Lysine acetylation is a major posttranslational modification involved in a broad array of
physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from …

Lysine acetylation is a reversible posttranslational modification that occurs at thousands of
sites on human proteins. However, the stoichiometry of acetylation remains poorly …

Matrix‐assisted laser desorption/ionization mass spectrometry and tandem mass
spectrometry (MS/MS) were used to determine the multiple acetylation sites in the histone …

Lysine acetylation, first identified in histones, was initially thought to be a posttranslational
modification occuring only in eukaryotic cells that controlled gene transcription either via …

Improved sample preparation techniques and increasingly sensitive mass spectrometry
(MS) analysis have revolutionized the study of protein post-translational modifications …

Post-translational modification of lysine residues by NƐ-acylation is an important regulator of
protein function. Many large-scale protein acylation studies have assessed relative changes …

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

Mass spectrometry (MS) is a powerful analytical method for the identification and
quantification of co-existing post-translational modifications in histone proteins. One of the …

The dynamic modification of histone proteins by lysine methylation has emerged over the
last decade as a key regulator of chromatin functions. In contrast, our understanding of the …

The availability and robustness of methods to analyze phosphorylated proteins has greatly
expanded our knowledge of phosphorylation based cell signaling. A key ingredient to the …