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dc.contributor.authorEnslen, Herve
dc.contributor.authorRaingeaud, Joel
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:09Z
dc.date.available2022-08-23T16:54:09Z
dc.date.issued1998-01-27
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 1998 Jan 16;273(3):1741-8.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.273.3.1741
dc.identifier.pmid9430721
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42435
dc.description.abstractThe cellular response to treatment with proinflammatory cytokines or exposure to environmental stress is mediated, in part, by the p38 group of mitogen-activated protein (MAP) kinases. We report the molecular cloning of a novel isoform of p38 MAP kinase, p38 beta 2. This p38 MAP kinase, like p38 alpha, is inhibited by the pyridinyl imidazole drug SB203580. The p38 MAP kinase kinase MKK6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma MAP kinase isoforms, while MKK3 activates only p38 alpha and p38 gamma MAP kinase isoforms. The MKK3 and MKK6 signal transduction pathways are therefore coupled to distinct, but overlapping, groups of p38 MAP kinases.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=9430721&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.273.3.1741
dc.subjectAmino Acid Sequence
dc.subjectAntibodies, Monoclonal
dc.subjectCalcium-Calmodulin-Dependent Protein Kinases
dc.subjectCloning, Molecular
dc.subjectEnzyme Activation
dc.subjectEnzyme Inhibitors
dc.subjectHumans
dc.subjectImidazoles
dc.subjectIsoenzymes
dc.subjectMAP Kinase Kinase 3
dc.subjectMAP Kinase Kinase 6
dc.subject*Mitogen-Activated Protein Kinase Kinases
dc.subject*Mitogen-Activated Protein Kinases
dc.subjectMolecular Sequence Data
dc.subjectPhosphorylation
dc.subjectProtein-Serine-Threonine Kinases
dc.subjectProtein-Tyrosine Kinases
dc.subjectPyridines
dc.subjectp38 Mitogen-Activated Protein Kinases
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleSelective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume273
dc.source.issue3
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/785
dc.identifier.contextkey564700
html.description.abstract<p>The cellular response to treatment with proinflammatory cytokines or exposure to environmental stress is mediated, in part, by the p38 group of mitogen-activated protein (MAP) kinases. We report the molecular cloning of a novel isoform of p38 MAP kinase, p38 beta 2. This p38 MAP kinase, like p38 alpha, is inhibited by the pyridinyl imidazole drug SB203580. The p38 MAP kinase kinase MKK6 is identified as a common activator of p38 alpha, p38 beta 2, and p38 gamma MAP kinase isoforms, while MKK3 activates only p38 alpha and p38 gamma MAP kinase isoforms. The MKK3 and MKK6 signal transduction pathways are therefore coupled to distinct, but overlapping, groups of p38 MAP kinases.</p>
dc.identifier.submissionpathoapubs/785
dc.contributor.departmentHughes Medical Institute, Program in Molecular Medicine
dc.source.pages1741-8


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