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GenomicsFree glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast
Free glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast
PRJNA535512 | ENA
TranscriptomicsFree glycans derived from O-mannosylated glycoproteins suggest the presence of an O-glycoprotein degradation pathway in yeast
In eukaryotic cells, unconjugated oligosaccharides structurally related to N-glycans (FNGs) are generated either from misfolded N-glycoproteins destined for endoplasmic reticulum (ER)-associated degradation (ERAD), or from lipid-linked oligosaccharides, donor substrates for N-glycosylation of protei...
ORGANISM(S): Saccharomyces cerevisiae 
2019-07-24 | GSE130332 | GEO
ProteomicsTargeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein
Ebola virus glycoprotein is one of the most heavily O-glycosylated viral envelope glycoproteins. The glycoprotein possesses a large mucin-like domain responsible for the cytopathic effect on infected cells, yet its structure or potential role in early entry events is poorly defined. To understand th...
ORGANISM(S): Homo sapiens (Human) 
2024-04-29 | PXD036213 | Pride
Glycoproteomics O-glycosylation Virus Ebola 
ProteomicsLarge scale intact glycopeptide identification by Mascot database search
We present the adaptability of Mascot search engine for automated identification of intact glycopeptide mass spectra. The steps involved in adopting Mascot for intact glycopeptide analysis include: i) assigning unique one letter codes for monosaccharides, ii) linearizing glycan sequences and iii) pr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-07-02 | MSV000082567 | MassIVE
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 
UnknownEngineering orthogonal human O-linked glycoprotein biosynthesis in bacteria.
Not available
S-EPMC7857696 | biostudies-literature
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