The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36

By R. Klose, K. Yamane, Yangjin Bae, Dianzheng Zhang, H. Erdjument‐Bromage, Paul Tempst, J. Wong, Yi Zhang. Nature, 2006

661 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f45c1b9ee6d12feaaa9241a7ff0f854dd73d7456

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In Molecular Biology

1. Ryuji Hamamoto
2. Yusuke Nakamura
3. S. Hayami
4. N. Dohmae
5. Takehiro Suzuki
6. Bruce A. J. Ponder
7. Tatsuhiko Tsunoda
8. David E. Neal

Citations in the corpus

• A Functional Link between the Histone Demethylase PHF8 and the Transcription Factor ZNF711 in X-Linked Mental Retardation (2010, neutral): “Moreover, we were not able to detect demethylation of nucleosomes as it has been observed before for other published histone demethylases (Iwase et al., 2007; Klose et al., 2006; Whetstine et al., 2006), suggesting that this is a poor substrate under standard assay conditions (Figure S2B).”
• Overexpression of the JmjC histone demethylase KDM5B in human carcinogenesis: involvement in the proliferation of cancer cells through the E2F/RB pathway (2010, background): “This is exemplified by JHDM3A/ JMJD2A, which displaces HP1 from chromatin by demethylating the H3K9 methylation and thereby preventing the spread of H3K9 methylation to the surrounding chromatin by HP1 [3,4].”