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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorWong, Tzutshinen_US
dc.contributor.authorGroutas, Christopher S.en_US
dc.contributor.authorMohan, Swathien_US
dc.contributor.authorLai, Zhongen_US
dc.contributor.authorAlliston, Kevin R.en_US
dc.contributor.authorVu, Nga T.en_US
dc.contributor.authorSchechter, Norman M.en_US
dc.contributor.authorGroutas, William C.en_US
dc.date.accessioned2012-02-06T17:15:46Z
dc.date.available2012-02-06T17:15:46Z
dc.date.issued2005-04-01en_US
dc.identifier15752703en_US
dc.identifier0372430en_US
dc.identifierS0003-9861(05)00052-4en_US
dc.identifierAI 45075/ HL 57788en_US
dc.identifier.citationArchives of biochemistry and biophysics. 2005 Apr 1; 436(1): 1-7.en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.abb.2005.01.022en_US
dc.identifier.urihttp://hdl.handle.net/10057/4260
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractWe describe herein the design, synthesis, and in vitro biochemical evaluation of a series of potent, time-dependent inhibitors of the mast cell-derived serine protease tryptase. The inhibitors were readily obtained by attaching various heterocyclic thiols, as well as a basic primary specificity residue P(1), to the 1,2,5-thiadiazolidin-3-one 1,1-dioxide scaffold. The inhibitors were found to be devoid of any inhibitory activity toward a neutral (elastase) or cysteine (papain) protease, however they were also fairly efficient inhibitors of bovine trypsin. The differential inhibition observed with trypsin suggests that enzyme selectivity can be optimized by exploiting differences in the S' subsites of the two enzymes. The results described herein demonstrate the versatility of the heterocyclic scaffold in fashioning mechanism-based inhibitors of neutral, basic, and acidic (chymo)trypsin-like serine proteases.en_US
dc.description.sponsorshipNIAID NIH HHS/ NHLBI NIH HHSen_US
dc.format.extent1-7en_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.meshAnimalsen_US
dc.subject.meshCattleen_US
dc.subject.meshChymotrypsin/chemistryen_US
dc.subject.meshCyclic S-Oxides/pharmacologyen_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshHeterocyclic Compounds/pharmacologyen_US
dc.subject.meshHumansen_US
dc.subject.meshLeukocyte Elastase/antagonists & inhibitorsen_US
dc.subject.meshPapain/antagonists & inhibitorsen_US
dc.subject.meshSerine Endopeptidases/drug effectsen_US
dc.subject.meshSerine Proteinase Inhibitors/chemical synthesisen_US
dc.subject.meshSulfides/pharmacologyen_US
dc.subject.meshThiadiazoles/chemical synthesisen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshTryptasesen_US
dc.subject.meshLeukocyte Elastase/drug effectsen_US
dc.subject.meshSerine Endopeptidases/metabolismen_US
dc.subject.meshSerine Proteinase Inhibitors/pharmacologyen_US
dc.subject.meshThiadiazoles/pharmacologyen_US
dc.title1,2,5-Thiadiazolidin-3-one 1,1-dioxide-based heterocyclic sulfides are potent inhibitors of human tryptaseen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2005, Elsevieren_US


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