Histone demethylation by a family of JmjC domain-containing proteins

By Y. Tsukada, Jia Fang, H. Erdjument‐Bromage, M. Warren, C. Borchers, Paul Tempst, Yi Zhang. Nature, 2006

2,168 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/3254c1c80159b5683f403c51e9b60bc94f237f12

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Citations in the corpus

Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “Whereas the H3K36me3/me2 mark is associated with transcriptional elongation (Joshi and Struhl 2005; Keogh et al. 2005; Lee and Shilatifard 2007) and possibly fulfills important roles in suppression of inappropriate transcription within the body of genes (Carrozza et al. 2005), the H3K9me3/me2 mark h”
Histone methylation: a dynamic mark in health, disease and inheritance (2012, background): “1 HBXIP t(19;17)(q13;p11) Hepatocellular carcinoma (HCC), hepatitis B virus related HCCs”
ALKBH5 Is a Mammalian RNA Demethylase that Impacts RNA Metabolism and Mouse Fertility (2012, background): “The recent discoveries of demethylases that actively remove methylations in DNA and histones provide a dynamic picture of mammalian gene expression regulation through reversible methylation (He et al., 2011; Ito et al., 2011; Shi et al., 2004; Tahiliani et al., 2009; Tsukada et al., 2006).”
Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. (2006, background): “In addition, one can not exclude the possibility that these proteins may display altered site specificities in vivo when complexed with different proteins, as has been reported for LSD1 (Metzger et al., 2005; Shi et al., 2005).”
Nucleosome-Interacting Proteins Regulated by DNA and Histone Methylation (2010, background): “This enzyme is a JmjC domain protein that demethylates lysine 36 on histone H3 (Tsukada et al., 2006).”
Active DNA demethylation: many roads lead to Rome (2010, background): “The same mechanism is used by the JmjC family of enzymes to demethylate histone substrate”
The JmjC domain‐containing histone demethylase KDM3A is a positive regulator of the G1/S transition in cancer cells via transcriptional regulation of the HOXA1 gene (2012, background): “Subsequently, the first JmjC-containing histone demethylase (KDM2A; also known as JHDM1a/FBXL11) was biochemically identified.(5) The JmjC domain is conserved from yeast to human and belongs to the superfamily of Fe2þ-dependent dioxygenases.”
Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. (2012, background): “While the KDMs catalyze the typical hydroxylation on the methyl group on the lysine residue (Tsukada et al. 2006), the recently discovered TET family of DNA hydroxylases catalyzes a three-step iterative oxidation reaction: converting 5mC to 5-hydroxymethylcytosine (5hmC), then converting 5hmC to…”
Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases (2011, positive): “, 2009; Loenarz and Schofield, 2008), including the JmjC domain containing histone demethylases (Tsukada et al., 2006) and recently discovered TET family of 5-methylcytosine (5mC) hydroxylases that convert 5mC to 5-hydroxylmethycytosine (5hmC [Tahiliani et al.”
JmjC-domain-containing proteins and histone demethylation (2006, background): “a non-redundant set of 98 JmjC-domain-containing proteins from human (30), mouse (30), Drosophila melanogaster (13), Caenorhabditis elegans (13), fission yeast (7) and budding yeast (5) (BOX 1) (see Supplementary information S1 (table) for the complete list of proteins).”