JMJD6 Is a Histone Arginine Demethylase
By B. Chang, Yue Chen, Yingming Zhao, R. Bruick. Science, 2007
709 citations recorded by the source corpus.
Subfields: Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/8fd79aa29ad3b9a83bb94676a187f92f28c84140
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In Cancer Research
In Molecular Biology
Citations in the corpus
- Protein Arginine Methylation in Mammals: Who, What, and Why (2009, background): “Thus, both H4R3me2s (repressive; me2s indicates SDMA modification) and H4R3me2a (active; me2a indicates ADMA modification) marks are produced in vivo.”
- Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, background): “Recently, JMJD6 (previously believed to be the phosphatidyl serine receptor and therefore denoted PTDSR) was identified as a histone demethylase with specificity to H3R2me2 and H4R3me2, demonstrating that also arginine methylations are reversible (Chang et al. 2007).”
- Epigenetic modifications and human disease (2010, background): “Because the modifications are dynamic, enzymes to remove these post-transcriptional modifications have also been reporte”
- An Apoptotic 'Eat Me' Signal: Phosphatidylserine Exposure. (2015, background): “While working on a transcription system, a later study [111] found that PSR is identical to JMJD6, which has histone arginine demethylase activity and functions as a chromatin remodeling factor.”