E
Emil F. Pai
Researcher at University of Toronto
Publications - 203
Citations - 15866
Emil F. Pai is an academic researcher from University of Toronto. The author has contributed to research in topics: Binding site & Xanthine dehydrogenase. The author has an hindex of 58, co-authored 203 publications receiving 14840 citations. Previous affiliations of Emil F. Pai include Toronto General Hospital & University of Georgia.
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Journal ArticleDOI
Structural determinants for the inhibitory ligands of orotidine-5'-monophosphate decarboxylase.
Maria Elena Meza-Aviña,Lianhu Wei,Yan Liu,Ewa Poduch,Angelica M. Bello,Ram Kumar Mishra,Emil F. Pai,Emil F. Pai,Lakshmi P. Kotra +8 more
TL;DR: A comprehensive study of potent, structurally diverse ligands of ODCase and an empirical model for the ligand structure for rational modifications in new drug design and potentially new lead structures are proposed.
Journal ArticleDOI
Development of Antibiotics That Dysregulate the Neisserial ClpP Protease.
Gursonika Binepal,Mark F. Mabanglo,Jordan D. Goodreid,Elisa Leung,Marim M Barghash,Keith S. Wong,Funing Lin,Michele Cossette,Jazmin Bansagi,Boxi Song,Vitor Serrão,Emil F. Pai,Emil F. Pai,Robert A. Batey,Scott D. Gray-Owen,Walid A. Houry +15 more
TL;DR: Based on the ACP-ClpP cocrystal structure solved here, it is demonstrated that ACPs could be designed to be species specific, validates the feasibility of drug-based targeting of ClpP in Gram-negative bacteria.
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Time-resolved crystallography on H-ras p21
Axel J. Scheidig,Emil F. Pai,Ilme Schlichting,John E. T. Corrie,Gordon P. Reid,Alfred Wittinghofer,Roger S. Goody,A. Liljas,Keith Moffat +8 more
TL;DR: In this paper, the results obtained to date on a project aimed at characterizing the changes occurring in the protein product (p21) of the H-ras proto-oncogene during and as a result of hydrolysis of GTP at its active site are described.
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The prion protein is embedded in a molecular environment that modulates transforming growth factor β and integrin signaling.
Farinaz Ghodrati,Mohadeseh Mehrabian,Declan Williams,Ondrej Halgas,Matthew E. C. Bourkas,Joel C. Watts,Emil F. Pai,Gerold Schmitt-Ulms +7 more
TL;DR: The interactome of the prion protein (PrP), best known for its central role in prion diseases, is interrogated in four mouse cell lines and a shared association of the majority of PrP candidate interactors with cellular events at the intersection of transforming growth factor β and integrin signaling is revealed.
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Conformational determinants of phosphotyrosine peptides complexed with the Src SH2 domain.
TL;DR: The results suggest that the structural basis for phopsphopeptide- Src SH2 interactions is more complex than the “two-pronged plug two-hole socket” model, and suggest a model where all three residues C-terminal to the phosphotyrosine determine the conformation of the bound phosphopeptides.