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dc.contributor.authorRathert, Philipp-
dc.date.accessioned2023-06-26T12:10:36Z-
dc.date.available2023-06-26T12:10:36Z-
dc.date.issued2021-
dc.identifier.issn2075-1729-
dc.identifier.other1852089296-
dc.identifier.urihttp://nbn-resolving.de/urn:nbn:de:bsz:93-opus-ds-132346de
dc.identifier.urihttp://elib.uni-stuttgart.de/handle/11682/13234-
dc.identifier.urihttp://dx.doi.org/10.18419/opus-13215-
dc.description.abstractNSD3 is one of six H3K36-specific lysine methyltransferases in metazoans, and the methylation of H3K36 is associated with active transcription. NSD3 is a member of the nuclear receptor-binding SET domain (NSD) family of histone methyltransferases together with NSD1 and NSD2, which generate mono- and dimethylated lysine on histone H3. NSD3 is mutated and hyperactive in some human cancers, but the biochemical mechanisms underlying such dysregulation are barely understood. In this review, the current knowledge of NSD3 is systematically reviewed. Finally, the molecular and functional characteristics of NSD3 in different tumor types according to the current research are summarized.en
dc.language.isoende
dc.relation.uridoi:10.3390/life11080726de
dc.rightsinfo:eu-repo/semantics/openAccessde
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/de
dc.subject.ddc540de
dc.subject.ddc570de
dc.titleStructure, activity and function of the NSD3 protein lysine methyltransferaseen
dc.typearticlede
dc.date.updated2021-08-01T18:16:36Z-
ubs.fakultaetChemiede
ubs.institutInstitut für Biochemie und Technische Biochemiede
ubs.publikation.seiten13de
ubs.publikation.sourceLife 11 (2021), No. 726de
ubs.publikation.typZeitschriftenartikelde
Enthalten in den Sammlungen:03 Fakultät Chemie

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