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Volumn 167, Issue 1-2, 1997, Pages 1-29

Biochemistry of peroxisomes in health and disease

Author keywords

Bile acids and plasmalogen; Fatty acid oxidation; Fatty acid oxidation; H2O2 metabolism; Peroxisomal diseases; Peroxisomes

Indexed keywords

BILE ACID; CHOLESTEROL; DICARBOXYLIC ACID; DOLICHOL; FATTY ACID; GLUTARIC ACID; GLYOXYLIC ACID; LONG CHAIN FATTY ACID; PIPECOLIC ACID; PLASMALOGEN; POLYAMINE; PROSTAGLANDIN; PURINE DERIVATIVE; REACTIVE OXYGEN METABOLITE; UNSATURATED FATTY ACID;

EID: 0031055817     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006883229684     Document Type: Review
Times cited : (139)

References (308)
  • 2
    • 77049276032 scopus 로고
    • Microbodies' and the problem of mitochondrial regeneration in liver cells
    • Rouiller C, Bernard W: 'Microbodies' and the problem of mitochondrial regeneration in liver cells. J Biophys Biochem Cytol 2: 355-359, 1956
    • (1956) J Biophys Biochem Cytol , vol.2 , pp. 355-359
    • Rouiller, C.1    Bernard, W.2
  • 3
    • 0014216690 scopus 로고
    • Association of the glyoxylate cycle enzymes in a novel subcellular particle from castor bean endosperm
    • Breidenbach RW, Beevers H: Association of the glyoxylate cycle enzymes in a novel subcellular particle from castor bean endosperm. Biochem Biophys Res Commun 27: 462-469, 1967
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 462-469
    • Breidenbach, R.W.1    Beevers, H.2
  • 4
    • 0013897667 scopus 로고
    • Peroxisomes (microbodies and related particles)
    • de Duve C, Baudhuin P: Peroxisomes (microbodies and related particles). Physiol Rev 46: 323-357, 1966
    • (1966) Physiol Rev , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 5
    • 0020759527 scopus 로고
    • Microbodies in the living cell
    • de Duve C: Microbodies in the living cell. Sci Am 248: 74-84, 1983
    • (1983) Sci Am , vol.248 , pp. 74-84
    • De Duve, C.1
  • 7
    • 0027176127 scopus 로고
    • Metabolic pathways in Mammalian Peroxisomes
    • Mannaerts GP, van Veldhoven PP: Metabolic pathways in Mammalian Peroxisomes. Biochimie 75: 147-158, 1993
    • (1993) Biochimie , vol.75 , pp. 147-158
    • Mannaerts, G.P.1    Van Veldhoven, P.P.2
  • 8
    • 8044251721 scopus 로고
    • Peroxisomes in biology and medicine
    • SK Malhotra (ed). Jai Press Inc, Greenwich, Conn
    • Singh I: Peroxisomes in biology and medicine. In: SK Malhotra (ed). Advances in Structural Biology. Jai Press Inc, Greenwich, Conn: 1994, 137-156
    • (1994) Advances in Structural Biology , pp. 137-156
    • Singh, I.1
  • 10
    • 0027200034 scopus 로고
    • Peroxisomal Diseases
    • Moser HW: Peroxisomal Diseases. Adv Hum Gen 21: 1-106, 443-451, 1993
    • (1993) Adv Hum Gen , vol.21 , pp. 1-106
    • Moser, H.W.1
  • 11
  • 13
    • 0021880518 scopus 로고
    • Serial section analysis of mouse hepatic peroxisomes
    • Gorgas K: Serial section analysis of mouse hepatic peroxisomes. Anat Embryol 172: 21-32, 1985
    • (1985) Anat Embryol , vol.172 , pp. 21-32
    • Gorgas, K.1
  • 14
    • 0001574989 scopus 로고
    • The endoplasmic reticulum in the golgi zone and its relations to microbodies, Golgi apparatus and autophagic vacuoles in rat liver cells
    • Novikoff AB, Shin WY: The endoplasmic reticulum in the golgi zone and its relations to microbodies, Golgi apparatus and autophagic vacuoles in rat liver cells. J Microse 3: 187-206, 1964
    • (1964) J Microse , vol.3 , pp. 187-206
    • Novikoff, A.B.1    Shin, W.Y.2
  • 15
    • 0024550296 scopus 로고
    • Heterogeneity of catalase staining in human hepatocellular peroxisomes
    • Roels F, Cornelis A: Heterogeneity of catalase staining in human hepatocellular peroxisomes. Histochem and Cytochem 37: 331-337, 1989
    • (1989) Histochem and Cytochem , vol.37 , pp. 331-337
    • Roels, F.1    Cornelis, A.2
  • 16
    • 0002420080 scopus 로고
    • Microbodies and related particles
    • Academic Press, New York
    • Hruban Z, Rechcigl M: Microbodies and related particles. Int Rev Cytol, Academic Press, New York: 296, 1969
    • (1969) Int Rev Cytol , pp. 296
    • Hruban, Z.1    Rechcigl, M.2
  • 17
    • 0015383176 scopus 로고
    • Microbodies: Constituent organelles of animal cells
    • Hruban Z, Vigil EL, Slesers A, Hopkins E: Microbodies: Constituent organelles of animal cells. Lab Invest 27: 184-191, 1972
    • (1972) Lab Invest , vol.27 , pp. 184-191
    • Hruban, Z.1    Vigil, E.L.2    Slesers, A.3    Hopkins, E.4
  • 18
    • 0017334065 scopus 로고
    • Distribution of organelles and membranes between hepatocytes and nonhepatocytes in the rat liver paranchyma. A stereological study
    • Blouin A, Bolender RP, Weibel R: Distribution of organelles and membranes between hepatocytes and nonhepatocytes in the rat liver paranchyma. A stereological study. J Cell Biol 72: 441-455, 1977
    • (1977) J Cell Biol , vol.72 , pp. 441-455
    • Blouin, A.1    Bolender, R.P.2    Weibel, R.3
  • 19
    • 0001661183 scopus 로고
    • Peroxisomes in nervous tissue
    • Holzmann E: Peroxisomes in nervous tissue. Ann NY Acad Sci 386: 523-535, 1982
    • (1982) Ann NY Acad Sci , vol.386 , pp. 523-535
    • Holzmann, E.1
  • 20
    • 0023931481 scopus 로고
    • Tissue specificity and species differences in the distribution of urate oxidase in peroxisomes
    • Usuda N, Reddy KM, Hashimoto T, Rao SM, Reddy JK: Tissue specificity and species differences in the distribution of urate oxidase in peroxisomes. Lab Invest 58: 100-111, 1988
    • (1988) Lab Invest , vol.58 , pp. 100-111
    • Usuda, N.1    Reddy, K.M.2    Hashimoto, T.3    Rao, S.M.4    Reddy, J.K.5
  • 21
    • 0023477159 scopus 로고
    • Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study
    • Angermuller S, Bruder G, Volkl A, Wesch H, Fahimi HD: Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study. Eur J Cell Biol 45: 137-144, 1987
    • (1987) Eur J Cell Biol , vol.45 , pp. 137-144
    • Angermuller, S.1    Bruder, G.2    Volkl, A.3    Wesch, H.4    Fahimi, H.D.5
  • 22
    • 0025897213 scopus 로고
    • Purification of marginal plates from bovine renal peroxisomes: Identification with L-alphahydroxyacid oxidase B
    • Zaar K, Volkl A, Fahimi HD: Purification of marginal plates from bovine renal peroxisomes: Identification with L-alphahydroxyacid oxidase B. J Cell Biol 113: 113-121, 1991
    • (1991) J Cell Biol , vol.113 , pp. 113-121
    • Zaar, K.1    Volkl, A.2    Fahimi, H.D.3
  • 23
    • 0001846763 scopus 로고
    • Serial section analysis of proximal shape and membrane relationship in the mouse prepucial gland
    • HD Fahimi, H Sies (eds). Springer-Verlag, Berlin, Heidelberg
    • Gorgas K: Serial section analysis of proximal shape and membrane relationship in the mouse prepucial gland. In: HD Fahimi, H Sies (eds). Peroxisomes in Biology and Medicine. Springer-Verlag, Berlin, Heidelberg: 1987, 3-17
    • (1987) Peroxisomes in Biology and Medicine , pp. 3-17
    • Gorgas, K.1
  • 24
    • 0023571885 scopus 로고
    • Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: Evidence of interconnections between heterogeneous segments
    • Yamamoto L, Fahimi HD: Three-dimensional reconstruction of a peroxisomal reticulum in regenerating rat liver: Evidence of interconnections between heterogeneous segments. J Cell Biol 105: 713-722, 1987
    • (1987) J Cell Biol , vol.105 , pp. 713-722
    • Yamamoto, L.1    Fahimi, H.D.2
  • 25
    • 0023664229 scopus 로고
    • Permeability of the peroxisomal membrane to cofactors of beta-oxidation. Evidence for the presence of a pore-forming protein
    • Van Veldhoven PP, Just WW, Mannaerts GP: Permeability of the peroxisomal membrane to cofactors of beta-oxidation. Evidence for the presence of a pore-forming protein. J Biol Chem 262: 4310-4318, 1987
    • (1987) J Biol Chem , vol.262 , pp. 4310-4318
    • Van Veldhoven, P.P.1    Just, W.W.2    Mannaerts, G.P.3
  • 27
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: Comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki Y, Fowler S, Shio H, Hubbard AL, Lazarow PB: Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes. J Cell Biol 93: 103-110, 1982
    • (1982) J Cell Biol , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 28
    • 0024989719 scopus 로고
    • Biogenesis of peroxisomes: Sequential biosynthesis of the membrane and matrix proteins in the course of hepatic regeneration
    • Luers G, Beier K, Hashimoto T, Fahimi HD, Volkl A: Biogenesis of peroxisomes: Sequential biosynthesis of the membrane and matrix proteins in the course of hepatic regeneration. Eur J Cell Biol 52: 175-184, 1990
    • (1990) Eur J Cell Biol , vol.52 , pp. 175-184
    • Luers, G.1    Beier, K.2    Hashimoto, T.3    Fahimi, H.D.4    Volkl, A.5
  • 29
    • 0024383785 scopus 로고
    • Biogenesis of peroxisomes: Immunocytochemical investigation of peroxisomal membrane proteins in proliferating rat liver peroxisomes and in catalase-negative membrane loops
    • Baumgart E, Volkl A, Hashimoto T, Fahimi HD: Biogenesis of peroxisomes: Immunocytochemical investigation of peroxisomal membrane proteins in proliferating rat liver peroxisomes and in catalase-negative membrane loops. J Cell Biol 108: 2221-2231, 1989
    • (1989) J Cell Biol , vol.108 , pp. 2221-2231
    • Baumgart, E.1    Volkl, A.2    Hashimoto, T.3    Fahimi, H.D.4
  • 30
    • 0027173703 scopus 로고
    • Ultrastructural aspects of the biogenesis of peroxisomes in rat liver
    • Fahimi HD, Baumgart E, Volkl A: Ultrastructural aspects of the biogenesis of peroxisomes in rat liver. Biochimie 75: 201-208, 1993
    • (1993) Biochimie , vol.75 , pp. 201-208
    • Fahimi, H.D.1    Baumgart, E.2    Volkl, A.3
  • 31
    • 0026511317 scopus 로고
    • Peroxisomal protein import. in vivo evidence for a novel translocation component compartment
    • Heinemann P, Just WW: Peroxisomal protein import. In vivo evidence for a novel translocation component compartment. FEBS Letts 300: 179-182, 1992
    • (1992) FEBS Letts , vol.300 , pp. 179-182
    • Heinemann, P.1    Just, W.W.2
  • 32
    • 0028939995 scopus 로고
    • Novel peroxisomal populations in subcellular fractions from rat liver
    • Wilcke M, Hultenby K, Alexson SEH: Novel peroxisomal populations in subcellular fractions from rat liver. J Biol Chem 270: 6949-6958, 1995
    • (1995) J Biol Chem , vol.270 , pp. 6949-6958
    • Wilcke, M.1    Hultenby, K.2    Alexson, S.E.H.3
  • 33
    • 0028956579 scopus 로고
    • Effect of ischemia-reperfusion injury on the morphology of peroxisomes
    • Singh AK, Gulati S: Effect of ischemia-reperfusion injury on the morphology of peroxisomes. Mol Cell Biochem 144: 19-26, 1995
    • (1995) Mol Cell Biochem , vol.144 , pp. 19-26
    • Singh, A.K.1    Gulati, S.2
  • 34
    • 0021962086 scopus 로고
    • Synthesis of 3-ketoacyl-CoA thiolase of rat liver peroxisomes on free polyribosomes as a larger precursor
    • Fujiki Y, Rachubinski RA, Martensen RM, Lazarow PB: Synthesis of 3-ketoacyl-CoA thiolase of rat liver peroxisomes on free polyribosomes as a larger precursor. Biochem J 226: 697-704, 1985
    • (1985) Biochem J , vol.226 , pp. 697-704
    • Fujiki, Y.1    Rachubinski, R.A.2    Martensen, R.M.3    Lazarow, P.B.4
  • 35
    • 0025425482 scopus 로고
    • Topogenesis of peroxisomal proteins
    • Osumi T, Fujiki Y: Topogenesis of peroxisomal proteins. Bio Essays 12: 217-222, 1990
    • (1990) Bio Essays , vol.12 , pp. 217-222
    • Osumi, T.1    Fujiki, Y.2
  • 36
    • 0026767701 scopus 로고
    • Import of proteins into peroxisomes and other microbodies
    • de Hoop MJ, Ab G: Import of proteins into peroxisomes and other microbodies. Biochem J 286: 657-669, 1992
    • (1992) Biochem J , vol.286 , pp. 657-669
    • De Hoop, M.J.1    Ab, G.2
  • 37
    • 0027333416 scopus 로고
    • Protein import into peroxisomes and biogenesis of the organelle
    • Subramani S: Protein import into peroxisomes and biogenesis of the organelle. Annu Rev Cell Biol 9: 445-478, 1993
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 445-478
    • Subramani, S.1
  • 38
    • 0028149887 scopus 로고
    • Peroxisomal biogenesis: Multiple pathway for protein imports
    • Perdue PE, Lazarow PB: Peroxisomal biogenesis: Multiple pathway for protein imports. J Biol Chem 269: 30065-30068, 1994
    • (1994) J Biol Chem , vol.269 , pp. 30065-30068
    • Perdue, P.E.1    Lazarow, P.B.2
  • 39
    • 0023548002 scopus 로고
    • Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase
    • Gould SJ, Keller GA, Subramani S: Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase. J Cell Biol 105: 2923-2931, 1987
    • (1987) J Cell Biol , vol.105 , pp. 2923-2931
    • Gould, S.J.1    Keller, G.A.2    Subramani, S.3
  • 40
    • 0024528893 scopus 로고
    • Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus
    • Miyaznwa S, Osumi T, Hashimoto T, Ohno K, Miura S, Fujiki Y: Peroxisome targeting signal of rat liver acyl-coenzyme A oxidase resides at the carboxy terminus. Mol Cell Biol 9: 83-91, 1989
    • (1989) Mol Cell Biol , vol.9 , pp. 83-91
    • Miyaznwa, S.1    Osumi, T.2    Hashimoto, T.3    Ohno, K.4    Miura, S.5    Fujiki, Y.6
  • 41
    • 0029047855 scopus 로고
    • Identification of three peroxisomal import defects in patients with peroxisome biogenesis disorders
    • Slawecki ML, Dodt G, Steinberg S, Moser AB, Moser HW, Gould SJ: Identification of three peroxisomal import defects in patients with peroxisome biogenesis disorders. J Cell Sci 108: 1817-1829, 1995
    • (1995) J Cell Sci , vol.108 , pp. 1817-1829
    • Slawecki, M.L.1    Dodt, G.2    Steinberg, S.3    Moser, A.B.4    Moser, H.W.5    Gould, S.J.6
  • 42
    • 0025941962 scopus 로고
    • A novel cleavable targeting signal at the amino terminus of the rat 3-ketoacyl-CoA thiolase
    • Swinkles BW, Gould SJ, Bodnar AJ, Rachubiuski RA, Subramani S: A novel cleavable targeting signal at the amino terminus of the rat 3-ketoacyl-CoA thiolase. Embo J 10: 3255-3262, 1991
    • (1991) Embo J , vol.10 , pp. 3255-3262
    • Swinkles, B.W.1    Gould, S.J.2    Bodnar, A.J.3    Rachubiuski, R.A.4    Subramani, S.5
  • 44
    • 0026643496 scopus 로고
    • Carboxyl-terminal consensus Ser-Lys-Leu-related tripeptide of peroxisomal proteins functions in vitro as a minimal peroxisome-targeting signal
    • Miura S, Kasuya-Arai I, Mori H, Miyazawa S, Osumi T, Hashimoto T, Fujiki Y: Carboxyl-terminal consensus Ser-Lys-Leu-related tripeptide of peroxisomal proteins functions in vitro as a minimal peroxisome-targeting signal. J Biol Chem 267: 14405-14411, 1992
    • (1992) J Biol Chem , vol.267 , pp. 14405-14411
    • Miura, S.1    Kasuya-Arai, I.2    Mori, H.3    Miyazawa, S.4    Osumi, T.5    Hashimoto, T.6    Fujiki, Y.7
  • 45
    • 0023541627 scopus 로고
    • Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential
    • Imanaka T, Small G, Lazarow P: Translocation of acyl-CoA oxidase into peroxisomes requires ATP hydrolysis but not a membrane potential. J Cell Biol 105: 2915-1922, 1987
    • (1987) J Cell Biol , vol.105 , pp. 2915-11922
    • Imanaka, T.1    Small, G.2    Lazarow, P.3
  • 46
    • 0027178239 scopus 로고
    • Import of firefly luciferase into mammalian peroxisomes in vivo requires nucleotide triphosphate
    • Soto U, Pepperkok R, Ansorge W, Just W: Import of firefly luciferase into mammalian peroxisomes in vivo requires nucleotide triphosphate. Expt Cell Res 205: 66-75, 1993
    • (1993) Expt Cell Res , vol.205 , pp. 66-75
    • Soto, U.1    Pepperkok, R.2    Ansorge, W.3    Just, W.4
  • 47
    • 0027448017 scopus 로고
    • Cytosol-dependent peroxisomal protein import in permealized cell system
    • Wendland M, Subramani S: Cytosol-dependent peroxisomal protein import in permealized cell system. J Cell Biol 120: 675-685, 1993
    • (1993) J Cell Biol , vol.120 , pp. 675-685
    • Wendland, M.1    Subramani, S.2
  • 49
    • 0028278166 scopus 로고
    • Mutagenesis of the amino targeting signal of saccharomyces cerevisae 3-ketoacyl-CoA thiolase reveals conserved amino acid required for import into peroxisomes in vivo
    • Glover JR, Andrews DW, Subramani S, Rachubinski R: Mutagenesis of the amino targeting signal of saccharomyces cerevisae 3-ketoacyl-CoA thiolase reveals conserved amino acid required for import into peroxisomes in vivo. J Biol Chem 269: 7558-7563, 1994
    • (1994) J Biol Chem , vol.269 , pp. 7558-7563
    • Glover, J.R.1    Andrews, D.W.2    Subramani, S.3    Rachubinski, R.4
  • 50
    • 0025737231 scopus 로고
    • Rhizomelic chondrodysplasia punctata: Biochemical studies of peroxisomes isolated from cultured skin fibroblasts
    • Singh I, Lazo O, Contreras M, Stanley W, Hashimoto T: Rhizomelic chondrodysplasia punctata: biochemical studies of peroxisomes isolated from cultured skin fibroblasts. Arch Biochem Biophys 286: 277-283, 1991
    • (1991) Arch Biochem Biophys , vol.286 , pp. 277-283
    • Singh, I.1    Lazo, O.2    Contreras, M.3    Stanley, W.4    Hashimoto, T.5
  • 53
    • 0029903045 scopus 로고    scopus 로고
    • The import receptor of the peroxisomal targeting signal-2 (PTS-2) in saccharomyces cerevisiae is encoded by the PAS 7 gene
    • Rehling P, Marzioch M, Niesen F, Wittke E, Veenhuis M, Kunau W-H: The import receptor of the peroxisomal targeting signal-2 (PTS-2) in saccharomyces cerevisiae is encoded by the PAS 7 gene. Embo J 15: 2901-2913, 1996
    • (1996) Embo J , vol.15 , pp. 2901-2913
    • Rehling, P.1    Marzioch, M.2    Niesen, F.3    Wittke, E.4    Veenhuis, M.5    Kunau, W.-H.6
  • 55
    • 0028817372 scopus 로고
    • Mutation in the PTS-1 receptor gene, PXR1, define complimentation group 2 of the peroxisome biogenesis disorders
    • Dodt G, Braverman N, Wong C, Moser A, Moser HW et al.: Mutation in the PTS-1 receptor gene, PXR1, define complimentation group 2 of the peroxisome biogenesis disorders. Nature 9: 115-125, 1995
    • (1995) Nature , vol.9 , pp. 115-125
    • Dodt, G.1    Braverman, N.2    Wong, C.3    Moser, A.4    Moser, H.W.5
  • 56
    • 0029153135 scopus 로고
    • Phenotype of patients with peroxisomal disorders subdivided into 16 complimentation groups
    • Moser AE, Rasmussen M, Naidu S, Watkins P, McGuinness M, Hajra AK et al.: Phenotype of patients with peroxisomal disorders subdivided into 16 complimentation groups. J Pediatr 127: 13-22, 1995
    • (1995) J Pediatr , vol.127 , pp. 13-22
    • Moser, A.E.1    Rasmussen, M.2    Naidu, S.3    Watkins, P.4    McGuinness, M.5    Hajra, A.K.6
  • 57
    • 0029888487 scopus 로고    scopus 로고
    • The peroxisome biogenesis disorder group 4 gene, PxAAA1, encodes a cytoplasmic ATPase required for stability of the PTS-1 receptor
    • Yahraus T, Braverman N, Dodt G, Kalish JE, Morrell JC, Moser HW, Valle D, Gould SJ: The peroxisome biogenesis disorder group 4 gene, PxAAA1, encodes a cytoplasmic ATPase required for stability of the PTS-1 receptor. Embo J 15: 2914-2923, 1996
    • (1996) Embo J , vol.15 , pp. 2914-2923
    • Yahraus, T.1    Braverman, N.2    Dodt, G.3    Kalish, J.E.4    Morrell, J.C.5    Moser, H.W.6    Valle, D.7    Gould, S.J.8
  • 59
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • Walton PA, Hill PE, Subramani S: Import of stably folded proteins into peroxisomes. Mol Biol Cell 6: 675-683, 1995
    • (1995) Mol Biol Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 60
    • 0028231695 scopus 로고
    • An inter- Nal region of the peroxisomal membrane protein PMP47 is essential for sorting to peroxisomes
    • McCammon MT, McNew JA, Willy PJ, Goodman JM: An inter- nal region of the peroxisomal membrane protein PMP47 is essential for sorting to peroxisomes. J Cell Biol 124: 915-925, 1994
    • (1994) J Cell Biol , vol.124 , pp. 915-925
    • McCammon, M.T.1    McNew, J.A.2    Willy, P.J.3    Goodman, J.M.4
  • 63
    • 0028092023 scopus 로고
    • Lipid composition of liver peroxisomes isolated from untreated and clofibrate-treated mice and rat
    • Kyrklund T, Meijer J: Lipid composition of liver peroxisomes isolated from untreated and clofibrate-treated mice and rat. Comp Biochem Physiol 109: 665-673, 1994
    • (1994) Comp Biochem Physiol , vol.109 , pp. 665-673
    • Kyrklund, T.1    Meijer, J.2
  • 64
    • 0024891625 scopus 로고
    • The relevance of peroxisome proliferation and cell proliferation in peroxisome proliferator-induced hepatocarcinogenesis
    • Rao SM, Reddy JK: The relevance of peroxisome proliferation and cell proliferation in peroxisome proliferator-induced hepatocarcinogenesis. Drug Metab Rev 21: 103-110, 1989
    • (1989) Drug Metab Rev , vol.21 , pp. 103-110
    • Rao, S.M.1    Reddy, J.K.2
  • 65
    • 0026100678 scopus 로고
    • Peroxisome proliferation and nongenotoxic carcinogenesis: Commentary on a symposium
    • Moody DE, Reddy JK, Lake BG, Popp JA, Reese DH: Peroxisome proliferation and nongenotoxic carcinogenesis: Commentary on a symposium. Fundam Appl Toxicol 16: 223-248, 1991
    • (1991) Fundam Appl Toxicol , vol.16 , pp. 223-248
    • Moody, D.E.1    Reddy, J.K.2    Lake, B.G.3    Popp, J.A.4    Reese, D.H.5
  • 66
    • 0026529169 scopus 로고
    • Receptor-mediated mechanisms of peroxisome proliferators
    • Green S: Receptor-mediated mechanisms of peroxisome proliferators. Biochem Pharmacol 43: 393-401, 1992
    • (1992) Biochem Pharmacol , vol.43 , pp. 393-401
    • Green, S.1
  • 68
    • 0022560429 scopus 로고
    • Comparison of hepatic peroxisome proliferative effect and its implication for hepatocarcinogenicity of phthalate esters, di(2-ethylhexyl) phthlate and di(2-ethylhexyl) adipate with a hypolipidemic drug
    • Reddy JK, Reddy MK, Usman MI, Lalwani ND, Rao MS: Comparison of hepatic peroxisome proliferative effect and its implication for hepatocarcinogenicity of phthalate esters, di(2-ethylhexyl) phthlate and di(2-ethylhexyl) adipate with a hypolipidemic drug. Environ Health Prospect 65: 317-327, 1986
    • (1986) Environ Health Prospect , vol.65 , pp. 317-327
    • Reddy, J.K.1    Reddy, M.K.2    Usman, M.I.3    Lalwani, N.D.4    Rao, M.S.5
  • 69
    • 0028987876 scopus 로고
    • Mechanism of hepatocarcinogenicity of peroxisome-proliferating drugs and chemicals
    • Lake BG: Mechanism of hepatocarcinogenicity of peroxisome-proliferating drugs and chemicals. Annu Rev Pharm Toxicol 35: 483-507, 1995
    • (1995) Annu Rev Pharm Toxicol , vol.35 , pp. 483-507
    • Lake, B.G.1
  • 70
    • 0025132245 scopus 로고
    • Activation of a number of the steroid hormone receptor superfamily by peroxisome proliferators
    • Isseman I, Green S: Activation of a number of the steroid hormone receptor superfamily by peroxisome proliferators. Nature 347: 645-650, 1990
    • (1990) Nature , vol.347 , pp. 645-650
    • Isseman, I.1    Green, S.2
  • 71
    • 0026517010 scopus 로고
    • Control of peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors
    • Dreyer C, Kray G, Keller H, Givel F, Helftenbein G, Wahli W: Control of peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors. Cell 68: 879-887, 1992
    • (1992) Cell , vol.68 , pp. 879-887
    • Dreyer, C.1    Kray, G.2    Keller, H.3    Givel, F.4    Helftenbein, G.5    Wahli, W.6
  • 72
    • 0026730908 scopus 로고
    • The peroxisome proliferator-activated receptor mediates the induction of cyp4A6, a cytochrome P-450 fatty acid omega hydroxylase, by clofibric acid
    • Muerhoff AS: The peroxisome proliferator-activated receptor mediates the induction of cyp4A6, a cytochrome P-450 fatty acid omega hydroxylase, by clofibric acid. J Biol Chem 267: 19051-19053, 1992
    • (1992) J Biol Chem , vol.267 , pp. 19051-19053
    • Muerhoff, A.S.1
  • 73
    • 0025726848 scopus 로고
    • Two cis-acting regulatory sequences in the peroxisome proliferator responsive enhance region of rat acyl-CoA oxidase gene
    • Osumi T, Wen JK, Hashimoto T: Two cis-acting regulatory sequences in the peroxisome proliferator responsive enhance region of rat acyl-CoA oxidase gene. Biochem Biophys Res Commun 175: 866-871, 1991
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 866-871
    • Osumi, T.1    Wen, J.K.2    Hashimoto, T.3
  • 74
    • 0026541591 scopus 로고
    • The mouse peroxisome proliferator activated receptor recognises a response element in the 5′flanking sequence of the rat acyl-CoA oxidase gene
    • Tugwood JD: The mouse peroxisome proliferator activated receptor recognises a response element in the 5′flanking sequence of the rat acyl-CoA oxidase gene. EMBO J 11: 433-439, 1992
    • (1992) EMBO J , vol.11 , pp. 433-439
    • Tugwood, J.D.1
  • 75
    • 0023755328 scopus 로고
    • Comparison of conservative and inducible levels of expression of peroxisomal beta-oxidation and catalase genes in liver and extrahepatic tissues of the rat
    • Numali MR, Usuda N, Reddy MK, Oyasu K, Hashimoto T, Osumi T, Rao MS, Reddy JK: Comparison of conservative and inducible levels of expression of peroxisomal beta-oxidation and catalase genes in liver and extrahepatic tissues of the rat. Cancer Res 48: 5316-5324, 1988
    • (1988) Cancer Res , vol.48 , pp. 5316-5324
    • Numali, M.R.1    Usuda, N.2    Reddy, M.K.3    Oyasu, K.4    Hashimoto, T.5    Osumi, T.6    Rao, M.S.7    Reddy, J.K.8
  • 76
    • 0027314960 scopus 로고
    • The retinoid X receptor enhances the function of the peroxisome proliferator activated receptor
    • Isseman, I, Prince RA, Tugwood JD Green S: The retinoid X receptor enhances the function of the peroxisome proliferator activated receptor. Biochemie 75: 251-256, 1995
    • (1995) Biochemie , vol.75 , pp. 251-256
    • Isseman, I.1    Prince, R.A.2    Tugwood, J.D.3    Green, S.4
  • 77
    • 0027161015 scopus 로고
    • PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene
    • Bardot O, Aldridge TC, Latruffe N, Green S: PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene. Biochem Biophys Res Commun 192: 37-45, 1993
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 37-45
    • Bardot, O.1    Aldridge, T.C.2    Latruffe, N.3    Green, S.4
  • 78
    • 0027504874 scopus 로고
    • Identification of two mPPAR related receptors and the evidence for the five superfamily members
    • Chen F, Law SW, O'Malley BW: Identification of two mPPAR related receptors and the evidence for the five superfamily members. Biochem Biophys Res Commun 196: 671-677, 1993
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 671-677
    • Chen, F.1    Law, S.W.2    O'Malley, B.W.3
  • 79
    • 0026551309 scopus 로고
    • Differential expression and activation of a family of murine peroxisome proliferator-activated receptors
    • Gottlicher M, Widmark E, Li Q, Gustafsson JA: Differential expression and activation of a family of murine peroxisome proliferator-activated receptors. Proc Natl Acad Sci (USA) 89: 4653-4657, 1992
    • (1992) Proc Natl Acad Sci (USA) , vol.89 , pp. 4653-4657
    • Gottlicher, M.1    Widmark, E.2    Li, Q.3    Gustafsson, J.A.4
  • 80
    • 0026785388 scopus 로고
    • Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acid
    • Schmidt A, Endo N, Rutledge SJ, Vogel R, Shinar D, Rodan GA: Identification of a new member of the steroid hormone receptor superfamily that is activated by a peroxisome proliferator and fatty acid. Mol Endocrinol 6: 1634-1641, 1992
    • (1992) Mol Endocrinol , vol.6 , pp. 1634-1641
    • Schmidt, A.1    Endo, N.2    Rutledge, S.J.3    Vogel, R.4    Shinar, D.5    Rodan, G.A.6
  • 81
    • 0027749599 scopus 로고
    • Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver
    • Zhu Y, Alvares K, Huang O, Rao MS, Reddy JK: Cloning of a new member of the peroxisome proliferator-activated receptor gene family from mouse liver. J Biol Chem 268: 26817-26820, 1993
    • (1993) J Biol Chem , vol.268 , pp. 26817-26820
    • Zhu, Y.1    Alvares, K.2    Huang, O.3    Rao, M.S.4    Reddy, J.K.5
  • 82
    • 0027191040 scopus 로고
    • CDNA cloning, chromosomal mapping and functional characterization of the human peroxisomal proliferator activated receptor
    • Sher T, Yi H-F, McBride W, Gonzalez F: cDNA cloning, chromosomal mapping and functional characterization of the human peroxisomal proliferator activated receptor. Biochem 32: 5598-5604, 1993
    • (1993) Biochem , vol.32 , pp. 5598-5604
    • Sher, T.1    Yi, H.-F.2    McBride, W.3    Gonzalez, F.4
  • 83
    • 0026517010 scopus 로고
    • Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors
    • Dreyer C, Krey G, Keller H, Givel F, Helftenbein G, Wahli W: Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors. Cell 68: 879-887, 1992
    • (1992) Cell , vol.68 , pp. 879-887
    • Dreyer, C.1    Krey, G.2    Keller, H.3    Givel, F.4    Helftenbein, G.5    Wahli, W.6
  • 85
    • 0003717603 scopus 로고
    • The relationship between the levels of long chain acyl-CoA and clofibrate-CoA and the induction of peroxisomal β-oxidation
    • HD Fahimi and H Sies (eds). Springer-Verlag, Berlin
    • Berge RK, Aarsland A, Omundsen H, Aasaether N, Male R: The relationship between the levels of long chain acyl-CoA and clofibrate-CoA and the induction of peroxisomal β-oxidation. In: HD Fahimi and H Sies (eds). Peroxisomes in Biology and Medicine. Springer-Verlag, Berlin, 1987, 273-276
    • (1987) Peroxisomes in Biology and Medicine , pp. 273-276
    • Berge, R.K.1    Aarsland, A.2    Omundsen, H.3    Aasaether, N.4    Male, R.5
  • 86
    • 0024509605 scopus 로고
    • Biochemical mechanisms of induction of hepatic peroxisome proliferation
    • Lock EA: Biochemical mechanisms of induction of hepatic peroxisome proliferation. Annu Rev Pharm Toxicol 29: 145-163, 1989
    • (1989) Annu Rev Pharm Toxicol , vol.29 , pp. 145-163
    • Lock, E.A.1
  • 87
    • 0022924249 scopus 로고
    • Peroxisome proliferation due to di (2-ethyl) phthalate (DEHP): Species differences and possible mechanisms
    • Elcombe CR: Peroxisome proliferation due to di (2-ethyl) phthalate (DEHP): Species differences and possible mechanisms. Environ Health Prospect 70: 211-219, 1986
    • (1986) Environ Health Prospect , vol.70 , pp. 211-219
    • Elcombe, C.R.1
  • 88
    • 0026705751 scopus 로고
    • Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors
    • Kliewer SA, Umesono K, Noonan DJ, Heyman RA, Evans RM: Convergence of 9-cis retinoic acid and peroxisome proliferator signalling pathways through heterodimer formation of their receptors. Nature 358: 771-774, 1992
    • (1992) Nature , vol.358 , pp. 771-774
    • Kliewer, S.A.1    Umesono, K.2    Noonan, D.J.3    Heyman, R.A.4    Evans, R.M.5
  • 89
    • 0027476494 scopus 로고
    • Genotype effects of selected peroxisome proliferators
    • Reisenbicher H, Eckl PM: Genotype effects of selected peroxisome proliferators. Mutat Res 286: 135-144, 1993
    • (1993) Mutat Res , vol.286 , pp. 135-144
    • Reisenbicher, H.1    Eckl, P.M.2
  • 90
    • 0027161015 scopus 로고
    • PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene
    • Bardot O, Aldridge TC, Latruffe N, Green S: PPAR-RXR heterodimer activates a peroxisome proliferator response element upstream of the bifunctional enzyme gene. Biochim Biophys Res Commun 192: 37-45, 1993
    • (1993) Biochim Biophys Res Commun , vol.192 , pp. 37-45
    • Bardot, O.1    Aldridge, T.C.2    Latruffe, N.3    Green, S.4
  • 91
    • 0027290892 scopus 로고
    • Chicken ovalbumin upstream promoter transcription factor (COUP-TF) binds to a peroxisome proliferator-responsive element and antagonizes peroxisome proliferator-mediated signaling
    • Miyata KS, Zhang B, Marcus SL, Capone JP, Rachubinski RA: Chicken ovalbumin upstream promoter transcription factor (COUP-TF) binds to a peroxisome proliferator-responsive element and antagonizes peroxisome proliferator-mediated signaling. J Biol Chem 268: 19169-19172, 1993
    • (1993) J Biol Chem , vol.268 , pp. 19169-19172
    • Miyata, K.S.1    Zhang, B.2    Marcus, S.L.3    Capone, J.P.4    Rachubinski, R.A.5
  • 92
    • 0027526347 scopus 로고
    • Induction of sister chromatid exchange and micronuclei in primary cultures of rat and human hepatocytes by the peroxisome proliferator, Wy-14, 643
    • Hwang J-J, Hsia MT, Jirtle RL: Induction of sister chromatid exchange and micronuclei in primary cultures of rat and human hepatocytes by the peroxisome proliferator, Wy-14, 643. Mutat Res 286: 123-133, 1993
    • (1993) Mutat Res , vol.286 , pp. 123-133
    • Hwang, J.-J.1    Hsia, M.T.2    Jirtle, R.L.3
  • 93
    • 0027276531 scopus 로고
    • Ability of peroxisome proliferators to induce cell transformation, chromosome aberrations and peroxisome proliferation in cultured Syrian hamster embryo cells
    • Tsutsui T, Watnabe E, Barrett JC: Ability of peroxisome proliferators to induce cell transformation, chromosome aberrations and peroxisome proliferation in cultured Syrian hamster embryo cells. Carcin 14: 611-618, 1993
    • (1993) Carcin , vol.14 , pp. 611-618
    • Tsutsui, T.1    Watnabe, E.2    Barrett, J.C.3
  • 94
    • 0022965484 scopus 로고
    • Increased hydroxyl radical production in liver peroxisomal fractions from rats treated with peroxisome proliferators
    • Elliott BM, Dodd NJ, Elcombe CR: Increased hydroxyl radical production in liver peroxisomal fractions from rats treated with peroxisome proliferators. Carcin 7: 795-799, 1986
    • (1986) Carcin , vol.7 , pp. 795-799
    • Elliott, B.M.1    Dodd, N.J.2    Elcombe, C.R.3
  • 96
    • 0028021576 scopus 로고
    • Antioxidant enzymes in ciprofibrate-induced oxidative stress
    • Dhaunsi GS, Singh I, Orak JK, Singh AK: Antioxidant enzymes in ciprofibrate-induced oxidative stress. Carcin 15: 1923-1930, 1994
    • (1994) Carcin , vol.15 , pp. 1923-1930
    • Dhaunsi, G.S.1    Singh, I.2    Orak, J.K.3    Singh, A.K.4
  • 98
    • 0024507717 scopus 로고
    • Induction of microsomal NADPH-cytochrome P-450 reductase and cytochrome P-450IVA1 (P-450LA omega) by dehydroepian-drosterone in rats: A possible peroxisomal proliferator
    • Wu H, Masset-Brown J, Tweedie DJ, Milewich L, Frenkel RA, Martin-Wixtrom C, Estabrook RW, Prough RA: Induction of microsomal NADPH-cytochrome P-450 reductase and cytochrome P-450IVA1 (P-450LA omega) by dehydroepian-drosterone in rats: A possible peroxisomal proliferator. Cancer Res 49: 2337-2343, 1989
    • (1989) Cancer Res , vol.49 , pp. 2337-2343
    • Wu, H.1    Masset-Brown, J.2    Tweedie, D.J.3    Milewich, L.4    Frenkel, R.A.5    Martin-Wixtrom, C.6    Estabrook, R.W.7    Prough, R.A.8
  • 99
    • 0026028977 scopus 로고
    • Induction of rat liver DNA alterations by chronic administration of peroxisome proliferators as detected by 32P-postlabeling
    • Randernath E, Randernath K, Reddy R, Danna TF, Rao MS, Reddy JK: Induction of rat liver DNA alterations by chronic administration of peroxisome proliferators as detected by 32P-postlabeling. Mutat Res 247: 64-76, 1991
    • (1991) Mutat Res , vol.247 , pp. 64-76
    • Randernath, E.1    Randernath, K.2    Reddy, R.3    Danna, T.F.4    Rao, M.S.5    Reddy, J.K.6
  • 100
    • 0024323931 scopus 로고
    • Formation of 8-hydroxydeoxyguanosine in liver DNA of rats following long-term exposure to a peroxisome proliferator
    • Kasai H, Okada Y, Nishimura S, Rao MS, Reddy JK: Formation of 8-hydroxydeoxyguanosine in liver DNA of rats following long-term exposure to a peroxisome proliferator. Cancer Res 49: 2603-2605, 1989
    • (1989) Cancer Res , vol.49 , pp. 2603-2605
    • Kasai, H.1    Okada, Y.2    Nishimura, S.3    Rao, M.S.4    Reddy, J.K.5
  • 101
    • 0342704171 scopus 로고
    • Production of 8-hydroxydeoxyguanosine in rodent liver by the administration of peroxisome proliferators
    • G Gibson and B Lake (eds). Taylor and Francis, London
    • Takagi A, Sai K, Umemura T, Hasegawa R, Kurokawa Y: Production of 8-hydroxydeoxyguanosine in rodent liver by the administration of peroxisome proliferators. In: G Gibson and B Lake (eds). Peroxisomes: Biology and Importance in Toxicology and Medicine. Taylor and Francis, London, 1993, 569-594
    • (1993) Peroxisomes: Biology and Importance in Toxicology and Medicine , pp. 569-594
    • Takagi, A.1    Sai, K.2    Umemura, T.3    Hasegawa, R.4    Kurokawa, Y.5
  • 102
    • 0020002346 scopus 로고
    • Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway
    • Hajra AK, Bishop JE: Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway. Ann NY Acad Sci 386: 170-182, 1982
    • (1982) Ann NY Acad Sci , vol.386 , pp. 170-182
    • Hajra, A.K.1    Bishop, J.E.2
  • 103
    • 0342528190 scopus 로고
    • A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug
    • Lazarow PB, de Duve C: A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug. Proc Natl Acad Sci 73: 2043-2046, 1976
    • (1976) Proc Natl Acad Sci , vol.73 , pp. 2043-2046
    • Lazarow, P.B.1    De Duve, C.2
  • 104
    • 0017805412 scopus 로고
    • Rat liver peroxisomes catalyze the Beta-oxidation of fatty acids
    • Lazarow PB: Rat liver peroxisomes catalyze the Beta-oxidation of fatty acids. J Biol Chem 253: 1522-1528, 1978
    • (1978) J Biol Chem , vol.253 , pp. 1522-1528
    • Lazarow, P.B.1
  • 105
    • 0344803532 scopus 로고
    • Lignoceric acid is oxidized in the peroxisome: Implications for the Zellweger cerebro-hepato-renal syndrome and adrenoleukodystrophy
    • Singh I, Moser AE, Goldfischer S, Moser HW: Lignoceric acid is oxidized in the peroxisome: Implications for the Zellweger cerebro-hepato-renal syndrome and adrenoleukodystrophy. Proc Natl Acad Sci (USA) 81: 4203-4207, 1984
    • (1984) Proc Natl Acad Sci (USA) , vol.81 , pp. 4203-4207
    • Singh, I.1    Moser, A.E.2    Goldfischer, S.3    Moser, H.W.4
  • 106
    • 0022600896 scopus 로고
    • Peroxisomal oxidation of lignoceric acid in rat brain
    • Singh RP, Singh I: Peroxisomal oxidation of lignoceric acid in rat brain. Neurochem Res 11: 281-289, 1986
    • (1986) Neurochem Res , vol.11 , pp. 281-289
    • Singh, R.P.1    Singh, I.2
  • 107
    • 0026766117 scopus 로고
    • Metabolic zonation of the liver: Regulation and implications for liver functions
    • Gebhard R: Metabolic zonation of the liver: regulation and implications for liver functions. Pharmacol Ther 53: 275-354, 1992
    • (1992) Pharmacol Ther , vol.53 , pp. 275-354
    • Gebhard, R.1
  • 108
    • 0002435178 scopus 로고
    • Organization and zonation of hepatic lipid metabolism
    • Bass NM: Organization and zonation of hepatic lipid metabolism. Cell Biol Rev 19: 61-89, 1989
    • (1989) Cell Biol Rev , vol.19 , pp. 61-89
    • Bass, N.M.1
  • 109
    • 0028064874 scopus 로고
    • Zonal heterogeneity of peroxisomal enzymes in rat liver: Differential induction by three divergent hypolipidemic drugs
    • Lindauer M, Beier K, Volkl A, Fahimi HD: Zonal heterogeneity of peroxisomal enzymes in rat liver: Differential induction by three divergent hypolipidemic drugs. Hepatol 20: 475-486, 1994
    • (1994) Hepatol , vol.20 , pp. 475-486
    • Lindauer, M.1    Beier, K.2    Volkl, A.3    Fahimi, H.D.4
  • 110
    • 0000228425 scopus 로고
    • Disorders of peroxisome biogenesis
    • CR Scriver, AL Beaudet, WS Sly, D Valle, D McGraw-Hill, (eds)
    • Lazarow PB, Moser HW: Disorders of peroxisome biogenesis. In: CR Scriver, AL Beaudet, WS Sly, D Valle, D McGraw-Hill, (eds). The Metabolic Basis of Inherited Diseases. 6th Edn. 1989, 479-1509
    • (1989) The Metabolic Basis of Inherited Diseases. 6th Edn. , pp. 479-1509
    • Lazarow, P.B.1    Moser, H.W.2
  • 111
    • 7944238371 scopus 로고
    • The pathway from 'activated acetic acid' to the terpenes and fatty acids
    • American Elsevier, New York
    • Lynen F: The pathway from 'activated acetic acid' to the terpenes and fatty acids. In: Physiology or Medicine Nobel Lecturers 1963-1970. American Elsevier, New York, 1973, 103-108
    • (1973) Physiology or Medicine Nobel Lecturers 1963-1970 , pp. 103-108
    • Lynen, F.1
  • 112
    • 0014670256 scopus 로고
    • Beta oxidation in glyoxysomes from castor bean endosperm
    • Cooper TG, Beever H: Beta oxidation in glyoxysomes from castor bean endosperm. J Biol Chem 244: 3514-3520, 1969
    • (1969) J Biol Chem , vol.244 , pp. 3514-3520
    • Cooper, T.G.1    Beever, H.2
  • 113
    • 0019296591 scopus 로고
    • Conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoic acid into cholic acid by rat liver peroxisomes
    • Pedersen JI, Gustaffson J: Conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestanoic acid into cholic acid by rat liver peroxisomes. FEBS Lett. 121: 345-348, 1980
    • (1980) FEBS Lett , vol.121 , pp. 345-348
    • Pedersen, J.I.1    Gustaffson, J.2
  • 114
    • 8044242133 scopus 로고
    • Liver peroxisomal oxidizing activities in physiologi- Cal and pathological conditions
    • HD Fahimi and H Sies (eds). Springer-Verlag, Berlin, Heidelberg
    • Vamecq J: Liver peroxisomal oxidizing activities in physiologi- cal and pathological conditions. In: HD Fahimi and H Sies (eds). Peroxisomes in Biology and Medicine. Springer-Verlag, Berlin, Heidelberg, 1987, 364-373
    • (1987) Peroxisomes in Biology and Medicine , pp. 364-373
    • Vamecq, J.1
  • 115
    • 0022859794 scopus 로고
    • Chain-shortening of a xenobiotic acyl compound by the peroxisomal betaoxidation system in rat liver
    • Yamada J, Itoh S, Horie S, Watanabe T, Suga T: Chain-shortening of a xenobiotic acyl compound by the peroxisomal betaoxidation system in rat liver. Biochem Pharmacol 35: 4363-4368, 1986
    • (1986) Biochem Pharmacol , vol.35 , pp. 4363-4368
    • Yamada, J.1    Itoh, S.2    Horie, S.3    Watanabe, T.4    Suga, T.5
  • 116
    • 0024272115 scopus 로고
    • Peroxisomal chain-shortening of prostaglandin F2 alpha
    • Diczfalusy UG, Alexson SEH: Peroxisomal chain-shortening of prostaglandin F2 alpha. J Lipid Res 29: 1629-1636, 1988
    • (1988) J Lipid Res , vol.29 , pp. 1629-1636
    • Diczfalusy, U.G.1    Alexson, S.E.H.2
  • 117
    • 0022870148 scopus 로고
    • β-Oxidation of polyunsaturated fatty acids by rat liver peroxisomes. A role for 2,4-dienoyl-coenzyme A reductase in peroxisomal beta oxidation
    • Hiltunen JK, Karki T, Hassinen IE, Osmundsen H: β-Oxidation of polyunsaturated fatty acids by rat liver peroxisomes. A role for 2,4-dienoyl-coenzyme A reductase in peroxisomal beta oxidation. J Biol Chem 261: 16484-16493, 1986
    • (1986) J Biol Chem , vol.261 , pp. 16484-16493
    • Hiltunen, J.K.1    Karki, T.2    Hassinen, I.E.3    Osmundsen, H.4
  • 118
    • 0025304695 scopus 로고
    • A comparative study of straight chain and branched chain fatty acid oxidation in skin fibroblasts from patients with peroxisomal disorders
    • Singh H, Usher S, Johnson D, Poulos A: A comparative study of straight chain and branched chain fatty acid oxidation in skin fibroblasts from patients with peroxisomal disorders. J Lipid Res 31: 217-225, 1990
    • (1990) J Lipid Res , vol.31 , pp. 217-225
    • Singh, H.1    Usher, S.2    Johnson, D.3    Poulos, A.4
  • 119
    • 0017861910 scopus 로고
    • Lysine metabolism in the rat brain: Blood-brain barrier transport, formation of pipecolic acid and human hyperpipecolatemia
    • Chang YF: Lysine metabolism in the rat brain: blood-brain barrier transport, formation of pipecolic acid and human hyperpipecolatemia. J Neurochem 30: 355-360, 1978
    • (1978) J Neurochem , vol.30 , pp. 355-360
    • Chang, Y.F.1
  • 120
    • 0021930092 scopus 로고
    • Aberration in de novo ether lipid biosynthesis in peroxisomal disorders. Mitochondrial and peroxisomal metabolism of glutaryl-CoA
    • Vamecq J, Hoffman E, van Hoof F: Aberration in de novo ether lipid biosynthesis in peroxisomal disorders. Mitochondrial and peroxisomal metabolism of glutaryl-CoA. Eur J Biochem 146: 663-669, 1985
    • (1985) Eur J Biochem , vol.146 , pp. 663-669
    • Vamecq, J.1    Hoffman, E.2    Van Hoof, F.3
  • 121
    • 0013319440 scopus 로고
    • Comparison of enzymes of lipid β-oxidation in peroxisomes and mitochondria
    • HD Fahimi and H Sies (eds). Springer-Verlag, Berlin, Heidelberg
    • Hashimoto T: Comparison of enzymes of lipid β-oxidation in peroxisomes and mitochondria. In: HD Fahimi and H Sies (eds). Peroxisomes in Biology and Medicine. Springer-Verlag, Berlin, Heidelberg, 1987, 97-104
    • (1987) Peroxisomes in Biology and Medicine , pp. 97-104
    • Hashimoto, T.1
  • 122
    • 0024314080 scopus 로고
    • Pathophysiology of peroxisomal betaoxidation
    • Vamecq J, Draye JP: Pathophysiology of peroxisomal betaoxidation. Essays in Biochem 24: 115-223, 1989
    • (1989) Essays in Biochem , vol.24 , pp. 115-223
    • Vamecq, J.1    Draye, J.P.2
  • 124
    • 0025257335 scopus 로고
    • Presence of three acyl-CoA oxidase in rat liver peroxisomes: An inducible fatty acid acyl-CoA oxidase, noninducible acyl-CoA oxidase and an noninducible trihydroxycoprostanoyl-CoA oxidase
    • Schepers L, Van Veldhoven PP, Casteels M, Eyssen H, Mannaerts GP: Presence of three acyl-CoA oxidase in rat liver peroxisomes: An inducible fatty acid acyl-CoA oxidase, noninducible acyl-CoA oxidase and an noninducible trihydroxycoprostanoyl-CoA oxidase. J Biol Chem 265: 5242-5248, 1990
    • (1990) J Biol Chem , vol.265 , pp. 5242-5248
    • Schepers, L.1    Van Veldhoven, P.P.2    Casteels, M.3    Eyssen, H.4    Mannaerts, G.P.5
  • 125
    • 0025356024 scopus 로고
    • Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities
    • Palosauri PM, Hiltunen JK: Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. J Biol Chem 265: 2446-2449, 1990
    • (1990) J Biol Chem , vol.265 , pp. 2446-2449
    • Palosauri, P.M.1    Hiltunen, J.K.2
  • 127
    • 0025231591 scopus 로고
    • Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated genes
    • Hijikata M, Wen J-K, Osumi T, Hashimoto T: Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated genes. J Biol Chem 265: 4600-4606, 1990
    • (1990) J Biol Chem , vol.265 , pp. 4600-4606
    • Hijikata, M.1    Wen, J.-K.2    Osumi, T.3    Hashimoto, T.4
  • 128
    • 0025182565 scopus 로고
    • Cloning and sequence determination of cDNA encoding a second rat liver peroxisomal 3-ketoacyl-CoA thiolase
    • Bodnar AG, Rachubinski RA: Cloning and sequence determination of cDNA encoding a second rat liver peroxisomal 3-ketoacyl-CoA thiolase. Gene (Amst) 91: 193-199, 1990
    • (1990) Gene (Amst) , vol.91 , pp. 193-199
    • Bodnar, A.G.1    Rachubinski, R.A.2
  • 129
    • 0025900705 scopus 로고
    • Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient
    • Bout A, Franse MM, Collins J, Blonden L, Tager JM, Benne R: Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient. Biochim Biophys Acta 1090: 43-51, 1991
    • (1991) Biochim Biophys Acta , vol.1090 , pp. 43-51
    • Bout, A.1    Franse, M.M.2    Collins, J.3    Blonden, L.4    Tager, J.M.5    Benne, R.6
  • 130
    • 0021910745 scopus 로고
    • Lignoceroyl-CoA ligase activity in rat brain microsomal fraction: Topographical localization and effect of detergents and Alpha-cyclodextrin
    • Singh I, Singh RP, Bhushan A, Singh AK: Lignoceroyl-CoA ligase activity in rat brain microsomal fraction: Topographical localization and effect of detergents and Alpha-cyclodextrin. Arch Biochem Biophys 236: 418-426, 1985
    • (1985) Arch Biochem Biophys , vol.236 , pp. 418-426
    • Singh, I.1    Singh, R.P.2    Bhushan, A.3    Singh, A.K.4
  • 131
    • 0023737516 scopus 로고
    • Distinct long chain and very long chain fatty acyl-CoA synthetase in rat liver peroxisomes and microsomes
    • Singh H, Poulos A: Distinct long chain and very long chain fatty acyl-CoA synthetase in rat liver peroxisomes and microsomes. Arch Biochem Biophys 266: 486-495, 1988
    • (1988) Arch Biochem Biophys , vol.266 , pp. 486-495
    • Singh, H.1    Poulos, A.2
  • 132
    • 0025352608 scopus 로고
    • Cellular oxidation of lignoceric acid is regulated by the subcellular localization of lignoceroyl-CoA ligases
    • Lazo O, Contreras M, Yoshida Y, Singh AK, Stanley W, Weise MJ, Singh I: Cellular oxidation of lignoceric acid is regulated by the subcellular localization of lignoceroyl-CoA ligases. J Lipid Res 31: 583-595, 1990
    • (1990) J Lipid Res , vol.31 , pp. 583-595
    • Lazo, O.1    Contreras, M.2    Yoshida, Y.3    Singh, A.K.4    Stanley, W.5    Weise, M.J.6    Singh, I.7
  • 133
    • 0025181353 scopus 로고
    • D-3-hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters
    • Li J, Smeland TE, Shulz H: D-3-hydroxyacyl coenzyme A dehydratase from rat liver peroxisomes. Purification and characterization of a novel enzyme necessary for the epimerization of 3-hydroxyacyl-CoA thioesters. J Biol Chem 265: 13629-13634, 1990
    • (1990) J Biol Chem , vol.265 , pp. 13629-13634
    • Li, J.1    Smeland, T.E.2    Shulz, H.3
  • 134
    • 0022586313 scopus 로고
    • Evidence for peroxisomal retroconversion of adrenic acid (22:4(n-6)) and docosahexaenoic acids (22:6(n-3)) in isolated liver cells
    • Hague TA, Christophersen BO: Evidence for peroxisomal retroconversion of adrenic acid (22:4(n-6)) and docosahexaenoic acids (22:6(n-3)) in isolated liver cells. Biochim Biophys Acta 875: 165-173, 1986
    • (1986) Biochim Biophys Acta , vol.875 , pp. 165-173
    • Hague, T.A.1    Christophersen, B.O.2
  • 135
    • 0024320081 scopus 로고
    • Epimerization of 3-hydroxyacyl-CoA esters in rat liver. Involvement of two 2-enoyl-CoA hydratases
    • Hiltunen JK, Palosuari PM, Kunan WH: Epimerization of 3-hydroxyacyl-CoA esters in rat liver. Involvement of two 2-enoyl-CoA hydratases. J Biol Chem 264: 13536-13540, 1989
    • (1989) J Biol Chem , vol.264 , pp. 13536-13540
    • Hiltunen, J.K.1    Palosuari, P.M.2    Kunan, W.H.3
  • 136
    • 0024354290 scopus 로고
    • The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: A revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation
    • Smeland TE, Li JX, Chen CH, Cuebas D, Shulz H: The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: A revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation. Biochem Biophys Res Commun 160: 988-992, 1989
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 988-992
    • Smeland, T.E.1    Li, J.X.2    Chen, C.H.3    Cuebas, D.4    Shulz, H.5
  • 137
    • 0023446398 scopus 로고
    • Peroxisomal β-oxidation of long chain fatty acid processing different extent of unsaturation
    • Hovik R, Omundsen H: Peroxisomal β-oxidation of long chain fatty acid processing different extent of unsaturation. Biochem J 247: 531-535, 1987
    • (1987) Biochem J , vol.247 , pp. 531-535
    • Hovik, R.1    Omundsen, H.2
  • 138
    • 0024296424 scopus 로고
    • The Zellweger syndrome: Deficient chain shortening of erucic acid (22:1(n-9)) and adrenic acid (22:4(n-6)) in cultured skin fibroblasts
    • Christensen E, Hague TA, Christopherson BO: The Zellweger syndrome: Deficient chain shortening of erucic acid (22:1(n-9)) and adrenic acid (22:4(n-6)) in cultured skin fibroblasts. Biochim Biophys Acta 959: 134-142, 1988
    • (1988) Biochim Biophys Acta , vol.959 , pp. 134-142
    • Christensen, E.1    Hague, T.A.2    Christopherson, B.O.3
  • 139
    • 0021710106 scopus 로고
    • The eicosanoids in biology and medicine
    • Marcus AJ: The eicosanoids in biology and medicine. J Lipid Res 25: 1511-1516, 1984
    • (1984) J Lipid Res , vol.25 , pp. 1511-1516
    • Marcus, A.J.1
  • 143
    • 0026620659 scopus 로고
    • Role of peroxisomes in the degradation of prostaglandins
    • Diczfalusy UG, Alexson EH: Role of peroxisomes in the degradation of prostaglandins. Prog Clin Biol Res 375: 253-261, 1992
    • (1992) Prog Clin Biol Res , vol.375 , pp. 253-261
    • Diczfalusy, U.G.1    Alexson, E.H.2
  • 144
    • 0027270309 scopus 로고
    • Peroxisomal oxidation of steroid side chain in bile acid formation
    • Pederson JI: Peroxisomal oxidation of steroid side chain in bile acid formation. Biochemie 75: 167-174, 1993
    • (1993) Biochemie , vol.75 , pp. 167-174
    • Pederson, J.I.1
  • 145
    • 0022515485 scopus 로고
    • In vitro formation of bile acids from di- And trihydroxy-5 beta-cholestanoic acid in human liver peroxisomes
    • Kase BF, Prydz K, Bjorkhem I, Pederson JI: In vitro formation of bile acids from di- and trihydroxy-5 beta-cholestanoic acid in human liver peroxisomes. Biochim Biophys Acta 877: 37-42, 1986
    • (1986) Biochim Biophys Acta , vol.877 , pp. 37-42
    • Kase, B.F.1    Prydz, K.2    Bjorkhem, I.3    Pederson, J.I.4
  • 146
    • 0022357561 scopus 로고
    • Bile acid synthesis in rat liver peroxisomes: Metabolism of 26-hydroxycholesterol to 3 beta-hydroxy-5-cholenoic acid
    • Krisans SK, Thompson SL, Pena LA, Kok E, Javitt NB: Bile acid synthesis in rat liver peroxisomes: metabolism of 26-hydroxycholesterol to 3 beta-hydroxy-5-cholenoic acid. J Lipid Res 26: 1324-1332, 1985
    • (1985) J Lipid Res , vol.26 , pp. 1324-1332
    • Krisans, S.K.1    Thompson, S.L.2    Pena, L.A.3    Kok, E.4    Javitt, N.B.5
  • 147
    • 0023926491 scopus 로고
    • Inhibition of 3 alpha, 7 alpha, 12 alpha-trlhydroxy-5 betacholestanoic acid oxidation and of bile acid secretion in rat liver by fatty acids
    • Casteels M, Schepers L, van Eldere JR, Eyssen HJ, Mannaerts GP: Inhibition of 3 alpha, 7 alpha, 12 alpha-trlhydroxy-5 betacholestanoic acid oxidation and of bile acid secretion in rat liver by fatty acids. J Biol Chem 263: 4654-4661, 1988
    • (1988) J Biol Chem , vol.263 , pp. 4654-4661
    • Casteels, M.1    Schepers, L.2    Van Eldere, J.R.3    Eyssen, H.J.4    Mannaerts, G.P.5
  • 148
    • 0024554625 scopus 로고
    • Identification of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholest-24-enoic acid as an intermediate in the peroxisomal conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5-beta-cholestanoic acid to cholic acid
    • Ostlund Farrants AK, Bjorkhem I, Pederson JI: Identification of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholest-24-enoic acid as an intermediate in the peroxisomal conversion of 3 alpha, 7 alpha, 12 alpha-trihydroxy-5-beta-cholestanoic acid to cholic acid. Biochim Biophys Acta 1002 (2): 198-202, 1989
    • (1989) Biochim Biophys Acta , vol.1002 , Issue.2 , pp. 198-202
    • Ostlund Farrants, A.K.1    Bjorkhem, I.2    Pederson, J.I.3
  • 151
    • 0025169032 scopus 로고
    • A new peroxisomal disorder: Di- And trihydroxycholestanaemia due to a presumed trihydroxycholestanoyl-CoA oxidase deficiency
    • Christensen E, van Eldere JR, Brandt NJ, Schutgens RB, Wanders RJA, Eyssen HJ: A new peroxisomal disorder: di- and trihydroxycholestanaemia due to a presumed trihydroxycholestanoyl-CoA oxidase deficiency. J Inher Metab Dis 13: 363-366, 1990
    • (1990) J Inher Metab Dis , vol.13 , pp. 363-366
    • Christensen, E.1    Van Eldere, J.R.2    Brandt, N.J.3    Schutgens, R.B.4    Wanders, R.J.A.5    Eyssen, H.J.6
  • 152
    • 0025875876 scopus 로고
    • Inborn Errors of Bile Acid Metabolism
    • Clayton PT: Inborn Errors of Bile Acid Metabolism. J Inher Metab Dis 14: 478-496, 1991
    • (1991) J Inher Metab Dis , vol.14 , pp. 478-496
    • Clayton, P.T.1
  • 153
    • 0025359856 scopus 로고
    • Bile acid profiles in peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency
    • Clayton PT, Patel E, Lawson AM, Curruthers RA: Bile acid profiles in peroxisomal 3-oxoacyl-coenzyme A thiolase deficiency. J Clin Invest 85: 1267-1273, 1990
    • (1990) J Clin Invest , vol.85 , pp. 1267-1273
    • Clayton, P.T.1    Patel, E.2    Lawson, A.M.3    Curruthers, R.A.4
  • 155
    • 0024374648 scopus 로고
    • Peroxisomal bile acid CoA: Amino acid N-acetyltransferase in rat liver
    • Kase BE, Bjorkhem I: Peroxisomal bile acid CoA: Amino acid N-acetyltransferase in rat liver. J Biol Chem 264: 9220-9223, 1989
    • (1989) J Biol Chem , vol.264 , pp. 9220-9223
    • Kase, B.E.1    Bjorkhem, I.2
  • 156
    • 0022535484 scopus 로고
    • Conjugation of cholic acid with taurine and glycine by rat liver peroxisomes
    • Kase BE, Prydz K, Bjorkhem I, Pedersen JI: Conjugation of cholic acid with taurine and glycine by rat liver peroxisomes. Biochem Biophys Res Commun 138: 167-173, 1986
    • (1986) Biochem Biophys Res Commun , vol.138 , pp. 167-173
    • Kase, B.E.1    Prydz, K.2    Bjorkhem, I.3    Pedersen, J.I.4
  • 157
    • 0022357211 scopus 로고
    • Identity of long-chain acyl-Coenzyme A synthetase of microsomes, mitochondria, and peroxisomes in rat liver
    • Miyazawa S, Hashimoto T, Yokoda S: Identity of long-chain acyl-Coenzyme A synthetase of microsomes, mitochondria, and peroxisomes in rat liver. J Biochem 98: 723-733, 1985
    • (1985) J Biochem , vol.98 , pp. 723-733
    • Miyazawa, S.1    Hashimoto, T.2    Yokoda, S.3
  • 158
    • 0019333103 scopus 로고
    • Acyl-CoA Synthetase in Rat Liver Peroxisomes. Computer-assisted analysis of cell fractionation experiments
    • Krisans SK, Mortensen RM, Lazarow PB: Acyl-CoA Synthetase in Rat Liver Peroxisomes. Computer-assisted analysis of cell fractionation experiments. J Biol Chem 255: 9599-9607, 1980
    • (1980) J Biol Chem , vol.255 , pp. 9599-9607
    • Krisans, S.K.1    Mortensen, R.M.2    Lazarow, P.B.3
  • 159
    • 0025232317 scopus 로고
    • Transverse-plane topography of long chain acyl-CoA synthetase in the mitochondrial outer membrane
    • Hester CB, Olymbois C, Halder D: Transverse-plane topography of long chain acyl-CoA synthetase in the mitochondrial outer membrane. J Biol Chem 265: 6600-6605, 1990
    • (1990) J Biol Chem , vol.265 , pp. 6600-6605
    • Hester, C.B.1    Olymbois, C.2    Halder, D.3
  • 160
    • 0015211317 scopus 로고
    • The separation and properties of two forms of carnitine palmitoyltransferase from ox liver mitochondria
    • West DW, Chase JFA, Tubbs PK: The separation and properties of two forms of carnitine palmitoyltransferase from ox liver mitochondria. Biochem Biophys Res Commun 42: 912-918, 1971
    • (1971) Biochem Biophys Res Commun , vol.42 , pp. 912-918
    • West, D.W.1    Chase, J.F.A.2    Tubbs, P.K.3
  • 161
    • 0020483106 scopus 로고
    • Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane
    • Mannaerts GP, van Veldhoven P, van Brockhoven A, van de Broek G, De Beer LJ: Evidence that peroxisomal acyl-CoA synthetase is located at the cytoplasmic side of the peroxisomal membrane. Biochem J 204: 17-23, 1982
    • (1982) Biochem J , vol.204 , pp. 17-23
    • Mannaerts, G.P.1    Van Veldhoven, P.2    Van Brockhoven, A.3    Van de Broek, G.4    De Beer, L.J.5
  • 162
    • 0025332595 scopus 로고
    • Topographical localization of peroxisomal acyl-CoA ligases: Differential localization of palmitoyl-CoA and lignoceroyl-CoA ligases
    • Lazo O, Contreras M, Singh I: Topographical localization of peroxisomal acyl-CoA ligases: differential localization of palmitoyl-CoA and lignoceroyl-CoA ligases. Biochem 29: 3982-3986, 1990
    • (1990) Biochem , vol.29 , pp. 3982-3986
    • Lazo, O.1    Contreras, M.2    Singh, I.3
  • 163
    • 0025908307 scopus 로고
    • Topography of very-long-chain-fatty-acid-activating activity in peroxisomes from rat liver
    • Lage weg W, Tager JM, Wanders RJA: Topography of very-long-chain-fatty-acid-activating activity in peroxisomes from rat liver. Biochem J 276: 53-56, 1991
    • (1991) Biochem J , vol.276 , pp. 53-56
    • Lage Weg, W.1    Tager, J.M.2    Wanders, R.J.A.3
  • 165
    • 0026621732 scopus 로고
    • Peroxisomal activation, transport and oxidation of fatty acids: Implications to peroxisomal disorders
    • P Coates and K Tanaka (eds). John Wiley & Sons, Inc, New York
    • Singh I: Peroxisomal activation, transport and oxidation of fatty acids: Implications to peroxisomal disorders. In: P Coates and K Tanaka (eds). Proceedings of Second International Symposium on Clinical, Biochemical and Molecular Aspects of Fatty Acid Oxidation. John Wiley & Sons, Inc, New York, 1992, pp 211-222
    • (1992) Proceedings of Second International Symposium on Clinical, Biochemical and Molecular Aspects of Fatty Acid Oxidation , pp. 211-222
    • Singh, I.1
  • 166
    • 0026770745 scopus 로고
    • Transport of fatty acids into human peroxisomes and rat peroxisomes: Differential transport of palmitic and lignoceric acids and its implications to X-adrenoleukodystrophy
    • Singh I, Lazo O, Dhaunsi GS, Contreras M: Transport of fatty acids into human peroxisomes and rat peroxisomes: Differential transport of palmitic and lignoceric acids and its implications to X-adrenoleukodystrophy. J Biol Chem 267: 13306-13313, 1992
    • (1992) J Biol Chem , vol.267 , pp. 13306-13313
    • Singh, I.1    Lazo, O.2    Dhaunsi, G.S.3    Contreras, M.4
  • 167
    • 0025256865 scopus 로고
    • Effect of Clofibrate on peroxisomal lignoceroyl-CoA ligase
    • Yoshida Y, Singh I: Effect of Clofibrate on peroxisomal lignoceroyl-CoA ligase. Biochem Med Met Biol 43: 22-29, 1990
    • (1990) Biochem Med Met Biol , vol.43 , pp. 22-29
    • Yoshida, Y.1    Singh, I.2
  • 168
    • 0026008521 scopus 로고
    • Effect of ciprofibrate on the activation and oxidation of very long chain fatty acids
    • Lazo O, Contreras M, Singh I: Effect of ciprofibrate on the activation and oxidation of very long chain fatty acids. Mol Cell Biochem 100: 159-167, 1991
    • (1991) Mol Cell Biochem , vol.100 , pp. 159-167
    • Lazo, O.1    Contreras, M.2    Singh, I.3
  • 169
    • 0024601068 scopus 로고
    • Adrenoleukodystrophy: Impaired oxidation of fatty acids due to peroxisomal lignoceroyl-CoA ligase deficiency
    • Lazo O, Contreras M, Bhushan W, Stanley W, Singh I: Adrenoleukodystrophy: impaired oxidation of fatty acids due to peroxisomal lignoceroyl-CoA ligase deficiency. Arch Biochem Biophys 270: 722-728, 1989
    • (1989) Arch Biochem Biophys , vol.270 , pp. 722-728
    • Lazo, O.1    Contreras, M.2    Bhushan, W.3    Stanley, W.4    Singh, I.5
  • 170
    • 0002575617 scopus 로고
    • Refsum disease
    • R Scriver, AL Beaudet, WS Sly and D Valle (eds). McGraw-Hill Book Co., New York
    • Steinberg D: Refsum disease. In: R Scriver, AL Beaudet, WS Sly and D Valle (eds). The Metabolic Basis of Inherited Disease. 6th ed. McGraw-Hill Book Co., New York, 1989, pp 1533-1550
    • (1989) The Metabolic Basis of Inherited Disease. 6th Ed. , pp. 1533-1550
    • Steinberg, D.1
  • 172
    • 0014690479 scopus 로고
    • Studies on the α-oxidation of phytanic acid by rat liver mitochondria
    • Tsai S-C, Avigan J, Steinberg D: Studies on the α-oxidation of phytanic acid by rat liver mitochondria. J Biol Chem 244: 2682-2692, 1969
    • (1969) J Biol Chem , vol.244 , pp. 2682-2692
    • Tsai, S.-C.1    Avigan, J.2    Steinberg, D.3
  • 173
    • 0021743363 scopus 로고
    • Phytanic acid α-oxidation in rat liver. Requirement of cytosolic factor
    • Muralidharan VB, Kishimoto Y. Phytanic acid α-oxidation in rat liver. Requirement of cytosolic factor. J Biol Chem 259: 13021-13026, 1984
    • (1984) J Biol Chem , vol.259 , pp. 13021-13026
    • Muralidharan, V.B.1    Kishimoto, Y.2
  • 174
    • 0023644098 scopus 로고
    • The subcellular localization of phytanic acid oxidase in rat liver
    • Skjeldal OH, Stokke O: The subcellular localization of phytanic acid oxidase in rat liver. Biochim Biophys Acta 921: 3842, 1987
    • (1987) Biochim Biophys Acta , vol.921 , pp. 3842
    • Skjeldal, O.H.1    Stokke, O.2
  • 175
    • 0023901534 scopus 로고
    • Evidence against alpha-hydroxyphytanic acid as an intermediate in the metabolism of phytanic acid
    • Skjeldal OH, Stokke O: Evidence against alpha-hydroxyphytanic acid as an intermediate in the metabolism of phytanic acid. Scand J Clin Lab Invest 48: 97-102, 1988
    • (1988) Scand J Clin Lab Invest , vol.48 , pp. 97-102
    • Skjeldal, O.H.1    Stokke, O.2
  • 176
    • 0025274261 scopus 로고
    • Mitochondrial oxidation of phytanic acid in human and monkey liver: Implication that Refsum's disease is not a peroxisomal disorder
    • Watkins PA, Mihalik SJ: Mitochondrial oxidation of phytanic acid in human and monkey liver: Implication that Refsum's disease is not a peroxisomal disorder. Biochem Biophys Res Commun 167: 580-586, 1990
    • (1990) Biochem Biophys Res Commun , vol.167 , pp. 580-586
    • Watkins, P.A.1    Mihalik, S.J.2
  • 177
    • 0025835578 scopus 로고
    • Identification of pristanoyl CoA oxidase and phytanic acid decarboxylation in peroxisomes and mitochondria from human liver: Implications for Zellweger syndrome
    • Wanders RJA, Van Roermund CWT, Jakobs C, Ten Brink HJ: Identification of pristanoyl CoA oxidase and phytanic acid decarboxylation in peroxisomes and mitochondria from human liver: Implications for Zellweger syndrome. J Inher Metab Dis 14: 349-352, 1991
    • (1991) J Inher Metab Dis , vol.14 , pp. 349-352
    • Wanders, R.J.A.1    Van Roermund, C.W.T.2    Jakobs, C.3    Ten Brink, H.J.4
  • 179
    • 0026479078 scopus 로고
    • Phytanic acid α-oxidation in human cultured skin fibroblasts
    • Singh I, Lazo O, Pahan K, Singh AK: Phytanic acid α-oxidation in human cultured skin fibroblasts. Biochim Biophys Acta 1180: 221-224, 1992
    • (1992) Biochim Biophys Acta , vol.1180 , pp. 221-224
    • Singh, I.1    Lazo, O.2    Pahan, K.3    Singh, A.K.4
  • 180
    • 0027270301 scopus 로고
    • Phytanic acid α-oxidation. Differential subcellular localization in rat and human tissues and its inhibition by nycodenz
    • Singh I, Pahan K, Dhaunsi GS, Lazo O, Ozand P: Phytanic acid α-oxidation. Differential subcellular localization in rat and human tissues and its inhibition by nycodenz. J Biol Chem 268: 9972-9979, 1993
    • (1993) J Biol Chem , vol.268 , pp. 9972-9979
    • Singh, I.1    Pahan, K.2    Dhaunsi, G.S.3    Lazo, O.4    Ozand, P.5
  • 181
    • 0027369118 scopus 로고
    • Refsum disease: A defect in the α-oxidation of phytanic acid in peroxisomes
    • Singh I, Pahan K, Singh AK, Barbosa E: Refsum disease: a defect in the α-oxidation of phytanic acid in peroxisomes. J Lipid Res 34: 1755-1764, 1993
    • (1993) J Lipid Res , vol.34 , pp. 1755-1764
    • Singh, I.1    Pahan, K.2    Singh, A.K.3    Barbosa, E.4
  • 182
    • 0027289172 scopus 로고
    • Identification of phytanoyl-CoA ligase as a distinct acyl-CoA ligase in peroxisomes from cultured skin fibroblasts
    • Pahan K, Cofer J, Baliga P, Singh I. Identification of phytanoyl-CoA ligase as a distinct acyl-CoA ligase in peroxisomes from cultured skin fibroblasts. FEBS Lett 322: 101-104, 1993
    • (1993) FEBS Lett , vol.322 , pp. 101-104
    • Pahan, K.1    Cofer, J.2    Baliga, P.3    Singh, I.4
  • 183
    • 0027525272 scopus 로고
    • Intraorganellar localization of CoASH-inde- Pendent phytanic acid oxidation in human liver peroxisomes
    • Pahan K, Singh I: Intraorganellar localization of CoASH-inde- pendent phytanic acid oxidation in human liver peroxisomes. FEBS Lett 333: 154-158, 1993
    • (1993) FEBS Lett , vol.333 , pp. 154-158
    • Pahan, K.1    Singh, I.2
  • 184
    • 0029017096 scopus 로고
    • Phytanic acid oxidation: Topographical localization of phytanoy-CoA ligase and transport of phytanic acid into human peroxisomes
    • Pahan K, Singh I: Phytanic acid oxidation: Topographical localization of phytanoy-CoA ligase and transport of phytanic acid into human peroxisomes. J Lipid Res 36: 986-997, 1995
    • (1995) J Lipid Res , vol.36 , pp. 986-997
    • Pahan, K.1    Singh, I.2
  • 185
    • 0023903643 scopus 로고
    • Accumulation of pristanic acid in the plasma of patients with generalized peroxisomal dysfunction
    • Poulos A, Sharp P, Fallenberg AJ, Johnson DW: Accumulation of pristanic acid in the plasma of patients with generalized peroxisomal dysfunction. Eur J Pediatr 147: 143-147, 1988
    • (1988) Eur J Pediatr , vol.147 , pp. 143-147
    • Poulos, A.1    Sharp, P.2    Fallenberg, A.J.3    Johnson, D.W.4
  • 186
    • 0028172483 scopus 로고
    • Phytanic acid α-oxidation in rat liver mitochondria
    • Pahan K, Gulati S, Singh I: Phytanic acid α-oxidation in rat liver mitochondria. Biochim Biophys Acta 1201: 491-497, 1994
    • (1994) Biochim Biophys Acta , vol.1201 , pp. 491-497
    • Pahan, K.1    Gulati, S.2    Singh, I.3
  • 188
    • 0001918294 scopus 로고
    • Ether-Linked glycerolipids and their bioactive species: Enzymes and metabolic regulation
    • AN Martinosi (ed). Plenum Press, New York
    • Snyder F, Lee T, Wykle RL: Ether-Linked glycerolipids and their bioactive species: Enzymes and metabolic regulation. In: AN Martinosi (ed). The enzymes of biological membranes, Vol. 2. Plenum Press, New York, 1985, pp 1-58
    • (1985) The Enzymes of Biological Membranes , vol.2 , pp. 1-58
    • Snyder, F.1    Lee, T.2    Wykle, R.L.3
  • 189
    • 0024200531 scopus 로고
    • The role of peroxisomes in glycerol ether lipid metabolism
    • Hajra AK, Horie S, Weber KO: The role of peroxisomes in glycerol ether lipid metabolism. Prog Clin Biol Res 282: 99-116, 1988
    • (1988) Prog Clin Biol Res , vol.282 , pp. 99-116
    • Hajra, A.K.1    Horie, S.2    Weber, K.O.3
  • 190
    • 0018569248 scopus 로고
    • Subcellular localization of acyl coenzyme A: Dihydroxyacetone phosphate acyltransferase in rat liver peroxisomes (microbodies)
    • Hajra AK, Burke CL, Jones CL: Subcellular localization of acyl coenzyme A: dihydroxyacetone phosphate acyltransferase in rat liver peroxisomes (microbodies). J Biol Chem 254: 10896-10900, 1979
    • (1979) J Biol Chem , vol.254 , pp. 10896-10900
    • Hajra, A.K.1    Burke, C.L.2    Jones, C.L.3
  • 191
    • 0023806575 scopus 로고
    • Rat liver dihydroxyacetone-phosphate acyltransferase: Enzyme characteristics and localization studies
    • Hardeman D, Van den Bosch H: Rat liver dihydroxyacetone-phosphate acyltransferase: enzyme characteristics and localization studies. Biochem Biophys Acta 963: 1-9, 1988
    • (1988) Biochem Biophys Acta , vol.963 , pp. 1-9
    • Hardeman, D.1    Van den Bosch, H.2
  • 192
    • 0025967985 scopus 로고
    • Localization of enzymes involved in glycero-ether bond formation in rat liver
    • Hardeman D, Van den Bosch H: Localization of enzymes involved in glycero-ether bond formation in rat liver. Biochim Biophys Acta 1081: 285-292, 1991
    • (1991) Biochim Biophys Acta , vol.1081 , pp. 285-292
    • Hardeman, D.1    Van den Bosch, H.2
  • 193
    • 0025779114 scopus 로고
    • Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells
    • Burdett K, Larkins LK, Das AK, Hajra AK: Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells. J Biol Chem 266: 12201-12206, 1991
    • (1991) J Biol Chem , vol.266 , pp. 12201-12206
    • Burdett, K.1    Larkins, L.K.2    Das, A.K.3    Hajra, A.K.4
  • 194
    • 0022455281 scopus 로고
    • Subcellular distribution and properties of acyl/alkyl dihydroxyacetone phosphate reductase in rodent livers
    • Ghosh MK, Hajra AK: Subcellular distribution and properties of acyl/alkyl dihydroxyacetone phosphate reductase in rodent livers. Arch Biochem Biophys 245: 523-530, 1986
    • (1986) Arch Biochem Biophys , vol.245 , pp. 523-530
    • Ghosh, M.K.1    Hajra, A.K.2
  • 196
    • 0021132819 scopus 로고
    • Deficiency of enzymes catalyzing the biosynthesis of glycerol ether lipids in Zellweger syndrome. A new category of metabolic disease involving the absence of peroxisomes
    • Datta NS, Wilson GN, Hajra AK: Deficiency of enzymes catalyzing the biosynthesis of glycerol ether lipids in Zellweger syndrome. A new category of metabolic disease involving the absence of peroxisomes. N Eng J Med 311: 1080-1083, 1984
    • (1984) N Eng J Med , vol.311 , pp. 1080-1083
    • Datta, N.S.1    Wilson, G.N.2    Hajra, A.K.3
  • 198
    • 0023782245 scopus 로고
    • A possible role for plasmalogens in protecting animal cells against photosensitized killing
    • Zoeller RA, Morand OH, Raetz CR: A possible role for plasmalogens in protecting animal cells against photosensitized killing. J Biol Chem 263: 11590-11596, 1988
    • (1988) J Biol Chem , vol.263 , pp. 11590-11596
    • Zoeller, R.A.1    Morand, O.H.2    Raetz, C.R.3
  • 199
    • 0026352236 scopus 로고
    • Photosensitized killing of cultured fibroblasts from patients with peroxisomal disorders due to pyrene fatty acid-mediated ultraviolet damage
    • Hoefler G, Paschke E, Hoefler S, Moser AB, Moser HW: Photosensitized killing of cultured fibroblasts from patients with peroxisomal disorders due to pyrene fatty acid-mediated ultraviolet damage. J Clin Invest 88: 1873, 1991
    • (1991) J Clin Invest , vol.88 , pp. 1873
    • Hoefler, G.1    Paschke, E.2    Hoefler, S.3    Moser, A.B.4    Moser, H.W.5
  • 200
    • 0028000278 scopus 로고
    • Reactivity of plasmalogens to singlet oxygen and radicals
    • Morand OH: Reactivity of plasmalogens to singlet oxygen and radicals. Meth Enzymol 234: 603-620, 1994
    • (1994) Meth Enzymol , vol.234 , pp. 603-620
    • Morand, O.H.1
  • 201
    • 0023711006 scopus 로고
    • Disappearance of plasmalogens from membranes of animal cells subjected to photosensitized oxidation
    • Murand Rh, Zoeller RA, Raetz CRH: Disappearance of plasmalogens from membranes of animal cells subjected to photosensitized oxidation. J Biol Chem 263: 11597-11606, 1988
    • (1988) J Biol Chem , vol.263 , pp. 11597-11606
    • Murand, Rh.1    Zoeller, R.A.2    Raetz, C.R.H.3
  • 202
    • 0028003675 scopus 로고
    • Myo- Cardial salvage by 1 -0 hexadecyl-Sn-glycerol: Possible role of peroxisomal dysfunction in ischemia-reperfusion injury
    • Maulik N, Tosaki A, Engelman RM, Cordis GA, Das DK: Myo- cardial salvage by 1 -0 hexadecyl-Sn-glycerol: Possible role of peroxisomal dysfunction in ischemia-reperfusion injury. Cardiovasc Pharm 24: 686-692, 1994
    • (1994) Cardiovasc Pharm , vol.24 , pp. 686-692
    • Maulik, N.1    Tosaki, A.2    Engelman, R.M.3    Cordis, G.A.4    Das, D.K.5
  • 205
    • 0027246192 scopus 로고
    • Biosynthesis of dolichol and cholesterol in rat liver peroxisomes
    • Ericsson J, Appelvist EL, Runquist M, Dallner G: Biosynthesis of dolichol and cholesterol in rat liver peroxisomes. Biochemie 75: 167-173, 1993
    • (1993) Biochemie , vol.75 , pp. 167-173
    • Ericsson, J.1    Appelvist, E.L.2    Runquist, M.3    Dallner, G.4
  • 206
    • 0028216631 scopus 로고
    • Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins
    • Grunler J, Ericsson J, Dallner G: Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins. Biochim Biophys Acta 1212: 259-277, 1994
    • (1994) Biochim Biophys Acta , vol.1212 , pp. 259-277
    • Grunler, J.1    Ericsson, J.2    Dallner, G.3
  • 207
    • 0026932050 scopus 로고
    • The role of peroxisomes in cholesterol metabolism
    • Krisans SK: The role of peroxisomes in cholesterol metabolism. Am J Resp Cell Mol Biol 7: 358-364, 1992
    • (1992) Am J Resp Cell Mol Biol , vol.7 , pp. 358-364
    • Krisans, S.K.1
  • 208
    • 0023794005 scopus 로고
    • Nonspecific lipid transfer protein (sterol carrier protein-2) is located in rat liver peroxisomes
    • Tsuneoka M, Yamamoto A, Fujiki Y, Tashiro Y: Nonspecific lipid transfer protein (sterol carrier protein-2) is located in rat liver peroxisomes. J Biochem 104: 560-564, 1988
    • (1988) J Biochem , vol.104 , pp. 560-564
    • Tsuneoka, M.1    Yamamoto, A.2    Fujiki, Y.3    Tashiro, Y.4
  • 209
    • 0021961770 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells
    • Keller GA, Barton MC, Shapiro DJ, Singer SJ: 3-Hydroxy-3-methylglutaryl-coenzyme A reductase is present in peroxisomes in normal rat liver cells. Proc Natl Acad Sci 82: 770-774, 1985
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 770-774
    • Keller, G.A.1    Barton, M.C.2    Shapiro, D.J.3    Singer, S.J.4
  • 210
    • 0025233867 scopus 로고
    • Rat liver peroxisomes catalyze the initial step in cholesterol synthesis. the condensation of acetyl-CoA units into acetoacetyl-CoA
    • Thompson SL, Krisans SK: Rat liver peroxisomes catalyze the initial step in cholesterol synthesis. The condensation of acetyl-CoA units into acetoacetyl-CoA. J Biol Chem 265: 5731-5735, 1990
    • (1990) J Biol Chem , vol.265 , pp. 5731-5735
    • Thompson, S.L.1    Krisans, S.K.2
  • 211
    • 0023624475 scopus 로고
    • Cholesterol synthesis in rat liver peroxisomes. Conversion of mevalonic acid to cholesterol
    • Thompson SL, Burrows R, Laub RJ, Krisans SK: Cholesterol synthesis in rat liver peroxisomes. Conversion of mevalonic acid to cholesterol. J Biol Chem 262: 17420-17425, 1987
    • (1987) J Biol Chem , vol.262 , pp. 17420-17425
    • Thompson, S.L.1    Burrows, R.2    Laub, R.J.3    Krisans, S.K.4
  • 212
    • 0025866944 scopus 로고
    • Involvement of sterol carrier protein-2 in dolichol biosynthesis
    • Ericsson J, Scallen TJ, Chojnacki T, Dallner G: Involvement of sterol carrier protein-2 in dolichol biosynthesis. J Biol Chem 266: 10602-10607, 1991
    • (1991) J Biol Chem , vol.266 , pp. 10602-10607
    • Ericsson, J.1    Scallen, T.J.2    Chojnacki, T.3    Dallner, G.4
  • 213
    • 0028124563 scopus 로고
    • Modulation of hepatic branch-point enzymes involved in isoprenoid biosynthesis upon dietary and drug treatment of rats
    • Andersson M, Ericsson J, Appelkvist E-L, Scheldin S, Chojnaki T, Dallner G: Modulation of hepatic branch-point enzymes involved in isoprenoid biosynthesis upon dietary and drug treatment of rats. Biochim Biophys Acta 1214: 79-87, 1994
    • (1994) Biochim Biophys Acta , vol.1214 , pp. 79-87
    • Andersson, M.1    Ericsson, J.2    Appelkvist, E.-L.3    Scheldin, S.4    Chojnaki, T.5    Dallner, G.6
  • 214
    • 0028961536 scopus 로고
    • Estimation of dolichol and cholesterol synthesis in microsomes and peroxisomes isolated from rat liver
    • Gruler J, Olsson JM, Dallner G: Estimation of dolichol and cholesterol synthesis in microsomes and peroxisomes isolated from rat liver. FEBS Letts 358: 230-232, 1995
    • (1995) FEBS Letts , vol.358 , pp. 230-232
    • Gruler, J.1    Olsson, J.M.2    Dallner, G.3
  • 216
    • 0019781933 scopus 로고
    • Accumulation and metabolism of pipecolic acid in the brain and other organs of the mouse
    • Nishio H, Ortiz J, Giacobini E: Accumulation and metabolism of pipecolic acid in the brain and other organs of the mouse. Neurochem Res 6: 1241-1252, 1981
    • (1981) Neurochem Res , vol.6 , pp. 1241-1252
    • Nishio, H.1    Ortiz, J.2    Giacobini, E.3
  • 217
    • 0016590970 scopus 로고
    • Hyperpipecolic acidemia associated with hepatomegaly, mental retardation, optic nerve dysplasia and progressive neurological disease
    • Thomas GH, Harlam RHA, Batashaw ML, Capute AJ, Neidengard L, Ransom JL: Hyperpipecolic acidemia associated with hepatomegaly, mental retardation, optic nerve dysplasia and progressive neurological disease. Clin Genetics 8: 376-382, 1975
    • (1975) Clin Genetics , vol.8 , pp. 376-382
    • Thomas, G.H.1    Harlam, R.H.A.2    Batashaw, M.L.3    Capute, A.J.4    Neidengard, L.5    Ransom, J.L.6
  • 218
    • 0018902143 scopus 로고
    • Electrophoretic study of pipecolic acid, a biogenic imino acid, in the mammalian brain
    • Kase Y, Takahama K, Hashimoto T, Kaisaku J, Okano J, Miyata T: Electrophoretic study of pipecolic acid, a biogenic imino acid, in the mammalian brain. Brain Res 193: 608-613, 1980
    • (1980) Brain Res , vol.193 , pp. 608-613
    • Kase, Y.1    Takahama, K.2    Hashimoto, T.3    Kaisaku, J.4    Okano, J.5    Miyata, T.6
  • 219
    • 0024501676 scopus 로고
    • L-pipecolic acid oxidation in the rabbit and cynomolgus monkey. Evidence for differing organellar locations and cofactor requirements in each species
    • Mihalic SJ, Rhead WJ: L-pipecolic acid oxidation in the rabbit and cynomolgus monkey. Evidence for differing organellar locations and cofactor requirements in each species. J Biol Chem 264: 2509-2517, 1989
    • (1989) J Biol Chem , vol.264 , pp. 2509-2517
    • Mihalic, S.J.1    Rhead, W.J.2
  • 220
  • 221
    • 0026099826 scopus 로고
    • Postnatal development and isolation of peroxisomes from brain
    • Lazo O, Singh AK, Singh I: Postnatal development and isolation of peroxisomes from brain. J Neurochem 56: 1343-1353, 1991
    • (1991) J Neurochem , vol.56 , pp. 1343-1353
    • Lazo, O.1    Singh, A.K.2    Singh, I.3
  • 223
    • 0019780183 scopus 로고
    • Hyperpipecolic acidemia: Clinical and biochemical observations in two male siblings
    • Burton BK, Reed SP, Remy WT: Hyperpipecolic acidemia: Clinical and biochemical observations in two male siblings. J Pediatr 99: 729-734, 1987
    • (1987) J Pediatr , vol.99 , pp. 729-734
    • Burton, B.K.1    Reed, S.P.2    Remy, W.T.3
  • 225
    • 0017804429 scopus 로고
    • Characteristics of hepatic alamine: Glyoxylate aminotransferase in different mammalian species
    • Noguchi T, Okunu S, Takada Y, Minatogawa Y, Okai K, Kido R: Characteristics of hepatic alamine: Glyoxylate aminotransferase in different mammalian species. Biochem J 169: 113-122, 1978
    • (1978) Biochem J , vol.169 , pp. 113-122
    • Noguchi, T.1    Okunu, S.2    Takada, Y.3    Minatogawa, Y.4    Okai, K.5    Kido, R.6
  • 226
    • 0023928620 scopus 로고
    • Identification of mammalian aminotransferase utilizing glyoxylate or pyruvate as amino receptor
    • Noguchi T, Fujiwara S: Identification of mammalian aminotransferase utilizing glyoxylate or pyruvate as amino receptor. J Biol Chem 263: 182-186, 1988
    • (1988) J Biol Chem , vol.263 , pp. 182-186
    • Noguchi, T.1    Fujiwara, S.2
  • 227
    • 0002316115 scopus 로고
    • Amino acid metabolism in animal peroxisomes
    • HD Fahimi, H Sies (eds). Springer-Verlag, Berlin, Heidelberg
    • Naguchi T: Amino acid metabolism in animal peroxisomes. In: HD Fahimi, H Sies (eds). Peroxisomes in Biology and Medicine. Springer-Verlag, Berlin, Heidelberg, 1987, 234-243
    • (1987) Peroxisomes in Biology and Medicine , pp. 234-243
    • Naguchi, T.1
  • 228
    • 0000216004 scopus 로고
    • Primary Hyperoxaluria
    • JB Stanbury, JB Wyngaarden, D Frederickson, JL Goldstein, MS Brown (eds). McGraw-Hill, New York
    • Williams HE, Smith LH: Primary Hyperoxaluria. In: JB Stanbury, JB Wyngaarden, D Frederickson, JL Goldstein, MS Brown (eds). Molecular Basis of Inherited Diseases. McGraw-Hill, New York, 1983, 204-208
    • (1983) Molecular Basis of Inherited Diseases , pp. 204-208
    • Williams, H.E.1    Smith, L.H.2
  • 229
    • 0018715602 scopus 로고
    • Peroxisomal localization of alanine-glyoxylate aminotransferase in human liver
    • Naguchi T, Takada Y: Peroxisomal localization of alanine-glyoxylate aminotransferase in human liver. Arch Biochem Biophys 196: 645-647, 1979
    • (1979) Arch Biochem Biophys , vol.196 , pp. 645-647
    • Naguchi, T.1    Takada, Y.2
  • 230
    • 0022516472 scopus 로고
    • Peroxisomal alanine: Glyoxylate aminotransferase deficiency in primary hyperoxaluria type I
    • Danpure CJ, Jennings PR: Peroxisomal alanine: glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. FEBS Lett 201: 20-24, 1986
    • (1986) FEBS Lett , vol.201 , pp. 20-24
    • Danpure, C.J.1    Jennings, P.R.2
  • 231
    • 0026724618 scopus 로고
    • Molecular evolution of alanine/glyoxylate aminotransferase intracellular targeting analysis of the marmoset and rabbit genes
    • Purdue PE, Lund MJ and Danpure CJ: Molecular evolution of alanine/glyoxylate aminotransferase intracellular targeting analysis of the marmoset and rabbit genes. Eur J Biochem 207: 757-766, 1992
    • (1992) Eur J Biochem , vol.207 , pp. 757-766
    • Purdue, P.E.1    Lund, M.J.2    Danpure, C.J.3
  • 232
    • 0027246197 scopus 로고
    • Primary hyperoxaluria type 1 and peroxisome-to-mitochondria mistargeting of alanine: Glyoxylate aminotransferase
    • Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondria mistargeting of alanine: glyoxylate aminotransferase. Biochemie 75: 309-315, 1993
    • (1993) Biochemie , vol.75 , pp. 309-315
    • Danpure, C.J.1
  • 233
    • 0025320713 scopus 로고
    • Generation from a single gene of two mRNAs that encode the mitochondrial and peroxisomal serine: Pyruvate aminotransferase of rat liver
    • Oda T, Funai T, Ichiyama A: Generation from a single gene of two mRNAs that encode the mitochondrial and peroxisomal serine: Pyruvate aminotransferase of rat liver. J Biol Chem 265: 7513-7519, 1990
    • (1990) J Biol Chem , vol.265 , pp. 7513-7519
    • Oda, T.1    Funai, T.2    Ichiyama, A.3
  • 234
    • 0024535978 scopus 로고
    • An enzyme trafficking defect in two patients with primary hyperoxaluria Type 1: Peroxisomal alanine/glyoxylate amino transferase rerouted to mitochondria
    • Danpure CJ, Cooper PJ, Wise PJ, Jennings PR: An enzyme trafficking defect in two patients with primary hyperoxaluria Type 1: Peroxisomal alanine/glyoxylate amino transferase rerouted to mitochondria. J Cell Biol 108: 1345-1352, 1989
    • (1989) J Cell Biol , vol.108 , pp. 1345-1352
    • Danpure, C.J.1    Cooper, P.J.2    Wise, P.J.3    Jennings, P.R.4
  • 235
    • 0025640818 scopus 로고
    • Identification of mutations associated with peroxisome to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria
    • Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria. J Cell Biol 111: 2341-2351, 1990
    • (1990) J Cell Biol , vol.111 , pp. 2341-2351
    • Purdue, P.E.1    Takada, Y.2    Danpure, C.J.3
  • 236
    • 0008173537 scopus 로고
    • Measurement of oxidative stress in vivo
    • KJA Davies and W Fulvio (eds). Cleup University Press, Italy
    • Floyd, RA: Measurement of oxidative stress in vivo. In: KJA Davies and W Fulvio (eds). The Oxygen Paradox. Cleup University Press, Italy, 1995, pp 89-104
    • (1995) The Oxygen Paradox , pp. 89-104
    • Floyd, R.A.1
  • 237
    • 0028117114 scopus 로고
    • The glumerulosclerosis gene MPV17 encodes a peroxisomal protein producing reactive oxygen species
    • Zwacka RM, Reuier A, Plaff E, Moll J, Gorges K, Karasawa M, Weiher H: The glumerulosclerosis gene MPV17 encodes a peroxisomal protein producing reactive oxygen species. EMBO J 13: 5129-5134, 1994
    • (1994) EMBO J , vol.13 , pp. 5129-5134
    • Zwacka, R.M.1    Reuier, A.2    Plaff, E.3    Moll, J.4    Gorges, K.5    Karasawa, M.6    Weiher, H.7
  • 239
    • 0024004290 scopus 로고
    • Demonstration of cytochrome reductases in rat liver peroxisomes: Biochemical and immunochemical analysis
    • Gutierrez C, Okita R, Krisans S: Demonstration of cytochrome reductases in rat liver peroxisomes: Biochemical and immunochemical analysis. J Lipid Res 29: 613-628, 1988
    • (1988) J Lipid Res , vol.29 , pp. 613-628
    • Gutierrez, C.1    Okita, R.2    Krisans, S.3
  • 240
    • 0029561281 scopus 로고
    • Ketoconazole and other imidazole derivatives as potent inhibitors of peroxisomal phytanic acid alpha oxidation
    • Pahan K, Khan M, Smith B, Singh I: Ketoconazole and other imidazole derivatives as potent inhibitors of peroxisomal phytanic acid alpha oxidation. FEBS Letts 377: 213-216, 1995
    • (1995) FEBS Letts , vol.377 , pp. 213-216
    • Pahan, K.1    Khan, M.2    Smith, B.3    Singh, I.4
  • 241
    • 0025915727 scopus 로고
    • Cu-Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells
    • Keller G, Warner TG, Steimer KS, Halewell RA: Cu-Zn superoxide dismutase is a peroxisomal enzyme in human fibroblasts and hepatoma cells. Proc Natl Acad Sci (USA) 88: 7381-7385, 1991
    • (1991) Proc Natl Acad Sci (USA) , vol.88 , pp. 7381-7385
    • Keller, G.1    Warner, T.G.2    Steimer, K.S.3    Halewell, R.A.4
  • 242
    • 0026502540 scopus 로고
    • Identification of superoxide dismutase in rat liver peroxisomes
    • Wanders RJA, Denis S: Identification of superoxide dismutase in rat liver peroxisomes. Biochim Biophys Acta 1115: 259-262, 1992
    • (1992) Biochim Biophys Acta , vol.1115 , pp. 259-262
    • Wanders, R.J.A.1    Denis, S.2
  • 243
    • 0026733451 scopus 로고
    • Demonstration of CuZn superoxide dismutase in rat liver peroxisomes: Biochemical and immunochemical evidence
    • Dhaunsi GS, Gulati S, Singh AK, Orak JK, Asayama K, Singh I: Demonstration of CuZn superoxide dismutase in rat liver peroxisomes: Biochemical and immunochemical evidence. J Biol Chem 267: 870-6873, 1992
    • (1992) J Biol Chem , vol.267 , pp. 870-6873
    • Dhaunsi, G.S.1    Gulati, S.2    Singh, A.K.3    Orak, J.K.4    Asayama, K.5    Singh, I.6
  • 244
  • 245
    • 0028308669 scopus 로고
    • CuZn superoxide dismutase: Intraorganellar distribution in peroxisomes
    • Singh I, Dhaunsi GS, Orak JK, Singh AK: CuZn superoxide dismutase: Intraorganellar distribution in peroxisomes. Annals New York Acad Sci 723: 406-408, 1994
    • (1994) Annals New York Acad Sci , vol.723 , pp. 406-408
    • Singh, I.1    Dhaunsi, G.S.2    Orak, J.K.3    Singh, A.K.4
  • 247
    • 0028130643 scopus 로고
    • Demonstration of glutathione peroxidase in rat liver peroxisomes and its intraorganellar distribution
    • Singh AK, Dhaunsi GS, Asayama K, Orak JK, Singh I: Demonstration of glutathione peroxidase in rat liver peroxisomes and its intraorganellar distribution. Arch Biochem Biophys 315: 331-338, 1994
    • (1994) Arch Biochem Biophys , vol.315 , pp. 331-338
    • Singh, A.K.1    Dhaunsi, G.S.2    Asayama, K.3    Orak, J.K.4    Singh, I.5
  • 248
    • 0025779746 scopus 로고
    • Studies on the intracellular distributions of soluble epoxide hydrolase and of catalase by digitonin-permealization of hepatocytes isolated from control and ciprofibrate treated mice
    • Messing Eriksson A, Zeltergvist MA, Lundgren P, Andersson K, Beije B, DePierre JW: Studies on the intracellular distributions of soluble epoxide hydrolase and of catalase by digitonin-permealization of hepatocytes isolated from control and ciprofibrate treated mice. Eur J Biochem 198: 471-476, 1991
    • (1991) Eur J Biochem , vol.198 , pp. 471-476
    • Messing Eriksson, A.1    Zeltergvist, M.A.2    Lundgren, P.3    Andersson, K.4    Beije, B.5    Depierre, J.W.6
  • 249
    • 0030061496 scopus 로고    scopus 로고
    • Epoxide hydrolase in human and rat peroxisomes: Implications to disorders of peroxisomal biogenesis
    • Pahan K, Smith B, Singh I: Epoxide hydrolase in human and rat peroxisomes: Implications to disorders of peroxisomal biogenesis. J Lipid Res 37: 159-167, 1996
    • (1996) J Lipid Res , vol.37 , pp. 159-167
    • Pahan, K.1    Smith, B.2    Singh, I.3
  • 250
    • 0025760294 scopus 로고
    • Pharmacological approach to tissue injury mediated by free radicals and other reactive oxygen metabolites
    • Reilly PM, Schiller HJ and Buckley JB: Pharmacological approach to tissue injury mediated by free radicals and other reactive oxygen metabolites. Am J Surg 161: 488-503, 1991
    • (1991) Am J Surg , vol.161 , pp. 488-503
    • Reilly, P.M.1    And, S.H.J.2    Buckley, J.B.3
  • 252
    • 0027451869 scopus 로고
    • Alterations of peroxisomal functions in ischemia-reperfusion injury of rat kidney
    • Gulati S, Ainol L, Orak JK, Singh AK, Singh I: Alterations of peroxisomal functions in ischemia-reperfusion injury of rat kidney. Biochim Biophys Acta 1182: 291-298, 1993
    • (1993) Biochim Biophys Acta , vol.1182 , pp. 291-298
    • Gulati, S.1    Ainol, L.2    Orak, J.K.3    Singh, A.K.4    Singh, I.5
  • 253
    • 0029180718 scopus 로고
    • Effect of hypoxia-reoxygenation on peroxisomal functions in cultured human skin fibroblasts from control and Zellweger Syndrome patients
    • Kremser K, Kremser-Jezik M, Singh I: Effect of hypoxia-reoxygenation on peroxisomal functions in cultured human skin fibroblasts from control and Zellweger Syndrome patients. Free Rad Res 22: 39-46, 1994
    • (1994) Free Rad Res , vol.22 , pp. 39-46
    • Kremser, K.1    Kremser-Jezik, M.2    Singh, I.3
  • 254
    • 0028136569 scopus 로고
    • Down-regulation of P4501A1 and P4501A2 rnRNA expression in isolated hepatocytes by oxidative stress
    • Baker CW, Fagan JB, Pasco DS: Down-regulation of P4501A1 and P4501A2 rnRNA expression in isolated hepatocytes by oxidative stress. J Biol Chem 269: 3985-3990, 1994
    • (1994) J Biol Chem , vol.269 , pp. 3985-3990
    • Baker, C.W.1    Fagan, J.B.2    Pasco, D.S.3
  • 256
    • 0021906855 scopus 로고
    • Ultrastructural and cytochemical demonstration of peroxisomes in cultured fibroblasts from patients with peroxisomal deficiency disorders
    • Arias JA, Moser AB, Goldfischer S: Ultrastructural and cytochemical demonstration of peroxisomes in cultured fibroblasts from patients with peroxisomal deficiency disorders. J Cell Biol 100: 1789-1792, 1985
    • (1985) J Cell Biol , vol.100 , pp. 1789-1792
    • Arias, J.A.1    Moser, A.B.2    Goldfischer, S.3
  • 259
    • 0024397520 scopus 로고
    • Genetic and phenotypic heterogeneity in disorders of peroxisome biogenesis-a complementation study involving cell lines from 19 patients
    • Roscher AA, Hoefler S, Hoefler G, Pasekke E, Paltauf F, Moser AE, Moser HW: Genetic and phenotypic heterogeneity in disorders of peroxisome biogenesis-a complementation study involving cell lines from 19 patients. Pediatr Res 26: 67-72, 1989
    • (1989) Pediatr Res , vol.26 , pp. 67-72
    • Roscher, A.A.1    Hoefler, S.2    Hoefler, G.3    Pasekke, E.4    Paltauf, F.5    Moser, A.E.6    Moser, H.W.7
  • 260
    • 0023809656 scopus 로고
    • Peroxisomal integral membrane proteins in control and Zellweger fibroblasts
    • Santos MJ, Imanaka T, Shio H, Lazarow PB: Peroxisomal integral membrane proteins in control and Zellweger fibroblasts. J Biol Chem 263: 10502-10509, 1988
    • (1988) J Biol Chem , vol.263 , pp. 10502-10509
    • Santos, M.J.1    Imanaka, T.2    Shio, H.3    Lazarow, P.B.4
  • 262
    • 0021265709 scopus 로고
    • The cerebro-hepato-renal (Zellweger) syndrome. Increased levels and impaired degradation of very long chain fatty acids and their use in prenatal diagnosis
    • Moser AE, Singh I, Brown FR, Solish G, Kelley RI, Benke P, Moser HW: The cerebro-hepato-renal (Zellweger) syndrome. Increased levels and impaired degradation of very long chain fatty acids and their use in prenatal diagnosis. New Eng J Med 310: 1141-1146, 1984
    • (1984) New Eng J Med , vol.310 , pp. 1141-1146
    • Moser, A.E.1    Singh, I.2    Brown, F.R.3    Solish, G.4    Kelley, R.I.5    Benke, P.6    Moser, H.W.7
  • 263
    • 0020574070 scopus 로고
    • Severe plasmalogen deficiency in tissues or infants without peroxisomes (Zellweger syndrome)
    • Heymans HSA, Schutgens RBH, Tan R, Van den Bosch H, Borst P: Severe plasmalogen deficiency in tissues or infants without peroxisomes (Zellweger syndrome). Nature 308: 69-70, 1983
    • (1983) Nature , vol.308 , pp. 69-70
    • Heymans, H.S.A.1    Schutgens, R.B.H.2    Tan, R.3    Van den Bosch, H.4    Borst, P.5
  • 266
    • 0005782267 scopus 로고
    • Biosynthesis and maturation of peroxisomal beta-oxidation enzymes in fibroblasts in relation to the Zellweger syndrome and infantile Refsum disease
    • Schram A, Strijland A, Hashimoto T, Wanders RJA, Schutgens RBH, Van den Bosch, Tager JM: Biosynthesis and maturation of peroxisomal beta-oxidation enzymes in fibroblasts in relation to the Zellweger syndrome and infantile Refsum disease. Proc Natl Acad Sci (USA) 83: 6156-6158, 1986
    • (1986) Proc Natl Acad Sci (USA) , vol.83 , pp. 6156-6158
    • Schram, A.1    Strijland, A.2    Hashimoto, T.3    Wanders, R.J.A.4    Schutgens, R.B.H.5    Van den Bosch6    Tager, J.M.7
  • 267
    • 0026849933 scopus 로고
    • Mutations in the 70 K peroxisomal membrane protein in Zellweger Syndrome
    • Gartner J, Moser H, Valle D: Mutations in the 70 K peroxisomal membrane protein in Zellweger Syndrome. Nature Genetics 1: 16-23, 1992
    • (1992) Nature Genetics , vol.1 , pp. 16-23
    • Gartner, J.1    Moser, H.2    Valle, D.3
  • 268
    • 0026523576 scopus 로고
    • A human gene responsible for Zellweger syndrome that affects peroxisome assembly
    • Shimozawa N, Tsukamoto T, Suzuki Y et al.: A human gene responsible for Zellweger syndrome that affects peroxisome assembly. Science 255: 1132-1134, 1992
    • (1992) Science , vol.255 , pp. 1132-1134
    • Shimozawa, N.1    Tsukamoto, T.2    Suzuki, Y.3
  • 269
    • 0001574585 scopus 로고
    • Adrenoleukodystrophy (X-linked)
    • CR Scriver, AL Beaudet, WS Sly and D Valle (eds). Wiley Liss, New York
    • Moser HW, Moser AB: Adrenoleukodystrophy (X-linked). In: CR Scriver, AL Beaudet, WS Sly and D Valle (eds). The Molecular Basis of Inherited Diseases. 7th Ed. Wiley Liss, New York, 1991, pp 177-191
    • (1991) The Molecular Basis of Inherited Diseases. 7th Ed. , pp. 177-191
    • Moser, H.W.1    Moser, A.B.2
  • 270
    • 8044239562 scopus 로고
    • H Harris and K Hirschhorn (eds). Plenum Press, New York
    • Moser, HW: Advances in Human Genetics, Volume 21, H Harris and K Hirschhorn (eds). Plenum Press, New York, 1993
    • (1993) Advances in Human Genetics , vol.21
    • Moser, H.W.1
  • 273
    • 0019789966 scopus 로고
    • Adrenoleukodystrophy: Impaired oxidation of long chain fatty acids in cultured skin fibroblasts an adrenal cortex
    • Singh I, Moser HW, Moser AE, Kishimoto Y: Adrenoleukodystrophy: Impaired oxidation of long chain fatty acids in cultured skin fibroblasts an adrenal cortex. Biochem Biophys Res Commun 102: 1223-1229, 1981
    • (1981) Biochem Biophys Res Commun , vol.102 , pp. 1223-1229
    • Singh, I.1    Moser, H.W.2    Moser, A.E.3    Kishimoto, Y.4
  • 274
    • 0021333393 scopus 로고
    • Adrenoleukodystrophy: Impaired oxidation of very long chain fatty acids in white blood cells, cultured skin fibroblasts, and amniocytes
    • Singh I, Moser HW, Moser AE, Kishimoto Y: Adrenoleukodystrophy: Impaired oxidation of very long chain fatty acids in white blood cells, cultured skin fibroblasts, and amniocytes. Pediatr Res 18: 286-289, 1984
    • (1984) Pediatr Res , vol.18 , pp. 286-289
    • Singh, I.1    Moser, H.W.2    Moser, A.E.3    Kishimoto, Y.4
  • 275
    • 0022551325 scopus 로고
    • Lignoceroyl-CoASH ligase: Enzyme defect in fatty acid beta-oxidation system in X-linked childhood adrenoleukodystrophy
    • Hashmi M, Stanley W, Singh I: Lignoceroyl-CoASH ligase: enzyme defect in fatty acid beta-oxidation system in X-linked childhood adrenoleukodystrophy. FEBS Letts 196: 247-250, 1986
    • (1986) FEBS Letts , vol.196 , pp. 247-250
    • Hashmi, M.1    Stanley, W.2    Singh, I.3
  • 276
    • 0001112876 scopus 로고
    • Peroxisomal lignoceroyl-CoA ligase deficiency in childhood adrenoleukodystrophy and adrenomyeloneuropathy
    • Lazo O, Contreras M, Hashmi M, Stanley W, Irazu C, Singh I: Peroxisomal lignoceroyl-CoA ligase deficiency in childhood adrenoleukodystrophy and adrenomyeloneuropathy. Proc Natl Acad Sci 85: 7647-7651, 1988
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 7647-7651
    • Lazo, O.1    Contreras, M.2    Hashmi, M.3    Stanley, W.4    Irazu, C.5    Singh, I.6
  • 277
    • 0023886918 scopus 로고
    • Direct demonstration that the deficient oxidation of very long chain fatty acids in X-linked adrenoleukodystrophy is due to an impaired ability of peroxisomes to activate very long chain fatty acids
    • Wanders RJA, Van Roermunds CWT, Van Wijland MJA, Schutgens RBH, Van den Bosch H, Schram AW, Tager JM: Direct demonstration that the deficient oxidation of very long chain fatty acids in X-linked adrenoleukodystrophy is due to an impaired ability of peroxisomes to activate very long chain fatty acids. Biochem Biophys Res Commun 153: 6618-6624, 1988
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 6618-6624
    • Wanders, R.J.A.1    Van Roermunds, C.W.T.2    Van Wijland, M.J.A.3    Schutgens, R.B.H.4    Van den Bosch, H.5    Schram, A.W.6    Tager, J.M.7
  • 278
    • 0022386792 scopus 로고
    • Metabolism of [17, 18-3H2]hexacosanoic acid and from patients with adrenoleukodystrophy (ALD) and adrenomyeloneuropathy (AMN)
    • Tsuji S, Sano Kawamura T, Ariga T, Miyatake T: Metabolism of [17, 18-3H2]hexacosanoic acid and from patients with adrenoleukodystrophy (ALD) and adrenomyeloneuropathy (AMN). J Neurol Sci 71: 359-367, 1985
    • (1985) J Neurol Sci , vol.71 , pp. 359-367
    • Tsuji, S.1    Sano Kawamura, T.2    Ariga, T.3    Miyatake, T.4
  • 279
    • 0027532282 scopus 로고
    • Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
    • Mosser J, Douar AM, Sarde CO et al.: Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. Nature 361: 726-730, 1993
    • (1993) Nature , vol.361 , pp. 726-730
    • Mosser, J.1    Douar, A.M.2    Sarde, C.O.3
  • 280
    • 0028175513 scopus 로고
    • Protein coded by the X-ALD gene is a peroxisomal integral membrane protein
    • Contreras M, Mosser J, Mandel JL, Aubourg P, Singh I: Protein coded by the X-ALD gene is a peroxisomal integral membrane protein. FEBS Letts 344: 211-215, 1994
    • (1994) FEBS Letts , vol.344 , pp. 211-215
    • Contreras, M.1    Mosser, J.2    Mandel, J.L.3    Aubourg, P.4    Singh, I.5
  • 281
    • 0026621245 scopus 로고
    • ABC transporters: From microorganisms to man
    • Higgins CF: ABC transporters: From microorganisms to man. Annu Rev Cell Biol 8: 67-113, 1992
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 282
    • 0028890665 scopus 로고
    • Spectrum of mutations in the gene encoding the adrenoleukodystrophy protein
    • Ligtenberg MJL, Kemp S, Sarde CO et al.: Spectrum of mutations in the gene encoding the adrenoleukodystrophy protein. Am J Hum Genet 56: 44-50, 1995
    • (1995) Am J Hum Genet , vol.56 , pp. 44-50
    • Ligtenberg, M.J.L.1    Kemp, S.2    Sarde, C.O.3
  • 283
    • 0028930085 scopus 로고
    • Mutations in the gene for X-linked adrenoleukodystrophy in patients with different clinical phenotypes
    • Braum A, Ambach H, Kammerer S et al.: Mutations in the gene for X-linked adrenoleukodystrophy in patients with different clinical phenotypes. Am J Hum Genet 56: 854-861, 1995
    • (1995) Am J Hum Genet , vol.56 , pp. 854-861
    • Braum, A.1    Ambach, H.2    Kammerer, S.3
  • 284
    • 0028566461 scopus 로고
    • X-linked adrenoleukodystrophy (ALD): A novel mutation of the ALD gene in 6 members of a family presenting with 5 different phenotypes
    • Berger J, Molzer B, Fae I, Bernheimer H: X-linked adrenoleukodystrophy (ALD): a novel mutation of the ALD gene in 6 members of a family presenting with 5 different phenotypes. Biochem Biophys Res Commun 205: 1638-1643, 1994
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1638-1643
    • Berger, J.1    Molzer, B.2    Fae, I.3    Bernheimer, H.4
  • 285
    • 0028962332 scopus 로고
    • Retroviral-mediated gene transfer corrects very long chain fatty acid metabolism in adrenoleukodystrophy fibroblasts
    • Cartier N, Lopez J, Moullier P et al.: Retroviral-mediated gene transfer corrects very long chain fatty acid metabolism in adrenoleukodystrophy fibroblasts. Proc Natl Acad Sci (USA) 92: 1674-1678, 1995
    • (1995) Proc Natl Acad Sci (USA) , vol.92 , pp. 1674-1678
    • Cartier, N.1    Lopez, J.2    Moullier, P.3
  • 286
    • 0029087359 scopus 로고
    • Adrenoleukodystrophy: The restoration of peroxisomal β-oxidation by transfection of normal cDNA
    • Shinnoh N, Yamada T, Yoshimura T et al.: Adrenoleukodystrophy: The restoration of peroxisomal β-oxidation by transfection of normal cDNA. Biochim Biophys Res Commun 210: 830-836, 1995
    • (1995) Biochim Biophys Res Commun , vol.210 , pp. 830-836
    • Shinnoh, N.1    Yamada, T.2    Yoshimura, T.3
  • 287
    • 0026770745 scopus 로고
    • Transport of fatty acids into human and rat peroxisomes: Differential transport of palmitic and lignoceric acids and its implication to X-adrenoleukodystrophy
    • Singh I, Lazo O, Dhaunsi GS, Contreras M: Transport of fatty acids into human and rat peroxisomes: Differential transport of palmitic and lignoceric acids and its implication to X-adrenoleukodystrophy. J Biol Chem 267: 13306-13313, 1992
    • (1992) J Biol Chem , vol.267 , pp. 13306-13313
    • Singh, I.1    Lazo, O.2    Dhaunsi, G.S.3    Contreras, M.4
  • 289
    • 0028083220 scopus 로고
    • Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy
    • Fournier B, Saudubray J-M, Benichou B et al.: Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. J Clin Invest 94: 526-531, 1994
    • (1994) J Clin Invest , vol.94 , pp. 526-531
    • Fournier, B.1    Saudubray, J.-M.2    Benichou, B.3
  • 291
    • 0022626531 scopus 로고
    • Pseudo-Zellweger syndrome: Deficiencies in several peroxisomal oxidative activities
    • Goldfischer S, Collins J, Rapin I et al.: Pseudo-Zellweger syndrome: Deficiencies in several peroxisomal oxidative activities. J Pediatr 108: 25-32, 1986
    • (1986) J Pediatr , vol.108 , pp. 25-32
    • Goldfischer, S.1    Collins, J.2    Rapin, I.3
  • 292
    • 0002248566 scopus 로고
    • Heredopathia Atactica Polyneuritoformis
    • Refsum S: Heredopathia Atactica Polyneuritoformis. Acta Psychiatr Scan (Suppl) 38: 9, 1946
    • (1946) Acta Psychiatr Scan (Suppl) , vol.38 , pp. 9
    • Refsum, S.1
  • 293
    • 0014528369 scopus 로고
    • Refsum's Disease: Characterization of the enzyme defect in cell culture
    • Herndon JA Jr, Steinberg D, Uhlendorf W, Fales HM: Refsum's Disease: Characterization of the enzyme defect in cell culture. J Clin Invest 48: 1017-1032, 1969
    • (1969) J Clin Invest , vol.48 , pp. 1017-1032
    • Herndon Jr., J.A.1    Steinberg, D.2    Uhlendorf, W.3    Fales, H.M.4
  • 294
    • 0026528902 scopus 로고
    • Pristanic acid and phytanic acid in plasma from patients with peroxisomal disorders: Stable isotope dilution analysis with electron cature negative ion fragmentation
    • Ten Brink HJ, Stellaard F, Van den Heuvel CMM et al.: Pristanic acid and phytanic acid in plasma from patients with peroxisomal disorders: stable isotope dilution analysis with electron cature negative ion fragmentation. J Lipid Res 33: 41-47, 1992
    • (1992) J Lipid Res , vol.33 , pp. 41-47
    • Ten Brink, H.J.1    Stellaard, F.2    Van den Heuvel, C.M.M.3
  • 295
    • 0027311182 scopus 로고
    • Formic acid is a product of the α-oxidation of fatty acids by human skin fibroblasts: Deficiency of formic acid production in peroxisome-deficient fibroblasts
    • Poulos A, Sharp P, Singh I, Johnson DW, Corey WF, Easton C: Formic acid is a product of the α-oxidation of fatty acids by human skin fibroblasts: Deficiency of formic acid production in peroxisome-deficient fibroblasts. Biochem J 292: 457-461, 1993
    • (1993) Biochem J , vol.292 , pp. 457-461
    • Poulos, A.1    Sharp, P.2    Singh, I.3    Johnson, D.W.4    Corey, W.F.5    Easton, C.6
  • 296
    • 0029898759 scopus 로고    scopus 로고
    • Phytanic acid oxidation: Normal activation and transport yet defective α-hydroxylation of phytanic acid in peroxisomes from Refsum disease and Rhizomelic Chondrodysplasia Punctata
    • Pahan K, Khan M and Singh I: Phytanic acid oxidation: Normal activation and transport yet defective α-hydroxylation of phytanic acid in peroxisomes from Refsum disease and Rhizomelic Chondrodysplasia Punctata. J Lipid Res 37: 1137-1143, 1996
    • (1996) J Lipid Res , vol.37 , pp. 1137-1143
    • Pahan, K.1    Khan, M.2    Singh, I.3
  • 297
    • 0011841322 scopus 로고
    • Acatalasemia
    • CR Scriver, AL Beaudet, WS Sly, D Valle. (eds). McGraw Hill Information Service Co., New York
    • Eaton JW: Acatalasemia. In: CR Scriver, AL Beaudet, WS Sly, D Valle. (eds). The Metabolic Basis of Inherited Disease. McGraw Hill Information Service Co., New York, 2: 1989, pp 1551-1561
    • (1989) The Metabolic Basis of Inherited Disease , vol.2 , pp. 1551-1561
    • Eaton, J.W.1
  • 298
    • 0022599598 scopus 로고
    • Isolation and characterization of the human catalase gene
    • Quan F, Korneluk R, Tropak M et al.: Isolation and characterization of the human catalase gene. Nucleic Acids Res 14: 5321-5345, 1986
    • (1986) Nucleic Acids Res , vol.14 , pp. 5321-5345
    • Quan, F.1    Korneluk, R.2    Tropak, M.3
  • 299
    • 0025794075 scopus 로고
    • Atypical riboflavin-responsive glutaric aciduria, and deficient peroxisomal glutaryl-CoA oxidase activity: A new peroxisomal disorder
    • Bennett MJ, Pollitt RJ, Hale DE, Goodman SI, Hale DE, Vamecq J: Atypical riboflavin-responsive glutaric aciduria, and deficient peroxisomal glutaryl-CoA oxidase activity: a new peroxisomal disorder. J Inher Metab Dis 14: 165-173, 1991
    • (1991) J Inher Metab Dis , vol.14 , pp. 165-173
    • Bennett, M.J.1    Pollitt, R.J.2    Hale, D.E.3    Goodman, S.I.4    Hale, D.E.5    Vamecq, J.6
  • 300
    • 8044227144 scopus 로고
    • Flourometric assay for peroxisomal diseases
    • Vamecq J: Flourometric assay for peroxisomal diseases. Analyt Biochem 186: 163-180, 1990
    • (1990) Analyt Biochem , vol.186 , pp. 163-180
    • Vamecq, J.1
  • 301
    • 0025169032 scopus 로고
    • A new peroxisomal disorder: Di and trihydroxycholestanemia due to a presumed trihydroxyxholestanoyl-CoA oxidase deficiency
    • Christenden E, Van Eldere J and Brandt NJ et al.: A new peroxisomal disorder: di and trihydroxycholestanemia due to a presumed trihydroxyxholestanoyl-CoA oxidase deficiency. J Inher Metab Dis 13: 363-366, 1990
    • (1990) J Inher Metab Dis , vol.13 , pp. 363-366
    • Christenden, E.1    Van Eldere, J.2    Brandt, N.J.3
  • 303
  • 304
    • 0026700936 scopus 로고
    • Zellweger-like phenotype in two siblings: A defect in peroxisomal beta-oxidation with elevated very long chain fatty acids but normal bile acids
    • Mandel H, Berant M, Aizin A et al.: Zellweger-like phenotype in two siblings: A defect in peroxisomal beta-oxidation with elevated very long chain fatty acids but normal bile acids. J Inher Metab Dis 15: 381-384, 1992
    • (1992) J Inher Metab Dis , vol.15 , pp. 381-384
    • Mandel, H.1    Berant, M.2    Aizin, A.3
  • 305
    • 0023902953 scopus 로고
    • Molecular analysis of peroxisomal beta-oxidation enzymes in infants with Zellweger syndrome and Zellweger-like syndrome: Further heterogeneity of the peroxisomal disorder
    • Suzuki Y, Shimozawa N, Orii T, Igarashi N, Kono N, Hashimoto T: Molecular analysis of peroxisomal beta-oxidation enzymes in infants with Zellweger syndrome and Zellweger-like syndrome: further heterogeneity of the peroxisomal disorder. Clin Chimica Acta 172: 65-76, 1988
    • (1988) Clin Chimica Acta , vol.172 , pp. 65-76
    • Suzuki, Y.1    Shimozawa, N.2    Orii, T.3    Igarashi, N.4    Kono, N.5    Hashimoto, T.6
  • 306
    • 0027234217 scopus 로고
    • Pseudo infantile Refsum Disease: Catalase deficient peroxisomes with partial deficiency of plasmalogen system and oxidation of fatty acids
    • Aubourg P, Kremser K, Roland MO, Hadchonel M, Singh I: Pseudo infantile Refsum Disease: Catalase deficient peroxisomes with partial deficiency of plasmalogen system and oxidation of fatty acids. Pediatr Res 34: 270-276, 1993
    • (1993) Pediatr Res , vol.34 , pp. 270-276
    • Aubourg, P.1    Kremser, K.2    Roland, M.O.3    Hadchonel, M.4    Singh, I.5
  • 308
    • 8044223332 scopus 로고
    • Normal bile acids in patient with Zellweger-like clinical and biochemical features: A new peroxisomal disease
    • Singh I, Voight R, Natowicz M, Brown FR: Normal bile acids in patient with Zellweger-like clinical and biochemical features: A new peroxisomal disease. Pediatr Res 37: 901A, 1995
    • (1995) Pediatr Res , vol.37
    • Singh, I.1    Voight, R.2    Natowicz, M.3    Brown, F.R.4


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