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Volumn 62, Issue 6, 2010, Pages 403-413

Impact of selected inborn errors of metabolism on prenatal and neonatal development

Author keywords

Fatty acid oxidation; Fetus; Galactosemia; Maternal PKU; Maturation; Metabolism; Mitochondria; Morbus niemann pick type C; Neonatal period; Pyruvate dehydrogenase; Respiratory chain; Urea cycle disorder

Indexed keywords

CARBOHYDRATE; MIGLUSTAT;

EID: 77953581934     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.336     Document Type: Review
Times cited : (40)

References (99)
  • 1
    • 0035933049 scopus 로고    scopus 로고
    • Inborn errors of metabolism: A cause of abnormal brain development
    • Nissenkorn, A., Michelson, M., Ben-Zeev, B., and Lerman-Sagie, T. (2001) Inborn errors of metabolism: a cause of abnormal brain development. Neurology 56, 1265-1272.
    • (2001) Neurology , vol.56 , pp. 1265-1272
    • Nissenkorn, A.1    Michelson, M.2    Ben-Zeev, B.3    Lerman-Sagie, T.4
  • 2
    • 69549122629 scopus 로고    scopus 로고
    • Primary disorders of metabolism and disturbed fetal brain development
    • Prasad, A. N., Malinger, G., and Lerman-Sagie, T. (2009) Primary disorders of metabolism and disturbed fetal brain development. Clin. Perinatol. 36, 621-638.
    • (2009) Clin. Perinatol. , vol.36 , pp. 621-638
    • Prasad, A.N.1    Malinger, G.2    Lerman-Sagie, T.3
  • 3
    • 4544366928 scopus 로고    scopus 로고
    • Living with the past: Evolution, development, and patterns of disease
    • Gluckman, P. D. and Hanson, M. A. (2004) Living with the past: evolution, development, and patterns of disease. Science 305, 1733-1736.
    • (2004) Science , vol.305 , pp. 1733-1736
    • Gluckman, P.D.1    Hanson, M.A.2
  • 6
    • 0017751829 scopus 로고
    • The activity of galactose-1-phosphate uridyltransferase and galactokinase in human fetal organs
    • Shin-Buehring, Y. S., Beier, T., Tan, A., Osang, M., and Schaub, J. (1977) The activity of galactose-1-phosphate uridyltransferase and galactokinase in human fetal organs. Pediatr. Res. 11, 1045-1051.
    • (1977) Pediatr. Res. , vol.11 , pp. 1045-1051
    • Shin-Buehring, Y.S.1    Beier, T.2    Tan, A.3    Osang, M.4    Schaub, J.5
  • 7
    • 0037747697 scopus 로고
    • Carbohydrate metabolism in liver from foetal and neonatal sheep
    • Ballard, F. J. and Oliver, I. T. (1965) Carbohydrate Metabolism in Liver from Foetal and Neonatal Sheep. Biochem. J. 95, 191-200.
    • (1965) Biochem. J. , vol.95 , pp. 191-200
    • Ballard, F.J.1    Oliver, I.T.2
  • 9
    • 0022388593 scopus 로고
    • Perinatal galactose metabolism
    • Kliegman, R. M. and Sparks, J. W. (1985) Perinatal galactose metabolism. J. Pediatr. 107, 831-841.
    • (1985) J. Pediatr. , vol.107 , pp. 831-841
    • Kliegman, R.M.1    Sparks, J.W.2
  • 10
    • 0017806089 scopus 로고
    • Effect of galactose on free radical reactions of polymorphonuclear leukocytes
    • Litchfield, W. J. and Wells, W. W. (1978) Effect of galactose on free radical reactions of polymorphonuclear leukocytes. Arch. Biochem. Biophys. 188, 26-30.
    • (1978) Arch. Biochem. Biophys. , vol.188 , pp. 26-30
    • Litchfield, W.J.1    Wells, W.W.2
  • 12
    • 0033914738 scopus 로고    scopus 로고
    • Galactose metabolism by the mouse with galactose-1-phosphate uridyltransferase deficiency
    • Ning, C., Reynolds, R., Chen, J., Yager, C., Berry, G. T., McNamara, P. D., Leslie, N., and Segal, S. (2000) Galactose metabolism by the mouse with galactose-1-phosphate uridyltransferase deficiency. Pediatr. Res. 48, 211-217. (Pubitemid 30497339)
    • (2000) Pediatric Research , vol.48 , Issue.2 , pp. 211-217
    • Ning, C.1    Reynolds, R.2    Chen, J.3    Yager, C.4    Berry, G.T.5    McNamara, P.D.6    Leslie, N.7    Segal, S.8
  • 13
    • 0023894728 scopus 로고
    • Galactose and cataract
    • Stambolian, D. (1988) Galactose and cataract. Surv. Ophthalmol. 32, 333-349.
    • (1988) Surv. Ophthalmol. , vol.32 , pp. 333-349
    • Stambolian, D.1
  • 14
    • 0018931130 scopus 로고
    • Pitfalls in the radioactive method of galactose-1-phosphate uridyltransferase activity measurement
    • Shin-Buehring, Y. S. and Schaub, J. (1980) Pitfalls in the radioactive method of galactose-1-phosphate uridyltransferase activity measurement. Clin. Chim. Acta. 106, 231-234.
    • (1980) Clin. Chim. Acta. , vol.106 , pp. 231-234
    • Shin-Buehring, Y.S.1    Schaub, J.2
  • 19
    • 13244292426 scopus 로고    scopus 로고
    • Maternal phenylketonuria: Report from the United Kingdom Registry 1978-97
    • Lee, P. J., Ridout, D., Walter, J. H., and Cockburn, F. (2005) Maternal phenylketonuria: report from the United Kingdom Registry 1978-97. Arch. Dis. Child. 90, 143-146.
    • (2005) Arch. Dis. Child. , vol.90 , pp. 143-146
    • Lee, P.J.1    Ridout, D.2    Walter, J.H.3    Cockburn, F.4
  • 22
    • 0029898949 scopus 로고    scopus 로고
    • Maternal phenylketonuria: Magnetic resonance imaging of the brain in offspring
    • Levy, H. L., Lobbregt, D., Barnes, P. D., and Poussaint, T. Y. (1996) Maternal phenylketonuria: magnetic resonance imaging of the brain in offspring. J. Pediatr. 128, 770-775.
    • (1996) J. Pediatr. , vol.128 , pp. 770-775
    • Levy, H.L.1    Lobbregt, D.2    Barnes, P.D.3    Poussaint, T.Y.4
  • 23
    • 0019156116 scopus 로고
    • Maternal phenylketonuria and hyperphenylalaninemia. An international survey of the outcome of untreated and treated pregnancies
    • Lenke, R. R., and Levy, H. L. (1980) Maternal phenylketonuria and hyperphenylalaninemia. An international survey of the outcome of untreated and treated pregnancies. N. Engl. J. Med. 303, 1202-1208.
    • (1980) N. Engl. J. Med. , vol.303 , pp. 1202-1208
    • Lenke, R.R.1    Levy, H.L.2
  • 25
    • 0025083324 scopus 로고
    • Transport of amino acids by the human placenta: Predicted effects thereon of maternal hyperphenylalaninaemia
    • Kudo, Y. and Boyd, C. A. (1990) Transport of amino acids by the human placenta: predicted effects thereon of maternal hyperphenylalaninaemia. J. Inherit. Metab. Dis. 13, 617-626.
    • (1990) J. Inherit. Metab. Dis. , vol.13 , pp. 617-626
    • Kudo, Y.1    Boyd, C.A.2
  • 26
    • 0029977276 scopus 로고    scopus 로고
    • Maternal phenylketonuria: A metabolic teratogen
    • Levy, H. L. and Ghavami, M. (1996) Maternal phenylketonuria: a metabolic teratogen. Teratology 53, 176-184.
    • (1996) Teratology , vol.53 , pp. 176-184
    • Levy, H.L.1    Ghavami, M.2
  • 27
    • 0025172172 scopus 로고
    • Phenylalanine and its metabolites induce embryopathies in mouse embryos in culture
    • Denno, K. M. and Sadler, T. W. (1990) Phenylalanine and its metabolites induce embryopathies in mouse embryos in culture. Teratology 42, 565-570.
    • (1990) Teratology , vol.42 , pp. 565-570
    • Denno, K.M.1    Sadler, T.W.2
  • 28
  • 30
    • 0346753967 scopus 로고    scopus 로고
    • Potential role of tetrahydrobiopterin in the treatment of maternal phenylketonuria
    • Trefz, F. K. and Blau, N. (2003) Potential role of tetrahydrobiopterin in the treatment of maternal phenylketonuria. Pediatrics 112, 1566-1569.
    • (2003) Pediatrics , vol.112 , pp. 1566-1569
    • Trefz, F.K.1    Blau, N.2
  • 31
    • 0141886877 scopus 로고    scopus 로고
    • Niemann-Pick disease type C
    • Vanier, M. T. and Millat, G. (2003) Niemann-Pick disease type C. Clin. Genet. 64, 269-281.
    • (2003) Clin. Genet. , vol.64 , pp. 269-281
    • Vanier, M.T.1    Millat, G.2
  • 32
    • 0033585476 scopus 로고    scopus 로고
    • Prevalence of lysosomal storage disorders
    • Meikle, P. J., Hopwood, J. J., Clague, A. E., and Carey, W. F. (1999) Prevalence of lysosomal storage disorders. JAMA 281, 249-254.
    • (1999) JAMA , vol.281 , pp. 249-254
    • Meikle, P.J.1    Hopwood, J.J.2    Clague, A.E.3    Carey, W.F.4
  • 35
    • 51849116835 scopus 로고    scopus 로고
    • The pathogenesis of Niemann-Pick type C disease: A role for autophagy?
    • Pacheco, C. D. and Lieberman, A. P. (2008) The pathogenesis of Niemann- Pick type C disease: a role for autophagy? Expert Rev. Mol. Med. 10, e26.
    • (2008) Expert Rev. Mol. Med. , vol.10
    • Pacheco, C.D.1    Lieberman, A.P.2
  • 36
    • 15744378799 scopus 로고    scopus 로고
    • Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function
    • Yu, W., Gong, J. S., Ko, M., Garver, W. S., Yanagisawa, K., and Michikawa, M. (2005) Altered cholesterol metabolism in Niemann-Pick type C1 mouse brains affects mitochondrial function. J. Biol. Chem. 280, 11731-11739.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11731-11739
    • Yu, W.1    Gong, J.S.2    Ko, M.3    Garver, W.S.4    Yanagisawa, K.5    Michikawa, M.6
  • 37
    • 64749110513 scopus 로고    scopus 로고
    • TNF-{alpha} plays a role in hepatocyte apoptosis in Niemann-Pick type C liver disease
    • Rimkunas, V. M., Graham, M. J., Crooke, R. M., and Liscum, L. (2009) TNF-{alpha} plays a role in hepatocyte apoptosis in Niemann- Pick type C liver disease. J. Lipid Res. 50, 327-333.
    • (2009) J. Lipid Res. , vol.50 , pp. 327-333
    • Rimkunas, V.M.1    Graham, M.J.2    Crooke, R.M.3    Liscum, L.4
  • 39
    • 0025319480 scopus 로고
    • Fetal ascites: An unusual presentation of Niemann-Pick disease type C
    • Manning, D. J., Price, W. I., and Pearse, R. G. (1990) Fetal ascites: an unusual presentation of Niemann-Pick disease type C. Arch. Dis. Child. 65, 335-336.
    • (1990) Arch. Dis. Child. , vol.65 , pp. 335-336
    • Manning, D.J.1    Price, W.I.2    Pearse, R.G.3
  • 43
    • 33748714980 scopus 로고    scopus 로고
    • Critical assessment of chitotriosidase analysis in the rational laboratory diagnosis of children with Gaucher disease and Niemann-Pick disease type A/B and C
    • Ries, M., Schaefer, E., Luhrs, T., Mani, L., Kuhn, J., Vanier, M. T., Krummenauer, F., Gal, A., Beck, M., and Mengel, E. (2006) Critical assessment of chitotriosidase analysis in the rational laboratory diagnosis of children with Gaucher disease and Niemann-Pick disease type A/B and C. J. Inherit. Metab. Dis. 29, 647-652.
    • (2006) J. Inherit. Metab. Dis. , vol.29 , pp. 647-652
    • Ries, M.1    Schaefer, E.2    Luhrs, T.3    Mani, L.4    Kuhn, J.5    Vanier, M.T.6    Krummenauer, F.7    Gal, A.8    Beck, M.9    Mengel, E.10
  • 46
    • 0035990150 scopus 로고    scopus 로고
    • Prenatal diagnosis of Niemann-Pick diseases types A, B and C
    • Vanier, M. T. (2002) Prenatal diagnosis of Niemann-Pick diseases types A, B and C. Prenat. Diagn. 22, 630-632.
    • (2002) Prenat. Diagn. , vol.22 , pp. 630-632
    • Vanier, M.T.1
  • 49
    • 0035928841 scopus 로고    scopus 로고
    • Critical role for glycosphingolipids in Niemann-Pick disease type C
    • Zervas, M., Somers, K. L., Thrall, M. A., and Walkley, S. U. (2001) Critical role for glycosphingolipids in Niemann-Pick disease type C. Curr. Biol. 11, 1283-1287.
    • (2001) Curr. Biol. , vol.11 , pp. 1283-1287
    • Zervas, M.1    Somers, K.L.2    Thrall, M.A.3    Walkley, S.U.4
  • 50
    • 34547753513 scopus 로고    scopus 로고
    • Miglustat for treatment of Niemann-Pick C disease: A randomised controlled study
    • Patterson, M. C., Vecchio, D., Prady, H., Abel, L., and Wraith, J. E. (2007) Miglustat for treatment of Niemann-Pick C disease: a randomised controlled study. Lancet Neurol. 6, 765-772.
    • (2007) Lancet Neurol. , vol.6 , pp. 765-772
    • Patterson, M.C.1    Vecchio, D.2    Prady, H.3    Abel, L.4    Wraith, J.E.5
  • 52
  • 53
    • 0036581549 scopus 로고    scopus 로고
    • Evidence for fatty acid oxidation in human placenta, and the relationship of fatty acid oxidation enzyme activities with gestational age
    • Rakheja, D., Bennett, M. J., Foster, B. M., Domiati-Saad, R., and Rogers, B. B. (2002) Evidence for fatty acid oxidation in human placenta, and the relationship of fatty acid oxidation enzyme activities with gestational age. Placenta 23, 447-450.
    • (2002) Placenta , vol.23 , pp. 447-450
    • Rakheja, D.1    Bennett, M.J.2    Foster, B.M.3    Domiati-Saad, R.4    Rogers, B.B.5
  • 59
    • 41649106228 scopus 로고    scopus 로고
    • Activities of respiratory chain complexes and pyruvate dehydrogenase in isolated muscle mitochondria in premature neonates
    • Honzik, T., Wenchich, L., Bohm, M., Hansikova, H., Pejznochova, M., Zapadlo, M., Plavka, R., and Zeman, J. (2008) Activities of respiratory chain complexes and pyruvate dehydrogenase in isolated muscle mitochondria in premature neonates. Early Hum. Dev. 84, 269-276.
    • (2008) Early Hum. Dev. , vol.84 , pp. 269-276
    • Honzik, T.1    Wenchich, L.2    Bohm, M.3    Hansikova, H.4    Pejznochova, M.5    Zapadlo, M.6    Plavka, R.7    Zeman, J.8
  • 60
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D. C. (1999) Mitochondrial diseases in man and mouse. Science 283, 1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 61
    • 33745215866 scopus 로고    scopus 로고
    • L-carnitine is synthesized in the human fetalplacental unit: Potential roles in placental and fetal metabolism
    • Oey, N. A., van Vlies, N., Wijburg, F. A., Wanders, R. J., Attie-Bitach, T., and Vaz, F. M. (2006) L-carnitine is synthesized in the human fetalplacental unit: potential roles in placental and fetal metabolism. Placenta 27, 841-846.
    • (2006) Placenta , vol.27 , pp. 841-846
    • Oey, N.A.1    Van Vlies, N.2    Wijburg, F.A.3    Wanders, R.J.4    Attie-Bitach, T.5    Vaz, F.M.6
  • 62
    • 4043162795 scopus 로고    scopus 로고
    • Disrupted blastocoele formation reveals a critical developmental role for long-chain acyl-CoA dehydrogenase
    • Berger, P. S. and Wood, P. A. (2004) Disrupted blastocoele formation reveals a critical developmental role for long-chain acyl-CoA dehydrogenase. Mol. Genet. Metab. 82, 266-272.
    • (2004) Mol. Genet. Metab. , vol.82 , pp. 266-272
    • Berger, P.S.1    Wood, P.A.2
  • 63
    • 0142213246 scopus 로고    scopus 로고
    • Acute respiratory distress syndrome in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies
    • Lundy, C. T., Shield, J. P., Kvittingen, E. A., Vinorum, O. J., Trimble, E. R., and Morris, A. A. (2003) Acute respiratory distress syndrome in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies. J. Inherit. Metab. Dis. 26, 537-541.
    • (2003) J. Inherit. Metab. Dis. , vol.26 , pp. 537-541
    • Lundy, C.T.1    Shield, J.P.2    Kvittingen, E.A.3    Vinorum, O.J.4    Trimble, E.R.5    Morris, A.A.6
  • 64
    • 0036140895 scopus 로고    scopus 로고
    • Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: Clinical presentation and follow-up of 50 patients
    • den Boer, M. E., Wanders, R. J., Morris, A. A., L, I. J., Heymans, H. S., and Wijburg, F. A. (2002) Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: clinical presentation and follow-up of 50 patients. Pediatrics 109, 99-104.
    • (2002) Pediatrics , vol.109 , pp. 99-104
    • Den Boer, M.E.1    Wanders, R.J.2    Morris, A.A.3    L, I.J.4    Heymans, H.S.5    Wijburg, F.A.6
  • 66
    • 0031981027 scopus 로고    scopus 로고
    • Pregnancy complications are frequent in long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency
    • Tyni, T., Ekholm, E., and Pihko, H. (1998) Pregnancy complications are frequent in long-chain 3-hydroxyacyl-coenzyme A dehydrogenase deficiency. Am. J. Obstet. Gynecol. 178, 603-608.
    • (1998) Am. J. Obstet. Gynecol. , vol.178 , pp. 603-608
    • Tyni, T.1    Ekholm, E.2    Pihko, H.3
  • 67
    • 0037603250 scopus 로고    scopus 로고
    • IUGR alters postnatal rat skeletal muscle peroxisome proliferator- activated receptorgamma coactivator-1 gene expression in a fiber specific manner
    • Lane, R. H., Maclennan, N. K., Daood, M. J., Hsu, J. L., Janke, S. M., Pham, T. D., Puri, A. R., and Watchko, J. F. (2003) IUGR alters postnatal rat skeletal muscle peroxisome proliferator-activated receptorgamma coactivator-1 gene expression in a fiber specific manner. Pediatr. Res. 53, 994-1000.
    • (2003) Pediatr. Res. , vol.53 , pp. 994-1000
    • Lane, R.H.1    Maclennan, N.K.2    Daood, M.J.3    Hsu, J.L.4    Janke, S.M.5    Pham, T.D.6    Puri, A.R.7    Watchko, J.F.8
  • 68
    • 0031661215 scopus 로고    scopus 로고
    • In utero programming of chronic disease
    • Barker, D. J. (1998) In utero programming of chronic disease. Clin. Sci. (Lond.) 95, 115-128.
    • (1998) Clin. Sci. (Lond.) , vol.95 , pp. 115-128
    • Barker, D.J.1
  • 69
    • 0029080735 scopus 로고
    • Lethal neonatal deficiency of carnitine palmitoyltransferase II associated with dysgenesis of the brain and kidneys
    • North, K. N., Hoppel, C. L., De Girolami, U., Kozakewich, H. P., and Korson, M. S. (1995) Lethal neonatal deficiency of carnitine palmitoyltransferase II associated with dysgenesis of the brain and kidneys. J. Pediatr. 127, 414-420.
    • (1995) J. Pediatr. , vol.127 , pp. 414-420
    • North, K.N.1    Hoppel, C.L.2    De Girolami, U.3    Kozakewich, H.P.4    Korson, M.S.5
  • 71
    • 0032898281 scopus 로고    scopus 로고
    • Inherited long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency and a fetal-maternal interaction cause maternal liver disease and other pregnancy complications
    • Strauss, A. W., Bennett, M. J., Rinaldo, P., Sims, H. F., O'Brien, L. K., Zhao, Y., Gibson, B., and Ibdah, J. (1999) Inherited long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency and a fetal-maternal interaction cause maternal liver disease and other pregnancy complications. Semin. Perinatol. 23, 100-112.
    • (1999) Semin. Perinatol. , vol.23 , pp. 100-112
    • Strauss, A.W.1    Bennett, M.J.2    Rinaldo, P.3    Sims, H.F.4    O'Brien, L.K.5    Zhao, Y.6    Gibson, B.7    Ibdah, J.8
  • 72
    • 0026085434 scopus 로고
    • Recurrent acute fatty liver of pregnancy associated with a fatty-acid oxidation defect in the offspring
    • Schoeman, M. N., Batey, R. G., and Wilcken, B. (1991) Recurrent acute fatty liver of pregnancy associated with a fatty-acid oxidation defect in the offspring. Gastroenterology 100, 544-548.
    • (1991) Gastroenterology , vol.100 , pp. 544-548
    • Schoeman, M.N.1    Batey, R.G.2    Wilcken, B.3
  • 74
    • 0347091766 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase E1alpha subunit deficiency in a female patient: Evidence of antenatal origin of brain damage and possible etiology of infantile spasms
    • Wada, N., Matsuishi, T., Nonaka, M., Naito, E., and Yoshino, M. (2004) Pyruvate dehydrogenase E1alpha subunit deficiency in a female patient: evidence of antenatal origin of brain damage and possible etiology of infantile spasms. Brain Dev. 26, 57-60.
    • (2004) Brain Dev. , vol.26 , pp. 57-60
    • Wada, N.1    Matsuishi, T.2    Nonaka, M.3    Naito, E.4    Yoshino, M.5
  • 75
    • 0029766887 scopus 로고    scopus 로고
    • Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex
    • Robinson, B. H., MacKay, N., Chun, K., and Ling, M. (1996) Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex. J. Inherit. Metab. Dis. 19, 452-462.
    • (1996) J. Inherit. Metab. Dis. , vol.19 , pp. 452-462
    • Robinson, B.H.1    MacKay, N.2    Chun, K.3    Ling, M.4
  • 76
    • 23044495384 scopus 로고    scopus 로고
    • Disorders of pyruvate metabolism and the tricarboxylic acid cycle
    • Pithukpakorn, M. (2005) Disorders of pyruvate metabolism and the tricarboxylic acid cycle. Mol. Genet. Metab. 85, 243-246.
    • (2005) Mol. Genet. Metab. , vol.85 , pp. 243-246
    • Pithukpakorn, M.1
  • 79
    • 0025757299 scopus 로고
    • Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency
    • Hansen, L. L., Brown, G. K., Kirby, D. M., and Dahl, H. H. (1991) Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency. J Inherit Metab Dis 14, 140-151.
    • (1991) J Inherit Metab Dis , vol.14 , pp. 140-151
    • Hansen, L.L.1    Brown, G.K.2    Kirby, D.M.3    Dahl, H.H.4
  • 83
    • 0030047534 scopus 로고    scopus 로고
    • Therapeutic efficacy of a case of pyruvate dehydrogenase complex deficiency monitored by localized proton magnetic resonance spectroscopy
    • Harada, M., Tanouchi, M., Arai, K., Nishitani, H., Miyoshi, H., and Hashimoto, T. (1996) Therapeutic efficacy of a case of pyruvate dehydrogenase complex deficiency monitored by localized proton magnetic resonance spectroscopy. Magn Reson Imaging 14, 129-133.
    • (1996) Magn Reson Imaging , vol.14 , pp. 129-133
    • Harada, M.1    Tanouchi, M.2    Arai, K.3    Nishitani, H.4    Miyoshi, H.5    Hashimoto, T.6
  • 85
    • 0034951326 scopus 로고    scopus 로고
    • Clinical spectrum and diagnosis of mitochondrial disorders
    • Munnich, A. and Rustin, P. (2001) Clinical spectrum and diagnosis of mitochondrial disorders. Am J Med Genet 106, 4-17.
    • (2001) Am J Med Genet , vol.106 , pp. 4-17
    • Munnich, A.1    Rustin, P.2
  • 87
    • 58149159261 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation disorders presenting in neonates: Clinical manifestations and enzymatic and molecular diagnoses
    • Gibson, K., Halliday, J. L., Kirby, D. M., Yaplito-Lee, J., Thorburn, D. R., and Boneh, A. (2008) Mitochondrial oxidative phosphorylation disorders presenting in neonates: clinical manifestations and enzymatic and molecular diagnoses. Pediatrics 122, 1003-1008.
    • (2008) Pediatrics , vol.122 , pp. 1003-1008
    • Gibson, K.1    Halliday, J.L.2    Kirby, D.M.3    Yaplito-Lee, J.4    Thorburn, D.R.5    Boneh, A.6
  • 90
    • 0033898736 scopus 로고    scopus 로고
    • Heart mitochondrial DNA and enzyme changes during early human development
    • Marin-Garcia, J., Ananthakrishnan, R., and Goldenthal, M. J. (2000) Heart mitochondrial DNA and enzyme changes during early human development. Mol. Cell Biochem. 210, 47-52.
    • (2000) Mol. Cell Biochem. , vol.210 , pp. 47-52
    • Marin-Garcia, J.1    Ananthakrishnan, R.2    Goldenthal, M.J.3
  • 91
    • 41949132639 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain complex as sembly and function during human fetal development
    • Minai, L., Martinovic, J., Chretien, D., Dumez, F., Razavi, F., Munnich, A., and Rotig, A. (2008) Mitochondrial respiratory chain complex as sembly and function during human fetal development. Mol. Genet. Metab. 94, 120-126.
    • (2008) Mol. Genet. Metab. , vol.94 , pp. 120-126
    • Minai, L.1    Martinovic, J.2    Chretien, D.3    Dumez, F.4    Razavi, F.5    Munnich, A.6    Rotig, A.7
  • 92
    • 34547839596 scopus 로고    scopus 로고
    • Mitochondrial differentiation and oxidative phosphorylation system capacity in rat embryo during placentation period
    • Alcolea, M. P., Colom, B., Llado, I., Garcia-Palmer, F. J., and Gianotti, M. (2007) Mitochondrial differentiation and oxidative phosphorylation system capacity in rat embryo during placentation period. Reproduction 134, 147-154.
    • (2007) Reproduction , vol.134 , pp. 147-154
    • Alcolea, M.P.1    Colom, B.2    Llado, I.3    Garcia-Palmer, F.J.4    Gianotti, M.5
  • 93
    • 0030581498 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications
    • Papa, S. (1996) Mitochondrial oxidative phosphorylation changes in the life span. Molecular aspects and physiopathological implications. Biochim. Biophys. Acta. 1276, 87-105.
    • (1996) Biochim. Biophys. Acta. , vol.1276 , pp. 87-105
    • Papa, S.1
  • 94
    • 0025313880 scopus 로고
    • Postnatal mitochondrial differentiation in rat liver. Regulation by thyroid hormones of the beta-subunit of the mitochondrial F1-ATPase complex
    • Izquierdo, J. M., Luis, A. M., and Cuezva, J. M. (1990) Postnatal mitochondrial differentiation in rat liver. Regulation by thyroid hormones of the beta-subunit of the mitochondrial F1-ATPase complex. J. Biol. Chem. 265, 9090-9097.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9090-9097
    • Izquierdo, J.M.1    Luis, A.M.2    Cuezva, J.M.3
  • 95
    • 0028925584 scopus 로고
    • Both nuclear and mitochondrial cytochrome c oxidase mRNA levels increase dramatically during mouse postnatal development
    • Kim, K., Lecordier, A., and Bowman, L. H. (1995) Both nuclear and mitochondrial cytochrome c oxidase mRNA levels increase dramatically during mouse postnatal development. Biochem. J. 306(Pt 2), 353-358.
    • (1995) Biochem. J. , vol.306 , Issue.PART 2 , pp. 353-358
    • Kim, K.1    Lecordier, A.2    Bowman, L.H.3
  • 96
    • 0023951073 scopus 로고
    • Mitochondrial myopathies and respiratory chain proteins
    • Capaldi, R. A. (1988) Mitochondrial myopathies and respiratory chain proteins. Trends Biochem. Sci. 13, 144-148.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 144-148
    • Capaldi, R.A.1
  • 97
    • 0023084648 scopus 로고
    • Benign reversible muscle cytochrome c oxidase deficiency: A second case
    • Zeviani, M., Peterson, P., Servidei, S., Bonilla, E., and DiMauro, S. (1987) Benign reversible muscle cytochrome c oxidase deficiency: a second case. Neurology 37, 64-67.
    • (1987) Neurology , vol.37 , pp. 64-67
    • Zeviani, M.1    Peterson, P.2    Servidei, S.3    Bonilla, E.4    DiMauro, S.5
  • 98
    • 53449088957 scopus 로고    scopus 로고
    • Reversible multiorgan system involvement in a neonate with complex IV deficiency
    • Low, E., Crushell, E. B., Harty, S. B., Ryan, S. P., and Treacy, E. P. (2008) Reversible multiorgan system involvement in a neonate with complex IV deficiency. Pediatr. Neurol. 39, 368-370.
    • (2008) Pediatr. Neurol. , vol.39 , pp. 368-370
    • Low, E.1    Crushell, E.B.2    Harty, S.B.3    Ryan, S.P.4    Treacy, E.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.