bms-262084 and Inflammation

bms-262084 has been researched along with Inflammation* in 1 studies

Other Studies

1 other study(ies) available for bms-262084 and Inflammation

Article	Year
Synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors. Bioorganic & medicinal chemistry letters, 2002, Nov-04, Volume: 12, Issue:21 A series of N1-activated C4-carboxy azetidinones was prepared and tested as inhibitors of human tryptase. The key stereochemical and functional features required for potency, serine protease specificity and aqueous stability were determined. From these studies compound 2, BMS-262084, was identified as a potent and selective tryptase inhibitor which, when dosed intratracheally in ovalbumin-sensitized guinea pigs, reduced allergen-induced bronchoconstriction and inflammatory cell infiltration into the lung. Topics: Animals; Anti-Asthmatic Agents; Asthma; Azetidines; Bronchoconstriction; Crystallography, X-Ray; Extracellular Space; Guinea Pigs; Half-Life; Humans; Inflammation; Lung; Molecular Conformation; Ovalbumin; Piperazines; Serine Endopeptidases; Serine Proteinase Inhibitors; Structure-Activity Relationship; Tryptases	2002

Article

Year

Synthesis and SAR of 4-carboxy-2-azetidinone mechanism-based tryptase inhibitors.

Bioorganic & medicinal chemistry letters, 2002, Nov-04, Volume: 12, Issue:21

A series of N1-activated C4-carboxy azetidinones was prepared and tested as inhibitors of human tryptase. The key stereochemical and functional features required for potency, serine protease specificity and aqueous stability were determined. From these studies compound 2, BMS-262084, was identified as a potent and selective tryptase inhibitor which, when dosed intratracheally in ovalbumin-sensitized guinea pigs, reduced allergen-induced bronchoconstriction and inflammatory cell infiltration into the lung.

Topics: Animals; Anti-Asthmatic Agents; Asthma; Azetidines; Bronchoconstriction; Crystallography, X-Ray; Extracellular Space; Guinea Pigs; Half-Life; Humans; Inflammation; Lung; Molecular Conformation; Ovalbumin; Piperazines; Serine Endopeptidases; Serine Proteinase Inhibitors; Structure-Activity Relationship; Tryptases

2002