[1] Morré, D.J. (1998) NADH Oxidase: A Multifunctional Ectoproteins of the Eukaryotic Cell Surface. In: Asard, H., Bérczi, A. and Caubergs, R., Eds., Plasma Membrane Redox Systems and Their Role in Biological Stress and Disease, Kluwer Academic Publishers, Dordrecht, 121-156.
http://dx.doi.org/10.1007/978-94-017-2695-5_5
[2] Morré, D.J. and Morré, D.M. (2003) Cell Surface NADH Oxidases (ECTO-NOX Proteins) with Roles in Cancer, Cellular Time-Keeping, Growth, Aging and Neurodegenerative Disease. Free Radical Research, 37, 795-808.
http://dx.doi.org/10.1080/1071576031000083107
[3] Morré, D.J. and Morré, D.M. (2013) ECTO-NOX Proteins. Springer, New York, 507 p.
http://dx.doi.org/10.1007/978-1-4614-3958-5
[4] Jiang, Z., Gorenstein, N.M., Morré, D.M. and Morré, D.J. (2008) Molecular Cloning and Characterization of a Candidate Human Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase. Biochemistry, 47, 14028-14038.
http://dx.doi.org/10.1021/bi801073p
[5] Chueh, P.-J., Morré, D.J., Wilkinson, F.E., Gibson, J. and Morré, D.M. (l997) A 33.5 kDa Heat- and Protease-Resistant NADH Oxidase Inhibited by Capsaicin from Sera of Cancer Patients. Archives of Biochemistry and Biophysics, 342, 38-47.
http://dx.doi.org/10.1006/abbi.1997.9992
[6] Chueh, P.-J., Kim, C., Cho, N., Morré, D.M. and Morré, D.J. (2002) Molecular Cloning and Characterization of a Tumor-Associated, Growth-Related and Time-Keeping Hydro-quinone (NADH) Oxidase (NOX) of the HeLa Cell Surface. Biochemistry, 41, 3732-3741.
http://dx.doi.org/10.1021/bi012041t
[7] Morré, D.J., Chueh, P.-J. and Morré, D.M. (1995) Capsaicin Inhibits Preferentially the NADH Oxidase and Growth of Transformed Cells in Culture. Proceedings of the National Academy of Sciences USA, 92, 1831-1835.
http://dx.doi.org/10.1073/pnas.92.6.1831
[8] Morré, D.J., Sun, E., Geilen, C., Wu, L.-Y., De Cabo, R., Krasagakis, K., Orfanos, C.E. and Morré, D.M. (1996) Capsaicin Inhibits Plasma Membrane NADH Oxidase and Growth of Human and Mouse Melanoma Lines. European Journal of Cancer, 32A, 1995-2003.
http://dx.doi.org/10.1016/0959-8049(96)00234-1
[9] Morré, D.J., Wu, L.-Y. and Morré, D.M. (1995) The Antitumor Sulfonylurea N-(4-methylphenylsulfonyl)-N(-(chlorophenyl)urea (LY181984) Inhibits NADH Oxidase Activity of HeLa Plasma Membranes. Biochimica et Biophysica Acta, 1240, 11-17.
http://dx.doi.org/10.1016/0005-2736(95)00164-7
[10] Morré, D.J., Wilkinson, F.E., Kim, C., Cho, N., Lawrence, J., Morré, D.M. and McClure, D. (l996) Antitumor Sulfonylurea-Inhibited NADH Oxidase of Cultured HeLa Cells Shed into Media. Biochimica et Biophysica Acta, 1280, 197- 206.
http://dx.doi.org/10.1016/0005-2736(95)00290-1
[11] Morré, D.J., Chueh, P.-J., Yagiz, K., Balicki, A., Kim, C. and Morré, D.M. (2007) ECTO-NOX Target for the Anticancer Isoflavene Phenoxodiol. Oncology Research, 16, 299-312.
[12] Morré, D.J., Grieco, P.A. and Morré, D.M. (1998) Mode of Action of the Anticancer Quas-sinoids-Inhibition of the Plasma Membrane NADH Oxidase. Life Science, 63, 595-604.
http://dx.doi.org/10.1016/S0024-3205(98)00310-5
[13] Morré, D.J. and Greico, P.A. (1999) Glaucarubolone and Simalikalactone D, Respectively, Preferentially Inhibit Auxin-Induced and Constitutive Components of Plant Cell Enlargement and the Plasma Membrane NADH Oxidase. International Journal of Plant Sciences, 160, 291-297.
http://dx.doi.org/10.1086/314133
[14] Wilkinson, F.E., Kim, C., Cho, N., Chueh, P.-J., Leslie, S., Mo-ya-Camarena, S., Wu, L.-Y., Morré, D.M. and Morré, D.J. (l996) Isolation and Identification of a Protein with Capsaicin-Inhibited NADH Oxidase Activity from Culture Media Conditioned by Growth of HeLa Cells. Archives of Bio-chemistry and Biophysics, 336, 275-282.
http://dx.doi.org/10.1006/abbi.1996.0558
[15] Sedlak, D., Morré, D.M. and Morré, D.J. (2001) A Drug-Unresponsive and Protease-Resistant CNOX Protein from Human Sera. Archives of Biochemistry and Biophysics, 386, 106-116.
http://dx.doi.org/10.1006/abbi.2000.2180
[16] Morré, D.M. and Morré, D.J. (2003) Specificity of Coenzyme Q Inhibition of an Aging-Related Cell Surface NADH Oxidase (ECTO-NOX) That Generates Superoxide. BioFactors, 18, 33-43.
http://dx.doi.org/10.1002/biof.5520180205
[17] Dick, S., Phung, C., Morré, D.M. and Morré, D.J. (2013) Molecular Cloning and Characterization of an ECTO-NOX3 (ENOX3) of Saccharomyces cerevisiae. Advances in Biological Chemistry, 3, 505-511.
http://dx.doi.org/10.4236/abc.2013.35055
[18] Morré, D.M., Guo, F. and Morré, D.J. (2003) An Aging-Related Cell Surface NADH Oxidase (arNOX) Generates Superoxide and Is Inhibited by Coenzyme Q. Molecular and Cellular Biochemistry, 254, 101-109.
http://dx.doi.org/10.1023/A:1027301405614
[19] Pogue, R., Morré, D.M. and Morré, D.J. (2000) CHO Cell Enlargement Oscillates with a Temperature-Compensated Period of 24 Minutes. Biochimica et Biophysica Acta, 1498, 44-51.
http://dx.doi.org/10.1016/S0167-4889(00)00076-8
[20] Morré, D.J., Pogue, R. and Morré, D.M. (2001) Soybean Cell Enlargement Oscillates with a Temperature-Compensated Period Length of ca. 24 Min. In Vitro Cellular & Devel-opmental Biology-Plant, 37, 19-23.
http://dx.doi.org/10.1007/s11627-001-0004-3
[21] Morré, D.J., Ternes, P. and Morré, D.M. (2002) Cell Enlargement of Plant Tissue Explants Oscillates with a Temperature-Compensated Period Length of ca. 24 Min. In Vitro Cellular & Developmental Biology-Plant, 38, 18-28.
http://dx.doi.org/10.1079/IVP2001249
[22] Morré, D.J., Brightman, A.O., Hidalgo, A. and Navas, P. (1995) Selective Inhibition of Auxin-Stimulated NADH Oxidase Activity and Elongation Growth of Soybean Hypocotyls by Thiol Reagents. Plant Physiology, 107, 1285-1291.
[23] Kishi, T., Morré, D.M. and Morré, D.J. (1999) The Plasma Membrane NADH Oxidase of HeLa Cells Has Hydroquinone Oxidase Activity. Biochimica et Biophysica Acta, 1412, 66-77.
http://dx.doi.org/10.1016/S0005-2728(99)00049-3
[24] Morré, D.J., De Cabo, R., Jacobs, E. and Morré, D.M. (1995) Auxin-Modulated Protein Disulfide-Thiol Interchange Activity from Soybean Plasma Membranes. Plant Physiology, 109, 573-578.
[25] Morré, D.J., Gomez-Rey, M.L., Schramke, C., Em, O., Lawler, J., Hobeck, J. and Morré, D.M. (1999) Use of Dipyridyl-Dithio Substrates to Measure Directly the Protein Disulfide-Thiol Interchange Activity of the Auxin Stimulated NADH: Protein Disulfide Reductase (NADH Oxidase) of Soybean Plasma Membranes. Molecular and Cellular Biochemistry, 200, 7-13.
http://dx.doi.org/10.1023/A:1006916116297
[26] Morré, D.J., Chueh, P.-J., Pletcher, J., Tang, X.Y., Wu, L.-Y. and Morré, D.M. (2002) Biochemical Basis for the Biological Clock. Biochemistry, 41, 11941-11945.
http://dx.doi.org/10.1021/bi020392h
[27] Chueh, P.-J., Morré, D.M. and Morré, D.J. (2002) A Site-Directed Mutagenesis Analysis of tNOX Functional Domains. Biochimica et Biophysica Acta, 1594, 74-83.
http://dx.doi.org/10.1016/S0167-4838(01)00286-2
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http://dx.doi.org/10.1093/nar/25.17.3389
[29] Dick, S.S., Ryuzoji, A., Morré, D.M. and Morré, D.J. (2013) Identification of the Constitutive Ultradian Oscillator of the Circadian Clock (ENOX1) in Saccharomyces cerevisiae. Advances in Biological Chemistry, 3, 320-328.
http://dx.doi.org/10.4236/abc.2013.33036
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[32] Brightman, A.O., Wang, J., Miu, R.K., Sun, I.L., Barr, R., Crane, F.L. and Morré, D.J. (1992) A Growth Factor- and Hormone-Stimulated NADH Oxidase from Rat Liver Plasma Membrane. Biochimica et Biophysica Acta, 1105, 109-117.
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[33] Morré, D.J. and Brightman, A.O. (1991) NADH Oxidase of Plasma Membranes. Journal of Bioenergetics and Biomembranes, 23, 469-489.
http://dx.doi.org/10.1007/BF00771015
[34] Brightman, A.O., Barr, R., Crane, F.L. and Morré, D.J. (1988) Aux-in-Stimulated NADH Oxidase Purified from Plasma Membrane of Soybean. Plant Physiology, 86, 1264-1269.
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http://dx.doi.org/10.1046/j.1365-313x.1998.00293.x
[36] Morré, D.J., Penel, C., Greppin, H. and Morré, D.M. (2002) The Plasma Membrane-Associated NADH Oxidase of Spinach Leaves Responds to Blue Light. Inter-national Journal of Plant Sciences, 613, 543-547.
http://dx.doi.org/10.1086/340543
[37] Kelker, M., Kim, C., Chueh, P.J., Guimont, R., Morré, D.M. and Morré, D.J. (2001) Cancer Isoform of a Tumor-As- sociated Cell Surface NADH Oxidase (tNOX) Has Properties of a Prion. Biochemistry, 40, 7351-7354.
http://dx.doi.org/10.1021/bi010596i
[38] Kim, C. and Morré, D.J. (2004) Prion Proteins and ECTO-NOX Proteins Exhibit Similar Oscillating Redox Activities. Biochemical and Biophysical Research Communications, 315, 1140-1146.
http://dx.doi.org/10.1016/j.bbrc.2004.02.007
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[42] del Castillo-Olivares, A., Yantiri, F., Chueh, P.-J., Wang, S., Sweeting, M., Sedlak, D., Morré, D.M., Burgess, J. and Morré, D.J. (1998) A Drug-Responsive and Protease-Resistant Peripheral NADH Oxidase Complex from the Surface of HeLa S Cells. Archives of Biochemistry and Biophysics, 358, 125-140.
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[43] Rangachari, V., Morré, B.D., Reed, D.K., Sonoda, L.K., Bridges, A.W., Conboy, E., Hartigan, D. and Rosenberry, T.L. (2007) Amyloid-(1-42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate. Biochemistry, 46, 12451-12462.
http://dx.doi.org/10.1021/bi701213s
[44] Orczyk, J., Morré, D.M. and Morré, D.J. (2005) Periodic Fluctuations in Oxygen Consumption Comparing HeLa (Cancer) and CHO (Non-Cancer) Cells and Response to External NAD(P)+/NAD(P)H. Molecular and Cellular Biochemistry, 273, 161-167.
http://dx.doi.org/10.1007/s11010-005-0326-2
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http://dx.doi.org/10.1089/ars.2000.2.2-231
[46] Hyun, D.-H., Hunt, N.D., Emerson, S.S., Hernandez, J.O., Mattson, M.P. and de Cabo, R. (2007) Up-Regulation of Plasma Membrane-Associated Redox Activities in Neuronal Cells Lacking Functional Mitochondria. Journal of Neurochemistry, 100, 1364-1374.
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