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- W2891301157 abstract "Protein O-GlcNAcylation is a non-canonical glycosylation of nuclear, mitochondrial, and cytoplasmic proteins with the attachment of a single O-linked β-N-acetyl-glucosamine (O-GlcNAc) moiety. Advances in labeling and identifying O-GlcNAcylated proteins have helped improve the understanding of O-GlcNAcylation at levels that range from basic molecular biology to cell signaling and gene regulation to physiology and disease. This review describes these advances in chemistry involving chemical reporters and their bioorthogonal reactions utilized for detection and construction of O-GlcNAc proteomes in a molecular mechanistic view. This detailed view will help better understand the principles of the chemistries utilized for biology discovery and promote continued efforts in developing new molecular tools and new strategies to further explore protein O-GlcNAcylation." @default.
- W2891301157 created "2018-09-27" @default.
- W2891301157 creator A5022253992 @default.
- W2891301157 date "2018-09-20" @default.
- W2891301157 modified "2023-10-18" @default.
- W2891301157 title "Chemical Reporters and Their Bioorthogonal Reactions for Labeling Protein O-GlcNAcylation" @default.
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- W2891301157 doi "https://doi.org/10.3390/molecules23102411" @default.
- W2891301157 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6222402" @default.
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- W2891301157 hasPublicationYear "2018" @default.
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