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dc.contributor.authorVanaja, Sivapriya K.
dc.contributor.authorRathinam, Vijay A. K.
dc.contributor.authorFitzgerald, Katherine A.
dc.date2022-08-11T08:09:09.000
dc.date.accessioned2022-08-23T16:19:07Z
dc.date.available2022-08-23T16:19:07Z
dc.date.issued2015-05-01
dc.date.submitted2015-04-27
dc.identifier.citationTrends Cell Biol. 2015 May;25(5):308-315. doi: 10.1016/j.tcb.2014.12.009. <a href="http://dx.doi.org/10.1016/j.tcb.2014.12.009">Link to article on publisher's site</a>
dc.identifier.issn0962-8924 (Linking)
dc.identifier.doi10.1016/j.tcb.2014.12.009
dc.identifier.pmid25639489
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34971
dc.description.abstractInflammasomes are cytosolic multiprotein platforms assembled in response to invading pathogens and other danger signals. Typically inflammasome complexes contain a sensor protein, an adaptor protein, and a zymogen - procaspase-1. Formation of inflammasome assembly results in processing of inactive procaspase-1 into an active cysteine-protease enzyme, caspase-1, which subsequently activates the proinflammatory cytokines, interleukins IL-1beta and IL-18, and induces pyroptosis, a highly-pyrogenic inflammatory form of cell death. Studies over the past year have unveiled exciting new players and regulatory pathways that are involved in traditional inflammasome signaling, some of them even challenging the existing dogma. This review outlines these new insights in inflammasome research and discusses areas that warrant further exploration.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=25639489&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.tcb.2014.12.009
dc.subjectBiochemistry
dc.subjectImmunity
dc.subjectImmunology and Infectious Disease
dc.subjectImmunology of Infectious Disease
dc.titleMechanisms of inflammasome activation: recent advances and novel insights
dc.typeJournal Article
dc.source.journaltitleTrends in cell biology
dc.source.volume25
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/infdis_pp/191
dc.identifier.contextkey7036108
html.description.abstract<p>Inflammasomes are cytosolic multiprotein platforms assembled in response to invading pathogens and other danger signals. Typically inflammasome complexes contain a sensor protein, an adaptor protein, and a zymogen - procaspase-1. Formation of inflammasome assembly results in processing of inactive procaspase-1 into an active cysteine-protease enzyme, caspase-1, which subsequently activates the proinflammatory cytokines, interleukins IL-1beta and IL-18, and induces pyroptosis, a highly-pyrogenic inflammatory form of cell death. Studies over the past year have unveiled exciting new players and regulatory pathways that are involved in traditional inflammasome signaling, some of them even challenging the existing dogma. This review outlines these new insights in inflammasome research and discusses areas that warrant further exploration.</p>
dc.identifier.submissionpathinfdis_pp/191
dc.contributor.departmentDepartment of Medicine, Division of Infectious Diseases and Immunology, Program in Innate Immunity
dc.source.pages308-315


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