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0026772314
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Stimulation of NADH oxidase activity from rat liver plasma membranes by growth factors and hormones is decreased or absent with hepatoma plasma membranes
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The hormone-responsive NADH oxidase of the plant plasma membrane has properties of a NADH: Protein disulfide reductase
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P.J. Chueh, D.M. Morré, C. Penel, T. DeHanhn and D.J. Morré, The hormone-responsive NADH oxidase of the plant plasma membrane has properties of a NADH: protein disulfide reductase, Journal Biological Chemistry 272 (1997), 11221-11227.
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Molecular cloning and characterization of a tumor-associated, growth-related, and time-keeping hydroquinone (NADH) oxidase (tNOX) of the HeLa cell surface
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A site-directed mutagenesis analysis of tNOX functional domains
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P.J. Chueh, D.M. Morré and D.J. Morré, A site-directed mutagenesis analysis of tNOX functional domains, Biochimica et Biophysica Acta 1594 (2002), 74-83.
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P.J. Chueh, L.-Y. Wu, D.M. Morré and D.J. Morré, tNOX is both necessary and sufficient as a cellular target for the anticancer actions of capsaicin and the green tea catechin (-)-epigallocatechin-3-gallate, BioFactors 20 (2004), 249-263.
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Benzo[b]thiophenesulphonamid 1,1-dioxide derivatives inhibits tNOX activity in a redox state-dependent manner
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NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients
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D.J. Morré, S. Caldwell, A. Mayorga, L.-Y. Wu and D.M. Morré, NADH oxidase activity from sera altered by capsaicin is widely distributed among cancer patients, Archives of Biochemistry Biophysics 342 (1997), 224-230.
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0030777179
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Is the drug-responsive NADH oxidase of the cancer cell plasma membrane a molecular target for adriamycin?
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Preferential inhibition by (-)-epigallocatechin-3-gallet of the cell surface NADH oxidase and growth of transformed cells in culture
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Biochemical basis for the biological clock
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