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MetabolomicsInositol triphosphate-triggered calcium release blocks lipid exchange at endoplasmic reticulum-Golgi contact sites
Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, and metabolites. Recruitment of membrane tethers to contact sites between the endoplasmic reticulum (ER) and the plasma membrane is often triggered by calcium. In contrast, we reveal here a funct...
2021-05-06 | MTBLS2444 | MetaboLights
GenomicsGenome-wide profiling of H3K56 acetylation and transcription factor binding sites in human adipocytes
We use ChIP-seq to discover the genome-wide sites of acetylation of lysine 56 of the histone H3 (H3K56), which is a target of three histone modifying enzymes with known roles in diabetes and insulin resistance, in human adipocytes derived from mesenchymal stem cells. Surprisingly, we find that a ver...
ORGANISM(S): Homo sapiens 
2011-05-31 | E-GEOD-24326 | biostudies-arrayexpress
ProteomicsIn-vitro acetylation assay of TULP3
Fig. S1D: An in-vitro assay that identified the acetylation sites on recombinant TULP3 with the addition of recombinant human p300.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-10-20 | MSV000086340 | MassIVE
ProteomicsSites of aspirin-mediated lysine acetylation in HeLa cells
Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino-acid side-chains, leading to speculation that aspiri...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080778 | MassIVE
ProteomicsSites of aspirin-mediated lysine acetylation in HeLa cells, part 2
Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino-acid side-chains, leading to speculation that aspiri...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080852 | MassIVE
TranscriptomicsComplex patterns of accessibility discriminate sites of PcG repression, H4K16 acetylation and replication initiation
Full title: Complex patterns of genome accessibility discriminate sites of PcG repression, H4K16 acetylation and replication initiation Histone modifications have been proposed to regulate gene expression in part by modulating DNA accessibility and higher-order chromatin structure. However, there i...
ORGANISM(S): Drosophila melanogaster 
2010-03-16 | E-GEOD-17697 | biostudies-arrayexpress
TranscriptomicsChromatin immunopreciptiation of human lymphoblastoid cells to identify histone H3K9/14 acetylation regions at common fragile sites
Map the histone H3K9/14 acetylation regions of in human cells at 7 common fragile sites and their flanking non-fragile sequences as well as a 200kb containing the rare fragile site FRAXA, a 1,075kb non-fragile region on chr22, a hyperacetylated region HALPHA44, and a heterochromatic region HET405. T...
ORGANISM(S): Homo sapiens 
2009-10-07 | E-TABM-347 | 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
ProteomicsAcetylation site mapping on TULP3
Fig. 2B: Semi-quantitative acetylation level on TULP3 in the presence of either empty pcDNA 3.1(+), Myc-p300, FLAG-PCAF or FLAG-GCN5 following immunoprecipitation.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-10-22 | MSV000086358 | MassIVE
GenomicsIdentification and Characterization of Hoxa9 Binding Sites in Hematopoietic Cells
The clustered homeobox proteins play crucial roles in development, hematopoiesis and leukemia yet the targets they regulate and their mechanisms of action are poorly understood. Here, we identified the binding sites for Hoxa9 and the Hox cofactor Meis1 on a genome-wide level and profiled their asso...
ORGANISM(S): Mus musculus 
2011-12-04 | E-GEOD-33509 | biostudies-arrayexpress
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