Author

Bryan J. Fraser

University of TorontoORCID 0000-0001-6398-106XUnclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

C.H. ArrowsmithiD· 3 shared François BénardiD· 2 shared Gregg B. MoriniD· 2 shared Jackie Lac· 2 shared Olzhas Ilyassov· 2 shared Ryan P. Wilson· 2 shared Yanjun LiiD· 2 shared A.M. EdwardsiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiochemistry

C.H. ArrowsmithORCID

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3 papers

Recent·Most cited

BiochemistryJournal of Biological ChemistryPeer-reviewedAug 12, 2026

Hepatocyte growth factor activator inhibitor-2 rapidly inactivates airway-expressed human Type II Transmembrane Serine Proteases

Bryan J. Fraser, Ryan P. Wilson, Jackie Lac…·C.H. Arrowsmith

This study shows HAI-2 inactivates TTSPs only after zymogen activation, revealing a novel mechanism for regulating these proteases and suggesting therapeutic applications.

DOI 10.1016/j.jbc.2026.113440

humanproteomics

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BiochemistrybioRxivPreprintOct 3, 2025

Cathepsin K as a Key Protease in Processing of SARS-CoV-2 Spike Activation Sites and a Target of Dual-Inhibition

S. Yasin Tabatabaei Dakhili, Dipon Saha, Preety Panwar…·Dieter Brömme

This study identifies Cathepsin K as a key host protease for SARS-CoV-2 spike activation and shows it can be inhibited by existing drugs.

DOI 10.1101/2025.10.03.680348

humanexperimental assay

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BiochemistryNature CommunicationsPeer-reviewedMay 10, 2025

Structural basis of TMPRSS11D specificity and autocleavage activation

Bryan J. Fraser, Ryan P. Wilson, Sára Ferková…·C.H. Arrowsmith

The paper determines the structural basis of TMPRSS11D autocleavage activation and shows that nafamostat mesylate is cleaved by TMPRSS11D, reducing its efficacy as a protease inhibitor.

10 citations

humanstructural biology

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