David Vocadlo

Professor

Simon Fraser University

Canada

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David Vocadlo is a Professor at Simon Fraser University in Canada. His research focuses on enzymatic activities related to glycosylation, particularly O-GlcNAc transferase and its implications in neurodegenerative diseases. Recent articles highlight his work on genetically encoded assay systems and innovative synthesis methods for enzyme inhibitors.

Articles (20)

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2025

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2025

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2025

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2025

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2025

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2024

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2023

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2023

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2023

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2023

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2023

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2023

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2023

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2023

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2022

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2022

Collaborators (10)

Paul Bernhardt

Professor

University of Queensland

AUSTRALIA

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Carme Rovira

Professor at University of Barcelona

University of Barcelona

SPAIN

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Carmen Ortiz Mellet

SPAIN

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Erivan Ramos-Junior

Assistant Professor

UNITED STATES

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Roberto Villaseñor

Lab Head

F Hoffmann-La Roche AG

SWITZERLAND

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Gideon Davies

Royal Society Ken Murray Research Professor

University of York

UNITED KINGDOM

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Zachary Armstrong

Assistant Professor

Leiden University

NETHERLANDS

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Verdon Taylor

Prof

University of Basel

SWITZERLAND

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Marco Maccarana

Ass. Professor/Researcher

Uppsala University

SWEDEN

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Richard Meek

University of Southampton

UNITED KINGDOM

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David Vocadlo

Research Interests

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About

Articles (20)

A Genetically Encoded Assay System to Quantify O‐GlcNAc Transferase (OGT) Activity in Live Cells

A Genetically Encoded Assay System to Quantify O‐GlcNAc Transferase (OGT) Activity in Live Cells

A gram-scale synthesis of β-L-carbafucose for engineering antibody glycans

A self-immolative Kdn-glycoside substrate enables high-throughput screening for inhibitors of Kdnases

A dual-functional substrate for quantitation of substrate levels and GCase activity in living cells

An Efficient and Accessible Hectogram-Scale Synthesis for the Selective O-GlcNAcase Inhibitor Thiamet-G

Synthesis of Uronic Acid 1‐Azasugars as Putative Inhibitors of α‐Iduronidase, β‐Glucuronidase and Heparanase**

HBP/O-GlcNAcylation Metabolic Axis Regulates Bone Resorption Outcome.

Potent De Novo Macrocyclic Peptides That Inhibit O‐GlcNAc Transferase through an Allosteric Mechanism

Potent De Novo Macrocyclic Peptides That Inhibit O‐GlcNAc Transferase through an Allosteric Mechanism

A Fixable Fluorescence‐Quenched Substrate for Quantitation of Lysosomal Glucocerebrosidase Activity in Both Live and Fixed Cells

A Fixable Fluorescence‐Quenched Substrate for Quantitation of Lysosomal Glucocerebrosidase Activity in Both Live and Fixed Cells

In Situ Imaging of O-Linked β-N-Acetylglucosamine Using On-Tissue Hydrolysis and MALDI Mass Spectrometry

Targeting neuronal lysosomal dysfunction caused by β-glucocerebrosidase deficiency with an enzyme-based brain shuttle construct

Human O-GlcNAcase Uses a Preactivated Boat-skew Substrate Conformation for Catalysis. Evidence from X-ray Crystallography and QM/MM Metadynamics

Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase

Strategies for quantifying the enzymatic activities of glycoside hydrolases within cells and in vivo

Understanding and exploiting the roles of O-GlcNAc in neurodegenerative diseases

The primary familial brain calcification-associated protein MYORG is an α-galactosidase with restricted substrate specificity.

sp<sup>2</sup>-Iminosugars targeting human lysosomal β-hexosaminidase as pharmacological chaperone candidates for late-onset Tay-Sachs disease.

Collaborators (10)

Paul Bernhardt

Carme Rovira

Carmen Ortiz Mellet

Erivan Ramos-Junior

Roberto Villaseñor

Gideon Davies

Zachary Armstrong

Verdon Taylor

Marco Maccarana

Richard Meek

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