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Role of Post-translational Modification of Silent Mating Type Information Regulator 2 Homolog 1 in Cancer and Other Disorders

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dc.contributor.authorLee, Yeon-Hwa-
dc.contributor.authorKim, Su-Jung-
dc.contributor.authorSurh, Young-Joon-
dc.date.accessioned2023-01-09T02:41:09Z-
dc.date.available2023-01-09T02:41:09Z-
dc.date.created2022-11-02-
dc.date.created2022-11-02-
dc.date.issued2022-09-
dc.identifier.citation대한암예방학회지, Vol.27 No.3, pp.157-169-
dc.identifier.issn2288-3649-
dc.identifier.urihttps://hdl.handle.net/10371/188930-
dc.description.abstractSilent mating type information regulator 2 homolog 1 (SIRT1), an NAD+-dependent histone/protein deacetylase, has multifarious physiological roles in development, metabolic regulation, and stress response. Thus, its abnormal expression or malfunction is implicated in pathogenesis of various diseases. SIRT1 undergoes post-translational modifications, including phosphorylation, oxi-dation/reduction, carbonylation, nitrosylation, glycosylation, ubiquitination/deubiquitination, SUMOylation etc. which can modulate its catalytic activity, stability, subcellular localization, and also binding affinity for substrate proteins. This short review highlights the regulation of SIRT1 post-translational modifications and their pathophysiologic implications.-
dc.language영어-
dc.publisher대한암예방학회-
dc.titleRole of Post-translational Modification of Silent Mating Type Information Regulator 2 Homolog 1 in Cancer and Other Disorders-
dc.typeArticle-
dc.citation.journaltitle대한암예방학회지-
dc.identifier.wosid000868952700003-
dc.citation.endpage169-
dc.citation.number3-
dc.citation.startpage157-
dc.citation.volume27-
dc.identifier.kciidART002883094-
dc.description.isOpenAccessY-
dc.contributor.affiliatedAuthorSurh, Young-Joon-
dc.type.docTypeReview-
dc.description.journalClass1-
dc.subject.keywordPlusFATTY-ACID OXIDATION-
dc.subject.keywordPlusHEPATIC STEATOSIS-
dc.subject.keywordPlusPROTEIN STABILITY-
dc.subject.keywordPlusO-GLCNACYLATION-
dc.subject.keywordPlusCELL-SURVIVAL-
dc.subject.keywordPlusSIRT1-
dc.subject.keywordPlusP53-
dc.subject.keywordPlusSUMOYLATION-
dc.subject.keywordPlusPHOSPHORYLATION-
dc.subject.keywordPlusDEACETYLASE-
dc.subject.keywordAuthorPost-translational modification-
dc.subject.keywordAuthorProtein processing-
dc.subject.keywordAuthorSirtuin 1-
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  • College of Pharmacy
  • Department of Pharmacy
Research Area Agricultural Sciences

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