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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorGroutas, William C.en_US
dc.contributor.authorEpp, Jeffrey B.en_US
dc.contributor.authorKuang, Rongzeen_US
dc.contributor.authorRuan, Sumeien_US
dc.contributor.authorChong, Lee S.en_US
dc.contributor.authorVenkataraman, Radhikaen_US
dc.contributor.authorTu, Juanen_US
dc.contributor.authorHe, Shuen_US
dc.contributor.authorYu, Hongyien_US
dc.contributor.authorFu, Qingfongen_US
dc.contributor.authorLi, Yue Heen_US
dc.contributor.authorTruong, Tien M.en_US
dc.contributor.authorVu, Nga T.en_US
dc.date.accessioned2012-02-06T17:15:22Z
dc.date.available2012-02-06T17:15:22Z
dc.date.issued2001-01-01en_US
dc.identifier11361013en_US
dc.identifier0372430en_US
dc.identifierS0003-9861(00)92139-8en_US
dc.identifierHL57788en_US
dc.identifier.citationArchives of biochemistry and biophysics. 2001 Jan 1; 385(1): 162-9.en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://dx.doi.org/10.1006/abbi.2000.2139en_US
dc.identifier.urihttp://hdl.handle.net/10057/4231
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractThe 1,2,5-thiadiazolidin-3-one 1,1 dioxide scaffold (I) embodies a motif that allows it to dock to the active site of (chymo)trypsin-like proteases in a predictable and substrate-like fashion. Consequently, inhibitors derived from this heterocyclic scaffold interact with both the S and S' subsites of an enzyme. Exploitation of binding interactions with both the S and S' subsites of a target enzyme may lead to compounds with greatly enhanced enzyme selectivity and inhibitory potency. This preliminary report describes the use of a series of compounds having the heterocyclic scaffold linked to various amino acids to probe the S' subsites of human leukocyte elastase (HLE), proteinase 3 (PR 3), and cathepsin G (Cat G). For comparative purposes, a series of compounds derived from a related scaffold, isothiazolidin-3-one 1,1 dioxide (II), was also generated. Several of the compounds were found to be highly potent and selective time-dependent inhibitors of HLE, PR 3, and Cat G.en_US
dc.description.sponsorshipNHLBI NIH HHSen_US
dc.format.extent162-9en_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.ispartofseriesArchives of biochemistry and biophysicsen_US
dc.relation.ispartofseriesArch. Biochem. Biophys.en_US
dc.sourceNLMen_US
dc.subjectResearch Support, Non-U.S. Gov'ten_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshCathepsin Gen_US
dc.subject.meshCathepsins/chemistryen_US
dc.subject.meshChymotrypsin/chemistryen_US
dc.subject.meshCyclic S-Oxides/chemistryen_US
dc.subject.meshHumansen_US
dc.subject.meshKineticsen_US
dc.subject.meshLeukocyte Elastase/chemistryen_US
dc.subject.meshModels, Chemicalen_US
dc.subject.meshMolecular Probes/chemistryen_US
dc.subject.meshMyeloblastinen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshSerine Endopeptidases/chemistryen_US
dc.subject.meshTemperatureen_US
dc.subject.meshThiazoles/chemistryen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshCathepsins/metabolismen_US
dc.subject.meshLeukocyte Elastase/metabolismen_US
dc.subject.meshSerine Endopeptidases/metabolismen_US
dc.title1,2,5-Thiadiazolidin-3-one 1,1 dioxide: a powerful scaffold for probing the S' subsites of (chymo)trypsin-like serine proteasesen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2001, Elsevieren_US


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