메뉴 건너뛰기




Volumn 1777, Issue 7-8, 2008, Pages 777-782

Complex I and energy thresholds in the brain

Author keywords

Brain mitochondria; Complex I; Metabolic control analysis; Neurodegeneration; Parkinson's disease

Indexed keywords

CYTOCHROME C OXIDASE; GLUTATHIONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 50949104833     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.05.443     Document Type: Review
Times cited : (40)

References (84)
  • 1
    • 0026584524 scopus 로고
    • Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?
    • Beal M.F. Does impairment of energy metabolism result in excitotoxic neuronal death in neurodegenerative illnesses?. Ann. Neurol. 31 2 (1992) 119-130
    • (1992) Ann. Neurol. , vol.31 , Issue.2 , pp. 119-130
    • Beal, M.F.1
  • 3
    • 0015577183 scopus 로고
    • Parkinson's disease: from brain homogenate to treatment
    • Hornykiewicz O. Parkinson's disease: from brain homogenate to treatment. Fed. Proc. 32 (1973) 183-190
    • (1973) Fed. Proc. , vol.32 , pp. 183-190
    • Hornykiewicz, O.1
  • 4
    • 0021089452 scopus 로고
    • Aetiology of Parkinson's disease
    • Calne D.B., and Langston J.W. Aetiology of Parkinson's disease. Lancet 8365 (1983) 1457-1459
    • (1983) Lancet , vol.8365 , pp. 1457-1459
    • Calne, D.B.1    Langston, J.W.2
  • 8
    • 10444243239 scopus 로고    scopus 로고
    • Mitochondrial ND5 mutations in idiopathic Parkinson's disease
    • Parker Jr. W.D., and Parks J.K. Mitochondrial ND5 mutations in idiopathic Parkinson's disease. Biochem. Biophys. Res. Commun. 326 (2005) 667-669
    • (2005) Biochem. Biophys. Res. Commun. , vol.326 , pp. 667-669
    • Parker Jr., W.D.1    Parks, J.K.2
  • 9
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney P.M., Xie J., Capaldi R.A., and Bennett Jr. J.P. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 26 (2006) 5256-5264
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett Jr., J.P.4
  • 10
    • 41749104745 scopus 로고    scopus 로고
    • Complex I deficiency in Parkinson's disease frontal cortex
    • Parker Jr. W.D., Parks J.K., and Swerdlow R.H. Complex I deficiency in Parkinson's disease frontal cortex. Brain Res. 1189 (2008) 215-218
    • (2008) Brain Res. , vol.1189 , pp. 215-218
    • Parker Jr., W.D.1    Parks, J.K.2    Swerdlow, R.H.3
  • 12
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson T.M., and Dawson V.L. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302 (2003) 819-822
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 13
    • 1542318096 scopus 로고    scopus 로고
    • Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease
    • Tretter L., Sipos I., and Adam-Vizi V. Initiation of neuronal damage by complex I deficiency and oxidative stress in Parkinson's disease. Neurochem. Res. (2004) 569-577
    • (2004) Neurochem. Res. , pp. 569-577
    • Tretter, L.1    Sipos, I.2    Adam-Vizi, V.3
  • 14
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower J.H., Chu Y., Hauser R.A., Freeman T.B., and Olanow C.W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 14 (2008) 504-506
    • (2008) Nat. Med. , vol.14 , pp. 504-506
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 15
    • 46349098565 scopus 로고    scopus 로고
    • Partial inhibition of complex I activity increases Ca(2+)-independent glutamate release rates from depolarized synaptosomes
    • (Electronic publication ahead of print)
    • Kilbride S.M., Telford J.E., Tipton K.F., and Davey G.P. Partial inhibition of complex I activity increases Ca(2+)-independent glutamate release rates from depolarized synaptosomes. J. Neurochem. (2008) (Electronic publication ahead of print)
    • (2008) J. Neurochem.
    • Kilbride, S.M.1    Telford, J.E.2    Tipton, K.F.3    Davey, G.P.4
  • 16
    • 0030707553 scopus 로고    scopus 로고
    • Threshold effects in synaptosomal and nonsynaptic mitochondria from hippocampal CA1 and paramedian neocortex brain regions
    • Davey G.P., Canevari L., and Clark J.B. Threshold effects in synaptosomal and nonsynaptic mitochondria from hippocampal CA1 and paramedian neocortex brain regions. J. Neurochem. 69 (1997) 2564-2570
    • (1997) J. Neurochem. , vol.69 , pp. 2564-2570
    • Davey, G.P.1    Canevari, L.2    Clark, J.B.3
  • 17
    • 0029873904 scopus 로고    scopus 로고
    • Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria
    • Davey G.P., and Clark J.B. Threshold effects and control of oxidative phosphorylation in nonsynaptic rat brain mitochondria. J. Neurochem. 66 (1996) 1617 24
    • (1996) J. Neurochem. , vol.66
    • Davey, G.P.1    Clark, J.B.2
  • 18
    • 0032557511 scopus 로고    scopus 로고
    • Energy thresholds in brain mitochondria: potential involvement in neurodegeneration
    • Davey G.P., Peuchen S., and Clark J.B. Energy thresholds in brain mitochondria: potential involvement in neurodegeneration. J. Biol. Chem. 273 (1998) 12753-12757
    • (1998) J. Biol. Chem. , vol.273 , pp. 12753-12757
    • Davey, G.P.1    Peuchen, S.2    Clark, J.B.3
  • 19
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • Groen A.K., Wanders R.J.A., Westerhoff H.V., van der Meer R., and Tager J.M. Quantification of the contribution of various steps to the control of mitochondrial respiration. J. Biol. Chem. 257 (1982) 2754-2757
    • (1982) J. Biol. Chem. , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.A.2    Westerhoff, H.V.3    van der Meer, R.4    Tager, J.M.5
  • 20
    • 0025952644 scopus 로고
    • Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates
    • Moreno-Sanchez R., Devars S., Lopez-Gomez F., Uribe A., and Corona N. Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates. Biochim. Biophys. Acta 1060 (1991) 284-292
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 284-292
    • Moreno-Sanchez, R.1    Devars, S.2    Lopez-Gomez, F.3    Uribe, A.4    Corona, N.5
  • 22
    • 0029853166 scopus 로고    scopus 로고
    • Factors determining the oxygen consumption rate (VO2) on-kinetics in skeletal muscles
    • Korzeniewski B., and Mazat J.P. Factors determining the oxygen consumption rate (VO2) on-kinetics in skeletal muscles. Biochem. J. 319 (1996) 143-148
    • (1996) Biochem. J. , vol.319 , pp. 143-148
    • Korzeniewski, B.1    Mazat, J.P.2
  • 23
    • 50949092375 scopus 로고    scopus 로고
    • Control of OXPHOS efficiency by complex I in brain mitochondria
    • (Electronic publication ahead of print)
    • Cocco T., Pacelli C., Sgobbo P., and Villani G. Control of OXPHOS efficiency by complex I in brain mitochondria. Neurobiol. Aging. (2008) (Electronic publication ahead of print)
    • (2008) Neurobiol. Aging.
    • Cocco, T.1    Pacelli, C.2    Sgobbo, P.3    Villani, G.4
  • 27
    • 0021106617 scopus 로고
    • Control of mitochondrial respiration. The contribution of the adenine nucleotide translocator depends on the ATP- and ADP-consuming enzymes
    • Gellerich F.N., Bohnensack R., and Kunz W. Control of mitochondrial respiration. The contribution of the adenine nucleotide translocator depends on the ATP- and ADP-consuming enzymes. Biochim. Biophys. Acta 722 (1983) 381-391
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 381-391
    • Gellerich, F.N.1    Bohnensack, R.2    Kunz, W.3
  • 28
    • 0023681888 scopus 로고
    • Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain
    • Brand M.D., Hafner R.P., and Brown G.C. Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain. Biochem. J. 255 (1988) 535-539
    • (1988) Biochem. J. , vol.255 , pp. 535-539
    • Brand, M.D.1    Hafner, R.P.2    Brown, G.C.3
  • 29
    • 0043068055 scopus 로고    scopus 로고
    • Oxidative phosphorylation by in situ synaptosomal mitochondria from whole brain of young and old rats
    • Joyce O.J., Farmer M.K., Tipton K.F., and Porter R.K. Oxidative phosphorylation by in situ synaptosomal mitochondria from whole brain of young and old rats. J. Neurochem. 86 (2003) 1032-1041
    • (2003) J. Neurochem. , vol.86 , pp. 1032-1041
    • Joyce, O.J.1    Farmer, M.K.2    Tipton, K.F.3    Porter, R.K.4
  • 31
    • 0027932783 scopus 로고
    • The kinetic basis of threshold effects observed in mitochondrial diseases: a systemic approach
    • Letellier T., Heinrich R., Malgat M., and Mazat J.P. The kinetic basis of threshold effects observed in mitochondrial diseases: a systemic approach. Biochem. J. 302 (1994) 171-174
    • (1994) Biochem. J. , vol.302 , pp. 171-174
    • Letellier, T.1    Heinrich, R.2    Malgat, M.3    Mazat, J.P.4
  • 33
    • 46349097650 scopus 로고    scopus 로고
    • 2 production and bioenergetics in rat brain synaptosomes, BBA Bioenergetics EBEC Special Edition (In Press).
    • 2 production and bioenergetics in rat brain synaptosomes, BBA Bioenergetics EBEC Special Edition (In Press).
  • 34
    • 0020308323 scopus 로고
    • Parkinson's disease: a disorder due to nigral glutathione deficiency?
    • Perry T.L., Godin D.V., and Hansen S. Parkinson's disease: a disorder due to nigral glutathione deficiency?. Neurosci. Lett. 33 (1982) 305-310
    • (1982) Neurosci. Lett. , vol.33 , pp. 305-310
    • Perry, T.L.1    Godin, D.V.2    Hansen, S.3
  • 35
    • 0022553605 scopus 로고
    • Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients
    • Perry T.L., and Yong V.W. Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients. Neurosci. Lett. 67 (1986) 269-274
    • (1986) Neurosci. Lett. , vol.67 , pp. 269-274
    • Perry, T.L.1    Yong, V.W.2
  • 38
    • 0026343403 scopus 로고
    • Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy
    • Meister A. Glutathione deficiency produced by inhibition of its synthesis, and its reversal; applications in research and therapy. Pharmacol. Ther. 51 (1991) 155-194
    • (1991) Pharmacol. Ther. , vol.51 , pp. 155-194
    • Meister, A.1
  • 40
    • 0028799706 scopus 로고
    • Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • Heales S.J.R., Davies S.E.C., Bates T.E., and Clark J.B. Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration. Neurochem. Res. 20 (1995) 31-38
    • (1995) Neurochem. Res. , vol.20 , pp. 31-38
    • Heales, S.J.R.1    Davies, S.E.C.2    Bates, T.E.3    Clark, J.B.4
  • 42
    • 0035097462 scopus 로고    scopus 로고
    • Depletion of glutathione up-regulates mitochondrial complex I expression in glial cells
    • Vásquez O.L., Almeida A., and Bolaños J.P. Depletion of glutathione up-regulates mitochondrial complex I expression in glial cells. J. Neurochem. 76 (2001) 1593-1596
    • (2001) J. Neurochem. , vol.76 , pp. 1593-1596
    • Vásquez, O.L.1    Almeida, A.2    Bolaños, J.P.3
  • 43
    • 4644327947 scopus 로고    scopus 로고
    • Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite
    • Muyderman H., Nilsson M., and Sims N.R. Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite. J. Neurosci. 24 (2004) 8019-8028
    • (2004) J. Neurosci. , vol.24 , pp. 8019-8028
    • Muyderman, H.1    Nilsson, M.2    Sims, N.R.3
  • 44
    • 0027304231 scopus 로고
    • The high sensitivity to rotenone of striatal dopamine uptake suggests the existence of a constitutive metabolic deficiency in dopaminergic neurons from the substantia nigra
    • Mary-Semper I., Gelman M., and Levi-Strauss M. The high sensitivity to rotenone of striatal dopamine uptake suggests the existence of a constitutive metabolic deficiency in dopaminergic neurons from the substantia nigra. Eur. J. Neurosci. 5 (1993) 1029-1034
    • (1993) Eur. J. Neurosci. , vol.5 , pp. 1029-1034
    • Mary-Semper, I.1    Gelman, M.2    Levi-Strauss, M.3
  • 45
    • 0029052829 scopus 로고
    • A selective toxicity toward cultured mesencephalic dopaminergic neurons is induced by the synergistic effects of energetic metabolism impairment and NMDA receptor activation
    • Mary-Semper I., Gelman M., and Levi-Strauss M. A selective toxicity toward cultured mesencephalic dopaminergic neurons is induced by the synergistic effects of energetic metabolism impairment and NMDA receptor activation. J. Neurosci. 15 (1995) 5912-5918
    • (1995) J. Neurosci. , vol.15 , pp. 5912-5918
    • Mary-Semper, I.1    Gelman, M.2    Levi-Strauss, M.3
  • 46
    • 0032535398 scopus 로고    scopus 로고
    • Thiol oxidation and loss of mitochondrial complex I precede excitatory amino acid-mediated neurodegeneration
    • Sriram K., Shankar S.K., Boyd M.R., and Ravindranath V. Thiol oxidation and loss of mitochondrial complex I precede excitatory amino acid-mediated neurodegeneration. J. Neurosci. 18 (1998) 10287-10296
    • (1998) J. Neurosci. , vol.18 , pp. 10287-10296
    • Sriram, K.1    Shankar, S.K.2    Boyd, M.R.3    Ravindranath, V.4
  • 47
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E.H., Greenamyre J.T., Liu R.M., Forman H.J., and Andersen J.K. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J. Biol. Chem. 275 (2000) 26096-26101
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6    Liu, R.M.7    Forman, H.J.8    Andersen, J.K.9
  • 48
    • 0037490142 scopus 로고    scopus 로고
    • Reversible glutathionylation of complex I increases mitochondrial superoxide formation
    • Taylor E.R., Hurrell F., Shannon R.J., Lin T.K., Hirst J., and Murphy M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 278 (2003) 19603-19610
    • (2003) J. Biol. Chem. , vol.278 , pp. 19603-19610
    • Taylor, E.R.1    Hurrell, F.2    Shannon, R.J.3    Lin, T.K.4    Hirst, J.5    Murphy, M.P.6
  • 50
    • 0021866528 scopus 로고
    • Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory chain NADH-dehydrogenase
    • Chomyn A., Mariottini P., Cleeter M.W.J., Ragan C.I., Matsuno-Yagi A., Hatefi Y., Doolite R.F., and Attardi G. Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory chain NADH-dehydrogenase. Nature 314 (1985) 592-597
    • (1985) Nature , vol.314 , pp. 592-597
    • Chomyn, A.1    Mariottini, P.2    Cleeter, M.W.J.3    Ragan, C.I.4    Matsuno-Yagi, A.5    Hatefi, Y.6    Doolite, R.F.7    Attardi, G.8
  • 51
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA codes for an NADH dehydrogenase subunit
    • Chomyn A., Cleeter M.W.J., Ragan C.I., Riley M., Doolite R.F., and Attardi G. URF6, last unidentified reading frame of human mtDNA codes for an NADH dehydrogenase subunit. Science 234 (1986) 614-618
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.J.2    Ragan, C.I.3    Riley, M.4    Doolite, R.F.5    Attardi, G.6
  • 52
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits
    • Carroll J., Shannon R.J., Fearnley I.M., Walker J.E., and Hirst J. Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits. J. Biol. Chem. 277 (2002) 50311-50317
    • (2002) J. Biol. Chem. , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 53
    • 0037009108 scopus 로고    scopus 로고
    • Import and assembly of proteins into mitochondria of mammalian cells
    • Hoogenraad N.J., Ward L.A., and Ryan M.T. Import and assembly of proteins into mitochondria of mammalian cells. Biochim. Biophys. Acta 1592 (2002) 97-105
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 97-105
    • Hoogenraad, N.J.1    Ward, L.A.2    Ryan, M.T.3
  • 54
    • 0026077298 scopus 로고
    • Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • Hofhaus G., Weiss H., and Leonard K. Electron microscopic analysis of the peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I). J. Mol. Biol. 221 (1991) 1027-1043
    • (1991) J. Mol. Biol. , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 55
    • 0031592480 scopus 로고    scopus 로고
    • Three dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • Guenebaut V., Vincentelli R., Mills D., Weiss H., and Leonard K.R. Three dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction. J. Mol. Biol. 265 (1997) 409-418
    • (1997) J. Mol. Biol. , vol.265 , pp. 409-418
    • Guenebaut, V.1    Vincentelli, R.2    Mills, D.3    Weiss, H.4    Leonard, K.R.5
  • 57
    • 0035914435 scopus 로고    scopus 로고
    • GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Fearnley I.M., Carroll J., Shannon R.J., Runswick M.J., Walker J.E., and Hirst J. GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 276 (2001) 38345-38348
    • (2001) J. Biol. Chem. , vol.276 , pp. 38345-38348
    • Fearnley, I.M.1    Carroll, J.2    Shannon, R.J.3    Runswick, M.J.4    Walker, J.E.5    Hirst, J.6
  • 58
    • 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
    • Ricci J.E., Munoz-Pinedo C., Fitzgerald P., Bailly-Maitre B., Perkins G.A., Yadava N., Scheffler I.E., Ellisman M.H., and Green D.R. 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
  • 59
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules
    • Friedrich T., and Weiss H. Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules. J. Theor. Biol. 187 (1997) 529-540
    • (1997) J. Theor. Biol. , vol.187 , pp. 529-540
    • Friedrich, T.1    Weiss, H.2
  • 60
    • 19544369483 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies
    • Ugalde C., Vogel R., Huijbens R., van der Heuvel L.P., Smeitlink J., and Nijtmans L. Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies. Hum. Mol. Genet. 13 (2004) 2461-2472
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2461-2472
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    van der Heuvel, L.P.4    Smeitlink, J.5    Nijtmans, L.6
  • 61
    • 1642451816 scopus 로고    scopus 로고
    • The gross structure of the respiratory complex I: a Lego system
    • Friedrich T., and Bottcher B. The gross structure of the respiratory complex I: a Lego system. Biochim. Biophys. Acta 1608 (2004) 1-9
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 1-9
    • Friedrich, T.1    Bottcher, B.2
  • 62
    • 34250164233 scopus 로고    scopus 로고
    • Analysis of the assembly profiles for mitochondrial and nuclear encoded subunits into complex I
    • Lazarou M., McKenzie M., Ohtake A., Thorburn D.R., and Ryan M.T. Analysis of the assembly profiles for mitochondrial and nuclear encoded subunits into complex I. Mol. Cell. Biol. 27 (2007) 4228-4237
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4228-4237
    • Lazarou, M.1    McKenzie, M.2    Ohtake, A.3    Thorburn, D.R.4    Ryan, M.T.5
  • 63
    • 34848911639 scopus 로고    scopus 로고
    • Human mitochondrial complex I assembly: a dynamic and versatile process
    • Vogel R.O., Smeitink J., and Nijtmans L. Human mitochondrial complex I assembly: a dynamic and versatile process. Biochim. Biophys. Acta 1767 (2007) 1215-1227
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1215-1227
    • Vogel, R.O.1    Smeitink, J.2    Nijtmans, L.3
  • 64
    • 34250164233 scopus 로고    scopus 로고
    • Analysis of the assembly profiles for mitochondrial and nuclear encoded subunits into complex I
    • Lazarou M., McKenzie M., Ohtake A., Thorburn D.R., and Ryan M.T. Analysis of the assembly profiles for mitochondrial and nuclear encoded subunits into complex I. Mol. Cell. Biol. 27 (2007) 4228-4237
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4228-4237
    • Lazarou, M.1    McKenzie, M.2    Ohtake, A.3    Thorburn, D.R.4    Ryan, M.T.5
  • 67
    • 27344435796 scopus 로고    scopus 로고
    • Mitochondrial complex I activity is impaired during HIV-1 induced T-cell apoptosis
    • Ladha J.S., Tripathy M.K., and Mitra D. Mitochondrial complex I activity is impaired during HIV-1 induced T-cell apoptosis. Cell Death Diff. 12 (2005) 1417-1428
    • (2005) Cell Death Diff. , vol.12 , pp. 1417-1428
    • Ladha, J.S.1    Tripathy, M.K.2    Mitra, D.3
  • 68
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock C.R., Chazotte B., and Gupte S.S. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J. Bioenerg. Biomembr. 18 (1986) 331-368
    • (1986) J. Bioenerg. Biomembr. , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 70
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schagger H., and Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19 (2000) 1777-1783
    • (2000) EMBO J. , vol.19 , pp. 1777-1783
    • Schagger, H.1    Pfeiffer, K.2
  • 71
    • 33748986546 scopus 로고    scopus 로고
    • Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation
    • Wittig I., Carrozzo R., Santorelli F.M., and Schagger H. Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation. Biochim. Biophys. Acta 1757 (2006) 1066-1072
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1066-1072
    • Wittig, I.1    Carrozzo, R.2    Santorelli, F.M.3    Schagger, H.4
  • 72
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis
    • Bianchi C., Genova M.L., Castelli G., and Lenaz G. The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis. J. Biol. Chem. 279 (2004) 36562-36569
    • (2004) J. Biol. Chem. , vol.279 , pp. 36562-36569
    • Bianchi, C.1    Genova, M.L.2    Castelli, G.3    Lenaz, G.4
  • 73
    • 4344630010 scopus 로고    scopus 로고
    • Significance of respirasomes for the assembly/stability of human respiratory chain complex I
    • Schagger H., de Coo R., Bauer M.F., Hofmann S., Godinot C., and Brandt U. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279 (2004) 36349-36353
    • (2004) J. Biol. Chem. , vol.279 , pp. 36349-36353
    • Schagger, H.1    de Coo, R.2    Bauer, M.F.3    Hofmann, S.4    Godinot, C.5    Brandt, U.6
  • 75
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schagger H., and Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J. Biol. Chem. 276 (2001) 37861-37867
    • (2001) J. Biol. Chem. , vol.276 , pp. 37861-37867
    • Schagger, H.1    Pfeiffer, K.2
  • 78
    • 0003310658 scopus 로고
    • Studies of the electron transfer system. 47. The role of phospholipids in electron transfer
    • Fleischer S., Brierley G., Klouwen H., and Slautterback D.B. Studies of the electron transfer system. 47. The role of phospholipids in electron transfer. J. Biol. Chem. 237 (1962) 3264-3272
    • (1962) J. Biol. Chem. , vol.237 , pp. 3264-3272
    • Fleischer, S.1    Brierley, G.2    Klouwen, H.3    Slautterback, D.B.4
  • 79
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain
    • Fry M., and Green D.E. Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain. J. Biol. Chem. 256 (1981) 1874-1880
    • (1981) J. Biol. Chem. , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, D.E.2
  • 80
    • 0017567464 scopus 로고
    • Lipid requirements for cytochrome c oxidase activity
    • Vik B., and Capaldi R.A. Lipid requirements for cytochrome c oxidase activity. Biochemistry 19 (1977) 5755-5759
    • (1977) Biochemistry , vol.19 , pp. 5755-5759
    • Vik, B.1    Capaldi, R.A.2
  • 82
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G., Petrosillo G., Pistolese M., and Ruggiero F.M. The effect of reactive oxygen species generated from mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett. 466 (2000) 323-326
    • (2000) FEBS Lett. , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 83
    • 0037387920 scopus 로고    scopus 로고
    • Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin
    • Petrosillo G., Ruggiero F.M., Di Venosa N., and Paradies G. Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: role of reactive oxygen species and cardiolipin. FASEB J. 17 (2003) 714-716
    • (2003) FASEB J. , vol.17 , pp. 714-716
    • Petrosillo, G.1    Ruggiero, F.M.2    Di Venosa, N.3    Paradies, G.4
  • 84
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients
    • McKenzie M., Lazarou M., Thoburn D.R., and Ryan M.T. Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J. Mol. Biol. 361 (2006) 462-469
    • (2006) J. Mol. Biol. , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thoburn, D.R.3    Ryan, M.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.