Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases

By Sunhwa Hong, Young-Wook Cho, Li-Rong Yu, Hong-Xiu Yu, Timothy D. Veenstra, Kai Ge. Proceedings of the National Academy of Sciences of the United States of America, 2007

692 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/758904d51dd47ee06a065ab2b0197675db6daafa

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In Genetics

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Citations in the corpus

• Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “Conversely, several parallel studies have independently found UTY to be enzymatically inactive (Hong et al. 2007; Lan et al. 2007a).”
• Distinct roles of GCN5/PCAF‐mediated H3K9ac and CBP/p300‐mediated H3K18/27ac in nuclear receptor transactivation (2011, methodology): “Western blot, qRT–PCR, ChIP and in vitro HAT assay Western blot and qRT–PCR using Taqman or Sybr Green assays were done as described (Hong et al, 2007; Cho et al, 2009).”
• The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection (2010, background): “Proteins harboring a Jumonji-C (JmjC) domain, such as Jmjd3, Utx and Uty, are known to act as H3K27 demethylases, catalyzing the conversion of H3K27me3 (trimethylated) to H3K27me1 (monomethylated”