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ProteomicsOxonium ion scanning mass spectrometry for large-scale plasma glycoproteomics
Protein glycosylation, a complex and heterogeneous post-translational modification that is frequently dysregulated in disease, has been difficult to analyse at scale. Here we report a data-independent acquisition technique for the large-scale mass-spectrometric quantification of glycopeptides in pla...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-05-29 | MSV000089567 | MassIVE
ProteomicsBloodstream infection N-glycoproteomics
Here we have performed targeted quantitative N-glycoproteomics from plasma samples of patients with confirmed positive blood culture together with age and sex matched febrile controls with negative blood culture reports. Three hundred and sixty eight potential N-glycopeptides were quantified by mass...
ORGANISM(S): Homo sapiens (Human) 
2018-04-09 | PXD009048 | Pride
Sepsis Human plasma Bloodstream infection N-glycoproteomics 
ProteomicsPlasma glycoproteomics delivers high-specificity disease biomarkers by detecting site-specific glycosylation abnormalities
The human plasma glycoproteome holds enormous potential to identify personalized biomarkers to diagnose and understand disease. Recent advances in mass spectrometry and software development are opening novel avenues to mine the glycoproteome for protein- and site-specific glycosylation changes. Here...
ORGANISM(S): Homo sapiens (Human) 
2022-06-01 | PXD034214 | Pride
Glycoproteomics Plasma Glycopeptide Congenital disorders of glycosylation Blood 
ProteomicsA pipeline for discovery and verification of glycoproteins from plasma-derived extracellular vesicles as breast cancer biomarkers
Glycoproteins comprise more than half of current FDA-approved protein cancer markers but the development of new glycoproteins as disease biomarkers has been stagnant. Here we present a pipeline to develop glycoproteins from extracellular vesicles (EVs) through integrating quantitative glycoproteomic...
ORGANISM(S): Homo sapiens (Human) 
2018-04-26 | PXD007572 | Pride
Extracellular vesicles Glycoproteomics Biomarker 
ProteomicsPlasma N-Glycoproteomics for BMI-discordant monozygotic twin pairs
The aim of the project was to identify altered plasma proteins and altered plasma N-glycopeptides from monozygotic twin pairs who are discordant for body weight. We performed targeted quantitative N-glycoproteomics from plasma samples from 48 twin pairs (n = 96 individuals). This is the N-Glycopept...
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD041584 | Pride
Obesity Human Plasma N-glycopeptidomics Monozygotic twins 
ProteomicsPlasma N-Glycoproteomics for BMI-discordant monozygotic twin pairs
The aim of the project was to identify altered plasma proteins and altered plasma N-glycopeptides from monozygotic twin pairs who are discordant for body weight. We performed targeted quantitative N-glycoproteomics from plasma samples from 48 twin pairs (n = 96 individuals).
ORGANISM(S): Homo sapiens (Human) 
2025-05-06 | PXD041384 | Pride
Glycosylation Proteomics Human Monozygotic twins 
ProteomicsSepsis related glycopeptides - Plasma Glycoproteomics Reveals Sepsis Outcomes Linked to Distinct Proteins in Common Pathways
The plasma of the sepsis patient survivors and non-survivors (n=10/group) were analyzed using glycoproteomics approach.
ORGANISM(S): Homo sapiens (Human) 
2018-10-19 | PXD001425 | Pride
Coagulation Proteomics Extracellular glycoproteins 
ProteomicsEThcD-sceHCD-MS/MS-based Clinical N-glycoproteomics
Site-specific N-glycosylation characterization requires intact N-glycopeptide analysis based on suitable tandem mass spectrometry (MS/MS) method. Electron-transfer/higher-energy collisional dissociation (EThcD), stepped collision energy/higher-energy collisional dissociation (sceHCD), and higher-ene...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD030288 | Pride
Glycoproteomics Mass spectrometry Ethcd-scehcd Fragmentation mode N-glycosylation Clinical sample 
UnknownPlasma glycoproteomics delivers high-specificity disease biomarkers by detecting site-specific glycosylation abnormalities.
Not available
S-EPMC11258658 | biostudies-literature
ProteomicsMaximizing glycoproteomics identification depth in complex mixtures on the timsTOF Pro platform
Glycoproteins play important roles in numerous physiological processes and are often implicated in disease. Analysis of site-specific protein glycobiology through glycoproteomics is evolving rapidly in recent years thanks to hardware and software innovations. Introduction of Parallel Accumulation Se...
ORGANISM(S): Homo sapiens (Human) 
2024-01-03 | PXD047898 | Pride
Glycoproteomics Trapped ion mobility spectrometry Glycopeptide Dda-pasef 
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