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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Nature (London), 2011-01, Vol.469 (7331), p.564-567

2011

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PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis

Nature cell biology, 2017-11, Vol.19 (11), p.1358

2017

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Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase

Nature communications, 2017-09, Vol.8 (1), p.666-5, Article 666

2017

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Biosynthesis of the earthy odorant geosmin by a bifunctional Streptomyces coelicolor enzyme

Nature chemical biology, 2007-11, Vol.3 (11), p.711-715

2007

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HCF-1 is cleaved in the active site of O-GlcNAc transferase

Science (American Association for the Advancement of Science), 2013-12, Vol.342 (6163), p.1235-1239

2013

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The Emerging Roles of Protein Interactions with O-GlcNAc Cycling Enzymes in Cancer

Cancers, 2022-10, Vol.14 (20), p.5135

2022

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Targeted covalent inhibition of O -GlcNAc transferase in cells

Chemical communications (Cambridge, England), 2019-10, Vol.55 (88), p.13291-13294

2019

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Isolation and Characterization of the Gene Associated with Geosmin Production in Cyanobacteria

Environmental science & technology, 2008-11, Vol.42 (21), p.8027-8032

2008

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Geosmin Biosynthesis. Streptomyces coelicolor Germacradienol/Germacrene D Synthase Converts Farnesyl Diphosphate to Geosmin

Journal of the American Chemical Society, 2006-06, Vol.128 (25), p.8128-8129

2006

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Geosmin Biosynthesis. Mechanism of the Fragmentation−Rearrangement in the Conversion of Germacradienol to Geosmin

Journal of the American Chemical Society, 2008-01, Vol.130 (2), p.428-429

2008

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Abstract 1977: Motif-dependent interactions with OGlcNAc transferase regulate substrate selection and cellular responses

The Journal of biological chemistry, 2023, Vol.299 (3), p.103754, Article 103754

2023

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Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode

Nature structural & molecular biology, 2017-04, Vol.24 (4), p.362

2017

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The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control

Current opinion in chemical biology, 2024-08, Vol.81, p.102476, Article 102476

2024

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Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms

Current opinion in structural biology, 2019-06, Vol.56, p.97-106

2019

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Identification of (8S,9S,10S)-8,10-Dimethyl-1-octalin, a Key Intermediate in the Biosynthesis of Geosmin in Bacteria

Journal of the American Chemical Society, 2008-01, Vol.130 (2), p.430-431

2008

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Molecular Interrogation to Crack the Case of O‐GlcNAc

Chemistry : a European journal, 2020-09, Vol.26 (53), p.12086-12100

2020

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Deciphering the Functions of Protein O‑GlcNAcylation with Chemistry

ACS chemical biology, 2017-02, Vol.12 (2), p.326-335

2017

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Editorial overview: Protein–carbohydrate complexes and glycosylation: A new age of discovery in the glycosciences

Current opinion in structural biology, 2021-06, Vol.68, p.iii-v

2021

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Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase

Nature chemical biology, 2023-11, Vol.19 (11), p.1423

2023

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Frontispiece: Molecular Interrogation to Crack the Case of O‐GlcNAc

Chemistry : a European journal, 2020-09, Vol.26 (53), p.n/a

2020

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Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe

International journal of biological macromolecules, 2021-02, Vol.169, p.51-59

2021

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A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase

Nature chemical biology, 2011-11, Vol.8 (1), p.72

2011

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A Small Molecule That Inhibits OGT Activity in Cells

ACS chemical biology, 2015-06, Vol.10 (6), p.1392-1397

2015

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Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase

Nature chemical biology, 2017-12, Vol.13 (12), p.1267

2017

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Distributive O‑GlcNAcylation on the Highly Repetitive C‑Terminal Domain of RNA Polymerase II

Biochemistry (Easton), 2016-02, Vol.55 (7), p.1149-1158

2016

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Structure of human O-GlcNAc transferase and its complex with a peptide substrate

PKM2 methylation by CARM1 activates aerobic glycolysis to promote tumorigenesis

Structural insights into the substrate binding adaptability and specificity of human O-GlcNAcase

Biosynthesis of the earthy odorant geosmin by a bifunctional Streptomyces coelicolor enzyme

HCF-1 is cleaved in the active site of O-GlcNAc transferase

The Emerging Roles of Protein Interactions with O-GlcNAc Cycling Enzymes in Cancer

Targeted covalent inhibition of O -GlcNAc transferase in cells

Isolation and Characterization of the Gene Associated with Geosmin Production in Cyanobacteria

Geosmin Biosynthesis. Streptomyces coelicolor Germacradienol/Germacrene D Synthase Converts Farnesyl Diphosphate to Geosmin

Geosmin Biosynthesis. Mechanism of the Fragmentation−Rearrangement in the Conversion of Germacradienol to Geosmin

Abstract 1977: Motif-dependent interactions with OGlcNAc transferase regulate substrate selection and cellular responses

Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode

The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control

Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms

Identification of (8S,9S,10S)-8,10-Dimethyl-1-octalin, a Key Intermediate in the Biosynthesis of Geosmin in Bacteria

Molecular Interrogation to Crack the Case of O‐GlcNAc

Deciphering the Functions of Protein O‑GlcNAcylation with Chemistry

Editorial overview: Protein–carbohydrate complexes and glycosylation: A new age of discovery in the glycosciences

Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase

Frontispiece: Molecular Interrogation to Crack the Case of O‐GlcNAc

Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe

A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase

A Small Molecule That Inhibits OGT Activity in Cells

Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase

Distributive O‑GlcNAcylation on the Highly Repetitive C‑Terminal Domain of RNA Polymerase II

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