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
Structure and Immunogenicity of a Peptide Vaccine, Including the Complete HIV-1 gp41 2F5 Epitope IMPLICATIONS FOR ANTIBODY RECOGNITION MECHANISM AND IMMUNOGEN DESIGN
Soraya Serrano,Aitziber Araujo,Beatriz Apellaniz,Steve Bryson,Steve Bryson,Pablo Carravilla,Igor de la Arada,Nerea Huarte,Edurne Rujas,Emil F. Pai,Emil F. Pai,José Luis R. Arrondo,Carmen Domene,Carmen Domene,María Angeles Jiménez,José L. Nieva +15 more
TL;DR: A proof-of-concept to support MPER-based peptides in combination with liposomes as stand-alone immunogens and suggest new approaches for structure-aided MPER vaccine development.
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N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins.
Braden Sweeting,Eric M. Brown,M. Qasim Khan,M. Qasim Khan,Avijit Chakrabartty,Avijit Chakrabartty,Emil F. Pai +6 more
TL;DR: It is demonstrated that the sequence of the β2−α2 helix-cap affects refolding to the β-state and subsequently, may influence susceptibility to prion disease.
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Substrate Distortion Contributes to the Catalysis of Orotidine 5'-Monophosphate Decarboxylase
Masahiro Fujihashi,Toyokazu Ishida,Shingo Kuroda,Lakshmi P. Kotra,Lakshmi P. Kotra,Emil F. Pai,Kunio Miki +6 more
TL;DR: These results are consistent with ODCase using both substrate distortion and transition-state stabilization, primarily exerted by K72, in its catalysis of the OMP decarboxylation reaction.
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Distinct conformation-mediated functions of an active site loop in the catalytic reactions of NAD-dependent D-lactate dehydrogenase and formate dehydrogenase.
Takeshi Shinoda,Kazuhito Arai,Mayu Shigematsu-Iida,Yoshirou Ishikura,Satoru Tanaka,Takashi Yamada,Matthew S. Kimber,Emil F. Pai,Shinya Fushinobu,Hayao Taguchi +9 more
TL;DR: The results indicate that the active site loops play different roles in the catalytic reactions of d-LDH and FDH, stabilization of substrate binding and promotion of hydrogen transfer, respectively, and that Asn97 and Glu141, which stabilize suitable loop conformations, are essential elements for proper loop functioning.
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Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607.
TL;DR: The flavoenzyme mercuric ion reductase from Bacillus sp.