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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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FAD-binding site of glutathione reductase

TL;DR: The FAD-binding site in dimeric glutathione reductase has been elucidated by application of sequence and X-ray analyses in parallel and the conformation of FAD is compared with those of other protein-bound nucleotides.
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Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase.

TL;DR: The binding of the substrate NADPH as well as a number of fragments and derivatives of NADPH to glutathione reductase from human erythrocytes has been investigated by using X-ray crystallography, showing differential binding between the adenine end and the nicotinamide end of the molecule.
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Prion disease susceptibility is affected by β-structure folding propensity and local side-chain interactions in PrP

TL;DR: Using a novel approach to quantify conformational states of PrP by circular dichroism (CD), it is found that prion susceptibility tracks with the intrinsic propensity of mammalian PrP to convert from the native, α-helical state to a cytotoxic β-structured state, which exists in a monomer–octamer equilibrium.
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A structural basis for Mg2+ homeostasis and the CorA translocation cycle.

TL;DR: Ten metal sites identified within the cytoplasmic funnel domain are linked to long extensions of the pore helices and regulate the transport status of CorA, and characterized this region as an intrinsic divalent cation sensor and provide evidence that it functions as a Mg2+‐specific homeostatic molecular switch.
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Data publication with the structural biology data grid supports live analysis.

Peter A. Meyer, +73 more
TL;DR: A diffraction data publication and dissemination system, Structural Biology Data Grid (SBDG), to preserve primary experimental data sets that support scientific publications and demonstrates that the information archived by SBDG is sufficient to reprocess data to statistics that meet or exceed the quality of the original published structures.