Methylation of specific amino acids in histone tails is responsible for packaging DNA into
condensed, repressed chromatin, and into open chromatin that is accessible to the …

Complex patterns of histone lysine methylation encode distinct functions within chromatin.
We previously reported that trimethylation of lysine 9 of histone H3 (H3K9) occurs at both …

Methylation of lysine 4 of histone H3 (K4/H3) is linked to transcriptional activity, whereas
methylation of K9/H3 is tightly associated with gene inactivity. These are well characterized …

Posttranslational modification of histones is a common means of regulating chromatin
structure and thus diverse nuclear processes. Using a hydrophilic interaction liquid …

Mono-, di-, and trimethylation of specific histone residues adds an additional level of
complexity to the range of histone modifications that may contribute to a histone code …

Methylation and acetylation of position-specific lysine residues in the N-terminal tail of
histones H3 and H4 play an important role in regulating chromatin structure and function. In …

The molecular biology of histone H4 lysine 20 (H4K20) methylation, like many other post-
translational modifications of histones, has been the subject of intensive interest in recent …

Methylation of histones modulates chromatin structure and function. Whereas methylation of
histone H3 on lysines 4, 36, and 79 has been linked with gene activation, methylation of H3 …

Methylation of histone H4 at lysine 20 (K20) has been implicated in transcriptional activation,
gene silencing, heterochromatin formation, mitosis, and DNA repair. However, little is known …

Histone methylation acts as an epigenetic regulator of chromatin activity through the
modification of arginine and lysine residues on histones H3 and H4. In the case of lysine …