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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
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 
ProteomicsGlycoproteomic Analyses of Prostate Cancer Cells
Integrated Proteomic and Glycoproteomic Analyses of Prostate Cancer Cells Reveals Glycoprotein Alteration in Protein Abundance and Glycosylation
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080799 | MassIVE
UnknownComprehensive analysis of protein glycosylation by solid-phase extraction of N-linked glycans and glycosite-containing peptides.
Not available
S-EPMC4872599 | biostudies-literature
ProteomicsN-linked glycoproteome of human seminal plasma
N-linked glycosylation is an important type of post-translational modification. This modification plays important roles in many cellular functions including cell-cell and receptor-ligand interactions, immune response, apoptosis, and pathogenesis of many diseases. Seminal plasma is a mixture of secre...
ORGANISM(S): Homo sapiens (Human) 
2014-12-15 | PXD000959 | Pride
Lc-ms/ms Seminal plasma Glycoproteome Human 
UnknownGlycoFish: a database of zebrafish N-linked glycoproteins identified using SPEG method coupled with LC/MS.
Not available
S-EPMC3128545 | biostudies-literature
UnknownSite-Specific Profiling of Serum Glycoproteins Using N-Linked Glycan and Glycosite Analysis Revealing Atypical N-Glycosylation Sites on Albumin and α-1B-Glycoprotein.
Not available
S-EPMC6467210 | biostudies-literature
UnknownN-linked glycosylation enzymes in the diatom Thalassiosira oceanica exhibit a diel cycle in transcript abundance and favor for NXT-type sites.
Not available
S-EPMC7864949 | biostudies-literature
ProteomicsN-Linked Glycoprotein Profiles of Human Breast Normal/Benign Cell Lines
Secreted proteins and transmembrane proteins with extracellular domains are frequently glycosylated; this group of proteins includes those that participate in the various intercellular junctions and signaling pathways of an epithelium. In this study we characterized the differences in glycoprotein ...
ORGANISM(S): Homo sapiens (Human) 
2017-03-23 | PXD005339 | Pride
Human Breast Lc-msms Cell line N-linked Glycoprotein 
ProteomicsN-Linked Glycoprotein Profiles of Human Breast Luminal Malignant Cell Lines
Secreted proteins and transmembrane proteins with extracellular domains are frequently glycosylated; this group of proteins includes those that participate in the various intercellular junctions and signaling pathways of an epithelium. In this study we characterized the differences in glycoprotein ...
ORGANISM(S): Homo sapiens (Human) 
2017-03-22 | PXD005390 | Pride
Human Breast Lc-msms Cell line Luminal N-linked Glycoprotein 
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