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Volumn 1863, Issue 5, 2016, Pages 922-933

Human disorders of peroxisome metabolism and biogenesis

Author keywords

Biogenesis; Enzyme deficiencies; Metabolism; Peroxisomes; PEX genes; Zellweger spectrum disorders

Indexed keywords

BILE ACID; DOCOSAHEXAENOIC ACID; ENZYME; ETHER PHOSPHOLIPID; FATTY ACID; G PROTEIN COUPLED RECEPTOR 40; GLYOXYLIC ACID; ISOPROTEIN; MEMBRANE PROTEIN; PEX1 PROTEIN, HUMAN; PLASMALOGEN; SIGNAL PEPTIDE;

EID: 84961122547     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.11.015     Document Type: Article
Times cited : (275)

References (174)
  • 1
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mamalian peroxisomes revisited
    • Wanders R.J.A., Waterham H.R. Biochemistry of mamalian peroxisomes revisited. Annu. Rev. Biochem. 2006, 75:295-332.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 2
    • 0032948460 scopus 로고    scopus 로고
    • 3-hydroxy-3-methylglutaryl coenzyme A lyase: targeting and processing in peroxisomes and mitochondria
    • Ashmarina L.I., Pshezhetsky A.V., Branda S.S., Isaya G., Mitchell G.A. 3-hydroxy-3-methylglutaryl coenzyme A lyase: targeting and processing in peroxisomes and mitochondria. J. Lipid Res. 1999, 40:70-75.
    • (1999) J. Lipid Res. , vol.40 , pp. 70-75
    • Ashmarina, L.I.1    Pshezhetsky, A.V.2    Branda, S.S.3    Isaya, G.4    Mitchell, G.A.5
  • 3
    • 0029976299 scopus 로고    scopus 로고
    • Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria
    • Ashmarina L.I., Robert M.F., Elsliger M.A., Mitchell G.A. Characterization of the hydroxymethylglutaryl-CoA lyase precursor, a protein targeted to peroxisomes and mitochondria. Biochem. J. 1996, 315(Pt 1):71-75.
    • (1996) Biochem. J. , vol.315 , pp. 71-75
    • Ashmarina, L.I.1    Robert, M.F.2    Elsliger, M.A.3    Mitchell, G.A.4
  • 5
    • 0033747547 scopus 로고
    • Subcellular localization and physiological role of alpha-methylacyl-CoA racemase
    • L I.J.
    • Ferdinandusse S., Denis S., L I.J., Dacremont G., Waterham H.R., Wanders R.J. subcellular localization and physiological role of alpha-methylacyl-CoA racemase. J. Lipid Res. 1890-1896, 41(2000).
    • (1890) J. Lipid Res. , vol.41 , Issue.2000
    • Ferdinandusse, S.1    Denis, S.2    Dacremont, G.3    Waterham, H.R.4    Wanders, R.J.5
  • 6
  • 7
    • 36148992142 scopus 로고    scopus 로고
    • Defects in mitochondrial and peroxisomal fatty acid oxidation
    • Elsevier, Amsterdam-Tokyo, G. van der Vusse (Ed.)
    • Wanders R.J.A. Defects in mitochondrial and peroxisomal fatty acid oxidation. Lipobiology 2004, 295-317. Elsevier, Amsterdam-Tokyo. G. van der Vusse (Ed.).
    • (2004) Lipobiology , pp. 295-317
    • Wanders, R.J.A.1
  • 9
    • 77956867734 scopus 로고    scopus 로고
    • Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism
    • Van Veldhoven P.P. Biochemistry and genetics of inherited disorders of peroxisomal fatty acid metabolism. J. Lipid Res. 2010, 51:2863-2895.
    • (2010) J. Lipid Res. , vol.51 , pp. 2863-2895
    • Van Veldhoven, P.P.1
  • 11
    • 0037451008 scopus 로고    scopus 로고
    • Phytanic acid alpha-oxidation, new insights into an old problem: a review
    • Wanders R.J.A., Jansen G.A., Lloyd M.D. Phytanic acid alpha-oxidation, new insights into an old problem: a review. Biochim. Biophys. Acta 2003, 1631:119-135.
    • (2003) Biochim. Biophys. Acta , vol.1631 , pp. 119-135
    • Wanders, R.J.A.1    Jansen, G.A.2    Lloyd, M.D.3
  • 13
    • 84864038743 scopus 로고    scopus 로고
    • Primary hyperoxalurias: disorders of glyoxylate detoxification
    • Salido E., Pey A.L., Rodriguez R., Lorenzo V. Primary hyperoxalurias: disorders of glyoxylate detoxification. Biochim. Biophys. Acta 2012, 1822:1453-1464.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1453-1464
    • Salido, E.1    Pey, A.L.2    Rodriguez, R.3    Lorenzo, V.4
  • 14
    • 84864046701 scopus 로고    scopus 로고
    • Functions of plasmalogen lipids in health and disease
    • Braverman N.E., Moser A.B. Functions of plasmalogen lipids in health and disease. Biochim. Biophys. Acta 2012, 1822:1442-1452.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1442-1452
    • Braverman, N.E.1    Moser, A.B.2
  • 15
    • 2942633430 scopus 로고    scopus 로고
    • Functions and biosynthesis of plasmalogens in health and disease
    • Brites P., Waterham H.R., Wanders R.J. Functions and biosynthesis of plasmalogens in health and disease. Biochim. Biophys. Acta 2004, 1636:219-231.
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 219-231
    • Brites, P.1    Waterham, H.R.2    Wanders, R.J.3
  • 17
    • 79959786449 scopus 로고    scopus 로고
    • Disorders of bile acid synthesis
    • Clayton P.T. Disorders of bile acid synthesis. J. Inherit. Metab. Dis. 2011, 34:593-604.
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 593-604
    • Clayton, P.T.1
  • 20
    • 0037790917 scopus 로고    scopus 로고
    • The enzymes, regulation, and genetics of bile acid synthesis
    • Russell D.W. The enzymes, regulation, and genetics of bile acid synthesis. Annu. Rev. Biochem. 2003, 72:137-174.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 137-174
    • Russell, D.W.1
  • 21
    • 0033970416 scopus 로고    scopus 로고
    • Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid alpha- and beta-oxidation systems in humans
    • Wanders R.J.A., van Grunsven E.G., Jansen G.A. Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid alpha- and beta-oxidation systems in humans. Biochem. Soc. Trans. 2000, 28:141-149.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 141-149
    • Wanders, R.J.A.1    van Grunsven, E.G.2    Jansen, G.A.3
  • 22
  • 23
    • 80051473761 scopus 로고    scopus 로고
    • Plasmalogens the neglected regulatory and scavenging lipid species
    • Wallner S., Schmitz G. Plasmalogens the neglected regulatory and scavenging lipid species. Chem. Phys. Lipids 2011, 164:573-589.
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 573-589
    • Wallner, S.1    Schmitz, G.2
  • 24
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: struggling for balance
    • (Oxford, England)
    • Bonekamp N.A., Volkl A., Fahimi H.D., Schrader M. Reactive oxygen species and peroxisomes: struggling for balance. BioFactors 2009, 35:346-355. (Oxford, England).
    • (2009) BioFactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Volkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 25
    • 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 H.D. Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study. Eur. J. Cell. Biol. 1987, 45:137-144.
    • (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
  • 27
    • 0026502540 scopus 로고
    • Identification of superoxide dismutase in rat liver peroxisomes
    • Wanders R.J.A., Denis S. Identification of superoxide dismutase in rat liver peroxisomes. Biochim. Biophys. Acta 1992, 1115:259-262.
    • (1992) Biochim. Biophys. Acta , vol.1115 , pp. 259-262
    • Wanders, R.J.A.1    Denis, S.2
  • 29
    • 70350650138 scopus 로고    scopus 로고
    • Hitchhiking of Cu/Zn superoxide dismutase to peroxisomes-evidence for a natural piggyback import mechanism in mammals
    • Islinger M., Li K.W., Seitz J., Volkl A., Luers G.H. Hitchhiking of Cu/Zn superoxide dismutase to peroxisomes-evidence for a natural piggyback import mechanism in mammals. Traffic 2009, 10:1711-1721.
    • (2009) Traffic , vol.10 , pp. 1711-1721
    • Islinger, M.1    Li, K.W.2    Seitz, J.3    Volkl, A.4    Luers, G.H.5
  • 35
    • 84864029381 scopus 로고    scopus 로고
    • Genetics and molecular basis of human peroxisome biogenesis disorders
    • Waterham H.R., Ebberink M.S. Genetics and molecular basis of human peroxisome biogenesis disorders. Biochim. Biophys. Acta 2012, 1822:1430-1441.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1430-1441
    • Waterham, H.R.1    Ebberink, M.S.2
  • 38
    • 33845503273 scopus 로고    scopus 로고
    • Growth and division of peroxisomes
    • Schrader M., Fahimi H.D. Growth and division of peroxisomes. Int. Rev. Cytol. 2006, 255:237-290.
    • (2006) Int. Rev. Cytol. , vol.255 , pp. 237-290
    • Schrader, M.1    Fahimi, H.D.2
  • 40
    • 79955505833 scopus 로고    scopus 로고
    • Peroxisome assembly: matrix and membrane protein biogenesis
    • Ma C., Agrawal G., Subramani S. Peroxisome assembly: matrix and membrane protein biogenesis. J. Cell Biol. 2011, 193:7-16.
    • (2011) J. Cell Biol. , vol.193 , pp. 7-16
    • Ma, C.1    Agrawal, G.2    Subramani, S.3
  • 41
    • 84885358006 scopus 로고    scopus 로고
    • Emerging role of the endoplasmic reticulum in peroxisome biogenesis
    • Agrawal G., Subramani S. Emerging role of the endoplasmic reticulum in peroxisome biogenesis. Front. Physiol. 2013, 4:286.
    • (2013) Front. Physiol. , vol.4 , pp. 286
    • Agrawal, G.1    Subramani, S.2
  • 42
    • 33646791462 scopus 로고    scopus 로고
    • The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER
    • Kim P.K., Mullen R.T., Schumann U., Lippincott-Schwartz J. The origin and maintenance of mammalian peroxisomes involves a de novo PEX16-dependent pathway from the ER. J. Cell Biol. 2006, 173:521-532.
    • (2006) J. Cell Biol. , vol.173 , pp. 521-532
    • Kim, P.K.1    Mullen, R.T.2    Schumann, U.3    Lippincott-Schwartz, J.4
  • 43
    • 0345861756 scopus 로고    scopus 로고
    • PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
    • Jones J.M., Morrell J.C., Gould S.J. PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins. J. Cell Biol. 2004, 164:57-67.
    • (2004) J. Cell Biol. , vol.164 , pp. 57-67
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 44
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner H., Kramer A., Lorenzen S., Stein K., Landgraf C., Volkmer-Engert R., Erdmann R. Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 2004, 15:3406-3417.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 45
    • 0035844874 scopus 로고    scopus 로고
    • Multiple distinct targeting signals in integral peroxisomal membrane proteins
    • Jones J.M., Morrell J.C., Gould S.J. Multiple distinct targeting signals in integral peroxisomal membrane proteins. J. Cell Biol. 2001, 153:1141-1150.
    • (2001) J. Cell Biol. , vol.153 , pp. 1141-1150
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 46
    • 1642394134 scopus 로고    scopus 로고
    • PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
    • Fang Y., Morrell J.C., Jones J.M., Gould S.J. PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. J. Cell Biol. 2004, 164:863-875.
    • (2004) J. Cell Biol. , vol.164 , pp. 863-875
    • Fang, Y.1    Morrell, J.C.2    Jones, J.M.3    Gould, S.J.4
  • 47
    • 1642394134 scopus 로고    scopus 로고
    • PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins
    • Fang Y., Morrell J.C., Jones J.M., Gould S.J. PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins. J. Cell Biol. 2004, 164:863-875.
    • (2004) J. Cell Biol. , vol.164 , pp. 863-875
    • Fang, Y.1    Morrell, J.C.2    Jones, J.M.3    Gould, S.J.4
  • 48
    • 0034733909 scopus 로고    scopus 로고
    • Peroxisome biogenesis and peroxisome biogenesis disorders
    • Fujiki Y. Peroxisome biogenesis and peroxisome biogenesis disorders. FEBS Lett. 2000, 476:42-46.
    • (2000) FEBS Lett. , vol.476 , pp. 42-46
    • Fujiki, Y.1
  • 49
    • 33845318535 scopus 로고    scopus 로고
    • Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions
    • Fujiki Y., Matsuzono Y., Matsuzaki T., Fransen M. Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions. Biochim. Biophys. Acta 2006, 1763:1639-1646.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1639-1646
    • Fujiki, Y.1    Matsuzono, Y.2    Matsuzaki, T.3    Fransen, M.4
  • 50
    • 0037113975 scopus 로고    scopus 로고
    • The membrane biogenesis peroxin Pex16p. Topogenesis and functional roles in peroxisomal membrane assembly
    • Honsho M., Hiroshige T., Fujiki Y. The membrane biogenesis peroxin Pex16p. Topogenesis and functional roles in peroxisomal membrane assembly. J. Biol. Chem. 2002, 277:44513-44524.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44513-44524
    • Honsho, M.1    Hiroshige, T.2    Fujiki, Y.3
  • 51
    • 33845335481 scopus 로고    scopus 로고
    • The import receptor Pex7p and the PTS2 targeting sequence
    • Lazarow P.B. The import receptor Pex7p and the PTS2 targeting sequence. Biochim. Biophys. Acta 2006, 1763:1599-1604.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1599-1604
    • Lazarow, P.B.1
  • 52
    • 0026526811 scopus 로고
    • Targeting of proteins into the peroxisomal matrix
    • Subramani S. Targeting of proteins into the peroxisomal matrix. J. Membr. Biol. 1992, 125:99-106.
    • (1992) J. Membr. Biol. , vol.125 , pp. 99-106
    • Subramani, S.1
  • 53
    • 0031854532 scopus 로고    scopus 로고
    • An isoform of pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes
    • Braverman N., Dodt G., Gould S.J., Valle D. An isoform of pex5p, the human PTS1 receptor, is required for the import of PTS2 proteins into peroxisomes. Hum. Mol. Genet. 1998, 7:1195-1205.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1195-1205
    • Braverman, N.1    Dodt, G.2    Gould, S.J.3    Valle, D.4
  • 54
    • 0035834711 scopus 로고    scopus 로고
    • Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p
    • Dodt G., Warren D., Becker E., Rehling P., Gould S.J. Domain mapping of human PEX5 reveals functional and structural similarities to Saccharomyces cerevisiae Pex18p and Pex21p. J. Biol. Chem. 2001, 276:41769-41781.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41769-41781
    • Dodt, G.1    Warren, D.2    Becker, E.3    Rehling, P.4    Gould, S.J.5
  • 55
    • 0035917528 scopus 로고    scopus 로고
    • The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol
    • Dammai V., Subramani S. The human peroxisomal targeting signal receptor, Pex5p, is translocated into the peroxisomal matrix and recycled to the cytosol. Cell 2001, 105:187-196.
    • (2001) Cell , vol.105 , pp. 187-196
    • Dammai, V.1    Subramani, S.2
  • 56
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor
    • Dodt G., Gould S.J. Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p, the PTS1 receptor: evidence that PTS1 protein import is mediated by a cycling receptor. J. Cell Biol. 1996, 135:1763-1774.
    • (1996) J. Cell Biol. , vol.135 , pp. 1763-1774
    • Dodt, G.1    Gould, S.J.2
  • 57
    • 0033571690 scopus 로고    scopus 로고
    • PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import
    • Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J. PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import. J. Cell Biol. 1999, 147:761-774.
    • (1999) J. Cell Biol. , vol.147 , pp. 761-774
    • Chang, C.C.1    Warren, D.S.2    Sacksteder, K.A.3    Gould, S.J.4
  • 63
    • 77953507085 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins insert into the endoplasmic reticulum
    • van der Zand A., Braakman I., Tabak H.F. Peroxisomal membrane proteins insert into the endoplasmic reticulum. Mol. Biol. Cell 2010, 21:2057-2065.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2057-2065
    • van der Zand, A.1    Braakman, I.2    Tabak, H.F.3
  • 64
    • 84878954796 scopus 로고    scopus 로고
    • Peroxisome formation and maintenance are dependent on the endoplasmic reticulum
    • Tabak H.F., Braakman I., van der Zand A. Peroxisome formation and maintenance are dependent on the endoplasmic reticulum. Annu. Rev. Biochem. 2013, 82:723-744.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 723-744
    • Tabak, H.F.1    Braakman, I.2    van der Zand, A.3
  • 67
    • 84885336706 scopus 로고    scopus 로고
    • Peroxisome interactions and cross-talk with other subcellular compartments in animal cells
    • Schrader M., Grille S., Fahimi H.D., Islinger M. Peroxisome interactions and cross-talk with other subcellular compartments in animal cells. Subcell. Biochem. 2013, 69:1-22.
    • (2013) Subcell. Biochem. , vol.69 , pp. 1-22
    • Schrader, M.1    Grille, S.2    Fahimi, H.D.3    Islinger, M.4
  • 69
    • 27144513797 scopus 로고    scopus 로고
    • Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation
    • Thoms S., Erdmann R. Dynamin-related proteins and Pex11 proteins in peroxisome division and proliferation. FEBS J. 2005, 272:5169-5181.
    • (2005) FEBS J. , vol.272 , pp. 5169-5181
    • Thoms, S.1    Erdmann, R.2
  • 70
    • 84867336378 scopus 로고    scopus 로고
    • PEX11 proteins attract Mff and human Fis1 to coordinate peroxisomal fission
    • Koch J., Brocard C. PEX11 proteins attract Mff and human Fis1 to coordinate peroxisomal fission. J. Cell Sci. 2012, 125:3813-3826.
    • (2012) J. Cell Sci. , vol.125 , pp. 3813-3826
    • Koch, J.1    Brocard, C.2
  • 71
    • 77955986557 scopus 로고    scopus 로고
    • PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance
    • Koch J., Pranjic K., Huber A., Ellinger A., Hartig A., Kragler F., Brocard C. PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance. J. Cell Sci. 2010, 123:3389-3400.
    • (2010) J. Cell Sci. , vol.123 , pp. 3389-3400
    • Koch, J.1    Pranjic, K.2    Huber, A.3    Ellinger, A.4    Hartig, A.5    Kragler, F.6    Brocard, C.7
  • 73
    • 0036882106 scopus 로고    scopus 로고
    • PEX11alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation
    • Li X., Baumgart E., Dong G.X., Morrell J.C., Jimenez-Sanchez G., Valle D., Smith K.D., Gould S.J. PEX11alpha is required for peroxisome proliferation in response to 4-phenylbutyrate but is dispensable for peroxisome proliferator-activated receptor alpha-mediated peroxisome proliferation. Mol. Cell. Biol. 2002, 22:8226-8240.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8226-8240
    • Li, X.1    Baumgart, E.2    Dong, G.X.3    Morrell, J.C.4    Jimenez-Sanchez, G.5    Valle, D.6    Smith, K.D.7    Gould, S.J.8
  • 75
    • 0036261777 scopus 로고    scopus 로고
    • PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function
    • Li X., Baumgart E., Morrell J.C., Jimenez-Sanchez G., Valle D., Gould S.J. PEX11 beta deficiency is lethal and impairs neuronal migration but does not abrogate peroxisome function. Mol. Cell. Biol. 2002, 22:4358-4365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4358-4365
    • Li, X.1    Baumgart, E.2    Morrell, J.C.3    Jimenez-Sanchez, G.4    Valle, D.5    Gould, S.J.6
  • 77
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 2004, 5:133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 80
    • 4444236087 scopus 로고    scopus 로고
    • Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1
    • Koch A., Schneider G., Luers G.H., Schrader M. Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1. J. Cell Sci. 2004, 117:3995-4006.
    • (2004) J. Cell Sci. , vol.117 , pp. 3995-4006
    • Koch, A.1    Schneider, G.2    Luers, G.H.3    Schrader, M.4
  • 82
    • 27144557499 scopus 로고    scopus 로고
    • A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells
    • Koch A., Yoon Y., Bonekamp N.A., McNiven M.A., Schrader M. A role for Fis1 in both mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2005, 16:5077-5086.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5077-5086
    • Koch, A.1    Yoon, Y.2    Bonekamp, N.A.3    McNiven, M.A.4    Schrader, M.5
  • 83
    • 84864042465 scopus 로고    scopus 로고
    • X-linked adrenoleukodystrophy: clinical, metabolic, genetic and pathophysiological aspects
    • Kemp S., Berger J., Aubourg P. X-linked adrenoleukodystrophy: clinical, metabolic, genetic and pathophysiological aspects. Biochim. Biophys. Acta 2012, 1822:1465-1474.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1465-1474
    • Kemp, S.1    Berger, J.2    Aubourg, P.3
  • 87
    • 79953326378 scopus 로고    scopus 로고
    • ABC subfamily D proteins and very long chain fatty acid metabolism as novel targets in adrenoleukodystrophy
    • Morita M., Shimozawa N., Kashiwayama Y., Suzuki Y., Imanaka T. ABC subfamily D proteins and very long chain fatty acid metabolism as novel targets in adrenoleukodystrophy. Curr. Drug Targets 2011, 12:694-706.
    • (2011) Curr. Drug Targets , vol.12 , pp. 694-706
    • Morita, M.1    Shimozawa, N.2    Kashiwayama, Y.3    Suzuki, Y.4    Imanaka, T.5
  • 88
  • 89
    • 57349105177 scopus 로고    scopus 로고
    • The human peroxisomal ABC half transporter ALDP functions as a homodimer and accepts acyl-CoA esters
    • A.G.v.C.
    • van Roermund C.W.T., Visser W.F., IJlst L., A.G.v.C., Boek M., Kulik W., Waterham H.R., Wanders R.J.A. the human peroxisomal ABC half transporter ALDP functions as a homodimer and accepts acyl-CoA esters. FASEB J. 2008, 22:4201-4208.
    • (2008) FASEB J. , vol.22 , pp. 4201-4208
    • van Roermund, C.W.T.1    Visser, W.F.2    Ijlst, L.3    Boek, M.4    Kulik, W.5    Waterham, H.R.6    Wanders, R.J.A.7
  • 90
    • 78651253382 scopus 로고    scopus 로고
    • Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid beta-oxidation
    • van Roermund C.W.T., Visser W.F., IJlst L., Waterham H.R., Wanders R.J.A. Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid beta-oxidation. BBA-Mol. Cell. Biol. L. 2011, 1811:148-152.
    • (2011) BBA-Mol. Cell. Biol. L. , vol.1811 , pp. 148-152
    • van Roermund, C.W.T.1    Visser, W.F.2    Ijlst, L.3    Waterham, H.R.4    Wanders, R.J.A.5
  • 92
    • 84920102189 scopus 로고    scopus 로고
    • Enzymatic characterization of ELOVL1, a key enzyme in very long-chain fatty acid synthesis
    • Schackmann M.J., Ofman R., Dijkstra I.M., Wanders R.J., Kemp S. Enzymatic characterization of ELOVL1, a key enzyme in very long-chain fatty acid synthesis. Biochim. Biophys. Acta 2015, 1851:231-237.
    • (2015) Biochim. Biophys. Acta , vol.1851 , pp. 231-237
    • Schackmann, M.J.1    Ofman, R.2    Dijkstra, I.M.3    Wanders, R.J.4    Kemp, S.5
  • 93
    • 84864042465 scopus 로고    scopus 로고
    • X-linked adrenoleukodystrophy: clinical, metabolic, genetic and pathophysiological aspects
    • Kemp S., Berger J., Aubourg P. X-linked adrenoleukodystrophy: clinical, metabolic, genetic and pathophysiological aspects. Biochim. Biophys. Acta 2012, 1822:1465-1474.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1465-1474
    • Kemp, S.1    Berger, J.2    Aubourg, P.3
  • 98
    • 0027316040 scopus 로고
    • Studies on the substrate specificity of the inducible and non-inducible acyl-CoA oxidases from rat kidney peroxisomes
    • Wanders R.J.A., Denis S., Dacremont G. Studies on the substrate specificity of the inducible and non-inducible acyl-CoA oxidases from rat kidney peroxisomes. J. Biochem. 1993, 113:577-582.
    • (1993) J. Biochem. , vol.113 , pp. 577-582
    • Wanders, R.J.A.1    Denis, S.2    Dacremont, G.3
  • 101
    • 0026753328 scopus 로고
    • Bifunctional enzyme deficiency: identification of a new type of peroxisomal disorder in a patient with an impairment in peroxisomal beta-oxidation of unknown aetiology by means of complementation analysis
    • Wanders R.J.A., van Roermund C.W.T., Brul S., Schutgens R.B.H., Tager J.M. Bifunctional enzyme deficiency: identification of a new type of peroxisomal disorder in a patient with an impairment in peroxisomal beta-oxidation of unknown aetiology by means of complementation analysis. J. Inherit. Metab. Dis. 1992, 15:385-388.
    • (1992) J. Inherit. Metab. Dis. , vol.15 , pp. 385-388
    • Wanders, R.J.A.1    van Roermund, C.W.T.2    Brul, S.3    Schutgens, R.B.H.4    Tager, J.M.5
  • 108
    • 0028123083 scopus 로고
    • Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
    • Seedorf U., Brysch P., Engel T., Schrage K., Assmann G. Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity. J. Biol. Chem. 1994, 269:21277-21283.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21277-21283
    • Seedorf, U.1    Brysch, P.2    Engel, T.3    Schrage, K.4    Assmann, G.5
  • 109
    • 0031879234 scopus 로고    scopus 로고
    • Identification of the newly discovered 58 kDa peroxisomal thiolase SCPx as the main thiolase involved in both pristanic acid and trihydroxycholestanoic acid oxidation: implications for peroxisomal beta-oxidation disorders
    • Wanders R.J.A., Denis S., van Berkel E., Wouters F., Wirtz K.W.A., Seedorf U. Identification of the newly discovered 58 kDa peroxisomal thiolase SCPx as the main thiolase involved in both pristanic acid and trihydroxycholestanoic acid oxidation: implications for peroxisomal beta-oxidation disorders. J. Inherit. Metab. Dis. 1998, 21:302-305.
    • (1998) J. Inherit. Metab. Dis. , vol.21 , pp. 302-305
    • Wanders, R.J.A.1    Denis, S.2    van Berkel, E.3    Wouters, F.4    Wirtz, K.W.A.5    Seedorf, U.6
  • 111
    • 0028982895 scopus 로고
    • Purification and characterization of an alpha-methylacyl-CoA racemase from human liver
    • Schmitz W., Albers C., Fingerhut R., Conzelmann E. Purification and characterization of an alpha-methylacyl-CoA racemase from human liver. Eur. J. Biochem. 1995, 231:815-822.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 815-822
    • Schmitz, W.1    Albers, C.2    Fingerhut, R.3    Conzelmann, E.4
  • 113
    • 0034864582 scopus 로고    scopus 로고
    • Fibroblast studies documenting a case of peroxisomal 2-methylacyl-CoA racemase deficiency: possible link between racemase deficiency and malabsorption and vitamin K deficiency
    • Van Veldhoven P.P., Meyhi E., Squires R.H., Fransen M., Fournier B., Brys V., Bennett M.J., Mannaerts G.P. Fibroblast studies documenting a case of peroxisomal 2-methylacyl-CoA racemase deficiency: possible link between racemase deficiency and malabsorption and vitamin K deficiency. Eur. J. Clin. Investig. 2001, 31:714-722.
    • (2001) Eur. J. Clin. Investig. , vol.31 , pp. 714-722
    • Van Veldhoven, P.P.1    Meyhi, E.2    Squires, R.H.3    Fransen, M.4    Fournier, B.5    Brys, V.6    Bennett, M.J.7    Mannaerts, G.P.8
  • 118
    • 0034864582 scopus 로고    scopus 로고
    • Fibroblast studies documenting a case of peroxisomal 2-methylacyl-CoA racemase deficiency: possible link between racemase deficiency and malabsorption and vitamin K deficiency
    • Van Veldhoven P.P., Meyhi E., Squires R.H., Fransen M., Fournier B., Brys V., Bennett M.J., Mannaerts G.P. Fibroblast studies documenting a case of peroxisomal 2-methylacyl-CoA racemase deficiency: possible link between racemase deficiency and malabsorption and vitamin K deficiency. Eur. J. Clin. Investig. 2001, 31:714-722.
    • (2001) Eur. J. Clin. Investig. , vol.31 , pp. 714-722
    • Van Veldhoven, P.P.1    Meyhi, E.2    Squires, R.H.3    Fransen, M.4    Fournier, B.5    Brys, V.6    Bennett, M.J.7    Mannaerts, G.P.8
  • 121
    • 1542724509 scopus 로고    scopus 로고
    • Molecular basis of refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7)
    • Jansen G.A., Waterham H.R., Wanders R.J.A. Molecular basis of refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7). Hum. Mutat. 2004, 23:209-218.
    • (2004) Hum. Mutat. , vol.23 , pp. 209-218
    • Jansen, G.A.1    Waterham, H.R.2    Wanders, R.J.A.3
  • 124
    • 36749099619 scopus 로고    scopus 로고
    • Peroxisomal disorders affecting phytanic acid alpha-oxidation: a review
    • Wierzbicki A.S. Peroxisomal disorders affecting phytanic acid alpha-oxidation: a review. Biochem. Soc. Trans. 2007, 35:881-886.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 881-886
    • Wierzbicki, A.S.1
  • 127
    • 0022516472 scopus 로고
    • Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I
    • Danpure C.J., Jennings P.R. Peroxisomal alanine:glyoxylate aminotransferase deficiency in primary hyperoxaluria type I. FEBS Lett. 1986, 201:20-24.
    • (1986) FEBS Lett. , vol.201 , pp. 20-24
    • Danpure, C.J.1    Jennings, P.R.2
  • 128
    • 0032837155 scopus 로고    scopus 로고
    • The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II
    • Cramer S.D., Ferree P.M., Lin K., Milliner D.S., Holmes R.P. The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II. Hum. Mol. Genet. 1999, 8:2063-2069.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2063-2069
    • Cramer, S.D.1    Ferree, P.M.2    Lin, K.3    Milliner, D.S.4    Holmes, R.P.5
  • 130
    • 84884211351 scopus 로고    scopus 로고
    • Primary hyperoxaluria type III-a model for studying perturbations in glyoxylate metabolism
    • (Berlin, Germany)
    • Belostotsky R., Pitt J.J., Frishberg Y. Primary hyperoxaluria type III-a model for studying perturbations in glyoxylate metabolism. J. Mol. Med. 2012, 90:1497-1504. (Berlin, Germany).
    • (2012) J. Mol. Med. , vol.90 , pp. 1497-1504
    • Belostotsky, R.1    Pitt, J.J.2    Frishberg, Y.3
  • 131
    • 0029875738 scopus 로고    scopus 로고
    • Variant rhizomelic chondrodysplasia punctata (RCDP) with normal plasma phytanic acid: clinico-biochemical delineation of a subtype and complementation studies
    • Barth P.G., Wanders R.J.A., Schutgens R.B.H., Staalman C.R. Variant rhizomelic chondrodysplasia punctata (RCDP) with normal plasma phytanic acid: clinico-biochemical delineation of a subtype and complementation studies. Am. J. Med. Genet. 1996, 62:164-168.
    • (1996) Am. J. Med. Genet. , vol.62 , pp. 164-168
    • Barth, P.G.1    Wanders, R.J.A.2    Schutgens, R.B.H.3    Staalman, C.R.4
  • 137
    • 0032693473 scopus 로고    scopus 로고
    • Ether lipid biosynthesis. Alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities
    • de Vet E.C., IJlst L., Oostheim W., Dekker C., Moser H.W., van den Bosch H., Wanders R.J.A. Ether lipid biosynthesis. Alkyl-dihydroxyacetonephosphate synthase protein deficiency leads to reduced dihydroxyacetonephosphate acyltransferase activities. J. Lipid Res. 1999, 40:1998-2003.
    • (1999) J. Lipid Res. , vol.40 , pp. 1998-2003
    • de Vet, E.C.1    Ijlst, L.2    Oostheim, W.3    Dekker, C.4    Moser, H.W.5    van den Bosch, H.6    Wanders, R.J.A.7
  • 138
    • 84889072644 scopus 로고    scopus 로고
    • Topogenesis and homeostasis of fatty acyl-CoA reductase 1
    • Honsho M., Asaoku S., Fukumoto K., Fujiki Y. Topogenesis and homeostasis of fatty acyl-CoA reductase 1. J. Biol. Chem. 2013, 288:34588-34598.
    • (2013) J. Biol. Chem. , vol.288 , pp. 34588-34598
    • Honsho, M.1    Asaoku, S.2    Fukumoto, K.3    Fujiki, Y.4
  • 143
    • 0000296829 scopus 로고
    • Progressive oral gangrene probably due to lack of catalase in the blood (acatalasaemia); report of nine cases
    • Takahara S. Progressive oral gangrene probably due to lack of catalase in the blood (acatalasaemia); report of nine cases. Lancet 1952, 2:1101-1104.
    • (1952) Lancet , vol.2 , pp. 1101-1104
    • Takahara, S.1
  • 144
    • 84864623859 scopus 로고    scopus 로고
    • Acatalasemia and diabetes mellitus
    • Goth L., Nagy T. Acatalasemia and diabetes mellitus. Arch. Biochem. Biophys. 2012, 525:195-200.
    • (2012) Arch. Biochem. Biophys. , vol.525 , pp. 195-200
    • Goth, L.1    Nagy, T.2
  • 145
    • 84887022354 scopus 로고    scopus 로고
    • Inherited catalase deficiency: is it benign or a factor in various age related Disorders?
    • Goth L., Nagy T. Inherited catalase deficiency: is it benign or a factor in various age related Disorders?. Mutat. Res. 2013, 753:147-154.
    • (2013) Mutat. Res. , vol.753 , pp. 147-154
    • Goth, L.1    Nagy, T.2
  • 146
    • 78650546151 scopus 로고    scopus 로고
    • Genetic classification and mutational spectrum of more than 600 patients with a Zellweger syndrome spectrum disorder
    • Ebberink M.S., Mooijer P.A., Gootjes J., Koster J., Wanders R.J.A., Waterham H.R. Genetic classification and mutational spectrum of more than 600 patients with a Zellweger syndrome spectrum disorder. Hum. Mutat. 2011, 32:59-69.
    • (2011) Hum. Mutat. , vol.32 , pp. 59-69
    • Ebberink, M.S.1    Mooijer, P.A.2    Gootjes, J.3    Koster, J.4    Wanders, R.J.A.5    Waterham, H.R.6
  • 147
    • 61649120588 scopus 로고    scopus 로고
    • Identification of novel mutations and sequence variation in the Zellweger syndrome spectrum of peroxisome biogenesis disorders
    • Yik W.Y., Steinberg S.J., Moser A.B., Moser H.W., Hacia J.G. Identification of novel mutations and sequence variation in the Zellweger syndrome spectrum of peroxisome biogenesis disorders. Hum. Mutat. 2009, 30:E467-E480.
    • (2009) Hum. Mutat. , vol.30 , pp. E467-E480
    • Yik, W.Y.1    Steinberg, S.J.2    Moser, A.B.3    Moser, H.W.4    Hacia, J.G.5
  • 148
    • 0001687866 scopus 로고    scopus 로고
    • The peroxisomal biogenesis disorder
    • Mc Graw-Hill, New York, C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.)
    • Gould S.J., Raymond G.V., Valle D. The peroxisomal biogenesis disorder. The Metabolic & Molecular Bases of Inherited Disease 2001, 3181-3217. Mc Graw-Hill, New York. C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.).
    • (2001) The Metabolic & Molecular Bases of Inherited Disease , pp. 3181-3217
    • Gould, S.J.1    Raymond, G.V.2    Valle, D.3
  • 150
    • 0022480922 scopus 로고
    • Neonatal adrenoleukodystrophy: new cases, biochemical studies, and differentiation from Zellweger and related peroxisomal polydystrophy syndromes
    • Kelley R.I., Datta N.S., Dobyns W.B., Hajra A.K., Moser A.B., Noetzel M.J., Zackai E.H., Moser H.W. Neonatal adrenoleukodystrophy: new cases, biochemical studies, and differentiation from Zellweger and related peroxisomal polydystrophy syndromes. Am. J. Med. Genet. 1986, 23:869-901.
    • (1986) Am. J. Med. Genet. , vol.23 , pp. 869-901
    • Kelley, R.I.1    Datta, N.S.2    Dobyns, W.B.3    Hajra, A.K.4    Moser, A.B.5    Noetzel, M.J.6    Zackai, E.H.7    Moser, H.W.8
  • 161
    • 84878588576 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease-associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission
    • Huber N., Guimaraes S., Schrader M., Suter U., Niemann A. Charcot-Marie-Tooth disease-associated mutants of GDAP1 dissociate its roles in peroxisomal and mitochondrial fission. EMBO Rep. 2013, 14:545-552.
    • (2013) EMBO Rep. , vol.14 , pp. 545-552
    • Huber, N.1    Guimaraes, S.2    Schrader, M.3    Suter, U.4    Niemann, A.5
  • 163
    • 0033804524 scopus 로고    scopus 로고
    • Temperature-sensitive mutation of PEX6 in peroxisome biogenesis disorders in complementation group C (CG-C): comparative study of PEX6 and PEX1
    • Imamura A., Shimozawa N., Suzuki Y., Zhang Z., Tsukamoto T., Fujiki Y., Orii T., Osumi T., Wanders R.J.A., Kondo N. Temperature-sensitive mutation of PEX6 in peroxisome biogenesis disorders in complementation group C (CG-C): comparative study of PEX6 and PEX1. Pediatr. Res. 2000, 48:541-545.
    • (2000) Pediatr. Res. , vol.48 , pp. 541-545
    • Imamura, A.1    Shimozawa, N.2    Suzuki, Y.3    Zhang, Z.4    Tsukamoto, T.5    Fujiki, Y.6    Orii, T.7    Osumi, T.8    Wanders, R.J.A.9    Kondo, N.10
  • 165
  • 166
    • 0032440308 scopus 로고    scopus 로고
    • Rapid stable isotope dilution analysis of very-long-chain fatty acids, pristanic acid and phytanic acid using gas chromatography-electron impact mass spectrometry
    • Vreken P., Van Lint A.E.M., Bootsma A.H., Overmars H., Wanders R.J.A., Van Gennip A.H. Rapid stable isotope dilution analysis of very-long-chain fatty acids, pristanic acid and phytanic acid using gas chromatography-electron impact mass spectrometry. J. Chromatogr. 1998, 713:281-287.
    • (1998) J. Chromatogr. , vol.713 , pp. 281-287
    • Vreken, P.1    Van Lint, A.E.M.2    Bootsma, A.H.3    Overmars, H.4    Wanders, R.J.A.5    Van Gennip, A.H.6
  • 167
    • 0033039199 scopus 로고    scopus 로고
    • Rapid analysis of conjugated bile acids in plasma using electrospray tandem mass spectrometry: application for selective screening of peroxisomal disorders
    • Bootsma A.H., Overmars H., van Rooij A., Van Lint A.E.M., Wanders R.J.A., Van Gennip A.H., Vreken P. Rapid analysis of conjugated bile acids in plasma using electrospray tandem mass spectrometry: application for selective screening of peroxisomal disorders. J. Inherit. Metab. Dis. 1999, 22:307-310.
    • (1999) J. Inherit. Metab. Dis. , vol.22 , pp. 307-310
    • Bootsma, A.H.1    Overmars, H.2    van Rooij, A.3    Van Lint, A.E.M.4    Wanders, R.J.A.5    Van Gennip, A.H.6    Vreken, P.7
  • 168
    • 0029613810 scopus 로고
    • Assay of plasmalogens and polyunsaturated fatty acids (PUFA) in erythrocytes and fibroblasts
    • Dacremont G., Vincent G. Assay of plasmalogens and polyunsaturated fatty acids (PUFA) in erythrocytes and fibroblasts. J. Inherit. Metab. Dis. 1995, 18(Suppl. 1):84-89.
    • (1995) J. Inherit. Metab. Dis. , vol.18 , pp. 84-89
    • Dacremont, G.1    Vincent, G.2
  • 169
    • 0028238269 scopus 로고
    • Purification of peroxisomal acyl-CoA: dihydroxyacetonephosphate acyltransferase from human placenta
    • Ofman R., Wanders R.J.A. Purification of peroxisomal acyl-CoA: dihydroxyacetonephosphate acyltransferase from human placenta. Biochim. Biophys. Acta 1994, 1206:27-34.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 27-34
    • Ofman, R.1    Wanders, R.J.A.2
  • 171
    • 0027278174 scopus 로고
    • Studies on phytanic acid alpha-oxidation in rat liver and cultured human skin fibroblasts
    • Wanders R.J.A., van Roermund C.W.T. Studies on phytanic acid alpha-oxidation in rat liver and cultured human skin fibroblasts. Biochim. Biophys. Acta 1993, 1167:345-350.
    • (1993) Biochim. Biophys. Acta , vol.1167 , pp. 345-350
    • Wanders, R.J.A.1    van Roermund, C.W.T.2
  • 173
    • 0024374750 scopus 로고
    • Prenatal diagnosis of Zellweger syndrome by direct visualization of peroxisomes in chorionic villus fibroblasts by immunofluorescence microscopy
    • Wanders R.J.A., Wiemer E.A., Brul S., Schutgens R.B.H., van den Bosch H., Tager J.M. Prenatal diagnosis of Zellweger syndrome by direct visualization of peroxisomes in chorionic villus fibroblasts by immunofluorescence microscopy. J. Inherit. Metab. Dis. 1989, 12(Suppl 2):301-304.
    • (1989) J. Inherit. Metab. Dis. , vol.12 , pp. 301-304
    • Wanders, R.J.A.1    Wiemer, E.A.2    Brul, S.3    Schutgens, R.B.H.4    van den Bosch, H.5    Tager, J.M.6
  • 174
    • 67349229271 scopus 로고    scopus 로고
    • Rational diagnostic strategy for Zellweger syndrome spectrum patients
    • Krause C., Rosewich H., Gartner J. Rational diagnostic strategy for Zellweger syndrome spectrum patients. Eur. J. Hum. Genet. 2009, 17:741-748.
    • (2009) Eur. J. Hum. Genet. , vol.17 , pp. 741-748
    • Krause, C.1    Rosewich, H.2    Gartner, J.3


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