Dynamic regulation of histone lysine methylation by demethylases.
By Yang Shi, J. Whetstine. Molecules and Cells, 2007
709 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a263eaa72764c7226c35f573ac1897f5750a4b01
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In Molecular Biology
- Ryuji Hamamoto
- Yusuke Nakamura
- Takehiro Suzuki
- N. Dohmae
- Lianhua Piao
- Yang Shi
- K. Helin
- J. Christensen
Citations in the corpus
- SUV39H2 methylates and stabilizes LSD1 by inhibiting polyubiquitination in human cancer cells (2015, background): “LSD1 is composed of three domains; a SWIRM domain that is a conserved motif shared by many chromatin regulatory complexes, an amine oxidase (AO) domain and a Tower domain [2-4].”
- Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact (2012, neutral): “The levels of SAM and SAH are primarily balanced by the SAH hydrolase that converts SAH into adenosine and homocysteine (Huang, 2002).”
- Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. (2008, methodology): “Candidate enzymes include NADH/NADPH-dependent oxidoreductases, which could demethylate histones by cycling the NAD/NADH cofactor in a mechanism similar to that used by LSD1; radical S-adenosyl-methionine (SAM) proteins; or enzymes with two iron centers as ribonucleotide reductases or methane mono-o”
- Histone lysine demethylases: emerging roles in development, physiology and disease (2007, background): “Although histone methylation was long considered irreversible, the recent identification of numerous site-specific histone demethylases provides compelling evidence that this modification is dynamically regulate”
- Mechanisms of diabetic complications. (2013, background): “There are also numerous lysine demethylases (HDMs) that have been discovered which can also alter gene expression, emphasizing the bidirectional nature of histone methylation (543, 608).”