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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorGroutas, William C.en_US
dc.contributor.authorChong, Lee S.en_US
dc.contributor.authorVenkataraman, Radhikaen_US
dc.contributor.authorEpp, Jeffrey B.en_US
dc.contributor.authorKuang, Rongzeen_US
dc.contributor.authorBrubaker, Michael J.en_US
dc.contributor.authorHouser-Archield, Nadeneen_US
dc.contributor.authorHuang, Heen_US
dc.contributor.authorMcClenahan, Jerald J.en_US
dc.date.accessioned2012-02-06T17:15:58Z
dc.date.available2012-02-06T17:15:58Z
dc.date.issued1993-08-16en_US
dc.identifier8352807en_US
dc.identifier0372516en_US
dc.identifierS0006291X83719935en_US
dc.identifierHL 38048en_US
dc.identifier.citationBiochemical and biophysical research communications. 1993 Aug 16; 194(3): 1491-9.en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10057/4288
dc.descriptionFull text of this article is not available in SOAR.en_US
dc.description.abstractNeutrophil-derived mediators such as, for example, the serine proteinase elastase, cathepsin G and proteinase 3, play a critical role in inflammatory lung disease. This report describes the design, synthesis and in vitro inhibitory activity of some novel mechanism-based inhibitors of human leukocyte elastase and cathepsin G. The design of the inhibitors is based on the Gabriel-Colman rearrangement. The behavior of the synthesized compounds toward elastase and cathepsin G with respect to inhibitory prowess, mode of interaction, specificity, etc., has been found to be dependent on the recognition and reactivity elements present in each inhibitor.en_US
dc.description.sponsorshipNHLBI NIH HHSen_US
dc.format.extent1491-9en_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.ispartofseriesBiochemical and biophysical research communicationsen_US
dc.relation.ispartofseriesBiochem. Biophys. Res. Commun.en_US
dc.sourceNLMen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshCathepsin Gen_US
dc.subject.meshCathepsins/antagonists & inhibitorsen_US
dc.subject.meshDrug Designen_US
dc.subject.meshHumansen_US
dc.subject.meshLeukocytes/enzymologyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPancreatic Elastase/antagonists & inhibitorsen_US
dc.subject.meshSerine Endopeptidasesen_US
dc.titleMechanism-based inhibitors of serine proteinases based on the Gabriel-Colman rearrangementen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1993, Elsevieren_US


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