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Techniques to Study Automethylation of Histone Methyltransferases and its Functional Impact

DC Field Value Language
dc.contributor.authorPopoca, Luis-
dc.contributor.authorLee, Chul-Hwan-
dc.date.accessioned2024-05-14T06:36:36Z-
dc.date.available2024-05-14T06:36:36Z-
dc.date.created2023-05-09-
dc.date.issued2022-01-
dc.identifier.citationMethods in molecular biology (Clifton, N.J.), Vol.2529, pp.109-120-
dc.identifier.issn1064-3745-
dc.identifier.urihttps://hdl.handle.net/10371/201837-
dc.description.abstractThe catalytic activity of histone methyltransferases is not restricted to histones but also includes noncanonical substrates. Increasing evidence shows that histone methyltransferases methylate themselves, and automethylation has emerged as a self-regulatory mechanism. Here, we introduce experimental procedures to identify automethylation sites of histone methyltransferases and to investigate the function of automethylation in a reconstituted biochemical system and in cellular contexts.-
dc.language영어-
dc.publisherHumana Press, Inc.-
dc.titleTechniques to Study Automethylation of Histone Methyltransferases and its Functional Impact-
dc.typeArticle-
dc.identifier.doi10.1007/978-1-0716-2481-4_5-
dc.citation.journaltitleMethods in molecular biology (Clifton, N.J.)-
dc.identifier.scopusid2-s2.0-85132611193-
dc.citation.endpage120-
dc.citation.startpage109-
dc.citation.volume2529-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorLee, Chul-Hwan-
dc.type.docTypeBook Chapter-
dc.description.journalClass1-
dc.subject.keywordAuthorActive conformation-
dc.subject.keywordAuthorAutomethylation-
dc.subject.keywordAuthorHistone methyltransferase assay-
dc.subject.keywordAuthorRegulation of catalytic activity-
dc.subject.keywordAuthorSelf-regulatory mechanism-
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  • College of Medicine
Research Area Epigenetics, Heterochromatin, Histone Modifications

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