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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorYang, Qingliangen_US
dc.contributor.authorLi, Yien_US
dc.contributor.authorDou, Dengfengen_US
dc.contributor.authorGan, Xiangdongen_US
dc.contributor.authorMohan, Swathien_US
dc.contributor.authorGroutas, Christopher S.en_US
dc.contributor.authorStevenson, Laura E.en_US
dc.contributor.authorLai, Zhongen_US
dc.contributor.authorAlliston, Kevin R.en_US
dc.contributor.authorZhong, Jiayingen_US
dc.contributor.authorWilliams, Todd D.en_US
dc.contributor.authorGroutas, William C.en_US
dc.date.accessioned2012-02-06T17:16:40Z
dc.date.available2012-02-06T17:16:40Z
dc.date.issued2008-07-15en_US
dc.identifier18457652en_US
dc.identifier0372430en_US
dc.identifierS0003-9861(08)00205-1en_US
dc.identifierHL 57788/ R01 HL057788-05/ R01 HL057788-06/ R01 HL057788-07/ R01 HL057788-08en_US
dc.identifier.citationArchives of biochemistry and biophysics. 2008 Jul 15; 475(2): 115-20.en_US
dc.identifier.issn1096-0384en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://dx.doi.org/10.1016/j.abb.2008.04.020en_US
dc.identifier.urihttp://hdl.handle.net/10057/4337
dc.descriptionClick on the DOI link below to access the article.en_US
dc.description.abstractA new class of carbamylating agents based on the cyclosulfamide scaffold is reported. These compounds were found to be efficient time-dependent inhibitors of human neutrophil elastase (HNE). Exploitation of the three sites of diversity present in the cyclosulfamide scaffold yielded compounds which inhibited HNE but not proteinase 3 (PR 3) or bovine trypsin. The findings reported herein suggest that the introduction of appropriate recognition elements into the cyclosulfamide scaffold may lead to highly selective agents of potential value in the design of activity-based probes suitable for investigating proteases associated with the pathogenesis of chronic obstructive pulmonary disease.en_US
dc.description.sponsorshipNHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHS/ NHLBI NIH HHSen_US
dc.format.extent115-20en_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, N.I.H., Extramuralen_US
dc.subject.meshCyclizationen_US
dc.subject.meshDrug Designen_US
dc.subject.meshHumansen_US
dc.subject.meshLeukocyte Elastase/antagonists & inhibitorsen_US
dc.subject.meshSerine Endopeptidases/drug effectsen_US
dc.subject.meshSerine Proteinase Inhibitors/chemistryen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.subject.meshSulfonamides/chemical synthesisen_US
dc.subject.meshTime Factorsen_US
dc.subject.meshSerine Proteinase Inhibitors/pharmacologyen_US
dc.subject.meshSulfonamides/chemistryen_US
dc.subject.meshSulfonamides/pharmacologyen_US
dc.titleInhibition of serine proteases by a new class of cyclosulfamide-based carbamylating agentsen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2008, Elsevieren_US


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