메뉴 건너뛰기




Volumn 19, Issue 1, 2013, Pages 61-69

Complex I deficiencies in neurological disorders

Author keywords

CAMP PKA signaling; Down syndrome; Mitochondrial biogenesis; Mitochondrial disease; Mitochondrial ROS balance; Neurological disorders; Parkinson disease; Respiratory complex I

Indexed keywords

CYCLIC AMP; HEAT SHOCK PROTEIN 70; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; REACTIVE OXYGEN METABOLITE; SIRTUIN 1; SIRTUIN 3; SIRTUIN 4; SIRTUIN 5;

EID: 84871717112     PISSN: 14714914     EISSN: 1471499X     Source Type: Journal    
DOI: 10.1016/j.molmed.2012.11.005     Document Type: Review
Times cited : (62)

References (85)
  • 1
    • 84859903797 scopus 로고    scopus 로고
    • The oxidative phosphorylation system in mammalian mitochondria
    • Papa S., et al. The oxidative phosphorylation system in mammalian mitochondria. Adv. Exp. Med. Biol. 2012, 942:3-37.
    • (2012) Adv. Exp. Med. Biol. , vol.942 , pp. 3-37
    • Papa, S.1
  • 2
    • 36549046060 scopus 로고    scopus 로고
    • Regulation of mitochondrial oxidative phosphorylation through cell signalling
    • Hüttemann M., et al. Regulation of mitochondrial oxidative phosphorylation through cell signalling. Biochim. Biophys. Acta 2007, 1773:1701-1720.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1701-1720
    • Hüttemann, M.1
  • 3
    • 80052097536 scopus 로고    scopus 로고
    • Respiratory complex I: 'steam engine' of the cell?
    • Efremov R.G., Sazanov L.A. Respiratory complex I: 'steam engine' of the cell?. Curr. Opin. Struct. Biol. 2011, 4:532-540.
    • (2011) Curr. Opin. Struct. Biol. , vol.4 , pp. 532-540
    • Efremov, R.G.1    Sazanov, L.A.2
  • 4
    • 84859886931 scopus 로고    scopus 로고
    • Mitochondria and reactive oxygen species. Which role in physiology and pathology?
    • Lenaz G. Mitochondria and reactive oxygen species. Which role in physiology and pathology?. Adv. Exp. Med. Biol. 2012, 942:93-136.
    • (2012) Adv. Exp. Med. Biol. , vol.942 , pp. 93-136
    • Lenaz, G.1
  • 5
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • Dröse S., Brandt U. Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. Adv. Exp. Med. Biol. 2012, 748:145-169.
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 145-169
    • Dröse, S.1    Brandt, U.2
  • 6
    • 33751574953 scopus 로고    scopus 로고
    • Bovine complex I is a complex of 45 different subunits
    • Carroll J., et al. Bovine complex I is a complex of 45 different subunits. J. Biol. Chem. 2006, 281:32724-32727.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32724-32727
    • Carroll, J.1
  • 7
    • 84865771586 scopus 로고    scopus 로고
    • NDUFA4 is a subunit of complex IV of the mammalian electron transport chain
    • Balsa E., et al. NDUFA4 is a subunit of complex IV of the mammalian electron transport chain. Cell Metab. 2012, 16:378-386.
    • (2012) Cell Metab. , vol.16 , pp. 378-386
    • Balsa, E.1
  • 8
    • 0242414752 scopus 로고    scopus 로고
    • Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex I affect the expression of the protein and the assembly and function of the complex
    • Scacco S., et al. Pathological mutations of the human NDUFS4 gene of the 18-kDa (AQDQ) subunit of complex I affect the expression of the protein and the assembly and function of the complex. J. Biol. Chem. 2003, 278:44161-44167.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44161-44167
    • Scacco, S.1
  • 9
    • 39049110244 scopus 로고    scopus 로고
    • Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly
    • Yadava N., et al. Investigations of the potential effects of phosphorylation of the MWFE and ESSS subunits on complex I activity and assembly. Int. J. Biochem. Cell Biol. 2008, 40:447-460.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 447-460
    • Yadava, N.1
  • 10
    • 84860697620 scopus 로고    scopus 로고
    • Understanding mitochondrial complex I assembly in health and disease
    • Mimaki M., et al. Understanding mitochondrial complex I assembly in health and disease. Biochim. Biophys. Acta 2012, 1817:851-862.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 851-862
    • Mimaki, M.1
  • 11
    • 77953810111 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase regulates post-translational processing and expression of complex I subunits in mammalian cells
    • Papa S., et al. cAMP-dependent protein kinase regulates post-translational processing and expression of complex I subunits in mammalian cells. Biochim. Biophys. Acta 2010, 1797:649-658.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 649-658
    • Papa, S.1
  • 12
    • 77955413685 scopus 로고    scopus 로고
    • Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain
    • De Rasmo D., et al. Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain. Mitochondrion 2010, 10:464-471.
    • (2010) Mitochondrion , vol.10 , pp. 464-471
    • De Rasmo, D.1
  • 13
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn B.H., et al. A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:14447-14452.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14447-14452
    • Ahn, B.H.1
  • 14
    • 54049146740 scopus 로고    scopus 로고
    • Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage
    • Hurd T.R., et al. Complex I within oxidatively stressed bovine heart mitochondria is glutathionylated on Cys-531 and Cys-704 of the 75-kDa subunit: potential role of CYS residues in decreasing oxidative damage. J. Biol. Chem. 2008, 283:24801-24815.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24801-24815
    • Hurd, T.R.1
  • 15
    • 65449188311 scopus 로고    scopus 로고
    • Pathogenetic mechanisms in hereditary dysfunctions of complex I of the respiratory chain in neurological diseases
    • Papa S., et al. Pathogenetic mechanisms in hereditary dysfunctions of complex I of the respiratory chain in neurological diseases. Biochim. Biophys. Acta 2009, 1787:502-517.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 502-517
    • Papa, S.1
  • 16
    • 33746326475 scopus 로고    scopus 로고
    • CAMP controls oxygen metabolism in mammalian cells
    • Piccoli C., et al. cAMP controls oxygen metabolism in mammalian cells. FEBS Lett. 2006, 580:4539-4543.
    • (2006) FEBS Lett. , vol.580 , pp. 4539-4543
    • Piccoli, C.1
  • 17
    • 84858057118 scopus 로고    scopus 로고
    • Mitochondrial complex I plays an essential role in human respirasome assembly
    • Moreno-Lastres D., et al. Mitochondrial complex I plays an essential role in human respirasome assembly. Cell Metab. 2012, 15:324-335.
    • (2012) Cell Metab. , vol.15 , pp. 324-335
    • Moreno-Lastres, D.1
  • 18
    • 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., et al. Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. Cell 2004, 117:773-786.
    • (2004) Cell , vol.117 , pp. 773-786
    • Ricci, J.E.1
  • 19
    • 77950371493 scopus 로고    scopus 로고
    • Mitochondrial bioenergetics and dynamics interplay in complex I-deficient fibroblasts
    • Morán M., et al. Mitochondrial bioenergetics and dynamics interplay in complex I-deficient fibroblasts. Biochim. Biophys. Acta 2010, 1802:443-453.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 443-453
    • Morán, M.1
  • 20
    • 0030581498 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
    • Papa S. Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications. Biochim. Biophys. Acta 1996, 1276:87-105.
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 87-105
    • Papa, S.1
  • 21
    • 84871821553 scopus 로고    scopus 로고
    • Proteolytic control of mitochondrial function and morphogenesis
    • in press, doi:10.1016/j.bbamcr.2012.06.025
    • Anand, R. et al. (2012) Proteolytic control of mitochondrial function and morphogenesis. Biochim. Biophys. Acta (in press) doi:10.1016/j.bbamcr.2012.06.025.
    • (2012) Biochim. Biophys. Acta
    • Anand, R.1
  • 22
    • 78650867108 scopus 로고    scopus 로고
    • The β-adrenoceptor agonist isoproterenol promotes the activity of respiratory chain complex I and lowers cellular reactive oxygen species in fibroblasts and heart myoblasts
    • De Rasmo D., et al. The β-adrenoceptor agonist isoproterenol promotes the activity of respiratory chain complex I and lowers cellular reactive oxygen species in fibroblasts and heart myoblasts. Eur. J. Pharmacol. 2011, 652:15-22.
    • (2011) Eur. J. Pharmacol. , vol.652 , pp. 15-22
    • De Rasmo, D.1
  • 23
    • 79954497176 scopus 로고    scopus 로고
    • Deficit of complex I activity in human skin fibroblasts with chromosome 21 trisomy and overproduction of reactive oxygen species by mitochondria: involvement of the cAMP/PKA signalling pathway
    • Valenti D., et al. Deficit of complex I activity in human skin fibroblasts with chromosome 21 trisomy and overproduction of reactive oxygen species by mitochondria: involvement of the cAMP/PKA signalling pathway. Biochem. J. 2011, 435:679-688.
    • (2011) Biochem. J. , vol.435 , pp. 679-688
    • Valenti, D.1
  • 24
    • 84856228626 scopus 로고    scopus 로고
    • Activation of the cAMP cascade in human fibroblast cultures rescues the activity of oxidatively damaged complex I
    • De Rasmo D., et al. Activation of the cAMP cascade in human fibroblast cultures rescues the activity of oxidatively damaged complex I. Free Radic. Biol. Med. 2012, 52:757-764.
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 757-764
    • De Rasmo, D.1
  • 25
    • 33749469540 scopus 로고    scopus 로고
    • Occurrence of A kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria
    • Sardanelli A.M., et al. Occurrence of A kinase anchor protein and associated cAMP-dependent protein kinase in the inner compartment of mammalian mitochondria. FEBS Lett. 2006, 580:5690-5696.
    • (2006) FEBS Lett. , vol.580 , pp. 5690-5696
    • Sardanelli, A.M.1
  • 26
    • 0037070143 scopus 로고    scopus 로고
    • Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria
    • Signorile A., et al. Serine (threonine) phosphatase(s) acting on cAMP-dependent phosphoproteins in mammalian mitochondria. FEBS Lett. 2002, 512:91-94.
    • (2002) FEBS Lett. , vol.512 , pp. 91-94
    • Signorile, A.1
  • 27
    • 77953567491 scopus 로고    scopus 로고
    • Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects
    • Acin-Perez R., et al. Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects. EMBO Mol. Med. 2009, 1:392-406.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 392-406
    • Acin-Perez, R.1
  • 28
    • 80052219693 scopus 로고    scopus 로고
    • A phosphodiesterase 2A isoform localized to mitochondria regulates respiration
    • Acin-Perez R., et al. A phosphodiesterase 2A isoform localized to mitochondria regulates respiration. J. Biol. Chem. 2011, 286:30423-30432.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30423-30432
    • Acin-Perez, R.1
  • 29
    • 84859208807 scopus 로고    scopus 로고
    • Mitochondrial CB(1) receptors regulate neuronal energy metabolism
    • Bénard G., et al. Mitochondrial CB(1) receptors regulate neuronal energy metabolism. Nat. Neurosci. 2012, 15:558-564.
    • (2012) Nat. Neurosci. , vol.15 , pp. 558-564
    • Bénard, G.1
  • 30
    • 39849104755 scopus 로고    scopus 로고
    • CAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I
    • De Rasmo D., et al. cAMP-dependent protein kinase regulates the mitochondrial import of the nuclear encoded NDUFS4 subunit of complex I. Cell. Signal. 2008, 20:989-997.
    • (2008) Cell. Signal. , vol.20 , pp. 989-997
    • De Rasmo, D.1
  • 31
    • 0038482043 scopus 로고    scopus 로고
    • Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70
    • Robin M.A., et al. Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70. J. Biol. Chem. 2003, 278:18960-18970.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18960-18970
    • Robin, M.A.1
  • 32
    • 24144463983 scopus 로고    scopus 로고
    • Metabolic control through the PGC-1 family of transcription coactivators
    • Lin J., et al. Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab. 2005, 1:361-370.
    • (2005) Cell Metab. , vol.1 , pp. 361-370
    • Lin, J.1
  • 33
    • 79955469432 scopus 로고    scopus 로고
    • Mitochondrial dynamic remodeling in strenuous exercise-induced muscle and mitochondrial dysfunction: regulatory effects of hydroxytyrosol
    • Feng Z., et al. Mitochondrial dynamic remodeling in strenuous exercise-induced muscle and mitochondrial dysfunction: regulatory effects of hydroxytyrosol. Free Radic. Biol. Med. 2011, 50:1437-1446.
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 1437-1446
    • Feng, Z.1
  • 34
    • 84855994224 scopus 로고    scopus 로고
    • A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction
    • Fusco S., et al. A role for neuronal cAMP responsive-element binding (CREB)-1 in brain responses to calorie restriction. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:621-626.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 621-626
    • Fusco, S.1
  • 35
    • 33645011201 scopus 로고    scopus 로고
    • Nuclear control of respiratory gene expression in mammalian cells
    • Scarpulla R.C. Nuclear control of respiratory gene expression in mammalian cells. J. Cell. Biochem. 2006, 97:673-683.
    • (2006) J. Cell. Biochem. , vol.97 , pp. 673-683
    • Scarpulla, R.C.1
  • 36
    • 25444515720 scopus 로고    scopus 로고
    • Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons
    • Ryu H., et al. Antioxidants modulate mitochondrial PKA and increase CREB binding to D-loop DNA of the mitochondrial genome in neurons. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:13915-13920.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 13915-13920
    • Ryu, H.1
  • 37
    • 68749094302 scopus 로고    scopus 로고
    • CAMP response element-binding protein (CREB) is imported into mitochondria and promotes protein synthesis
    • De Rasmo D., et al. cAMP response element-binding protein (CREB) is imported into mitochondria and promotes protein synthesis. FEBS J. 2009, 276:4325-4333.
    • (2009) FEBS J. , vol.276 , pp. 4325-4333
    • De Rasmo, D.1
  • 38
    • 79958206937 scopus 로고    scopus 로고
    • Franklin H. Epstein Lecture: Sirtuins, aging, and medicine
    • Guarente L. Franklin H. Epstein Lecture: Sirtuins, aging, and medicine. N. Engl. J. Med. 2011, 364:2235-2244.
    • (2011) N. Engl. J. Med. , vol.364 , pp. 2235-2244
    • Guarente, L.1
  • 39
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha
    • Jager S., et al. AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1alpha. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:12017-12022.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12017-12022
    • Jager, S.1
  • 40
    • 84255198350 scopus 로고    scopus 로고
    • The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD(+)
    • Gerhart-Hines Z., et al. The cAMP/PKA pathway rapidly activates SIRT1 to promote fatty acid oxidation independently of changes in NAD(+). Mol. Cell 2011, 44:851-863.
    • (2011) Mol. Cell , vol.44 , pp. 851-863
    • Gerhart-Hines, Z.1
  • 41
    • 77954353059 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha) and sirtuin 1 (SIRT1) reside in mitochondria: possible direct function in mitochondrial biogenesis
    • Aquilano K., et al. Peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha) and sirtuin 1 (SIRT1) reside in mitochondria: possible direct function in mitochondrial biogenesis. J. Biol. Chem. 2010, 285:21590-21599.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21590-21599
    • Aquilano, K.1
  • 42
    • 60749090581 scopus 로고    scopus 로고
    • The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies
    • Maalouf M., et al. The neuroprotective properties of calorie restriction, the ketogenic diet, and ketone bodies. Brain Res. Rev. 2009, 59:293-315.
    • (2009) Brain Res. Rev. , vol.59 , pp. 293-315
    • Maalouf, M.1
  • 43
    • 84863011114 scopus 로고    scopus 로고
    • Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases
    • Park S.J., et al. Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. Cell 2012, 148:421-433.
    • (2012) Cell , vol.148 , pp. 421-433
    • Park, S.J.1
  • 44
    • 77953807035 scopus 로고    scopus 로고
    • Hydroxytyrosol promotes mitochondrial biogenesis and mitochondrial function in 3T3-L1 adipocytes
    • Hao J., et al. Hydroxytyrosol promotes mitochondrial biogenesis and mitochondrial function in 3T3-L1 adipocytes. J. Nutr. Biochem. 2010, 21:634-644.
    • (2010) J. Nutr. Biochem. , vol.21 , pp. 634-644
    • Hao, J.1
  • 45
    • 84855687153 scopus 로고    scopus 로고
    • Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease
    • Sheng B., et al. Impaired mitochondrial biogenesis contributes to mitochondrial dysfunction in Alzheimer's disease. J. Neurochem. 2012, 120:419-429.
    • (2012) J. Neurochem. , vol.120 , pp. 419-429
    • Sheng, B.1
  • 46
    • 57449084690 scopus 로고    scopus 로고
    • Mitochondrial complex I dysfunction in rat heart with aging: critical role of reactive oxygen species and cardiolipin
    • Petrosillo G., et al. Mitochondrial complex I dysfunction in rat heart with aging: critical role of reactive oxygen species and cardiolipin. Free Radic. Biol. Med. 2009, 46:88-94.
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 88-94
    • Petrosillo, G.1
  • 47
    • 80052092729 scopus 로고    scopus 로고
    • The molecular basis of human complex I deficiency
    • Tucker E.J., et al. The molecular basis of human complex I deficiency. IUBMB Life 2011, 63:669-677.
    • (2011) IUBMB Life , vol.63 , pp. 669-677
    • Tucker, E.J.1
  • 48
    • 65249126910 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency: from organelle dysfunction to clinical disease
    • Distelmaier F., et al. Mitochondrial complex I deficiency: from organelle dysfunction to clinical disease. Brain 2009, 132:833-842.
    • (2009) Brain , vol.132 , pp. 833-842
    • Distelmaier, F.1
  • 49
    • 17344365132 scopus 로고    scopus 로고
    • Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit
    • van den Heuvel L., et al. Demonstration of a new pathogenic mutation in human complex I deficiency: a 5-bp duplication in the nuclear gene encoding the 18-kD (AQDQ) subunit. Am. J. Hum. Genet. 1998, 62:262-268.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 262-268
    • van den Heuvel, L.1
  • 50
    • 84855606038 scopus 로고    scopus 로고
    • A novel mutation in NDUFS4 causes Leigh syndrome in an Ashkenazi Jewish family
    • Anderson S.L., et al. A novel mutation in NDUFS4 causes Leigh syndrome in an Ashkenazi Jewish family. J. Inherit. Metab. Dis. 2008, 31(Suppl. 2):S461-S467.
    • (2008) J. Inherit. Metab. Dis. , vol.31 , Issue.SUPPL. 2
    • Anderson, S.L.1
  • 51
    • 84859359272 scopus 로고    scopus 로고
    • A constant and similar assembly defect of mitochondrial respiratory chain complex I allows rapid identification of NDUFS4 mutations in patients with Leigh syndrome
    • Assouline Z., et al. A constant and similar assembly defect of mitochondrial respiratory chain complex I allows rapid identification of NDUFS4 mutations in patients with Leigh syndrome. Biochim. Biophys. Acta 2012, 1822:1062-1069.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1062-1069
    • Assouline, Z.1
  • 52
    • 84862001736 scopus 로고    scopus 로고
    • Proteomic and metabolomic analyses of mitochondrial complex I-deficient mouse model generated by spontaneous B2 short interspersed nuclear element (SINE) insertion into NADH dehydrogenase (ubiquinone) Fe-S protein 4 (Ndufs4) gene
    • Leong D.W., et al. Proteomic and metabolomic analyses of mitochondrial complex I-deficient mouse model generated by spontaneous B2 short interspersed nuclear element (SINE) insertion into NADH dehydrogenase (ubiquinone) Fe-S protein 4 (Ndufs4) gene. J. Biol. Chem. 2012, 287:20652-20663.
    • (2012) J. Biol. Chem. , vol.287 , pp. 20652-20663
    • Leong, D.W.1
  • 53
    • 84864701822 scopus 로고    scopus 로고
    • Metabolic consequences of NDUFS4 gene deletion in immortalized mouse embryonic fibroblasts
    • Valsecchi F., et al. Metabolic consequences of NDUFS4 gene deletion in immortalized mouse embryonic fibroblasts. Biochim. Biophys. Acta 2012, 1817:1925-1936.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 1925-1936
    • Valsecchi, F.1
  • 54
    • 83455169110 scopus 로고    scopus 로고
    • Mitochondrial complex III stabilizes complex I in the absence of NDUFS4 to provide partial activity
    • Calvaruso M.A., et al. Mitochondrial complex III stabilizes complex I in the absence of NDUFS4 to provide partial activity. Hum. Mol. Genet. 2012, 21:115-120.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 115-120
    • Calvaruso, M.A.1
  • 55
    • 41449089840 scopus 로고    scopus 로고
    • Mice with mitochondrial complex I deficiency develop a fatal encephalomyopathy
    • Kruse S.E., et al. Mice with mitochondrial complex I deficiency develop a fatal encephalomyopathy. Cell Metab. 2008, 7:312-320.
    • (2008) Cell Metab. , vol.7 , pp. 312-320
    • Kruse, S.E.1
  • 56
    • 84856976662 scopus 로고    scopus 로고
    • Altered dopamine metabolism and increased vulnerability to MPTP in mice with partial deficiency of mitochondrial complex I in dopamine neurons
    • Sterky F.H., et al. Altered dopamine metabolism and increased vulnerability to MPTP in mice with partial deficiency of mitochondrial complex I in dopamine neurons. Hum. Mol. Genet. 2012, 21:1078-1089.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1078-1089
    • Sterky, F.H.1
  • 57
    • 77954638436 scopus 로고    scopus 로고
    • Complex I deficiency due to loss of Ndufs4 in the brain results in progressive encephalopathy resembling Leigh syndrome
    • Quintana A., et al. Complex I deficiency due to loss of Ndufs4 in the brain results in progressive encephalopathy resembling Leigh syndrome. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:10996-11001.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 10996-11001
    • Quintana, A.1
  • 58
    • 84871021675 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress due to complex I dysfunction promotes fibroblast activation and melanoma cell invasiveness
    • Taddei M.L., et al. Mitochondrial oxidative stress due to complex I dysfunction promotes fibroblast activation and melanoma cell invasiveness. J. Signal Transduct. 2012, 2012:684592.
    • (2012) J. Signal Transduct. , vol.2012 , pp. 684592
    • Taddei, M.L.1
  • 59
    • 77954862456 scopus 로고    scopus 로고
    • Molecular and clinical prodrome of Parkinson disease: implications for treatment
    • Schapira A.H., Tolosa E. Molecular and clinical prodrome of Parkinson disease: implications for treatment. Nat. Rev. Neurol. 2010, 6:309-317.
    • (2010) Nat. Rev. Neurol. , vol.6 , pp. 309-317
    • Schapira, A.H.1    Tolosa, E.2
  • 60
    • 54449089025 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibition is not required for dopaminergic neuron death induced by rotenone, MPP+, or paraquat
    • Choi W.S., et al. Mitochondrial complex I inhibition is not required for dopaminergic neuron death induced by rotenone, MPP+, or paraquat. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:15136-15141.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 15136-15141
    • Choi, W.S.1
  • 61
    • 79952368703 scopus 로고    scopus 로고
    • Loss of mitochondrial complex I activity potentiates dopamine neuron death induced by microtubule dysfunction in a Parkinson's disease model
    • Choi W.S., et al. Loss of mitochondrial complex I activity potentiates dopamine neuron death induced by microtubule dysfunction in a Parkinson's disease model. J. Cell Biol. 2011, 192:873-882.
    • (2011) J. Cell Biol. , vol.192 , pp. 873-882
    • Choi, W.S.1
  • 62
    • 77957905690 scopus 로고    scopus 로고
    • Genetic analysis of pathways to Parkinson disease
    • Hardy J. Genetic analysis of pathways to Parkinson disease. Neuron 2010, 68:201-206.
    • (2010) Neuron , vol.68 , pp. 201-206
    • Hardy, J.1
  • 63
    • 76949107596 scopus 로고    scopus 로고
    • Mitochondrial respiratory dysfunction and mutations in mitochondrial DNA in PINK1 familial parkinsonism
    • Papa S., et al. Mitochondrial respiratory dysfunction and mutations in mitochondrial DNA in PINK1 familial parkinsonism. J. Bioenerg. Biomembr. 2009, 41:509-516.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 509-516
    • Papa, S.1
  • 64
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente E.M., Abou-Sleiman P.M. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 2004, 304:1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2
  • 65
    • 51849137779 scopus 로고    scopus 로고
    • Coexistence of mutations in PINK1 and mitochondrial DNA in early onset parkinsonism
    • Piccoli C., et al. Coexistence of mutations in PINK1 and mitochondrial DNA in early onset parkinsonism. J. Med. Genet. 2008, 45:596-602.
    • (2008) J. Med. Genet. , vol.45 , pp. 596-602
    • Piccoli, C.1
  • 66
    • 56349137588 scopus 로고    scopus 로고
    • Mitochondrial respiratory dysfunction in familiar parkinsonism associated with PINK1 mutation
    • Piccoli C., et al. Mitochondrial respiratory dysfunction in familiar parkinsonism associated with PINK1 mutation. Neurochem. Res. 2008, 33:2565-2574.
    • (2008) Neurochem. Res. , vol.33 , pp. 2565-2574
    • Piccoli, C.1
  • 67
    • 77953666757 scopus 로고    scopus 로고
    • Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function
    • Morais V.A., et al. Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function. EMBO Mol. Med. 2009, 1:99-111.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 99-111
    • Morais, V.A.1
  • 68
    • 81155128499 scopus 로고    scopus 로고
    • Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease
    • Dagda R.K., et al. Mitochondrially localized PKA reverses mitochondrial pathology and dysfunction in a cellular model of Parkinson's disease. Cell Death Differ. 2011, 18:1914-1923.
    • (2011) Cell Death Differ. , vol.18 , pp. 1914-1923
    • Dagda, R.K.1
  • 69
    • 84856817318 scopus 로고    scopus 로고
    • A novel neuroprotective therapy for Parkinson's disease using a viral noncoding RNA that protects mitochondrial complex I activity
    • Kuan W.L., et al. A novel neuroprotective therapy for Parkinson's disease using a viral noncoding RNA that protects mitochondrial complex I activity. J. Exp. Med. 2012, 209:1-10.
    • (2012) J. Exp. Med. , vol.209 , pp. 1-10
    • Kuan, W.L.1
  • 70
    • 34249871137 scopus 로고    scopus 로고
    • Complex I binding by a virally encoded RNA regulates mitochondria-induced cell death
    • Reeves M.B., et al. Complex I binding by a virally encoded RNA regulates mitochondria-induced cell death. Science 2007, 316:1345-1348.
    • (2007) Science , vol.316 , pp. 1345-1348
    • Reeves, M.B.1
  • 71
    • 79961208847 scopus 로고    scopus 로고
    • GRIM-19 function in cancer development
    • Moreira S., et al. GRIM-19 function in cancer development. Mitochondrion 2011, 11:693-699.
    • (2011) Mitochondrion , vol.11 , pp. 693-699
    • Moreira, S.1
  • 72
    • 34249736347 scopus 로고    scopus 로고
    • The phosphorylation pattern of bovine heart complex I subunits
    • Palmisano G., et al. The phosphorylation pattern of bovine heart complex I subunits. Proteomics 2007, 7:1575-1583.
    • (2007) Proteomics , vol.7 , pp. 1575-1583
    • Palmisano, G.1
  • 73
    • 0034721920 scopus 로고    scopus 로고
    • Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-beta and retinoic acid combination, using a genetic approach
    • Angell J.E., et al. Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-beta and retinoic acid combination, using a genetic approach. J. Biol. Chem. 2000, 275:33416-33426.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33416-33426
    • Angell, J.E.1
  • 74
    • 34548496286 scopus 로고    scopus 로고
    • Altered expression of mitochondrial and extracellular matrix genes in the heart of human fetuses with chromosome 21 trisomy
    • Conti A., et al. Altered expression of mitochondrial and extracellular matrix genes in the heart of human fetuses with chromosome 21 trisomy. BMC Genomics 2007, 8:268.
    • (2007) BMC Genomics , vol.8 , pp. 268
    • Conti, A.1
  • 75
    • 84859842601 scopus 로고    scopus 로고
    • Regional susceptibilities to mitochondrial dysfunctions in the CNS
    • Pinto M., et al. Regional susceptibilities to mitochondrial dysfunctions in the CNS. Biol. Chem. 2012, 393:275-281.
    • (2012) Biol. Chem. , vol.393 , pp. 275-281
    • Pinto, M.1
  • 76
    • 0030614644 scopus 로고    scopus 로고
    • Neuronal vulnerability in Parkinson's disease
    • Hirsch E.C., et al. Neuronal vulnerability in Parkinson's disease. J. Neural Transm. Suppl. 1997, 50:79-88.
    • (1997) J. Neural Transm. Suppl. , vol.50 , pp. 79-88
    • Hirsch, E.C.1
  • 77
    • 0033584845 scopus 로고    scopus 로고
    • Threshold effect and tissue specificity. Implication for mitochondrial cytopathies
    • Rossignol R., et al. Threshold effect and tissue specificity. Implication for mitochondrial cytopathies. J. Biol. Chem. 1999, 274:33426-33432.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33426-33432
    • Rossignol, R.1
  • 78
    • 0034213455 scopus 로고    scopus 로고
    • CAMP response element-mediated gene transcription is upregulated by chronic antidepressant treatment
    • Thome J., et al. cAMP response element-mediated gene transcription is upregulated by chronic antidepressant treatment. J. Neurosci. 2000, 20:4030-4036.
    • (2000) J. Neurosci. , vol.20 , pp. 4030-4036
    • Thome, J.1
  • 79
    • 26644441875 scopus 로고    scopus 로고
    • Differential expression and regulation of the cAMP-selective phosphodiesterase type 4A splice variants in rat brain by chronic antidepressant administration
    • D'Sa C., et al. Differential expression and regulation of the cAMP-selective phosphodiesterase type 4A splice variants in rat brain by chronic antidepressant administration. Eur. J. Neurosci. 2005, 22:1463-1475.
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 1463-1475
    • D'Sa, C.1
  • 80
    • 79952959359 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and pathology in bipolar disorder and schizophrenia
    • Clay H.B., et al. Mitochondrial dysfunction and pathology in bipolar disorder and schizophrenia. Int. J. Dev. Neurosci. 2011, 29:311-324.
    • (2011) Int. J. Dev. Neurosci. , vol.29 , pp. 311-324
    • Clay, H.B.1
  • 81
    • 79954578338 scopus 로고    scopus 로고
    • Beyond the serotonin hypothesis: mitochondria, inflammation and neurodegeneration in major depression and affective spectrum disorders
    • Gardner A., Boles R.G. Beyond the serotonin hypothesis: mitochondria, inflammation and neurodegeneration in major depression and affective spectrum disorders. Prog. Neuropsychopharmacol. Biol. Psychiatry 2011, 35:730-743.
    • (2011) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.35 , pp. 730-743
    • Gardner, A.1    Boles, R.G.2
  • 82
    • 84856652686 scopus 로고    scopus 로고
    • Phosphodiesterase 4 inhibition enhances the dopamine D1 receptor/PKA/DARPP-32 signaling cascade in frontal cortex
    • Kuroiwa M., et al. Phosphodiesterase 4 inhibition enhances the dopamine D1 receptor/PKA/DARPP-32 signaling cascade in frontal cortex. Psychopharmacology (Berl.) 2012, 219:1065-1079.
    • (2012) Psychopharmacology (Berl.) , vol.219 , pp. 1065-1079
    • Kuroiwa, M.1
  • 83
    • 79960561364 scopus 로고    scopus 로고
    • ATP synthase superassemblies in animals and plants: two or more are better
    • Seelert H., Dencher N.A. ATP synthase superassemblies in animals and plants: two or more are better. Biochim. Biophys. Acta 2011, 1807:118511-118597.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 118511-118597
    • Seelert, H.1    Dencher, N.A.2
  • 84
    • 78649660058 scopus 로고    scopus 로고
    • Different effects of oleate vs palmitate on mitochondrial function, apoptosis, and insulin signaling in L6 skeletal muscle cells: role of oxidative stress
    • Yuzefovych L., et al. Different effects of oleate vs palmitate on mitochondrial function, apoptosis, and insulin signaling in L6 skeletal muscle cells: role of oxidative stress. Am. J. Physiol. Endocrinol. Metab. 2010, 299:E1096-E10105.
    • (2010) Am. J. Physiol. Endocrinol. Metab. , vol.299
    • Yuzefovych, L.1
  • 85
    • 84872602219 scopus 로고    scopus 로고
    • Oncogenic K-ras expression is associated with derangement of the cAMP/PKA pathway and forskolin-reversible alterations of mitochondrial dynamics and respiration
    • Oncogene, doi:10.1038/onc.2012.50
    • Palorini, R. et al. (2012) Oncogenic K-ras expression is associated with derangement of the cAMP/PKA pathway and forskolin-reversible alterations of mitochondrial dynamics and respiration. Oncogene doi:10.1038/onc.2012.50.
    • (2012)
    • Palorini, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.