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UnknownHDAC6 and SIRT2 regulate the acetylation state and oncogenic activity of mutant K-RAS.
Not available
S-EPMC3778089 | biostudies-literature
UnknownThe Impact of ackA, pta, and ackA-pta Mutations on Growth, Gene Expression and Protein Acetylation in Escherichia coli K-12.
Not available
S-EPMC7047895 | biostudies-literature
ProteomicsMetabolic regulation of N-terminal acetylation in yeast
N-terminal (Nt) acetylation, catalyzed by N-terminal acetyltransferases (NATs), has emerged as an important co-translational modification in eukaryotes, and involves the transfer of the acetyl moiety from acetyl-CoA (Ac-CoA) to the α-amino group of a nascent polypeptide. Here, we report the first gl...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-07 | PXD004326 | Pride
Metabolism Acetyl coenzyme a Saccharomyces cerevisiae N-terminal acetylation N-terminomics 
ProteomicsIntegrated lysine acetylation stoichiometry and proteomics analysis in human cells
Lysine acetylation is a widespread posttranslational modification that targets a large number of biological pathways. Recent studies reveal that lysine acetylation sites exhibit mainly low stoichiometry. Here we explored three sample preparation methods, the use of detergents for the chemical acetyl...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-11-09 | MSV000081704 | MassIVE
ProteomicsGlobal profiling of acetylation reveals a new family with dual-specific lysine and N-terminal acetyltransferase activity in the plastids of Arabidopsis
Protein acetylation is a universally conserved modification occurring on N-termini (N--acetylation, NTA) and on internal lysines residues (-lysine-acetylation, KA). So far, NTA and KA were known to be supported by distinct families of enzymes (NATs and KATs, respectively), despite most of them sha...
ORGANISM(S): Escherichia Coli 
2020-07-07 | PXD015875 | JPOST Repository
TranscriptomicsAcetylation of p65 at lysine 314 is important for late NF-k(kappa)B-dependent gene expression
We provided earlier evidence that acetylation of p65 at lysines 310, 314 and 315 is important for the expression of a defined subset of genes; acetylation at these residues regulates both positively and negatively gene expression, in a gene-specific manner. These earlier studies provided a first gla...
ORGANISM(S): Mus musculus 
2010-04-08 | E-GEOD-15196 | biostudies-arrayexpress
GenomicsMitochondrial ACSS1-K-635 acetylation mimic knock-in mice exhibit altered lipid metabolism, hepatic cell senescence, and acute non-alcoholic fatty liver [2ndSet_analysis]
Mitochondrial ACSS1-K-635 acetylation mimic knock-in mice exhibit altered lipid metabolism, hepatic cell senescence, and acute non-alcoholic fatty liver [2ndSet_analysis]
PRJNA1082272 | ENA
GenomicsMitochondrial ACSS1-K-635 acetylation mimic knock-in mice exhibit altered lipid metabolism, hepatic cell senescence, and acute non-alcoholic fatty liver [1stSet_analysis]
Mitochondrial ACSS1-K-635 acetylation mimic knock-in mice exhibit altered lipid metabolism, hepatic cell senescence, and acute non-alcoholic fatty liver [1stSet_analysis]
PRJNA1082273 | ENA
GenomicsGATA4 represses an ileal program of gene expression in the proximal small intestine by inhibiting the acetylation of histone H3, lysine 27.
GATA4 is expressed in the proximal 85% of small intestine where it promotes a proximal intestinal ('jejunal') identity while repressing a distal intestinal ('ileal') identity, but its molecular mechanisms are unclear. Here, we tested the hypothesis that GATA4 promotes a jejunal versus ileal identity...
ORGANISM(S): Mus musculus 
2015-05-16 | E-GEOD-68957 | biostudies-arrayexpress
TranscriptomicsHistone H3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells
Lysine 56 acetylation in the helical core of histone H3 opens yeast chromatin and enables histone gene transcription, DNA replication, DNA repair, and prevents epigenetic silencing. While K56Ac is globally abundant in yeast and flies its presence has been uncertain in mammals. We show here using mas...
ORGANISM(S): Homo sapiens 
2009-02-09 | E-GEOD-14749 | biostudies-arrayexpress
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