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
Atomic structure of the actin:DNase I complex.
TL;DR: The atomic models of the complex between rabbit skeletal muscle actin and bovine pancreatic deoxyribonuclease I both in the ATP and ADP forms have been determined byo X-ray analysis at an effective resolution of 2.8 Å and 3 Å.
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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution : implications for the mechanism of GTP hydrolysis
Emil F. Pai,Ute Krengel,Gregory A. Petsko,Roger S. Goody,Wolfgang Kabsch,Alfred Wittinghofer +5 more
TL;DR: A mechanism for GTP hydrolysis involving mainly Gln61 and Glu63 as activating species for in‐line attack of water as well as a mechanism for rate enhancement by GAP is proposed.
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Structure of the guanine-nucleotide-binding domain of the ha-ras oncogene product p21 in the triphosphate conformation
TL;DR: The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1–166) complexed to the Guanosine triphosphate analogue guanosine-5′-(β, γ-imido)triphosphates (GppNp) has been determined at a resolution of 2.6 Å.
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Crystal structure of metarhodopsin II.
Hui-Woog Choe,Yong Ju Kim,Jung Hee Park,Takefumi Morizumi,Takefumi Morizumi,Emil F. Pai,Norbert Krauss,Klaus Peter Hofmann,Klaus Peter Hofmann,Patrick Scheerer,Oliver P. Ernst,Oliver P. Ernst +11 more
TL;DR: By comparison with early photoproducts, it is proposed how retinal translocation and rotation induce the gross conformational changes characteristic for Meta’II, and the structures can now serve as models for the large GPCR family.
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Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
TL;DR: The crystal structure of the dimeric bovine milk XDH is presented and the major changes that occur on the proteolytic transformation of XDH to the XO form are described, reflecting the switch of substrate specificity observed for the two forms of this enzyme.