The O-GlcNAc Modification on Kinases
Author:
Affiliation:
1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States
Funder
U.S. Department of Health and Human Services
Harvard University
Alfred P. Sloan Foundation
Burroughs Wellcome Fund
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acschembio.9b01015
Reference125 articles.
1. Topography and polypeptide distribution of terminal N-acetylglucosamine residues on the surfaces of intact lymphocytes. Evidence for O-linked GlcNAc.
2. Nutrient Regulation of Signaling, Transcription, and Cell Physiology by O-GlcNAcylation
3. O-GlcNAc protein modification in plants: Evolution and function
4. Glycosylated DNA-Binding Proteins from Filamentous Fungus,Aspergillus oryzae: Modification withN-Acetylglucosamine Monosaccharide through anO-Glycosidic Linkage
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