메뉴 건너뛰기




Volumn 40, Issue 7, 2006, Pages 1131-1143

Mechanism of cell death induction by nitroxide and hyperthermia

Author keywords

Apoptosis; Calcium; Free radicals; Hyperthermia; Mitochondria; ROS; Tempo

Indexed keywords

2,2,6,6 TETRAMETHYLPIPERIDINE N OXIDE; ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; CALCIUM; CASPASE 3; CASPASE INHIBITOR; CYTOCHROME C; DNA FRAGMENT; GLUTAMIC ACID; GLUTATHIONE; HEAT SHOCK PROTEIN; HYDROGEN PEROXIDE; NITROXIDE DERIVATIVE; OXYGEN; PEPTIDE; PROTEIN BAX; PROTEIN BCL 2; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VALINE;

EID: 33644895407     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2005.10.064     Document Type: Article
Times cited : (118)

References (68)
  • 1
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • R.W. Johnstone, A.A. Ruefli, and S.W. Lowe Apoptosis: a link between cancer genetics and chemotherapy Cell 108 2002 153 164
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 2
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • D.R. Green, and G. Kroemer The pathophysiology of mitochondrial cell death Science 305 2004 626 629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 3
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • B. Antonsson, S. Montessuit, S. Lauper, R. Eskes, and J.C. Martinou Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria Biochem. J. 345 Pt. 2 2000 271 278
    • (2000) Biochem. J. , vol.345 , Issue.PART 2 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 5
    • 0035931765 scopus 로고    scopus 로고
    • Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells
    • S. Shimizu, Y. Matsuoka, Y. Shinohara, Y. Yoneda, and Y. Tsujimoto Essential role of voltage-dependent anion channel in various forms of apoptosis in mammalian cells J. Cell Biol. 152 2001 237 250
    • (2001) J. Cell Biol. , vol.152 , pp. 237-250
    • Shimizu, S.1    Matsuoka, Y.2    Shinohara, Y.3    Yoneda, Y.4    Tsujimoto, Y.5
  • 6
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • M. Crompton The mitochondrial permeability transition pore and its role in cell death Biochem. J. 341 1999 233 249
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 7
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • A.P. Halestrap, K.Y. Woodfield, and C.P. Connern Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase J. Biol. Chem. 272 1997 3346 3354
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 8
    • 0013078509 scopus 로고    scopus 로고
    • Heat shock suppresses the permeability transition in rat liver mitochondria
    • L. He, and J.J. Lemasters Heat shock suppresses the permeability transition in rat liver mitochondria J. Biol. Chem. 278 2003 16755 16760
    • (2003) J. Biol. Chem. , vol.278 , pp. 16755-16760
    • He, L.1    Lemasters, J.J.2
  • 10
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ
    • V. Petronilli, D. Penzo, L. Scorrano, P. Bernardi, and F. Di Lisa The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ J. Biol. Chem. 276 2001 12030 12034
    • (2001) J. Biol. Chem. , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 11
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function?
    • L. He, and J.J. Lemasters Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function? FEBS Lett. 512 2002 1 7
    • (2002) FEBS Lett. , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 12
    • 0037087782 scopus 로고    scopus 로고
    • 2+ and sustained opening of the permeability transition pore
    • 2+ and sustained opening of the permeability transition pore J. Cell Sci. 115 2002 1175 1188
    • (2002) J. Cell Sci. , vol.115 , pp. 1175-1188
    • Jacobson, J.1    Duchen, M.R.2
  • 14
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • D.R. Green, and J.C. Reed Mitochondria and apoptosis Science 281 1998 1309 1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 15
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • G. Kroemer, and J.C. Reed Mitochondrial control of cell death Nat. Med. 6 2000 513 519
    • (2000) Nat. Med. , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 16
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • P. Li, D. Nijhawan, I. Budihardjo, S.M. Srinivasula, M. Ahmad, E.S. Alnemri, and X. Wang Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade Cell 91 1997 479 489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 17
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • T. Finkel, and N.J. Holbrook Oxidants, oxidative stress and the biology of ageing Nature 408 2000 239 247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 18
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat
    • S. Moncada, and J.D. Erusalimsky Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat Rev. Mol. Cell. Biol. 3 2002 214 220
    • (2002) Rev. Mol. Cell. Biol. , vol.3 , pp. 214-220
    • Moncada, S.1    Erusalimsky, J.D.2
  • 19
    • 0035200326 scopus 로고    scopus 로고
    • Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae
    • J.F. Davidson, and R.H. Schiestl Mitochondrial respiratory electron carriers are involved in oxidative stress during heat stress in Saccharomyces cerevisiae Mol. Cell. Biol. 21 2001 8483 8489
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8483-8489
    • Davidson, J.F.1    Schiestl, R.H.2
  • 20
    • 0032541026 scopus 로고    scopus 로고
    • Increased flux of free radicals in cells subjected to hyperthermia: Detection by electron paramagnetic resonance spin trapping
    • S.W. Flanagan, P.L. Moseley, and G.R. Buettner Increased flux of free radicals in cells subjected to hyperthermia: detection by electron paramagnetic resonance spin trapping FEBS Lett. 431 1998 285 286
    • (1998) FEBS Lett. , vol.431 , pp. 285-286
    • Flanagan, S.W.1    Moseley, P.L.2    Buettner, G.R.3
  • 21
    • 0032991543 scopus 로고    scopus 로고
    • Antioxidant-mediated inhibition of the heat shock response leads to apoptosis
    • A.M. Gorman, B. Heavey, E. Creagh, T.G. Cotter, and A. Samali Antioxidant-mediated inhibition of the heat shock response leads to apoptosis FEBS Lett. 445 1999 98 102
    • (1999) FEBS Lett. , vol.445 , pp. 98-102
    • Gorman, A.M.1    Heavey, B.2    Creagh, E.3    Cotter, T.G.4    Samali, A.5
  • 22
    • 0034647691 scopus 로고    scopus 로고
    • Pivotal role of reactive oxygen species as intracellular mediators of hyperthermia-induced apoptosis
    • D.M. Katschinski, K. Boos, S.G. Schindler, and J. Fandrey Pivotal role of reactive oxygen species as intracellular mediators of hyperthermia-induced apoptosis J. Biol. Chem. 275 2000 21094 21098
    • (2000) J. Biol. Chem. , vol.275 , pp. 21094-21098
    • Katschinski, D.M.1    Boos, K.2    Schindler, S.G.3    Fandrey, J.4
  • 24
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Y. Liu, G. Fiskum, and D. Schubert Generation of reactive oxygen species by the mitochondrial electron transport chain J. Neurochem. 80 2002 780 787
    • (2002) J. Neurochem. , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 25
    • 0036468510 scopus 로고    scopus 로고
    • A cross talk between cellular signalling and cellular redox state during heat-induced apoptosis in a rat histiocytoma
    • A.S. Sreedhar, B.V. Pardhasaradhi, A. Khar, and U.K. Srinivas A cross talk between cellular signalling and cellular redox state during heat-induced apoptosis in a rat histiocytoma Free Radic. Biol. Med. 32 2002 221 227
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 221-227
    • Sreedhar, A.S.1    Pardhasaradhi, B.V.2    Khar, A.3    Srinivas, U.K.4
  • 26
    • 0033538451 scopus 로고    scopus 로고
    • Oxidative stress inhibits apoptosis in human lymphoma cells
    • Y.J. Lee, and E. Shacter Oxidative stress inhibits apoptosis in human lymphoma cells J. Biol. Chem. 274 1999 19792 19798
    • (1999) J. Biol. Chem. , vol.274 , pp. 19792-19798
    • Lee, Y.J.1    Shacter, E.2
  • 27
    • 0033524857 scopus 로고    scopus 로고
    • A comparative study of apoptosis and necrosis in HepG2 cells: Oxidant-induced caspase inactivation leads to necrosis
    • A. Samali, H. Nordgren, B. Zhivotovsky, E. Peterson, and S. Orrenius A comparative study of apoptosis and necrosis in HepG2 cells: oxidant-induced caspase inactivation leads to necrosis Biochem. Biophys. Res. Commun. 255 1999 6 11
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 6-11
    • Samali, A.1    Nordgren, H.2    Zhivotovsky, B.3    Peterson, E.4    Orrenius, S.5
  • 31
    • 0035113848 scopus 로고    scopus 로고
    • A randomized clinical trial of radiation therapy versus thermoradiotherapy in stage IIIB cervical carcinoma
    • Y. Harima, K. Nagata, K. Harima, V.V. Ostapenko, Y. Tanaka, and S. Sawada A randomized clinical trial of radiation therapy versus thermoradiotherapy in stage IIIB cervical carcinoma Int. J. Hyperthermia 17 2001 97 105
    • (2001) Int. J. Hyperthermia , vol.17 , pp. 97-105
    • Harima, Y.1    Nagata, K.2    Harima, K.3    Ostapenko, V.V.4    Tanaka, Y.5    Sawada, S.6
  • 32
    • 0342545492 scopus 로고    scopus 로고
    • Comparison of radiotherapy alone with radiotherapy plus hyperthermia in locally advanced pelvic tumours: A prospective, randomised, multicentre trial. Dutch Deep Hyperthermia Group
    • J. van der Zee, D. Gonzalez Gonzalez, G.C. van Rhoon, J.D. van Dijk, W.L. van Putten, and A.A. Hart Comparison of radiotherapy alone with radiotherapy plus hyperthermia in locally advanced pelvic tumours: a prospective, randomised, multicentre trial. Dutch Deep Hyperthermia Group Lancet 355 2000 1119 1125
    • (2000) Lancet , vol.355 , pp. 1119-1125
    • Van Der Zee, J.1    Gonzalez Gonzalez, D.2    Van Rhoon, G.C.3    Van Dijk, J.D.4    Van Putten, W.L.5    Hart, A.A.6
  • 33
    • 0032520098 scopus 로고    scopus 로고
    • Hyperthermia for the treatment of patients with malignant germ cell tumors: A phase I/II study in ten children and adolescents with recurrent or refractory tumors
    • R. Wessalowski, H. Kruck, H. Pape, T. Kahn, R. Willers, and U. Gobel Hyperthermia for the treatment of patients with malignant germ cell tumors: a phase I/II study in ten children and adolescents with recurrent or refractory tumors Cancer 82 1998 793 800
    • (1998) Cancer , vol.82 , pp. 793-800
    • Wessalowski, R.1    Kruck, H.2    Pape, H.3    Kahn, T.4    Willers, R.5    Gobel, U.6
  • 34
    • 0037613718 scopus 로고    scopus 로고
    • A free radical initiator, 2,2′-azobis (2-aminopropane) dihydrochloride enhances hyperthermia-induced apoptosis in human uterine cervical cancer cell lines
    • H. Yuki, T. Kondo, Q.-L. Zhao, Y. Fujiwara, K. Tanabe, R. Ogawa, A. Nakashima, H. Fushiki, M. Fujimura, and S. Saito A free radical initiator, 2,2′-azobis (2-aminopropane) dihydrochloride enhances hyperthermia-induced apoptosis in human uterine cervical cancer cell lines Free Radic. Res. 37 2003 631 643
    • (2003) Free Radic. Res. , vol.37 , pp. 631-643
    • Yuki, H.1    Kondo, T.2    Zhao, Q.-L.3    Fujiwara, Y.4    Tanabe, K.5    Ogawa, R.6    Nakashima, A.7    Fushiki, H.8    Fujimura, M.9    Saito, S.10
  • 37
    • 0026731503 scopus 로고
    • Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical
    • E.E. Voest, E. van Faassen, B.S. van Asbeck, J.P. Neijt, and J.J. Marx Increased hydrogen peroxide concentration in human tumor cells due to a nitroxide free radical Biochim. Biophys. Acta 1136 1992 113 118
    • (1992) Biochim. Biophys. Acta , vol.1136 , pp. 113-118
    • Voest, E.E.1    Van Faassen, E.2    Van Asbeck, B.S.3    Neijt, J.P.4    Marx, J.J.5
  • 38
    • 0032053876 scopus 로고    scopus 로고
    • Antiproliferative effect of the piperidine nitroxide TEMPOL on neoplastic and nonneoplastic mammalian cell lines
    • M.B. Gariboldi, S. Lucchi, C. Caserini, R. Supino, C. Oliva, and E. Monti Antiproliferative effect of the piperidine nitroxide TEMPOL on neoplastic and nonneoplastic mammalian cell lines Free Radic. Biol. Med. 24 1998 913 923
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 913-923
    • Gariboldi, M.B.1    Lucchi, S.2    Caserini, C.3    Supino, R.4    Oliva, C.5    Monti, E.6
  • 39
    • 0032504176 scopus 로고    scopus 로고
    • Nitroxides tempol and tempo induce divergent signal transduction pathways in MDA-MB 231 breast cancer cells
    • S. Suy, J.B. Mitchell, D. Ehleiter, A. Haimovitz-Friedman, and U. Kasid Nitroxides tempol and tempo induce divergent signal transduction pathways in MDA-MB 231 breast cancer cells J. Biol. Chem. 273 1998 17871 17878
    • (1998) J. Biol. Chem. , vol.273 , pp. 17871-17878
    • Suy, S.1    Mitchell, J.B.2    Ehleiter, D.3    Haimovitz-Friedman, A.4    Kasid, U.5
  • 40
    • 0028967848 scopus 로고
    • Nitrone spin traps and a nitroxide antioxidant inhibit a common pathway of thymocyte apoptosis
    • A.F. Slater, C.S. Nobel, E. Maellaro, J. Bustamante, M. Kimland, and S. Orrenius Nitrone spin traps and a nitroxide antioxidant inhibit a common pathway of thymocyte apoptosis Biochem. J. 306 1995 771 778
    • (1995) Biochem. J. , vol.306 , pp. 771-778
    • Slater, A.F.1    Nobel, C.S.2    Maellaro, E.3    Bustamante, J.4    Kimland, M.5    Orrenius, S.6
  • 41
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • N. Li, K. Ragheb, G. Lawler, J. Sturgis, B. Rajwa, J.A. Melendez, and J.P. Robinson Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production J. Biol. Chem. 278 2003 8516 8525
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 42
    • 0034905658 scopus 로고    scopus 로고
    • Enhancement of hyperthermia-induced apoptosis by a free radical initiator, 2,2′-azobis (2-amidinopropane) dihydrochloride, in human histiocytic lymphoma U937 cells
    • F.-J. Li, T. Kondo, Q.-L. Zhao, K. Tanabe, R. Ogawa, M. Li, and Y. Arai Enhancement of hyperthermia-induced apoptosis by a free radical initiator, 2,2′-azobis (2-amidinopropane) dihydrochloride, in human histiocytic lymphoma U937 cells Free Radic. Res. 35 2001 281 299
    • (2001) Free Radic. Res. , vol.35 , pp. 281-299
    • Li, F.-J.1    Kondo, T.2    Zhao, Q.-L.3    Tanabe, K.4    Ogawa, R.5    Li, M.6    Arai, Y.7
  • 43
    • 0032950961 scopus 로고    scopus 로고
    • Mitochondrial and intracellular free-calcium regulation of radiation-induced apoptosis in human leukemic cells
    • Q.-L. Zhao, T. Kondo, A. Noda, and Y. Fujiwara Mitochondrial and intracellular free-calcium regulation of radiation-induced apoptosis in human leukemic cells Int. J. Radiat. Biol. 75 1999 493 504
    • (1999) Int. J. Radiat. Biol. , vol.75 , pp. 493-504
    • Zhao, Q.-L.1    Kondo, T.2    Noda, A.3    Fujiwara, Y.4
  • 44
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • J.E. Ricci, R.A. Gottlieb, and D.R. Green Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis J. Cell Biol. 160 2003 65 75
    • (2003) J. Cell Biol. , vol.160 , pp. 65-75
    • Ricci, J.E.1    Gottlieb, R.A.2    Green, D.R.3
  • 46
    • 0031423791 scopus 로고    scopus 로고
    • Dichlorodihydrofluorescein and dihydrorhodamine 123 are sensitive indicators of peroxynitrite in vitro: Implications for intracellular measurement of reactive nitrogen and oxygen species
    • J.P. Crow Dichlorodihydrofluorescein and dihydrorhodamine 123 are sensitive indicators of peroxynitrite in vitro: implications for intracellular measurement of reactive nitrogen and oxygen species Nitric Oxide 1 1997 145 157
    • (1997) Nitric Oxide , vol.1 , pp. 145-157
    • Crow, J.P.1
  • 47
    • 0032783532 scopus 로고    scopus 로고
    • Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: Comparison with 2′,7′-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123
    • S.L. Hempel, G.R. Buettner, Y.Q. O'Malley, D.A. Wessels, and D.M. Flaherty Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: comparison with 2′,7′-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123 Free Radic. Biol. Med. 27 1999 146 159
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 146-159
    • Hempel, S.L.1    Buettner, G.R.2    O'Malley, Y.Q.3    Wessels, D.A.4    Flaherty, D.M.5
  • 49
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • M.E. Anderson Determination of glutathione and glutathione disulfide in biological samples Methods Enzymol. 113 1985 548 555
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 50
    • 2942581328 scopus 로고    scopus 로고
    • Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain
    • J.E. Ricci, C. Munoz-Pinedo, P. Fitzgerald, B. Bailly-Maitre, G.A. Perkins, N. Yadava, I.E. Scheffler, M.H. Ellisman, and D.R. Green Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain Cell 117 2004 773 786
    • (2004) Cell , vol.117 , pp. 773-786
    • Ricci, J.E.1    Munoz-Pinedo, C.2    Fitzgerald, P.3    Bailly-Maitre, B.4    Perkins, G.A.5    Yadava, N.6    Scheffler, I.E.7    Ellisman, M.H.8    Green, D.R.9
  • 51
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • N.J. Waterhouse, J.C. Goldstein, O. von Ahsen, M. Schuler, D.D. Newmeyer, and D.R. Green Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process J. Cell Biol. 153 2001 319 328
    • (2001) J. Cell Biol. , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    Von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 52
    • 0032479469 scopus 로고    scopus 로고
    • The mitochondrial small heat-shock protein protects NADH: Ubiquinone oxidoreductase of the electron transport chain during heat stress in plants
    • C.A. Downs, and S.A. Heckathorn The mitochondrial small heat-shock protein protects NADH: ubiquinone oxidoreductase of the electron transport chain during heat stress in plants FEBS Lett. 430 1998 246 250
    • (1998) FEBS Lett. , vol.430 , pp. 246-250
    • Downs, C.A.1    Heckathorn, S.A.2
  • 55
    • 0037166358 scopus 로고    scopus 로고
    • Enhancement of hyperthermia-induced apoptosis by local anesthetics on human histiocytic lymphoma U937 cells
    • Y. Arai, T. Kondo, K. Tanabe, Q.-L. Zhao, F.-J. Li, R. Ogawa, M. Li, and M. Kasuya Enhancement of hyperthermia-induced apoptosis by local anesthetics on human histiocytic lymphoma U937 cells J. Biol. Chem. 277 2002 18986 18993
    • (2002) J. Biol. Chem. , vol.277 , pp. 18986-18993
    • Arai, Y.1    Kondo, T.2    Tanabe, K.3    Zhao, Q.-L.4    Li, F.-J.5    Ogawa, R.6    Li, M.7    Kasuya, M.8
  • 56
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Y. Kirichok, G. Krapivinsky, and D.E. Clapham The mitochondrial calcium uniporter is a highly selective ion channel Nature 427 2004 360 364
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 59
    • 0032054648 scopus 로고    scopus 로고
    • Severe energy impairment consequent to inactivation of mitochondrial ATP synthase as an early event in cell death: A mechanism for the selective sensitivity to H2O2 of differentiating erythroleukemia cells
    • M. Comelli, D. Londero, and I. Mavelli Severe energy impairment consequent to inactivation of mitochondrial ATP synthase as an early event in cell death: a mechanism for the selective sensitivity to H2O2 of differentiating erythroleukemia cells Free Radic. Biol. Med. 24 1998 924 932
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 924-932
    • Comelli, M.1    Londero, D.2    Mavelli, I.3
  • 60
    • 1542359582 scopus 로고    scopus 로고
    • Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis
    • K. England, C. O'Driscoll, and T.G. Cotter Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis Cell Death Differ. 11 2004 252 260
    • (2004) Cell Death Differ. , vol.11 , pp. 252-260
    • England, K.1    O'Driscoll, C.2    Cotter, T.G.3
  • 62
    • 0042164447 scopus 로고    scopus 로고
    • The selection between apoptosis and necrosis is differentially regulated in hydrogen peroxide-treated and glutathione-depleted human promonocytic cells
    • A. Troyano, P. Sancho, C. Fernandez, E. de Blas, P. Bernardi, and P. Aller The selection between apoptosis and necrosis is differentially regulated in hydrogen peroxide-treated and glutathione-depleted human promonocytic cells Cell Death Differ. 10 2003 889 898
    • (2003) Cell Death Differ. , vol.10 , pp. 889-898
    • Troyano, A.1    Sancho, P.2    Fernandez, C.3    De Blas, E.4    Bernardi, P.5    Aller, P.6
  • 63
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • M. Leist, B. Single, A.F. Castoldi, S. Kuhnle, and P. Nicotera Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis J. Exp. Med. 185 1997 1481 1486
    • (1997) J. Exp. Med. , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 65
    • 0035842896 scopus 로고    scopus 로고
    • VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release
    • M. Madesh, and G. Hajnóczky VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release J. Cell Biol. 155 2001 1003 1015
    • (2001) J. Cell Biol. , vol.155 , pp. 1003-1015
    • Madesh, M.1    Hajnóczky, G.2
  • 66
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • E. Bossy-Wetzel, D.D. Newmeyer, and D.R. Green Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization EMBO J. 17 1998 37 49
    • (1998) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 67
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • J.C. Goldstein, N.J. Waterhouse, P. Juin, G.I. Evan, and D.R. Green The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant Nat. Cell Biol. 2 2000 156 162
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1    Waterhouse, N.J.2    Juin, P.3    Evan, G.I.4    Green, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.