The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.
2-oxoglutarate non-heme oxygenase
JmjC-KDM
epigenetics
histone N-methyl arginine/lysine demethylase
post translational modification
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
04 2023
04 2023
Historique:
revised:
13
12
2022
received:
27
10
2022
accepted:
28
12
2022
medline:
12
4
2023
pubmed:
27
1
2023
entrez:
26
1
2023
Statut:
ppublish
Résumé
The demethylation of N
Identifiants
pubmed: 36700827
doi: 10.1002/1873-3468.14586
doi:
Substances chimiques
Jumonji Domain-Containing Histone Demethylases
EC 1.14.11.-
Arginine
94ZLA3W45F
Histone Demethylases
EC 1.14.11.-
Histones
0
KDM5A protein, human
EC 1.14.11.-
Retinoblastoma-Binding Protein 2
EC 1.14.11.27
KDM5D protein, human
EC 1.14.11.-
Minor Histocompatibility Antigens
0
KDM4A protein, human
EC 1.5.-
KDM1A protein, human
EC 1.5.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
933-946Subventions
Organisme : Cancer Research UK
ID : C8717/A18245
Pays : United Kingdom
Organisme : Cancer Research UK
ID : 28285
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 106244/Z/14/Z
Pays : United Kingdom
Organisme : Cancer Research UK
ID : 18245
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C8717/A28285
Pays : United Kingdom
Informations de copyright
© 2023 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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