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ProteomicsChemical proteomics profiling of N-terminal and lysine acetyltransferases
Acetylation of amino groups is a prevalent protein modification in all kingdoms of life. Acetyl groups are transferred from Coenzyme A (CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA ...
ORGANISM(S): Homo Sapiens (human) 
2021-04-14 | PXD018544 | JPOST Repository
ProteomicsInvestigating peptide-Coenzyme A-conjugates as chemical probes for proteomic profiling of N-terminal and lysine acetyltransferases
Acetyl groups are transferred from Acetyl-Coenzyme A (Ac-CoA) to protein N-termini and lysine side chains by N-terminal acetyltransferases (NATs) and lysine acetyltransferases (KATs), respectively. Building on lysine-CoA conjugates as KAT probes, we have synthesized peptide probes with CoA conjugate...
ORGANISM(S): Homo Sapiens (human) 
2022-05-02 | PXD032957 | JPOST Repository
GenomicsChIP-seq of MYST acetyltransferases
Histone acetyltransferases (HAT) assemble into multisubunit complexes in order to target distinct lysine residues on nucleosomal histones. Here, we characterize native HAT complexes assembled by the BRPF-family of scaffold proteins. Their PHD-ZnKnuckle-PHD domain is essential for binding chromatin...
ORGANISM(S): Homo sapiens 
2013-10-09 | E-GEOD-47190 | biostudies-arrayexpress
ProteomicsTargeted degradation of the enhancer lysine acetyltransferases CBP and p300
The enhancer factors CBP/p300 maintain gene expression programs through lysine acetylation of chromatin and transcriptional regulators and by scaffolding functions mediated by several protein-protein interaction domains. We have designed dCBP-1, a compound that induces degradation of CBP/p300, and ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-11-15 | MSV000086457 | MassIVE
TranscriptomicsHistone posttranslational modifications and cell fate determination: Lens induction requires the lysine acetyltransferases CBP and p300
This SuperSeries is composed of the SubSeries listed below. Refer to individual Series
ORGANISM(S): Mus musculus 
2013-09-23 | E-GEOD-49219 | biostudies-arrayexpress
ProteomicsHierarchical small molecule inhibition of MYST acetyltransferases
MYST lysine acetyltransferases (KATs) is a class of epigenetic enzymes critical for cellular function that constitute an emerging therapeutic target in cancer. Recently, several drug-like MYST inhibitors have been reported that show promise in a variety of preclinical models as well as in clinical t...
ORGANISM(S): Homo sapiens (Human) 
2026-06-01 | PXD074488 | Pride
Histone acetylation Lysine acetyltransferases Wm-1119 Wm-3835 Drug-like myst inhibitors Chemoproteomics Myst Foxk2 Pf-9363 Wm-8014 
TranscriptomicsChromatin immunoprecipitation genome wide occupancy of 4 different chromatin regulating complexes encoded in yeast
We explore the genome-wide occupancy of 4 different chromatin regulating complexes encoded in S. cerevisiae. We provide the data for histone acetyltransferases Gcn5 and Esa1 and histone deacetylases Hst1 and Rpd3/Sin3 under rich growth condition (YPD medium). We also include the occupancy data for R...
ORGANISM(S): Saccharomyces cerevisiae 
2005-11-03 | E-WMIT-2 | biostudies-arrayexpress
UnknownInsights into the specificity of lysine acetyltransferases.
Not available
S-EPMC4276886 | biostudies-literature
GenomicsEffect of depletion of histone acetyltransferases and histone deacetylases on gene expression in Drosophila embryos
Effect of depletion of histone acetyltransferases and histone deacetylases on gene expression in Drosophila embryos
PRJNA853323 | ENA
UnknownRegulating histone acetyltransferases and deacetylases.
Not available
S-EPMC1326399 | biostudies-literature
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