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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
ProteomicsHuman serum N-linked intact glycopeptides LC-MS/MS
Large-scale identification of N-linked intact glycopeptides by liquid chromatography coupled tandem mass spectrometry (LC-MS/MS) in human serum is challenging due to the wide dynamic range of serum protein abundances, the lack of a complete serum N-Glycan database and the existence of non-specifical...
ORGANISM(S): Armoracia rusticana Homo sapiens (Human) Gallus gallus (Chicken) 
2020-04-21 | PXD015622 | Pride
N-linked intact glycopeptide Co-elution Spectral library search Human serum Isotopic distribution 
ProteomicsIdentification of N-linked glycosylated peptides in the open ocean diatom Thalassiosira oceanica
N-linked glycosylation is a posttranslational modification affecting protein folding and protein function. The N-linked glycosylation pathway in algae is poorly characterized, and further knowledge is needed to understand the cell biology of algae and the evolution of N-linked glycosylation. This st...
ORGANISM(S): Thalassiosira oceanica 
2021-09-09 | PXD021782 | Pride
Diatom Solid-phase extraction of n-linked glycosylated peptides N-linked glycosylation 
ProteomicsLC-MS/MS-based 4D Label-Free N-Glycosylation Proteomics Analysis of Bone Marrow Cells from ADO2 Mouse
This project aims to investigate N-linked glycosylation modifications in bone marrow cells (BMCs) of an autosomal dominant osteopetrosis type 2 (ADO2) mouse model carrying the Clcn7 (r284w) mutation. Using LC-MS/MS-based 4D Label-Free N-Glycosylation Proteomics Analysis, we identified significant al...
ORGANISM(S): Mus Musculus 
2025-02-05 | PXD060501 |
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 (Human) 
2015-11-23 | PXD001571 | Pride
Lc-msms Glycosylation Deglycopeptide Glycosites Speg Spegag 
ProteomicsSite specific N-linked glycosylation analysis of spike proteins of SARS-CoV, MERS-CoV, HCoV-HKU1, HCoV-NL63, and HCoV-229E
Site specific N-linked glycosylation analysis of spike proteins of SARS-CoV, MERS-CoV, HCoV-HKU1, HCoV-NL63, and HCoV-229E
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
MSV000092889 | MassIVE
GenomicsN-linked glycosylation is essential for anti-tumor activities of KIAA1324 in gastric cancer
N-linked glycosylation is essential for anti-tumor activities of KIAA1324 in gastric cancer
PRJNA1001364 | ENA
ProteomicsN-linked glycosylation of recombinant Porcine Delta Coronavirus spike protein ectodomain from drosophila S2 cells
Recombinant PDCoV spike glycoprotein was produced from Drosophile S2 cells for structural characterization by cryo electron microscopy and mass spectrometry. MS was used to assess the N-linked glycosylation profile of the purified material. We used a multiple protease digestion in combination with R...
ORGANISM(S): Deltacoronavirus PDCoV/USA/Illinois121/2014 
2017-10-24 | PXD007107 | Pride
Virus  n-linked glycosylation 
ProteomicsComprehensive analysis of the proteome, phosphoproteome and N-linked sialylated glycoproteome of C2C12 myoblasts
C2C12 myoblast is a model that has been used extensively to study the process of skeletal muscle differentiation. Proteomics has advanced our understanding of skeletal muscle biology and the process of myogenesis. However, there is still no deep coverage of C2C12 myoblast proteome, which is importan...
ORGANISM(S): Mus musculus (Mouse) 
2020-11-27 | PXD011334 | Pride
Ptmome Mouse Skeletal myoblasts Proteome 
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 
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