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Volumn 51, Issue 9, 2011, Pages 1621-1635

Assessing bioenergetic function in response to oxidative stress by metabolic profiling

Author keywords

4 Hydroxynonenal; Extracellular flux; Free radicals; Mitochondria; Mitochondrial profile; Nitric oxide; Oxidative stress; Oxygen consumption rate; Reserve capacity

Indexed keywords

DACTINOMYCIN; DEOXYGLUCOSE; DIPHENYLIODONIUM SALT; ETOMOXIR; HYDROGEN PEROXIDE; IODOACETIC ACID; KONINGIC ACID; OLIGOMYCIN; OXAMIC ACID;

EID: 80053614458     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.08.005     Document Type: Short Survey
Times cited : (359)

References (73)
  • 1
    • 34147159979 scopus 로고    scopus 로고
    • Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes
    • Y. Will, J. Hynes, V.I. Ogurtsov, and D.B. Papkovsky Analysis of mitochondrial function using phosphorescent oxygen-sensitive probes Nat. Protoc. 1 2006 2563 2572
    • (2006) Nat. Protoc. , vol.1 , pp. 2563-2572
    • Will, Y.1    Hynes, J.2    Ogurtsov, V.I.3    Papkovsky, D.B.4
  • 2
    • 79953180902 scopus 로고    scopus 로고
    • Assessing mitochondrial dysfunction in cells
    • M.D. Brand, and D.G. Nicholls Assessing mitochondrial dysfunction in cells Biochem. J. 435 2011 297 312
    • (2011) Biochem. J. , vol.435 , pp. 297-312
    • Brand, M.D.1    Nicholls, D.G.2
  • 3
    • 0001322362 scopus 로고
    • Continuous recording of blood oxygen tensions by polarography
    • L.C. Clark Jr., R. Wolf, D. Granger, and Z. Taylor Continuous recording of blood oxygen tensions by polarography J. Appl. Physiol. 6 1953 189 193
    • (1953) J. Appl. Physiol. , vol.6 , pp. 189-193
    • Clark, Jr.L.C.1    Wolf, R.2    Granger, D.3    Taylor, Z.4
  • 5
    • 0032104153 scopus 로고    scopus 로고
    • Oscillatory and steady laminar shear stress differentially affect human endothelial redox state: Role of a superoxide-producing NADH oxidase
    • G.W. De Keulenaer, D.C. Chappell, N. Ishizaka, R.M. Nerem, R.W. Alexander, and K.K. Griendling Oscillatory and steady laminar shear stress differentially affect human endothelial redox state: role of a superoxide-producing NADH oxidase Circ. Res. 82 1998 1094 1101 (Pubitemid 28249070)
    • (1998) Circulation Research , vol.82 , Issue.10 , pp. 1094-1101
    • De Keulenaer, G.W.1    Chappell, D.C.2    Ishizaka, N.3    Nerem, R.M.4    Wayne Alexander, R.5    Griendling, K.K.6
  • 8
    • 79955525026 scopus 로고    scopus 로고
    • Analysis of regional brain mitochondrial bioenergetics and susceptibility to mitochondrial inhibition utilizing a microplate based system
    • A. Sauerbeck, J. Pandya, I. Singh, K. Bittman, R. Readnower, G. Bing, and P. Sullivan Analysis of regional brain mitochondrial bioenergetics and susceptibility to mitochondrial inhibition utilizing a microplate based system J. Neurosci. Methods 198 2011 36 43
    • (2011) J. Neurosci. Methods , vol.198 , pp. 36-43
    • Sauerbeck, A.1    Pandya, J.2    Singh, I.3    Bittman, K.4    Readnower, R.5    Bing, G.6    Sullivan, P.7
  • 9
    • 79960712083 scopus 로고    scopus 로고
    • High throughput microplate respiratory measurements using minimal quantities of isolated mitochondria
    • G.W. Rogers, M.D. Brand, S. Petrosyan, D. Ashok, A.A. Elorza, D.A. Ferrick, and A.N. Murphy High throughput microplate respiratory measurements using minimal quantities of isolated mitochondria PLoS One 6 2011 e21746
    • (2011) PLoS One , vol.6 , pp. 21746
    • Rogers, G.W.1    Brand, M.D.2    Petrosyan, S.3    Ashok, D.4    Elorza, A.A.5    Ferrick, D.A.6    Murphy, A.N.7
  • 10
    • 34248199965 scopus 로고    scopus 로고
    • Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase
    • DOI 10.1074/jbc.M608310200
    • Y. Wu, P. Song, J. Xu, M. Zhang, and M.H. Zou Activation of protein phosphatase 2A by palmitate inhibits AMP-activated protein kinase J. Biol. Chem. 282 2007 9777 9788 (Pubitemid 47104626)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.13 , pp. 9777-9788
    • Wu, Y.1    Song, P.2    Xu, J.3    Zhang, M.4    Zou, M.-H.5
  • 11
    • 40649083487 scopus 로고    scopus 로고
    • Advances in measuring cellular bioenergetics using extracellular flux
    • D.A. Ferrick, A. Neilson, and C. Beeson Advances in measuring cellular bioenergetics using extracellular flux Drug Discov. Today 13 2008 268 274
    • (2008) Drug Discov. Today , vol.13 , pp. 268-274
    • Ferrick, D.A.1    Neilson, A.2    Beeson, C.3
  • 13
    • 0018864653 scopus 로고
    • Energy transduction in intact synaptosomes: Influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ
    • I.D. Scott, and D.G. Nicholls Energy transduction in intact synaptosomes: influence of plasma-membrane depolarization on the respiration and membrane potential of internal mitochondria determined in situ Biochem. J. 186 1980 21 33 (Pubitemid 10152072)
    • (1980) Biochemical Journal , vol.186 , Issue.1 , pp. 21-33
    • Scott, I.D.1    Nicholls, D.G.2
  • 14
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-κB and IRF3
    • DOI 10.1016/j.cell.2005.08.012, PII S0092867405008160
    • R.B. Seth, L. Sun, C.K. Ea, and Z.J. Chen Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3 Cell 122 2005 669 682 (Pubitemid 41242633)
    • (2005) Cell , vol.122 , Issue.5 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.-K.3    Chen, Z.J.4
  • 15
    • 33750475625 scopus 로고    scopus 로고
    • Free radicals, mitochondria, and oxidized lipids: The emerging role in signal transduction in vascular cells
    • DOI 10.1161/01.RES.0000248212.86638.e9, PII 0000301220061027000005
    • J. Gutierrez, S.W. Ballinger, V.M. Darley-Usmar, and A. Landar Free radicals, mitochondria, and oxidized lipids: the emerging role in signal transduction in vascular cells Circ. Res. 99 2006 924 932 (Pubitemid 44657795)
    • (2006) Circulation Research , vol.99 , Issue.9 , pp. 924-932
    • Gutierrez, J.1    Ballinger, S.W.2    Darley-Usmar, V.M.3    Landar, A.4
  • 19
    • 0344012010 scopus 로고    scopus 로고
    • Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion
    • DOI 10.1016/j.freeradbiomed.2003.08.003
    • V. Borutaite, and G.C. Brown Nitric oxide induces apoptosis via hydrogen peroxide, but necrosis via energy and thiol depletion Free Radic. Biol. Med. 35 2003 1457 1468 (Pubitemid 37452471)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.11 , pp. 1457-1468
    • Borutaite, V.1    Brown, G.C.2
  • 22
    • 33845656956 scopus 로고    scopus 로고
    • Mitochondrial retrograde signaling
    • DOI 10.1146/annurev.genet.40.110405.090613
    • Z. Liu, and R.A. Butow Mitochondrial retrograde signaling Annu. Rev. Genet. 40 2006 159 185 (Pubitemid 44956783)
    • (2006) Annual Review of Genetics , vol.40 , pp. 159-185
    • Liu, Z.1    Butow, R.A.2
  • 23
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • DOI 10.1016/S0006-291X(03)00615-6
    • L. Scorrano, and S.J. Korsmeyer Mechanisms of cytochrome c release by proapoptotic BCL-2 family members Biochem. Biophys. Res. Commun. 304 2003 437 444 (Pubitemid 36506515)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.3 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 24
    • 0037401562 scopus 로고    scopus 로고
    • Cell death regulation by the Bcl-2 protein family in the mitochondria
    • DOI 10.1002/jcp.10254
    • Y. Tsujimoto Cell death regulation by the Bcl-2 protein family in the mitochondria J. Cell. Physiol. 195 2003 158 167 (Pubitemid 36384290)
    • (2003) Journal of Cellular Physiology , vol.195 , Issue.2 , pp. 158-167
    • Tsujimoto, Y.1
  • 25
    • 33749846225 scopus 로고    scopus 로고
    • Role of Bax and Bak in mitochondrial morphogenesis
    • DOI 10.1038/nature05111, PII NATURE05111
    • M. Karbowski, K.L. Norris, M.M. Cleland, S.Y. Jeong, and R.J. Youle Role of Bax and Bak in mitochondrial morphogenesis Nature 443 2006 658 662 (Pubitemid 44564703)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 658-662
    • Karbowski, M.1    Norris, K.L.2    Cleland, M.M.3    Jeong, S.-Y.4    Youle, R.J.5
  • 27
    • 33746207800 scopus 로고    scopus 로고
    • Translocation of connexin 43 to the inner mitochondrial membrane of cardiomyocytes through the heat shock protein 90-dependent TOM pathway and its importance for cardioprotection
    • DOI 10.1161/01.RES.0000230315.56904.de, PII 0000301220060707000015
    • A. Rodriguez-Sinovas, K. Boengler, A. Cabestrero, P. Gres, M. Morente, M. Ruiz-Meana, I. Konietzka, E. Miro, A. Totzeck, G. Heusch, R. Schulz, and D. Garcia-Dorado Translocation of connexin 43 to the inner mitochondrial membrane of cardiomyocytes through the heat shock protein 90-dependent TOM pathway and its importance for cardioprotection Circ. Res. 99 2006 93 101 (Pubitemid 44297060)
    • (2006) Circulation Research , vol.99 , Issue.1 , pp. 93-101
    • Rodriguez-Sinovas, A.1    Boengler, K.2    Cabestrero, A.3    Gres, P.4    Morente, M.5    Ruiz-Meana, M.6    Konietzka, I.7    Miro, E.8    Totzeck, A.9    Heusch, G.10    Schulz, R.11    Garcia-Dorado, D.12
  • 29
    • 34147188924 scopus 로고    scopus 로고
    • Loss of ischemic preconditioning's cardioprotection in aged mouse hearts is associated with reduced gap junctional and mitochondrial levels of connexin 43
    • K. Boengler, I. Konietzka, A. Buechert, Y. Heinen, D. Garcia-Dorado, G. Heusch, and R. Schulz Loss of ischemic preconditioning's cardioprotection in aged mouse hearts is associated with reduced gap junctional and mitochondrial levels of connexin 43 Am. J. Physiol. Heart Circ. Physiol. 292 2007 H1764 H1769
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Boengler, K.1    Konietzka, I.2    Buechert, A.3    Heinen, Y.4    Garcia-Dorado, D.5    Heusch, G.6    Schulz, R.7
  • 30
    • 48749116067 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion
    • M.M. Cohen, G.P. Leboucher, N. Livnat-Levanon, M.H. Glickman, and A.M. Weissman Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion Mol. Biol. Cell 19 2008 2457 2464
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2457-2464
    • Cohen, M.M.1    Leboucher, G.P.2    Livnat-Levanon, N.3    Glickman, M.H.4    Weissman, A.M.5
  • 32
    • 67650665535 scopus 로고    scopus 로고
    • Hexokinase-mitochondrial interaction in cardiac tissue: Implications for cardiac glucose uptake, the 18FDG lumped constant and cardiac protection
    • R. Southworth Hexokinase-mitochondrial interaction in cardiac tissue: implications for cardiac glucose uptake, the 18FDG lumped constant and cardiac protection J. Bioenerg. Biomembr. 41 2009 187 193
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 187-193
    • Southworth, R.1
  • 33
    • 77950801465 scopus 로고    scopus 로고
    • Hydrogen sulfide and oxygen sensing in the cardiovascular system
    • K.R. Olson, and N.L. Whitfield Hydrogen sulfide and oxygen sensing in the cardiovascular system Antioxid. Redox Signal. 12 2010 1219 1234
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 1219-1234
    • Olson, K.R.1    Whitfield, N.L.2
  • 34
    • 77953425159 scopus 로고    scopus 로고
    • Mitochondrial therapies for Parkinson's disease
    • B. Thomas, and M.F. Beal Mitochondrial therapies for Parkinson's disease Mov. Disord. 25 2010 S155 S160
    • (2010) Mov. Disord. , vol.25
    • Thomas, B.1    Beal, M.F.2
  • 37
    • 18044383110 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cardiovascular disease
    • DOI 10.1016/j.freeradbiomed.2005.02.014
    • S.W. Ballinger Mitochondrial dysfunction in cardiovascular disease Free Radic. Biol. Med. 38 2005 1278 1295 (Pubitemid 40602831)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.10 , pp. 1278-1295
    • Ballinger, S.W.1
  • 38
    • 33947512416 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in atherosclerosis
    • DOI 10.1161/01.RES.0000258450.44413.96, PII 0000301220070302000006
    • N.R. Madamanchi, and M.S. Runge Mitochondrial dysfunction in atherosclerosis Circ. Res. 100 2007 460 473 (Pubitemid 46673256)
    • (2007) Circulation Research , vol.100 , Issue.4 , pp. 460-473
    • Madamanchi, N.R.1    Runge, M.S.2
  • 39
    • 77249126523 scopus 로고    scopus 로고
    • Mitochondrial reserve capacity in endothelial cells: The impact of nitric oxide and reactive oxygen species
    • B.P. Dranka, B.G. Hill, and V.M. Darley-Usmar Mitochondrial reserve capacity in endothelial cells: the impact of nitric oxide and reactive oxygen species Free Radic. Biol. Med. 48 2010 905 914
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 905-914
    • Dranka, B.P.1    Hill, B.G.2    Darley-Usmar, V.M.3
  • 40
    • 70350694223 scopus 로고    scopus 로고
    • Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal
    • B.G. Hill, B.P. Dranka, L. Zou, J.C. Chatham, and V.M. Darley-Usmar Importance of the bioenergetic reserve capacity in response to cardiomyocyte stress induced by 4-hydroxynonenal Biochem. J. 424 2009 99 107
    • (2009) Biochem. J. , vol.424 , pp. 99-107
    • Hill, B.G.1    Dranka, B.P.2    Zou, L.3    Chatham, J.C.4    Darley-Usmar, V.M.5
  • 41
    • 73249150574 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation
    • B.G. Hill, A.N. Higdon, B.P. Dranka, and V.M. Darley-Usmar Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation Biochim. Biophys. Acta 1797 2010 285 295
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 285-295
    • Hill, B.G.1    Higdon, A.N.2    Dranka, B.P.3    Darley-Usmar, V.M.4
  • 42
    • 77952555680 scopus 로고    scopus 로고
    • Role of cellular bioenergetics in smooth muscle cell proliferation induced by platelet-derived growth factor
    • J. Perez, B.G. Hill, G.A. Benavides, B.P. Dranka, and V.M. Darley-Usmar Role of cellular bioenergetics in smooth muscle cell proliferation induced by platelet-derived growth factor Biochem. J. 428 2010 255 267
    • (2010) Biochem. J. , vol.428 , pp. 255-267
    • Perez, J.1    Hill, B.G.2    Benavides, G.A.3    Dranka, B.P.4    Darley-Usmar, V.M.5
  • 45
    • 79957576648 scopus 로고    scopus 로고
    • Bioenergetic function in cardiovascular cells: The importance of the reserve capacity and its biological regulation
    • B.E. Sansbury, S.P. Jones, D.W. Riggs, V.M. Darley-Usmar, and B.G. Hill Bioenergetic function in cardiovascular cells: the importance of the reserve capacity and its biological regulation Chem. Biol. Interact. 191 2011 288 295
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 288-295
    • Sansbury, B.E.1    Jones, S.P.2    Riggs, D.W.3    Darley-Usmar, V.M.4    Hill, B.G.5
  • 46
    • 79953196858 scopus 로고    scopus 로고
    • Responses of hypertrophied myocytes to reactive species: Implications for glycolysis and electrophile metabolism
    • B.E. Sansbury, D.W. Riggs, R.E. Brainard, J.K. Salabei, S.P. Jones, and B.G. Hill Responses of hypertrophied myocytes to reactive species: implications for glycolysis and electrophile metabolism Biochem. J. 435 2011 519 528
    • (2011) Biochem. J. , vol.435 , pp. 519-528
    • Sansbury, B.E.1    Riggs, D.W.2    Brainard, R.E.3    Salabei, J.K.4    Jones, S.P.5    Hill, B.G.6
  • 47
    • 76549096602 scopus 로고    scopus 로고
    • Mitochondrial targeting of the electrophilic lipid 15-deoxy-Delta12,14- prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms
    • A.R. Diers, A.N. Higdon, K.C. Ricart, M.S. Johnson, A. Agarwal, B. Kalyanaraman, A. Landar, and V.M. Darley-Usmar Mitochondrial targeting of the electrophilic lipid 15-deoxy-Delta12,14-prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms Biochem. J. 426 2010 31 41
    • (2010) Biochem. J. , vol.426 , pp. 31-41
    • Diers, A.R.1    Higdon, A.N.2    Ricart, K.C.3    Johnson, M.S.4    Agarwal, A.5    Kalyanaraman, B.6    Landar, A.7    Darley-Usmar, V.M.8
  • 48
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide: Implications for neurodegenerative diseases
    • M.W. Cleeter, J.M. Cooper, V.M. Darley-Usmar, S. Moncada, and A.H. Schapira Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide: implications for neurodegenerative diseases FEBS Lett. 345 1994 50 54
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 49
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128 (Pubitemid 121003917)
    • (1991) Free Radical Biology and Medicine , vol.11 , Issue.1 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 50
    • 42449119839 scopus 로고    scopus 로고
    • 2 adduct formation with Keap1 over time: Effects on potency for intracellular antioxidant defence induction
    • DOI 10.1042/BJ20071189
    • J.Y. Oh, N. Giles, A. Landar, and V. Darley-Usmar Accumulation of 15-deoxy-delta(12,14)-prostaglandin J2 adduct formation with Keap1 over time: effects on potency for intracellular antioxidant defence induction Biochem. J. 411 2008 297 306 (Pubitemid 351580182)
    • (2008) Biochemical Journal , vol.411 , Issue.2 , pp. 297-306
    • Oh, J.Y.1    Giles, N.2    Landar, A.3    Darley-Usmar, V.4
  • 51
    • 77953752629 scopus 로고    scopus 로고
    • What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology
    • B.G. Hill, B.P. Dranka, S.M. Bailey, J.R. Lancaster Jr., and V.M. Darley-Usmar What part of NO don't you understand? Some answers to the cardinal questions in nitric oxide biology J. Biol. Chem. 285 2010 19699 19704
    • (2010) J. Biol. Chem. , vol.285 , pp. 19699-19704
    • Hill, B.G.1    Dranka, B.P.2    Bailey, S.M.3    Lancaster, Jr.J.R.4    Darley-Usmar, V.M.5
  • 52
    • 70349801984 scopus 로고    scopus 로고
    • Regulation of Nrf2-dependent gene expression by 15-deoxy-Δ12,14- prostaglandin J2
    • E. Kansanen, A.M. Kivela, and A.L. Levonen Regulation of Nrf2-dependent gene expression by 15-deoxy-Δ12,14-prostaglandin J2 Free Radic. Biol. Med. 47 2009 1310 1317
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1310-1317
    • Kansanen, E.1    Kivela, A.M.2    Levonen, A.L.3
  • 53
    • 77951240010 scopus 로고    scopus 로고
    • SH-SY5Y human neuroblastoma cell line: In vitro cell model of dopaminergic neurons in Parkinson's disease
    • H.R. Xie, L.S. Hu, and G.Y. Li SH-SY5Y human neuroblastoma cell line: in vitro cell model of dopaminergic neurons in Parkinson's disease Chin. Med. J. (Engl. Ed.) 123 2010 1086 1092
    • (2010) Chin. Med. J. (Engl. Ed.) , vol.123 , pp. 1086-1092
    • Xie, H.R.1    Hu, L.S.2    Li, G.Y.3
  • 55
    • 1642396537 scopus 로고    scopus 로고
    • Role of Nrf2 in the Regulation of CD36 and Stress Protein Expression in Murine Macrophages: Activation by Oxidatively Modified LDL and 4-Hydroxynonenal
    • DOI 10.1161/01.RES.0000119171.44657.45
    • T. Ishii, K. Itoh, E. Ruiz, D.S. Leake, H. Unoki, M. Yamamoto, and G.E. Mann Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: activation by oxidatively modified LDL and 4-hydroxynonenal Circ. Res. 94 2004 609 616 (Pubitemid 38387743)
    • (2004) Circulation Research , vol.94 , Issue.5 , pp. 609-616
    • Ishii, T.1    Itoh, K.2    Ruiz, E.3    Leake, D.S.4    Unoki, H.5    Yamamoto, M.6    Mann, G.E.7
  • 56
    • 21344473623 scopus 로고    scopus 로고
    • HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells
    • DOI 10.1016/j.freeradbiomed.2005.03.026, PII S0891584905001681
    • K.E. Iles, D.A. Dickinson, A.F. Wigley, N.E. Welty, V. Blank, and H.J. Forman HNE increases HO-1 through activation of the ERK pathway in pulmonary epithelial cells Free Radic. Biol. Med. 39 2005 355 364 (Pubitemid 40910192)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.3 , pp. 355-364
    • Iles, K.E.1    Dickinson, D.A.2    Wigley, A.F.3    Welty, N.E.4    Blank, V.5    Forman, H.J.6
  • 57
    • 3543030406 scopus 로고    scopus 로고
    • In Situ respiration and bioenergetic status of mitochondria in primary cerebellar granule neuronal cultures exposed continuously to glutamate
    • DOI 10.1074/jbc.M401540200
    • M.B. Jekabsons, and D.G. Nicholls In situ respiration and bioenergetic status of mitochondria in primary cerebellar granule neuronal cultures exposed continuously to glutamate J. Biol. Chem. 279 2004 32989 33000 (Pubitemid 39014759)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32989-33000
    • Jekabsons, M.B.1    Nicholls, D.G.2
  • 59
    • 65649092131 scopus 로고    scopus 로고
    • Bioenergetic analysis of isolated cerebrocortical nerve terminals on a microgram scale: Spare respiratory capacity and stochastic mitochondrial failure
    • S.W. Choi, A.A. Gerencser, and D.G. Nicholls Bioenergetic analysis of isolated cerebrocortical nerve terminals on a microgram scale: spare respiratory capacity and stochastic mitochondrial failure J. Neurochem. 109 2009 1179 1191
    • (2009) J. Neurochem. , vol.109 , pp. 1179-1191
    • Choi, S.W.1    Gerencser, A.A.2    Nicholls, D.G.3
  • 60
    • 0037443672 scopus 로고    scopus 로고
    • Variations in spare electron transport chain capacity: The answer to an old riddle?
    • DOI 10.1002/jnr.10553
    • R. Fern Variations in spare electron transport chain capacity: the answer to an old riddle? J. Neurosci. Res. 71 2003 759 762 (Pubitemid 36292994)
    • (2003) Journal of Neuroscience Research , vol.71 , Issue.6 , pp. 759-762
    • Fern, R.1
  • 61
    • 0015621219 scopus 로고
    • Fluorocitrate inhibition of aconitate hydratase and the tricarboxylate carrier of rat liver mitochondria
    • M.D. Brand, S.M. Evans, J. Mendes-Mourao, and J.B. Chappell Fluorocitrate inhibition of aconitate hydratase and the tricarboxylate carrier of rat liver mitochondria Biochem. J. 134 1973 217 224
    • (1973) Biochem. J. , vol.134 , pp. 217-224
    • Brand, M.D.1    Evans, S.M.2    Mendes-Mourao, J.3    Chappell, J.B.4
  • 64
    • 55249118618 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation is regulated by fructose 1,6-bisphosphate: A possible role in Crabtree effect induction?
    • R. Diaz-Ruiz, N. Averet, D. Araiza, B. Pinson, S. Uribe-Carvajal, A. Devin, and M. Rigoulet Mitochondrial oxidative phosphorylation is regulated by fructose 1,6-bisphosphate: a possible role in Crabtree effect induction? J. Biol. Chem. 283 2008 26948 26955
    • (2008) J. Biol. Chem. , vol.283 , pp. 26948-26955
    • Diaz-Ruiz, R.1    Averet, N.2    Araiza, D.3    Pinson, B.4    Uribe-Carvajal, S.5    Devin, A.6    Rigoulet, M.7
  • 65
    • 79955601028 scopus 로고    scopus 로고
    • Inhibition of fatty acid oxidation by etomoxir impairs NADPH production and increases reactive oxygen species resulting in ATP depletion and cell death in human glioblastoma cells
    • L.S. Pike, A.L. Smift, N.J. Croteau, D.A. Ferrick, and M. Wu Inhibition of fatty acid oxidation by etomoxir impairs NADPH production and increases reactive oxygen species resulting in ATP depletion and cell death in human glioblastoma cells Biochim. Biophys. Acta 1807 2011 726 734
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 726-734
    • Pike, L.S.1    Smift, A.L.2    Croteau, N.J.3    Ferrick, D.A.4    Wu, M.5
  • 66
    • 0021040819 scopus 로고
    • Compartmentation of glycolytic and glycogenolytic metabolism in vascular smooth muscle
    • R.M. Lynch, and R.J. Paul Compartmentation of glycolytic and glycogenolytic metabolism in vascular smooth muscle Science 222 1983 1344 1346 (Pubitemid 14204707)
    • (1983) Science , vol.222 , Issue.4630 , pp. 1344-1346
    • Lynch, R.M.1    Paul, R.J.2
  • 67
    • 54049155807 scopus 로고    scopus 로고
    • The metabolic basis of vascular oxygen sensing: Diversity, compartmentalization, and lessons from cancer
    • E.D. Michelakis, and E.K. Weir The metabolic basis of vascular oxygen sensing: diversity, compartmentalization, and lessons from cancer Am. J. Physiol. Heart Circ. Physiol. 295 2008 H928 H930
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.295
    • Michelakis, E.D.1    Weir, E.K.2
  • 69
    • 0026029166 scopus 로고
    • Identification of koningic acid (heptelidic acid)-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase
    • K. Sakai, K. Hasumi, and A. Endo Identification of koningic acid (heptelidic acid)-modified site in rabbit muscle glyceraldehyde-3-phosphate dehydrogenase Biochim. Biophys. Acta 1077 1991 192 196
    • (1991) Biochim. Biophys. Acta , vol.1077 , pp. 192-196
    • Sakai, K.1    Hasumi, K.2    Endo, A.3
  • 70
    • 0021934322 scopus 로고
    • Specific inhibition of glyceraldehyde-3-phosphate dehydrogenase by koningic acid (heptelidic acid)
    • A. Endo, K. Hasumi, K. Sakai, and T. Kanbe Specific inhibition of glyceraldehyde-3-phosphate dehydrogenase by koningic acid (heptelidic acid) J. Antibiot. (Tokyo) 38 1985 920 925 (Pubitemid 15236245)
    • (1985) Journal of Antibiotics , vol.38 , Issue.7 , pp. 920-925
    • Endo, A.1    Hasumi, K.2    Sakai, K.3    Kanbe, T.4
  • 73
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: Mortality and millivolts
    • DOI 10.1016/S0166-2236(99)01534-9, PII S0166223699015349
    • D.G. Nicholls, and M.W. Ward Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts Trends Neurosci. 23 2000 166 174 (Pubitemid 30151213)
    • (2000) Trends in Neurosciences , vol.23 , Issue.4 , pp. 166-174
    • Nicholls, D.G.1    Ward, M.W.2


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