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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
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
High-throughput intact glycopeptide analysis is crucial for elucidating the physiological and pathological status of the glycans attached to each glycoprotein. Mass spectrometry-based glycoproteomic methods are challenging because of the diversity and heterogeneity of glycan structures. Therefore, w...
ORGANISM(S): Homo Sapiens (human) 
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
Protein glycosylation is ubiquitous and plays critical roles in biology. However, study of O-linked glycoproteome (O-glycoproteome), a major type of protein glycosylation, has been severely impeded due to paucity of technology. We presented a chemoenzymatic strategy for extraction of site-specific O...
ORGANISM(S): Homo sapiens (Human) 
2022-02-28 | PXD007895 | Pride
Glycosylation represents a major post-translational modification of proteins that can influence their structure and function.Telesot immunoglobulin M (IgM) is an especially important product of the immune system because it is the main Abs in seum and plays a critical role against defense infection. ...
ORGANISM(S): Ctenopharyngodon idella 
2018-11-29 | PXD010308 | Pride
To understand biological and pathological functions of protein glycosylations, it is crucial to uncover glycan heterogeneities, which depend on the type and status of cells, for each glycosite of single glycoprotein. For evaluating the glycan heterogeneities at macro-, micro-, and meta-levels, a rel...
ORGANISM(S): Mus Musculus (mouse) 
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
This study is aimed to comprehensively and globally characterize seminal plasma glycoproteins in a site-specific manner with information of N-glycosites and corresponding glycan structures, as well as glycan isomers using mass spectrometry. Furthermore, the function of specific glycan structures is ...
ORGANISM(S): Homo sapiens (Human) 
2023-03-04 | PXD030804 | Pride
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
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