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.
Papers
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Journal ArticleDOI
A point mutation in the Ch3 domain of human IgG3 inhibits antibody secretion without affecting antigen specificity.
Gary R. McLean,Marcela Torres,Brendon Trotter,Michela Noseda,Steve Bryson,Steve Bryson,Emil F. Pai,Emil F. Pai,John W. Schrader,Arturo Casadevall +9 more
TL;DR: The results indicate that correct IgG3 Ch3 domain folding is essential for secretion and effective function but does not affect specificity for antigen.
Patent
ODCase inhibitors for the treatment of malaria
TL;DR: In this paper, the authors present methods of treating or preventing malaria by administering an anti-malarial effective amount of 6-substituted uridine derivatives to a subject need thereof.
Book ChapterDOI
Three-dimensional structure and properties of wild-type and mutant H-ras-encoded p21.
Alfred Wittinghofer,Sybille M. Franken,Axel J. Scheidig,Hans Rensland,Alfred Lautwein,Emil F. Pai,Roger S. Goody +6 more
TL;DR: The structure of the guanine nucleotide-binding domain of H-Ras (or p21H-ras) in the triphosphate conformation was determined at very high resolution and a mechanism for the intrinsic GTP hydrolysis has been proposed.
Journal ArticleDOI
Mutational, structural, and kinetic studies of the ATP-binding site of Methanobacterium thermoautotrophicum nicotinamide mononucleotide adenylyltransferase.
TL;DR: Surprisingly, this H19A mutant displayed a novel and distinct mode of NAD+ binding when co-crystallized in the presence of NAD+, as well as His-16 and His-19, part of the HXGH active site motif and postulated to be of importance in catalysis.
Journal ArticleDOI
Structural diversity and plasticity associated with nucleotides targeting orotidine monophosphate decarboxylase.
TL;DR: This work investigated the kinetic properties of eight common and endogenous nucleotides with ODCases from three species: Methanobacterium thermoautotrophicum, Plasmodium falciparum, and Homo sapiens and found UMP and XMP exhibited higher affinities as compared to the other nucleotide tested.