RT Book, Section
T1 Inhibitors of Jumonji-C domain-containing histone demethylases
A1 Sian, Veronica
A1 Souto Salgado, Jose Antonio
A1 Álvarez Rodríguez, Maria Rosana
A1 Nebbioso, Angela
A1 Rodríguez de Lera, Ángel
A1 Altucci, Lucia
A2 Elsevier
K1 2306 Química Orgánica
AB [Inicio] Histone methylation represents an epigenetic modification that plays important roles not only for the transcriptional regulation but also for the preservation of genomic stability in eukaryotes. The methylation status of specific lysines is kept in balance by the competitive roles of two enzyme families, that is, the histone methyltransferases (HMTs) [1,2] and the histone demethylases (KDMs) [3-7]. A variety of diseases, including inflammation, leukemia, and breast and prostate cancers, are linked to alterations from its normal status of this epigenetic modification [8,9].Nine groups of human Nε-methyl-lysine demethylases (KDM1-9) have been identified that catalyze the demethylation of N-methyl-lysine residues in histones through oxidative mechanisms acting on different Nε-methylation states and specific protein sequences [3]. KDMs are grouped into two families: the flavin-dependent lysine-specific demethylases (LSDs/KDM1s) and the 2-oxoglutarate (2OG)-, ferrous iron-, and oxygen-dependent demethylases [Jumonji-C (JmjC) KDMs], the latter being the largest family of KDMs. More than 100 members of the JmJC domaincontaining proteins have been reported, including KDMs [10]. [...]
SN 9780128004715
YR 2023
FD 2023
LK http://hdl.handle.net/11093/8045
UL http://hdl.handle.net/11093/8045
LA eng
NO En Steven G. Gray (Eds.) Epigenetic gene expression and regulation (407-457)
NO Agencia Estatal de Investigación | Ref. PID2019-107855RB-I00
DS Investigo
RD 17-mar-2025