35 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
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Article Title
Organization
Isolation and structure of SCH 351633: a novel hepatitis C virus (HCV) NS3 protease inhibitor from the fungus Penicillium griseofulvum.
Schering-Plough Research Institute
Phenylglycine as a novel P2 scaffold in hepatitis C virus NS3 protease inhibitors.
Uppsala University
Design and synthesis of depeptidized macrocyclic inhibitors of hepatitis C NS3-4A protease using structure-based drug design.
Schering-Plough Research Institute
Antiviral compounds from traditional Chinese medicines Galla Chinese as inhibitors of HCV NS3 protease.
Peking University
Inhibition of hepatitis C virus NS3 protease activity by product-based peptides is dependent on helicase domain.
Uppsala University
NMR line-broadening and transferred NOESY as a medicinal chemistry tool for studying inhibitors of the hepatitis C virus NS3 protease domain.
Boehringer Ingelheim Pharmaceuticals
Highly potent and selective peptide-based inhibitors of the hepatitis C virus serine protease: towards smaller inhibitors.
Boehringer Ingelheim Pharmaceuticals
Peptide-based inhibitors of the hepatitis C virus serine protease.
Boehringer Ingelheim (Canada)
P2-P4 macrocyclic inhibitors of hepatitis C virus NS3-4A serine protease.
Schering-Plough Research Institute
Discovery of proline sulfonamides as potent and selective hepatitis C virus NS5b polymerase inhibitors. Evidence for a new NS5b polymerase binding site.
Wyeth Research
Design and synthesis of 3,4-dihydro-1H-[1]-benzothieno[2,3-c]pyran and 3,4-dihydro-1H-pyrano[3,4-b]benzofuran derivatives as non-nucleoside inhibitors of HCV NS5B RNA dependent RNA polymerase.
Wyeth Research
Design, synthesis, and biological activity of m-tyrosine-based 16- and 17-membered macrocyclic inhibitors of hepatitis C virus NS3 serine protease.
Schering-Plough Research Institute
Synthesis and biological activity of macrocyclic inhibitors of hepatitis C virus (HCV) NS3 protease.
Schering-Plough Research Institute
Investigation of glycine alpha-ketoamide HCV NS3 protease inhibitors: effect of carboxylic acid isosteres.
Pharmaceutical Research Institute
The design and enzyme-bound crystal structure of indoline based peptidomimetic inhibitors of hepatitis C virus NS3 protease.
Mrl Rome
P4 and P1' optimization of bicycloproline P2 bearing tetrapeptidyl alpha-ketoamides as HCV protease inhibitors.
Eli Lilly
P4 cap modified tetrapeptidyl alpha-ketoamides as potent HCV NS3 protease inhibitors.
Eli Lilly
Non-peptidic small-molecule inhibitors of the single-chain hepatitis C virus NS3 protease/NS4A cofactor complex discovered by structure-based NMR screening.
Schering-Plough Research Institute
Inhibitors of hepatitis C virus NS3.4A protease 2. Warhead SAR and optimization.
Vertex Pharmaceuticals
NMR structural characterization of peptide inhibitors bound to the Hepatitis C virus NS3 protease: design of a new P2 substituent.
Boehringer Ingelheim (Canada)
Two antiviral compounds from the plant Stylogne cauliflora as inhibitors of HCV NS3 protease.
Schering-Plough Research Institute
Novel, potent phenethylamide inhibitors of the hepatitis C virus (HCV) NS3 protease: probing the role of P2 aryloxyprolines with hybrid structures.
Mrl Rome
Design and synthesis of potent, non-peptide inhibitors of HCV NS3 protease.
Bristol-Myers Squibb
Design and synthesis of bicyclic pyrimidinone-based HCV NS3 protease inhibitors.
Bristol-Myers Squibb Pharmaceutical Research Institute
Phenethyl amides as novel noncovalent inhibitors of hepatitis C virus NS3/4A protease: discovery, initial SAR, and molecular modeling.
Mrl Rome
P1 Phenethyl peptide boronic acid inhibitors of HCV NS3 protease.
Bristol-Myers Squibb Pharmaceutical Research Institute
Azapeptides as inhibitors of the hepatitis C virus NS3 serine protease.
Schering-Plough Research Institute
Solution and solid-phase synthesis of potent inhibitors of hepatitis C virus NS3 proteinase.
Roche Discovery Welwyn
Structure-activity relationship studies of a bisbenzimidazole-based, Zn(2+)-dependent inhibitor of HCV NS3 serine protease.
Bristol-Myers Squibb Pharmaceutical Research Institute
Arylalkylidene rhodanine with bulky and hydrophobic functional group as selective HCV NS3 protease inhibitor.
Institute of Molecular and Cell Biology
Alpha-ketoamides, alpha-ketoesters and alpha-diketones as HCV NS3 protease inhibitors.
Dupont Pharmaceuticals
Potent noncovalent thrombin inhibitors that utilize the unique amino acid D-dicyclohexylalanine in the P3 position. Implications on oral bioavailability and antithrombotic efficacy.
Merck Research Laboratories