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ProteomicsPervanadate reveals a new redox model of cellular phosphotyrosine 1 signaling C4PR_LIV
Protein tyrosine phosphorylation (pTyr) is controlled by protein tyrosine kinases and phosphatases (PTPs) and allows cells to sense and respond to changes in their environment. Pervanadate is a widely used chemical tool that induces global pTyr, a phenomenon attributed to its properties as a PTP inh...
ORGANISM(S): Homo sapiens (Human) 
2026-03-10 | PXD059641 | Pride
ProteomicsRedox Regulation of Brain Selective Kinases BRSK1/2: Implications for Dynamic Control of the Eukaryotic AMPK family through Cys-based mechanisms
In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs). While regulation by activation segment phosphorylation in Ser/Thr kinases is well understood, relatively little is known about how oxidation of cysteine (Cys) amino acids modulates cat...
ORGANISM(S): Homo sapiens (Human) 
2025-04-01 | PXD044990 | Pride
Brsk1 Redox Disulfide Brsk2 Cysteine 
ProteomicsPSKH1 co-immunoprecipitation from human cells and binding partner analysis
PSKH1 co-immunoprecipitation from human cells and binding partner analysis
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD055768 | Pride
Co-ip Pskh1 
ProteomicsDiscovery of a new Cushing’s syndrome PKAc mutant that is retained within anchored type I holoenzymes
Adrenal Cushing’s syndrome is a disease of cortisol hypersecretion often caused by mutations in protein kinase A catalytic subunit (PKAc). Using a personalized medicine screening platform, we discovered a new Cushing’s driver mutation, PKAc-W196G, in ~20% of patient samples analyzed. Proximity prote...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2024-02-10 | PXD045556 | Pride
Cushing's syndrome Pka 
ProteomicsA bespoke analytical workflow for the identification of sulfopep-tides and confident discrimination from phosphopeptides_C4PR_LIV
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalysed by Golgi-resident Tyrosyl Protein Sul-foTransferases (TPSTs). Information on protein tyrosine sulfation is currently limited to ~50 human proteins with only a handful of those having verified sites of sulfation. The...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD043723 | Pride
Tyrosine-o-sulfation Sulfotyrosine Sulfation 
ProteomicsA bespoke analytical workflow for the identification of sulfopep-tides and confident discrimination from phosphopeptides_C4PR_LIV
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalysed by Golgi-resident Tyrosyl Protein Sul-foTransferases (TPSTs). Information on protein tyrosine sulfation is currently limited to ~50 human proteins with only a handful of those having verified sites of sulfation. The...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD043713 | Pride
Tyrosine-o-sulfation Sulfotyrosine Sulfation 
ProteomicsAn optimized SP3 sample processing workflow for in-depth phos-phoproteomics and improved identification of multiply phosphory-lated peptides
Protein phosphorylation is a critical and ubiquitous post-translational modification (PTM) found across the kingdoms of life. Advances in high-throughput mass spectrometry have transformed our ability to interrogate the phosphoproteome. However, sample prepara-tion methodologies optimized for phosp...
ORGANISM(S): Homo sapiens (Human) 
2025-08-25 | PXD061013 | Pride
Phosphorylation  multiply phosphorylated  mass spectrometry  ptm  sp3  tio2  c18. 
ProteomicsEvolutionary and cellular analysis of the'dark'pseudokinase PSKH2
Pseudokinases, so named because they lack one or more conserved canonical amino acids that define their catalytically-active relatives, have evolved a variety of biological functions in both prokaryotic and eukaryotic organisms. Human PSKH2 is closely related to the canonical kinase PSKH1, which map...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD039306 | Pride
Pseudokinase Pskh2 
ProteomicsOxygen-dependent changes in HIF binding partners and post-translational modifications regulate stability and transcriptional activity C4PR_LIV
Adaption of cells to low oxygen environments is an essential process mediated in part by the Hypoxia Inducible Factors (HIFs). Like other transcription factors, the stability and transcriptional activity of HIFs, and consequently the hypoxic response, are regulated by post-translational modification...
ORGANISM(S): Homo sapiens (Human) 
2026-03-10 | PXD022479 | Pride
ProteomicsDisplacement of PKA catalytic subunit from AKAP signaling islands drives pathology in Cushing’s syndrome C4PR_LIV
Mutations in the catalytic subunit of protein kinase A (PKAc) drive the stress hormone disorder adrenal Cushing’s syndrome. We define mechanisms of action for the PKAcL205R and W196R variants. Proximity proteomic techniques demonstrate that both Cushing’s mutants are excluded from A kinase anchoring...
ORGANISM(S): Homo sapiens (Human) 
2022-07-12 | PXD030888 | Pride
Cortisol Proximity biotinylation Prkaca Scaffold Stress hormone Anchoring Signaling Photoactivation Adrenal 
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