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1 g 2C (JMJD2C), a recently identified histone lysine demethylase.
2 ex 2, and its erasers, Jumonji-class histone lysine demethylases.
3 nvolving the KDM4A, KDM4B, and KDM4C histone lysine demethylases.
4 KG-dependent enzyme of the Jumonji family of lysine demethylases.
5 bitors of the KDM4 (JMJD2) family of histone lysine demethylases.
6 entially inhibits the subfamily of trimethyl lysine demethylases.
11 iC (JmjC) and ARID domain-containing histone lysine demethylase 1a (JARID1a) formed a complex with CL
13 -2HG competitively inhibited the activity of lysine demethylase 2B (KDM2B), an alpha-ketoglutarate-de
26 eraction between BRWD3 and the H3K4-specific lysine demethylase 5 (KDM5/Lid), an enzyme that removes
27 rmined the regulation of MPC-1 expression by Lysine demethylase 5A (KDM5A) and critical impact of thi
28 ation of one of the JmjC-containing enzymes, lysine demethylase 5A (KDM5A), mimics hypoxia-induced ce
29 s RNA sequencing, we show that the ASD gene, lysine demethylase 5A (KDM5A), regulates the development
30 6 ADHD cases and 5002 controls), we identify lysine demethylase 5B (KDM5B) as a high-confidence risk
34 histone H3 at lysine 27 (H3K27) demethylase lysine demethylase 6A (KDM6A) is a tumor suppressor in m
37 ression of lysine demethylase 6A (KDM6A) and lysine demethylase 6B (KDM6B) has been reported in prost
44 SL produces fumarate, which in turn inhibits lysine demethylase 8-mediated Beclin1 demethylation, res
47 Here, we demonstrate that LSD1, a histone lysine demethylase, also participates in the trans-repre
49 ase 1 (LSD1) is the first discovered histone lysine demethylase and, with the help of its cofactor Co
51 a histone protease, as an N(epsilon)-methyl lysine demethylase, and as an arginine residue hydroxyla
53 ygenase family, including prolylhydroxylase, lysine demethylase, and DNA demethylase, have emerged as
55 tural topology is similar to known oxidases, lysine demethylases, and monooxygenases, but its active
56 us, we suggest that, during gene repression, lysine demethylases can directly interact and function i
57 KDM2A/FBXL11 is a Jumonji-domain containing lysine demethylase catalyzing the removal of mono- and d
58 , we identified de novo variants in KDM2A, a lysine demethylase crucial for embryonic development, in
59 report in this study, KDM8/JMJD5, a histone lysine demethylase/dioxygnase, exhibits a novel property
60 JMJD2) and KDM5 (JARID1) families of histone lysine demethylases (e.g., 1), further optimization led
62 ET domain-containing protein 1 (NSD1), and a lysine demethylase, F-box and leucine-rich repeat protei
64 r of the Jumonji C domain-containing histone lysine demethylase family, specifically targets lower me
68 transcriptomic analysis reveal that Kdm5b, a lysine demethylase gene carrying "bivalent" chromatin do
69 nactivating somatic mutations in the histone lysine demethylase gene UTX, pointing to histone H3 lysi
71 stone lysine methyltransferases, and histone lysine demethylases, have a role in diverse cancers, spe
72 ydroxylase FIH and histone N(epsilon)-methyl lysine demethylases, identifies branch points in 2OG-dep
73 Since the discovery of the first histone lysine demethylase in 2004, two protein families with nu
74 describe a unique role for the KDM4C histone lysine demethylase in KDM4C-amplified basal breast cance
75 nistic understanding of the roles of histone lysine demethylases in eukaryotic transcription, genome
76 ecent insights into the roles of the histone lysine demethylases in multiple aspects of development a
77 the ligand-dependent recruitment of histone lysine demethylases, including lysine-specific demethyla
79 e 1 (CES1) confers resistance to the histone lysine demethylase inhibitor GSK-J4 by direct enzymatic
81 LSDs or KDM1s) and JmjC families of N-methyl-lysine demethylases (JmjC KDMs, KDM2-7), focusing on the
83 m involving OCA-B recruitment of the histone lysine demethylase Jmjd1a to targets such as Il2, Ifng,
86 aches, we were able to simultaneously delete Lysine Demethylase (KDM) 5A, 5B and 5C efficiently in vi
90 es, a series of potent JmjC histone N-methyl lysine demethylase (KDM) inhibitors which bind to Fe(II)
91 G) and succinate metabolism, including TET2, lysine demethylase (KDM) KDM6A, BRCA1-associated BAP1, a
92 Recently, we identified hepatic demethylases lysine demethylase (KDM)5B and KDM5C as important epigen
93 state cancer, two different types of histone lysine demethylases (KDM), LSD1/KDM1 and JMJD2/KDM4, are
94 g) domain 1 (AOF1), a protein related to the lysine demethylase KDM1 (also known as LSD1), functions
97 ed with epigenetic modifications mediated by lysine demethylases KDM1A and KDM5A, further exacerbated
98 MSN-specific expressional changes of histone lysine demethylases Kdm1a, Kdm6a, and Kdm5c in NAc after
99 nic cellular model, here we identify histone lysine demethylase KDM2A as a molecular vulnerability se
100 71) determine a crystal structure of histone lysine demethylase KDM2A that specifically targets lower
103 onditions by directly repressing the histone lysine demethylase, Kdm2a, whose expression increases in
106 ion in the 15-LOX-1 promoter via the histone lysine demethylase KDM3A was an early and specific histo
107 lance is controlled by the crosstalk between lysine demethylase KDM3B and methyltransferase G9a/EHMT2
111 The KDM4/JMJD2 Jumonji C-containing histone lysine demethylases (KDM4A-KDM4D), which selectively rem
112 hat oncometabolite-induced inhibition of the lysine demethylase KDM4B results in aberrant hypermethyl
113 on this promoter is to displace the histone lysine demethylase KDM5A, thereby favoring trimethylatio
114 tive removal of broad H3K4me3 domains by the lysine demethylases KDM5A and KDM5B is required for norm
117 nsferases Ash1l, Smyd2, and Ezh2 and histone lysine demethylases Kdm5b and Kdm6b in J774 macrophages
119 emonstrated enhanced binding of the H3K27me3 lysine demethylase KDM6A, which significantly correlated
128 pecific lysine methyltransferases (KMTs) and lysine demethylases (KDMs) have been implicated in the d
131 detransferases and successfully apply it to lysine demethylases (KDMs) which catalyze the removal of
132 asing interest in targeting histone N-methyl-lysine demethylases (KDMs) with small molecules both for
133 ylation-lysine methyltransferases (KMTs) and lysine demethylases (KDMs), respectively-are frequently
134 ive sites of selected iron-dependent histone lysine demethylases (KDMs), resulting in pan inhibition
136 ly, which includes histone N(epsilon)-methyl lysine-demethylases (KDMs) and hydroxylases catalysing f
139 to pharmacological inhibition of the histone lysine demethylase LSD1 and genetic ablation of the PRC2
141 ltiple clinically relevant inhibitors of the lysine demethylase LSD1 were tested to determine which i
142 ing corepressor that recruits the repressive lysine demethylase LSD1/KDM1A to Notch target genes.
143 We establish a requirement for the histone lysine demethylase, LSD1, in directing specific interchr
146 d and erase the methylated histone residues, lysine demethylases must specifically recognize the hist
147 hough, histone lysine methyltransferases and lysine demethylases orchestrate these events, their role
149 ase 1 (LSD1) as the first identified histone/lysine demethylase regulates gene expression and protein
152 is a member of the JARID1 family of histone lysine demethylases responsible for the demethylation of
153 ing repressor complexes that include histone lysine demethylases, such as KDM1 in animals and KDM1C i
155 change with the recent discovery of histone lysine demethylases that reversibly remove methyl marks?
156 methylation, as catalysed by two families of lysine demethylases (the flavin-dependent KDM1 enzymes a
157 we show that Oct1 recruits the Jmjd1a/KDM3A lysine demethylase to catalyze the removal of the inhibi
159 r Oct1 overlapped with those for the histone lysine demethylase Utx, and an interaction between Oct1
161 d 2-oxoglutarate-dependent N(epsilon)-methyl lysine demethylase, which acts on histone substrates.