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GenomicsProteo-Genomic Characterization and Mapping of Nucleosomes Decoded by Brd and HP1 Proteins (Chip-Seq data)
Background: Histone post-translational modifications (PTMs) constitute a branch of epigenetic mechanisms that can control the expression of eukaryotic genes in a heritable manner. Recent studies have identified several PTM-binding proteins containing diverse specialized domains whose recognition of ...
ORGANISM(S): Homo sapiens 
2012-07-31 | E-GEOD-39579 | biostudies-arrayexpress
UnknownIntegrative Multi-PTM Proteomics Reveals Dynamic Global, Redox, Phosphorylation, and Acetylation Regulation in Cytokine-Treated Pancreatic Beta Cells.
Not available
S-EPMC11700301 | biostudies-literature
UnknownPTM-Shepherd: Analysis and Summarization of Post-Translational and Chemical Modifications From Open Search Results.
Not available
S-EPMC7950090 | biostudies-literature
UnknownPTMoreR-enabled cross-species PTM mapping and comparative phosphoproteomics across mammals.
Not available
S-EPMC11440062 | biostudies-literature
ProteomicsFAIMS enhances the detection of PTM crosstalk sites
Protein post-translational modification (PTMs) enable cells to rapidly change in response to biological stimuli. With over 400 PTMs, understanding these control mechanisms is complex. To date, efforts have focused on investigating the effect of single PTMs on protein function. Yet, many proteins con...
ORGANISM(S): Homo sapiens (Human) 
2025-03-11 | PXD026448 | Pride
Faims Lc-ms Post-translational modifications Interplay Crosstalk 
ProteomicsAn Integrative SP3 Workflow for Multi-PTM Proteomics Profiling
Global proteomic, redox proteomic, and phosphoproteomic data from mouse C10 epithelial cells and skeletal muscle tissue, no treatments used for method development experiments using these biological sytems. Global proteomic, redox proteomic, phosphoproteomic, and acetylomic data from mouse Beta-TC-6 ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2024-07-06 | MSV000095264 | MassIVE
UnknownIntegrating Clinical Cancer and PTM Proteomics Data Identifies a Mechanism of ACK1 Kinase Activation.
Not available
S-EPMC10831333 | biostudies-literature
ProteomicsSystems level analysis of histone H3 post-translational modifications reveals features of PTM crosstalk in chromatin regulation
Chromatin structure and function is maintained by dynamic protein-protein and protein-nucleic acid interactions. Histones are a family of proteins that are abundant chromatin constituents and that carry numerous post-translational modifications (PTMs). Histone PTMs mediate a variety of biological ac...
ORGANISM(S): Mus musculus (Mouse) 
2016-06-16 | PXD002560 | Pride
Post-translational modification  crosstalk  histone  mass spectrometry  proteomics 
UnknownStructural Analysis of PTM Hotspots (SAPH-ire)--A Quantitative Informatics Method Enabling the Discovery of Novel Regulatory Elements in Protein Families.
Not available
S-EPMC4528253 | biostudies-literature
UnknownMSFragger-Labile: A Flexible Method to Improve Labile PTM Analysis in Proteomics.
Not available
S-EPMC10182319 | biostudies-literature
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