Sort   by:  
 Page size 
UnknownDevelopment of IsoTaG, a Chemical Glycoproteomics Technique for Profiling Intact N- and O-Glycopeptides from Whole Cell Proteomes.
Not available
S-EPMC5507588 | biostudies-literature
UnknownIsotope-targeted glycoproteomics (IsoTaG): a mass-independent platform for intact N- and O-glycopeptide discovery and analysis.
Not available
S-EPMC4599779 | biostudies-literature
ProteomicsCharacterization of sialylated N- and O-glycopeptides from complex proteomes on an Orbitrap Fusion Tribrid mass spectrometer by Isotope Targeted Glycoproteomics (IsoTaG). Application to azido and alkynyl sugars
Protein glycosylation is a post-translational modification (PTM) responsible for many aspects of proteomic diversity and biological regulation. Correlation of the intact glycoform to the protein attachment site is a critical step to assign functional roles to specific glycoproteins. Isotope targeted...
ORGANISM(S): Homo sapiens (Human) 
2017-02-22 | PXD004302 | Pride
Lc-ms/ms Tissue culture Glycoproteomics Metabolic labeling 
UnknownIsotope-targeted glycoproteomics (IsoTaG) analysis of sialylated N- and O-glycopeptides on an Orbitrap Fusion Tribrid using azido and alkynyl sugars.
Not available
S-EPMC5342897 | biostudies-literature
ProteomicsO-Acetylated chemical reporters of glycosylation can display metabolism-dependent background labeling of proteins but are generally reliable tools for the identification of glycoproteins
Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins. More recently, proteomics analyses have shown that per-O-acetylated...
ORGANISM(S): Homo sapiens (Human) 
2020-04-01 | PXD016217 | Pride
Ac42azman Isotag Ac44azgal O-glcnac modifications 
UnknownMapping and Quantification of Over 2000 O-linked Glycopeptides in Activated Human T Cells with Isotope-Targeted Glycoproteomics (Isotag).
Not available
S-EPMC5880114 | biostudies-literature
UnknownO-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
Not available
S-EPMC7198827 | biostudies-literature
ProteomicsAspartate residues far from the active site drive O-GlcNAc transferase substrate selection
Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection. Changing these residues to alanines alters substrate selectivity and unexpectedly increases rate...
ORGANISM(S): Homo sapiens (Human) 
2019-07-26 | PXD014731 | Pride
Glycoproteomics O-glcnac 
Proteomics4-deoxy-4-fluoro-GalNAz (4FGalNAz) is a metabolic chemical reporter of O-GlcNAc modifications, highlighting the notable substrate flexibility of O-GlcNAc transferase
Bioorthogonal chemistries have revolutionized many fields. For example, metabolic chemical reporters (MCRs) of glycosylation are analogs of monosaccharides that contain bioorthogonal functionality, like azides or alkynes. MCRs are metabolically incorporated into glycoproteins by living systems, and ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027333 | Pride
O-glcnac  tmt 
ProteomicsTruncation of the TPR domain of OGT alters substrate and glycosite selection
Nucleocytoplasmic O-linked N-acetylglucosamine (O-GlcNAc) is an essential post-translational modification that is installed to thousands of protein substrates by O-GlcNAc transferase (OGT). Substrate selection by OGT and its isoforms is primarily mediated by the tetratricopeptide repeat (TPR) domain...
ORGANISM(S): Homo sapiens (Human) 
2021-11-01 | PXD028141 | Pride
Ogt Glycoproteomics Tetratricopeptide repeats (tprs) O-glcnac 
Sort   by:  
 Page size