Sort   by:  
 Page size 
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 
TranscriptomicsHistone acetylation and DNA demethylation of T-cells result in an anaplastic large cell lymphoma-like phenotype.
A characteristic feature of anaplastic large cell lymphoma (ALCL) is the significant reduction of the T-cell expression program despite its T-cell origin, a finding very similar to the loss of B-cell identity of classical Hodgkin lymphoma (cHL). Previously we demonstrated that epigenetic mechanisms ...
ORGANISM(S): Homo sapiens 
2012-08-19 | E-GEOD-26101 | biostudies-arrayexpress
ProteomicsAntibody-free targeted proteomics assay for absolute measurement of α-tubulin acetylation
Acetylation of α-tubulin at conserved lysine 40 (K40) amino acid residue regulates microtubule dynamics and controls a wide range of cellular activities. Dysregulated microtubule dynamics characterised by differential α-tubulin acetylation is a hallmark of cancer, neurodegeneration and other complex...
ORGANISM(S): Homo Sapiens Mus Musculus 
2020-07-30 | PXD018626 | panorama
GenomicsTranscriptional regulation by H3K122 acetylation in the lateral surface of the histone octamer
We characterize the acetylation of H3K122 for the first time. Towards this we mapped the genomic distribution of H3K122Ac, identified the enzyme introducing H3K122Ac, and addressed the functional contribution H3K122Ac to transcription. We found that H3K122Ac is associated with chromatin marks and ge...
ORGANISM(S): Homo sapiens 
2013-02-14 | E-GEOD-35954 | biostudies-arrayexpress
GenomicsGenome-wide H3K9 acetylation state before and after VPA treatment
Genome-wide maps of the H3K9 acetylation state in embryonic stem cells (ESCs) before and after treatment with low levels of the histone deacetylase (HDAC) inhibitor valproic acid (VPA). ChIP-seq for 3 samples: untreated E14 cells, cells treated with VPA for 4 hrs and cells treated with VPA for 16 hr...
ORGANISM(S): Mus musculus 
2011-09-17 | E-GEOD-24211 | biostudies-arrayexpress
GenomicsDUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes
Ectopic expression of the double homeodomain transcription factor DUX4 causes facioscapulohumeral muscular dystrophy (FSHD). Mechanisms of action of DUX4 are currently unknown. Using immortalized human myoblasts with a titratable DUX4 transgene, we identify by mass spectrometry an interaction betwee...
ORGANISM(S): Homo sapiens 
2016-03-10 | E-GEOD-78158 | biostudies-arrayexpress
TranscriptomicsChromatin immunoprecipitation genome wide map of nucleosome acetylation and methylation in Yeast
Genomes are packaged into nucleosomes whose position and modification state can profoundly influence regulation of gene expression. We have established new ChIP-based high-resolution genome-wide maps of histone acetylation and methylation that take into account changes in nucleosome occupancy at act...
ORGANISM(S): Saccharomyces cerevisiae 
2005-08-25 | E-WMIT-3 | biostudies-arrayexpress
TranscriptomicsChromatin immunoprecipitation to map nucleosomes and H3 lysine 14 acetylation in two unrelated strains of yeast
Nucleosome mapping and histone H3 lysine 14 acetylation chromatin immuno-precipitation in two unrelated strains of yeast (BY and RM).
ORGANISM(S): Saccharomyces cerevisiae 
2009-08-29 | E-MEXP-1777 | biostudies-arrayexpress
UnknownIncreasing cell permeability of N-acetylglucosamine via 6-acetylation enhances capacity to suppress T-helper 1 (TH1)/TH17 responses and autoimmunity.
Not available
S-EPMC6435169 | biostudies-literature
ProteomicsStructural insights into p300 regulation and acetylation-dependent genome organisation
Histone modifications are deposited by chromatin modifying enzymes and read out by proteins that recognize the modified state. BRD4-NUT is an oncogenic fusion protein of the acetyl lysine reader BRD4 that binds to the acetylase p300 and enables formation of long-range intra- and interchromosomal int...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD038798 | Pride
P300 Nucleosome Acetylation 
Sort   by:  
 Page size