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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.authorKuang, Rongzeen_US
dc.contributor.authorEpp, Jeffrey B.en_US
dc.contributor.authorHouser-Archield, Nadeneen_US
dc.contributor.authorHuang, Heen_US
dc.contributor.authorHoidal, John R.en_US
dc.date.accessioned2012-02-06T17:15:59Z
dc.date.available2012-02-06T17:15:59Z
dc.date.issued1996-08-15en_US
dc.identifier8806743en_US
dc.identifier0372430en_US
dc.identifierS0003-9861(96)90350-1en_US
dc.identifierHL 38048en_US
dc.identifier.citationArchives of biochemistry and biophysics. 1996 Aug 15; 332(2): 335-40.en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://dx.doi.org/10.1006/abbi.1996.0350en_US
dc.identifier.urihttp://hdl.handle.net/10057/4289
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractAmino acid-derived phthalimide and saccharin derivatives have been investigated for their inhibitory activity toward the serine proteinases human leukocyte elastase, cathepsin G, and proteinase 3. The saccharin derivatives were found to be effective time-dependent inhibitors of elastase and proteinase 3 (kobs/[I] values ranged between 180 and 3620 M-1 S-1) and showed weak or no inhibition toward cathepsin G. The corresponding phthalimide derivatives were found to be inactive.en_US
dc.description.sponsorshipNHLBI NIH HHSen_US
dc.format.extent335-40en_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.subjectIn Vitroen_US
dc.subjectResearch Support, Non-U.S. Gov'ten_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCathepsin Gen_US
dc.subject.meshCathepsins/antagonists & inhibitorsen_US
dc.subject.meshDrug Designen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen Bondingen_US
dc.subject.meshLeukocyte Elastase/antagonists & inhibitorsen_US
dc.subject.meshLeukocytes/enzymologyen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMyeloblastinen_US
dc.subject.meshPhthalimides/chemistryen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshSaccharin/antagonists & inhibitorsen_US
dc.subject.meshSerine Endopeptidases/metabolismen_US
dc.subject.meshSerine Proteinase Inhibitors/chemistryen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.subject.meshLeukocyte Elastase/chemistryen_US
dc.subject.meshLeukocyte Elastase/geneticsen_US
dc.subject.meshPhthalimides/pharmacologyen_US
dc.subject.meshSaccharin/chemistryen_US
dc.subject.meshSaccharin/pharmacologyen_US
dc.subject.meshSerine Proteinase Inhibitors/pharmacologyen_US
dc.titleAmino acid-derived phthalimide and saccharin derivatives as inhibitors of human leukocyte elastase, cathepsin G, and proteinase 3en_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 1996, Elsevieren_US


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