Small Molecule-Activated O-GlcNAcase for Spatiotemporal Removal of O-GlcNAc in Live Cells
Author:
Affiliation:
1. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States
2. Institute of Chemical Biology, Shenzhen Bay Laboratory, Shenzhen 518107, China
Funder
National Cancer Institute
Harvard University
Shenzhen Bay Laboratory
Alfred P. Sloan Foundation
Camille and Henry Dreyfus Foundation
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acschembio.2c00894
Reference51 articles.
1. Protein O-GlcNAcylation: emerging mechanisms and functions
2. Spatial and temporal proteomics reveals the distinct distributions and dynamics of O-GlcNAcylated proteins
3. Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors
4. O-GlcNAcase Expression is Sensitive to Changes in O-GlcNAc Homeostasis
5. A Conserved Splicing Silencer Dynamically Regulates O-GlcNAc Transferase Intron Retention and O-GlcNAc Homeostasis
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