J
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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Journal ArticleDOI
Inward- and outward-facing homology modeling of human concentrative nucleoside transporter 3 (hCNT3) predicts an elevator-type transport mechanism.
Sylvia Y.M. Yao,James D. Young +1 more
TL;DR: 3D structural homology models of hCNT3 based upon inward-facing, intermediates and outward-facing crystal structures of the bacterial CNT Neisseria wadsworthii CNTNW validate the previously published PCMBS SCAM data, and confirm an elevator-type mechanism of membrane transport.
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Passive and carrier-mediated permeation of different nucleosides through the reconstituted nucleoside transporter
Chung Ming Tse,James D. Young +1 more
TL;DR: When reconstituted into proteoliposomes, the human erythrocyte nucleoside transporter catalysed nitrobenzylthioguanosine (NBTGR)-sensitive zero-trans influx of three different nucleosides at broadly similar rates (inosine, uridine greater than adenosine).
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Characterization of a novel variant of amino acid transport system asc in erythrocytes from Przewalski's horse (Equus przewalskii).
TL;DR: The novel high apparent affinity of the Przewalski's horse transporter for L-lysine provides additional key evidence of functional and possible structural similarities between asc and the classical Na(+)-dependent system ASC and between these systems and the Na( +)-independent dibasic amino acid transport system y+.
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Role of cysteine 416 in N-ethylmaleimide sensitivity of human equilibrative nucleoside transporter 1 (hENT1).
TL;DR: A cysteine-less version of hENT1 is created, and it displays wild-type uridine transport and NBMPR-binding characteristics when produced in the Xenopus oocyte heterologous expression system, indicating that endogenous Cysteine residues are not essential for hent1 function.