Associated Papers
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms.
Hansen SB et al.
Nature Communications, 2025
OGA mutant aberrantly hydrolyzes O-GlcNAc modification from PDLIM7 to modulate p53 and cytoskeleton in promoting cancer cell malignancy.
Hu CW et al.
Proceedings of the National Academy of Sciences of the United States of America, 2024
Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase.
Blankenship CM et al.
Nature Chemical Biology, 2023
Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex.
Lu P et al.
Nature Communications, 2023
Human O-GlcNAcase Uses a Preactivated Boat-skew Substrate Conformation for Catalysis. Evidence from X-ray Crystallography and QM/MM Metadynamics.
Calvelo M et al.
Acs Catalysis, 2023
Cancer-derived mutation in the OGA stalk domain promotes cell malignancy through dysregulating PDLIM7 and p53.
Hu CW et al.
Research Square, 2023
A novel binding site on the cryptic intervening domain is a motif-dependent regulator of O-GlcNAc transferase.
Blankenship C et al.
Research Square, 2023
Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe.
Kositzke A et al.
International Journal of Biological Macromolecules, 2021
Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.
Joiner CM et al.
Current Opinion in Structural Biology, 2019
Structural studies of a surface-entropy reduction mutant of O-GlcNAcase.
Males A et al.
Acta Crystallographica. Section D, Structural Biology, 2019
Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase.
Hu CW et al.
Nature Chemical Biology, 2017
Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.
Li B et al.
Nature Communications, 2017
Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.
Li B et al.
Nature Structural & Molecular Biology, 2017
Human OGA binds substrates in a conserved peptide recognition groove.
Schimpl M et al.
The Biochemical Journal, 2010
Identification of a catalytic residue of Clostridium paraputrificum N-acetyl-beta-D-glucosaminidase Nag3A by site-directed mutagenesis.
Li H et al.
Bioscience, Biotechnology, and Biochemistry, 2006