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Systematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells Click to copy article link Article link copied!
Glycosylation is one of the most important and common protein modifications, and it plays vital roles in regulating protein activities and many cellular events. Unlike modifications with a single defined moiety, such as phosphorylation and acetylation, protein glycosylation encompasses structurally diverse modification types, including N-glycosylation, mucin-type O-glycosylation, and O-GlcNAcylation.
A Chemoenzymatic Method To Systematically Quantify Core Fucosylation Stoichiometry of Glycoproteins and Reveal Its Roles in EMT and Embryonic Development
Analytical Chemistry Cite this: Anal. Chem. 2026, XXXX, XXX Click to copy citationCitation copied! . This publication is licensed under CC-BY 4.0 . You are free to share (copy and redistribute) this article in any medium or format and to adapt (remix, transform, and build upon) the material for any purpose, even commercially within the parameters below: Creative Commons (CC): This is a Creative Commons license. Attribution (BY): Credit must be given to the creator.
Comprehensive and Site-Specific Characterization of Protein N-Glycosylation in AD Samples Reveals Its Potential Roles in Protein Aggregation and Synaptic Dysfunction
Analytical Chemistry Cite this: Anal. Chem. 2025, XXXX, XXX Click to copy citationCitation copied! . This publication is licensed under CC-BY 4.0 . You are free to share (copy and redistribute) this article in any medium or format and to adapt (remix, transform, and build upon) the material for any purpose, even commercially within the parameters below: Creative Commons (CC): This is a Creative Commons license. Attribution (BY): Credit must be given to the creator.
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