Identification and profiling of histone acetyltransferase substrates by bioorthogonal labeling
Histone acetyltransferases (HATs, also known as lysine acetyltransferases, KATs) catalyze
acetylation of their cognate protein substrates using acetyl‐CoA (Ac‐CoA) as a cofactor and …
acetylation of their cognate protein substrates using acetyl‐CoA (Ac‐CoA) as a cofactor and …
Advances in label-free screening approaches for studying histone acetyltransferases
PT Rye, LE Frick, CC Ozbal… - Journal of Biomolecular …, 2011 - journals.sagepub.com
Histone acetyltransferases (HATs) catalyze the transfer of an acetyl group from an acetyl-
coenzyme A donor molecule to specific lysine residues within proteins. The acetylation state …
coenzyme A donor molecule to specific lysine residues within proteins. The acetylation state …
A quantitative multiplexed mass spectrometry assay for studying the kinetic of residue-specific histone acetylation
YM Kuo, RA Henry, AJ Andrews - Methods, 2014 - Elsevier
Histone acetylation is involved in gene regulation and, most importantly, aberrant regulation
of histone acetylation is correlated with major human diseases. Although many lysine …
of histone acetylation is correlated with major human diseases. Although many lysine …
Fluorescent reporters of the histone acetyltransferase
J Wu, YG Zheng - Analytical biochemistry, 2008 - Elsevier
Histone acetyltransferases (HATs) are important chromatin modifying enzymes that catalyze
acetylation of specific lysine residues in histone and nonhistone substrates. They participate …
acetylation of specific lysine residues in histone and nonhistone substrates. They participate …
Probing lysine acetylation in proteins: strategies, limitations, and pitfalls of in vitro acetyltransferase assays
W Dormeyer, M Ott, M Schnölzer - Molecular & Cellular Proteomics, 2005 - ASBMB
The acetylation of proteins at specific lysine residues by acetyltransferase enzymes has
emerged as a posttranslational modification of high biological impact. Although lysine …
emerged as a posttranslational modification of high biological impact. Although lysine …
Chemoproteomic profiling of protein substrates of a major lysine acetyltransferase in the native cellular context
The family of lysine acetyltransferases (KATs) regulates epigenetics and signaling pathways
in eukaryotic cells. So far, knowledge of different KAT members contributing to the cellular …
in eukaryotic cells. So far, knowledge of different KAT members contributing to the cellular …
Isotopic labeling and quantitative proteomics of acetylation on histones and beyond
Lysine acetylation is an important posttranslational modification (PTM) that regulates the
function of proteins by affecting their localization, stability, binding, and enzymatic activity …
function of proteins by affecting their localization, stability, binding, and enzymatic activity …
Comparative studies of thiol-sensitive fluorogenic probes for HAT assays
T Gao, C Yang, YG Zheng - Analytical and bioanalytical chemistry, 2013 - Springer
Histone acetyltransferases (HATs) catalyze the acetylation of specific lysine residues in
histone and nonhistone proteins. Recent studies showed that acetylation is widely …
histone and nonhistone proteins. Recent studies showed that acetylation is widely …
Bioorthogonal reporters for detecting and profiling protein acetylation and acylation
Protein acylation, exemplified by lysine acetylation, is a type of indispensable and
widespread protein posttranslational modification in eukaryotes. Functional annotation of …
widespread protein posttranslational modification in eukaryotes. Functional annotation of …
Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
S Rajkumar, D Dixon, AM Lipchik, JJ Gruber - JoVE (Journal of Visualized …, 2024 - jove.com
HAT1, also known as Histone acetyltransferase 1, plays a crucial role in chromatin synthesis
by stabilizing and acetylating nascent H4 before nucleosome assembly. It is required for …
by stabilizing and acetylating nascent H4 before nucleosome assembly. It is required for …