Regulation of histone methylation by demethylimination and demethylation

By R. Klose, Yi Zhang. Nature reviews. Molecular cell biology, 2007

921 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/7e4f8bc085224c02477e62e50efb15da750464b4

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Citations in the corpus

Active DNA demethylation: many roads lead to Rome (2010, background): “In fact, numerous histone demethylases that can break a carbon–nitrogen bond have recently been discovere”
Pollutants inducing epigenetic changes and diseases (2019, background): “The number of methyl groups added to histones can be either mono (Me), dimethyl (Me2) and trimethyl (Me3) group states (Klose and Zhang 2007; Martin and Zhang 2005; Meissner et al.”
Covalent histone modifications: miswritten, misinterpreted, and miserased in human cancers (2010, background): “1a ), and removed by the lysine-specific histone demethylase 1 (LSD1) and jumonji AT-rich interactive domain 1 (JARID1) family of histone demethylases (HDMs”
A Functional Link between the Histone Demethylase PHF8 and the Transcription Factor ZNF711 in X-Linked Mental Retardation (2010, positive): “This protein family has 27 members, and several of these have recently been shown to be histone lysine demethylases playing important roles in development and differentiation (Cloos et al., 2008; Klose and Zhang, 2007; Lan et al., 2008).”
Covalent modifications of histones during development and disease pathogenesis (2007, background): “Histone lysine methylation is also reversible, being carried out by two families of enzymes, amine oxidases such as LSD1 and hydroxylases of the JmjC famil”
Metabolic regulation of epigenetics (2012, background): “Subsequently a family of HDMs named Jumonji-C domain containing HDM (JHDM) were identified and characterized (Klose and Zhang, 2007).”