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Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase.
- Published in:
- Nature Communications, 2017, v. 8, n. 1, p. 1, doi. 10.1038/s41467-017-00865-1
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Structure of human O-GlcNAc transferase and its complex with a peptide substrate.
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- Nature, 2011, v. 469, n. 7331, p. 564, doi. 10.1038/nature09638
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- Article
Frontispiece: Molecular Interrogation to Crack the Case of O‐GlcNAc.
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- Chemistry - A European Journal, 2020, v. 26, n. 53, p. 1, doi. 10.1002/chem.202085361
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- Article
Molecular Interrogation to Crack the Case of O‐GlcNAc.
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- Chemistry - A European Journal, 2020, v. 26, n. 53, p. 12086, doi. 10.1002/chem.202000155
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- Article
Chemical and Biochemical Strategies To Explore the Substrate Recognition of O‐GlcNAc‐Cycling Enzymes.
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- ChemBioChem, 2019, v. 20, n. 3, p. 312, doi. 10.1002/cbic.201800481
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- Article
The Emerging Roles of Protein Interactions with O-GlcNAc Cycling Enzymes in Cancer.
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- Cancers, 2022, v. 14, n. 20, p. 5135, doi. 10.3390/cancers14205135
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- Article
Structural snapshots of the reaction coordinate for O-GlcNAc transferase.
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- Nature Chemical Biology, 2012, v. 8, n. 12, p. 966, doi. 10.1038/nchembio.1109
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- Article
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase.
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- Nature Chemical Biology, 2012, v. 8, n. 1, p. 72, doi. 10.1038/nchembio.711
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- Article
Biosynthesis of the earthy odorant geosmin by a bifunctional Streptomyces coelicolor enzyme.
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- Nature Chemical Biology, 2007, v. 3, n. 11, p. 711, doi. 10.1038/nchembio.2007.29
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- Article