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ProteomicsSite-specific O-Glycosylation Analysis of Human Blood Plasma Proteins
Here, we report on the site-specific O-glycosylation analysis of human blood plasma glycoproteins. To this end pooled human blood plasma of healthy donors was digested non-specifically using Protein-ase K, followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2015-06-05 | MSV000079141 | MassIVE
ProteomicsSite-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of individual healthy donors
The uploaded dateset corresponds to MS1 and MS2 spectra obtained for Fc gamma receptor IIIb isolated from neutrophils of individual healthy donors. They represent NA1/NA2, NA2/NA2, NA2/NA2 allotype respectively. Based on the data, the targeted analysis of the N-glycosylation has been performed for t...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-08-05 | MSV000085913 | MassIVE
TranscriptomicsCoordinate Regulation of Metabolites Glycosylation and Stress Hormones Biosynthesis by TT8 in Arabidopsis
Secondary metabolites play a key role in coordinating ecology and defense strategies of plants. Diversity of these metabolites arise by conjugation of core structures with diverse chemical moieties, such as sugars in glycosylation. Active pools of phytohormones, including those involved in plant str...
ORGANISM(S): Arabidopsis thaliana 
2016-07-20 | E-GEOD-59048 | biostudies-arrayexpress
ProteomicsIn-depth site-specific O-glycosylation analysis of glycoproteins and endogenous peptides in cerebrospinal fluid (CSF) from healthy individual mild cognitive impairment (MCI) and Alzheimer disease (AD) patients
Site-specific O-glycoproteome mapping in complex biological system provides molecular basis for understanding the structure-function relationships of glycoproteins and their roles in physiological and pathological processes. Previous O-glycoproteome analysis in cerebrospinal fluid (CSF) focused on s...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-05 | MSV000087160 | MassIVE
ProteomicsSolid-phase extraction of N-linked glycans and glycosite-containing peptides (NGAG) for comprehensive characterization of glycoproteins
A novel chemoenzymatic method termed solid phase extraction of N-linked Glycans And Glycosite-containing peptides (NGAG) for the simultaneous analysis of N-glycans, glycosite-containing peptides, and intact N-glycopeptides with site-specific glycosylation information.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080840 | MassIVE
ProteomicsGlycoPCT: quantitative glycoproteomics based on pressure cycling technology reveals distinctive N-glycosylation in human liver with non-alcoholic fatty liver disease
Protein N-glycosylation plays a crucial role in the human liver, impacting key functions like hepatocyte lipid metabolism hepatocyte apoptosis, and inflammatory response. Despite its significance, the site-specific N-glycosylation patterns and their variations of liver biosy samples between healthy ...
ORGANISM(S): Homo Sapiens 
PXD053626 |
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 
ProteomicsN-glycosylation analysis of human alpha-1-acid glycoprotein LC-MS
Alpha-1-acid glycoprotein (AGP) is an acute phase glycoprotein in blood, which is primarily synthetized in the liver and whose biological role is not completely understood. It consists 45% of carbohydrates attached in the form of five N-linked complex glycans. AGP N-glycosylation was shown to be cha...
ORGANISM(S): Homo sapiens (Human) 
2021-01-04 | PXD020387 | Pride
Agp Lc-ms High troughput N-glycosylation 
ProteomicsGlycoproteomics identify disease-associated N-glycans and reduced occupancy of glycosylation sites in PMM2-CDG
The routine diagnostic pathway for congenital disorders of glycosylation (CDG) relies on carbohydrate deficient transferrin, a test that incompletely captures defects in N linked glycosylation and may yield false negative results even in classical N glycosylation disorders such as PMM2 CDG. To explo...
ORGANISM(S): Homo sapiens (Human) 
2026-09-28 | PXD080194 | Pride
N‐linked glycosylation Carbohydrate metabolism Glycoproteomics Congenital disorders of glycosylation (cdg) Glycopeptide Glycomics Biomarker Inborn error of metabolism 
ProteomicsSugarQuant: a streamlined pipeline for multiplexed quantitative site-specific N-glycoproteomics
Site-specific regulation of protein N-glycosylation is essential in human cells. However, accurate quantification of glycosylation sites and their individual glycan moieties in a cell-wide manner is still technically challenging. Here, we introduce SugarQuant, an integrated mass spectrometry-based p...
ORGANISM(S): Homo sapiens (Human) 
2020-08-24 | PXD018349 | Pride
Glycosylation 
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