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ProteomicsC4PR_LIV Evaluation of Parameters for Confident Phosphorylation Site Localization using an Orbitrap Fusion Tribrid Mass Spectrometer
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-03-31 | MSV000085203 | MassIVE
MetabolomicsMulti-omics and biophysical phosphoproteomics uncover functional phosphorylation networks of BRAFV600E-driven signaling

Dysregulated kinase activity drives oncogenic signalling, perturbs cellular homeostasis, and promotes tumour progression. Despite major success in targeting kinases therapeutically, the downstream consequences of kinase inhibition and the mechanisms underlying drug resistance remain incompletely ...

2025-12-09 | MTBLS7390 | MetaboLights
ProteomicsPTMProphet: Fast and Accurate Mass Modification Localization for the Trans-Proteomic Pipeline
Analysis of synthetic peptide reference datasets to demonstrate the performance of PTMProphet, a free and open-source software tool integrated into the Trans-Proteomic Pipeline, which reanalyzes identified spectra from any search engine for which pepXML output is available to provide localization co...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2025-01-10 | MSV000096828 | MassIVE
ProteomicsComprehensive Identification of Phosphorylation Sites on the Numb Endocytic Adaptor Protein
Numb is an endocytic adaptor protein that functions in the endocytosis and intracellular trafficking of membrane receptors and adhesion molecules. Numb localization and function have been shown to be regulated by phosphorylation through atypcial protein kinase C at several key sites. Here, we use ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2016-10-04 | MSV000080218 | MassIVE
ProteomicsC4PR_LIV Evaluation of Parameters for Confident Phosphorylation Site Localization using an Orbitrap Fusion Tribrid Mass Spectrometer
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo sapiens (Human) 
2019-09-27 | PXD007058 | Pride
Mascot/ptmrs Andromeda/ptmscore Orbitrap fusion Mass spectrometry Phosphoproteomics 
TranscriptomicsBudding yeast RNA polymerase II CTD phosphorylation and transcription termination factor localization
Whole genome analysis of total RNA pol II, Ser2-, Ser5- and Ser7-phosphorylated RNA pol II, in WT and mutants of the C-terminal domain (CTD) kinases Ctk1 and Kin28, and localization of the termination factors Pcf11, Nrd1 and Rat1. ChIP-chip using ligation-mediated PCR-amplified material hybridized t...
ORGANISM(S): Saccharomyces cerevisiae 
2010-09-15 | E-GEOD-23960 | biostudies-arrayexpress
ProteomicsSimulated phosphopeptide spectral library for confident site localization
We have developed a new workflow to unambiguously localize phosphorylation sites on proteins. We demonstrate that spectral matching of phosphopeptide datasets against a library of the well-simulated spectra provided higher sensitivity for confident site localization than other tested programs. To co...
ORGANISM(S): Homo sapiens (Human) 
2015-03-17 | PXD000474 | Pride
Synthetic peptide Simulated spectral library Hela Phosphopeptide Lc-ms/ms 
TranscriptomicsEffect of mutating androgen receptor phosphorylation site Tyr-267
Reactivation of androgen receptor (AR) may drive recurrent prostate cancer in castrate patients. Ack1 tyrosine kinase is overexpressed in prostate cancer and promotes castrate resistant xenograft tumor growth and enhances androgen target gene expression and AR recruitment to enhancers. Ack1 phosph...
ORGANISM(S): Homo sapiens 
2015-06-10 | E-GEOD-69712 | biostudies-arrayexpress
ProteomicsThe plasma membrane localization of PLEKHA5 is regulated by the phosphorylation status of S161
The phosphorylation of PLEKHA5 serine 161 residue affects the subcellular localization of the protein. Mutations of this site led to changes in plasma mebrane association during mitosis. The IP-MS experiment was conducted to confirm the phosphorylation at S161.
ORGANISM(S): Homo sapiens (Human) 
2024-07-03 | PXD052237 | Pride
Phosphorylation Mitosis Plekha5 Plasma membrane 
ProteomicsIdentification and phosphorylation site mapping of a sperm specific PKA C subunit isoform from Mytilus galloprovincialis
This project investigates a sperm-specific isoform of the catalytic (C) subunit of cAMP-dependent protein kinase (PKA) in the marine mussel Mytilus galloprovincialis, an externally fertilizing invertebrate widely used as a model for gamete activation studies. A C-subunit isoform purified from male g...
ORGANISM(S): Crenomytilus 
2026-09-07 | PXD076788 | Pride
Camp-dependent protein kinase  pka  catalytic subunit  lc–ms/ms  phosphoproteomics  phosphorylation sites  tio₂ enrichment  mytilus galloprovincialis  sperm 
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