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James D. Young

Researcher at University of Alberta

Publications -  241
Citations -  16156

James D. Young is an academic researcher from University of Alberta. The author has contributed to research in topics: Nucleoside & Nucleoside transporter. The author has an hindex of 63, co-authored 240 publications receiving 15574 citations. Previous affiliations of James D. Young include Cornell University & Cross Cancer Institute.

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Nucleoside transport. Photoaffinity labelling of high-affinity nitrobenzylthioinosine binding sites in rat and guinea pig lung.

TL;DR: Exposure of site-bound [3H]nitrobenzylthioinosine to high intensity U.V. light resulted in the photoaffinity labelling of lung proteins with apparent molecular weights similar to that of the human erythrocyte nucleoside transporter (45,000-65,000).
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Nucleoside transport and metabolism in erythrocytes from the Yucatan miniature pig. Evidence that inosine functions as an in vivo energy substrate.

TL;DR: Inosine is a major physiological energy source of pig erythrocytes and cells 'protected' themselves against some of the consequences of deprivation of energy substrate by glycolyzing the ribose moiety of inosine produced during ATP catabolism.
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Residues 334 and 338 in Transmembrane Segment 8 of Human Equilibrative Nucleoside Transporter 1 Are Important Determinants of Inhibitor Sensitivity, Protein Folding, and Catalytic Turnover

TL;DR: A helical wheel projection of TM 8 predicted that Phe-334 and Asn-338 lie in close proximity to other highly conserved and/or hydrophilic residues, suggesting that they form part of a structurally important region that influences interactions with inhibitors, protein folding, and rates of conformational change during the transport cycle.
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Haemolysis of normal and glutathione-deficient sheep erythrocytes by selenite and tellurite

TL;DR: Selenite and tellurite-induced haemolysis therefore provides a simple method for detecting GSH-deficient cells and the lytic effect of selenite may explain some of the symptoms associated with selenium poisoning.
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Amino acid transport defect in glutathione-deficient sheep erythrocytes.

TL;DR: The tripeptide, reduced glutathione (GSH), is present in high concentration in mammalian red blood cells, where its major role is thought to be the protection of the cell against oxidative damage.