitutions.
Eli Lilly
Aromatic amidines: comparison of their ability to block respiratory syncytial virus induced cell fusion and to inhibit plasmin, urokinase, thrombin, and trypsin.
TBA
Three-dimensional quantitative structure-activity relationship analyses using comparative molecular field analysis and comparative molecular similarity indices analysis to elucidate selectivity differences of inhibitors binding to trypsin, thrombin, and factor Xa.
University of Marburg
Cyclotides, a versatile ultrastable micro-protein scaffold for biotechnological applications.
University of Southern California
Engineering potent mesotrypsin inhibitors based on the plant-derived cyclic peptide, sunflower trypsin inhibitor-1.
The University of Queensland
Inhibition of human leukocyte elastase. 1. Inhibition by C-7-substituted cephalosporin tert-butyl esters.
Merck Sharp and Dohme Research Laboratories
Effect of conformational mobility and hydrogen-bonding interactions on the selectivity of some guanidinoaryl-substituted mechanism-based inhibitors of trypsin-like serine proteases.
University of Illinois
Tailored cyclodepsipeptides as potent non-covalent serine protease inhibitors
UniversitÄT Duisburg-Essen
Polyphenol fatty acid esters as serine protease inhibitors: a quantum-chemical QSAR analysis.
Slovak University of Technology
Identification and characterization of nonsubstrate based inhibitors of the essential dengue and West Nile virus proteases.
University of Alabama At Birmingham
Design, parallel synthesis, and crystal structures of biphenyl antithrombotics as selective inhibitors of tissue factor FVIIa complex. Part 1: Exploration of S2 pocket pharmacophores.
Biocryst Pharmaceuticals
Structure-based design of novel guanidine/benzamidine mimics: potent and orally bioavailable factor Xa inhibitors as novel anticoagulants.
Bristol-Myers Squibb
Structural basis for inhibition promiscuity of dual specific thrombin and factor Xa blood coagulation inhibitors.
Boehringer Ingelheim Pharma
Preparation, characterization, and the crystal structure of the inhibitor ZK-807834 (CI-1031) complexed with factor Xa.
Berlex
Crystallographic analysis of potent and selective factor Xa inhibitors complexed to bovine trypsin.
Berlex
Thiophene-anthranilamides as highly potent and orally available factor xa inhibitors
Berlex Biosciences
Crystals of the urokinase type plasminogen activator variant beta(c)-uPAin complex with small molecule inhibitors open the way towards structure-based drug design.
Max-Planck-Institut Fuer Biochemie
A selective, slow binding inhibitor of factor VIIa binds to a nonstandard active site conformation and attenuates thrombus formation in vivo.
Genentech
Elaborate manifold of short hydrogen bond arrays mediating binding of active site-directed serine protease inhibitors.
Celera
Structural basis for selectivity of a small molecule, S1-binding, submicromolar inhibitor of urokinase-type plasminogen activator.
Axys Pharmaceutical
Engineering inhibitors highly selective for the S1 sites of Ser190 trypsin-like serine protease drug targets.
Axys Pharmaceutical
In-depth study of tripeptide-based alpha-ketoheterocycles as inhibitors of thrombin. Effective utilization of the S1' subsite and its implications to structure-based drug design.
Johnson & Johnson Pharmaceutical
A novel serine protease inhibition motif involving a multi-centered short hydrogen bonding network at the active site.
Axys Pharmaceuticals
Dose-dependent antithrombotic activity of an orally active tissue factor/factor VIIa inhibitor without concomitant enhancement of bleeding propensity.
F. Hoffmann-La Roche
Design of selective phenylglycine amide tissue factor/factor VIIa inhibitors.
F. Hoffmann-La Roche
Selective and orally bioavailable phenylglycine tissue factor/factor VIIa inhibitors.
F. Hoffmann-La Roche
Sulfonamidopyrrolidinone factor Xa inhibitors: potency and selectivity enhancements via P-1 and P-4 optimization.
Rhone-Poulenc Rorer
Preparation of 1-(4-methoxyphenyl)-1H-pyrazolo[4,3-d]pyrimidin-7(6H)-ones as potent, selective and bioavailable inhibitors of coagulation factor Xa.
Bristol-Myers Squibb
Discovery of 1-(3'-aminobenzisoxazol-5'-yl)-3-trifluoromethyl-N-[2-fluoro-4-[(2'-dimethylaminomethyl)imidazol-1-yl]phenyl]-1H-pyrazole-5-carboxyamide hydrochloride (razaxaban), a highly potent, selective, and orally bioavailable factor Xa inhibitor.
Bristol-Myers Squibb Pharmaceutical Research Institute
Molecular structures of human factor Xa complexed with ketopiperazine inhibitors: preference for a neutral group in the S1 pocket.
Aventis Pharma
Phylogenomic Analysis of the Microviridin Biosynthetic Pathway Coupled with Targeted Chemo-Enzymatic Synthesis Yields Potent Protease Inhibitors.
University of Helsinki