Results 261 to 270 of about 257,789 (305)

The involvement of RNA N6-methyladenosine and histone methylation modification in decidualization and endometriosis-associated infertility. [PDF]

Clin Transl Med
Lin X, Dai Y, Gu W, Zhang Y, Zhuo F, Zhao F, Jin X, Li C, Huang D, Tong X, Zhang S.   +10 more
europepmc   +1 more source

RNA-directed DNA methylation mutants reduce histone methylation at the paramutated maize booster1 enhancer. [PDF]

Plant Physiol
Hövel I, Bader R, Louwers M, Haring M, Peek K, Gent JI, Stam M.   +6 more
europepmc   +1 more source

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Histone Methylation in Higher Plants

Annual Review of Plant Biology, 2010
Histone methylation plays a fundamental role in regulating diverse developmental processes and is also involved in silencing repetitive sequences in order to maintain genome stability. The methylation marks are written on lysine or arginine by distinct enzymes, namely, histone lysine methyltransferases (HKMTs) or protein arginine methyltransferases ...
Chunyan, Liu, Falong, Lu, Xia, Cui, Xiaofeng, Cao   +3 more
openaire   +4 more sources

Histone methylation boosts liver regeneration

Nature Reviews Molecular Cell Biology, 2019
Upon loss of liver DNA methylation, H3K27me3 is redistributed from pro-regeneration genes to hypomethylated transposons, thereby potentiating liver regeneration.
openaire   +4 more sources

Reversing histone methylation

Nature, 2005
Histones package DNA, and post-translational modifications of histones can regulate access to DNA. Until recently, histone methylation-unlike all other histone modifications-was considered a permanent mark. The discovery of enzymes that reverse the methylation of lysines and arginines challenges our current thinking on the unique nature of histone ...
Andrew J, Bannister, Tony, Kouzarides
openaire   +2 more sources

Enzymatic methylation of histones

Archives of Biochemistry and Biophysics, 1969
Abstract Various proteins were methylated by purified protein methylase I. Since the enzyme also methylates its endogenous histones, detailed studies on the protein methylation by the purified protein methylase I were carried out with added histone. Exogenous histone methylated enzymatically gave rise to guanidyl-methylated and α-N-methyl, guanidyl ...
W K, Paik, S, Kim
openaire   +2 more sources

Inhibitors of histone methylation

Chemico-Biological Interactions, 1974
Two classes of inhibitors of histone methyltransferase I from calf thymus are reported. High concentrations (≧ 10 mM) of various alkyl or aralkyl amines and polyamines were inhibitory to the enzyme. Spermine and spermidine were among the most potent compounds in this group.
M, Cory, D W, Henry, D L, Taylor, K J, Koskela   +3 more
openaire   +2 more sources

Histone Methylation: Recognizing the Methyl Mark

2003
Publisher Summary Histone N-terminal tails are subject to a variety of covalent modifications that ultimately affect chromatin structure. One such modification is N-methylation, which occurs on Lys (K) and Arg (R) amino acids. The enzymes performing these modifications are the histone N-methyl transferases (HMTs) that catalyze the transfer of a ...
Andrew J, Bannister, Tony, Kouzarides
openaire   +2 more sources

SET domains and histone methylation

Current Opinion in Structural Biology, 2003
The realisation that SET domains, which are found in numerous proteins involved in chromatin regulation, catalyse the methylation of lysine residues has led to intense interest in their cellular, biochemical and structural properties. The structures of five SET domain proteins have been reported over the past year. SET domains possess a novel fold, and
Bing, Xiao, Jonathan R, Wilson, Steven J, Gamblin   +2 more
openaire   +2 more sources

DNA methylation models histone acetylation

Nature, 1998
One of the main determinants of chromatin structure is histone acetylation1. Local chromosomal acetylation can be regulated dynamically, both through the involvement of transactivating factors with intrinsic histone acetylase activity, and through the recruitment of deacetylase complexes that repress gene expression2.
Eden, S., Hashimshony, I., Keshet, H., Cedar, H., Thorne, Alan   +4 more
openaire   +3 more sources