메뉴 건너뛰기




Volumn 9, Issue 6, 1996, Pages 477-485

Fatty acid mitochondrial β-oxidation and hypoglycaemia in children

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACID;

EID: 0030469997     PISSN: 13507540     EISSN: None     Source Type: Journal    
DOI: 10.1097/00019052-199612000-00015     Document Type: Review
Times cited : (29)

References (88)
  • 1
    • 0002149987 scopus 로고
    • Effects of glucose deprivation on glucose metabolism in the central nervous system
    • Edited by Frier BM, Fisher BM. London: Edward Arnold
    • McCall AL: Effects of glucose deprivation on glucose metabolism in the central nervous system. In Hypoglycaemia and diabetes: clinical and physiological aspects. Edited by Frier BM, Fisher BM. London: Edward Arnold; 1993:56-71.
    • (1993) Hypoglycaemia and Diabetes: Clinical and Physiological Aspects , pp. 56-71
    • McCall, A.L.1
  • 2
    • 0028941073 scopus 로고
    • Hypoglycemic disorders
    • Service FJ: Hypoglycemic disorders. N Engl J Med 1995, 332:1144-1152.
    • (1995) N Engl J Med , vol.332 , pp. 1144-1152
    • Service, F.J.1
  • 3
    • 0028237748 scopus 로고
    • The enzymes of mitochondrial fatty acid oxidation
    • Bennett MJ: The enzymes of mitochondrial fatty acid oxidation. Clin Chim Acta 1994, 226:211-224.
    • (1994) Clin Chim Acta , vol.226 , pp. 211-224
    • Bennett, M.J.1
  • 4
    • 0028850504 scopus 로고
    • Primary and secondary carnitine deficiency syndromes
    • Pons R, DeVivo DC: Primary and secondary carnitine deficiency syndromes. J Child Neurol 1995, 10:2S8-2S24.
    • (1995) J Child Neurol , vol.10
    • Pons, R.1    DeVivo, D.C.2
  • 5
    • 0000576457 scopus 로고
    • Mitochondrial fatty acid oxidation disorders
    • Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill
    • Roe CR, Coates PM: Mitochondrial fatty acid oxidation disorders. In The metabolic and molecular bases of inherited disease, edn 7. Edited by Scriver CR, Beaudet AL, Sly WS, Valle D. New York: McGraw-Hill; 1995:1501-1533. An authoritative and comprehensive review of the metabolic basis and clinical findings of fatty acid oxidation defects. The authors include a thorough evaluation of the diagnostic approach to patients with suspected β-oxidation disorders.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, Edn 7. , pp. 1501-1533
    • Roe, C.R.1    Coates, P.M.2
  • 6
    • 0029437586 scopus 로고
    • Carnitine disorders
    • Stanley C: Carnitine disorders. Adv Pediatr 1995, 42:209-242.
    • (1995) Adv Pediatr , vol.42 , pp. 209-242
    • Stanley, C.1
  • 7
    • 0027252589 scopus 로고
    • Regulation of fatty acid oxidation in mammalian liver
    • Guzmán M, Geelen MJH: Regulation of fatty acid oxidation in mammalian liver. Biochim Biophys Acta 1993, 1167:227-241.
    • (1993) Biochim Biophys Acta , vol.1167 , pp. 227-241
    • Guzmán, M.1    Geelen, M.J.H.2
  • 8
    • 0027959194 scopus 로고
    • Carnitine-acylcarnitine translocase deficiency: Implications in human pathology
    • Pande SV, Murthy MS: Carnitine-acylcarnitine translocase deficiency: implications in human pathology. Biochim Biophys Acta 1994, 1226:269-276.
    • (1994) Biochim Biophys Acta , vol.1226 , pp. 269-276
    • Pande, S.V.1    Murthy, M.S.2
  • 9
    • 84911349560 scopus 로고    scopus 로고
    • Beta oxidation of fatty acids in mitochondria, peroxisomes and bacteria. A century of continued progress
    • In press
    • Kunau WH, Dommes V, Schulz H: Beta oxidation of fatty acids in mitochondria, peroxisomes and bacteria. A century of continued progress. Prog Lipid Res 1996 (In press).
    • (1996) Prog Lipid Res
    • Kunau, W.H.1    Dommes, V.2    Schulz, H.3
  • 10
    • 0029146749 scopus 로고
    • Characterisation of a novel enzyme of human fatty acid beta-oxidation: A matrix-associated, mitochondrial 2-enoyl-CoA hydratase
    • Jackson S, Schaefer J, Middleton B, Turnbull DM: Characterisation of a novel enzyme of human fatty acid beta-oxidation: a matrix-associated, mitochondrial 2-enoyl-CoA hydratase. Biochem Biophys Res Commun 1995, 214:247-53.
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 247-253
    • Jackson, S.1    Schaefer, J.2    Middleton, B.3    Turnbull, D.M.4
  • 12
    • 0026518372 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long chain acyl-coenzyme A dehydrogenase
    • Izai K, Uchida Y, Orii T, Yamamoto S, Hashimoto T: Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long chain acyl-coenzyme A dehydrogenase. J Biol Chem 1992, 267:1027-1033.
    • (1992) J Biol Chem , vol.267 , pp. 1027-1033
    • Izai, K.1    Uchida, Y.2    Orii, T.3    Yamamoto, S.4    Hashimoto, T.5
  • 13
    • 0026515859 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
    • Uchida Y, Izai K, Orii T, Hashimoto T: Novel fatty acid β-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein. J Biol Chem 1992, 267:1034-1041.
    • (1992) J Biol Chem , vol.267 , pp. 1034-1041
    • Uchida, Y.1    Izai, K.2    Orii, T.3    Hashimoto, T.4
  • 15
    • 0026012964 scopus 로고
    • Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain
    • Sumegi B, Porpaczy Z, Alkonyi I: Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain. Biochim Biophys Acta 1991, 1081:121-128.
    • (1991) Biochim Biophys Acta , vol.1081 , pp. 121-128
    • Sumegi, B.1    Porpaczy, Z.2    Alkonyi, I.3
  • 16
    • 0004173864 scopus 로고
    • Carnitine palmitoyltransferase deficiency
    • (CD-ROM) edn 1. Edited by Gilman S, Goldstein GW, Waxman SG. La Jolla: Arbor Publishing
    • Taroni F: Carnitine palmitoyltransferase deficiency. In Neurobase, (CD-ROM) edn 1. Edited by Gilman S, Goldstein GW, Waxman SG. La Jolla: Arbor Publishing; 1995. An exhaustive review of the clinical, biochemical and molecular aspects of defects of the mitochondrial carnitine palmitoyltransferases.
    • (1995) Neurobase
    • Taroni, F.1
  • 18
    • 0029933864 scopus 로고    scopus 로고
    • The clinical spectrum of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency
    • Pons R, Roig M, Riudor E, Ribes A, Briones P, Ortigosa L, Baldellou A, Gil-Gibernau J, Olesti M, Navarro C, Wanders RJA: The clinical spectrum of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. Pediatr Neurol 1996, 14:236-243. Interesting paper that presents the clinical and biochemical findings in four original LCHAD-deficient patients along with a detailed review of patients with LCHAD deficiency reported in the literature.
    • (1996) Pediatr Neurol , vol.14 , pp. 236-243
    • Pons, R.1    Roig, M.2    Riudor, E.3    Ribes, A.4    Briones, P.5    Ortigosa, L.6    Baldellou, A.7    Gil-Gibernau, J.8    Olesti, M.9    Navarro, C.10    Wanders, R.J.A.11
  • 19
    • 0028353551 scopus 로고
    • Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients
    • Kamijo T, Wanders RJA, Saudubray J-M, Aoyama T, Komiyama A, Hashimoto T: Mitochondrial trifunctional protein deficiency. Catalytic heterogeneity of the mutant enzyme in two patients. J Clin Invest 1994, 93:1740-1747.
    • (1994) J Clin Invest , vol.93 , pp. 1740-1747
    • Kamijo, T.1    Wanders, R.J.A.2    Saudubray, J.-M.3    Aoyama, T.4    Komiyama, A.5    Hashimoto, T.6
  • 20
    • 0029060330 scopus 로고
    • Clinical and biochemical characterization of short-chain acyl-coenzyme A dehydrogenase deficiency
    • Bhala A, Willi SM, Rinaldo P, Bennett MJ, Schmidt Sommerfeld E, Hale DE: Clinical and biochemical characterization of short-chain acyl-coenzyme A dehydrogenase deficiency. J Pediatr 1995, 126:910-915.
    • (1995) J Pediatr , vol.126 , pp. 910-915
    • Bhala, A.1    Willi, S.M.2    Rinaldo, P.3    Bennett, M.J.4    Schmidt Sommerfeld, E.5    Hale, D.E.6
  • 21
    • 0030041154 scopus 로고    scopus 로고
    • Mitochondrial short-chain i-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: A new defect of fatty acid oxidation
    • Bennett MJ, Weinberger MJ, Kobori JA, Rinaldo P, Burlina AB: Mitochondrial short-chain i-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: a new defect of fatty acid oxidation. Pediatr Res 1996, 39:185-188. First documented cases of short-chain L-3-hydroxyacyl-CoA deficiency. Demonstration of the enzyme defect in fibroblasts from two children presenting with fasting-induced vomiting and ketosis, with or without hypoglycaemia.
    • (1996) Pediatr Res , vol.39 , pp. 185-188
    • Bennett, M.J.1    Weinberger, M.J.2    Kobori, J.A.3    Rinaldo, P.4    Burlina, A.B.5
  • 22
    • 0025240731 scopus 로고
    • Glutaric acidemia type II: Heterogeneity of clinical and biochemical phenotypes
    • Loehr JP, Goodman SI, Frerman FE: Glutaric acidemia type II: heterogeneity of clinical and biochemical phenotypes. Pediatr Res 1990, 27:311-315.
    • (1990) Pediatr Res , vol.27 , pp. 311-315
    • Loehr, J.P.1    Goodman, S.I.2    Frerman, F.E.3
  • 23
    • 0027948406 scopus 로고
    • Late-onset riboflavin-responsive myopathy with combined multiple acyl coenzyme A dehydrogenase and respiratory chain deficiency
    • Antozzi C, Garavaglia B, Mora M, Rimoldi M, Morandi L, Ursino E, DiDonato S: Late-onset riboflavin-responsive myopathy with combined multiple acyl coenzyme A dehydrogenase and respiratory chain deficiency. Neurology 1994, 44:2153-2158.
    • (1994) Neurology , vol.44 , pp. 2153-2158
    • Antozzi, C.1    Garavaglia, B.2    Mora, M.3    Rimoldi, M.4    Morandi, L.5    Ursino, E.6    DiDonato, S.7
  • 25
    • 0028040626 scopus 로고
    • Genetic disorders of mitochondrial fatty acid oxidation
    • Stanley CA, Hale DE. Genetic disorders of mitochondrial fatty acid oxidation. Curr Opin Pediatr 1994, 6:476-481.
    • (1994) Curr Opin Pediatr , vol.6 , pp. 476-481
    • Stanley, C.A.1    Hale, D.E.2
  • 26
    • 0025856468 scopus 로고
    • Clinical diagnosis of long-chain acyl-coenzyme A-dehydrogenase deficiency: Use of stress and fat-loading tests
    • Parini R, Garavaglia B, Saudubray JM, Bardelli P, Melotti D, Zecca G, DiDonato S: Clinical diagnosis of long-chain acyl-coenzyme A-dehydrogenase deficiency: use of stress and fat-loading tests. J Pediatr 1991, 119:77-80.
    • (1991) J Pediatr , vol.119 , pp. 77-80
    • Parini, R.1    Garavaglia, B.2    Saudubray, J.M.3    Bardelli, P.4    Melotti, D.5    Zecca, G.6    DiDonato, S.7
  • 29
    • 0028347574 scopus 로고
    • Inherited cardiomyopathies
    • Kelly DP, Strauss AW: Inherited cardiomyopathies. N Engl J Med 1994, 330:913-919.
    • (1994) N Engl J Med , vol.330 , pp. 913-919
    • Kelly, D.P.1    Strauss, A.W.2
  • 30
    • 0028085284 scopus 로고
    • Effects of glucose and fatty acids on myocardial ischaemia and arrhythmias
    • Oliver MF, Opie LH: Effects of glucose and fatty acids on myocardial ischaemia and arrhythmias. Lancet 1994, 343:155-158.
    • (1994) Lancet , vol.343 , pp. 155-158
    • Oliver, M.F.1    Opie, L.H.2
  • 33
    • 0029925716 scopus 로고    scopus 로고
    • Inhibitory effect of 3-hydroxyacyl-CoAs and other long-chain fatty acid β-oxidation intermediates on mitochondrial oxidative phosphorylation
    • •] that present in-vitro evidence of a toxic effect of long-chain acyl-CoA esters on mitochondrial oxidative phosphorylation. The results provide a biochemical rationale for the occurrence of lactic acidemia in some disorders of long-chain fatty acid oxidation.
    • (1996) J Inher Metab Dis , vol.19 , pp. 161-164
    • Ventura, F.V.1    Ruiter, J.P.2    Ijlst, L.3    Tavares De Almeida, I.4    Wanders, R.J.5
  • 35
    • 0028589872 scopus 로고
    • Analysis of fatty acid oxidation intermediates in cultured fibroblasts to detect mitochondrial oxidation disorders
    • Pourfarzam M, Schaefer J, Turnbull DM, Bartlett K: Analysis of fatty acid oxidation intermediates in cultured fibroblasts to detect mitochondrial oxidation disorders. Clin Chem 1994, 40:2267-2275.
    • (1994) Clin Chem , vol.40 , pp. 2267-2275
    • Pourfarzam, M.1    Schaefer, J.2    Turnbull, D.M.3    Bartlett, K.4
  • 36
    • 0031040157 scopus 로고    scopus 로고
    • Characterisation of cellular carnitine acyltransferases in patients with a carnitine palmitoyltransferase deficiency: Implications for diagnosis and therapy
    • In press
    • Schaefer J, Jackson S, Taroni F, Swift P, Turnbull DM: Characterisation of cellular carnitine acyltransferases in patients with a carnitine palmitoyltransferase deficiency: implications for diagnosis and therapy. J Neurol Neurosurg Psychiatry 1996 (In press).
    • (1996) J Neurol Neurosurg Psychiatry
    • Schaefer, J.1    Jackson, S.2    Taroni, F.3    Swift, P.4    Turnbull, D.M.5
  • 37
    • 0028931890 scopus 로고
    • Fatty acid oxidation in peripheral blood cells: Characterisation and use for the diagnosis of defects of fatty acid oxidation
    • 14C]hexadecanoate, β-oxidation flux and acylcarnitine esters formed were measured, demonstrating a characteristic accumulation of acylcarnitines that was pathognomonic for the site of the defect.
    • (1995) Pediatr Res , vol.37 , pp. 354-360
    • Schaefer, J.1    Pourfarzam, M.2    Bartlett, K.3    Jackson, S.4    Turnbull, D.M.5
  • 38
    • 0029090038 scopus 로고
    • Inborn errors of metabolism diagnosed in sudden death cases by acylcarnitine analysis of postmortem bile
    • Rashed MS, Ozand PT, Bennert MJ, Barnard JJ, Govindaraju DR, Rinaldo P: Inborn errors of metabolism diagnosed in sudden death cases by acylcarnitine analysis of postmortem bile. Clin Chem 1995, 41:1109-1114.
    • (1995) Clin Chem , vol.41 , pp. 1109-1114
    • Rashed, M.S.1    Ozand, P.T.2    Bennert, M.J.3    Barnard, J.J.4    Govindaraju, D.R.5    Rinaldo, P.6
  • 39
    • 0029067962 scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system: Its broadening role in fuel homeostasis and new insights into its molecular features
    • McGarry JD: The mitochondrial carnitine palmitoyltransferase system: its broadening role in fuel homeostasis and new insights into its molecular features. Biochem Soc Trans 1995, 23:321-324.
    • (1995) Biochem Soc Trans , vol.23 , pp. 321-324
    • McGarry, J.D.1
  • 41
    • 0028904122 scopus 로고
    • Human liver carnitine palmitoyltransferase I: Characterization of its cDNA and chromosomal localization and partial analysis of the gene
    • Britton CH, Schultz RA, Zhang B, Esser V, Foster DW, McGarry JD: Human liver carnitine palmitoyltransferase I: characterization of its cDNA and chromosomal localization and partial analysis of the gene. Proc Natl Acad Sci U S A 1995, 92:1984-1988.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1984-1988
    • Britton, C.H.1    Schultz, R.A.2    Zhang, B.3    Esser, V.4    Foster, D.W.5    McGarry, J.D.6
  • 44
    • 0029130484 scopus 로고
    • Malonyl-CoA and carnitine palmitoyltransferase I: An expanding partnership
    • McGarry J: Malonyl-CoA and carnitine palmitoyltransferase I: an expanding partnership. Biochem Soc Trans 1995, 23:481-485. A concise review of the current concepts on the carnitine palmitoyltransferase system, mostly based on the author's seminal work on the subject.
    • (1995) Biochem Soc Trans , vol.23 , pp. 481-485
    • McGarry, J.1
  • 46
    • 0025906746 scopus 로고
    • Infantile form of carnitine palmitoyltransferase II deficiency with hepatomuscular symptoms and sudden death. Physiopathological approach to carnitine palmitoyltransferase II deficiencies
    • Demaugre F, Bonnefont J-P, Colonna M, Cepanec C, Leroux J-P, Saudubray JM: Infantile form of carnitine palmitoyltransferase II deficiency with hepatomuscular symptoms and sudden death. Physiopathological approach to carnitine palmitoyltransferase II deficiencies. J Clin Invest 1991, 87:859-864.
    • (1991) J Clin Invest , vol.87 , pp. 859-864
    • Demaugre, F.1    Bonnefont, J.-P.2    Colonna, M.3    Cepanec, C.4    Leroux, J.-P.5    Saudubray, J.M.6
  • 47
    • 0026410146 scopus 로고
    • Lethal neonatal multiorgan deficiency of carnitine palmitoyltransferase II
    • Hug G, Bove KE, Soukup S: Lethal neonatal multiorgan deficiency of carnitine palmitoyltransferase II. N Engl J Med 1991, 325:1862-1864.
    • (1991) N Engl J Med , vol.325 , pp. 1862-1864
    • Hug, G.1    Bove, K.E.2    Soukup, S.3
  • 48
    • 0026620041 scopus 로고
    • Biochemical and molecular studies of carnitine palmitoyltransferase II deficiency with hepatocardiomyopathic presentation
    • Edited by Coates PM, Tanaka K. New York: Wiley-Liss
    • Taroni F, Verderio E, Garavaglia B, Fiorucci S, Finocchiaro G, Uziel G, DiDonato S: Biochemical and molecular studies of carnitine palmitoyltransferase II deficiency with hepatocardiomyopathic presentation. In New developments in fatty acid oxidation. Edited by Coates PM, Tanaka K. New York: Wiley-Liss; 1992:521-531.
    • (1992) New Developments in Fatty Acid Oxidation , pp. 521-531
    • Taroni, F.1    Verderio, E.2    Garavaglia, B.3    Fiorucci, S.4    Finocchiaro, G.5    Uziel, G.6    DiDonato, S.7
  • 49
    • 0027302901 scopus 로고
    • Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients
    • Taroni F, Verderio E, Dworzak F, Willems PJ, Cavadini P, DiDonato S: Identification of a common mutation in the carnitine palmitoyltransferase II gene in familial recurrent myoglobinuria patients. Nature Genet 1993, 4:314-320.
    • (1993) Nature Genet , vol.4 , pp. 314-320
    • Taroni, F.1    Verderio, E.2    Dworzak, F.3    Willems, P.J.4    Cavadini, P.5    DiDonato, S.6
  • 51
    • 0029080735 scopus 로고
    • Lethal neonatal deficiency carnitine palmitoyltransferase II associated with dysgenesis of the brain and kidneys
    • North KN, Hoppel CL, DeGirolami U, Kozakewich HPW, Korson MS: Lethal neonatal deficiency carnitine palmitoyltransferase II associated with dysgenesis of the brain and kidneys. J Pediatr 1995, 127:414-420. An interesting paper that reports the clinicopathologic findings in a patient with the recently recognized neonatal-onset form of CPT-II deficiency. Differential diagnosis with other metabolic defects associated with congenital anomalies of brain and kidney is discussed.
    • (1995) J Pediatr , vol.127 , pp. 414-420
    • North, K.N.1    Hoppel, C.L.2    DeGirolami, U.3    Kozakewich, H.P.W.4    Korson, M.S.5
  • 54
    • 0028840007 scopus 로고
    • Atypical presentation of carnitine palmitoyltransferase (CPT) deficiency as status epilepticus
    • Shintani S, Shiigai T, Sugiyama N: Atypical presentation of carnitine palmitoyltransferase (CPT) deficiency as status epilepticus. J Neurol Sci 1995, 129:69-73.
    • (1995) J Neurol Sci , vol.129 , pp. 69-73
    • Shintani, S.1    Shiigai, T.2    Sugiyama, N.3
  • 55
    • 0029865178 scopus 로고    scopus 로고
    • Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression
    • Bonnefont J-P, Taroni F, Cavadini P, Cepanec C, Brivet M, Saudubray J-M, Leroux J-P, Demaugre F: Molecular analysis of carnitine palmitoyltransferase II deficiency with hepatocardiomuscular expression. Am J Hum Genet 1996, 58:971-978. An interesting report of a second CPT-II mutation causing the hepatocardiomuscular form of the disease. The functional consequences of the mutation were investigated in transfected COS cells. Evidence is presented that a correlation exists between residual LCFA oxidation rates and phenotypic presentation and that CPT-II activity has to be reduced below a critical threshold in order for LCFA oxidation to be impaired.
    • (1996) Am J Hum Genet , vol.58 , pp. 971-978
    • Bonnefont, J.-P.1    Taroni, F.2    Cavadini, P.3    Cepanec, C.4    Brivet, M.5    Saudubray, J.-M.6    Leroux, J.-P.7    Demaugre, F.8
  • 56
    • 0030049020 scopus 로고    scopus 로고
    • Inheritance of the S113L mutation within an inbred family with carnitine palmitoyltransferase enzyme deficiency
    • Handig I, Dams E, Taroni F, van Laere S, de Barsy T, Willems PJ: Inheritance of the S113L mutation within an inbred family with carnitine palmitoyltransferase enzyme deficiency. Hum Genet 1996, 97:291-293.
    • (1996) Hum Genet , vol.97 , pp. 291-293
    • Handig, I.1    Dams, E.2    Taroni, F.3    Van Laere, S.4    De Barsy, T.5    Willems, P.J.6
  • 62
    • 0027207327 scopus 로고
    • Identification of very-long-chain acyl-CoA dehydrogenase deficiency in three patients previously diagnosed with long-chain acyl-CoA dehydrogenase deficiency
    • Yamaguchi S, Indo Y, Coates PM, Hashimoto T, Tanaka K: Identification of very-long-chain acyl-CoA dehydrogenase deficiency in three patients previously diagnosed with long-chain acyl-CoA dehydrogenase deficiency. Pediatr Res 1993, 34:111-113.
    • (1993) Pediatr Res , vol.34 , pp. 111-113
    • Yamaguchi, S.1    Indo, Y.2    Coates, P.M.3    Hashimoto, T.4    Tanaka, K.5
  • 63
    • 0027404491 scopus 로고
    • Very long chain acyl-CoA dehydrogenase deficiency: Identification of a new inborn error of mitochondrial fatty acid oxidation in fibroblasts
    • Bertrand C, Largillière C, Zabot MT, Mathieu M, Vianey-Saban C: Very long chain acyl-CoA dehydrogenase deficiency: identification of a new inborn error of mitochondrial fatty acid oxidation in fibroblasts. Biochim Biophys Acta 1993, 1180:327-329.
    • (1993) Biochim Biophys Acta , vol.1180 , pp. 327-329
    • Bertrand, C.1    Largillière, C.2    Zabot, M.T.3    Mathieu, M.4    Vianey-Saban, C.5
  • 70
    • 0342372539 scopus 로고    scopus 로고
    • Very-long-chain acyl-CoA dehydrogenase deficiency: Two phenotypes with distinctive biochemical findings
    • Nada MA, Vianey-Saban C, Roe CR: Very-long-chain acyl-CoA dehydrogenase deficiency: two phenotypes with distinctive biochemical findings [Abstract]. J Inher Metab Dis 1996, 19(suppl 1):53.
    • (1996) J Inher Metab Dis , vol.19 , Issue.1 SUPPL. , pp. 53
    • Nada, M.A.1    Vianey-Saban, C.2    Roe, C.R.3
  • 71
    • 0028221809 scopus 로고
    • Very long-chain acyl coenzyme A dehydrogenase deficiency presenting with exercise-induced myoglobinuria
    • Ogilvie I, Pourfarzam M, Jackson S, Stockdale C, Bartlett K, Turnbull DM: Very long-chain acyl coenzyme A dehydrogenase deficiency presenting with exercise-induced myoglobinuria. Neurology 1994, 44:467-473.
    • (1994) Neurology , vol.44 , pp. 467-473
    • Ogilvie, I.1    Pourfarzam, M.2    Jackson, S.3    Stockdale, C.4    Bartlett, K.5    Turnbull, D.M.6
  • 73
    • 0029976189 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial trifunctional protein deficiency: Formation of the enzyme complex is important for stabilization of both α- And β-subunits
    • Ushikubo S, Aoyama T, Kamijo T, Wanders RJA, Rinaldo P, Vockley J, Hashimoto T: Molecular characterization of mitochondrial trifunctional protein deficiency: formation of the enzyme complex is important for stabilization of both α- and β-subunits. Am J Hum Genet 1996, 58:979-988. An important paper on the identification and functional characterization of MTP α-and β-subunit mutations in patients with trifunctional protein deficiency. The mutations were modeled in patients' fibroblasts using a vaccinia virus-based expression system. Evidence is provided that mutations in the β-subunit interfere with hetero-octamer assembly and result in a rapid decomposition of MTP.
    • (1996) Am J Hum Genet , vol.58 , pp. 979-988
    • Ushikubo, S.1    Aoyama, T.2    Kamijo, T.3    Rja, W.4    Rinaldo, P.5    Vockley, J.6    Hashimoto, T.7
  • 74
    • 0028597508 scopus 로고
    • Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: Identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein
    • IJlst L, Wanders RJ, Ushikubo S, Kamijo T, Hashimoto T: Molecular basis of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: identification of the major disease-causing mutation in the alpha-subunit of the mitochondrial trifunctional protein. Biochim Biophys Acta 1994, 1215:347-350.
    • (1994) Biochim Biophys Acta , vol.1215 , pp. 347-350
    • Ijlst, L.1    Wanders, R.J.2    Ushikubo, S.3    Kamijo, T.4    Hashimoto, T.5
  • 76
    • 0029063809 scopus 로고
    • Clinical and biochemical presentation of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency
    • Hagenfeldt L, Venizelos N, von Döbeln U: Clinical and biochemical presentation of long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency. J Inher Metab Dis 1995, 18:245-248.
    • (1995) J Inher Metab Dis , vol.18 , pp. 245-248
    • Hagenfeldt, L.1    Venizelos, N.2    Von Döbeln, U.3
  • 77
    • 0028888960 scopus 로고
    • The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy
    • Sims HF, Brackett JC, Powell CK, Treem WR, Hale DE, Bennett MJ, Gibson B, Shapiro S, Strauss AW: The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancy. Proc Natl Acad Sci U S A 1995, 92:841-845. An interesting paper on the identification of the common Glu510Gln mutation in the LCHAD domain of MTP α-subunit in families with children with LCHAD deficiency and mothers with the acute fatty liver of pregnancy syndrome. The pathogenic role of the mutation was demonstrated in a bacterial expression system.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 841-845
    • Sims, H.F.1    Brackett, J.C.2    Powell, C.K.3    Treem, W.R.4    Hale, D.E.5    Bennett, M.J.6    Gibson, B.7    Shapiro, S.8    Strauss, A.W.9
  • 78
    • 0029020112 scopus 로고
    • Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: High frequency of the G1528C mutation with no apparent correlation with the clinical phenotype
    • IJlst L, Ushikubo S, Kamijo T, Hashimoto T, Ruiter JPN, de Klerk JBC, Wanders RJA: Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: high frequency of the G1528C mutation with no apparent correlation with the clinical phenotype. J Inher Metab Dis 1995, 18:241-244.
    • (1995) J Inher Metab Dis , vol.18 , pp. 241-244
    • Ijlst, L.1    Ushikubo, S.2    Kamijo, T.3    Hashimoto, T.4    Ruiter, J.P.N.5    De Klerk, J.B.C.6    Wanders, R.J.A.7
  • 79
    • 0029984560 scopus 로고    scopus 로고
    • Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: A new method to identify the G1528C mutation in genomic DNA showing its high frequency (≈90%) and identification of a new mutation (T2198C)
    • IJlst L, Ruiter JPN, Vreijling J, Wanders RJA: Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency: a new method to identify the G1528C mutation in genomic DNA showing its high frequency (≈90%) and identification of a new mutation (T2198C). J Inher Metab Dis 1996, 19:165-168.
    • (1996) J Inher Metab Dis , vol.19 , pp. 165-168
    • Ijlst, L.1    Ruiter, J.P.N.2    Vreijling, J.3    Wanders, R.J.A.4
  • 83
    • 0028955733 scopus 로고
    • Clinical and neurophysiologic response of myopathy and neuropathy in long-chain i-3-hydroxyacyl-CoA dehydrogenase deficiency to oral prednisone
    • Tein I, Donner EJ, Hale DE, Murphy EG: Clinical and neurophysiologic response of myopathy and neuropathy in long-chain i-3-hydroxyacyl-CoA dehydrogenase deficiency to oral prednisone. Pediatr Neurol 1995, 12:68-76.
    • (1995) Pediatr Neurol , vol.12 , pp. 68-76
    • Tein, I.1    Donner, E.J.2    Hale, D.E.3    Murphy, E.G.4
  • 87
    • 0028859689 scopus 로고
    • Neonatal onset of medium-chain acyl-coenzyme A dehydrogenase deficiency with confusing biochemical features
    • Christodoulou J, Hoare J, Hammond J, Ip WC, Wilcken B: Neonatal onset of medium-chain acyl-coenzyme A dehydrogenase deficiency with confusing biochemical features. J Pediatr 1995, 126:65-68.
    • (1995) J Pediatr , vol.126 , pp. 65-68
    • Christodoulou, J.1    Hoare, J.2    Hammond, J.3    Ip, W.C.4    Wilcken, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.