Histone N-termini (tails) undergo diverse post-translational modifications, including
acetylation, phosphorylation, methylation, ubiquitination and ADP-ribosylation (van Holde …

Diverse post-translational modifications of histone amino termini represent an important
epigenetic mechanism for the organisation of chromatin structure and the regulation of gene …

The rapid progress in deciphering the processes of covalent histone modifications has
broadened our understanding of transcriptional regulation. Histone lysine methylation, along …

Post-translational addition of methyl groups to the amino-terminal tails of histone proteins
was discovered more than three decades ago. Only now, however, is the biological …

Covalent modifications of histone tails have fundamental roles in chromatin structure and
function. One such modification, lysine methylation, has important functions in many …

Histone acetylation, methylation, and phosphorylation occur predominantly in the
unstructured N‐terminal domains or histone “tails”. These modifications and others comprise …

It is more evident now than ever that nucleosomes can transmit epigenetic information from
one cell generation to the next. It has been demonstrated during the past decade that the …

The N termini of nucleosomal histone polypeptides are both highly accessible and
extensively modified by various chemical moieties. Interpreting the language of these …

Covalent modifications of the amino termini of the core histones in nucleosomes have
important roles in gene regulation. Research in the past two years reveals these …

Post-translational modification of histones, a major protein component of eukaryotic
chromosomes, contributes to the epigenetic regulation of gene expression. Distinct patterns …