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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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Y-700 (1-(3-Cyano-4-(2,2-dimethylpropoxy)phenyl)-1H- pyrazole-4-carboxylic Acid): A Potent Xanthine Oxidoreductase Inhibitor with Hepatic Excretion

TL;DR: Y-700 was hardly excreted via the kidneys but was mainly cleared via the liver, suggesting that Y-700 will be a promising candidate for the treatment of hyperuricemia and other diseases in which XOR may be involved
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Computational design of high-affinity epitope scaffolds by backbone grafting of a linear epitope.

TL;DR: Backbone grafting of linear motifs is a general method to transplant functional motifs when backbone remodeling of the target scaffold is necessary and bound antibody 2F5 with 30- and 9-fold higher affinity than corresponding side-chain grafting designs.
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Mechanism of inhibition of xanthine oxidoreductase by allopurinol: crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol.

TL;DR: The crystal structure of reduced bovine milk xanthine oxidoreductase complexed with oxipurinol was determined and clear electron density was observed between the N2 nitrogen of oxipirinol and themolybdenum atom of the molybdopterin cofactor, indicating that oxipURinol coordinated directly to molyb denum.
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Activators of Cylindrical Proteases as Antimicrobials: Identification and Development of Small Molecule Activators of ClpP Protease

TL;DR: The ACP1 chemical structure was considered to have drug-like characteristics and was further optimized to give analogs with bactericidal activity, hence, the ACPs represent classes of compounds that can activate ClpP and that can be developed as potential novel antibiotics.