Reversible posttranslational modification of internal lysines in many cellular or viral proteins
is now emerging as part of critical signalling processes controlling a variety of cellular …

Lysine acetylation appears to be crucial for diverse biological phenomena, including all the
DNA-templated processes, metabolism, cytoskeleton dynamics, cell signaling, and circadian …

Post-translational acetylation of lysine residues has emerged as a key regulatory
mechanism in all eukaryotic organisms. Originally discovered in 1963 as a unique …

Acetylation of proteins on lysine residues is a dynamic posttranslational modification that is
known to play a key role in regulating transcription and other DNA-dependent nuclear …

Recent proteomic studies reveal that 5–10% of mammalian and bacterial proteins undergo
lysine acetylation, a post-translational modification that adds an acetyl group to the ɛ-amino …

Lysine acetylation has emerged as a major posttranslational modification for histones.
Crossregulation between this and other modifications is crucial in modulating chromatin …

The 'language'of covalent histone modifications translates environmental and cellular cues
into gene expression. This vast array of post-translational modifications on histones are …

Lysine acetylation is a post-translational modification that critically regulates gene
transcription by targeting histones as well as a variety of transcription factors in the nucleus …

Lysine acetylation is a reversible modification controlled by two groups of enzymes: lysine
acetyltransferases (KATs) and lysine deacetylases (KDACs). Acetylated lysine residues are …

Introduction Lysine acetylation is a reversible post-translational modification (PTM)
regulated through the action of specific types of enzymes: lysine acetyltransferases (KATs) …