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Volumn 5, Issue 4, 1996, Pages 461-472

Cloning and characterization of human very-long-chain acyl-CoA dehydrogenase cDNA, chromosomal assignment of the gene and identification in four patients of nine different mutations within the VLCAD gene

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; COMPLEMENTARY DNA; MESSENGER RNA;

EID: 0029881587     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (104)

References (62)
  • 1
    • 0001464908 scopus 로고
    • Boyer, P.D., Lardy, H. and Myrback, K. (eds), Academic Press, New York
    • Beinert, H. (1963) In Boyer, P.D., Lardy, H. and Myrback, K. (eds), The Enzymes. Academic Press, New York, Vol. 7, pp. 447-476.
    • (1963) The Enzymes , vol.7 , pp. 447-476
    • Beinert, H.1
  • 2
    • 0026518372 scopus 로고
    • Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain-acyl-CoA dehydrogenase
    • Izai, K., Uchida, Y., Orii, T , Yamamoto, S. and Hashimoto, T. (1992) Novel fatty acid β-oxidation enzymes in rat liver mitochondria. I. Purification and properties of very-long-chain-acyl-CoA dehydrogenase. J. Biol. Chem., 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
  • 4
    • 0016693009 scopus 로고
    • The purification and some properties of electron transfer flavoprotein and general fatty acyl-Coenzyme A dehydrogenase from pis liver mitochondria
    • Hall, C.L. and Kamin, H. (1975) The purification and some properties of electron transfer flavoprotein and general fatty acyl-Coenzyme A dehydrogenase from pis liver mitochondria. J. Biol. Chem., 250, 3476-3486
    • (1975) J. Biol. Chem. , vol.250 , pp. 3476-3486
    • Hall, C.L.1    Kamin, H.2
  • 5
    • 0022506081 scopus 로고
    • Biosynthesis of variant medium-chain acyl-CoA dehydrogenase in cultured fibroblasts from patients with medium-chain acyl-CoA dehydrogenase deficiency
    • Ikeda, Y., Hale, D.E., Keese, S.M., Coates, P.M. and Tanaka, K. (1986) Biosynthesis of variant medium-chain acyl-CoA dehydrogenase in cultured fibroblasts from patients with medium-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res., 20, 843-847.
    • (1986) Pediatr. Res. , vol.20 , pp. 843-847
    • Ikeda, Y.1    Hale, D.E.2    Keese, S.M.3    Coates, P.M.4    Tanaka, K.5
  • 6
    • 0344221869 scopus 로고
    • Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue
    • Kelly, D P., Kim, J.J.P., Billadello, J.J , Hainline, B.E., Chu, T W and Strauss, A.W. (1987) Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and its expression in enzyme-deficient human tissue. Proc. Natl Acad. Sci. USA, 84, 4068-4072.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4068-4072
    • Kelly, D.P.1    Kim, J.J.P.2    Billadello, J.J.3    Hainline, B.E.4    Chu, T.W.5    Strauss, A.W.6
  • 7
    • 0025273156 scopus 로고
    • Nucleotide sequence of mRNA encoding human isovaleryl-CoA dehydrogenase and its expression in isovaleric acidemia fibroblast cell lines
    • Matsubara, Y., Ito, M., Glassberg, R., Satyabhama, S., Ikeda, Y. and Tanaka K (1990) Nucleotide sequence of mRNA encoding human isovaleryl-CoA dehydrogenase and its expression in isovaleric acidemia fibroblast cell lines. J. Clin. Invest., 85, 1058-1064.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1058-1064
    • Matsubara, Y.1    Ito, M.2    Glassberg, R.3    Satyabhama, S.4    Ikeda, Y.5    Tanaka, K.6
  • 8
    • 0024599589 scopus 로고
    • Molecular cloning and nucleotide sequence of complementary DNAs encoding human short-chain acyl-CoA dehydrogenase and the study of the molecular basis of human short-chain acyl-Coenzyme A dehydrogenase deficiency
    • Naito, E., Ozasa, H., Ikeda, Y. and Tanaka, K. (1989) Molecular cloning and nucleotide sequence of complementary DNAs encoding human short-chain acyl-CoA dehydrogenase and the study of the molecular basis of human short-chain acyl-Coenzyme A dehydrogenase deficiency. J. Clin. Invest., 83, 1605-1613.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1605-1613
    • Naito, E.1    Ozasa, H.2    Ikeda, Y.3    Tanaka, K.4
  • 9
    • 0025991444 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase (LCAD) and assignment of the location of its gene (ACADL) to chromosome 2
    • Indo, Y., Yang-Feng, T., Glassberg, R. and Tanaka, K. (1991) Molecular cloning and nucleotide sequence of cDNAs encoding human long-chain acyl-CoA dehydrogenase (LCAD) and assignment of the location of its gene (ACADL) to chromosome 2. Genomics, 11, 609-620.
    • (1991) Genomics , vol.11 , pp. 609-620
    • Indo, Y.1    Yang-Feng, T.2    Glassberg, R.3    Tanaka, K.4
  • 10
    • 0028569536 scopus 로고
    • Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family
    • Rozen, R., Vockley, J., Zhou, L., Milos, R., Willard, J., Fu, K., Vicanek, C., Low-Nang, L., Torban, E. and Fournier, B. (1994) Isolation and expression of a cDNA encoding the precursor for a novel member (ACADSB) of the acyl-CoA dehydrogenase gene family. Genomics, 24, 280-287.
    • (1994) Genomics , vol.24 , pp. 280-287
    • Rozen, R.1    Vockley, J.2    Zhou, L.3    Milos, R.4    Willard, J.5    Fu, K.6    Vicanek, C.7    Low-Nang, L.8    Torban, E.9    Fournier, B.10
  • 11
    • 0025115139 scopus 로고
    • The Acyl-CoA dehydrogenase family: Homology and divergence of primary sequence of four acyl-CoA dehydrogenases, and consideration of their functional significance
    • Tanaka, K. and Coates, P. (eds) Alan R. Liss, New York
    • Tanaka, K., Matsubara, Y., Indo, Y., Naito, E., Kraus, J. and Ozasa, H. (1990) The Acyl-CoA dehydrogenase family: Homology and divergence of primary sequence of four acyl-CoA dehydrogenases, and consideration of their functional significance. In Tanaka, K. and Coates, P. (eds) Fatty acid oxidation: clinical, biochemical and molecular aspects, Alan R. Liss, New York, pp. 577-589.
    • (1990) Fatty Acid Oxidation: Clinical, Biochemical and Molecular Aspects , pp. 577-589
    • Tanaka, K.1    Matsubara, Y.2    Indo, Y.3    Naito, E.4    Kraus, J.5    Ozasa, H.6
  • 13
    • 0027404491 scopus 로고
    • Very-long-chain acyl-CoA dehydrogenase deficiency: Identification of new inborn error of mitochondrial fatty acid oxidation in fibroblasts
    • Bertrand, C., Largillière, C., Zabot, M.T., Mathieu, M. and Vianey-Saban C (1993) Very-long-chain acyl-CoA dehydrogenase deficiency: identification of new inborn error of mitochondrial fatty acid oxidation in fibroblasts. Biochim. Biophys. Acta., 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
  • 14
    • 0000576457 scopus 로고
    • Mitochondrial fatty acid oxidation disorders
    • Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle, D. (eds), McGraw-Hill, New York
    • Roe, C.R. and Coates, P.M. (1995) Mitochondrial fatty acid oxidation disorders In: Scriver, C.R., Beaudet, A.L., Sly, W.S. and Valle, D. (eds), The metabolic and molecular bases of inherited disease. McGraw-Hill, New York, pp. 1501-1533.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1501-1533
    • Roe, C.R.1    Coates, P.M.2
  • 15
    • 0021970335 scopus 로고
    • Purification and characterization of short-chain, medium-chain and long-chain acyl-CoA dehydrogenases from rat liver mitochondria
    • Ikeda, Y., Okamura-Ikeda, K. and Tanaka, K. (1985) Purification and characterization of short-chain, medium-chain and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. J. Biol. Chem., 260, 1311-1325.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1311-1325
    • Ikeda, Y.1    Okamura-Ikeda, K.2    Tanaka, K.3
  • 16
  • 17
    • 0025913135 scopus 로고
    • Immunochemical characterization of variant long-chain acyl-CoA dehydrogenase in cultured fibroblasts from nine patients with long-chain acyl-CoA dehydrogenase deficiency
    • Indo, Y., Coates, P.M., Hale, D.E. and Tanaka, K. (1991) Immunochemical characterization of variant long-chain acyl-CoA dehydrogenase in cultured fibroblasts from nine patients with long-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res., 30, 211-215
    • (1991) Pediatr. Res. , vol.30 , pp. 211-215
    • Indo, Y.1    Coates, P.M.2    Hale, D.E.3    Tanaka, K.4
  • 18
    • 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, P.M., Hashimoto, T. and Tanaka, K (1993) Identification of very-long-chain Acyl-CoA dehydrogenase deficiency in three patients previously diagnosed with long-chain acyl-CoA dehydrogenase deficiency. Pediatr. Res., 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
  • 19
    • 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. and Turnbull, D.M. (1994) Very long-chain acyl-coenzyme A dehydrogenase deficiency presenting with exercise-induced myoglobinuria. Neurology, 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
  • 20
    • 0029073089 scopus 로고
    • Cloning of human very-long-chain acyl-Coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients
    • Aoyama, T., Souri, M., Ueno, I., Kamijo, T., Yamaguchi, S., Rhead, W.J., Tanaka, K. and Hashimoto, T. (1995) Cloning of human very-long-chain acyl-Coenzyme A dehydrogenase and molecular characterization of its deficiency in two patients. Am J. Hum. Genet., 57, 273-283.
    • (1995) Am J. Hum. Genet. , vol.57 , pp. 273-283
    • Aoyama, T.1    Souri, M.2    Ueno, I.3    Kamijo, T.4    Yamaguchi, S.5    Rhead, W.J.6    Tanaka, K.7    Hashimoto, T.8
  • 21
    • 0028229531 scopus 로고
    • Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial Acyl-CoA dehydrogenase gene product is a rate-limiting enzyme in long-chain fatty acid β-oxidation system
    • Aoyama, T., Ueno, I., Kamijo, T. and Hashimoto, T. (1994) Rat very-long-chain acyl-CoA dehydrogenase, a novel mitochondrial Acyl-CoA dehydrogenase gene product is a rate-limiting enzyme in long-chain fatty acid β-oxidation system. J. Biol. Chem , 269, 19088-19094.
    • (1994) J. Biol. Chem , vol.269 , pp. 19088-19094
    • Aoyama, T.1    Ueno, I.2    Kamijo, T.3    Hashimoto, T.4
  • 22
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. (1989) The scanning model for translation: an update. J. Cell. Biol , 108, 229-241.
    • (1989) J. Cell. Biol , vol.108 , pp. 229-241
    • Kozak, M.1
  • 23
    • 0022366770 scopus 로고
    • Transcription termination and 3′ processing: The end is in site!
    • Birnstiel, M.L. Busslinger, M. and Strub, K (1985) Transcription termination and 3′ processing: The end is in site! Cell, 41, 349-359.
    • (1985) Cell , vol.41 , pp. 349-359
    • Birnstiel, M.L.1    Busslinger, M.2    Strub, K.3
  • 24
    • 0026793436 scopus 로고
    • Purification of electron transfer flavoprotein from pig liver mitochondria and its application to the diagnosis of deficiencies of acyl-CoA dehydrogenases in human fibroblasts Clin
    • Bertrand, C., Dumoulin, R., Divry, P., Mathieu, M. and Vianey-Saban, C. (1992) Purification of electron transfer flavoprotein from pig liver mitochondria and its application to the diagnosis of deficiencies of acyl-CoA dehydrogenases in human fibroblasts Clin. Chim. Acta., 210, 75-91.
    • (1992) Chim. Acta. , vol.210 , pp. 75-91
    • Bertrand, C.1    Dumoulin, R.2    Divry, P.3    Mathieu, M.4    Vianey-Saban, C.5
  • 26
    • 0025355921 scopus 로고
    • Characterization of wild-type and an active site mutant of human medium-chain acyl-CoA dehydrogenase after expression in Escherichia coli
    • Bross, P., Engst, S., Strauss, A.W., Kelly, D.P., Rasched, I. and Ghisla, S. (1990) Characterization of wild-type and an active site mutant of human medium-chain acyl-CoA dehydrogenase after expression in Escherichia coli. J. Biol. Chem., 265, 7116-7119.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7116-7119
    • Bross, P.1    Engst, S.2    Strauss, A.W.3    Kelly, D.P.4    Rasched, I.5    Ghisla, S.6
  • 27
    • 0027304244 scopus 로고
    • Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate
    • Kim, J.J P., Wang, M. and Paschke, R. (1993) Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate. Proc. Natl Acad. Sci. USA, 90, 7523-7527.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7523-7527
    • Kim, J.J.P.1    Wang, M.2    Paschke, R.3
  • 29
    • 0026719449 scopus 로고
    • Evolution of the acyl-CoA dehydrogenase/ oxidase superfamily
    • Coates, P.M. and Tanaka, K. (eds): Wiley-Liss Inc. New York
    • Tanaka, K. and Indo, Y. (1992) Evolution of the acyl-CoA dehydrogenase/ oxidase superfamily. In Coates, P.M. and Tanaka, K. (eds): New developments in fatty acid oxidation. Wiley-Liss Inc. New York, pp. 95-110.
    • (1992) New Developments in Fatty Acid Oxidation , pp. 95-110
    • Tanaka, K.1    Indo, Y.2
  • 31
    • 0028919340 scopus 로고
    • Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of the medium-chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria
    • Saijo, T. and Tanaka, K. (1995) Isoalloxazine ring of FAD is required for the formation of the core in the Hsp60-assisted folding of the medium-chain acyl-CoA dehydrogenase subunit into the assembly competent conformation in mitochondria. J. Biol. Chem., 270, 1899-1907.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1899-1907
    • Saijo, T.1    Tanaka, K.2
  • 36
    • 0028022999 scopus 로고
    • An in-frame deletion of codon 298 of the NADH-Cytochrome b5 reductase gene results in Methemoglobinemia type II
    • Shirabe K., Fujimoto, Y., Yubisui, T. and Takeshita, M (1994) An in-frame deletion of codon 298 of the NADH-Cytochrome b5 reductase gene results in Methemoglobinemia type II. J. Biol. Chem., 269, 5952-5957.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5952-5957
    • Shirabe, K.1    Fujimoto, Y.2    Yubisui, T.3    Takeshita, M.4
  • 37
    • 0027487912 scopus 로고
    • Deletion of arginine (608) in acid sphingomyelinase is the prevalent mutation among Niemann-Pick disease type B patients from northern Africa
    • Vanier, M.T., Ferlinz, K., Rousson, R., Duthel, S., Louisot, P., Sandhoff, K. and Suzuki, K. (1993) Deletion of arginine (608) in acid sphingomyelinase is the prevalent mutation among Niemann-Pick disease type B patients from northern Africa. Hum. Genet., 92, 325-330.
    • (1993) Hum. Genet. , vol.92 , pp. 325-330
    • Vanier, M.T.1    Ferlinz, K.2    Rousson, R.3    Duthel, S.4    Louisot, P.5    Sandhoff, K.6    Suzuki, K.7
  • 38
    • 0027369381 scopus 로고
    • Cooverexpression of bacterial GroESL chaperonins overcomes non-productive folding into tetramers assembly of E.coli expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation
    • Bross, P., Andresen, B.S., Winter, V., Kräutle, F., Jensen, T.G., Nandy, A., Kølvraa, S., Ghisla, S., Bolund, L. and Gregersen, N. (1993) Cooverexpression of bacterial GroESL chaperonins overcomes non-productive folding into tetramers assembly of E.coli expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim. Biophys. Acta., 1182, 264-274.
    • (1993) Biochim. Biophys. Acta , vol.1182 , pp. 264-274
    • Bross, P.1    Andresen, B.S.2    Winter, V.3    Kräutle, F.4    Jensen, T.G.5    Nandy, A.6    Kølvraa, S.7    Ghisla, S.8    Bolund, L.9    Gregersen, N.10
  • 42
    • 0025912906 scopus 로고
    • Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia
    • Vockley, J., Parimoo, B and Tanaka, K. (1991) Molecular characterization of four different classes of mutations in the isovaleryl-CoA dehydrogenase gene responsible for isovaleric acidemia. Am. J Hum. Genet., 49, 147-157.
    • (1991) Am. J Hum. Genet. , vol.49 , pp. 147-157
    • Vockley, J.1    Parimoo, B.2    Tanaka, K.3
  • 43
    • 0018764020 scopus 로고
    • β0 thalassemia, a nonsense mutation in man
    • Chang, J.C. and Kan, Y.W. (1979) β0 thalassemia, a nonsense mutation in man. Proc. Natl Acad. Sci. USA., 76, 2886-2889.
    • (1979) Proc. Natl Acad. Sci. USA. , vol.76 , pp. 2886-2889
    • Chang, J.C.1    Kan, Y.W.2
  • 44
    • 0024121631 scopus 로고
    • Nonsense mutations in the human β-globin gene affect mRNA metabolism
    • Baserga, S.J. and Benz, E.J. Jr. (1988) Nonsense mutations in the human β-globin gene affect mRNA metabolism. Proc. Natl Acad. Sci. USA., 85, 2056-2060.
    • (1988) Proc. Natl Acad. Sci. USA. , vol.85 , pp. 2056-2060
    • Baserga, S.J.1    Benz Jr., E.J.2
  • 45
    • 0026506370 scopus 로고
    • β-globin nonsense mutation: Deficient accumulation of mRNA occurs despite normal cytoplasmic stability
    • Baserga, S.J. and Benz, E.J. Jr. (1992) β-globin nonsense mutation: deficient accumulation of mRNA occurs despite normal cytoplasmic stability. Proc. Natl Acad. Sci. USA., 89, 2935-2939.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2935-2939
    • Baserga, S.J.1    Benz Jr., E.J.2
  • 46
    • 0026096951 scopus 로고
    • Hypoglycemia, hypotonia and cardiomyopathy: The evolving clinical picture of long-chain acyl-CoA dehydrogenase deficiency
    • Treem, W.R., Stanley, C.A., Hale, D.E., Leopold, H.B. and Hyams, J.S. (1991) Hypoglycemia, hypotonia and cardiomyopathy: The evolving clinical picture of long-chain acyl-CoA dehydrogenase deficiency. Pediatrics, 87, 328-333.
    • (1991) Pediatrics , vol.87 , pp. 328-333
    • Treem, W.R.1    Stanley, C.A.2    Hale, D.E.3    Leopold, H.B.4    Hyams, J.S.5
  • 47
    • 0028950214 scopus 로고
    • Evidence for intermediate channeling in mitochondrial β-oxidation
    • Nada, M.A., Rhead, W.J., Sprecher, H., Schulz, H. and Roe, C.R. (1995) Evidence for intermediate channeling in mitochondrial β-oxidation. J. Biol. Chem., 270, 530-535.
    • (1995) J. Biol. Chem. , vol.270 , pp. 530-535
    • Nada, M.A.1    Rhead, W.J.2    Sprecher, H.3    Schulz, H.4    Roe, C.R.5
  • 48
    • 0024551414 scopus 로고
    • Prophylaxis of early ventricular fibrillation by inhibition of acylcarnitine accumulation
    • Corr, P.B., Creer, M H., Yamada, K.A., Saffitz, J.E. and Sobel, B.E. (1988) Prophylaxis of early ventricular fibrillation by inhibition of acylcarnitine accumulation. J. Clin. Invest., 83, 927-936.
    • (1988) J. Clin. Invest. , vol.83 , pp. 927-936
    • Corr, P.B.1    Creer, M.H.2    Yamada, K.A.3    Saffitz, J.E.4    Sobel, B.E.5
  • 49
    • 0026621735 scopus 로고
    • The role of tandem mass spectrometry in the diagnosis of fatty acid oxidation disorders
    • Coates, P.M. and Tanaka, K. (eds): New York, Wiley-Liss
    • Millington, D.S., Terada, N., Chace, D.H., Chen, Y.T., Ding, J.H., Kodo, N., Roe, C.R. (1992) The role of tandem mass spectrometry in the diagnosis of fatty acid oxidation disorders. In Coates, P.M. and Tanaka, K. (eds): New Developments in Fatty Acid Oxidation, New York, Wiley-Liss, pp. 339-354.
    • (1992) New Developments in Fatty Acid Oxidation , pp. 339-354
    • Millington, D.S.1    Terada, N.2    Chace, D.H.3    Chen, Y.T.4    Ding, J.H.5    Kodo, N.6    Roe, C.R.7
  • 50
    • 0026010499 scopus 로고
    • Specific diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in dried blood spots by a polymerase chain reaction (PCR) assay detecting a point-mutation (G985) in the MCAD gene
    • Gregersen, N., Blakemore, A.I.F., Winter, V., Andresen, B.S., Kølvraa, S., Bolund, L., Curtis, D. and Engel, P.C. (1991) Specific diagnosis of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency in dried blood spots by a polymerase chain reaction (PCR) assay detecting a point-mutation (G985) in the MCAD gene. Clin. Chim. Acta., 203, 23-34.
    • (1991) Clin. Chim. Acta. , vol.203 , pp. 23-34
    • Gregersen, N.1    Blakemore, A.I.F.2    Winter, V.3    Andresen, B.S.4    Kølvraa, S.5    Bolund, L.6    Curtis, D.7    Engel, P.C.8
  • 51
    • 0026322069 scopus 로고
    • Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency
    • Yokota, I., Coates, P., Hale, D.E., Rinaldo, P. and Tanaka, K. (1991) Molecular survey of a prevalent mutation, 985A-to-G transition, and identification of five infrequent mutations in the medium-chain acyl-CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency Am. J. Hum. Genet., 49, 1280-1291.
    • (1991) Am. J. Hum. Genet. , vol.49 , pp. 1280-1291
    • Yokota, I.1    Coates, P.2    Hale, D.E.3    Rinaldo, P.4    Tanaka, K.5
  • 53
    • 0022974709 scopus 로고
    • Molecular cloning of cDNAs encoding rat and human medium-chain acyl-CoA dehydrogenase and assignment of the gene to human chromosome 1
    • Matsubara, Y., Kraus, J.P., Yang-Feng, T.L., Francke, U , Rosenberg, L.E. and Tanaka, K. (1986) Molecular cloning of cDNAs encoding rat and human medium-chain acyl-CoA dehydrogenase and assignment of the gene to human chromosome 1. Proc. Natl Acad. Sci. USA, 83, 6543-6547.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6543-6547
    • Matsubara, Y.1    Kraus, J.P.2    Yang-Feng, T.L.3    Francke, U.4    Rosenberg, L.E.5    Tanaka, K.6
  • 54
    • 0028915206 scopus 로고
    • Localization of short/branched chain acyl-CoA dehydrogenase (ACADSB) to human chromosome 10
    • Arden, K.C., Viars, C.S., Fu, K. and Rozen, R. (1995) Localization of short/branched chain acyl-CoA dehydrogenase (ACADSB) to human chromosome 10. Genomics, 25, 743-745.
    • (1995) Genomics , vol.25 , pp. 743-745
    • Arden, K.C.1    Viars, C.S.2    Fu, K.3    Rozen, R.4
  • 55
    • 0343672573 scopus 로고
    • Short chain acyl-CoA dehydrogenase (ACADS) maps to chromosome 12 (q22-qter) and electron transfer flavoprotein (ETFA) to 15 (q23-q25)
    • Barton, D.E., Yang-Feng, T.L., Finocchiaro, G., Ozasa, H., Tanaka, K. and Francke, U. (1987) Short chain acyl-CoA dehydrogenase (ACADS) maps to chromosome 12 (q22-qter) and electron transfer flavoprotein (ETFA) to 15 (q23-q25). Cytogenet. Cell. Genet., 46, 577.
    • (1987) Cytogenet. Cell. Genet. , vol.46 , pp. 577
    • Barton, D.E.1    Yang-Feng, T.L.2    Finocchiaro, G.3    Ozasa, H.4    Tanaka, K.5    Francke, U.6
  • 56
    • 0028199629 scopus 로고
    • Isolation of the human peroxisomal acyl-CoA oxidase gene: Organization, promoter analysis, and chromosomal localization
    • Varanasi, U., Chu, R., Chu, S., Espinosa, R., LeBeau, M.M and Reddy, J.K. (1994) Isolation of the human peroxisomal acyl-CoA oxidase gene: Organization, promoter analysis, and chromosomal localization. Proc. Natl Acad. Sci. USA, 91, 3107-3111
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3107-3111
    • Varanasi, U.1    Chu, R.2    Chu, S.3    Espinosa, R.4    LeBeau, M.M.5    Reddy, J.K.6
  • 57
    • 0029084073 scopus 로고
    • Cloning of glutaryl-CoA dehydrogenase, and expression of wild type and mutant enzymes in Escherichia coli
    • Goodman, S.I., Kratz, L.E., DiGiulio, K.A., Biery, B.J., Goodman, K., Isaya, G. and Frerman, F.E. (1995) Cloning of glutaryl-CoA dehydrogenase, and expression of wild type and mutant enzymes in Escherichia coli. Hum. Mol. Genet., 9, 1493-1498.
    • (1995) Hum. Mol. Genet. , vol.9 , pp. 1493-1498
    • Goodman, S.I.1    Kratz, L.E.2    DiGiulio, K.A.3    Biery, B.J.4    Goodman, K.5    Isaya, G.6    Frerman, F.E.7
  • 58
  • 59
    • 0021943592 scopus 로고
    • Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts
    • Frerman, F.E. and Goodman, S.J. (1985) Fluorometric assay of acyl-CoA dehydrogenases in normal and mutant human fibroblasts. Biochem. Med , 33, 38-44.
    • (1985) Biochem. Med , vol.33 , pp. 38-44
    • Frerman, F.E.1    Goodman, S.J.2
  • 60
    • 0025808797 scopus 로고
    • Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: Identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant protein in E. coli
    • Gregersen, N., Andresen, B.S., Bross, P., Winter, V., Rüdiger, N., Engst, S., Christensen, E., Kelly, D., Strauss, A.W., Kølvraa, S., Bolund, L., and Ghisla, S. (1991) Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: Identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant protein in E. coli. Hum. Genet., 86, 545-551.
    • (1991) Hum. Genet. , vol.86 , pp. 545-551
    • Gregersen, N.1    Andresen, B.S.2    Bross, P.3    Winter, V.4    Rüdiger, N.5    Engst, S.6    Christensen, E.7    Kelly, D.8    Strauss, A.W.9    Kølvraa, S.10    Bolund, L.11    Ghisla, S.12
  • 61
    • 0021381028 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A P. and Vogelstein, B. (1984) A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 137, 66-267
    • (1984) Anal. Biochem. , vol.137 , pp. 66-267
    • Feinberg, A.P.1    Vogelstein, B.2


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