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Volumn 7, Issue 2, 2014, Pages

Citation analysis of the scientific publications of Britton Chance in ISI citation indexes

Author keywords

citation tree; Histcite; impact; metabolism; mitochondria; Scientometric analysis

Indexed keywords

BIOCHEMISTRY; BIOGRAPHIES; EMPLOYMENT; METABOLISM; MITOCHONDRIA; PHOTONICS; PHYSIOLOGY; REACTION KINETICS; RESEARCH;

EID: 84898460791     PISSN: 17935458     EISSN: 17937205     Source Type: Journal    
DOI: 10.1142/S1793545814300031     Document Type: Article
Times cited : (7)

References (81)
  • 1
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    • Dedication: Britton Chance, M.D., Ph.D., D.Sc
    • L. Z. Li, S. Nioka, K. A. Kang, \Dedication: Britton Chance, M.D., Ph.D., D.Sc.," Adv. Exp. Med. Biol. 765, v-xiv (2013)
    • (2013) Adv. Exp. Med. Biol. , vol.765
    • Li, L.Z.1    Nioka, S.2    Kang, K.A.3
  • 2
    • 84858762145 scopus 로고    scopus 로고
    • Eugene Garfield and algorithmic historiography: Co-words co-authors, and journal names
    • L. Leydesdor®, \Eugene Garfield and algorithmic historiography: Co-words, co-authors, and journal names," Ann Library Inform. Stud. 57, 248-260 (2010)
    • (2010) Ann Library Inform. Stud. , vol.57 , pp. 248-260
    • Leydesdor, L.1
  • 3
    • 3042854295 scopus 로고
    • The kinetics of the enzyme-substrate compound of peroxidase and their relation to the Michaelis theory
    • B. Chance, J. Brainerd, F. Cajori, G. Millikan, \The kinetics of the enzyme-substrate compound of peroxidase and their relation to the Michaelis theory," Science 92, 455 (1940)
    • (1940) Science , vol.92 , pp. 455
    • Chance, B.1    Brainerd, J.2    Cajori, F.3    Millikan, G.4
  • 4
    • 0001277376 scopus 로고
    • The kinteics of the enzyme-substrate compound of peroxidase
    • B. Chance, \The kinteics of the enzyme-substrate compound of peroxidase," J. Biol. Chem. 151, 553-577 (1943)
    • (1943) J. Biol. Chem , vol.151 , pp. 553-577
    • Chance, B.1
  • 5
    • 0001211645 scopus 로고
    • Studies on liver alcohol dehydrogenase. II. The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide
    • H. Theorell, B. Chance, \Studies on liver alcohol dehydrogenase. II. The kinetics of the compound of horse liver alcohol dehydrogenase and reduced diphosphopyridine nucleotide," Acta Chem. Scand. 5, 1127-1144 (1951)
    • (1951) Acta Chem. Scand , vol.5 , pp. 1127-1144
    • Theorell, H.1    Chance, B.2
  • 6
    • 36849116712 scopus 로고
    • Rapid and sensitive spectrophotometry. III. A double beam apparatus
    • B. Chance, \Rapid and sensitive spectrophotometry. III. A double beam apparatus," Rev. Sci. Instrum. 22, 634-638 (1951)
    • (1951) Rev. Sci. Instrum , vol.22 , pp. 634-638
    • Chance, B.1
  • 7
    • 0001332716 scopus 로고
    • An intermediate compound in the catalase-hydrogen peroxide reaction
    • B. Chance, \An intermediate compound in the catalase-hydrogen peroxide reaction," Acta Chem. Scand. 1, 236-267 (1947)
    • (1947) Acta Chem. Scand , vol.1 , pp. 236-267
    • Chance, B.1
  • 8
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization
    • B. Chance, G. R. Williams, \Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization," J. Biol. Chem. 217, 383-393 (1955)
    • (1955) J. Biol. Chem , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 9
    • 0000432007 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. II. Dierence spectra
    • B. Chance, G. R. Williams, \Respiratory enzymes in oxidative phosphorylation. II. Di®erence spectra," J. Biol. Chem. 217, 395-407 (1955)
    • (1955) J. Biol. Chem , vol.217 , pp. 395-407
    • Chance, B.1    Williams, G.R.2
  • 10
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. III. The steady state
    • B. Chance, G. R. Williams, \Respiratory enzymes in oxidative phosphorylation. III. The steady state," J. Biol. Chem. 217, 409-427 (1955)
    • (1955) J. Biol. Chem , vol.217 , pp. 409-427
    • Chance, B.1    Williams, G.R.2
  • 11
    • 77049248708 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. IV. The respiratory chain
    • B. Chance, G. R. Williams, \Respiratory enzymes in oxidative phosphorylation. IV. The respiratory chain," J. Biol. Chem. 217, 429-438 (1955)
    • (1955) J. Biol. Chem , vol.217 , pp. 429-438
    • Chance, B.1    Williams, G.R.2
  • 12
    • 0000439760 scopus 로고
    • Metabolic control mechanisms. IV. The e®ect of glucose upon the steady state of respiratory enzymes in the ascites cell
    • B. Chance, B. Hess, \Metabolic control mechanisms. IV. The e®ect of glucose upon the steady state of respiratory enzymes in the ascites cell," J. Biol. Chem. 234, 2421-2427 (1959)
    • (1959) J. Biol. Chem , vol.234 , pp. 2421-2427
    • Chance, B.1    Hess, B.2
  • 13
    • 1542793426 scopus 로고
    • Metabolic control mechanisms. III. Kinetics of oxygen utilization in ascites tumor cells
    • B. Chance, B. Hess, \Metabolic control mechanisms. III. Kinetics of oxygen utilization in ascites tumor cells," J. Biol. Chem. 234, 2416-2420 (1959)
    • (1959) J. Biol. Chem , vol.234 , pp. 2416-2420
    • Chance, B.1    Hess, B.2
  • 14
    • 33749742873 scopus 로고
    • Metabolic control mechanisms. II. Crossover phenomena in mitochondria of ascites tumor cells
    • B. Chance, B. Hess, \Metabolic control mechanisms. II. Crossover phenomena in mitochondria of ascites tumor cells," J. Biol. Chem. 234, 2413-2415 (1959)
    • (1959) J. Biol. Chem , vol.234 , pp. 2413-2415
    • Chance, B.1    Hess, B.2
  • 15
    • 0000439761 scopus 로고
    • Metabolic control mechanisms. I. Electron transfer in the mammalian cell
    • B. Chance, B. Hess, \Metabolic control mechanisms. I. Electron transfer in the mammalian cell," J. Biol. Chem. 234, 2404-2412 (1959)
    • (1959) J. Biol. Chem , vol.234 , pp. 2404-2412
    • Chance, B.1    Hess, B.2
  • 16
    • 0003381877 scopus 로고
    • Metabolic control mechanisms. V. A solution for the equations representing interaction between glycolysis and respiration in ascites tumor cells
    • B. Chance, D. Garfinkel, J. Higgins, B. Hess, \Metabolic control mechanisms. V. A solution for the equations representing interaction between glycolysis and respiration in ascites tumor cells," J. Biol. Chem. 235, 2426-2439 (1960)
    • (1960) J. Biol. Chem , vol.235 , pp. 2426-2439
    • Chance, B.1    Garfinkel, D.2    Higgins, J.3    Hess, B.4
  • 17
    • 0001097630 scopus 로고
    • Metabolic control mechanisms. VI. Chemical events after glucose addition to ascites tumor cells
    • B. Hess, B. Chance, \Metabolic control mechanisms. VI. chemical events after glucose addition to ascites tumor cells," J. Biol. Chem. 236, 239-246 (1961)
    • (1961) J. Biol. Chem , vol.236 , pp. 239-246
    • Hess, B.1    Chance, B.2
  • 18
    • 0001696061 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. VII. Binding of intramitochondrial reduced pyridine nucleotide
    • B. Chance, H. Baltsche®sky, \Respiratory enzymes in oxidative phosphorylation. VII. Binding of intramitochondrial reduced pyridine nucleotide," J. Biol. Chem. 233, 736-739 (1958)
    • (1958) J. Biol. Chem , vol.233 , pp. 736-739
    • Chance, B.1    Baltschesky, H.2
  • 19
    • 0012182561 scopus 로고
    • Changes in uorescence in a frog sartorius muscle following a twitch
    • B. Chance, F. Jobsis, \Changes in uorescence in a frog sartorius muscle following a twitch," Nature 184, 195-196 (1959)
    • (1959) Nature , vol.184 , pp. 195-196
    • Chance, B.1    Jobsis, F.2
  • 20
    • 10144236677 scopus 로고
    • Localized uorometry of oxidation-reduction states of intracellular pyridine nucleotide in brain and kidney cortex of anesthetized rat
    • B. Chance, B. Schoener, P. Cohen, F. Jobsis, \Localized uorometry of oxidation-reduction states of intracellular pyridine nucleotide in brain and kidney cortex of anesthetized rat," Science 136, 325 (1962)
    • (1962) Science , vol.136 , pp. 325
    • Chance, B.1    Schoener, B.2    Cohen, P.3    Jobsis, F.4
  • 21
    • 0000613615 scopus 로고
    • Intracellular oxidation-reduction states in vivo
    • B. Chance, P. Cohen, F. Jobsis, B. Schoener, \Intracellular oxidation-reduction states in vivo," Science 137, 499-508 (1962)
    • (1962) Science , vol.137 , pp. 499-508
    • Chance, B.1    Cohen, P.2    Jobsis, F.3    Schoener, B.4
  • 22
    • 0000299271 scopus 로고
    • Correlation of oxidationreduction changes of intracellular reduced pyridine nucleotide and changes in electroencephalogram of the rat in anoxia
    • B. Chance, B. Schoener, \Correlation of oxidationreduction changes of intracellular reduced pyridine nucleotide and changes in electroencephalogram of the rat in anoxia," Nature 195, 956-958 (1962)
    • (1962) Nature , vol.195 , pp. 956-958
    • Chance, B.1    Schoener, B.2
  • 23
    • 0013966412 scopus 로고
    • Studies of photosynthesis using a pulsed laser. I. Temperature dependence of cytochrome oxidation rate in chromatium. Evidence for tunneling
    • D. DeVault, B. Chance, \Studies of photosynthesis using a pulsed laser. I. Temperature dependence of cytochrome oxidation rate in chromatium. Evidence for tunneling," Biophys. J. 6, 825-847 (1966)
    • (1966) Biophys. J , vol.6 , pp. 825-847
    • Devault, D.1    Chance, B.2
  • 24
    • 34247586600 scopus 로고    scopus 로고
    • Quantum catalysis in enzymes: Beyond the transition state theory paradigm. A Discussion Meeting held at the Royal Society on 14 and 15 November 2005
    • DOI 10.1098/rsif.2006.0122
    • N. S. Scrutton, M. J. Sutcli®e, P. Leslie Dutton, \Quantum catalysis in enzymes: Beyond the transition state theory paradigm. A Discussion Meeting held at the Royal Society on 14 and 15 November 2005," J. R. Soc. Interface / the R. Soc. 3, 465-469 (2006) (Pubitemid 46682101)
    • (2006) Journal of the Royal Society Interface , vol.3 , Issue.8 , pp. 465-469
    • Scrutton, N.S.1    Sutcliffe, M.J.2    Dutton, P.L.3
  • 27
    • 0014432856 scopus 로고
    • Oxidation-reduction properties of the mitochondrial avoprotein chain
    • I. Hassinen, B. Chance, \Oxidation-reduction properties of the mitochondrial avoprotein chain," Biochem. Biophys. Res. Commun. 31, 895-900 (1968)
    • (1968) Biochem. Biophys. Res. Commun , vol.31 , pp. 895-900
    • Hassinen, I.1    Chance, B.2
  • 28
    • 0014674055 scopus 로고
    • Cytochrome oxidase and its derivatives. IX. Spectrophotometric studies on the rapid reaction of ferrous cytochrome c oxidase with molecular oxygen under conditions of complete and partial oxygenation
    • M. V. Gilmour, M. R. Lemberg, B. Chance, \Cytochrome oxidase and its derivatives. IX. Spectrophotometric studies on the rapid reaction of ferrous cytochrome c oxidase with molecular oxygen under conditions of complete and partial oxygenation," BBA - Bioenergetics 172, 37-51 (1969)
    • (1969) BBA - Bioenergetics , vol.172 , pp. 37-51
    • Gilmour, M.V.1    Lemberg, M.R.2    Chance, B.3
  • 29
    • 0014407215 scopus 로고
    • Cytochromes: Chemical and structural aspects
    • B. Chance, \Cytochromes: Chemical and structural aspects," Science 159, 654-658 (1968)
    • (1968) Science , vol.159 , pp. 654-658
    • Chance, B.1
  • 30
    • 0016709349 scopus 로고
    • Functional intermediates in the reaction of membrane bound cytochrome oxidase with oxygen
    • B. Chance, C. Saronio, J. S. Leigh Jr, \Functional intermediates in the reaction of membrane bound cytochrome oxidase with oxygen," J. Biol. Chem. 250, 9226-9237 (1975)
    • (1975) J. Biol. Chem , vol.250 , pp. 9226-9237
    • Chance, B.1    Saronio, C.2    Leigh Jr., J.S.3
  • 31
    • 0001699841 scopus 로고
    • The energy-linked reaction of calcium with mitochondria
    • B. Chance, \The energy-linked reaction of calcium with mitochondria," J. Biol. Chem. 240, 2729-2748 (1965)
    • (1965) J. Biol. Chem , vol.240 , pp. 2729-2748
    • Chance, B.1
  • 32
    • 0000466588 scopus 로고
    • Respiratory chain linked H2O2 production in pigeon heart mitochondria
    • G. Loschen, L. Flohe, B. Chance, \Respiratory chain linked H2O2 production in pigeon heart mitochondria," FEBS Lett. 18, 261-264 (1971)
    • (1971) FEBS Lett , vol.18 , pp. 261-264
    • Loschen, G.1    Flohe, L.2    Chance, B.3
  • 37
    • 0032498179 scopus 로고    scopus 로고
    • Scientists who fund themselves
    • DOI 10.1126/science.279.5348.178
    • J. Cohen, \Scientists who fund themselves," Science 279, 178-181 (1998) (Pubitemid 28103861)
    • (1998) Science , vol.279 , Issue.5348 , pp. 178-181
    • Cohen, J.1
  • 38
    • 84908714633 scopus 로고
    • Enhancement of the chemiluminescence of perfused rat liver and of isolated mitochondria and microsomes by hydroperoxides
    • A. Boveris, B. Chance et al., \Enhancement of the chemiluminescence of perfused rat liver and of isolated mitochondria and microsomes by hydroperoxides," Adv. Exp. Med. Biol. 2, 975-984 (1978)
    • (1978) Adv. Exp. Med. Biol , vol.2 , pp. 975-984
    • Boveris, A.1    Chance, B.2
  • 40
    • 0019317204 scopus 로고
    • Low level chemiluminescence of the cytochrome c-catalyzed decomposition of hydrogen peroxide
    • E. Cadenas, A. I. Varsavsky, A. Boveris, B. Chance, \Low level chemiluminescence of the cytochrome c-catalyzed decomposition of hydrogen peroxide," FEBS Lett. 113, 141-144 (1980)
    • (1980) FEBS Lett , vol.113 , pp. 141-144
    • Cadenas, E.1    Varsavsky, A.I.2    Boveris, A.3    Chance, B.4
  • 41
    • 0019888827 scopus 로고
    • Low level chemiluminescence of alveolar macrophages: Spectral evidence for singlet oxygen generation
    • E. Cadenas, R. P. Daniele, B. Chance, \Low level chemiluminescence of alveolar macrophages: Spectral evidence for singlet oxygen generation," FEBS Lett. 123, 225-228 (1981)
    • (1981) FEBS Lett , vol.123 , pp. 225-228
    • Cadenas, E.1    Daniele, R.P.2    Chance, B.3
  • 42
    • 33845478539 scopus 로고    scopus 로고
    • Christopher Foote's discovery of the role of singlet oxygen [1O2 (1-g)] in photosensitized oxidation reactions
    • A. Greer, \Christopher Foote's discovery of the role of singlet oxygen [1O2 (1-g)] in photosensitized oxidation reactions," Acc. Chem. Res. 39, 797-804 (2006)
    • (2006) Acc. Chem. Res , vol.39 , pp. 797-804
    • Greer, A.1
  • 44
    • 84898482513 scopus 로고
    • Structure and function of copper atoms in cytochrome oxidase
    • L. Powers, W. E. Blumberg, B. Chance, C. H. Barlow, J. Leigh, J. S., J. Smith, T. Yonetani, S. Vik, \Structure and function of copper atoms in cytochrome oxidase," Adv. Exp. Med. Biol. 2, 863-871 (1978)
    • (1978) Adv. Exp. Med. Biol , vol.2 , pp. 863-871
    • Powers, L.1    Blumberg, W.E.2    Chance, B.3    Barlow, C.H.4    Leigh, J.5
  • 46
    • 0020148877 scopus 로고
    • Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy
    • J. Peisach, L. Powers, W. E. Blumberg, B. Chance, \Stellacyanin. Studies of the metal-binding site using x-ray absorption spectroscopy," Biophys. J. 38, 277-285 (1982)
    • (1982) Biophys. J , vol.38 , pp. 277-285
    • Peisach, J.1    Powers, L.2    Blumberg, W.E.3    Chance, B.4
  • 47
    • 0020620612 scopus 로고
    • Structure and kinetics of the photoproduct of carboxymyoglobin at low temperatures: An X-ray absorption study
    • B. Chance, R. Fischetti, L. Powers, \Structure and kinetics of the photoproduct of carboxymyoglobin at low temperatures: An X-ray absorption study," Biochemistry 22, 3820-3829 (1983) (Pubitemid 13035556)
    • (1983) Biochemistry , vol.22 , Issue.16 , pp. 3820-3829
    • Chance, B.1    Fischetti, R.2    Powers, L.3
  • 51
    • 84975647283 scopus 로고
    • Time resolved reectance and transmittance for the noninvasive measurement of tissue optical properties
    • M. S. Patterson, B. Chance, B. C. Wilson, \Time resolved reectance and transmittance for the noninvasive measurement of tissue optical properties," Appl. Opt. 28, 2331-2336 (1989)
    • (1989) Appl. Opt , vol.28 , pp. 2331-2336
    • Patterson, M.S.1    Chance, B.2    Wilson, B.C.3
  • 55
    • 11944261890 scopus 로고
    • Spectroscopy and imaging with di®using light
    • A. Yodh, B. Chance, \Spectroscopy and imaging with di®using light," Phys. Today 48, 34-40 (1995)
    • (1995) Phys. Today , vol.48 , pp. 34-40
    • Yodh, A.1    Chance, B.2
  • 56
    • 0000852354 scopus 로고    scopus 로고
    • Diffraction tomography for biochemical imaging with diffuse-photon density waves
    • X. D. Li, T. Durduran, A. G. Yodh, B. Chance, D. N. Pattanayak, \Di®raction tomography for biochemical imaging with di®use-photon density waves," Opt. Lett. 22, 573-575 (1997) (Pubitemid 127588055)
    • (1997) Optics Letters , vol.22 , Issue.8 , pp. 573-575
    • Li, X.D.1    Durduran, T.2    Yodh, A.G.3    Chance, B.4    Pattanayak, D.N.5
  • 58
    • 0036020205 scopus 로고    scopus 로고
    • MRI-guided diffuse optical spectroscopy of malignant and benign breast lesions
    • DOI 10.1038/sj.neo.7900244
    • V. Ntziachristos, A. G. Yodh, M. D. Schnall, B. Chance, \MRI-guided di®use optical spectroscopy of malignant and benign breast lesions," Neoplasia 4, 347-354 (2002) (Pubitemid 34755845)
    • (2002) Neoplasia , vol.4 , Issue.4 , pp. 347-354
    • Ntziachristos, V.1    Yodh, A.G.2    Schnall, M.D.3    Chance, B.4
  • 59
    • 24744439989 scopus 로고    scopus 로고
    • Time-dependent blood ow and oxygenation in human skeletal muscles measured with noninvasive near-infrared di®use optical spectroscopies
    • G. Yu, T. Durduran, G. Lech, C. Zhou, B. Chance, E. R. Mohler, 3rd, A. G. Yodh, \Time-dependent blood ow and oxygenation in human skeletal muscles measured with noninvasive near-infrared di®use optical spectroscopies," J. Biomed. Opt. 10, 024027 (2005)
    • (2005) J. Biomed. Opt , vol.10 , pp. 024027
    • Yu, G.1    Durduran, T.2    Lech, G.3    Zhou, C.4    Chance, B.5    Mohler, E.R.6    Yodh III, G.A.7
  • 60
    • 0000807212 scopus 로고    scopus 로고
    • Interfering di®usive photon-density waves with an absorbing-uorescent inhomogeneity
    • X. Intes, B. Chance, M. J. Holboke, A. G. Yodh, \Interfering di®usive photon-density waves with an absorbing-uorescent inhomogeneity," Opt. Express 8, 223-231 (2001)
    • (2001) Opt. Express , vol.8 , pp. 223-231
    • Intes, X.1    Chance, B.2    Holboke, M.J.3    Yodh, A.G.4
  • 61
    • 0030843420 scopus 로고    scopus 로고
    • Non-invasive optical spectroscopy and imaging of human brain function
    • DOI 10.1016/S0166-2236(97)01132-6
    • A. Villringer, B. Chance, \Non-invasive optical spectroscopy and imaging of human brain function," Trends Neurosci. 20, 435-442 (1997) (Pubitemid 27421703)
    • (1997) Trends in Neurosciences , vol.20 , Issue.10 , pp. 435-442
    • Villringer, A.1    Chance, B.2
  • 63
    • 0025735421 scopus 로고
    • Quantitation of time- and frequency-resolved optical spectra for the determination of tissue oxygenation
    • E. M. Sevick, B. Chance, J. Leigh, S. Nioka, M. Maris, \Quantitation of time- and frequency-resolved optical spectra for the determination of tissue oxygenation," Anal. Biochem. 195, 330-351 (1991)
    • (1991) Anal. Biochem , vol.195 , pp. 330-351
    • Sevick, E.M.1    Chance, B.2    Leigh, J.3    Nioka, S.4    Maris, M.5
  • 65
    • 0037013436 scopus 로고    scopus 로고
    • Tricarbocyanine cholesteryl laurates labeled LDL: New near infrared fluorescent probes (NIRFs) for monitoring tumors and gene therapy of familial hypercholesterolemia
    • DOI 10.1016/S0960-894X(02)00193-2, PII S0960894X02001932
    • G. Zheng, H. Li, K. Yang, D. Blessington, K. Licha, S. Lund-Katz, B. Chance, J. D. Glickson, \Tricarbocyanine cholesteryl laurates labeled LDL: New near infrared uorescent probes (NIRFs) for monitoring tumors and gene therapy of familial hypercholesterolemia," Bioorg. Med. Chem. Lett. 12, 1485-1488 (2002) (Pubitemid 34521918)
    • (2002) Bioorganic and Medicinal Chemistry Letters , vol.12 , Issue.11 , pp. 1485-1488
    • Zheng, G.1    Li, H.2    Yang, K.3    Blessington, D.4    Licha, K.5    Lund-Katz, S.6    Chance, B.7    Glickson, J.D.8
  • 69
    • 7444264033 scopus 로고    scopus 로고
    • Metabolic imaging of tumors using intrinsic and extrinsic fluorescent markers
    • DOI 10.1016/j.bios.2004.03.034, PII S0956566304001708, Optical Biosensing
    • Z. Zhang, H. Li, Q. Liu, L. Zhou, M. Zhang, Q. Luo, J. Glickson, B. Chance, G. Zheng, \Metabolic imaging of tumors using intrinsic and extrinsic uorescent markers," Biosens. Bioelectron. 20, 643-650 (2004) (Pubitemid 39445780)
    • (2004) Biosensors and Bioelectronics , vol.20 , Issue.3 , pp. 643-650
    • Zhang, Z.1    Li, H.2    Liu, Q.3    Zhou, L.4    Zhang, M.5    Luo, Q.6    Glickson, J.7    Chance, B.8    Zheng, G.9
  • 72
    • 79954516693 scopus 로고    scopus 로고
    • Quantitative mitochondrial redox imaging of breast cancer metastatic potential
    • H. N. Xu, S. Nioka, J. D. Glickson, B. Chance, L. Z. Li, \Quantitative mitochondrial redox imaging of breast cancer metastatic potential," J. Biomed. Opt. 15, 036010 (2010)
    • (2010) J. Biomed. Opt. , vol.15 , pp. 036010
    • Xu, H.N.1    Nioka, S.2    Glickson, J.D.3    Chance, B.4    Li, L.Z.5
  • 73
    • 84867497518 scopus 로고    scopus 로고
    • Imaging the redox states of human breast cancer core biopsies
    • H. N. Xu, J. Tchou, B. Chance, L. Z. Li, \Imaging the redox states of human breast cancer core biopsies," Adv. Exp. Med. Biol. 765, 343-349 (2013)
    • (2013) Adv. Exp. Med. Biol. , vol.765 , pp. 343-349
    • Xu, H.N.1    Tchou, J.2    Chance, B.3    Li, L.Z.4
  • 75
    • 80052041000 scopus 로고    scopus 로고
    • A novel time-shared uorometer gives the mitochondrial redox state as the ratio of two components of the respiratory chain of the animal and human buccal cavity with quantitative measures of the redox energy state
    • J.-R. Horng, S. Nioka, A. Quo, B. Chance, \A novel time-shared uorometer gives the mitochondrial redox state as the ratio of two components of the respiratory chain of the animal and human buccal cavity with quantitative measures of the redox energy state," J. Innov. Opt. Health Sci. 3, 235-245 (2010)
    • (2010) J. Innov. Opt. Health Sci. , vol.3 , pp. 235-245
    • Horng, J.-R.1    Nioka, S.2    Quo, A.3    Chance, B.4
  • 76
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, A. Boveris, \Hydroperoxide metabolism in mammalian organs," Physiol. Rev. 59, 527-605 (1979) (Pubitemid 9236599)
    • (1979) Physiological Reviews , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 77
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide. General properties and e®ect of hyperbaric oxygen
    • A. Boveris, B. Chance, \The mitochondrial generation of hydrogen peroxide. General properties and e®ect of hyperbaric oxygen," Biochem. J. 134, 707-716 (1973)
    • (1973) Biochem. J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 79
    • 77957006400 scopus 로고
    • Assay of catalases and peroxidases
    • B. Chance, A. C. Maehly, \Assay of catalases and peroxidases," Methods Enzymol. 2, 764-775 (1955)
    • (1955) Methods Enzymol , vol.2 , pp. 764-775
    • Chance, B.1    Maehly, A.C.2
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.