5-Substituted Pyridine-2,4-dicarboxylate Derivatives Have Potential for Selective Inhibition of Human Jumonji-C Domain-Containing Protein 5.
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
10 08 2023
10 08 2023
Historique:
medline:
11
8
2023
pubmed:
2
8
2023
entrez:
1
8
2023
Statut:
ppublish
Résumé
Jumonji-C domain-containing protein 5 (JMJD5) is a 2-oxoglutarate (2OG)-dependent oxygenase that plays important roles in development, circadian rhythm, and cancer through unclear mechanisms. JMJD5 has been reported to have activity as a histone protease, as an
Identifiants
pubmed: 37527664
doi: 10.1021/acs.jmedchem.3c01114
pmc: PMC10424186
doi:
Substances chimiques
Histones
0
Pyridines
0
Oxygenases
EC 1.13.-
Jumonji Domain-Containing Histone Demethylases
EC 1.14.11.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
10849-10865Subventions
Organisme : Cancer Research UK
ID : TICCPP-2022/100001
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C8717/A18245
Pays : United Kingdom
Organisme : Cancer Research UK
ID : 16466
Pays : United Kingdom
Organisme : Cancer Research UK
ID : 28285
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 106244/Z/14/Z
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/J003018/1
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Cancer Research UK
ID : 24552
Pays : United Kingdom
Organisme : Cancer Research UK
ID : C33483/A2567
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R000344/1
Pays : United Kingdom
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