Peter N. Lewis

Peter N. Lewis

Professor Emeritus

BSc, University of Calgary, 1968
PhD, Cornell University, 1972
Postdoc, Portsmouth Polytechnic, 1972-1974
Visiting Scientist, National University of Singapore, 2002
Visiting Scientist, Institute for Systems Biology, 2002
Associate Vice President, Research, Simcoe Hall, 2010 - 2016

Address Office: Medical Sciences Building, Room 5318
Toronto, ON M5S 1A8
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Office Phone 416-978-6759

Professor Lewis served as Associate Vice-President, Research and Innovation specializing in Global Research Partnerships from January 2010 through March 2016. He returned to his research activities in April 2016. An accomplished biochemist, Professor Lewis has been an academic leader, faculty member and researcher at U of T since 1974. Prior to joining the Office of the Vice-President, Research and Innovation, Professor Lewis served as Vice-Dean, Research and International Relations in the Faculty of Medicine for seven years. He served as Chair of the U of T Department of Biochemistry from 1991-2001. His research interests include neurodegeneration; the structure and function of chromosomes with specific reference to gene regulation; and protein folding.In 2018 along with Professor Angus McQuibban he launched a drug discovery startup Rosetta Therapeutics which is located in JLabs.

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ROCK inhibitors upregulate the neuroprotective Parkin-mediated mitophagy pathway
Natalia Moskal, Victoria Riccio, Mikhail Bashkurov, Rediet Taddese, Alessandro Datti, Peter N. Lewis & G. Angus McQuibban
Nature Communications volume 11, Article number: 88 (2020)   Read

Association with the Origin Recognition Complex suggests a novel role for histone acetyltransferase Hat1p/Hat2p.
Suter B, Pogoutse O, Guo X, Krogan NJ, Lewis P, Greenblatt JF, Rine J, Emili A.
BMC Biol. 2007 Sep 19;5(1):38

Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the SIR2 family of NAD-dependent protein deacetylases.
Khan, A. Lewis, P.N.
J Biol Chem. 2006 Apr 28;281:11702-1

Unstructured conformations are a substrate requirement for the Sir2 family of NAD-dependent protein deacetylases.
Khan, A. Lewis, P.N.
J Biol Chem. 2005. 280(43):36073-8