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Volumn 95, Issue 1, 2009, Pages 46-57

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

Author keywords

Associated anisotropy; Dehydrogenase; Hs578Bst; Hs578T; NADH; Two photon FLIM

Indexed keywords

LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; POTASSIUM CYANIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 62049086106     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2008.12.010     Document Type: Article
Times cited : (246)

References (80)
  • 3
    • 0004155427 scopus 로고    scopus 로고
    • W.H. Freeman and Company, New York
    • Stryer L. Biochemistry (1999), W.H. Freeman and Company, New York
    • (1999) Biochemistry
    • Stryer, L.1
  • 5
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg O. On the origin of cancer cells. Science 123 (1956) 309-314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 8
    • 12544256565 scopus 로고    scopus 로고
    • Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia
    • Xu R.H., Pelicano H., Zhou Y., Carew J.S., Feng L., Bhalla K.N., Keating M.J., and Huang P. Inhibition of glycolysis in cancer cells: a novel strategy to overcome drug resistance associated with mitochondrial respiratory defect and hypoxia. Cancer Res. 65 (2005) 613-621
    • (2005) Cancer Res. , vol.65 , pp. 613-621
    • Xu, R.H.1    Pelicano, H.2    Zhou, Y.3    Carew, J.S.4    Feng, L.5    Bhalla, K.N.6    Keating, M.J.7    Huang, P.8
  • 9
    • 21644450243 scopus 로고    scopus 로고
    • Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy
    • Vishwasrao H.D., Heikal A.A., Kasischke K.A., and Webb W.W. Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy. J. Biol. Chem. 280 (2005) 25119-25126
    • (2005) J. Biol. Chem. , vol.280 , pp. 25119-25126
    • Vishwasrao, H.D.1    Heikal, A.A.2    Kasischke, K.A.3    Webb, W.W.4
  • 10
    • 25444510346 scopus 로고    scopus 로고
    • Metabolic mapping of MCF 10A human breast cells via multiphoton fluorescence lifetime imaging of the coenzyme NADH
    • Bird D.K., Yan L., Vrotsos K.M., Eliceiri K.W., Vaughan E.M., Keely P.J., White J.G., and Ramanujam N. Metabolic mapping of MCF 10A human breast cells via multiphoton fluorescence lifetime imaging of the coenzyme NADH. Cancer Res. 65 (2005) 8766-8773
    • (2005) Cancer Res. , vol.65 , pp. 8766-8773
    • Bird, D.K.1    Yan, L.2    Vrotsos, K.M.3    Eliceiri, K.W.4    Vaughan, E.M.5    Keely, P.J.6    White, J.G.7    Ramanujam, N.8
  • 11
    • 0037328368 scopus 로고    scopus 로고
    • Measurements of NADH concentration in normal and malignant human tissues from breast and oral cavity
    • Uppal A., and Gupta P.K. Measurements of NADH concentration in normal and malignant human tissues from breast and oral cavity. Biotechnol. Appl. Biochem. 37 (2003) 45-50
    • (2003) Biotechnol. Appl. Biochem. , vol.37 , pp. 45-50
    • Uppal, A.1    Gupta, P.K.2
  • 12
    • 37549068090 scopus 로고    scopus 로고
    • NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences
    • Wang W. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences. Antioxid. Redox Signal 10 (2008) 179-206
    • (2008) Antioxid. Redox Signal , vol.10 , pp. 179-206
    • Wang, W.1
  • 14
    • 2942531063 scopus 로고    scopus 로고
    • Mitochondrial defects in cancer
    • Carew J.S., and Huang P. Mitochondrial defects in cancer. Mol. Cancer 1 (2002) 9
    • (2002) Mol. Cancer , vol.1 , pp. 9
    • Carew, J.S.1    Huang, P.2
  • 15
    • 34347389118 scopus 로고    scopus 로고
    • Mitochondria as targets for detection and treatment of cancer
    • Modica-Naplitano J.S., and Singh K.K. Mitochondria as targets for detection and treatment of cancer. Expert Rev. Mol. Med. 02 (2002) 1-18
    • (2002) Expert Rev. Mol. Med. , vol.2 , pp. 1-18
    • Modica-Naplitano, J.S.1    Singh, K.K.2
  • 16
    • 0032904412 scopus 로고    scopus 로고
    • An evaluation of the role of mitochondria in neurodegenerative diseases: mitochondrial mutation and oxidative pathology, protective nuclear response, and cell death in neurodegeneration
    • Cassarion D.S., and Bennett J.P. An evaluation of the role of mitochondria in neurodegenerative diseases: mitochondrial mutation and oxidative pathology, protective nuclear response, and cell death in neurodegeneration. Brain Res. Rev. 29 (1999) 1-25
    • (1999) Brain Res. Rev. , vol.29 , pp. 1-25
    • Cassarion, D.S.1    Bennett, J.P.2
  • 17
    • 0029056469 scopus 로고
    • High-performance liquid chromatography analysis of oxidized and reduced pyridine dinucleotides in specific brain regions
    • Klaidman L.K., Leung A.C., and Adams Jr. J.D. High-performance liquid chromatography analysis of oxidized and reduced pyridine dinucleotides in specific brain regions. Anal. Biochem. 228 (1995) 312-317
    • (1995) Anal. Biochem. , vol.228 , pp. 312-317
    • Klaidman, L.K.1    Leung, A.C.2    Adams Jr., J.D.3
  • 19
    • 0008346970 scopus 로고
    • Pyridine nucleotide as an indicator of the oxygen requirements for energy-linked functions of Mitochondria
    • Chance B. Pyridine nucleotide as an indicator of the oxygen requirements for energy-linked functions of Mitochondria. Circ. Res. (Suppl.) 138 Suppl. (1976) I-131-I-138
    • (1976) Circ. Res. (Suppl.) , vol.138 , Issue.SUPPL
    • Chance, B.1
  • 20
    • 0007715066 scopus 로고
    • Energy-linked pyridine nucleotide reduction: inhibitory effects of hyperbaric oxygen in vitro and in vivo
    • Chance B., Jamieson D., and Coles H. Energy-linked pyridine nucleotide reduction: inhibitory effects of hyperbaric oxygen in vitro and in vivo. Nature 206 (1965) 257-263
    • (1965) Nature , vol.206 , pp. 257-263
    • Chance, B.1    Jamieson, D.2    Coles, H.3
  • 21
    • 0001424746 scopus 로고
    • Metabolically linked changes in fluorescence emission spectra of cortex of rat brain, kidney and adrenal gland
    • Chance B., Legallais V., and Schoener B. Metabolically linked changes in fluorescence emission spectra of cortex of rat brain, kidney and adrenal gland. Nature 195 (1962) 1073-1075
    • (1962) Nature , vol.195 , pp. 1073-1075
    • Chance, B.1    Legallais, V.2    Schoener, B.3
  • 22
    • 0032876126 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of normal, SV40-transformed human keratinocytes, and carcinoma cells
    • Papadopoulos A.J., Zhadin N.N., Steinberg M.L., and Alfano R.R. Fluorescence spectroscopy of normal, SV40-transformed human keratinocytes, and carcinoma cells. Cancer Biochem. Biophys. 17 (1999) 13-23
    • (1999) Cancer Biochem. Biophys. , vol.17 , pp. 13-23
    • Papadopoulos, A.J.1    Zhadin, N.N.2    Steinberg, M.L.3    Alfano, R.R.4
  • 23
    • 0029451905 scopus 로고
    • Evaluation of changes in the NADH level between carcinogenic and normal tissue samples by use of fluorescence spectroscopy
    • Betz V., Scheneckenburger H., Alleroeder H.P., Sybrecht G.W., and Meyer J.-U. Evaluation of changes in the NADH level between carcinogenic and normal tissue samples by use of fluorescence spectroscopy. SPIE 2324 (1994) 284-291
    • (1994) SPIE , vol.2324 , pp. 284-291
    • Betz, V.1    Scheneckenburger, H.2    Alleroeder, H.P.3    Sybrecht, G.W.4    Meyer, J.-U.5
  • 24
    • 37549068090 scopus 로고    scopus 로고
    • +/NADPH in cellular functions and cell death: regulation and biological consequences
    • +/NADPH in cellular functions and cell death: regulation and biological consequences. Antioxid. Redox Signal. 10 (2008) 179-206
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 179-206
    • Ying, W.1
  • 25
    • 0028363016 scopus 로고
    • Time resolved and steady state fluorescence spectroscopy from normal and malignant cultured human breast cell lines
    • Glassman W.S., Steinberg M., and Alfano R.R. Time resolved and steady state fluorescence spectroscopy from normal and malignant cultured human breast cell lines. Lasers Life Sci. 6 (1994) 91-98
    • (1994) Lasers Life Sci. , vol.6 , pp. 91-98
    • Glassman, W.S.1    Steinberg, M.2    Alfano, R.R.3
  • 26
    • 0142129099 scopus 로고    scopus 로고
    • Autofluorescence spectroscopy of normal and malignant human breast cell lines
    • Palmer G.M., Keely P.J., Breslin T.M., and Ramanujam N. Autofluorescence spectroscopy of normal and malignant human breast cell lines. Photochem. Photobiol. 78 (2003) 462-469
    • (2003) Photochem. Photobiol. , vol.78 , pp. 462-469
    • Palmer, G.M.1    Keely, P.J.2    Breslin, T.M.3    Ramanujam, N.4
  • 27
    • 4344689464 scopus 로고    scopus 로고
    • Autofluorescence lifetime imaging of cultivated cells using a UV picosecond laser diode
    • Schneckenburger H., Wagner M., Weber P., Strauss W.S.L., and Sailer R. Autofluorescence lifetime imaging of cultivated cells using a UV picosecond laser diode. J. Fluoresc. 14 (2004) 649-654
    • (2004) J. Fluoresc. , vol.14 , pp. 649-654
    • Schneckenburger, H.1    Wagner, M.2    Weber, P.3    Strauss, W.S.L.4    Sailer, R.5
  • 28
    • 0028102269 scopus 로고
    • Two-photon molecular excitation provides intrinsic 3-dimensional resolution for laser-based microscopy and microphotochemistry
    • Williams R.M., Piston D.W., and Webb W.W. Two-photon molecular excitation provides intrinsic 3-dimensional resolution for laser-based microscopy and microphotochemistry. FASEB J. 8 (1994) 804-813
    • (1994) FASEB J. , vol.8 , pp. 804-813
    • Williams, R.M.1    Piston, D.W.2    Webb, W.W.3
  • 29
    • 18844374818 scopus 로고    scopus 로고
    • UV-induced DNA damage in human keratinocytes: quantitation and correlation with long-term survival
    • Lisby S., Gniadecki R., and Wulf H.C. UV-induced DNA damage in human keratinocytes: quantitation and correlation with long-term survival. Exp. Dermatol. 14 (2005) 349-355
    • (2005) Exp. Dermatol. , vol.14 , pp. 349-355
    • Lisby, S.1    Gniadecki, R.2    Wulf, H.C.3
  • 32
    • 0031719058 scopus 로고    scopus 로고
    • Multiphoton excitation provides optical sections from deeper within scattering specimens that confocal imaging
    • Centonze V.E., and White J.G. Multiphoton excitation provides optical sections from deeper within scattering specimens that confocal imaging. Biophys. J. 75 (1998) 2015-2024
    • (1998) Biophys. J. , vol.75 , pp. 2015-2024
    • Centonze, V.E.1    White, J.G.2
  • 33
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk W., Strickler J.H., and Webb W.W. Two-photon laser scanning fluorescence microscopy. Science 245 (1990) 73-76
    • (1990) Science , vol.245 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 34
    • 0017645944 scopus 로고
    • Two syngeneic cell lines from human breast tissue: the aneuploid mammary epithelial (Hs578T) and the diploid myoepithelial (Hs578Bst) cell lines
    • Hackett A.J., Smith H.S., Springer E.L., Owens R.B., Nelson-Rees W.A., Riggs J.L., and Gardner M.B. Two syngeneic cell lines from human breast tissue: the aneuploid mammary epithelial (Hs578T) and the diploid myoepithelial (Hs578Bst) cell lines. J. Natl. Cancer Inst. 58 (1977) 1795-1806
    • (1977) J. Natl. Cancer Inst. , vol.58 , pp. 1795-1806
    • Hackett, A.J.1    Smith, H.S.2    Springer, E.L.3    Owens, R.B.4    Nelson-Rees, W.A.5    Riggs, J.L.6    Gardner, M.B.7
  • 35
    • 0346751974 scopus 로고    scopus 로고
    • Antecedents of two-photon excitation laser scanning microscopy
    • Masters B.R., and So P.T. Antecedents of two-photon excitation laser scanning microscopy. Microsc. Res. Tech. 63 (2004) 3-11
    • (2004) Microsc. Res. Tech. , vol.63 , pp. 3-11
    • Masters, B.R.1    So, P.T.2
  • 36
    • 0037795542 scopus 로고    scopus 로고
    • Live tissue intrinsic emission microscopy using multiphoton-excited native fluorescence and second harmonic generation
    • Zipfel W.R., Williams R.M., Christie R., Nikitin A.Y., Hyman B.T., and Webb W.W. Live tissue intrinsic emission microscopy using multiphoton-excited native fluorescence and second harmonic generation. Proc. Natl. Acad. Sci. USA 100 (2003) 7075-7080
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7075-7080
    • Zipfel, W.R.1    Williams, R.M.2    Christie, R.3    Nikitin, A.Y.4    Hyman, B.T.5    Webb, W.W.6
  • 37
    • 0242353872 scopus 로고    scopus 로고
    • Nonlinear magic: multiphoton microscopy in the biosciences
    • Zipfel W.R., Williams R.M., and Webb W.W. Nonlinear magic: multiphoton microscopy in the biosciences. Nature Biotechnol. 21 (2003) 1369-1377
    • (2003) Nature Biotechnol. , vol.21 , pp. 1369-1377
    • Zipfel, W.R.1    Williams, R.M.2    Webb, W.W.3
  • 38
    • 0036224973 scopus 로고    scopus 로고
    • Two-photon fluorescence spectroscopy and microscopy of NAD(P)H and Flavoprotein
    • Huang S., Heikal A.A., and Webb W.W. Two-photon fluorescence spectroscopy and microscopy of NAD(P)H and Flavoprotein. Biophys. J. 82 (2002) 2811-2825
    • (2002) Biophys. J. , vol.82 , pp. 2811-2825
    • Huang, S.1    Heikal, A.A.2    Webb, W.W.3
  • 39
    • 0030532990 scopus 로고    scopus 로고
    • Measurement of two-photon excitation cross sections of molecular fluorophores with data from 690 to 1050 nm
    • Xu C., and Webb W.W. Measurement of two-photon excitation cross sections of molecular fluorophores with data from 690 to 1050 nm. J. Opt. Soc. Am. B. 13 (1996) 481-491
    • (1996) J. Opt. Soc. Am. B. , vol.13 , pp. 481-491
    • Xu, C.1    Webb, W.W.2
  • 40
    • 3042793425 scopus 로고    scopus 로고
    • Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis
    • Kasischke K.A., Vishwasrao H.D., Fisher P.J., Zipfel W.R., and Webb W.W. Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis. Science 305 (2004) 99-103
    • (2004) Science , vol.305 , pp. 99-103
    • Kasischke, K.A.1    Vishwasrao, H.D.2    Fisher, P.J.3    Zipfel, W.R.4    Webb, W.W.5
  • 41
    • 0034814636 scopus 로고    scopus 로고
    • Gluocose uptake and metabolism by cultured human skeletal muscle cells: rate-limiting steps
    • Perriott L.M., Kono T., R W.R., M K.S., Piston D.W., and K G.D. Gluocose uptake and metabolism by cultured human skeletal muscle cells: rate-limiting steps. Am. J. Physiol. Endocrinol. Metab. 281 (2001) E72-80
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.281
    • Perriott, L.M.1    Kono, T.2    Piston, D.W.3
  • 42
    • 10044228440 scopus 로고    scopus 로고
    • Non-invasive live-cell measurement of changes in macrophage NAD(P)H by two-photon microscopy
    • Kable E.P.W., and Kiemer A.K. Non-invasive live-cell measurement of changes in macrophage NAD(P)H by two-photon microscopy. Immunol. Lett. 96 (2005) 33-38
    • (2005) Immunol. Lett. , vol.96 , pp. 33-38
    • Kable, E.P.W.1    Kiemer, A.K.2
  • 43
    • 0030020423 scopus 로고    scopus 로고
    • Quantitative subcellular imaging of glucose metabolism within intact pancreatic islets
    • Bennett B.D., Jetton T.L., Ying G., Magnuson M.A., and Piston D.W. Quantitative subcellular imaging of glucose metabolism within intact pancreatic islets. J. Biol. Chem. 271 (1996) 3647-3651
    • (1996) J. Biol. Chem. , vol.271 , pp. 3647-3651
    • Bennett, B.D.1    Jetton, T.L.2    Ying, G.3    Magnuson, M.A.4    Piston, D.W.5
  • 44
    • 22144432969 scopus 로고    scopus 로고
    • Glucose-dependent changes in NAD(P)H-related fluorescence lifetime of adipocytes and fibroblasts in vitro: potential for non-invasive glucose sensing in diabetes mellitus
    • Evans N.D., Gnudi L., Rolinski O.J., Birch D.J.S., and Pickup J.C. Glucose-dependent changes in NAD(P)H-related fluorescence lifetime of adipocytes and fibroblasts in vitro: potential for non-invasive glucose sensing in diabetes mellitus. J. Photochem. Photobiol. B 80 (2005) 122-129
    • (2005) J. Photochem. Photobiol. B , vol.80 , pp. 122-129
    • Evans, N.D.1    Gnudi, L.2    Rolinski, O.J.3    Birch, D.J.S.4    Pickup, J.C.5
  • 46
    • 34250630832 scopus 로고    scopus 로고
    • Determination of hair cell metabolic state in isolated cochlear preparations by two-photon microscopy
    • 021004/021001-021004/021008
    • Tiede L.M., Rocha-Sanchez S.M., Hallworth R., Nichols M.G., and Beisel K. Determination of hair cell metabolic state in isolated cochlear preparations by two-photon microscopy. J. Biomed. Opt. 12 (2007) 021004/021001-021004/021008
    • (2007) J. Biomed. Opt. , vol.12
    • Tiede, L.M.1    Rocha-Sanchez, S.M.2    Hallworth, R.3    Nichols, M.G.4    Beisel, K.5
  • 48
    • 33751299761 scopus 로고    scopus 로고
    • Two-photon microscopes and in vivo multiphoton tomographs - powerful diagnostic tools for tissue engineering and drug delivery
    • Schenke-Layland K., Riemann I., Damour O., Stock U.A., and Konig K. Two-photon microscopes and in vivo multiphoton tomographs - powerful diagnostic tools for tissue engineering and drug delivery. Adv. Drug Deliver. Rev. 58 (2006) 878-896
    • (2006) Adv. Drug Deliver. Rev. , vol.58 , pp. 878-896
    • Schenke-Layland, K.1    Riemann, I.2    Damour, O.3    Stock, U.A.4    Konig, K.5
  • 49
    • 30944450665 scopus 로고    scopus 로고
    • Deep tissue two-photon microscopy
    • Helmchen F., and Denk W. Deep tissue two-photon microscopy. Nature Meth. 2 (2005) 932-940
    • (2005) Nature Meth. , vol.2 , pp. 932-940
    • Helmchen, F.1    Denk, W.2
  • 50
    • 0345120940 scopus 로고    scopus 로고
    • Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives
    • Scaduto Jr. R.C., and Grotyohann L.W. Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys. J. 76 (1999) 469-477
    • (1999) Biophys. J. , vol.76 , pp. 469-477
    • Scaduto Jr., R.C.1    Grotyohann, L.W.2
  • 51
    • 62049083305 scopus 로고    scopus 로고
    • Two-photon excited-state and conformation dynamics of NADH binding with dehydrogenases. In Femtochemistry VII: fundamental ultrafast processes in chemistry
    • Liu Y., Ariola S.F., Kim H.-R., Yu Q., Walvick R., and Heikal A.A. Two-photon excited-state and conformation dynamics of NADH binding with dehydrogenases. In Femtochemistry VII: fundamental ultrafast processes in chemistry. Phys. Biol. (2006) 396-401
    • (2006) Phys. Biol. , pp. 396-401
    • Liu, Y.1    Ariola, S.F.2    Kim, H.-R.3    Yu, Q.4    Walvick, R.5    Heikal, A.A.6
  • 52
    • 33749682631 scopus 로고    scopus 로고
    • Dynamics imaging of lipid phases and lipid-marker interactions in model biomembranes
    • Ariola S.F., Mudaliar D.J., Walvick R.P., and Heikal A.A. Dynamics imaging of lipid phases and lipid-marker interactions in model biomembranes. Phys. Chem. Chem. Phys. 8 (2006) 4517-4529
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 4517-4529
    • Ariola, S.F.1    Mudaliar, D.J.2    Walvick, R.P.3    Heikal, A.A.4
  • 53
    • 58149401303 scopus 로고    scopus 로고
    • Integrated biophotonics approach for noninvasive and multiscale studies of biomolecular and cellular biophysics
    • 0413151-0413114
    • Yu Q., Proia M., and Heikal A.A. Integrated biophotonics approach for noninvasive and multiscale studies of biomolecular and cellular biophysics. J. Biomed. Opt. 13 (2008) 0413151-0413114
    • (2008) J. Biomed. Opt. , vol.13
    • Yu, Q.1    Proia, M.2    Heikal, A.A.3
  • 54
    • 51649113170 scopus 로고    scopus 로고
    • Effect of refractive index on the fluorescence lifetime of green fluorescent protein
    • 031218/031211-031218/031218
    • Tregidgo C., Levitt J.A., and Suhling K. Effect of refractive index on the fluorescence lifetime of green fluorescent protein. J. Biomed. Opt. 13 (2008) 031218/031211-031218/031218
    • (2008) J. Biomed. Opt. , vol.13
    • Tregidgo, C.1    Levitt, J.A.2    Suhling, K.3
  • 57
    • 0023404609 scopus 로고
    • Demonstration of an associated anisotropy decay by frequency-domain fluorometry
    • Szmacinski H., Jayaweera R., Cherek H., and Lakowicz J.R. Demonstration of an associated anisotropy decay by frequency-domain fluorometry. Biophys. Chem. 27 (1987) 233-241
    • (1987) Biophys. Chem. , vol.27 , pp. 233-241
    • Szmacinski, H.1    Jayaweera, R.2    Cherek, H.3    Lakowicz, J.R.4
  • 58
    • 0034813706 scopus 로고    scopus 로고
    • Probing DNA polymerase fidelity mechanisms using time-resolved fluorescence anisotropy
    • Bailey M.F., Thompson E.H.Z., and Millar D.P. Probing DNA polymerase fidelity mechanisms using time-resolved fluorescence anisotropy. Methods 25 (2001) 62-77
    • (2001) Methods , vol.25 , pp. 62-77
    • Bailey, M.F.1    Thompson, E.H.Z.2    Millar, D.P.3
  • 59
    • 84985438407 scopus 로고
    • The fluorescence decay of reduced nicotinamides in aqueous solution after excitation with a UV-mode locked Ar Ion laser
    • Visser A.J.W.G., and Hoek A.v. The fluorescence decay of reduced nicotinamides in aqueous solution after excitation with a UV-mode locked Ar Ion laser. Photochem. Photobiol. 33 (1981) 35-40
    • (1981) Photochem. Photobiol. , vol.33 , pp. 35-40
    • Visser, A.J.W.G.1    Hoek, A.v.2
  • 60
    • 34250214344 scopus 로고    scopus 로고
    • In vivo multiphoton fluorescence lifetime imaging of protein-bound and free nicotinamide adenine dinucleotide in normal and precancerous epithelia
    • Skala M.C., Riching K.M., Bird D.K., Gendron-Fitzpatrick A., Eickhoff J., Eliceiri K.W., Keely P.J., and Ramanujam N. In vivo multiphoton fluorescence lifetime imaging of protein-bound and free nicotinamide adenine dinucleotide in normal and precancerous epithelia. J. Biomed. Opt. 12 (2007) 024014
    • (2007) J. Biomed. Opt. , vol.12 , pp. 024014
    • Skala, M.C.1    Riching, K.M.2    Bird, D.K.3    Gendron-Fitzpatrick, A.4    Eickhoff, J.5    Eliceiri, K.W.6    Keely, P.J.7    Ramanujam, N.8
  • 61
  • 62
    • 0018389150 scopus 로고
    • Carbocyanide dye orientation in red-cell membrane studied by microscopic fluorescence polarization
    • Axelrod D. Carbocyanide dye orientation in red-cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26 (1979) 557-573
    • (1979) Biophys. J. , vol.26 , pp. 557-573
    • Axelrod, D.1
  • 63
    • 0024572299 scopus 로고
    • Fluorescence polarization microscopy
    • Axelrod D. Fluorescence polarization microscopy. Methods Cell Biol. 30 (1989) 333-352
    • (1989) Methods Cell Biol. , vol.30 , pp. 333-352
    • Axelrod, D.1
  • 64
    • 0017841405 scopus 로고
    • Tumor mitochondria and the bioenergetics of cancer cells
    • Pederson P.L. Tumor mitochondria and the bioenergetics of cancer cells. Prog. Exp. Tumor Res. 22 (1978) 198-274
    • (1978) Prog. Exp. Tumor Res. , vol.22 , pp. 198-274
    • Pederson, P.L.1
  • 65
    • 0019876651 scopus 로고
    • The immobilization of mitochondrial malate dehydrogenase on Sepharose beads and the demonstration of catalytically active subunits
    • Jurgensen S.R., Wood D.C., Mahler J.C., and Harrison J.H. The immobilization of mitochondrial malate dehydrogenase on Sepharose beads and the demonstration of catalytically active subunits. J. Biol. Chem. 256 (1981) 2383-2388
    • (1981) J. Biol. Chem. , vol.256 , pp. 2383-2388
    • Jurgensen, S.R.1    Wood, D.C.2    Mahler, J.C.3    Harrison, J.H.4
  • 66
    • 0028456030 scopus 로고
    • Molecular weight of cytoplasmic malate dehydrogenase, mitochondrial malate dehydrogenase and lactate dehydrogenase of a freshwater catfish
    • Tripathi G. Molecular weight of cytoplasmic malate dehydrogenase, mitochondrial malate dehydrogenase and lactate dehydrogenase of a freshwater catfish. Biomed. Environ. Sci. 7 (1994) 122-129
    • (1994) Biomed. Environ. Sci. , vol.7 , pp. 122-129
    • Tripathi, G.1
  • 67
    • 0035799367 scopus 로고    scopus 로고
    • Dynamics of protein ligand binding on multiple time scale: NADH binding to lactate dehydrogenase
    • Deng H., Zhadin N., and Callender R. Dynamics of protein ligand binding on multiple time scale: NADH binding to lactate dehydrogenase. Biochemistry 40 (2001) 3767-3773
    • (2001) Biochemistry , vol.40 , pp. 3767-3773
    • Deng, H.1    Zhadin, N.2    Callender, R.3
  • 68
    • 33646571558 scopus 로고    scopus 로고
    • Ultraviolet-induced autofluorescence characterization of normal and tumoral esophageal epithelium cells with quantitation of NAD(P)H
    • Villette S., Pigaglio-Deshayes S., Vever-Bizet C., Validire P., and Bourg-Heckly G. Ultraviolet-induced autofluorescence characterization of normal and tumoral esophageal epithelium cells with quantitation of NAD(P)H. Photochem. Photobiol. Sci. 5 (2006) 483-492
    • (2006) Photochem. Photobiol. Sci. , vol.5 , pp. 483-492
    • Villette, S.1    Pigaglio-Deshayes, S.2    Vever-Bizet, C.3    Validire, P.4    Bourg-Heckly, G.5
  • 69
    • 0033790165 scopus 로고    scopus 로고
    • Effects of tachyplesin on the morphology and ultrastructure of human gastric carcinoma cell line BGC-823
    • Li Q.F., Ou Yang G.L., Li C.Y., and Hong S.G. Effects of tachyplesin on the morphology and ultrastructure of human gastric carcinoma cell line BGC-823. World J. Gastroenterol. 6 (2000) 676-680
    • (2000) World J. Gastroenterol. , vol.6 , pp. 676-680
    • Li, Q.F.1    Ou Yang, G.L.2    Li, C.Y.3    Hong, S.G.4
  • 70
    • 18244401090 scopus 로고    scopus 로고
    • Downregulation of XIAP expression induces apoptosis and enhances chemotherapeutic sensitivity in human gastric cancer cells
    • Tong Q.S., Zheng L.D., Wang L., Zeng F.Q., Chen F.M., Dong J.H., and Lu G.C. Downregulation of XIAP expression induces apoptosis and enhances chemotherapeutic sensitivity in human gastric cancer cells. Cancer Gene Ther. 12 (2005) 509-514
    • (2005) Cancer Gene Ther. , vol.12 , pp. 509-514
    • Tong, Q.S.1    Zheng, L.D.2    Wang, L.3    Zeng, F.Q.4    Chen, F.M.5    Dong, J.H.6    Lu, G.C.7
  • 72
    • 2442709313 scopus 로고    scopus 로고
    • Mitochondria in tumor cells studied by laser scanning confocal microscopy
    • Villa A.M., and Doglia S.M. Mitochondria in tumor cells studied by laser scanning confocal microscopy. J. Biomed. Opt. 9 (2004) 385-394
    • (2004) J. Biomed. Opt. , vol.9 , pp. 385-394
    • Villa, A.M.1    Doglia, S.M.2
  • 73
    • 3843091688 scopus 로고    scopus 로고
    • Quantitative NAD(P)H/flavoprotein autofluorescence imaging reveals metabolic mechanisms of pancreatic islet pyruvate response
    • Rocheleau J.V., Head W.S., and Piston D.W. Quantitative NAD(P)H/flavoprotein autofluorescence imaging reveals metabolic mechanisms of pancreatic islet pyruvate response. J. Biol. Chem. 279 (2004) 31780-31787
    • (2004) J. Biol. Chem. , vol.279 , pp. 31780-31787
    • Rocheleau, J.V.1    Head, W.S.2    Piston, D.W.3
  • 75
    • 41149100207 scopus 로고    scopus 로고
    • Multiphoton fluorescence lifetime imaging of intrinsic fluorescence in human and rat brain tissue reveals spatially distinct NADH binding
    • Chia T.H., Williamson A., Spencer D.D., and Levene M.J. Multiphoton fluorescence lifetime imaging of intrinsic fluorescence in human and rat brain tissue reveals spatially distinct NADH binding. Opt. Exp. 16 (2008) 4237-4249
    • (2008) Opt. Exp. , vol.16 , pp. 4237-4249
    • Chia, T.H.1    Williamson, A.2    Spencer, D.D.3    Levene, M.J.4
  • 76
    • 0028801627 scopus 로고
    • Nanosecond time-resolved circular polarization of fluorescence. Study of NADH bound to horse liver alcohol dehydrogenase
    • Schauerte J.A., Schlyer B.D., Steel D.G., and Gafni A. Nanosecond time-resolved circular polarization of fluorescence. Study of NADH bound to horse liver alcohol dehydrogenase. Proc. Natl. Acad. Sci. USA 92 (1995) 569-573
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 569-573
    • Schauerte, J.A.1    Schlyer, B.D.2    Steel, D.G.3    Gafni, A.4
  • 77
    • 0029922127 scopus 로고    scopus 로고
    • Dye-affinity labelling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site
    • Labrou N.E., Eliopoulos E., and Clonis Y.D. Dye-affinity labelling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site. Biochem. J. 315 Pt 2 (1996) 687-693
    • (1996) Biochem. J. , vol.315 , Issue.PART 2 , pp. 687-693
    • Labrou, N.E.1    Eliopoulos, E.2    Clonis, Y.D.3
  • 78
    • 0028674909 scopus 로고
    • Binding of malate dehydrogenase and NADH channeling to complex I
    • Ovadi J., Huang Y., and Spivey H.O. Binding of malate dehydrogenase and NADH channeling to complex I. J. Mol. Recognit. 7 (1994) 2650277
    • (1994) J. Mol. Recognit. , vol.7 , pp. 2650277
    • Ovadi, J.1    Huang, Y.2    Spivey, H.O.3
  • 79
    • 0001644129 scopus 로고
    • Determination of dissociation constants of coenzymes and abortive ternary complexes with rabbit muscle lactate dehydrogenase from fluorescence measurements
    • Fromm H. Determination of dissociation constants of coenzymes and abortive ternary complexes with rabbit muscle lactate dehydrogenase from fluorescence measurements. J. Biol. Chem. 238 (1963) 2938-2944
    • (1963) J. Biol. Chem. , vol.238 , pp. 2938-2944
    • Fromm, H.1
  • 80
    • 0018801362 scopus 로고
    • NADH binding to porcine mitochondrial malate dehydrogenase
    • Shore J.D., Evans S.A., Hobrook J., and Parker D.M. NADH binding to porcine mitochondrial malate dehydrogenase. J. Biol. Chem. 254 (1979) 9059-9062
    • (1979) J. Biol. Chem. , vol.254 , pp. 9059-9062
    • Shore, J.D.1    Evans, S.A.2    Hobrook, J.3    Parker, D.M.4


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