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Histone and Non-Histone Reversible Acetylation in Development, Aging, and Disease

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dc.authorscopusid6603432100
dc.authorscopusid57209202034
dc.authorscopusid55878163500
dc.authorscopusid59985373500
dc.authorscopusid57359414500
dc.contributor.authorGüneş, S.
dc.contributor.authorHekim, N.
dc.contributor.authorErgün, S.
dc.contributor.authorAlkan, E.N.
dc.contributor.authorCan, C.
dc.date.accessioned2025-12-11T00:35:55Z
dc.date.issued2025
dc.departmentOndokuz Mayıs Üniversitesien_US
dc.department-temp[Güneş] Sezgin Özgür, Department of Medical Biology, Ondokuz Mayis Üniversitesi, Samsun, Turkey, Stem Cell Research & Application Center, Ondokuz Mayis Üniversitesi, Samsun, Turkey; [Hekim] Neslihan Taşkurt, Department of Medical Biology, Ondokuz Mayis Üniversitesi, Samsun, Turkey; [Ergün] Sercan, Department of Medical Biology, Ondokuz Mayis Üniversitesi, Samsun, Turkey; [Alkan] Elzem Nisa, Department of Medical Biology, Ondokuz Mayis Üniversitesi, Samsun, Turkey; [Can] Cansu, Department of Medical Biology, Ondokuz Mayis Üniversitesi, Samsun, Turkeyen_US
dc.description.abstractPost-translational modifications (PTM) involve chemical modifications of amino acid residues within histone and non-histone proteins and are chemically diverse. PTM plays a vital role in regulating the chromatin structure in the nucleus, thus gene regulation. Among the various PTM, reversible acetylation of histone non-histone proteins has fundamental functions in various cellular processes. In all organisms, histone acetylation of lysine residues is connected with transcription activation. Acetyltransferases and deacetylases are well-known enzymes in the acetylation of the histone and non-histone proteins. This chapter will review the latest progress in histone and non-histone reversible acetylation epigenetic alterations and mechanisms and summarize how they affect development, aging, and diseases. © The Author(s), under exclusive license to Springer Nature Switzerland AG 2025.en_US
dc.identifier.doi10.1007/978-3-031-91459-1_1
dc.identifier.endpage24en_US
dc.identifier.isbn9783642216480
dc.identifier.isbn9783540699187
dc.identifier.isbn9783642030185
dc.identifier.isbn9783642190643
dc.identifier.isbn3540336850
dc.identifier.isbn3540345523
dc.identifier.isbn9783540336853
dc.identifier.isbn9783540786214
dc.identifier.isbn9783642141522
dc.identifier.isbn9783540368281
dc.identifier.issn0080-1844
dc.identifier.issn1861-0412
dc.identifier.pmid40593205
dc.identifier.scopus2-s2.0-105010291676
dc.identifier.scopusqualityQ4
dc.identifier.startpage3en_US
dc.identifier.urihttps://doi.org/10.1007/978-3-031-91459-1_1
dc.identifier.urihttps://hdl.handle.net/20.500.12712/37739
dc.identifier.volume75en_US
dc.language.isoenen_US
dc.publisherSpringer Science and Business Media Deutschland GmbHen_US
dc.relation.ispartofResults and Problems in Cell Differentiationen_US
dc.relation.publicationcategoryKitap Bölümü - Uluslararasıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.titleHistone and Non-Histone Reversible Acetylation in Development, Aging, and Diseaseen_US
dc.typeBook Parten_US
dspace.entity.typePublication

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