Sort   by:  
 Page size 
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
UnknownRedox-Controlled Site-Specific α2-6-Sialylation.
Not available
S-EPMC7239639 | biostudies-literature
ProteomicsErbB2 Site-Specific α2,6-Sialylation Regulates Gastric Cancer Cell Sensitivity to Trastuzumab
The clinical performance of trastuzumab in the treatment of ErbB2-positive gastric cancer is severely hampered by the emergence of molecular resistance. The glycosylation landscape of ErbB2’s extracellular domain, and the molecular mechanisms through which it tunes gastric cell malignancy, including...
ORGANISM(S): Homo sapiens (Human) 
2021-05-11 | PXD017609 | Pride
Glycosylation Glycoproteomics Trastuzumab Gastric cancer 
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
ProteomicsIdentifying Sialylation Linkages at the Glycopeptide Level by Glycosyltransferase Labeling Assisted Mass Spectrometry
Precise assignment of sialylation linkages at the glycopeptide level is of importance in bottom-up glycoproteomics, and is also an indispensable step to understand the function of glycoproteins in pathogen-host interactions and cancer progression. Even though some efforts have been dedicated to the ...
ORGANISM(S): Homo sapiens (Human) 
2020-04-21 | PXD016151 | Pride
Site-specific sialylation Glycopeptides Human serum Glycosyltransferase labeling 
ProteomicsSynaptic transmission induces site specific changes in sialylation on N-linked glycoproteins in nerve terminals
Synaptic transmission is an ultra-fast process that aims at transducing a signal from one neuron to another neuron or cell by the release of neurotransmitters. This process requires rapid response which can be transmitted through fast molecular switches such as post-translational modifications of pr...
ORGANISM(S): Rattus norvegicus (Rat) 
2020-06-12 | PXD016230 | Pride
Synaptic transmission Sialic acid N-glycosylation Rat Synaptosomes Lc-ms/ms 
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
ProteomicsSite-specific N-glycan Analysis of Neonatal Mouse Hearts
The heart of a newborn mouse has an exceptional capacity to regenerate from myocardial injury but lose it after a week of life, which has been utilized as a valuable model to explore the cues for heart regeneration. More and more researches indicated that glycoprotein played an important role in car...
ORGANISM(S): Mus musculus (Mouse) 
2020-05-26 | PXD017139 | Pride
Neonatal mouse heart Intact glycopeptides Site-specific glycosylation Glycoproteomics Lc-ms/ms 
UnknownDepolarization-dependent Induction of Site-specific Changes in Sialylation on N-linked Glycoproteins in Rat Nerve Terminals.
Not available
S-EPMC8143646 | biostudies-literature
ProteomicsSite-specific N-glycoproteomics of aging mouse uterus tissues for benchmarking the StrucGAP analysis platform
This project presents the site-specific N-glycoproteomics dataset of aging mouse uterus tissues used to demonstrate and validate StrucGAP, a modular and scalable downstream analysis platform for glycoproteomics. Uterine samples were collected from 2- and 12-month-old C57BL/6 female mice (n = 15 per ...
ORGANISM(S): Mus Musculus 
2025-04-23 | PXD063260 |
Sort   by:  
 Page size