Glyco-seek: ultrasensitive detection of protein-specific glycosylation by proximity ligation polymerase chain reaction
PV Robinson, C Tsai, AE de Groot… - Journal of the …, 2016 - ACS Publications
We report a non-destructive biochemical technique, termed “Glyco-seek”, for analysis of O-
GlcNAcylated proteins. Glyco-seek combines chemoenzymatic labeling, proximity ligation …
GlcNAcylated proteins. Glyco-seek combines chemoenzymatic labeling, proximity ligation …
Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor
the glycosylation stoichiometries of proteins obtained from cells. Here we describe a …
the glycosylation stoichiometries of proteins obtained from cells. Here we describe a …
Changes in Metabolic Chemical Reporter Structure Yield a Selective Probe of O-GlcNAc Modification
Metabolic chemical reporters (MCRs) of glycosylation are analogues of monosaccharides
that contain bioorthogonal functionalities and enable the direct visualization and …
that contain bioorthogonal functionalities and enable the direct visualization and …
Parallel Identification of O-GlcNAc-Modified Proteins from Cell Lysates
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins
from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated …
from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated …
WGA-based lectin affinity gel electrophoresis: A novel method for the detection of O-GlcNAc-modified proteins
Y Kubota, K Fujioka, M Takekawa - PLoS One, 2017 - journals.plos.org
Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc) occurs
selectively on serine and/or threonine residues of cytoplasmic and nuclear proteins, and …
selectively on serine and/or threonine residues of cytoplasmic and nuclear proteins, and …
Detection and Analysis of (O-linked β-N-Acetylglucosamine)-Modified Proteins
NE Zachara - The Nucleus: Volume 2: Chromatin, Transcription …, 2008 - Springer
Glycosylation is one of the most common and complex forms of posttranslational
modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have …
modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have …
Methods for the detection, study, and dynamic profiling of O-GlcNAc glycosylation
JW Thompson, ME Griffin, LC Hsieh-Wilson - Methods in enzymology, 2018 - Elsevier
The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine/threonine residues of
proteins is a ubiquitous posttranslational modification found in all multicellular organisms …
proteins is a ubiquitous posttranslational modification found in all multicellular organisms …
Visualization of O‐GlcNAc Glycosylation Stoichiometry and Dynamics Using Resolvable Poly(ethylene glycol) Mass Tags
PM Clark, JE Rexach… - Current protocols in …, 2013 - Wiley Online Library
Abstract O‐linked N‐acetylglucosamine (O‐GlcNAc) glycosylation is a dynamic protein
posttranslational modification with roles in processes such as transcription, cell cycle …
posttranslational modification with roles in processes such as transcription, cell cycle …
Analytical Methods for the Study of O-GlcNAc Glycoproteins and Glycopeptides
Over the past decade, numerous nuclear and cytosolic glycoproteins have been shown to
be modified by single N-acetylglucosamine (O-GlcNAc) residues attached to the side chain …
be modified by single N-acetylglucosamine (O-GlcNAc) residues attached to the side chain …
Gene expression analysis of glycosylation-related genes by real-time polymerase chain reaction
JJ García-Vallejo, SI Gringhuis, W van Dijk… - Glycobiology …, 2007 - Springer
Glycan molecules covalently linked to proteins or lipids control vital properties of cells, such
as signaling, adherence, and migration through the body. The biosynthesis of such glycans …
as signaling, adherence, and migration through the body. The biosynthesis of such glycans …