2014
Correction to Substrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase
Baguley T, Xu H, Chatterjee M, Nairn A, Lombroso P, Ellman J. Correction to Substrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase. Journal Of Medicinal Chemistry 2014, 57: 10564-10564. PMCID: PMC4364512, DOI: 10.1021/jm5018847.Peer-Reviewed Original Research
2007
Characterization and Optimization of Selective, Nonpeptidic Inhibitors of Cathepsin S with an Unprecedented Binding Mode †
Inagaki H, Tsuruoka H, Hornsby M, Lesley SA, Spraggon G, Ellman JA. Characterization and Optimization of Selective, Nonpeptidic Inhibitors of Cathepsin S with an Unprecedented Binding Mode †. Journal Of Medicinal Chemistry 2007, 50: 2693-2699. PMID: 17469812, DOI: 10.1021/jm070111+.Peer-Reviewed Original ResearchConceptsUnprecedented binding modePotent cathepsin S inhibitorsBinding modesX-ray structureLow molecular weightCathepsin S inhibitorsNonpeptidic inhibitorsK. CharacterizationMolecular weightS inhibitorsAldehyde inhibitorsFragment identificationCleavage efficiencyCathepsin SInhibitor 2SubstrateSelectivityScreening methodStructureKi valuesComplexesCathepsin BConversionCharacterizationSelectiveSubstrate‐Based Fragment Identification and Optimization for Inhibitor Discovery
Ellman J. Substrate‐Based Fragment Identification and Optimization for Inhibitor Discovery. The FASEB Journal 2007, 21: a209-a209. DOI: 10.1096/fasebj.21.5.a209-c.Peer-Reviewed Original ResearchFragment-based approachSmall molecule ligandsFragment-based methodsMolecule ligandsFragment approachInhibitor discoveryLow molecular weight inhibitorsEfficient conversionSubstrate screeningLigandsHigh-throughput methodSelective ligandsFragment identificationWeight inhibitorsSelective low molecular weight inhibitorsCleavage efficiencyThroughput methodEfficient methodSelective drugsRelevant proteasesDesign principlesFragmentsDiscoveryLow affinityConversion
2006
Identification of Selective, Nonpeptidic Nitrile Inhibitors of Cathepsin S Using the Substrate Activity Screening Method
Patterson AW, Wood WJ, Hornsby M, Lesley S, Spraggon G, Ellman JA. Identification of Selective, Nonpeptidic Nitrile Inhibitors of Cathepsin S Using the Substrate Activity Screening Method. Journal Of Medicinal Chemistry 2006, 49: 6298-6307. PMID: 17034136, DOI: 10.1021/jm060701s.Peer-Reviewed Original ResearchConceptsPotent cathepsin S inhibitorsX-ray structureLow molecular weightGood selectivityTriazole substratesCathepsin S inhibitorsK. ConversionK. IdentificationTriazole inhibitorsCrystal formsSelectivityMolecular weightPharmacophoreS inhibitorsModerate potencyAldehyde inhibitorsScreening methodFragment identificationCathepsin S.Cleavage efficiencyCathepsin SSelect substratesSubstrateComplexesConversion
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