메뉴 건너뛰기




Volumn 22, Issue 1, 2012, Pages 76-86

176th ENMC International Workshop: Diagnosis and treatment of coenzyme Q 10 deficiency

Author keywords

[No Author keywords available]

Indexed keywords

UBIDECARENONE;

EID: 84855992976     PISSN: 09608966     EISSN: 18732364     Source Type: Journal    
DOI: 10.1016/j.nmd.2011.05.001     Document Type: Article
Times cited : (82)

References (64)
  • 2
    • 67749089506 scopus 로고    scopus 로고
    • Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms
    • Kawamukai M. Biosynthesis and bioproduction of coenzyme Q10 by yeasts and other organisms. Biotechnol. Appl. Biochem. 2009, 53:217-226.
    • (2009) Biotechnol. Appl. Biochem. , vol.53 , pp. 217-226
    • Kawamukai, M.1
  • 4
    • 0020988620 scopus 로고
    • Biosynthesis of ubiquinone
    • Olson R.E., Rudney H. Biosynthesis of ubiquinone. Vitam. Horm. 1983, 40:1-43.
    • (1983) Vitam. Horm. , vol.40 , pp. 1-43
    • Olson, R.E.1    Rudney, H.2
  • 5
    • 34248195476 scopus 로고    scopus 로고
    • Endogenous synthesis of coenzyme Q in eukaryotes
    • Tran U.C., Clarke C.F. Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion 2007, 7(Suppl):S62-71.
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Tran, U.C.1    Clarke, C.F.2
  • 6
    • 0028258205 scopus 로고
    • Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase
    • Siebert M., Severin K., Heide L. Formation of 4-hydroxybenzoate in Escherichia coli: characterization of the ubiC gene and its encoded enzyme chorismate pyruvate-lyase. Microbiology 1994, 140(Pt 4):897-904.
    • (1994) Microbiology , vol.140 , Issue.PART 4 , pp. 897-904
    • Siebert, M.1    Severin, K.2    Heide, L.3
  • 7
    • 77954182740 scopus 로고    scopus 로고
    • Involvement of mitochondrial ferredoxin and para-aminobenzoic acid in yeast coenzyme Q biosynthesis
    • Pierrel F., Hamelin O., Douki T., et al. Involvement of mitochondrial ferredoxin and para-aminobenzoic acid in yeast coenzyme Q biosynthesis. Chem. Biol. 2010, 17:449-459.
    • (2010) Chem. Biol. , vol.17 , pp. 449-459
    • Pierrel, F.1    Hamelin, O.2    Douki, T.3
  • 8
    • 77956251553 scopus 로고    scopus 로고
    • Para-Aminobenzoic acid is a precursor in coenzyme Q6 biosynthesis in Saccharomyces cerevisiae
    • Marbois B., Xie L.X., Choi S., Hirano K., Hyman K., Clarke C.F. Para-Aminobenzoic acid is a precursor in coenzyme Q6 biosynthesis in Saccharomyces cerevisiae. J. Biol. Chem. 2010, 285:27827-27838.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27827-27838
    • Marbois, B.1    Xie, L.X.2    Choi, S.3    Hirano, K.4    Hyman, K.5    Clarke, C.F.6
  • 9
    • 77953808600 scopus 로고    scopus 로고
    • 4-Nitrobenzoate inhibits coenzyme Q biosynthesis in mammalian cell cultures
    • Forsman U., Sjoberg M., Turunen M., Sindelar P.J. 4-Nitrobenzoate inhibits coenzyme Q biosynthesis in mammalian cell cultures. Nat. Chem. Biol. 2010, 6:515-517.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 515-517
    • Forsman, U.1    Sjoberg, M.2    Turunen, M.3    Sindelar, P.J.4
  • 10
    • 0141610413 scopus 로고
    • Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy
    • Ogasahara S., Engel A.G., Frens D., Mack D. Muscle coenzyme Q deficiency in familial mitochondrial encephalomyopathy. Proc. Natl. Acad. Sci. U.S.A. 1989, 86:2379-2382.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 2379-2382
    • Ogasahara, S.1    Engel, A.G.2    Frens, D.3    Mack, D.4
  • 12
    • 41149134880 scopus 로고    scopus 로고
    • CABC1 gene mutations cause ubiquinone deficiency with cerebellar ataxia and seizures
    • Mollet J., Delahodde A., Serre V., et al. CABC1 gene mutations cause ubiquinone deficiency with cerebellar ataxia and seizures. Am. J. Hum. Genet. 2008, 82:623-630.
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 623-630
    • Mollet, J.1    Delahodde, A.2    Serre, V.3
  • 13
    • 0034730011 scopus 로고    scopus 로고
    • Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency
    • Rötig A., Appelkvist E.L., Geromel V., et al. Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency. Lancet 2000, 356:391-395.
    • (2000) Lancet , vol.356 , pp. 391-395
    • Rötig, A.1    Appelkvist, E.L.2    Geromel, V.3
  • 14
    • 33845232634 scopus 로고    scopus 로고
    • Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations
    • Lopez L.C., Schuelke M., Quinzii C.M., et al. Leigh syndrome with nephropathy and CoQ10 deficiency due to decaprenyl diphosphate synthase subunit 2 (PDSS2) mutations. Am. J. Hum. Genet. 2006, 79:1125-1129.
    • (2006) Am. J. Hum. Genet. , vol.79 , pp. 1125-1129
    • Lopez, L.C.1    Schuelke, M.2    Quinzii, C.M.3
  • 15
    • 33847347629 scopus 로고    scopus 로고
    • Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders
    • Mollet J., Giurgea I., Schlemmer D., et al. Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders. J. Clin. Invest. 2007, 117:765-772.
    • (2007) J. Clin. Invest. , vol.117 , pp. 765-772
    • Mollet, J.1    Giurgea, I.2    Schlemmer, D.3
  • 16
    • 31544480133 scopus 로고    scopus 로고
    • A Mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency
    • Quinzii C., Naini A., Salviati L., et al. A Mutation in para-hydroxybenzoate-polyprenyl transferase (COQ2) causes primary coenzyme Q10 deficiency. Am. J. Hum. Genet. 2006, 78:345-349.
    • (2006) Am. J. Hum. Genet. , vol.78 , pp. 345-349
    • Quinzii, C.1    Naini, A.2    Salviati, L.3
  • 17
  • 18
    • 23844469463 scopus 로고    scopus 로고
    • Infantile encephalomyopathy and nephropathy with CoQ10 deficiency: a CoQ10-responsive condition
    • Salviati L., Sacconi S., Murer L., et al. Infantile encephalomyopathy and nephropathy with CoQ10 deficiency: a CoQ10-responsive condition. Neurology 2005, 65:606-608.
    • (2005) Neurology , vol.65 , pp. 606-608
    • Salviati, L.1    Sacconi, S.2    Murer, L.3
  • 19
    • 0037426430 scopus 로고    scopus 로고
    • Cerebellar ataxia and coenzyme Q10 deficiency
    • Lamperti C., Naini A., Hirano M., et al. Cerebellar ataxia and coenzyme Q10 deficiency. Neurology 2003, 60:1206-1208.
    • (2003) Neurology , vol.60 , pp. 1206-1208
    • Lamperti, C.1    Naini, A.2    Hirano, M.3
  • 20
    • 0035836740 scopus 로고    scopus 로고
    • Familial cerebellar ataxia with muscle coenzyme Q10 deficiency
    • Musumeci O., Naini A., Slonim A.E., et al. Familial cerebellar ataxia with muscle coenzyme Q10 deficiency. Neurology 2001, 56:849-855.
    • (2001) Neurology , vol.56 , pp. 849-855
    • Musumeci, O.1    Naini, A.2    Slonim, A.E.3
  • 21
    • 41149121580 scopus 로고    scopus 로고
    • ADCK3, an ancestral kinase, is mutated in a form of recessive ataxia associated with coenzyme Q10 deficiency
    • Lagier-Tourenne C., Tazir M., Lopez L.C., et al. ADCK3, an ancestral kinase, is mutated in a form of recessive ataxia associated with coenzyme Q10 deficiency. Am. J. Hum. Genet. 2008, 82:661-672.
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 661-672
    • Lagier-Tourenne, C.1    Tazir, M.2    Lopez, L.C.3
  • 22
    • 13244277454 scopus 로고    scopus 로고
    • Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation
    • Quinzii C.M., Kattah A.G., Naini A., et al. Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation. Neurology 2005, 64:539-541.
    • (2005) Neurology , vol.64 , pp. 539-541
    • Quinzii, C.M.1    Kattah, A.G.2    Naini, A.3
  • 23
    • 33846446004 scopus 로고    scopus 로고
    • Muscle coenzyme Q10 deficiencies in ataxia with oculomotor apraxia 1
    • Le Ber I., Dubourg O., Benoist J.F., et al. Muscle coenzyme Q10 deficiencies in ataxia with oculomotor apraxia 1. Neurology 2007, 68:295-297.
    • (2007) Neurology , vol.68 , pp. 295-297
    • Le Ber, I.1    Dubourg, O.2    Benoist, J.F.3
  • 24
    • 0036895391 scopus 로고    scopus 로고
    • Coenzyme Q-responsive Leigh's encephalopathy in two sisters
    • Van Maldergem L., Trijbels F., DiMauro S., et al. Coenzyme Q-responsive Leigh's encephalopathy in two sisters. Ann. Neurol. 2002, 52:750-754.
    • (2002) Ann. Neurol. , vol.52 , pp. 750-754
    • Van Maldergem, L.1    Trijbels, F.2    DiMauro, S.3
  • 25
    • 33644921803 scopus 로고    scopus 로고
    • Coenzyme Q10 deficiency and isolated myopathy
    • Horvath R., Schneiderat P., Schoser B.G., et al. Coenzyme Q10 deficiency and isolated myopathy. Neurology 2006, 66:253-255.
    • (2006) Neurology , vol.66 , pp. 253-255
    • Horvath, R.1    Schneiderat, P.2    Schoser, B.G.3
  • 27
    • 34248171499 scopus 로고    scopus 로고
    • The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene
    • Gempel K., Topaloglu H., Talim B., et al. The myopathic form of coenzyme Q10 deficiency is caused by mutations in the electron-transferring-flavoprotein dehydrogenase (ETFDH) gene. Brain 2007, 130:2037-2044.
    • (2007) Brain , vol.130 , pp. 2037-2044
    • Gempel, K.1    Topaloglu, H.2    Talim, B.3
  • 28
    • 78650693958 scopus 로고    scopus 로고
    • Clinical, neuroradiological and genetic findings in pontocerebellar hypoplasia
    • Namavar Y., Barth P.G., Kasher P.R., et al. Clinical, neuroradiological and genetic findings in pontocerebellar hypoplasia. Brain 2011, 134:143-156.
    • (2011) Brain , vol.134 , pp. 143-156
    • Namavar, Y.1    Barth, P.G.2    Kasher, P.R.3
  • 29
    • 28044432748 scopus 로고    scopus 로고
    • Determination of coenzyme Q10 status in blood mononuclear cells, skeletal muscle, and plasma by HPLC with di-propoxy-coenzyme Q10 as an internal standard
    • Duncan A.J., Heales S.J., Mills K., Eaton S., Land J.M., Hargreaves I.P. Determination of coenzyme Q10 status in blood mononuclear cells, skeletal muscle, and plasma by HPLC with di-propoxy-coenzyme Q10 as an internal standard. Clin. Chem. 2005, 51:2380-2382.
    • (2005) Clin. Chem. , vol.51 , pp. 2380-2382
    • Duncan, A.J.1    Heales, S.J.2    Mills, K.3    Eaton, S.4    Land, J.M.5    Hargreaves, I.P.6
  • 30
    • 65549087610 scopus 로고    scopus 로고
    • A nonsense mutation in COQ9 causes autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency: a potentially treatable form of mitochondrial disease
    • Duncan A.J., Bitner-Glindzicz M., Meunier B., et al. A nonsense mutation in COQ9 causes autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency: a potentially treatable form of mitochondrial disease. Am. J. Hum. Genet. 2009, 84:558-566.
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 558-566
    • Duncan, A.J.1    Bitner-Glindzicz, M.2    Meunier, B.3
  • 31
    • 79955520308 scopus 로고    scopus 로고
    • COQ6 mutations cause nephrotic syndrome with sensorineural deafness in humans, concurrent with increased apoptosis
    • Heeringa S., Chernin G., Chak iM, et al. COQ6 mutations cause nephrotic syndrome with sensorineural deafness in humans, concurrent with increased apoptosis. J Clin Invest 2011, 121:2013-2024.
    • (2011) J Clin Invest , vol.121 , pp. 2013-2024
    • Heeringa, S.1    Chernin, G.2    Chak, I.3
  • 32
    • 34250668197 scopus 로고    scopus 로고
    • COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement
    • Diomedi-Camassei F., Di Giandomenico S., Santorelli F.M., et al. COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement. J. Am. Soc. Nephrol. 2007, 18:2773-2780.
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 2773-2780
    • Diomedi-Camassei, F.1    Di Giandomenico, S.2    Santorelli, F.M.3
  • 33
    • 77955594306 scopus 로고    scopus 로고
    • Treatment of CoQ10 deficient fibroblasts with ubiquinone, analogs, and vitamin C: time- and compound-dependent effects on bioenergetic and oxidative stress status
    • Lopez L.C., Quinzii C., Area E., et al. Treatment of CoQ10 deficient fibroblasts with ubiquinone, analogs, and vitamin C: time- and compound-dependent effects on bioenergetic and oxidative stress status. PLoS One 2010, 5:e11897.
    • (2010) PLoS One , vol.5
    • Lopez, L.C.1    Quinzii, C.2    Area, E.3
  • 34
    • 77955424107 scopus 로고    scopus 로고
    • Nonsense mutations in CABC1/ADCK3 cause progressive cerebellar ataxia and atrophy
    • Gerards M., van den Bosch B., Calis C., et al. Nonsense mutations in CABC1/ADCK3 cause progressive cerebellar ataxia and atrophy. Mitochondrion 2010, 10:510-515.
    • (2010) Mitochondrion , vol.10 , pp. 510-515
    • Gerards, M.1    van den Bosch, B.2    Calis, C.3
  • 35
    • 0025886262 scopus 로고
    • ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex
    • Bousquet I., Dujardin G., Slonimski P.P. ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex. EMBO J. 1991, 10:2023-2031.
    • (1991) EMBO J. , vol.10 , pp. 2023-2031
    • Bousquet, I.1    Dujardin, G.2    Slonimski, P.P.3
  • 36
    • 0030917335 scopus 로고    scopus 로고
    • The nuclear ABC1 gene is essential for the correct conformation and functioning of the cytochrome bc1 complex and the neighbouring complexes II and IV in the mitochondrial respiratory chain
    • Brasseur G., Tron G., Dujardin G., Slonimski P.P., Brivet-Chevillotte P. The nuclear ABC1 gene is essential for the correct conformation and functioning of the cytochrome bc1 complex and the neighbouring complexes II and IV in the mitochondrial respiratory chain. Eur. J. Biochem. 1997, 246:103-111.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 103-111
    • Brasseur, G.1    Tron, G.2    Dujardin, G.3    Slonimski, P.P.4    Brivet-Chevillotte, P.5
  • 37
    • 0036493983 scopus 로고    scopus 로고
    • Isolation of a novel gene, CABC1, encoding a mitochondrial protein that is highly homologous to Yyast activity of bc1 complex
    • Iiizumi M., Arakawa H., Mori T., Ando A., Nakamura Y. Isolation of a novel gene, CABC1, encoding a mitochondrial protein that is highly homologous to Yyast activity of bc1 complex. Cancer Res. 2002, 62:1246-1250.
    • (2002) Cancer Res. , vol.62 , pp. 1246-1250
    • Iiizumi, M.1    Arakawa, H.2    Mori, T.3    Ando, A.4    Nakamura, Y.5
  • 38
    • 0035947594 scopus 로고    scopus 로고
    • A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants
    • Do T.Q., Hsu A.Y., Jonassen T., Lee P.T., Clarke C.F. A defect in coenzyme Q biosynthesis is responsible for the respiratory deficiency in Saccharomyces cerevisiae abc1 mutants. J. Biol. Chem. 2001, 276:18161-18168.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18161-18168
    • Do, T.Q.1    Hsu, A.Y.2    Jonassen, T.3    Lee, P.T.4    Clarke, C.F.5
  • 39
    • 1842478452 scopus 로고    scopus 로고
    • A tRNA(TRP) gene mediates the suppression of cbs2-223 previously attributed to ABC1/COQ8
    • Hsieh E.J., Dinoso J.B., Clarke C.F. A tRNA(TRP) gene mediates the suppression of cbs2-223 previously attributed to ABC1/COQ8. Biochem. Biophys. Res. Commun. 2004, 317:648-653.
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 648-653
    • Hsieh, E.J.1    Dinoso, J.B.2    Clarke, C.F.3
  • 40
    • 55349084786 scopus 로고    scopus 로고
    • Ubiquinone biosynthesis in Saccharomyces cerevisiae: the molecular organization of O-methylase Coq3p depends on Abc1p/Coq8p
    • Tauche A., Krause-Bucholz U., Rodel G. Ubiquinone biosynthesis in Saccharomyces cerevisiae: the molecular organization of O-methylase Coq3p depends on Abc1p/Coq8p. FEMS Yeast Res. 2008, 8:1263-1275.
    • (2008) FEMS Yeast Res. , vol.8 , pp. 1263-1275
    • Tauche, A.1    Krause-Bucholz, U.2    Rodel, G.3
  • 41
    • 34547809952 scopus 로고    scopus 로고
    • ETFDH mutations as a major cause of riboflavin-responsive multiple acyl-CoA dehydrogenation deficiency
    • Olsen R.K., Olpin S.E., Andresen B.S., Miedzybrodzka Z.H., Pourfarzam M., Merinero B., et al. ETFDH mutations as a major cause of riboflavin-responsive multiple acyl-CoA dehydrogenation deficiency. Brain 2007, 130:2045-2054.
    • (2007) Brain , vol.130 , pp. 2045-2054
    • Olsen, R.K.1    Olpin, S.E.2    Andresen, B.S.3    Miedzybrodzka, Z.H.4    Pourfarzam, M.5    Merinero, B.6
  • 42
    • 61849090857 scopus 로고    scopus 로고
    • ETFDH mutations, CoQ10 levels, and respiratory chain activities in patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency
    • Liang W.C., Ohkuma A., Hayashi Y.K., et al. ETFDH mutations, CoQ10 levels, and respiratory chain activities in patients with riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency. Neuromuscul. Disord. 2009, 19:212-216.
    • (2009) Neuromuscul. Disord. , vol.19 , pp. 212-216
    • Liang, W.C.1    Ohkuma, A.2    Hayashi, Y.K.3
  • 43
    • 62849112102 scopus 로고    scopus 로고
    • Clinical and genetic analysis of lipid storage myopathies
    • Ohkuma A., Noguchi S., Sugie H., et al. Clinical and genetic analysis of lipid storage myopathies. Muscle Nerve 2009, 39:333-342.
    • (2009) Muscle Nerve , vol.39 , pp. 333-342
    • Ohkuma, A.1    Noguchi, S.2    Sugie, H.3
  • 44
    • 0344875066 scopus 로고    scopus 로고
    • Cerebellar ataxia with oculomotor apraxia type 1: clinical and genetic studies
    • Le Ber I., Moreira M.C., Rivaud-Pechoux S., et al. Cerebellar ataxia with oculomotor apraxia type 1: clinical and genetic studies. Brain 2003, 126:2761-2772.
    • (2003) Brain , vol.126 , pp. 2761-2772
    • Le Ber, I.1    Moreira, M.C.2    Rivaud-Pechoux, S.3
  • 45
  • 46
    • 74249105071 scopus 로고    scopus 로고
    • Coenzyme Q10 is frequently reduced in muscle of patients with mitochondrial myopathy
    • Sacconi S., Trevisson E., Salviati L., et al. Coenzyme Q10 is frequently reduced in muscle of patients with mitochondrial myopathy. Neuromuscul. Disord. 2010, 20:44-48.
    • (2010) Neuromuscul. Disord. , vol.20 , pp. 44-48
    • Sacconi, S.1    Trevisson, E.2    Salviati, L.3
  • 47
    • 0034908612 scopus 로고    scopus 로고
    • Human cultured skin fibroblasts survive profound inherited ubiquinone depletion
    • Geromel V., Kadhom N., Ceballos-Picot I., et al. Human cultured skin fibroblasts survive profound inherited ubiquinone depletion. Free Radic. Res. 2001, 35:11-21.
    • (2001) Free Radic. Res. , vol.35 , pp. 11-21
    • Geromel, V.1    Kadhom, N.2    Ceballos-Picot, I.3
  • 48
    • 34447295112 scopus 로고    scopus 로고
    • Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis
    • Lopez-Martin J.M., Salviati L., Trevisson E., et al. Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis. Hum. Mol. Genet. 2007, 16:1091-1097.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 1091-1097
    • Lopez-Martin, J.M.1    Salviati, L.2    Trevisson, E.3
  • 49
    • 58149376131 scopus 로고    scopus 로고
    • Coenzyme Q deficiency triggers mitochondrial degradation by mitophagy
    • Rodriguéz-Hernandez A., Cordero M.D., Salviati L., et al. Coenzyme Q deficiency triggers mitochondrial degradation by mitophagy. Autophagy 2009, 5:19-32.
    • (2009) Autophagy , vol.5 , pp. 19-32
    • Rodriguéz-Hernandez, A.1    Cordero, M.D.2    Salviati, L.3
  • 50
    • 44949220201 scopus 로고    scopus 로고
    • Respiratory chain dysfunction and oxidative stress correlate with severity of primary CoQ10 deficiency
    • Quinzii C.M., Lopez L.C., Von-Moltke J., et al. Respiratory chain dysfunction and oxidative stress correlate with severity of primary CoQ10 deficiency. FASEB J. 2008, 22:1874-1885.
    • (2008) FASEB J. , vol.22 , pp. 1874-1885
    • Quinzii, C.M.1    Lopez, L.C.2    Von-Moltke, J.3
  • 51
    • 77957844254 scopus 로고    scopus 로고
    • Reactive oxygen species, oxidative stress, and cell death correlate with level of CoQ10 deficiency
    • Quinzii C.M., Lopez L.C., Gilkerson R.W., et al. Reactive oxygen species, oxidative stress, and cell death correlate with level of CoQ10 deficiency. FASEB J. 2010, 24:3733-3743.
    • (2010) FASEB J. , vol.24 , pp. 3733-3743
    • Quinzii, C.M.1    Lopez, L.C.2    Gilkerson, R.W.3
  • 52
    • 0031030678 scopus 로고    scopus 로고
    • Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1
    • Ewbank J.J., Barnes T.M., Lakowski B., Lussier M., Bussey H., Hekimi S. Structural and functional conservation of the Caenorhabditis elegans timing gene clk-1. Science 1997, 275:980-983.
    • (1997) Science , vol.275 , pp. 980-983
    • Ewbank, J.J.1    Barnes, T.M.2    Lakowski, B.3    Lussier, M.4    Bussey, H.5    Hekimi, S.6
  • 53
    • 2942707861 scopus 로고    scopus 로고
    • Demethoxy-Q, an intermediate of coenzyme Q biosynthesis, fails to support respiration in Saccharomyces cerevisiae and lacks antioxidant activity
    • Padilla S., Jonassen T., Jimenez-Hidalgo M.A., et al. Demethoxy-Q, an intermediate of coenzyme Q biosynthesis, fails to support respiration in Saccharomyces cerevisiae and lacks antioxidant activity. J. Biol. Chem. 2004, 279:25995-26004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25995-26004
    • Padilla, S.1    Jonassen, T.2    Jimenez-Hidalgo, M.A.3
  • 54
    • 59049084701 scopus 로고    scopus 로고
    • Coenzyme Q supports distinct developmental processes in Caenorhabditis elegans
    • Asencio C., Navas P., Cabello J., et al. Coenzyme Q supports distinct developmental processes in Caenorhabditis elegans. Mech. Ageing Dev. 2009, 130:145-153.
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 145-153
    • Asencio, C.1    Navas, P.2    Cabello, J.3
  • 55
    • 0015030432 scopus 로고
    • An inherited kidney disease of mice resembling human nephronophthisis
    • Lyon M.F., Hulse E.V. An inherited kidney disease of mice resembling human nephronophthisis. J. Med. Genet. 1971, 8:41-48.
    • (1971) J. Med. Genet. , vol.8 , pp. 41-48
    • Lyon, M.F.1    Hulse, E.V.2
  • 56
    • 0030766553 scopus 로고    scopus 로고
    • Characterisation of cellular infiltration and adhesion molecule expression in CBA/CaH-kdkd mice with tubulointerstitial renal disease
    • Sibalic V., Fan X., Wuthrich R.P. Characterisation of cellular infiltration and adhesion molecule expression in CBA/CaH-kdkd mice with tubulointerstitial renal disease. Histochem. Cell Biol. 1997, 108:235-242.
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 235-242
    • Sibalic, V.1    Fan, X.2    Wuthrich, R.P.3
  • 57
    • 3042842582 scopus 로고    scopus 로고
    • Mutant prenyltransferase-like mitochondrial protein (PLMP) and mitochondrial abnormalities in kd/kd mice
    • Peng M., Jarett L., Meade R., et al. Mutant prenyltransferase-like mitochondrial protein (PLMP) and mitochondrial abnormalities in kd/kd mice. Kidney Int. 2004, 66:20-28.
    • (2004) Kidney Int. , vol.66 , pp. 20-28
    • Peng, M.1    Jarett, L.2    Meade, R.3
  • 59
    • 57349192861 scopus 로고    scopus 로고
    • Coenzyme Q10 supplementation rescues renal disease in Pdss2kd/kd mice with mutations in prenyl diphosphate synthase subunit 2
    • Saiki R., Lunceford A.L., Shi Y., et al. Coenzyme Q10 supplementation rescues renal disease in Pdss2kd/kd mice with mutations in prenyl diphosphate synthase subunit 2. Am. J. Physiol. Renal. Physiol. 2008, 295:F1535-1544.
    • (2008) Am. J. Physiol. Renal. Physiol. , vol.295
    • Saiki, R.1    Lunceford, A.L.2    Shi, Y.3
  • 61
    • 33645099245 scopus 로고    scopus 로고
    • Coenzyme Q10: Absorption, tissue uptake, metabolism and pharmacokinetics
    • Bhagavan H.N., Chopra R.K. Coenzyme Q10: Absorption, tissue uptake, metabolism and pharmacokinetics. Free Radic. Res. 2006, 40:445-453.
    • (2006) Free Radic. Res. , vol.40 , pp. 445-453
    • Bhagavan, H.N.1    Chopra, R.K.2
  • 62
    • 33645068499 scopus 로고    scopus 로고
    • Tolerance of high-dose (3000mg/day) coenzyme Q10 in ALS
    • Ferrante K.L., Shefner J., Zhang H., et al. Tolerance of high-dose (3000mg/day) coenzyme Q10 in ALS. Neurology 2005, 65:1834-1836.
    • (2005) Neurology , vol.65 , pp. 1834-1836
    • Ferrante, K.L.1    Shefner, J.2    Zhang, H.3
  • 63
    • 45949099527 scopus 로고    scopus 로고
    • Early coenzyme Q10 supplementation in primary coenzyme Q10 deficiency
    • Montini G., Malaventura C., Salviati L. Early coenzyme Q10 supplementation in primary coenzyme Q10 deficiency. N. Engl. J. Med. 2008, 358:2849-2850.
    • (2008) N. Engl. J. Med. , vol.358 , pp. 2849-2850
    • Montini, G.1    Malaventura, C.2    Salviati, L.3
  • 64
    • 77955082584 scopus 로고    scopus 로고
    • Coenzyme Q(10)-responsive ataxia: 2-year-treatment follow-up
    • Pineda M., Montero R., Aracil A., et al. Coenzyme Q(10)-responsive ataxia: 2-year-treatment follow-up. Mov. Disord. 2010, 25:1262-1268.
    • (2010) Mov. Disord. , vol.25 , pp. 1262-1268
    • Pineda, M.1    Montero, R.2    Aracil, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.