Genetically Encoded Fluorescent Sensors for Intracellular NADH Detection

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works

Mitochondria, Oxidants, and Aging

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The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation

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The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver

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A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein

Nakai, J., Ohkura, M., & Imoto, K. (2001) · Nature Biotechnology · doi:10.1038/84397 · Cited by 1,619 · see citing works

Genetically encoded fluorescent indicator for intracellular hydrogen peroxide

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Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors

Rutter, J., Reick, M., Wu, L. C., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1060698 · Cited by 1,059 · see citing works

Expanded dynamic range of fluorescent indicators for Ca ²⁺ by circularly permuted yellow fluorescent proteins

Nagai, T., Yamada, S., Tominaga, T., Ichikawa, M., & Miyawaki, A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400417101 · Cited by 1,030 · see citing works

In vivo multiphoton microscopy of NADH and FAD redox states, fluorescence lifetimes, and cellular morphology in precancerous epithelia

Skala, M. C., Riching, K. M., Gendron‐Fitzpatrick, A., Eickhoff, J. C., Eliceiri, K. W., White, J. G., & Ramanujam, N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708425104 · Cited by 1,004 · see citing works

Nutrient-Sensitive Mitochondrial NAD+ Levels Dictate Cell Survival

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Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis

Kasischke, K. A., Vishwasrao, H. D., Fisher, P. J., Zipfel, W. R., & Webb, W. W. (2004) · Science · doi:10.1126/science.1096485 · Cited by 742 · see citing works

Superoxide flashes in single mitochondria

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DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite.

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Regulation of Corepressor Function by Nuclear NADH

Zhang, Q., Piston, D. W., & Goodman, R. H. (2002) · Science · doi:10.1126/science.1069300 · Cited by 620 · see citing works

Mitochondrial remodeling in adipose tissue associated with obesity and treatment with rosiglitazone.

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Role of NADH Shuttle System in Glucose-Induced Activation of Mitochondrial Metabolism and Insulin Secretion

Eto, K., Tsubamoto, Y., Terauchi, Y., 杉山, 拓., Kishimoto, T. E., Takahashi, N. K., Yamauchi, N., Kubota, N., Murayama, S., Aizawa, T., et al. (1999) · Science · doi:10.1126/science.283.5404.981 · Cited by 491 · see citing works

A genetically encoded fluorescent reporter of ATP:ADP ratio

Berg, J., Hung, Y. P., & Yellen, G. (2009) · Nature Methods · doi:10.1038/nmeth.1288 · Cited by 481 · see citing works

Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease

Lin, S.-J., & Guarente, L. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00006-1 · Cited by 478 · see citing works

Imaging Intracellular pH in Live Cells with a Genetically Encoded Red Fluorescent Protein Sensor

Tantama, M., Hung, Y. P., & Yellen, G. (2011) · Journal of the American Chemical Society · doi:10.1021/ja202902d · Cited by 411 · see citing works

Mitochondrial function in vivo evaluated by NADH fluorescence: from animal models to human studies

Mayevsky, A., & Rogatsky, G. G. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00249.2006 · Cited by 381 · see citing works

Increasing NADH oxidation reduces overflow metabolism in Saccharomyces cerevisiae

Vemuri, G. N., Eiteman, M. A., McEwen, J. E., Lisbeth Olsson, A., & Nielsen, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607469104 · Cited by 373 · see citing works

Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools

McKenna, M. C., Waagepetersen, H. S., Schousboe, A., & Sonnewald, U. (2006) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.10.011 · Cited by 328 · see citing works

NAD+ and Vitamin B3: From Metabolism to Therapies

Sauve, A. A. (2007) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.120758 · Cited by 303 · see citing works

Conformational Dependence of Intracellular NADH on Metabolic State Revealed by Associated Fluorescence Anisotropy*♦

Vishwasrao, H. D., Heikal, A. A., Kasischke, K. A., & Webb, W. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502475200 · Cited by 297 · see citing works

Two-photon autofluorescence dynamics imaging reveals sensitivity of intracellular NADH concentration and conformation to cell physiology at the single-cell level

Yu, Q., & Heikal, A. A. (2008) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2008.12.010 · Cited by 291 · see citing works

Separation of the glucose-stimulated cytoplasmic and mitochondrial NAD(P)H responses in pancreatic islet β cells

Patterson, G. H., Knobel, S. M., Arkhammar, P. O. G., Thastrup, M., & Piston, D. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090098797 · Cited by 284 · see citing works

Nicotinamide adenine dinucleotide fluorescence spectroscopy and imaging of isolated cardiac myocytes

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Redox sensor CtBP mediates hypoxia-induced tumor cell migration

Zhang, Q., Wang, S.-Y., Nottke, A. C., Rocheleau, J. V., Piston, D. W., & Goodman, R. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603269103 · Cited by 200 · see citing works

Poly(ADP-ribose) glycohydrolase mediates oxidative and excitotoxic neuronal death

Ying, W., Sevigny, M. B., Chen, Y., & Swanson, R. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211202598 · Cited by 199 · see citing works

Nicotinamide adenine dinucleotide metabolism as an attractive target for drug discovery

Khan, J., Forouhar, F., Tao, X., & Tong, L. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.5.695 · Cited by 174 · see citing works

State of Oxidation-Reduction and State of Binding in the Cytosolic NADH-System as Disclosed by Equilibration with Extracellular Lactate/Pyruvate in Hemoglobin-Free Perfused Rat Liver

Bücher, T., Brauser, B., CONZE, A., KLEIN, F., Langguth, O., & Sies, H. (1972) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1972.tb01840.x · Cited by 165 · see citing works

Increased lactate/pyruvate ratio augments blood flow in physiologically activated human brain

Mintun, M. A., Vlassenko, A. G., Rundle, M. M., & Raichle, M. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307457100 · Cited by 157 · see citing works

Distribution of Mitochondrial NADH Fluorescence Lifetimes: Steady-State Kinetics of Matrix NADH Interactions

Blinova, K., Carroll, S. L., Bose, S., Smirnov, A. V., Harvey, J. J., Knutson, J. R., & Balaban, R. S. (2005) · Biochemistry · doi:10.1021/bi0485124 · Cited by 150 · see citing works

Control of the redox state of the nicotinamide–adenine dinucleotide couple in rat liver cytoplasm

Stubbs, M., Veech, R. L., & Krebs, H. A. (1972) · Biochemical Journal · doi:10.1042/bj1260059 · Cited by 149 · see citing works

Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex

Wang, E., Bauer, M. C., Rogstam, A., Linse, S. S., Logan, D. T., & von Wachenfeldt, C. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06295.x · Cited by 143 · see citing works

Determination of NAD+and NADH in a Single Cell under Hydrogen Peroxide Stress by Capillary Electrophoresis

谢文俊, Xu, A., & Yeung, E. S. (2009) · Analytical Chemistry · doi:10.1021/ac802249m · Cited by 141 · see citing works

Fluorescence of Pyridine Nucleotides in Mitochondria

Avi‐Dor, Y., Olson, J. M., Doherty, M. D., & Kaplan, N. O. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63448-4 · Cited by 127 · see citing works

Some Characteristics of the Fluorescence Lifetime of Reduced Pyridine Nucleotides in Isolated Mitochondria, Isolated Hepatocytes, and Perfused Rat Liver In Situ

Wakita, M., Nishimura, G., & Tamura, M. (1995) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a125001 · Cited by 110 · see citing works

Structural Basis for NADH/NAD+ Redox Sensing by a Rex Family Repressor

McLaughlin, K. J., Strain-Damerell, C. M., Xie, K., Brekasis, D., Soares, A. S., Paget, M. S. B., & Kielkopf, C. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.006 · Cited by 93 · see citing works

The Free NADH Concentration Is Kept Constant in Plant Mitochondria under Different Metabolic Conditions

Kasimova, M. R., Grigienė, J., Krab, K., Hagedorn, P., Flyvbjerg, H., Andersen, P. E., & Møller, I. M. (2006) · The Plant Cell · doi:10.1105/tpc.105.039354 · Cited by 92 · see citing works

Regulation of blood flow in activated human brain by cytosolic NADH/NAD + ratio

Vlassenko, A. G., Rundle, M. M., Raichle, M. E., & Mintun, M. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510632103 · Cited by 84 · see citing works

Brain energy metabolism of the conscious rat exposed to various physiological and pathological situations

Mayevsky, A. (1976) · Brain Research · doi:10.1016/0006-8993(76)90944-6 · Cited by 76 · see citing works

P2X7 receptors mediate NADH transport across the plasma membranes of astrocytes

Lü, H., Burns, D., Garnier, P. E., Wei, G., Zhu, K., & Ying, W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.095 · Cited by 57 · see citing works

Redox regulation of mitochondrial function

Handy, D. E., & Loscalzo, J. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4123 · Cited by 588 · see citing works

Complementation of mitochondrial electron transport chain by manipulation of the NAD ⁺ /NADH ratio

Titov, D. V., Cracan, V., Goodman, R. P., Peng, J., Grabarek, Z., & Mootha, V. K. (2016) · Science · doi:10.1126/science.aad4017 · Cited by 518 · see citing works

Glutamine‐driven oxidative phosphorylation is a major ATP source in transformed mammalian cells in both normoxia and hypoxia

Fan, J., Kamphorst, J. J., Mathew, R., Chung, M. K., White, E., Shlomi, T., & Rabinowitz, J. D. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.65 · Cited by 428 · see citing works

Imaging Mitochondrial Flux in Single Cells with a FRET Sensor for Pyruvate

San Martín, A., Ceballo, S., Baeza-Lehnert, F., Lerchundi, R., Valdebenito, R., Contreras-Baeza, Y., Alegría, K., & Barros, L. F. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085780 · Cited by 197 · see citing works

Monitoring ATP dynamics in electrically active white matter tracts

Trevisiol, A., Saab, A. S., Winkler, U., Marx, G., Imamura, H., Möbius, W., Kusch, K., Nave, K.-A., & Hirrlinger, J. (2017) · eLife · doi:10.7554/elife.24241 · Cited by 151 · see citing works

Location, Location, Location: Compartmentalization of NAD+ Synthesis and Functions in Mammalian Cells

Cambronne, X. A., & Kraus, W. L. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.05.010 · Cited by 137 · see citing works

Cytosolic NADH-NAD ⁺ Redox Visualized in Brain Slices by Two-Photon Fluorescence Lifetime Biosensor Imaging

Mongeon, R., Venkatachalam, V., & Yellen, G. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6593 · Cited by 100 · see citing works

Axonal energy metabolism, and the effects in aging and neurodegenerative diseases

Yang, S., Park, J. H., & Lu, H.-C. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00634-3 · Cited by 94 · see citing works

SIRT5 deficiency suppresses mitochondrial ATP production and promotes AMPK activation in response to energy stress

Zhang, M., Wu, J., Sun, R., Tao, X., Wang, X., Kang, Q., Wang, H., Zhang, L., Liu, P., Zhang, J., et al. (2019) · PLOS ONE · doi:10.1371/journal.pone.0211796 · Cited by 72 · see citing works

The simultaneous determination of NAD(H) and NADP(H) utilization by glutamate dehydrogenase

Treberg, J. R., Brosnan, M. E., & Brosnan, J. T. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0549-8 · Cited by 10 · see citing works

Metabolism of Pyridine Coenzymes in Microorganisms

Kuwahara, M., Tachiki, T., Tochikura, T., et al. (1971) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.35.177 · Cited by 2 · see citing works

Two Different Methods of Quantification of Oxidized Nicotinamide Adenine Dinucleotide (NAD+) and Reduced Nicotinamide Adenine Dinucleotide (NADH) Intracellular Levels: Enzymatic Coupled Cycling Assay and Ultra-performance Liquid Chromatography (UPLC)-Mass Spectrometry

Kanamori, K. S., de Oliveira, G. C., Auxiliadora‐Martins, M., Schoon, R. A., Reid, J. M., & Chini, E. N. (2018) · BIO-PROTOCOL · doi:10.21769/bioprotoc.2937 · Cited by 28 · see citing works

Metabolism of Pyridine Coenzymes in Microorganisms

Kuwahara, M., Tachiki, T., Tochikura, T., et al. (1971) · Agricultural and Biological Chemistry · doi:10.1080/00021369.1971.10859898

ON ENHANCING NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD) ACTIVITY IN LIVING SYSTEMS

Kohane, M. J., & Tiller, W. A. (2001) · Subtle energies & energy medicine · Cited by 1 · see citing works