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Pyrin Domain (PYD)-containing Inflammasome in Innate Immunity

DC Field Value Language
dc.contributor.author유제욱-
dc.date.accessioned2014-12-20T17:51:47Z-
dc.date.available2014-12-20T17:51:47Z-
dc.date.issued2011-
dc.identifier.issn1598-2467-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/95397-
dc.description.abstractInflammasome is a cytosolic multiprotein complex to activate caspase-1 leading to the subsequent processing of inactive pro-interleukin-1-beta (Pro-IL-1beta) into its active interleukin-1 beta (IL-1beta) in response to pathogen- or danger-associated molecular pattern. In recent years, a huge progress has been made to identify inflammasome component as a molecular platform to recruit and activate caspase-1. Nucleotide-binding oligomerization domain-like receptor (NLR) family proteins such as NLRP1, NLRP3 or interleukin-1beta-converting enzyme (ICE)-protease activating factor (IPAF) have been first characterized to form inflammasome complex to induce caspase-1 activation. More recently, non-NLR type, pyrin-domain (PYD)-containing proteins such as pyrin or absent in melanoma2 (AIM2) were also proposed to form caspase-1-activating inflammasome machinery with apoptosis-associated speck-like protein containing a CARD (ASC), an essential adaptor molecule. Inflammasome pathways were shown to be crucial for protecting host organisms against diverse pathogen infections, but accumulating evidences also suggest that excessive activation of inflammasome/caspase-1 might be related to the pathogenesis of inflammation-related diseases. Indeed, mutations in NLRP3 or pyrin are closely associated with autoinflammatory diseases such as familial Mediterranean fever (FMF) syndrome or Muckle-Wells syndrome (MWS), indicating that the regulation of caspase-1 activity by inflammasome is a central process in these hereditary inflammatory disorders. Here, recent advances on the molecular mechanism of caspase-1 activation by PYD-containing inflammasomes are summarized and discussed.-
dc.description.statementOfResponsibilityopen-
dc.format.extent133~146-
dc.relation.isPartOfJournal of Bacteriology and Virology-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHAnimals-
dc.subject.MESHChromatography, Liquid/methods*-
dc.subject.MESHDrug Interactions-
dc.subject.MESHDrug Stability-
dc.subject.MESHFemale-
dc.subject.MESHIsoflavones/blood*-
dc.subject.MESHIsoflavones/pharmacokinetics*-
dc.subject.MESHLimit of Detection-
dc.subject.MESHMale-
dc.subject.MESHRats, Wistar-
dc.subject.MESHReproducibility of Results-
dc.subject.MESHRhodanine/analogs & derivatives*-
dc.subject.MESHRhodanine/blood-
dc.subject.MESHRhodanine/pharmacokinetics-
dc.subject.MESHTandem Mass Spectrometry/methods*-
dc.subject.MESHThiazolidines/blood*-
dc.subject.MESHThiazolidines/pharmacokinetics*-
dc.titlePyrin Domain (PYD)-containing Inflammasome in Innate Immunity-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Microbiology (미생물학)-
dc.contributor.googleauthorSujeong Hong-
dc.contributor.googleauthorSangjun Park-
dc.contributor.googleauthorJe-Wook Yu-
dc.identifier.doi10.4167/jbv.2011.41.3.133-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA02508-
dc.relation.journalcodeJ01255-
dc.identifier.pmid27650591-
dc.subject.keywordEpalrestat-
dc.subject.keywordUHPLC-MS/MS-
dc.subject.keywordpharmacokinetic interaction-
dc.subject.keywordpuerarin-
dc.subject.keywordrat plasma-
dc.contributor.alternativeNameYu, Je Wook-
dc.contributor.affiliatedAuthorYu, Je Wook-
dc.rights.accessRightsfree-
dc.citation.volume41-
dc.citation.number3-
dc.citation.startPage133-
dc.citation.endPage146-
dc.identifier.bibliographicCitationJournal of Bacteriology and Virology, Vol.41(3) : 133-146, 2011-
dc.identifier.rimsid48341-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers

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