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ProteomicsHeLa cell protein interactome of polyamine affinity-based probes (probe-modified peptides)
HeLa cells were incubated with affinity-based probes designed as synthetic analogs of endogenous metabolites: putrescine, spermidine, and spermine. Probe-protein interactions were captured in situ using UV-induced crosslinking. After cell lysis, the probe–protein conjugates were subjected to bioorth...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD066655 | Pride
Photoaffinity probes Polyamines Probe-modified peptides 
ProteomicsIdentification of myristoylated proteins in Human cell lines (HEK293, HeLa, MCF7)
Multi-functional capture reagents reported here enable robust identification of metabolically-tagged myristoylated proteomes with unprecedented confidence resulting from the combination of chemical probe-based enrichment, and release and direct detection of lipid-modified peptides by MS. Whilst capt...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080690 | MassIVE
OtherMultifunctional Reagents for Quantitative Proteome-Wide Analysis of Protein Modification in Human Cells and Dynamic Profiling of Protein Lipidation During Vertebrate Development.
Data from ProteomeXchange, PXD ID: PXD001863. File: HEK_HeLa_MCF_ PEAKS7.mgf. Published as part of Angew Chem Int Ed Engl. 2015 Mar 25 . From the Abstract: {{i}} Novel multifunctional reagents were applied in combination with a lipid probe for affinity enrichment of myristoylated proteins and direc...
ORGANISM(S): Homo_sapiens_viruses, Human 
GPM32320014414 | GPMDB
Resource Reanalysis 
UnknownDetecting diagnostic features in MS/MS spectra of post-translationally modified peptides.
Not available
S-EPMC10338467 | biostudies-literature
ProteomicsQuantitative thiol reactivity profiling
Cysteine is unique among all protein-coding amino acids owing to its intrinsically high nucleophilicity. The cysteinyl thiol group can be covalently modified by both a broad range of redox mechanisms and various electrophiles derived from exogenous or endogenous sources. Measuring proteomic cysteine...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2020-07-24 | PXD016048 | Pride
Thiol Redox Chemical proteomics Electrophile 
UnknownRole of Peptides in Diagnostics.
Not available
S-EPMC8396325 | biostudies-literature
UnknownStudies of Surface Preparation for the Fluorosequencing of Peptides.
Not available
S-EPMC8982273 | biostudies-literature
ProteomicsProfiling of Methylglyoxal Blood Metabolism and Advanced Glycation End-Product Proteome using a Chemical Probe
Methylglyoxal (MG) is a toxic byproduct of the glycolytic pathway and is quantitatively the most important precursor to advanced glycation end-products (AGEs). Insight into which proteins and in particular their individual modification sites are central to understand the involvement of MG and AGE in...
ORGANISM(S): Homo sapiens (Human) 
2019-07-31 | PXD011314 | Pride
Human Erythrocytes Plasma Methylglyoxal 
ProteomicsEnrichment of Cysteine S-palmitoylated peptides using Sodium Deoxycholate Acid Precipitation - SDC-ACE
S-palmitoylation is a poorly understood post-translational modification that is gaining more attention as an essential regulator of cellular processes. The reversible nature of S-palmitoylation allows for fine-tuned control of cellular events and adaptation to stimuli. The enrichment of S-palmitoyla...
ORGANISM(S): Mus musculus (Mouse) Acyrthosiphon pisum (Pea aphid) 
2026-02-16 | PXD054682 | Pride
Cysteine palmitoylation  mouse brain palmitoylome  dbdb mice  mouse tissue specific palmitoylation 
ProteomicsMass spectrometric analysis of chondroitin sulfate-linked peptides
Chondroitin sulfate proteoglycans are integral components of the extracellular matrix. These are composed of repeating disaccharide units of glucuronic acid and N-acetylgalactosamine linked to a serine residue on the core protein through an oligosaccharide linker. The functions of chondroitin sulfat...
ORGANISM(S): Homo sapiens (Human) 
2022-10-13 | PXD029400 | Pride
Human Urine Chondroitin-sulfate linked peptides Plasma Proteoglycans Fibroblasts Lc-ms/ms 
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