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Michael acceptors as cysteine protease inhibitors

dc.contributor.authorSantos, Maria M. M.
dc.contributor.authorMoreira, Rui
dc.date.accessioned2011-08-01T11:07:39Z
dc.date.available2011-08-01T11:07:39Z
dc.date.issued2007
dc.date.updated2011-07-21T08:47:15Z
dc.description.abstractCysteine proteases selectively catalyze the hydrolysis of peptide bonds. Uncontrolled, unregulated, or undesired proteolysis can lead to many disease states including emphysema, stroke, viral infections, cancer, Alzheimer’s disease, inflammation, and arthritis. Cysteine proteases inhibitors thus have considerable potential utility for therapeutic intervention in a variety of disease states. This review emphasizes on the new developments from literature reports on Michael acceptors as potential cysteine protease inhibitors, namely vinyl sulfones, alfa,beta-unsaturated carbonyl derivatives and aza-peptides. These compounds irreversibly alkylate the active site cysteine residue via conjugate addition. Examples of Michael acceptors inhibitors that have already progressed to clinical testing are also presented.por
dc.identifier.citationSantos, Maria M. M.; Moreira, Rui. Michael acceptors as cysteine protease inhibitors, Mini Reviews Medicinal Chemistry, 7, 1040-1050, 2007.por
dc.identifier.issn1389-5575
dc.identifier.urihttp://hdl.handle.net/10451/3842
dc.identifier.urihttp://search.ebscohost.com/login.aspx?direct=true&db=a9h&AN=26882353&site=ehost-live&scope=site
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherBentham Science Publisherspor
dc.relation.publisherversionhttp://dx.doi.org/10.2174/138955707782110105por
dc.subjectCysteine protease inhibitorspor
dc.subjectVinyl sulfonepor
dc.subjectAlfa,beta-unsaturated carbonyl derivativepor
dc.subjectAza-peptide Michael acceptorpor
dc.subjectK-777por
dc.subjectRuprintivirpor
dc.titleMichael acceptors as cysteine protease inhibitorspor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage1050por
oaire.citation.startPage1040por
oaire.citation.titleMini Reviews Medicinal Chemistrypor
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor

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