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Walid A. Houry: Profile Photo

Walid A. Houry

Toronto

Position: Professor

Organization: University of Toronto

Dr. Walid A. Houry is Professor in the Department of Biochemistry and Department of Chemistry at the University of Toronto. Dr. Houry obtained his PhD from Cornell University and then did his postdoctoral training at the Sloan-Kettering Institute in New York City and at the Max-Planck-Institute for Biochemistry in Munich, Germany. He is interested in the general area of cellular stress responses and the role of molecular chaperones and proteases in these responses. His group is also interested in the development of novel anticancers, antibiotics, and antivirals by identifying compounds that target these chaperones and proteases and result in the dysregulation of protein homeostasis in the cell. He has been recognized with national and international awards including awards from the Tokyo Biochemical Research Foundation (2011), the National Research Foundation of South Africa (2015), the Sigma Xi Scientific Research Honor Society (2021), and OIC-COMSTECH Distinguished Scholar Program, Islamabad, Pakistan (2022). He is typically invited to present at several conferences per year. He is currently the President of the Canadian Society for Molecular Biosciences.

Areas of Expertise:

+ Protein quality control
+ Drug discovery
+ Protein biochemistry

Language(s):

+ English
+ Arabic


My Work

What I do:

My research is in the area of protein quality control. We study molecular chaperones and ATP-dependent proteases. I am also interested in contributing to University governance and to Scientific societies.

Ask me about:

Drug discovery (antibiotics, anticancers) Science in Canada Scientific publishing Scientific societies

Why me:

I have been actively involved in these areas.


About Me

Sector: Academia (Post Secondary)

English proficiency: Read, Write, Speak

Other Language(s): Arabic

Title: Professor

Pronouns: He/Him/His

Gender: Male

Demographic: West Asian


Recent Publications

Title Year
Tuning TCR complex recruitment to the T cell antigen coupler (TAC) enhances TAC-T cell function2025
Targeting protein homeostasis with small molecules as a strategy for the development of pan-coronavirus antiviral therapies2024
Structure-Based Design and Development of Phosphine Oxides as a Novel Chemotype for Antibiotics that Dysregulate Bacterial ClpP Proteases2024
Target-locked: A mechanism for disaggregase binding to aggregated proteins2024
Abstract 1205 The mitochondrial ClpP protease: from basic principles to drug discovery2024
DPCD is a regulator of R2TP in ciliogenesis initiation through Akt signaling2024
Second international symposium on the chaperone code, 20232024
Broad spectrum post-entry inhibitors of coronavirus replication: Cardiotonic steroids and monensin2023
On a path toward a broad-spectrum anti-viral: inhibition of HIV-1 and coronavirus replication by SR kinase inhibitor harmine2023
The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme2023
Unveiling the Role of Sorghum RPAP3 in the Function of R2TP Complex: Insights into Protein Assembly in Plants2023
Abstract 3843: Potent human ClpP protease agonists with anticancer properties bind the enzyme with improved structural complementarity and alter the mitochondrial N-terminome2023
Toward protein fingerprinting with a solid-state nanopore2023
Abstract 1267: The Role of Hsp90-R2TP in Ciliogenesis2023
Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8–9, 20222023
Potent ClpP agonists with anticancer properties bind with improved structural complementarity and alter the mitochondrial N-terminome2022
Characterization of TR‐107, a novel chemical activator of the human mitochondrial protease ClpP2022
Analysis of the Evolution of the MoxR ATPases2022
Assembly Principles of the Human R2TP Chaperone Complex Reveal the Presence of R2T and R2P Complexes2022
Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes2022
The Thiazole-5-Carboxamide GPS491 Inhibits HIV-1, Adenovirus, and Coronavirus Replication by Altering RNA Processing/Accumulation2021
Author Correction: Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex2021
Functional Cooperativity between the Trigger Factor Chaperone and the ClpXP Proteolytic Complex2021
Leishmania major RUVBL1 has a hexameric conformation in solution and, in the presence of RUVBL2, forms a heterodimer with ATPase activity2021
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex2021