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ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-figure 5
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020032 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Figure 4
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020053 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Fig6
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020034 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination-Fig3
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020048 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsOptimization of O-GIG for O-glycopeptide Characterization with Sialic Acid Linkage Determination -Figure 2
O-glycoprotein analysis has been historically challenging due, in part, to a dearth of available enzymes active in release of O-glycans. Moreover, chemical releasing methods, such as β-elimination/Michael addition are not specific to O-glycan release and can also eliminate phosphoryl substitutions....
ORGANISM(S): Bos taurus (Bovine) 
2020-07-28 | PXD020039 | Pride
Mucin O-glycopeptide immobilization Operator Lactoferrin O-glycosylation Sialic acid 
ProteomicsSite-specific glycosylation patterns of SARS-CoV-2 spike derived from recombinant protein and viral WA1 and D614G strains
We have characterized the site-specific glycosylation patterns of the HEK293 recombinant spike RBD and S1 domains as well as the intact spike derived from whole virus produced in Vero cells.
ORGANISM(S): Homo sapiens (Human) Cercopithecus aethiops (Green monkey) (Grivet) 
2022-02-16 | PXD029218 | Pride
Wa1 and d614g Sars-cov-2 Glycosylation 
ProteomicsA Linkage- Specific Sialic Acid Labeling Strategy Reveals Different Site-Specific Glycosylation Patterns in SARS-CoV-2 Spike Protein Produced in CHO and HEK Cell Substrates
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus utilizes an extensively glycosylated spike protein that protrudes from the viral envelope to bind to angiotensin-converting enzyme-related carboxypeptidase (ACE2) as its primary receptor to mediate host-cell entry. Currently, the...
ORGANISM(S): Homo sapiens (Human) Cricetulus barabensis 
2022-02-17 | PXD027536 | Pride
Lc-msms Glycopeptide Recombinant sars-2 spike Sialic acids labeling 
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