메뉴 건너뛰기




Volumn 272, Issue 19, 2005, Pages 4874-4883

3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease

Author keywords

oxidation disorder; Alzheimer's disease; Branched chain fatty acid oxidation; Mental retardation; Parkinson's disease

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; BUTYRYL COENZYME A DEHYDROGENASE; FATTY ACID; ISOLEUCINE;

EID: 26244465858     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04911.x     Document Type: Conference Paper
Times cited : (90)

References (78)
  • 1
    • 0034467588 scopus 로고    scopus 로고
    • Molecular mechanism of fatty acid β-oxidation enzyme catalysis
    • Yang SY & He XY (1999) Molecular mechanism of fatty acid β-oxidation enzyme catalysis. Adv Exp Med Biol 466, 133-143.
    • (1999) Adv Exp Med Biol , vol.466 , pp. 133-143
    • Yang, S.Y.1    He, X.Y.2
  • 2
    • 26244441799 scopus 로고    scopus 로고
    • Fatty acid oxidation
    • (Lennarz W & Lane MD, eds). Elsevier, San Diego, CA
    • Schulz H (2004) Fatty acid oxidation. In Encyclopedia of Biological Chemistry (Lennarz W & Lane MD, eds), pp. 90-94. Elsevier, San Diego, CA.
    • (2004) Encyclopedia of Biological Chemistry , pp. 90-94
    • Schulz, H.1
  • 3
    • 0000044868 scopus 로고    scopus 로고
    • Mitochondrial fatty acid oxidation disorders
    • (Scriver C, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW & Vogelstein B, eds), 8th edn. McGraw-Hill, New York, NY
    • Roe CR & Ding J (2001) Mitochondrial fatty acid oxidation disorders. In The Metabolic and Molecular Basis of Inherited Disease (Scriver C, Beaudet AL, Sly WS, Valle D, Childs B, Kinzler KW & Vogelstein B, eds), pp. 2297-2326, 8th edn. McGraw-Hill, New York, NY.
    • (2001) The Metabolic and Molecular Basis of Inherited Disease , pp. 2297-2326
    • Roe, C.R.1    Ding, J.2
  • 4
    • 0036985004 scopus 로고    scopus 로고
    • Defects of β-oxidation including carnitine deficiency
    • Bartlett K & Pourfarzam M (2002) Defects of β-oxidation including carnitine deficiency. Int Rev Neurobiol 53, 469-516.
    • (2002) Int Rev Neurobiol , vol.53 , pp. 469-516
    • Bartlett, K.1    Pourfarzam, M.2
  • 6
    • 0036171573 scopus 로고    scopus 로고
    • Defects of mitochondrial β-oxidation: A growing group of disorders
    • Vockley J & Whiteman DAH (2002) Defects of mitochondrial β-oxidation: a growing group of disorders. Neuromus Disord 12, 235-246.
    • (2002) Neuromus Disord , vol.12 , pp. 235-246
    • Vockley, J.1    Whiteman, D.A.H.2
  • 7
    • 19144367242 scopus 로고
    • β-hydroxyacyl-CoA dehydrogenase
    • (Boyer PD & Myrback K, eds). Academic Press, New York, NY
    • Wakil SJ (1963) β-Hydroxyacyl-CoA dehydrogenase. In The Enzyme (Boyer PD & Myrback K, eds), Vol. 7, pp. 97-103. Academic Press, New York, NY.
    • (1963) The Enzyme , vol.7 , pp. 97-103
    • Wakil, S.J.1
  • 8
    • 0015919670 scopus 로고
    • L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. I. Purification and properties
    • Noyes BE & Bradshaw RA (1973) L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. I. Purification and properties. J Biol Chem 248, 3052-3059.
    • (1973) J Biol Chem , vol.248 , pp. 3052-3059
    • Noyes, B.E.1    Bradshaw, R.A.2
  • 9
    • 0015919701 scopus 로고
    • L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. II. Subunit structure
    • Noyes BE & Bradshaw RA (1973) L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. II. Subunit structure. J Biol Chem 248, 3060-3066.
    • (1973) J Biol Chem , vol.248 , pp. 3060-3066
    • Noyes, B.E.1    Bradshaw, R.A.2
  • 10
    • 0024382885 scopus 로고
    • Assay of L-3-hydroxyacyl coenzyme A dehydrogenase with substrates of different chain lengths
    • He XY, Yang SY & Schulz H (1989) Assay of L-3-hydroxyacyl coenzyme A dehydrogenase with substrates of different chain lengths. Anal Biochem 180, 105-109.
    • (1989) Anal Biochem , vol.180 , pp. 105-109
    • He, X.Y.1    Yang, S.Y.2    Schulz, H.3
  • 11
    • 0033602116 scopus 로고    scopus 로고
    • Identity of heart and liver L-3-hydroxyacyl-CoA dehydrogenase
    • He XY, Zhang G, Blecha F & Yang SY (1999) Identity of heart and liver L-3-hydroxyacyl-CoA dehydrogenase. Biochim Biophys Acta 1437, 119-123.
    • (1999) Biochim Biophys Acta , vol.1437 , pp. 119-123
    • He, X.Y.1    Zhang, G.2    Blecha, F.3    Yang, S.Y.4
  • 14
    • 0020481368 scopus 로고
    • The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria
    • El-Fakhri M & Middleton B (1982) The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria. Biochim Biophys Acta 713, 270-279.
    • (1982) Biochim Biophys Acta , vol.713 , pp. 270-279
    • El-Fakhri, M.1    Middleton, B.2
  • 15
    • 0026558042 scopus 로고
    • Human liver long-chain 3-hydoxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria
    • Carpenter K, Pollitt RJ & Middleton B (1992) Human liver long-chain 3-hydoxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria. Biochem Biophys Res Commun 183, 443-448.
    • (1992) Biochem Biophys Res Commun , vol.183 , pp. 443-448
    • Carpenter, K.1    Pollitt, R.J.2    Middleton, B.3
  • 16
    • 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 (1992) 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 267, 1034-1041.
    • (1992) J Biol Chem , vol.267 , pp. 1034-1041
    • Uchida, Y.1    Izai, K.2    Orii, T.3    Hashimoto, T.4
  • 17
    • 0027426259 scopus 로고
    • Molecular cloning of the cDNA for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes
    • Kamijo T, Aoyama T, Miyazaki J & Hashimoto T (1993) Molecular cloning of the cDNA for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. Structural and functional relationships to other mitochondrial and peroxisomal β-oxidation enzymes. J Biol Chem 268, 26452-26460.
    • (1993) J Biol Chem , vol.268 , pp. 26452-26460
    • Kamijo, T.1    Aoyama, T.2    Miyazaki, J.3    Hashimoto, T.4
  • 18
    • 0027974112 scopus 로고
    • The large subunit of the pig heart mitochondrial membrane-bound β-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme
    • Yang SY (1994) The large subunit of the pig heart mitochondrial membrane-bound β-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. Comp Biochem Physiol 109B, 557-566.
    • (1994) Comp Biochem Physiol , vol.109 B , pp. 557-566
    • Yang, S.Y.1
  • 19
    • 0032562664 scopus 로고    scopus 로고
    • A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease
    • He XY, Schulz H & Yang SY (1998) A human brain L-3-hydroxyacyl- coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease. J Biol Chem 273, 10741-10746.
    • (1998) J Biol Chem , vol.273 , pp. 10741-10746
    • He, X.Y.1    Schulz, H.2    Yang, S.Y.3
  • 20
    • 0029153738 scopus 로고
    • Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: Purification and characterization of a novel enzyme of isoleucine metabolism
    • Luo MJ, Mao LF & Schulz H (1995) Short-chain 3-hydroxy-2-methylacyl- CoA dehydrogenase from rat liver: purification and characterization of a novel enzyme of isoleucine metabolism. Arch Biochem Biophys 321, 214-220.
    • (1995) Arch Biochem Biophys , vol.321 , pp. 214-220
    • Luo, M.J.1    Mao, L.F.2    Schulz, H.3
  • 21
    • 0029880653 scopus 로고    scopus 로고
    • Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver
    • Kobayashi A, Jiang LL & Hashimoto T (1996) Two mitochondrial 3-hydroxyacyl-CoA dehydrogenases in bovine liver. J Biochem 119, 775-782.
    • (1996) J Biochem , vol.119 , pp. 775-782
    • Kobayashi, A.1    Jiang, L.L.2    Hashimoto, T.3
  • 22
    • 0013079948 scopus 로고    scopus 로고
    • An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease
    • Yan SD, Fu J, Soto C, Chen X, Zhu H, Al-Mohanna F, Colison K, Zhu A, Stern E, Saido T et al. (1997) An intracellular protein that binds amyloid-β peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389, 689-695.
    • (1997) Nature , vol.389 , pp. 689-695
    • Yan, S.D.1    Fu, J.2    Soto, C.3    Chen, X.4    Zhu, H.5    Al-Mohanna, F.6    Colison, K.7    Zhu, A.8    Stern, E.9    Saido, T.10
  • 23
    • 0033591454 scopus 로고    scopus 로고
    • Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase
    • He XY, Merz G, Yang YZ, Pullarkat R, Mehta P, Schulz H & Yang SY (1999) Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. J Biol Chem 274, 15014-15019.
    • (1999) J Biol Chem , vol.274 , pp. 15014-15019
    • He, X.Y.1    Merz, G.2    Yang, Y.Z.3    Pullarkat, R.4    Mehta, P.5    Schulz, H.6    Yang, S.Y.7
  • 24
    • 0034791854 scopus 로고    scopus 로고
    • Characterization and localization of human type 10, 17β- hydroxysteroid dehydrogenase
    • He XY, Merz G, Yang YZ, Mehta P, Schulz H & Yang SY (2001) Characterization and localization of human type 10, 17β-hydroxysteroid dehydrogenase. Eur J Biochem 268, 4899-4907.
    • (2001) Eur J Biochem , vol.268 , pp. 4899-4907
    • He, X.Y.1    Merz, G.2    Yang, Y.Z.3    Mehta, P.4    Schulz, H.5    Yang, S.Y.6
  • 25
    • 16244392645 scopus 로고    scopus 로고
    • Multiple functions of type 10, 17beta-hydroxysteroid dehydrogenase
    • Yang SY, He XY & Schulz H (2005) Multiple functions of type 10, 17beta-hydroxysteroid dehydrogenase. Trends Endocrinol Metab 16, 167-175.
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 167-175
    • Yang, S.Y.1    He, X.Y.2    Schulz, H.3
  • 26
    • 0344741467 scopus 로고    scopus 로고
    • Expended substrate screenings of human and Drosophila type 10 17β-hydroxysteroid dehydrogenase reveal multiple specificities in bile acid and steroid hormone metabolism. Characterization of multifunctional 3α/7α/7β/20β/21-hydroxysteroid dehydrogenase
    • Shafqat N, Marschall H, Filling C, Nording E, Wu XQ, Bjork L, Thyberg J, Martensson E, Salim S, Jornvall H & Oppermann U (2003) Expended substrate screenings of human and Drosophila type 10 17β-hydroxysteroid dehydrogenase reveal multiple specificities in bile acid and steroid hormone metabolism. Characterization of multifunctional 3α/7α/7β/20β/21- hydroxysteroid dehydrogenase. Biochem J 376, 49-60.
    • (2003) Biochem J , vol.376 , pp. 49-60
    • Shafqat, N.1    Marschall, H.2    Filling, C.3    Nording, E.4    Wu, X.Q.5    Bjork, L.6    Thyberg, J.7    Martensson, E.8    Salim, S.9    Jornvall, H.10    Oppermann, U.11
  • 27
    • 0033985061 scopus 로고    scopus 로고
    • Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short chain L-3-hydroxyacyl-CoA dehydrogenase
    • He XY, Yang YZ, Schulz H & Yang SY (2000) Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short chain L-3-hydroxyacyl-CoA dehydrogenase. Biochem J 345, 139-143.
    • (2000) Biochem J , vol.345 , pp. 139-143
    • He, X.Y.1    Yang, Y.Z.2    Schulz, H.3    Yang, S.Y.4
  • 28
    • 0034630485 scopus 로고    scopus 로고
    • Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism
    • He XY, Merz G, Yang YZ, Pullarkat R, Mehta P, Schulz H & Yang SY (2000) Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism. Biochim Biophys Acta 1484, 267-277.
    • (2000) Biochim Biophys Acta , vol.1484 , pp. 267-277
    • He, X.Y.1    Merz, G.2    Yang, Y.Z.3    Pullarkat, R.4    Mehta, P.5    Schulz, H.6    Yang, S.Y.7
  • 29
    • 0034994142 scopus 로고    scopus 로고
    • Role of type 10 17β-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease
    • Yang SY & He XY (2001) Role of type 10 17β-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease. Adv Exp Med Biol 487, 101-110.
    • (2001) Adv Exp Med Biol , vol.487 , pp. 101-110
    • Yang, S.Y.1    He, X.Y.2
  • 33
    • 0016420267 scopus 로고
    • L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. EC 1.1.1.35 L-3-hydroxyacyl-CoA: NAD oxidoreductase
    • Bradshaw RA & Noyes BE (1975) L-3-Hydroxyacyl coenzyme A dehydrogenase from pig heart muscle. EC 1.1.1.35 L-3-hydroxyacyl-CoA: NAD oxidoreductase. Methods Enzymol 35, 122-128.
    • (1975) Methods Enzymol , vol.35 , pp. 122-128
    • Bradshaw, R.A.1    Noyes, B.E.2
  • 34
    • 0023516725 scopus 로고
    • Structure of L-3-hydroxyacyl-CoA dehydrogenase. Preliminary chain tracing at 2.8 Å resolution
    • Birktoft JJ, Holden HM, Hamlin R, Xuong NC & Banaszak LJ (1987) Structure of L-3-hydroxyacyl-CoA dehydrogenase. Preliminary chain tracing at 2.8 Å resolution. Proc Natl Acad Sci USA 84, 8262-8266.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8262-8266
    • Birktoft, J.J.1    Holden, H.M.2    Hamlin, R.3    Xuong, N.C.4    Banaszak, L.J.5
  • 35
    • 0019334636 scopus 로고
    • Amino acid sequence of L-3-hydroxyacyl-CoA dehydrogenase from pig heart muscle
    • Bitar KG, Perez-Aranda A & Bradshaw RA (1980) Amino acid sequence of L-3-hydroxyacyl-CoA dehydrogenase from pig heart muscle. FEBS Lett 116, 196-198.
    • (1980) FEBS Lett , vol.116 , pp. 196-198
    • Bitar, K.G.1    Perez-Aranda, A.2    Bradshaw, R.A.3
  • 36
    • 0033522493 scopus 로고    scopus 로고
    • Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insight into catalytic mechanism
    • Barycki JJ, O'Brien LK, Bratt JM, Zhang R, Sanishivili R, Strauss AW & Banaszak LJ (1999) Biochemical characterization and crystal structure determination of human heart short chain L-3-hydroxyacyl-CoA dehydrogenase provide insight into catalytic mechanism. Biochemistry 38, 5786-5798.
    • (1999) Biochemistry , vol.38 , pp. 5786-5798
    • Barycki, J.J.1    O'Brien, L.K.2    Bratt, J.M.3    Zhang, R.4    Sanishivili, R.5    Strauss, A.W.6    Banaszak, L.J.7
  • 37
    • 0023664837 scopus 로고
    • Kinetics of coupled enzyme reactions
    • Yang SY & Schulz H (1987) Kinetics of coupled enzyme reactions. Biochemistry 26, 5579-5584.
    • (1987) Biochemistry , vol.26 , pp. 5579-5584
    • Yang, S.Y.1    Schulz, H.2
  • 38
    • 0019048796 scopus 로고
    • Purification and properties of mitochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver
    • Osumi T & Hashimoto T (1980) Purification and properties of mitochondrial and peroxisomal 3-hydroxyacyl-CoA dehydrogenase from rat liver. Arch Biochem Biophys 203, 372-383.
    • (1980) Arch Biochem Biophys , vol.203 , pp. 372-383
    • Osumi, T.1    Hashimoto, T.2
  • 42
    • 0029944132 scopus 로고    scopus 로고
    • A new inhibitor of mitochondrial fatty acid oxidation
    • Hashimoto T, Shindo Y, Souri M & Baldwin GS (1996) A new inhibitor of mitochondrial fatty acid oxidation. J Biochem 119, 1196-1201.
    • (1996) J Biochem , vol.119 , pp. 1196-1201
    • Hashimoto, T.1    Shindo, Y.2    Souri, M.3    Baldwin, G.S.4
  • 43
    • 0034282901 scopus 로고    scopus 로고
    • Sequestration of the active site by interdomain shifting: Crystalographic and spectroscopic evidence for distinct conformation of L-3-hydroxyacyl-CoA dehydrogenase
    • Barycki JJ, O'Brien LK, Strauss AW & Banaszak LJ (2000) Sequestration of the active site by interdomain shifting: crystalographic and spectroscopic evidence for distinct conformation of L-3-hydroxyacyl-CoA dehydrogenase. J Biol Chem 275, 27186-27196.
    • (2000) J Biol Chem , vol.275 , pp. 27186-27196
    • Barycki, J.J.1    O'Brien, L.K.2    Strauss, A.W.3    Banaszak, L.J.4
  • 44
    • 0032550727 scopus 로고    scopus 로고
    • Molecular cloning, expression in Escherichia coli, and characterization of a novel L-3-hydroxyacyl coenzyme A dehydrogenase from pig liver
    • He XY & Yang SY (1998) Molecular cloning, expression in Escherichia coli, and characterization of a novel L-3-hydroxyacyl coenzyme A dehydrogenase from pig liver. Biochim Biophys Acta 1392, 119-126.
    • (1998) Biochim Biophys Acta , vol.1392 , pp. 119-126
    • He, X.Y.1    Yang, S.Y.2
  • 45
    • 0030055316 scopus 로고    scopus 로고
    • Histidine-450 is the catalytic residue of L-3-hydroxyacyl-coenzyme A dehydrogenase associated with the large α-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli
    • He XY & Yang SY (1996) Histidine-450 is the catalytic residue of L-3-hydroxyacyl-coenzyme A dehydrogenase associated with the large α-subunit of the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry 35, 9625-9630.
    • (1996) Biochemistry , vol.35 , pp. 9625-9630
    • He, X.Y.1    Yang, S.Y.2
  • 46
    • 0031012194 scopus 로고    scopus 로고
    • Importance of the γ-carboxyl group of glutamate-462 of the large α-subunit for the catalytic function and the stability of the multienzyme complex of fatty acid oxidation from Escherichia coli
    • He XY, Deng H & Yang SY (1997) Importance of the γ-carboxyl group of glutamate-462 of the large α-subunit for the catalytic function and the stability of the multienzyme complex of fatty acid oxidation from Escherichia coli. Biochemistry 36, 261-268.
    • (1997) Biochemistry , vol.36 , pp. 261-268
    • He, X.Y.1    Deng, H.2    Yang, S.Y.3
  • 47
    • 0035965209 scopus 로고    scopus 로고
    • Glutamate 170 of human L-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme
    • Barycki JJ, O'Brien LK, Strauss AW & Banaszak LJ (2001) Glutamate 170 of human L-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme. J Biol Chem 276, 36718-36726.
    • (2001) J Biol Chem , vol.276 , pp. 36718-36726
    • Barycki, J.J.1    O'Brien, L.K.2    Strauss, A.W.3    Banaszak, L.J.4
  • 48
    • 0028276957 scopus 로고
    • Primary structure of the large subunit of trifunctional β-oxidation complex from pig heart mitochondria
    • Yang SY, He XY, Style J, Luo MJ, Schulz H & Elzinga M (1994) Primary structure of the large subunit of trifunctional β-oxidation complex from pig heart mitochondria. Biochem Biophys Res Commun 198, 431-437.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 431-437
    • Yang, S.Y.1    He, X.Y.2    Style, J.3    Luo, M.J.4    Schulz, H.5    Elzinga, M.6
  • 50
    • 0028102553 scopus 로고
    • Domains of the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation. Demonstration of epimerase and isomerase activities on peptide lacking hydratase activity
    • Preisig-Muller R, Guhnemann-Schafer K & Kindl H (1994) Domains of the tetrafunctional protein acting in glyoxysomal fatty acid β-oxidation. Demonstration of epimerase and isomerase activities on peptide lacking hydratase activity. J Biol Chem 269, 20475-20481.
    • (1994) J Biol Chem , vol.269 , pp. 20475-20481
    • Preisig-Muller, R.1    Guhnemann-Schafer, K.2    Kindl, H.3
  • 51
    • 0025883684 scopus 로고
    • Nucleotide sequence of the promoter and fadB gene of the fadB A operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli
    • Yang XYH, Schulz H, Elzinga M & Yang SY (1991) Nucleotide sequence of the promoter and fadB gene of the fadB A operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli. Biochemistry 30, 6788-6795.
    • (1991) Biochemistry , vol.30 , pp. 6788-6795
    • Yang, X.Y.H.1    Schulz, H.2    Elzinga, M.3    Yang, S.Y.4
  • 52
    • 0344199888 scopus 로고    scopus 로고
    • Cloning of an L-3-hydroxyacyl-CoA dehydrogenase that interacts with the GLUT4 C-terminus
    • Shi Y, Samuel SJ, Lee W, Yu C, Zhang W, Lachaal M & Lung CY (1999) Cloning of an L-3-hydroxyacyl-CoA dehydrogenase that interacts with the GLUT4 C-terminus. Arch Biochem Biophys 363, 323-332.
    • (1999) Arch Biochem Biophys , vol.363 , pp. 323-332
    • Shi, Y.1    Samuel, S.J.2    Lee, W.3    Yu, C.4    Zhang, W.5    Lachaal, M.6    Lung, C.Y.7
  • 53
    • 0023796703 scopus 로고
    • λ-crystallin, a major rabbit lens protein, is related to hydroxyacyl coenzyme A dehydrogenase
    • Mudlers JWM, Hendriks W, Blankesteijn M, Bloemendal H & de Jong WW (1988) λ-Crystallin, a major rabbit lens protein, is related to hydroxyacyl coenzyme A dehydrogenase. J Biol Chem 263, 15462-15466.
    • (1988) J Biol Chem , vol.263 , pp. 15462-15466
    • Mudlers, J.W.M.1    Hendriks, W.2    Blankesteijn, M.3    Bloemendal, H.4    De Jong, W.W.5
  • 54
    • 0026076169 scopus 로고
    • Short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency in muscle: A new cause for recurrent myoglobinuria and encephalopathy
    • Tien I, De Vivo DC, Hale DE, Clarke JTR, Zinman H, Laxer R, Shore A & DiMauro S (1991) Short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency in muscle: a new cause for recurrent myoglobinuria and encephalopathy. Ann Neurol 30, 415-419.
    • (1991) Ann Neurol , vol.30 , pp. 415-419
    • Tien, I.1    De Vivo, D.C.2    Hale, D.E.3    Clarke, J.T.R.4    Zinman, H.5    Laxer, R.6    Shore, A.7    DiMauro, S.8
  • 55
    • 0030041154 scopus 로고    scopus 로고
    • Mitochondrial short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: A new defect of fatty acid oxidation
    • Bennett MJ, Weinberger MJ, Kobori JA, Rinaldo P & Burlina AB (1996) Mitochondrial short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: a new defect of fatty acid oxidation. Pediatr Res 39, 185-188.
    • (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
  • 56
    • 0033039270 scopus 로고    scopus 로고
    • Fatal hepatic short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: Clinical, biochemical, and pathological studies on three subjects with this recently identified disorder of mitochondrial β-oxidation
    • Bennett MJ, Spotswood SD, Ross KF, Comfort S, Koonce R, Boriack RL, IJlst L & Wanders RJA (1999) Fatal hepatic short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase deficiency: clinical, biochemical, and pathological studies on three subjects with this recently identified disorder of mitochondrial β-oxidation. Pediatr Dev Pathol 2, 337-345.
    • (1999) Pediatr Dev Pathol , vol.2 , pp. 337-345
    • Bennett, M.J.1    Spotswood, S.D.2    Ross, K.F.3    Comfort, S.4    Koonce, R.5    Boriack, R.L.6    Ijlst, L.7    Wanders, R.J.A.8
  • 58
    • 0027244111 scopus 로고
    • Purification and characterization of the trifunctional β-oxidation complex from pig heart mitochondria
    • Luo MJ, He XY, Sprecher H & Schulz H (1993) Purification and characterization of the trifunctional β-oxidation complex from pig heart mitochondria. Arch Biochem Biophys 304, 266-271.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 266-271
    • Luo, M.J.1    He, X.Y.2    Sprecher, H.3    Schulz, H.4
  • 60
    • 0032821582 scopus 로고    scopus 로고
    • Mitochondrial fatty acid oxidation disorders and cyclic vomiting syndrome
    • Rinaldo P (1999) Mitochondrial fatty acid oxidation disorders and cyclic vomiting syndrome. Dig Dis Sci 44, S97-S102.
    • (1999) Dig Dis Sci , vol.44
    • Rinaldo, P.1
  • 61
    • 0036534129 scopus 로고    scopus 로고
    • Alternative splicing: Multiple control mechanisms and involvement in human disease
    • Caceres JF & Kornblihtt AR (2002) Alternative splicing: multiple control mechanisms and involvement in human disease. Trends Genet 18, 186-193.
    • (2002) Trends Genet , vol.18 , pp. 186-193
    • Caceres, J.F.1    Kornblihtt, A.R.2
  • 62
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black DL (2003) Mechanisms of alternative pre-messenger RNA splicing. Annu Rev Biochem 72, 291-336.
    • (2003) Annu Rev Biochem , vol.72 , pp. 291-336
    • Black, D.L.1
  • 64
    • 0018287979 scopus 로고
    • Occurrence of two 3-hydroxyacyl-CoA dehydrogenases in rat liver
    • Osumi T & Hashimoto T (1979) Occurrence of two 3-hydroxyacyl-CoA dehydrogenases in rat liver. Biochim Biophys Acta 574, 258-267.
    • (1979) Biochim Biophys Acta , vol.574 , pp. 258-267
    • Osumi, T.1    Hashimoto, T.2
  • 65
    • 16244423717 scopus 로고    scopus 로고
    • Intracellular oxidation of allopregnanolone by human brain type 10 17beta-hydroxysteroid dehydrogenase
    • He XY, Wegiel J & Yang SY (2005) Intracellular oxidation of allopregnanolone by human brain type 10 17beta-hydroxysteroid dehydrogenase. Brain Res 1040, 29-35.
    • (2005) Brain Res , vol.1040 , pp. 29-35
    • He, X.Y.1    Wegiel, J.2    Yang, S.Y.3
  • 66
    • 0033667891 scopus 로고    scopus 로고
    • Progressive infantile neurodegeneration caused by 2-methyl-3- hydroxybutyryl-CoA dehydrogenase deficiency: A novel inborn error of branched-chain fatty acid and isoleucine metabolism
    • Zschocke J, Rutter JPN, Brand J, Lindner M, Hoffmann GF, Wanders RJA & Mayatepek E (2000) Progressive infantile neurodegeneration caused by 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency: a novel inborn error of branched-chain fatty acid and isoleucine metabolism. Pediatric Res 48, 852-855.
    • (2000) Pediatric Res , vol.48 , pp. 852-855
    • Zschocke, J.1    Rutter, J.P.N.2    Brand, J.3    Lindner, M.4    Hoffmann, G.F.5    Wanders, R.J.A.6    Mayatepek, E.7
  • 69
    • 10944225224 scopus 로고    scopus 로고
    • Type 10 17beta-hydroxysteroid dehydrogenase catalyzing the oxidation of steroid modulators of gamma-aminobutyric acid type A receptors
    • He XY, Wegiel J, Yang YZ, Pullarkat R, Schulz H & Yang SY (2005) Type 10 17beta-hydroxysteroid dehydrogenase catalyzing the oxidation of steroid modulators of gamma-aminobutyric acid type A receptors. Mol Cell Endocrinol 229, 111-117.
    • (2005) Mol Cell Endocrinol , vol.229 , pp. 111-117
    • He, X.Y.1    Wegiel, J.2    Yang, Y.Z.3    Pullarkat, R.4    Schulz, H.5    Yang, S.Y.6
  • 70
    • 0033046060 scopus 로고    scopus 로고
    • Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): Regulation of an SDR enzyme activity with implication for apoptosis in Alzheimer's disease
    • Oppermann UCT, Salim S, Tjernberg LO, Terenius L & Jornvall H (1999) Binding of amyloid β-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implication for apoptosis in Alzheimer's disease. FEBS Lett 451, 238-242.
    • (1999) FEBS Lett , vol.451 , pp. 238-242
    • Oppermann, U.C.T.1    Salim, S.2    Tjernberg, L.O.3    Terenius, L.4    Jornvall, H.5
  • 72
    • 0035854582 scopus 로고    scopus 로고
    • Deposition of Alzheimer's vascular amyloid-β is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB)
    • Frackowiak J, Mazur-Kolecka B, Kaczmarski W & Dickson D (2001) Deposition of Alzheimer's vascular amyloid-β is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB). Brain Res 907, 44-53.
    • (2001) Brain Res , vol.907 , pp. 44-53
    • Frackowiak, J.1    Mazur-Kolecka, B.2    Kaczmarski, W.3    Dickson, D.4
  • 74
    • 0024328787 scopus 로고
    • Molecular cloning and primary structure of human glial fibrillary acidic protein
    • Reeves SA, Helman LJ, Allison A & Israel MA (1989) Molecular cloning and primary structure of human glial fibrillary acidic protein. Proc Natl Acad Sci USA 86, 5178-5182.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5178-5182
    • Reeves, S.A.1    Helman, L.J.2    Allison, A.3    Israel, M.A.4
  • 76
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • Dauer W & Przedborski S (2003) Parkinson's disease: mechanisms and models. Neuron 39, 889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 77
    • 0020680904 scopus 로고
    • Chronic parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston JW, Ballard P & Irwin I (1983) Chronic parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219, 979-980.
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Irwin, I.3
  • 78
    • 10244222286 scopus 로고    scopus 로고
    • MPTP as a mitochondrial neurotoxic model of Parkinson's disease
    • Przedborski S, Tieu K, Perier C & Vila M (2004) MPTP as a mitochondrial neurotoxic model of Parkinson's disease. J Bioenerg Biomembr 36, 375-379.
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 375-379
    • Przedborski, S.1    Tieu, K.2    Perier, C.3    Vila, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.