Post-translational modification of lysine residues via reversible acylation occurs on proteins
from diverse pathways, functions, and organisms. While nuclear protein acylation reflects the …

Post-translational modifications (PTM) decorate proteins to provide functional heterogeneity
to an existing proteome. The large number of known PTMs highlights the many ways that …

Protein acylation links energetic substrate flux with cellular adaptive responses. SIRT5 is a
NAD+-dependent lysine deacylase and removes both succinyl and malonyl groups. Using …

Reversible protein acetylation is a major regulatory mechanism for controlling protein
function. Through genetic manipulations, dietary perturbations, and new proteomic …

Proteins are decorated with a diverse array of post-translational modifications (PTMs) that
regulate their spatial and temporal functions. Recent mass spectrometry (MS)-based studies …

Posttranslational modification of a protein, either alone or in combination with other
modifications, can control properties of that protein, such as enzymatic activity, localization …

Cellular signaling pathways are regulated in a highly dynamic fashion in order to quickly
adapt to distinct environmental conditions. Acetylation of lysine residues represents a central …

This study sought to examine the functional significance of mitochondrial protein acetylation
using a double knockout (DKO) mouse model harboring muscle-specific deficits in acetyl …

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 …

Although limited proteolysis of the histone H3 N-terminal tail (H3NT) is frequently observed
during mammalian differentiation, the specific genomic sites targeted for H3NT proteolysis …