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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
ProteomicsAn automated intact glycopeptide enrichment method for serum site-specific N-glycoproteomic analysis
We developed an automated glycopeptide enrichment method for the analysis of serum site-specific N-glycoproteome. This automated method allowed for processing one sample within 20 min. It showed higher enrichment specificity, more intact glycopeptide identifications, and better quantitative reproduc...
ORGANISM(S): Homo Sapiens (human) 
2021-04-06 | PXD025151 | JPOST Repository
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
ProteomicsSupporting information for tryptic EPO glycopeptide LC-MS analysis via cysteine aminoethylation
Supplementary information for a technical note describing the application of cysteine aminoethylation for the site-specific glycosylation analysis of recombinant human EPO using trypsin as sole protease.
ORGANISM(S): Cho Cells 
2020-04-21 | MSV000085318 | MassIVE
ProteomicsRelative Quantitative Analysis of Site-Specific N-Linked Glycosylation in Hyperglycosylated In-terferon-β via Mass Spectrometry
Glycosylation is a critical determinant of the efficacy, stability, and pharmacological behavior of therapeutic proteins. R27T, an engineered variant of interferon-β1a, contains two N-glycosylation sites (Asn25 and Asn80), increasing its structural complexity and analytical requirements. In this stu...
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD077477 | Pride
Interferon beta  n-linked glycan  site-specific glycosylation  relative quantitative analysis  r27t 
ProteomicsSite-specific Extraction of O-linked glycopeptides (EXoO) Maps Landscape of In Vivo O-linked Glycoproteome
Protein glycosylation is one of the most common protein modifications and plays essential roles in biology and therapeutics. However, the analysis of in vivo O-linked glycosylation, a major type of protein glycosylation, has been severely impeded by the scarcity of technology. Here, a chemoenzymatic...
ORGANISM(S): Homo sapiens (Human) 
2018-12-05 | PXD009476 | Pride
Site-specific Glycosylation Exoo In vivo O-linked 
ProteomicsSite-specific N-glycosylation of HeLa cell glycoproteins
HeLa cell line is frequently used in biomedical research, however little is known about N-glycan structures expressed on individual glycoproteins of this complex sample. We characterized site-specific N-glycosylation of HeLa N-glycoproteins using a complex workflow based on high and low energy tande...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2019-10-21 | PXD013930 | Pride
Hela Nanouhplc-ms/ms N-glycosylation Site-specific 
ProteomicsSite-Specific Glycosylation Profiling of Protein Subunit and Inactivated Virus Vaccines
Many protein subunit vaccines and biologics contain glycosylated antigens and antibodies, yet quantitative frameworks for comparing glycosylation across lots, manufacturers, and production platforms remain limited. We performed site specific glycosylation LC-MS/MS analysis for intact N-linked glycop...
ORGANISM(S): Influenza A virus (A/Panama/2007/1999(H3N2)) Influenza A virus (A/Philippines/2/1982(H3N2)) Human alphaherpesvirus 3 Influenza A virus (A/New Caledonia/20/1999(H1N1)) Severe acute respiratory syndrome coronavirus 2 Influenza A virus (A/Shandong/9/1993(H3N2)) 
2026-07-21 | PXD074672 | Pride
Glycosylation Mass spectrometry Site-specific Vaccines Proteomics 
ProteomicsAlterations in protein expression and site-specific N-glycosylation of prostate cancer tissues
Samples were analyzed using a Maxis II QTOF instrument (Bruker Daltonik GmbH, Bremen, Germany) equipped with CaptiveSpray nanoBooster ion source coupled to a Dionex UltiMate 3000 RSLCnano system (Sunnyvale, CA, USA). Peptides were separated on an Acquity M-Class BEH130 C18 analytical column using gr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-28 | MSV000087329 | MassIVE
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