2016
Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy
Tsutsui Y, Deredge D, Wintrode P, Hays F. Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy. Scientific Reports 2016, 6: 30832. PMID: 27480221, PMCID: PMC4969603, DOI: 10.1038/srep30832.Peer-Reviewed Original ResearchConceptsHuman c-SrcC-SrcNon-receptor tyrosine kinase inhibitorsFunctional regulatory sitesC-Src SH3SH2 domainKinase domainHydrogen-deuterium exchangeKinase activationConformational dynamicsRegulatory sitesAllosteric siteMutation sitesKinase inhibitorsPatient tissuesInhibition strategiesAnti-neoplastic drugsPeptide ligandsDevelopment of TKICurrent study identifiesImatinib-resistant mutationsTyrosine kinase inhibitorsImatinib analogsMass spectrometryAllostery
2007
Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions.
Tsutsui Y, Wintrode P. Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions. Current Medicinal Chemistry 2007, 14: 2344-58. PMID: 17896983, DOI: 10.2174/092986707781745596.Peer-Reviewed Original ResearchMeSH KeywordsDeuteriumDeuterium Exchange MeasurementHydrogenMass SpectrometryMolecular StructureProtein BindingProtein ConformationProteinsConceptsProtein assembliesMolecular basisProtein structureNuclear magnetic resonance spectroscopyHydrogen/deuterium exchangeLarge protein assembliesD exchange processX-ray crystallographyDrugs/inhibitorsDynamics of proteinsBackbone amide hydrogensExchange processMagnetic resonance spectroscopyLocal structural environmentPatho-physiological processesViral capsid structureAmide hydrogensHXMSDeuterium exchangeMass spectrometrySmall sample requirementDrug designHigh-quality crystalsResonance spectroscopyProtein conformation