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Roman Alexander Melnyk

Affiliations: 
2004 Hospital for Sick Children, Toronto, ON 
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"Roman Melnyk"
Bio:

Dr. Melnyk’s research focuses largely on bacterial toxins; on their role in disease, on their druggability, and on their potential as drug-delivery vectors. His doctoral studies at the University of Toronto (Supervisor: Dr. Charles Deber) focused on understanding how proteins and peptides interact with biological membranes. In his postdoctoral studies at Harvard Medical School (Supervisor: Dr. John Collier)
1993–1998: B.Sc. in Biochemistry, McMaster University (co-op)
1998–2004: PhD in Biochemistry, University of Toronto
2004–2006: Postdoctoral Fellow, Harvard Medical School
2006–2011: Senior Scientist, Merck Frosst Canada, Merck & Company

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Parents

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Charles Deber grad student 2004 Hospital for Sick Children
 (Design of soluble transmembrane peptides as mimics and inhibitors of membrane protein folding & function.)
R. John Collier post-doc 2004-2006 Harvard Medical School

Children

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Publications

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Lim S, Khoo R, Peh KM, et al. (2020) bioPROTACs as versatile modulators of intracellular therapeutic targets including proliferating cell nuclear antigen (PCNA). Proceedings of the National Academy of Sciences of the United States of America
Orrell KE, Tellgren-Roth Å, Di Bernardo M, et al. (2018) Direct detection of membrane-inserting fragments defines the translocation pores of a family of pathogenic toxins. Journal of Molecular Biology
Orrell KE, Zhang Z, Sugiman-Marangos SN, et al. (2017) Clostridium difficile toxins A and B: Receptors, pores, and translocation into cells. Critical Reviews in Biochemistry and Molecular Biology. 1-13
Chumbler NM, Rutherford SA, Zhang Z, et al. (2016) Crystal structure of Clostridium difficile toxin A. Nature Microbiology. 1: 15002
Chumbler NM, Rutherford SA, Zhang Z, et al. (2016) Crystal structure of Clostridium difficile toxin A. Nature Microbiology. 1
Zhang Z, Park M, Tam J, et al. (2014) Translocation domain mutations affecting cellular toxicity identify the Clostridium difficile toxin B pore. Proceedings of the National Academy of Sciences of the United States of America. 111: 3721-6
Lam V, Henault M, Khougaz K, et al. (2012) Resorufin butyrate as a soluble and monomeric high-throughput substrate for a triglyceride lipase. Journal of Biomolecular Screening. 17: 245-51
Tam J, Henault M, Li L, et al. (2011) An activity-based probe for high-throughput measurements of triacylglycerol lipases. Analytical Biochemistry. 414: 254-60
Wimalasena DS, Cramer JC, Janowiak BE, et al. (2007) Effect of 2-fluorohistidine labeling of the anthrax protective antigen on stability, pore formation, and translocation. Biochemistry. 46: 14928-36
Juris SJ, Melnyk RA, Bolcome RE, et al. (2007) Cross-linked forms of the isolated N-terminal domain of the lethal factor are potent inhibitors of anthrax toxin. Infection and Immunity. 75: 5052-8
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