B
Bryan Mackenzie
Researcher at University of Cincinnati Academic Health Center
Publications - 69
Citations - 8747
Bryan Mackenzie is an academic researcher from University of Cincinnati Academic Health Center. The author has contributed to research in topics: DMT1 & Ferroportin. The author has an hindex of 32, co-authored 64 publications receiving 8124 citations. Previous affiliations of Bryan Mackenzie include University of Dundee & Georgia Regents University.
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Journal ArticleDOI
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Hiromi Gunshin,Bryan Mackenzie,Urs V. Berger,Yoshimi Gunshin,Michael F. Romero,Walter F. Boron,Stephan Nussberger,John L. Gollan,Matthias A. Hediger +8 more
TL;DR: A new metal-ion transporter in the rat, DCT1, which has an unusually broad substrate range that includes Fe2+, Zn2+, Mn2+, Co2+, Cd2+, Cu2+, Ni2+ and Pb2+.
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A family of mammalian Na + -dependent L -ascorbic acid transporters
Hiroyasu Tsukaguchi,Taro Tokui,Bryan Mackenzie,Urs V. Berger,Xing-Zhen Chen,Yangxi Wang,Richard F. Brubaker,Matthias A. Hediger,Matthias A. Hediger +8 more
TL;DR: It is found that SVCT1 and SVCT2 each mediate concentrative, high-affinity L-ascorbic acid transport that is stereospecific and is driven by the Na+ electrochemical gradient.
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Sodium-coupled neutral amino acid (System N/A) transporters of the SLC38 gene family
TL;DR: The sodium-coupled neutral amino acid transporters (SNAT) of the SLC38 gene family resemble the classically-described System A and System N transport activities in terms of their functional properties and patterns of regulation.
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Molecular Characterization of a Broad Selectivity Neutral Solute Channel
Hiroyasu Tsukaguchi,Chairat Shayakul,Urs V. Berger,Bryan Mackenzie,Sreenivas Devidas,William B. Guggino,Alfred N. Van Hoek,Matthias A. Hediger +7 more
TL;DR: The expression cloning of a liver cDNA encoding a unique promiscuous solute channel (AQP9) that confers high permeability for both solute and water is reported, defining a new evolutionary branch of the major intrinsic protein family of aquaporin proteins and describing a previously unknown mechanism by which a large variety of solutes and water can pass through a single pore.
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ZIP8 Is an Iron and Zinc Transporter Whose Cell-surface Expression Is Up-regulated by Cellular Iron Loading
Chia-Yu Wang,Supak Jenkitkasemwong,Stephanie Duarte,Brian K. Sparkman,Ali Shawki,Bryan Mackenzie,Mitchell D. Knutson +6 more
TL;DR: Analysis of 20 different human tissues revealed abundant ZIP8 expression in lung and placenta and showed that its expression profile differs markedly from ZIP14, suggesting nonredundant functions, and identifies ZIP8 as an iron transport protein that may function in iron metabolism.