메뉴 건너뛰기




Volumn 1803, Issue 8, 2010, Pages 881-897

Be different-The diversity of peroxisomes in the animal kingdom

Author keywords

Differential protein expression; Metabolism; Molecular evolution; Peroxisomes; Species differences; Tissue variation

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALCOHOL; BILE ACID; CATALASE; FATTY ACID; GLYOXYLIC ACID; LUNG SURFACTANT; PEROXIN; PEROXISOME PROLIFERATOR; PURINE; REACTIVE OXYGEN METABOLITE; TESTOSTERONE; FUNGAL PROTEIN; MEMBRANE PROTEIN; PROTEOME; VEGETABLE PROTEIN;

EID: 77953715734     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.03.013     Document Type: Review
Times cited : (92)

References (282)
  • 1
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders R.J., Waterham H.R. Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 2006, 75:295-332.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.1    Waterham, H.R.2
  • 3
    • 34249908934 scopus 로고    scopus 로고
    • The peroxisomal protein import machinery
    • Platta H.W., Erdmann R. The peroxisomal protein import machinery. FEBS Lett. 2007, 581:2811-2819.
    • (2007) FEBS Lett. , vol.581 , pp. 2811-2819
    • Platta, H.W.1    Erdmann, R.2
  • 4
    • 0023755328 scopus 로고
    • Comparison of constitutive and inducible levels of expression of peroxisomal beta-oxidation and catalase genes in liver and extrahepatic tissues of rat
    • Nemali M.R., Usuda N., Reddy M.K., Oyasu K., Hashimoto T., Osumi T., Rao M.S., Reddy J.K. Comparison of constitutive and inducible levels of expression of peroxisomal beta-oxidation and catalase genes in liver and extrahepatic tissues of rat. Cancer Res. 1988, 48:5316-5324.
    • (1988) Cancer Res. , vol.48 , pp. 5316-5324
    • Nemali, 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
  • 7
    • 33748565936 scopus 로고    scopus 로고
    • PEX genes in fungal genomes: common, rare or redundant
    • Kiel J.A., Veenhuis M., van der Klei I.J. PEX genes in fungal genomes: common, rare or redundant. Traffic 2006, 7:1291-1303.
    • (2006) Traffic , vol.7 , pp. 1291-1303
    • Kiel, J.A.1    Veenhuis, M.2    van der Klei, I.J.3
  • 8
    • 0037650076 scopus 로고    scopus 로고
    • Modeling human peroxisome biogenesis disorders in the nematode Caenorhabditis elegans
    • Thieringer H., Moellers B., Dodt G., Kunau W.H., Driscoll M. Modeling human peroxisome biogenesis disorders in the nematode Caenorhabditis elegans. J. Cell Sci. 2003, 116:1797-1804.
    • (2003) J. Cell Sci. , vol.116 , pp. 1797-1804
    • Thieringer, H.1    Moellers, B.2    Dodt, G.3    Kunau, W.H.4    Driscoll, M.5
  • 9
    • 77953022588 scopus 로고    scopus 로고
    • Peroxisomal protein translocation, Biochim Biophys Acta, [Electronic publication].
    • W. Girzalsky, D. Saffian, R. Erdmann, Peroxisomal protein translocation, Biochim Biophys Acta, (2010) [Electronic publication].
    • (2010)
    • Girzalsky W1    Saffian D2    Erdmann, R.3
  • 11
    • 33845300838 scopus 로고    scopus 로고
    • Peroxisome targeting signal 1: is it really a simple tripeptide?
    • Brocard C., Hartig A. Peroxisome targeting signal 1: is it really a simple tripeptide?. Biochim. Biophys. Acta 2006, 1763:1565-1573.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1565-1573
    • Brocard, C.1    Hartig, A.2
  • 12
    • 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
  • 14
    • 33845340472 scopus 로고    scopus 로고
    • PTS2 co-receptors: diverse proteins with common features
    • Schliebs W., Kunau W.H. PTS2 co-receptors: diverse proteins with common features. Biochim. Biophys. Acta 2006, 1763:1605-1612.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 1605-1612
    • Schliebs, W.1    Kunau, W.H.2
  • 16
    • 0034231261 scopus 로고    scopus 로고
    • Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes
    • Motley A.M., Hettema E.H., Ketting R., Plasterk R., Tabak H.F. Caenorhabditis elegans has a single pathway to target matrix proteins to peroxisomes. EMBO Rep. 2000, 1:40-46.
    • (2000) EMBO Rep. , vol.1 , pp. 40-46
    • Motley, A.M.1    Hettema, E.H.2    Ketting, R.3    Plasterk, R.4    Tabak, H.F.5
  • 17
    • 0032515348 scopus 로고    scopus 로고
    • Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: evolutionary switching of peroxisomal targeting signals
    • de Vet E.C., Prinsen H.C., van den Bosch H. Nucleotide sequence of a cDNA clone encoding a Caenorhabditis elegans homolog of mammalian alkyl-dihydroxyacetonephosphate synthase: evolutionary switching of peroxisomal targeting signals. Biochem. Biophys. Res. Commun. 1998, 242:277-281.
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 277-281
    • de Vet, E.C.1    Prinsen, H.C.2    van den Bosch, H.3
  • 18
    • 4143138725 scopus 로고    scopus 로고
    • A new definition for the consensus sequence of the peroxisome targeting signal type 2
    • Petriv O.I., Tang L., Titorenko V.I., Rachubinski R.A. A new definition for the consensus sequence of the peroxisome targeting signal type 2. J. Mol. Biol. 2004, 341:119-134.
    • (2004) J. Mol. Biol. , vol.341 , pp. 119-134
    • Petriv, O.I.1    Tang, L.2    Titorenko, V.I.3    Rachubinski, R.A.4
  • 19
    • 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
  • 20
    • 59449104113 scopus 로고    scopus 로고
    • The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway
    • Matsuzaki T., Fujiki Y. The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway. J. Cell Biol. 2008, 183:1275-1286.
    • (2008) J. Cell Biol. , vol.183 , pp. 1275-1286
    • Matsuzaki, T.1    Fujiki, Y.2
  • 22
    • 73549108735 scopus 로고    scopus 로고
    • Divide et impera: the dictum of peroxisomes
    • Nagotu S., Veenhuis M., van der Klei I.J. Divide et impera: the dictum of peroxisomes. Traffic 2010, 11:175-184.
    • (2010) Traffic , vol.11 , pp. 175-184
    • Nagotu, S.1    Veenhuis, M.2    van der Klei, I.J.3
  • 23
    • 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
  • 24
    • 57749113632 scopus 로고    scopus 로고
    • Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes
    • Lingard M.J., Gidda S.K., Bingham S., Rothstein S.J., Mullen R.T., Trelease R.N. Arabidopsis PEROXIN11c-e, FISSION1b, and DYNAMIN-RELATED PROTEIN3A cooperate in cell cycle-associated replication of peroxisomes. Plant Cell 2008, 20:1567-1585.
    • (2008) Plant Cell , vol.20 , pp. 1567-1585
    • Lingard, M.J.1    Gidda, S.K.2    Bingham, S.3    Rothstein, S.J.4    Mullen, R.T.5    Trelease, R.N.6
  • 25
    • 77949876577 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of peroxisome proliferator protein PEX11 controls peroxisome abundance
    • Knoblach B., Rachubinski R.A. Phosphorylation-dependent activation of peroxisome proliferator protein PEX11 controls peroxisome abundance. J. Biol. Chem. 2009, 285:6670-6680.
    • (2009) J. Biol. Chem. , vol.285 , pp. 6670-6680
    • Knoblach, B.1    Rachubinski, R.A.2
  • 26
    • 33745742255 scopus 로고    scopus 로고
    • Shared components of mitochondrial and peroxisomal division
    • Schrader M. Shared components of mitochondrial and peroxisomal division. Biochim. Biophys. Acta 2006, 1763:531-541.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 531-541
    • Schrader, M.1
  • 27
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • Gandre-Babbe S., van der Bliek A.M. The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol. Biol. Cell 2008, 19:2402-2412.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    van der Bliek, A.M.2
  • 28
    • 64449084971 scopus 로고    scopus 로고
    • Organelle dynamics and dysfunction: a closer link between peroxisomes and mitochondria
    • Camoes F., Bonekamp N.A., Delille H.K., Schrader M. Organelle dynamics and dysfunction: a closer link between peroxisomes and mitochondria. J. Inherit. Metab. Dis. 2009, 32:163-180.
    • (2009) J. Inherit. Metab. Dis. , vol.32 , pp. 163-180
    • Camoes, F.1    Bonekamp, N.A.2    Delille, H.K.3    Schrader, M.4
  • 29
    • 64649093836 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes and mitochondria: linked by division
    • Delille H.K., Alves R., Schrader M. Biogenesis of peroxisomes and mitochondria: linked by division. Histochem. Cell Biol. 2009, 131:441-446.
    • (2009) Histochem. Cell Biol. , vol.131 , pp. 441-446
    • Delille, H.K.1    Alves, R.2    Schrader, M.3
  • 30
    • 70450188176 scopus 로고    scopus 로고
    • Dynamics of peroxisome abundance: a tale of division and proliferation
    • Kaur N., Hu J. Dynamics of peroxisome abundance: a tale of division and proliferation. Curr. Opin. Plant Biol. 2009, 12:781-788.
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 781-788
    • Kaur, N.1    Hu, J.2
  • 31
    • 36549083069 scopus 로고    scopus 로고
    • Orchestrating organelle inheritance in Saccharomyces cerevisiae
    • Fagarasanu A., Rachubinski R.A. Orchestrating organelle inheritance in Saccharomyces cerevisiae. Curr. Opin. Microbiol. 2007, 10:528-538.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 528-538
    • Fagarasanu, A.1    Rachubinski, R.A.2
  • 32
    • 0032851248 scopus 로고    scopus 로고
    • Enzymes involved in purine metabolism-a review of histochemical localization and functional implications
    • Moriwaki Y., Yamamoto T., Higashino K. Enzymes involved in purine metabolism-a review of histochemical localization and functional implications. Histol. Histopathol. 1999, 14:1321-1340.
    • (1999) Histol. Histopathol. , vol.14 , pp. 1321-1340
    • Moriwaki, Y.1    Yamamoto, T.2    Higashino, K.3
  • 33
    • 0014684527 scopus 로고
    • The enzymatic characteristics of peroxisomes of amphibian and avian liver and kidney
    • Scott P.J., Visentin L.P., Allen J.M. The enzymatic characteristics of peroxisomes of amphibian and avian liver and kidney. Ann. N. Y. Acad. Sci. 1969, 168:244-264.
    • (1969) Ann. N. Y. Acad. Sci. , vol.168 , pp. 244-264
    • Scott, P.J.1    Visentin, L.P.2    Allen, J.M.3
  • 34
    • 0016320450 scopus 로고
    • A new spectrophotometric assay method of xanthine oxidase in crude tissue homogenate
    • Hashimoto S. A new spectrophotometric assay method of xanthine oxidase in crude tissue homogenate. Anal. Biochem. 1974, 62:426-435.
    • (1974) Anal. Biochem. , vol.62 , pp. 426-435
    • Hashimoto, S.1
  • 35
    • 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
  • 36
    • 0023442484 scopus 로고
    • Peroxisomes in wild-type and rosy mutant Drosophila melanogaster
    • Beard M.E., Holtzman E. Peroxisomes in wild-type and rosy mutant Drosophila melanogaster. Proc. Natl. Acad. Sci. U. S. A. 1987, 84:7433-7437.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 7433-7437
    • Beard, M.E.1    Holtzman, E.2
  • 37
    • 0018363809 scopus 로고
    • Degradation of uric acid to urea and glyoxylate in peroxisomes
    • Noguchi T., Takada Y., Fujiwara S. Degradation of uric acid to urea and glyoxylate in peroxisomes. J. Biol. Chem. 1979, 254:5272-5275.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5272-5275
    • Noguchi, T.1    Takada, Y.2    Fujiwara, S.3
  • 38
    • 0018657569 scopus 로고
    • Intestinal peroxisomes of goldfish (Carassius auratus)-examination for hydrolase, dehydrogenase and carnitine acetyltransferase activities
    • Temple N.J., Martin P.A., Connock M.J. Intestinal peroxisomes of goldfish (Carassius auratus)-examination for hydrolase, dehydrogenase and carnitine acetyltransferase activities. Comp. Biochem. Physiol. B 1979, 64:57-63.
    • (1979) Comp. Biochem. Physiol. B , vol.64 , pp. 57-63
    • Temple, N.J.1    Martin, P.A.2    Connock, M.J.3
  • 40
    • 0031225220 scopus 로고    scopus 로고
    • Histochemistry of oxidases in several tissues of bivalve molluscs
    • Cancio I., Cajaraville M.P. Histochemistry of oxidases in several tissues of bivalve molluscs. Cell Biol. Int. 1997, 21:575-584.
    • (1997) Cell Biol. Int. , vol.21 , pp. 575-584
    • Cancio, I.1    Cajaraville, M.P.2
  • 41
    • 0036219276 scopus 로고    scopus 로고
    • Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells
    • Frederiks W.M., Vreeling-Sindelarova H. Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells. Acta Histochem. 2002, 104:29-37.
    • (2002) Acta Histochem. , vol.104 , pp. 29-37
    • Frederiks, W.M.1    Vreeling-Sindelarova, H.2
  • 42
    • 0034573311 scopus 로고    scopus 로고
    • Evolution of urate-degrading enzymes in animal peroxisomes
    • Spring
    • Hayashi S., Fujiwara S., Noguchi T. Evolution of urate-degrading enzymes in animal peroxisomes. Cell Biochem. Biophys. 2000, 32:123-129. Spring.
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 123-129
    • Hayashi, S.1    Fujiwara, S.2    Noguchi, T.3
  • 43
  • 44
    • 0024977939 scopus 로고
    • Degradation of uric acid in fish liver peroxisomes. Intraperoxisomal localization of hepatic allantoicase and purification of its peroxisomal membrane-bound form
    • Hayashi S., Fujiwara S., Noguchi T. Degradation of uric acid in fish liver peroxisomes. Intraperoxisomal localization of hepatic allantoicase and purification of its peroxisomal membrane-bound form. J. Biol. Chem. 1989, 264:3211-3215.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3211-3215
    • Hayashi, S.1    Fujiwara, S.2    Noguchi, T.3
  • 46
    • 0028316885 scopus 로고
    • Uric acid degrading enzymes, urate oxidase and allantoinase, are associated with different subcellular organelles in frog liver and kidney
    • Usuda N., Hayashi S., Fujiwara S., Noguchi T., Nagata T., Rao M.S., Alvares K., Reddy J.K., Yeldandi A.V. Uric acid degrading enzymes, urate oxidase and allantoinase, are associated with different subcellular organelles in frog liver and kidney. J. Cell Sci. 1994, 107(Pt 4):1073-1081.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 4 , pp. 1073-1081
    • Usuda, N.1    Hayashi, S.2    Fujiwara, S.3    Noguchi, T.4    Nagata, T.5    Rao, M.S.6    Alvares, K.7    Reddy, J.K.8    Yeldandi, A.V.9
  • 48
    • 0031127316 scopus 로고    scopus 로고
    • Variable peroxisomal and mitochondrial targeting of alanine: glyoxylate aminotransferase in mammalian evolution and disease
    • Danpure C.J. Variable peroxisomal and mitochondrial targeting of alanine: glyoxylate aminotransferase in mammalian evolution and disease. Bioessays 1997, 19:317-326.
    • (1997) Bioessays , vol.19 , pp. 317-326
    • Danpure, C.J.1
  • 49
    • 0002316115 scopus 로고
    • Amino acid metabolism in animal peroxisomes
    • Springer-Verlag, Berlin, H.D. Fahimi, H. Sies (Eds.)
    • Noguchi T. Amino acid metabolism in animal peroxisomes. Peroxisomes in Biology and Medicine 1987, 234-243. Springer-Verlag, Berlin. H.D. Fahimi, H. Sies (Eds.).
    • (1987) Peroxisomes in Biology and Medicine , pp. 234-243
    • Noguchi, T.1
  • 50
    • 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. 1990, 265:7513-7519.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7513-7519
    • Oda, T.1    Funai, T.2    Ichiyama, A.3
  • 51
    • 0026724618 scopus 로고
    • Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular targeting. Analysis of the marmoset and rabbit genes
    • Purdue P.E., Lumb M.J., Danpure C.J. Molecular evolution of alanine/glyoxylate aminotransferase 1 intracellular targeting. Analysis of the marmoset and rabbit genes. Eur. J. Biochem. 1992, 207:757-766.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 757-766
    • Purdue, P.E.1    Lumb, M.J.2    Danpure, C.J.3
  • 52
    • 0025372539 scopus 로고
    • Human peroxisomal l-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon
    • Takada Y., Kaneko N., Esumi H., Purdue P.E., Danpure C.J. Human peroxisomal l-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem. J. 1990, 268:517-520.
    • (1990) Biochem. J. , vol.268 , pp. 517-520
    • Takada, Y.1    Kaneko, N.2    Esumi, H.3    Purdue, P.E.4    Danpure, C.J.5
  • 53
    • 0032055790 scopus 로고    scopus 로고
    • Evolution of alanine:glyoxylate aminotransferase intracellular targeting: structural and functional analysis of the guinea pig gene
    • Birdsey G.M., Danpure C.J. Evolution of alanine:glyoxylate aminotransferase intracellular targeting: structural and functional analysis of the guinea pig gene. Biochem. J. 1998, 331(Pt 1):49-60.
    • (1998) Biochem. J. , vol.331 , Issue.PART 1 , pp. 49-60
    • Birdsey, G.M.1    Danpure, C.J.2
  • 54
    • 0030784914 scopus 로고    scopus 로고
    • A unique molecular basis for enzyme mistargeting in primary hyperoxaluria type 1
    • Leiper J.M., Danpure C.J. A unique molecular basis for enzyme mistargeting in primary hyperoxaluria type 1. Clin. Chim. Acta 1997, 266:39-50.
    • (1997) Clin. Chim. Acta , vol.266 , pp. 39-50
    • Leiper, J.M.1    Danpure, C.J.2
  • 58
    • 4744371532 scopus 로고    scopus 로고
    • Peroxisomes, lipid metabolism, and peroxisomal disorders
    • Wanders R.J. Peroxisomes, lipid metabolism, and peroxisomal disorders. Mol. Genet. Metab. 2004, 83:16-27.
    • (2004) Mol. Genet. Metab. , vol.83 , pp. 16-27
    • Wanders, R.J.1
  • 59
    • 0034717058 scopus 로고    scopus 로고
    • Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids
    • Baes M., Huyghe S., Carmeliet P., Declercq P.E., Collen D., Mannaerts G.P., Van Veldhoven P.P. Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids. J. Biol. Chem. 2000, 275:16329-16336.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16329-16336
    • Baes, M.1    Huyghe, S.2    Carmeliet, P.3    Declercq, P.E.4    Collen, D.5    Mannaerts, G.P.6    Van Veldhoven, P.P.7
  • 60
    • 34548166529 scopus 로고    scopus 로고
    • Rat liver peroxisomes after fibrate treatment. A survey using quantitative mass spectrometry
    • Islinger M., Luers G.H., Li K.W., Loos M., Volkl A. Rat liver peroxisomes after fibrate treatment. A survey using quantitative mass spectrometry. J. Biol. Chem. 2007, 282:23055-23069.
    • (2007) J. Biol. Chem. , vol.282 , pp. 23055-23069
    • Islinger, M.1    Luers, G.H.2    Li, K.W.3    Loos, M.4    Volkl, A.5
  • 61
    • 0034023704 scopus 로고    scopus 로고
    • Peroxisomes in molluscs, characterization by subcellular fractionation combined with western blotting, immunohistochemistry, and immunocytochemistry
    • Cancio I., Volkl A., Beier K., Fahimi H.D., Cajaraville M.P. Peroxisomes in molluscs, characterization by subcellular fractionation combined with western blotting, immunohistochemistry, and immunocytochemistry. Histochem. Cell Biol. 2000, 113:51-60.
    • (2000) Histochem. Cell Biol. , vol.113 , pp. 51-60
    • Cancio, I.1    Volkl, A.2    Beier, K.3    Fahimi, H.D.4    Cajaraville, M.P.5
  • 62
    • 0027074766 scopus 로고
    • Peroxisomes in digestive gland cells of the mussel Mytilus galloprovincialis Lmk. Biochemical, ultrastructural and immunocytochemical characterization
    • Cajaraville M.P., Volkl A., Fahimi H.D. Peroxisomes in digestive gland cells of the mussel Mytilus galloprovincialis Lmk. Biochemical, ultrastructural and immunocytochemical characterization. Eur. J. Cell Biol. 1992, 59:255-264.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 255-264
    • Cajaraville, M.P.1    Volkl, A.2    Fahimi, H.D.3
  • 63
    • 0015713701 scopus 로고
    • Localization of some enzymes of beta-oxidation of fatty acids in the peroxisomes of Tetrahymena
    • Blum J.J. Localization of some enzymes of beta-oxidation of fatty acids in the peroxisomes of Tetrahymena. J. Protozool 1973, 20:688-692.
    • (1973) J. Protozool , vol.20 , pp. 688-692
    • Blum, J.J.1
  • 64
    • 0037431017 scopus 로고    scopus 로고
    • Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase
    • Oba Y., Ojika M., Inouye S. Firefly luciferase is a bifunctional enzyme: ATP-dependent monooxygenase and a long chain fatty acyl-CoA synthetase. FEBS Lett. 2003, 540:251-254.
    • (2003) FEBS Lett. , vol.540 , pp. 251-254
    • Oba, Y.1    Ojika, M.2    Inouye, S.3
  • 66
    • 0024410242 scopus 로고
    • Comparative studies on nafenopin-induced hepatic peroxisome proliferation in the rat. Syrian hamster, guinea pig, and marmoset
    • Lake B.G., Evans J.G., Gray T.J., Korosi S.A., North C.J. Comparative studies on nafenopin-induced hepatic peroxisome proliferation in the rat. Syrian hamster, guinea pig, and marmoset. Toxicol. Appl. Pharmacol. 1989, 99:148-160.
    • (1989) Toxicol. Appl. Pharmacol. , vol.99 , pp. 148-160
    • Lake, B.G.1    Evans, J.G.2    Gray, T.J.3    Korosi, S.A.4    North, C.J.5
  • 67
    • 0024504510 scopus 로고
    • Species differences in the effects of bezafibrate, a hypolipidemic agent, on hepatic peroxisome-associated enzymes
    • Watanabe T., Horie S., Yamada J., Isaji M., Nishigaki T., Naito J., Suga T. Species differences in the effects of bezafibrate, a hypolipidemic agent, on hepatic peroxisome-associated enzymes. Biochem. Pharmacol. 1989, 38:367-371.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 367-371
    • Watanabe, T.1    Horie, S.2    Yamada, J.3    Isaji, M.4    Nishigaki, T.5    Naito, J.6    Suga, T.7
  • 69
    • 0026262231 scopus 로고
    • Peroxisomal beta-oxidation: insights from comparative biochemistry
    • Moyes C.D., Suarez R.K., Brown G.S., Hochachka P.W. Peroxisomal beta-oxidation: insights from comparative biochemistry. J. Exp. Zool. 1991, 260:267-273.
    • (1991) J. Exp. Zool. , vol.260 , pp. 267-273
    • Moyes, C.D.1    Suarez, R.K.2    Brown, G.S.3    Hochachka, P.W.4
  • 70
    • 0018641621 scopus 로고
    • Postnatal development of peroxisomal and mitochondrial enzymes in rat liver
    • Krahling J.B., Gee R., Gauger J.A., Tolbert N.E. Postnatal development of peroxisomal and mitochondrial enzymes in rat liver. J. Cell Physiol. 1979, 101:375-390.
    • (1979) J. Cell Physiol. , vol.101 , pp. 375-390
    • Krahling, J.B.1    Gee, R.2    Gauger, J.A.3    Tolbert, N.E.4
  • 71
    • 0020965193 scopus 로고
    • Effect of cold adaptation on liver peroxisomes and peroxisomal oxidative activities of rat. A morphometric/stereologic and biochemical study
    • Pollera M., Locci-Cubeddu T., Bergamini E. Effect of cold adaptation on liver peroxisomes and peroxisomal oxidative activities of rat. A morphometric/stereologic and biochemical study. Arch. Int. Physiol. Biochim. 1983, 91:35-42.
    • (1983) Arch. Int. Physiol. Biochim. , vol.91 , pp. 35-42
    • Pollera, M.1    Locci-Cubeddu, T.2    Bergamini, E.3
  • 72
    • 0023722255 scopus 로고
    • On the mechanism of induction of the enzyme systems for peroxisomal beta-oxidation of fatty acids in rat liver by diets rich in partially hydrogenated fish oil
    • Flatmark T., Nilsson A., Kvannes J., Eikhom T.S., Fukami M.H., Kryvi H., Christiansen E.N. On the mechanism of induction of the enzyme systems for peroxisomal beta-oxidation of fatty acids in rat liver by diets rich in partially hydrogenated fish oil. Biochim. Biophys. Acta 1988, 962:122-130.
    • (1988) Biochim. Biophys. Acta , vol.962 , pp. 122-130
    • Flatmark, T.1    Nilsson, A.2    Kvannes, J.3    Eikhom, T.S.4    Fukami, M.H.5    Kryvi, H.6    Christiansen, E.N.7
  • 73
    • 0028289751 scopus 로고
    • Peroxisomes in liver, heart, and kidney of mice fed a commercial fish oil preparation: original data and review on peroxisomal changes induced by high-fat diets
    • De Craemer D., Vamecq J., Roels F., Vallee L., Pauwels M., Van den Branden C. Peroxisomes in liver, heart, and kidney of mice fed a commercial fish oil preparation: original data and review on peroxisomal changes induced by high-fat diets. J. Lipid Res. 1994, 35:1241-1250.
    • (1994) J. Lipid Res. , vol.35 , pp. 1241-1250
    • De Craemer, D.1    Vamecq, J.2    Roels, F.3    Vallee, L.4    Pauwels, M.5    Van den Branden, C.6
  • 74
    • 0013854955 scopus 로고
    • Nature of the hepatomegalic effect produced by ethyl-chlorophenoxy-isobutyrate in the rat
    • Hess R., Staubli W., Riess W. Nature of the hepatomegalic effect produced by ethyl-chlorophenoxy-isobutyrate in the rat. Nature 1965, 208:856-858.
    • (1965) Nature , vol.208 , pp. 856-858
    • Hess, R.1    Staubli, W.2    Riess, W.3
  • 75
    • 0342528190 scopus 로고
    • A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug
    • Lazarow P.B., De Duve C. A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug. Proc. Natl. Acad. Sci. U. S. A. 1976, 73:2043-2046.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2043-2046
    • Lazarow, P.B.1    De Duve, C.2
  • 76
    • 0017284938 scopus 로고
    • Hepatocellular carcinomas in acatalasemic mice treated with nafenopin, a hypolipidemic peroxisome proliferator
    • Reddy J.K., Rao S., Moody D.E. Hepatocellular carcinomas in acatalasemic mice treated with nafenopin, a hypolipidemic peroxisome proliferator. Cancer Res. 1976, 36:1211-1217.
    • (1976) Cancer Res. , vol.36 , pp. 1211-1217
    • Reddy, J.K.1    Rao, S.2    Moody, D.E.3
  • 78
    • 0017815141 scopus 로고
    • Enhancement of fatty acyl-CoA oxidizing activity in rat liver peroxisomes by di-(i-ethylhexyl)phthalate
    • Osumi T., Hashimoto T. Enhancement of fatty acyl-CoA oxidizing activity in rat liver peroxisomes by di-(i-ethylhexyl)phthalate. J. Biochem. 1978, 83:1361-1365.
    • (1978) J. Biochem. , vol.83 , pp. 1361-1365
    • Osumi, T.1    Hashimoto, T.2
  • 79
    • 0021248040 scopus 로고
    • Quantitative microscopy comparison of peroxisome proliferation by the lipid-regulating agent gemfibrozil in several species
    • Gray R.H., de la Iglesia F.A. Quantitative microscopy comparison of peroxisome proliferation by the lipid-regulating agent gemfibrozil in several species. Hepatology 1984, 4:520-530.
    • (1984) Hepatology , vol.4 , pp. 520-530
    • Gray, R.H.1    de la Iglesia, F.A.2
  • 80
    • 0343415745 scopus 로고    scopus 로고
    • Species differences in induction of hepatic enzymes by BM 17.0744, an activator of peroxisome proliferator-activated receptor alpha (PPARalpha)
    • Meyer K., Volkl A., Endele R., Kuhnle H.F., Pill J. Species differences in induction of hepatic enzymes by BM 17.0744, an activator of peroxisome proliferator-activated receptor alpha (PPARalpha). Arch. Toxicol. 1999, 73:440-450.
    • (1999) Arch. Toxicol. , vol.73 , pp. 440-450
    • Meyer, K.1    Volkl, A.2    Endele, R.3    Kuhnle, H.F.4    Pill, J.5
  • 81
    • 0025183341 scopus 로고
    • Effect of ciprofibrate, bezafibrate, and LY171883 on peroxisomal beta-oxidation in cultured rat, dog, and rhesus monkey hepatocytes
    • Foxworthy P.S., White S.L., Hoover D.M., Eacho P.I. Effect of ciprofibrate, bezafibrate, and LY171883 on peroxisomal beta-oxidation in cultured rat, dog, and rhesus monkey hepatocytes. Toxicol. Appl. Pharmacol. 1990, 104:386-394.
    • (1990) Toxicol. Appl. Pharmacol. , vol.104 , pp. 386-394
    • Foxworthy, P.S.1    White, S.L.2    Hoover, D.M.3    Eacho, P.I.4
  • 84
    • 2942573031 scopus 로고    scopus 로고
    • Biochemical and morphological effects of K-111, a peroxisome proliferator-activated receptor (PPAR)alpha activator, in non-human primates
    • Schafer S.A., Hansen B.C., Volkl A., Fahimi H.D., Pill J. Biochemical and morphological effects of K-111, a peroxisome proliferator-activated receptor (PPAR)alpha activator, in non-human primates. Biochem. Pharmacol. 2004, 68:239-251.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 239-251
    • Schafer, S.A.1    Hansen, B.C.2    Volkl, A.3    Fahimi, H.D.4    Pill, J.5
  • 85
    • 0037205918 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor alpha (PPARalpha): role in hepatocarcinogenesis
    • Gonzalez F.J. The peroxisome proliferator-activated receptor alpha (PPARalpha): role in hepatocarcinogenesis. Mol. Cell. Endocrinol. 2002, 193:71-79.
    • (2002) Mol. Cell. Endocrinol. , vol.193 , pp. 71-79
    • Gonzalez, F.J.1
  • 86
    • 0032921022 scopus 로고    scopus 로고
    • Effect of clofibrate, a peroxisome proliferator, in sea bass (Dicentrarchus labrax), a marine fish
    • Pretti C., Novi S., Longo V., Gervasi P.G. Effect of clofibrate, a peroxisome proliferator, in sea bass (Dicentrarchus labrax), a marine fish. Environ. Res. 1999, 80:294-296.
    • (1999) Environ. Res. , vol.80 , pp. 294-296
    • Pretti, C.1    Novi, S.2    Longo, V.3    Gervasi, P.G.4
  • 87
    • 0028007570 scopus 로고
    • Evaluation of a rodent peroxisome proliferator in two species of freshwater fish: rainbow trout (Onchorynchus mykiss) and Japanese medaka (Oryzias latipes)
    • Scarano L.J., Calabrese E.J., Kostecki P.T., Baldwin L.A., Leonard D.A. Evaluation of a rodent peroxisome proliferator in two species of freshwater fish: rainbow trout (Onchorynchus mykiss) and Japanese medaka (Oryzias latipes). Ecotoxicol. Environ. Saf. 1994, 29:13-19.
    • (1994) Ecotoxicol. Environ. Saf. , vol.29 , pp. 13-19
    • Scarano, L.J.1    Calabrese, E.J.2    Kostecki, P.T.3    Baldwin, L.A.4    Leonard, D.A.5
  • 88
    • 0025770522 scopus 로고
    • The effect of clofibrate on amphibian hepatic peroxisomes
    • Ciolek E., Dauca M. The effect of clofibrate on amphibian hepatic peroxisomes. Biol. Cell 1991, 71:313-320.
    • (1991) Biol. Cell , vol.71 , pp. 313-320
    • Ciolek, E.1    Dauca, M.2
  • 90
    • 0021348339 scopus 로고
    • Induction of hepatic peroxisome proliferation in nonrodent species, including primates
    • Reddy J.K., Lalwani N.D., Qureshi S.A., Reddy M.K., Moehle C.M. Induction of hepatic peroxisome proliferation in nonrodent species, including primates. Am. J. Pathol. 1984, 114:171-183.
    • (1984) Am. J. Pathol. , vol.114 , pp. 171-183
    • Reddy, J.K.1    Lalwani, N.D.2    Qureshi, S.A.3    Reddy, M.K.4    Moehle, C.M.5
  • 91
    • 0031930576 scopus 로고    scopus 로고
    • Induction of peroxisomal oxidases in mussels: comparison of effects of lubricant oil and benzo(a)pyrene with two typical peroxisome proliferators on peroxisome structure and function in Mytilus galloprovincialis
    • Cancio I., Orbea A., Volkl A., Fahimi H.D., Cajaraville M.P. Induction of peroxisomal oxidases in mussels: comparison of effects of lubricant oil and benzo(a)pyrene with two typical peroxisome proliferators on peroxisome structure and function in Mytilus galloprovincialis. Toxicol. Appl. Pharmacol. 1998, 149:64-72.
    • (1998) Toxicol. Appl. Pharmacol. , vol.149 , pp. 64-72
    • Cancio, I.1    Orbea, A.2    Volkl, A.3    Fahimi, H.D.4    Cajaraville, M.P.5
  • 92
    • 0025132245 scopus 로고
    • Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators
    • Issemann I., Green S. Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators. Nature 1990, 347:645-650.
    • (1990) Nature , vol.347 , pp. 645-650
    • Issemann, I.1    Green, S.2
  • 93
    • 0027278522 scopus 로고
    • Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR)
    • Dreyer C., Keller H., Mahfoudi A., Laudet V., Krey G., Wahli W. Positive regulation of the peroxisomal beta-oxidation pathway by fatty acids through activation of peroxisome proliferator-activated receptors (PPAR). Biol. Cell 1993, 77:67-76.
    • (1993) Biol. Cell , vol.77 , pp. 67-76
    • Dreyer, C.1    Keller, H.2    Mahfoudi, A.3    Laudet, V.4    Krey, G.5    Wahli, W.6
  • 98
    • 0031915653 scopus 로고    scopus 로고
    • A peroxisome proliferator-activated receptor-alpha (PPARalpha) cDNA cloned from guinea-pig liver encodes a protein with similar properties to the mouse PPARalpha: implications for species differences in responses to peroxisome proliferators
    • Tugwood J.D., Holden P.R., James N.H., Prince R.A., Roberts R.A. A peroxisome proliferator-activated receptor-alpha (PPARalpha) cDNA cloned from guinea-pig liver encodes a protein with similar properties to the mouse PPARalpha: implications for species differences in responses to peroxisome proliferators. Arch. Toxicol. 1998, 72:169-177.
    • (1998) Arch. Toxicol. , vol.72 , pp. 169-177
    • Tugwood, J.D.1    Holden, P.R.2    James, N.H.3    Prince, R.A.4    Roberts, R.A.5
  • 99
    • 0032692724 scopus 로고    scopus 로고
    • Species differences in sequence and activity of the peroxisome proliferator response element (PPRE) within the acyl CoA oxidase gene promoter
    • Lambe K.G., Woodyatt N.J., Macdonald N., Chevalier S., Roberts R.A. Species differences in sequence and activity of the peroxisome proliferator response element (PPRE) within the acyl CoA oxidase gene promoter. Toxicol. Lett. 1999, 110:119-127.
    • (1999) Toxicol. Lett. , vol.110 , pp. 119-127
    • Lambe, K.G.1    Woodyatt, N.J.2    Macdonald, N.3    Chevalier, S.4    Roberts, R.A.5
  • 100
    • 0034678015 scopus 로고    scopus 로고
    • Suppression of mouse hepatocyte apoptosis by peroxisome proliferators: role of PPARalpha and TNFalpha
    • Hasmall S.C., James N.H., Macdonald N., Gonzalez F.J., Peters J.M., Roberts R.A. Suppression of mouse hepatocyte apoptosis by peroxisome proliferators: role of PPARalpha and TNFalpha. Mutat. Res. 2000, 448:193-200.
    • (2000) Mutat. Res. , vol.448 , pp. 193-200
    • Hasmall, S.C.1    James, N.H.2    Macdonald, N.3    Gonzalez, F.J.4    Peters, J.M.5    Roberts, R.A.6
  • 101
    • 33748422385 scopus 로고    scopus 로고
    • Differential regulation of the cynomolgus, human, and rat acyl-CoA oxidase promoters by PPARalpha
    • Kane C.D., Francone O.L., Stevens K.A. Differential regulation of the cynomolgus, human, and rat acyl-CoA oxidase promoters by PPARalpha. Gene 2006, 380:84-94.
    • (2006) Gene , vol.380 , pp. 84-94
    • Kane, C.D.1    Francone, O.L.2    Stevens, K.A.3
  • 102
    • 0035943681 scopus 로고    scopus 로고
    • Differential gene regulation in human versus rodent hepatocytes by peroxisome proliferator-activated receptor (PPAR) alpha. PPAR alpha fails to induce peroxisome proliferation-associated genes in human cells independently of the level of receptor expression
    • Lawrence J.W., Li Y., Chen S., DeLuca J.G., Berger J.P., Umbenhauer D.R., Moller D.E., Zhou G. Differential gene regulation in human versus rodent hepatocytes by peroxisome proliferator-activated receptor (PPAR) alpha. PPAR alpha fails to induce peroxisome proliferation-associated genes in human cells independently of the level of receptor expression. J. Biol. Chem. 2001, 276:31521-31527.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31521-31527
    • Lawrence, J.W.1    Li, Y.2    Chen, S.3    DeLuca, J.G.4    Berger, J.P.5    Umbenhauer, D.R.6    Moller, D.E.7    Zhou, G.8
  • 103
    • 0035958960 scopus 로고    scopus 로고
    • Identification of peroxisome proliferator-responsive human genes by elevated expression of the peroxisome proliferator-activated receptor alpha in HepG2 cells
    • Hsu M.H., Savas U., Griffin K.J., Johnson E.F. Identification of peroxisome proliferator-responsive human genes by elevated expression of the peroxisome proliferator-activated receptor alpha in HepG2 cells. J. Biol. Chem. 2001, 276:27950-27958.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27950-27958
    • Hsu, M.H.1    Savas, U.2    Griffin, K.J.3    Johnson, E.F.4
  • 104
    • 0034678013 scopus 로고    scopus 로고
    • Hydrogen peroxide generation in peroxisome proliferator-induced oncogenesis
    • Yeldandi A.V., Rao M.S., Reddy J.K. Hydrogen peroxide generation in peroxisome proliferator-induced oncogenesis. Mutat. Res. 2000, 448:159-177.
    • (2000) Mutat. Res. , vol.448 , pp. 159-177
    • Yeldandi, A.V.1    Rao, M.S.2    Reddy, J.K.3
  • 105
    • 0031781381 scopus 로고    scopus 로고
    • Role of peroxisome proliferator-activated receptor alpha in altered cell cycle regulation in mouse liver
    • Peters J.M., Aoyama T., Cattley R.C., Nobumitsu U., Hashimoto T., Gonzalez F.J. Role of peroxisome proliferator-activated receptor alpha in altered cell cycle regulation in mouse liver. Carcinogenesis 1998, 19:1989-1994.
    • (1998) Carcinogenesis , vol.19 , pp. 1989-1994
    • Peters, J.M.1    Aoyama, T.2    Cattley, R.C.3    Nobumitsu, U.4    Hashimoto, T.5    Gonzalez, F.J.6
  • 106
    • 13444311098 scopus 로고    scopus 로고
    • Role of peroxisome proliferator-activated receptor-alpha (PPARalpha) in bezafibrate-induced hepatocarcinogenesis and cholestasis
    • Hays T., Rusyn I., Burns A.M., Kennett M.J., Ward J.M., Gonzalez F.J., Peters J.M. Role of peroxisome proliferator-activated receptor-alpha (PPARalpha) in bezafibrate-induced hepatocarcinogenesis and cholestasis. Carcinogenesis 2005, 26:219-227.
    • (2005) Carcinogenesis , vol.26 , pp. 219-227
    • Hays, T.1    Rusyn, I.2    Burns, A.M.3    Kennett, M.J.4    Ward, J.M.5    Gonzalez, F.J.6    Peters, J.M.7
  • 107
    • 36949024511 scopus 로고    scopus 로고
    • The PPAR alpha-humanized mouse: a model to investigate species differences in liver toxicity mediated by PPAR alpha
    • Yang Q., Nagano T., Shah Y., Cheung C., Ito S., Gonzalez F.J. The PPAR alpha-humanized mouse: a model to investigate species differences in liver toxicity mediated by PPAR alpha. Toxicol. Sci. 2008, 101:132-139.
    • (2008) Toxicol. Sci. , vol.101 , pp. 132-139
    • Yang, Q.1    Nagano, T.2    Shah, Y.3    Cheung, C.4    Ito, S.5    Gonzalez, F.J.6
  • 108
    • 34250163202 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha regulates a microRNA-mediated signaling cascade responsible for hepatocellular proliferation
    • Shah Y.M., Morimura K., Yang Q., Tanabe T., Takagi M., Gonzalez F.J. Peroxisome proliferator-activated receptor alpha regulates a microRNA-mediated signaling cascade responsible for hepatocellular proliferation. Mol. Cell. Biol. 2007, 27:4238-4247.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4238-4247
    • Shah, Y.M.1    Morimura, K.2    Yang, Q.3    Tanabe, T.4    Takagi, M.5    Gonzalez, F.J.6
  • 109
    • 0027245446 scopus 로고
    • Transgenic mouse model for synergistic effects of nuclear oncogenes and growth factors in tumorigenesis: interaction of c-myc and transforming growth factor alpha in hepatic oncogenesis
    • Murakami H., Sanderson N.D., Nagy P., Marino P.A., Merlino G., Thorgeirsson S.S. Transgenic mouse model for synergistic effects of nuclear oncogenes and growth factors in tumorigenesis: interaction of c-myc and transforming growth factor alpha in hepatic oncogenesis. Cancer Res. 1993, 53:1719-1723.
    • (1993) Cancer Res. , vol.53 , pp. 1719-1723
    • Murakami, H.1    Sanderson, N.D.2    Nagy, P.3    Marino, P.A.4    Merlino, G.5    Thorgeirsson, S.S.6
  • 111
    • 0017178194 scopus 로고
    • Cytochemical demonstration of extraperoxisomal catalase. I. Sheep liver
    • Roels F. Cytochemical demonstration of extraperoxisomal catalase. I. Sheep liver. J. Histochem. Cytochem. 1976, 24:713-724.
    • (1976) J. Histochem. Cytochem. , vol.24 , pp. 713-724
    • Roels, F.1
  • 112
    • 0023988178 scopus 로고
    • Catalase in guinea pig hepatocytes is localized in cytoplasm, nuclear matrix and peroxisomes
    • Yamamoto K., Volkl A., Hashimoto T., Fahimi H.D. Catalase in guinea pig hepatocytes is localized in cytoplasm, nuclear matrix and peroxisomes. Eur. J. Cell Biol. 1988, 46:129-135.
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 129-135
    • Yamamoto, K.1    Volkl, A.2    Hashimoto, T.3    Fahimi, H.D.4
  • 113
    • 0023720131 scopus 로고
    • Selective induction of peroxisomal enzymes by the hypolipidemic drug bezafibrate. Detection of modulations by automatic image analysis in conjunction with immunoelectron microscopy and immunoblotting
    • Beier K., Volkl A., Hashimoto T., Fahimi H.D. Selective induction of peroxisomal enzymes by the hypolipidemic drug bezafibrate. Detection of modulations by automatic image analysis in conjunction with immunoelectron microscopy and immunoblotting. Eur. J. Cell Biol. 1988, 46:383-393.
    • (1988) Eur. J. Cell Biol. , vol.46 , pp. 383-393
    • Beier, K.1    Volkl, A.2    Hashimoto, T.3    Fahimi, H.D.4
  • 114
    • 0033551325 scopus 로고    scopus 로고
    • A cytosolic catalase is needed to extend adult lifespan in C. elegans daf-C and clk-1 mutants
    • Taub J., Lau J.F., Ma C., Hahn J.H., Hoque R., Rothblatt J., Chalfie M. A cytosolic catalase is needed to extend adult lifespan in C. elegans daf-C and clk-1 mutants. Nature 1999, 399:162-166.
    • (1999) Nature , vol.399 , pp. 162-166
    • Taub, J.1    Lau, J.F.2    Ma, C.3    Hahn, J.H.4    Hoque, R.5    Rothblatt, J.6    Chalfie, M.7
  • 115
    • 0029869726 scopus 로고    scopus 로고
    • Cytoplasmic and peroxisomal catalases of the guinea pig liver: evidence for two distinct proteins
    • Bulitta C., Ganea C., Fahimi H.D., Volkl A. Cytoplasmic and peroxisomal catalases of the guinea pig liver: evidence for two distinct proteins. Biochim. Biophys. Acta 1996, 1293:55-62.
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 55-62
    • Bulitta, C.1    Ganea, C.2    Fahimi, H.D.3    Volkl, A.4
  • 116
    • 0030931235 scopus 로고    scopus 로고
    • Proliferation of myocardial peroxisomes caused by several agents and conditions
    • Zipper J. Proliferation of myocardial peroxisomes caused by several agents and conditions. J Mol Cell Cardiol 1997, 29:149-161.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 149-161
    • Zipper, J.1
  • 117
    • 0034055373 scopus 로고    scopus 로고
    • Cellular and subcellular localization of catalase in the heart of transgenic mice
    • Zhou Z., Kang Y.J. Cellular and subcellular localization of catalase in the heart of transgenic mice. J. Histochem. Cytochem. 2000, 48:585-594.
    • (2000) J. Histochem. Cytochem. , vol.48 , pp. 585-594
    • Zhou, Z.1    Kang, Y.J.2
  • 120
    • 70449715463 scopus 로고    scopus 로고
    • Reactive oxygen species and peroxisomes: struggling for balance
    • Bonekamp N.A., Volkl A., Fahimi H.D., Schrader M. Reactive oxygen species and peroxisomes: struggling for balance. Biofactors 2009, 35:346-355.
    • (2009) Biofactors , vol.35 , pp. 346-355
    • Bonekamp, N.A.1    Volkl, A.2    Fahimi, H.D.3    Schrader, M.4
  • 123
    • 33745060757 scopus 로고    scopus 로고
    • Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei
    • Colasante C., Ellis M., Ruppert T., Voncken F. Comparative proteomics of glycosomes from bloodstream form and procyclic culture form Trypanosoma brucei brucei. Proteomics 2006, 6:3275-3293.
    • (2006) Proteomics , vol.6 , pp. 3275-3293
    • Colasante, C.1    Ellis, M.2    Ruppert, T.3    Voncken, F.4
  • 124
    • 0023895045 scopus 로고
    • Cytoplasmic organelles of trypanosomatids: a cytochemical and stereological study
    • Soares M.J., De Souza W. Cytoplasmic organelles of trypanosomatids: a cytochemical and stereological study. J. Submicrosc. Cytol. Pathol. 1988, 20:349-361.
    • (1988) J. Submicrosc. Cytol. Pathol. , vol.20 , pp. 349-361
    • Soares, M.J.1    De Souza, W.2
  • 127
    • 0014288490 scopus 로고
    • The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions
    • Leighton F., Poole B., Beaufay H., Baudhuin P., Coffey J.W., Fowler S., De Duve C. The large-scale separation of peroxisomes, mitochondria, and lysosomes from the livers of rats injected with triton WR-1339. Improved isolation procedures, automated analysis, biochemical and morphological properties of fractions. J. Cell Biol. 1968, 37:482-513.
    • (1968) J. Cell Biol. , vol.37 , pp. 482-513
    • Leighton, F.1    Poole, B.2    Beaufay, H.3    Baudhuin, P.4    Coffey, J.W.5    Fowler, S.6    De Duve, C.7
  • 128
    • 0013788558 scopus 로고
    • Combined biochemical and morphological study of particulate fractions from rat liver. Analysis of preparations enriched in lysosomes or in particles containing urate oxidase, d-amino acid oxidase, and catalase
    • Baudhuin P., Beaufay H., De Duve C. Combined biochemical and morphological study of particulate fractions from rat liver. Analysis of preparations enriched in lysosomes or in particles containing urate oxidase, d-amino acid oxidase, and catalase. J. Cell Biol. 1965, 26:219-243.
    • (1965) J. Cell Biol. , vol.26 , pp. 219-243
    • Baudhuin, P.1    Beaufay, H.2    De Duve, C.3
  • 131
    • 0028108409 scopus 로고
    • Glycine and taurine conjugation of bile acids by a single enzyme
    • Falany C.N., Johnson M.R., Barnes S., Diasio R.B. Glycine and taurine conjugation of bile acids by a single enzyme. J. Biol. Chem. 1994, 269:19375-19379.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19375-19379
    • Falany, C.N.1    Johnson, M.R.2    Barnes, S.3    Diasio, R.B.4
  • 132
    • 0345861749 scopus 로고    scopus 로고
    • Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization
    • He D., Barnes S., Falany C.N. Rat liver bile acid CoA:amino acid N-acyltransferase: expression, characterization, and peroxisomal localization. J. Lipid Res. 2003, 44:2242-2249.
    • (2003) J. Lipid Res. , vol.44 , pp. 2242-2249
    • He, D.1    Barnes, S.2    Falany, C.N.3
  • 134
    • 0019297785 scopus 로고
    • The activities of peroxisomal oxidases in periportal and perivenous zones of the rat liver acinus
    • Le Hir M., Dubach U.C. The activities of peroxisomal oxidases in periportal and perivenous zones of the rat liver acinus. Histochemistry 1980, 69:95-99.
    • (1980) Histochemistry , vol.69 , pp. 95-99
    • Le Hir, M.1    Dubach, U.C.2
  • 135
    • 0023868377 scopus 로고
    • Heterogenous staining of d-amino acid oxidase in peroxisomes of rat liver and kidney. A light and electron microscopic study
    • Angermuller S., Fahimi H.D. Heterogenous staining of d-amino acid oxidase in peroxisomes of rat liver and kidney. A light and electron microscopic study. Histochemistry 1988, 88:277-285.
    • (1988) Histochemistry , vol.88 , pp. 277-285
    • Angermuller, S.1    Fahimi, H.D.2
  • 136
    • 0024422138 scopus 로고
    • Peroxisomal oxidases: cytochemical localization and biological relevance
    • Angermuller S. Peroxisomal oxidases: cytochemical localization and biological relevance. Prog. Histochem. Cytochem. 1989, 20:1-65.
    • (1989) Prog. Histochem. Cytochem. , vol.20 , pp. 1-65
    • Angermuller, S.1
  • 137
    • 0029740595 scopus 로고    scopus 로고
    • In situ heterogeneity of peroxisomal oxidase activities: an update
    • Van den Munckhof R.J. In situ heterogeneity of peroxisomal oxidase activities: an update. Histochem. J. 1996, 28:401-429.
    • (1996) Histochem. J. , vol.28 , pp. 401-429
    • Van den Munckhof, R.J.1
  • 138
    • 73649083005 scopus 로고    scopus 로고
    • Peroxisomes from the heavy mitochondrial fraction: isolation by zonal free flow electrophoresis and quantitative mass spectrometrical characterization
    • Islinger M., Li K.W., Loos M., Liebler S., Angermuller S., Eckerskorn C., Weber G., Abdolzade A., Volkl A. Peroxisomes from the heavy mitochondrial fraction: isolation by zonal free flow electrophoresis and quantitative mass spectrometrical characterization. J. Proteome Res. 2010, 9:113-124.
    • (2010) J. Proteome Res. , vol.9 , pp. 113-124
    • Islinger, M.1    Li, K.W.2    Loos, M.3    Liebler, S.4    Angermuller, S.5    Eckerskorn, C.6    Weber, G.7    Abdolzade, A.8    Volkl, A.9
  • 139
    • 77953716605 scopus 로고
    • Correlation of ultrastructural organization and function in normal and experimentally controlled changes of proximal convoluted tubule cells of the mouse kidney, in: PhD Thesis, Stockholm.
    • J. Rhodin, Correlation of ultrastructural organization and function in normal and experimentally controlled changes of proximal convoluted tubule cells of the mouse kidney, in: PhD Thesis, Stockholm, 1954.
    • (1954)
    • Rhodin, J.1
  • 141
    • 36649014013 scopus 로고    scopus 로고
    • Peroxisomes in human and mouse testis: differential expression of peroxisomal proteins in germ cells and distinct somatic cell types of the testis
    • Nenicu A., Luers G.H., Kovacs W., David M., Zimmer A., Bergmann M., Baumgart-Vogt E. Peroxisomes in human and mouse testis: differential expression of peroxisomal proteins in germ cells and distinct somatic cell types of the testis. Biol. Reprod. 2007, 77:1060-1072.
    • (2007) Biol. Reprod. , vol.77 , pp. 1060-1072
    • Nenicu, A.1    Luers, G.H.2    Kovacs, W.3    David, M.4    Zimmer, A.5    Bergmann, M.6    Baumgart-Vogt, E.7
  • 142
    • 0022592886 scopus 로고
    • Isolation and characterization of peroxisomes from the renal cortex of beef, sheep, and cat
    • Zaar K., Volkl A., Fahimi H.D. Isolation and characterization of peroxisomes from the renal cortex of beef, sheep, and cat. Eur. J. Cell Biol. 1986, 40:16-24.
    • (1986) Eur. J. Cell Biol. , vol.40 , pp. 16-24
    • Zaar, K.1    Volkl, A.2    Fahimi, H.D.3
  • 143
    • 0025897213 scopus 로고
    • Purification of marginal plates from bovine renal peroxisomes: identification with l-alpha-hydroxyacid oxidase B
    • Zaar K., Volkl A., Fahimi H.D. Purification of marginal plates from bovine renal peroxisomes: identification with l-alpha-hydroxyacid oxidase B. J. Cell Biol. 1991, 113:113-121.
    • (1991) J. Cell Biol. , vol.113 , pp. 113-121
    • Zaar, K.1    Volkl, A.2    Fahimi, H.D.3
  • 144
    • 0025829613 scopus 로고
    • Immunoelectron microscopic localization of the isozymes of l-alpha-hydroxyacid oxidase in renal peroxisomes of beef and sheep: evidence of distinct intraorganellar subcompartmentation
    • Zaar K., Fahimi H.D. Immunoelectron microscopic localization of the isozymes of l-alpha-hydroxyacid oxidase in renal peroxisomes of beef and sheep: evidence of distinct intraorganellar subcompartmentation. J. Histochem. Cytochem. 1991, 39:801-808.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 801-808
    • Zaar, K.1    Fahimi, H.D.2
  • 145
    • 0028981066 scopus 로고
    • Immunocytochemical localization of l-alpha-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney
    • Yokota S., Hashimoto T. Immunocytochemical localization of l-alpha-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney. Histochem. Cell Biol. 1995, 104:55-61.
    • (1995) Histochem. Cell Biol. , vol.104 , pp. 55-61
    • Yokota, S.1    Hashimoto, T.2
  • 146
    • 0016007675 scopus 로고
    • Alpha-hydroxyacid oxidase genetics in the mouse: evidence for two genetic loci and a tetrameric subunit structure for the liver isozyme
    • Duley J., Holmes R.S. Alpha-hydroxyacid oxidase genetics in the mouse: evidence for two genetic loci and a tetrameric subunit structure for the liver isozyme. Genetics 1974, 76:93-97.
    • (1974) Genetics , vol.76 , pp. 93-97
    • Duley, J.1    Holmes, R.S.2
  • 147
    • 0034725053 scopus 로고    scopus 로고
    • Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases
    • Jones J.M., Morrell J.C., Gould S.J. Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J. Biol. Chem. 2000, 275:12590-12597.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12590-12597
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 149
    • 0014682271 scopus 로고
    • Localization of short and long chain l-alpha-hydroxyacid oxidases in peroxisomes of hog kidney
    • Saga M., Tsutsumi Y., Nakano M. Localization of short and long chain l-alpha-hydroxyacid oxidases in peroxisomes of hog kidney. Biochim. Biophys. Acta 1969, 184:213-215.
    • (1969) Biochim. Biophys. Acta , vol.184 , pp. 213-215
    • Saga, M.1    Tsutsumi, Y.2    Nakano, M.3
  • 150
    • 0022964323 scopus 로고
    • Electron microscopic cytochemical localization of alpha-hydroxyacid oxidase in rat liver. Association with the crystalline core and matrix of peroxisomes
    • Angermuller S., Leupold C., Volkl A., Fahimi H.D. Electron microscopic cytochemical localization of alpha-hydroxyacid oxidase in rat liver. Association with the crystalline core and matrix of peroxisomes. Histochemistry 1986, 85:403-409.
    • (1986) Histochemistry , vol.85 , pp. 403-409
    • Angermuller, S.1    Leupold, C.2    Volkl, A.3    Fahimi, H.D.4
  • 151
    • 0021808186 scopus 로고
    • Comparison of the activities of some peroxisomal and extraperoxisomal lipid-metabolizing enzymes in liver and extrahepatic tissues of the rat
    • Van Veldhoven P., Mannaerts G.P. Comparison of the activities of some peroxisomal and extraperoxisomal lipid-metabolizing enzymes in liver and extrahepatic tissues of the rat. Biochem. J. 1985, 227:737-741.
    • (1985) Biochem. J. , vol.227 , pp. 737-741
    • Van Veldhoven, P.1    Mannaerts, G.P.2
  • 152
    • 0023179622 scopus 로고
    • Immunoelectron microscopic localization of d-amino acid oxidase in rat kidney and liver
    • Perotti M.E., Gavazzi E., Trussardo L., Malgaretti N., Curti B. Immunoelectron microscopic localization of d-amino acid oxidase in rat kidney and liver. Histochem. J. 1987, 19:157-169.
    • (1987) Histochem. J. , vol.19 , pp. 157-169
    • Perotti, M.E.1    Gavazzi, E.2    Trussardo, L.3    Malgaretti, N.4    Curti, B.5
  • 153
    • 0022394808 scopus 로고
    • Luminometric determination of oxidase activity in peroxisomal fractions of rat liver: glycolate oxidase
    • Leupold C., Volkl A., Fahimi H.D. Luminometric determination of oxidase activity in peroxisomal fractions of rat liver: glycolate oxidase. Anal. Biochem. 1985, 151:63-69.
    • (1985) Anal. Biochem. , vol.151 , pp. 63-69
    • Leupold, C.1    Volkl, A.2    Fahimi, H.D.3
  • 154
    • 0022975970 scopus 로고
    • Immunocytochemical localization of d-amino acid oxidase in the central clear matrix of rat kidney peroxisomes
    • Usuda N., Yokota S., Hashimoto T., Nagata T. Immunocytochemical localization of d-amino acid oxidase in the central clear matrix of rat kidney peroxisomes. J. Histochem. Cytochem. 1986, 34:1709-1718.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1709-1718
    • Usuda, N.1    Yokota, S.2    Hashimoto, T.3    Nagata, T.4
  • 155
    • 0024370864 scopus 로고
    • D-Aspartate oxidase in rat, bovine and sheep kidney cortex is localized in peroxisomes
    • Zaar K., Volkl A., Fahimi H.D. d-Aspartate oxidase in rat, bovine and sheep kidney cortex is localized in peroxisomes. Biochem. J. 1989, 261:233-238.
    • (1989) Biochem. J. , vol.261 , pp. 233-238
    • Zaar, K.1    Volkl, A.2    Fahimi, H.D.3
  • 156
    • 0025977764 scopus 로고
    • D-Aspartate oxidase, a peroxisomal enzyme in liver of rat and man
    • Van Veldhoven P.P., Brees C., Mannaerts G.P. d-Aspartate oxidase, a peroxisomal enzyme in liver of rat and man. Biochim. Biophys. Acta 1991, 1073:203-208.
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 203-208
    • Van Veldhoven, P.P.1    Brees, C.2    Mannaerts, G.P.3
  • 157
    • 50549099422 scopus 로고    scopus 로고
    • D-Amino acids in the brain: d-serine in neurotransmission and neurodegeneration
    • Wolosker H., Dumin E., Balan L., Foltyn V.N. d-Amino acids in the brain: d-serine in neurotransmission and neurodegeneration. FEBS J. 2008, 275:3514-3526.
    • (2008) FEBS J. , vol.275 , pp. 3514-3526
    • Wolosker, H.1    Dumin, E.2    Balan, L.3    Foltyn, V.N.4
  • 158
    • 77953721494 scopus 로고    scopus 로고
    • Persistent increase of d-aspartate in d-aspartate oxidase mutant mice induces a precocious hippocampal age-dependent synaptic plasticity and spatial memory decay, Neurobiol Aging, [Electronic publication].
    • F. Errico, R. Nistico, F. Napolitano, A.B. Oliva, R. Romano, F. Barbieri, T. Florio, C. Russo, N.B. Mercuri, A. Usiello, Persistent increase of d-aspartate in d-aspartate oxidase mutant mice induces a precocious hippocampal age-dependent synaptic plasticity and spatial memory decay, Neurobiol Aging, (2009) [Electronic publication].
    • (2009)
    • Errico F1    Nistico R2    Napolitano F3    Oliva A.B4    Romano R5    Barbieri F6    Florio T7    Russo C8    Mercuri N.B9    Usiello A10
  • 159
    • 24944498795 scopus 로고    scopus 로고
    • Free d-aspartate in mammals
    • Furuchi T., Homma H. Free d-aspartate in mammals. Biol. Pharm. Bull. 2005, 28:1566-1570.
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 1566-1570
    • Furuchi, T.1    Homma, H.2
  • 161
    • 0034810498 scopus 로고    scopus 로고
    • Cloning, mapping, genomic organization, and expression of mouse M-LP, a new member of the peroxisomal membrane protein Mpv17 domain family
    • Iida R., Yasuda T., Tsubota E., Matsuki T., Kishi K. Cloning, mapping, genomic organization, and expression of mouse M-LP, a new member of the peroxisomal membrane protein Mpv17 domain family. Biochem. Biophys. Res. Commun. 2001, 283:292-296.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 292-296
    • Iida, R.1    Yasuda, T.2    Tsubota, E.3    Matsuki, T.4    Kishi, K.5
  • 162
    • 0037458610 scopus 로고    scopus 로고
    • M-LP, Mpv17-like protein, has a peroxisomal membrane targeting signal comprising a transmembrane domain and a positively charged loop and up-regulates expression of the manganese superoxide dismutase gene
    • Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T., Kishi K. M-LP, Mpv17-like protein, has a peroxisomal membrane targeting signal comprising a transmembrane domain and a positively charged loop and up-regulates expression of the manganese superoxide dismutase gene. J. Biol. Chem. 2003, 278:6301-6306.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6301-6306
    • Iida, R.1    Yasuda, T.2    Tsubota, E.3    Takatsuka, H.4    Masuyama, M.5    Matsuki, T.6    Kishi, K.7
  • 163
    • 52949142730 scopus 로고    scopus 로고
    • Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease
    • Krick S., Shi S., Ju W., Faul C., Tsai S.Y., Mundel P., Bottinger E.P. Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:14106-14111.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14106-14111
    • Krick, S.1    Shi, S.2    Ju, W.3    Faul, C.4    Tsai, S.Y.5    Mundel, P.6    Bottinger, E.P.7
  • 164
    • 0015334792 scopus 로고
    • Peroxisomes in absorptive cells of mammalian small intestine
    • Novikoff P.M., Novikoff A.B. Peroxisomes in absorptive cells of mammalian small intestine. J. Cell Biol. 1972, 53:532-560.
    • (1972) J. Cell Biol. , vol.53 , pp. 532-560
    • Novikoff, P.M.1    Novikoff, A.B.2
  • 165
    • 0016364739 scopus 로고
    • A zonal rotor method for the preparation of microperoxisomes from epithelial cells of guinea pig small intestine
    • Connock M.J., Kirk P.R., Sturdee A.P. A zonal rotor method for the preparation of microperoxisomes from epithelial cells of guinea pig small intestine. J. Cell Biol. 1974, 61:123-133.
    • (1974) J. Cell Biol. , vol.61 , pp. 123-133
    • Connock, M.J.1    Kirk, P.R.2    Sturdee, A.P.3
  • 166
    • 0020508163 scopus 로고
    • Localization of carnitine acyltransferases and acyl-CoA beta-oxidation enzymes in small intestinal microperoxisomes (peroxisomes) of normal and clofibrate treated mice
    • Small G.M., Burdett K., Connock M.J. Localization of carnitine acyltransferases and acyl-CoA beta-oxidation enzymes in small intestinal microperoxisomes (peroxisomes) of normal and clofibrate treated mice. Biochem. Int. 1983, 7:263-272.
    • (1983) Biochem. Int. , vol.7 , pp. 263-272
    • Small, G.M.1    Burdett, K.2    Connock, M.J.3
  • 167
    • 0028806411 scopus 로고
    • The immunohistochemical localization of the non-specific lipid transfer protein (sterol carrier protein-2) in rat small intestine enterocytes
    • Wouters F.S., Markman M., de Graaf P., Hauser H., Tabak H.F., Wirtz K.W., Moorman A.F. The immunohistochemical localization of the non-specific lipid transfer protein (sterol carrier protein-2) in rat small intestine enterocytes. Biochim. Biophys. Acta 1995, 1259:192-196.
    • (1995) Biochim. Biophys. Acta , vol.1259 , pp. 192-196
    • Wouters, F.S.1    Markman, M.2    de Graaf, P.3    Hauser, H.4    Tabak, H.F.5    Wirtz, K.W.6    Moorman, A.F.7
  • 168
    • 0031909446 scopus 로고    scopus 로고
    • Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase
    • Tappia P.S., Jones C.J., Connock M.J. Purification of guinea pig small intestinal peroxisomes and the subcellular localization of glucose-6-phosphate dehydrogenase. Mol. Cell. Biochem. 1998, 179:13-20.
    • (1998) Mol. Cell. Biochem. , vol.179 , pp. 13-20
    • Tappia, P.S.1    Jones, C.J.2    Connock, M.J.3
  • 169
    • 0024819223 scopus 로고
    • Enzymes of plasmalogen biosynthesis in microperoxisomes of guinea-pig intestinal mucosa
    • Gitsham A.M., Burdett K., Tappia P.S., Connock M.J., Johnson P. Enzymes of plasmalogen biosynthesis in microperoxisomes of guinea-pig intestinal mucosa. Biochem. Soc. Trans. 1989, 17:1074-1075.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 1074-1075
    • Gitsham, A.M.1    Burdett, K.2    Tappia, P.S.3    Connock, M.J.4    Johnson, P.5
  • 170
    • 0026525267 scopus 로고
    • Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate
    • Ruyter B., Lund J.S., Thomassen M.S., Christiansen E.N. Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate. Biochem. J. 1992, 282(Pt 2):565-570.
    • (1992) Biochem. J. , vol.282 , Issue.PART 2 , pp. 565-570
    • Ruyter, B.1    Lund, J.S.2    Thomassen, M.S.3    Christiansen, E.N.4
  • 171
    • 0025779114 scopus 로고
    • Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells
    • Burdett K., Larkins L.K., Das A.K., Hajra A.K. Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells. J. Biol. Chem. 1991, 266:12201-12206.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12201-12206
    • Burdett, K.1    Larkins, L.K.2    Das, A.K.3    Hajra, A.K.4
  • 172
    • 0025738191 scopus 로고
    • Immunoelectron microscopic evidence for organ differences in the composition of peroxisome-specific membrane polypeptides among three rat organs: liver, kidney, and small intestine
    • Usuda N., Kuwabara T., Ichikawa R., Hashimoto T., Nagata T. Immunoelectron microscopic evidence for organ differences in the composition of peroxisome-specific membrane polypeptides among three rat organs: liver, kidney, and small intestine. J. Histochem. Cytochem. 1991, 39:1357-1366.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1357-1366
    • Usuda, N.1    Kuwabara, T.2    Ichikawa, R.3    Hashimoto, T.4    Nagata, T.5
  • 173
    • 0037128209 scopus 로고    scopus 로고
    • PEX11 promotes peroxisome division independently of peroxisome metabolism
    • Li X., Gould S.J. PEX11 promotes peroxisome division independently of peroxisome metabolism. J. Cell Biol. 2002, 156:643-651.
    • (2002) J. Cell Biol. , vol.156 , pp. 643-651
    • Li, X.1    Gould, S.J.2
  • 174
    • 0017078733 scopus 로고
    • Response of microperoxisomes in rat small intestinal mucosa to CPIB, a hypolipidemic drug
    • Svoboda D.J. Response of microperoxisomes in rat small intestinal mucosa to CPIB, a hypolipidemic drug. Biochem. Pharmacol. 1976, 25:2750-2752.
    • (1976) Biochem. Pharmacol. , vol.25 , pp. 2750-2752
    • Svoboda, D.J.1
  • 179
    • 0027385504 scopus 로고
    • Peroxisomes and peroxisomal enzymes along the crypt-villus axis of the rat intestine
    • Cable S., Kedinger M., Dauca M. Peroxisomes and peroxisomal enzymes along the crypt-villus axis of the rat intestine. Differentiation 1993, 54:99-108.
    • (1993) Differentiation , vol.54 , pp. 99-108
    • Cable, S.1    Kedinger, M.2    Dauca, M.3
  • 180
    • 0033998709 scopus 로고    scopus 로고
    • Peroxisome distribution along the crypt-villus axis of the guinea pig small intestine
    • Phipps A.N., Connock M.J., Johnson P., Burdett K. Peroxisome distribution along the crypt-villus axis of the guinea pig small intestine. Mol. Cell. Biochem. 2000, 203:119-126.
    • (2000) Mol. Cell. Biochem. , vol.203 , pp. 119-126
    • Phipps, A.N.1    Connock, M.J.2    Johnson, P.3    Burdett, K.4
  • 181
    • 0030779161 scopus 로고    scopus 로고
    • Detection of mRNAs encoding peroxisomal proteins by non-radioactive in situ hybridization with digoxigenin-labelled cRNAs
    • Baumgart E., Schad A., Volkl A., Fahimi H.D. Detection of mRNAs encoding peroxisomal proteins by non-radioactive in situ hybridization with digoxigenin-labelled cRNAs. Histochem. Cell Biol. 1997, 108:371-379.
    • (1997) Histochem. Cell Biol. , vol.108 , pp. 371-379
    • Baumgart, E.1    Schad, A.2    Volkl, A.3    Fahimi, H.D.4
  • 182
    • 19244374483 scopus 로고    scopus 로고
    • Expression of peroxisomal proteins provides clear evidence for the presence of peroxisomes in the male germ cell line GC1spg
    • Luers G.H., Schad A., Fahimi H.D., Volkl A., Seitz J. Expression of peroxisomal proteins provides clear evidence for the presence of peroxisomes in the male germ cell line GC1spg. Cytogenet. Genome Res. 2003, 103:360-365.
    • (2003) Cytogenet. Genome Res. , vol.103 , pp. 360-365
    • Luers, G.H.1    Schad, A.2    Fahimi, H.D.3    Volkl, A.4    Seitz, J.5
  • 183
    • 33646871371 scopus 로고    scopus 로고
    • Peroxisomes are present in murine spermatogonia and disappear during the course of spermatogenesis
    • Luers G.H., Thiele S., Schad A., Volkl A., Yokota S., Seitz J. Peroxisomes are present in murine spermatogonia and disappear during the course of spermatogenesis. Histochem. Cell Biol. 2006, 125:693-703.
    • (2006) Histochem. Cell Biol. , vol.125 , pp. 693-703
    • Luers, G.H.1    Thiele, S.2    Schad, A.3    Volkl, A.4    Yokota, S.5    Seitz, J.6
  • 184
    • 33645877112 scopus 로고    scopus 로고
    • Peroxisomal multifunctional protein 2 is essential for lipid homeostasis in Sertoli cells and male fertility in mice
    • Huyghe S., Schmalbruch H., De Gendt K., Verhoeven G., Guillou F., Van Veldhoven P.P., Baes M. Peroxisomal multifunctional protein 2 is essential for lipid homeostasis in Sertoli cells and male fertility in mice. Endocrinology 2006, 147:2228-2236.
    • (2006) Endocrinology , vol.147 , pp. 2228-2236
    • Huyghe, S.1    Schmalbruch, H.2    De Gendt, K.3    Verhoeven, G.4    Guillou, F.5    Van Veldhoven, P.P.6    Baes, M.7
  • 185
    • 0019431106 scopus 로고
    • The testis in adreno-leukodystrophy
    • Powers J.M., Schaumburg H.H. The testis in adreno-leukodystrophy. Am. J. Pathol. 1981, 102:90-98.
    • (1981) Am. J. Pathol. , vol.102 , pp. 90-98
    • Powers, J.M.1    Schaumburg, H.H.2
  • 187
    • 0344874713 scopus 로고    scopus 로고
    • Antisteroidogenic actions of hydrogen peroxide on rat Leydig cells
    • Tsai S.C., Lu C.C., Lin C.S., Wang P.S. Antisteroidogenic actions of hydrogen peroxide on rat Leydig cells. J. Cell Biochem. 2003, 90:1276-1286.
    • (2003) J. Cell Biochem. , vol.90 , pp. 1276-1286
    • Tsai, S.C.1    Lu, C.C.2    Lin, C.S.3    Wang, P.S.4
  • 188
    • 0026506986 scopus 로고
    • Sterol carrier protein 2 (non-specific lipid transfer protein) is localized in membranous fractions of Leydig cells and Sertoli cells but not in germ cells
    • van Haren L., Teerds K.J., Ossendorp B.C., van Heusden G.P., Orly J., Stocco D.M., Wirtz K.W., Rommerts F.F. Sterol carrier protein 2 (non-specific lipid transfer protein) is localized in membranous fractions of Leydig cells and Sertoli cells but not in germ cells. Biochim. Biophys. Acta 1992, 1124:288-296.
    • (1992) Biochim. Biophys. Acta , vol.1124 , pp. 288-296
    • van Haren, L.1    Teerds, K.J.2    Ossendorp, B.C.3    van Heusden, G.P.4    Orly, J.5    Stocco, D.M.6    Wirtz, K.W.7    Rommerts, F.F.8
  • 189
    • 0030746701 scopus 로고    scopus 로고
    • Luteinizing hormone on Leydig cell structure and function
    • Mendis-Handagama S.M. Luteinizing hormone on Leydig cell structure and function. Histol. Histopathol. 1997, 12:869-882.
    • (1997) Histol. Histopathol. , vol.12 , pp. 869-882
    • Mendis-Handagama, S.M.1
  • 190
    • 0034026621 scopus 로고    scopus 로고
    • Peroxisomes and intracellular cholesterol trafficking in adult rat Leydig cells following Luteinizing hormone stimulation
    • Mendis-Handagama S.M. Peroxisomes and intracellular cholesterol trafficking in adult rat Leydig cells following Luteinizing hormone stimulation. Tissue Cell 2000, 32:102-106.
    • (2000) Tissue Cell , vol.32 , pp. 102-106
    • Mendis-Handagama, S.M.1
  • 191
    • 77951665500 scopus 로고    scopus 로고
    • , Muralidhara, D-Aspartic acid induced oxidative stress and mitochondrial dysfunctions in testis of prepubertal rats
    • Chandrashekar K.N. , Muralidhara, D-Aspartic acid induced oxidative stress and mitochondrial dysfunctions in testis of prepubertal rats. , Amino Acids 2010, 38:817-827.
    • (2010) , Amino Acids , vol.38 , pp. 817-827
    • Chandrashekar, K.N.1
  • 192
    • 0033305736 scopus 로고    scopus 로고
    • Expression of peroxisome proliferator-activated receptor alpha messenger ribonucleic acid and protein in human and rat testis
    • Schultz R., Yan W., Toppari J., Volkl A., Gustafsson J.A., Pelto-Huikko M. Expression of peroxisome proliferator-activated receptor alpha messenger ribonucleic acid and protein in human and rat testis. Endocrinology 1999, 140:2968-2975.
    • (1999) Endocrinology , vol.140 , pp. 2968-2975
    • Schultz, R.1    Yan, W.2    Toppari, J.3    Volkl, A.4    Gustafsson, J.A.5    Pelto-Huikko, M.6
  • 196
    • 0016229231 scopus 로고
    • Microbodies (peroxisomes) containing catalase in myocardium: morphological and biochemical evidence
    • Herzog V., Fahimi H.D. Microbodies (peroxisomes) containing catalase in myocardium: morphological and biochemical evidence. Science 1974, 185:271-273.
    • (1974) Science , vol.185 , pp. 271-273
    • Herzog, V.1    Fahimi, H.D.2
  • 197
    • 0017352772 scopus 로고
    • Peroxisomes (microbodies) in the myocardium of rodents and primates. A comparative ultrastructural cytochemical study
    • Hicks L., Fahimi H.D. Peroxisomes (microbodies) in the myocardium of rodents and primates. A comparative ultrastructural cytochemical study. Cell Tissue Res. 1977, 175:467-481.
    • (1977) Cell Tissue Res. , vol.175 , pp. 467-481
    • Hicks, L.1    Fahimi, H.D.2
  • 198
    • 0020966159 scopus 로고
    • Detection of acyl-CoA beta-oxidation enzymes in peroxisomes (microperoxisomes) of mouse heart
    • Connock M.J., Perry S.R. Detection of acyl-CoA beta-oxidation enzymes in peroxisomes (microperoxisomes) of mouse heart. Biochem. Int. 1983, 6:545-551.
    • (1983) Biochem. Int. , vol.6 , pp. 545-551
    • Connock, M.J.1    Perry, S.R.2
  • 199
    • 0035988932 scopus 로고    scopus 로고
    • Mouse PeP: a novel peroxisomal protein linked to myoblast differentiation and development
    • Ferrer-Martinez A., Ruiz-Lozano P., Chien K.R. Mouse PeP: a novel peroxisomal protein linked to myoblast differentiation and development. Dev. Dyn. 2002, 224:154-167.
    • (2002) Dev. Dyn. , vol.224 , pp. 154-167
    • Ferrer-Martinez, A.1    Ruiz-Lozano, P.2    Chien, K.R.3
  • 200
    • 0025067467 scopus 로고
    • Peroxisomes of the rat cardiac and soleus muscles increase after starvation. A biochemical and immunocytochemical study
    • Yokota S., Asayama K. Peroxisomes of the rat cardiac and soleus muscles increase after starvation. A biochemical and immunocytochemical study. Histochemistry 1990, 93:287-293.
    • (1990) Histochemistry , vol.93 , pp. 287-293
    • Yokota, S.1    Asayama, K.2
  • 201
    • 0027092977 scopus 로고
    • Proliferation of myocardial peroxisomes in experimental rat diabetes: a biochemical and immunocytochemical study
    • Yokota S., Asayama K. Proliferation of myocardial peroxisomes in experimental rat diabetes: a biochemical and immunocytochemical study. Virchows Arch. B. Cell Pathol. Incl. Mol. Pathol. 1992, 63:43-49.
    • (1992) Virchows Arch. B. Cell Pathol. Incl. Mol. Pathol. , vol.63 , pp. 43-49
    • Yokota, S.1    Asayama, K.2
  • 202
    • 0028173462 scopus 로고
    • The peroxisomal beta-oxidation enzyme system of rat heart. Basal level and effect of the peroxisome proliferator clofibrate
    • Kvannes J., Eikhom T.S., Flatmark T. The peroxisomal beta-oxidation enzyme system of rat heart. Basal level and effect of the peroxisome proliferator clofibrate. Biochim. Biophys. Acta 1994, 1201:203-216.
    • (1994) Biochim. Biophys. Acta , vol.1201 , pp. 203-216
    • Kvannes, J.1    Eikhom, T.S.2    Flatmark, T.3
  • 204
    • 0038279877 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of catalase rescues ventricular myocytes from ethanol-induced cardiac contractile defect
    • Zhang X., Klein A.L., Alberle N.S., Norby F.L., Ren B.H., Duan J., Ren J. Cardiac-specific overexpression of catalase rescues ventricular myocytes from ethanol-induced cardiac contractile defect. J. Mol. Cell Cardiol. 2003, 35:645-652.
    • (2003) J. Mol. Cell Cardiol. , vol.35 , pp. 645-652
    • Zhang, X.1    Klein, A.L.2    Alberle, N.S.3    Norby, F.L.4    Ren, B.H.5    Duan, J.6    Ren, J.7
  • 206
    • 0019779214 scopus 로고
    • Impaired myocardial performance and response to calcium in experimental alcoholic cardiomyopathy
    • Kino M., Thorp K.A., Bing O.H., Abelmann W.H. Impaired myocardial performance and response to calcium in experimental alcoholic cardiomyopathy. J. Mol. Cell Cardiol. 1981, 13:981-989.
    • (1981) J. Mol. Cell Cardiol. , vol.13 , pp. 981-989
    • Kino, M.1    Thorp, K.A.2    Bing, O.H.3    Abelmann, W.H.4
  • 207
    • 0023228910 scopus 로고
    • Effect of chronic ethanol treatment on peroxisomal acyl-CoA oxidase activity and lipid peroxidation in rat liver and heart
    • Panchenko L.F., Pirozhkov S.V., Popova S.V., Antonenkov V.D. Effect of chronic ethanol treatment on peroxisomal acyl-CoA oxidase activity and lipid peroxidation in rat liver and heart. Experientia 1987, 43:580-581.
    • (1987) Experientia , vol.43 , pp. 580-581
    • Panchenko, L.F.1    Pirozhkov, S.V.2    Popova, S.V.3    Antonenkov, V.D.4
  • 208
    • 0023814735 scopus 로고
    • Effect of chronic ethanol treatment under partial catalase inhibition on the activity of enzymes related to peroxide metabolism in rat liver and heart
    • Antonenkov V.D., Panchenko L.F. Effect of chronic ethanol treatment under partial catalase inhibition on the activity of enzymes related to peroxide metabolism in rat liver and heart. Int. J. Biochem. 1988, 20:823-828.
    • (1988) Int. J. Biochem. , vol.20 , pp. 823-828
    • Antonenkov, V.D.1    Panchenko, L.F.2
  • 209
    • 0015076242 scopus 로고
    • Fine structural identification of peroxisomes in mouse and rat bronchiolar and alveolar epithelium
    • Petrik P. Fine structural identification of peroxisomes in mouse and rat bronchiolar and alveolar epithelium. J. Histochem. Cytochem. 1971, 19:339-348.
    • (1971) J. Histochem. Cytochem. , vol.19 , pp. 339-348
    • Petrik, P.1
  • 210
    • 0015309224 scopus 로고
    • Acomparative cytochemical study of microbodies (peroxisomes) in great alveolar cells of rodents, rabbit and monkey
    • Schneeberger E.E. Acomparative cytochemical study of microbodies (peroxisomes) in great alveolar cells of rodents, rabbit and monkey. J. Histochem. Cytochem. 1972, 20:180-191.
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 180-191
    • Schneeberger, E.E.1
  • 211
    • 0018154873 scopus 로고
    • Catalase positive particles from pig lung. Biochemical preparations and morphological studies
    • Goldenberg H., Huttinger M., Kollner U., Kramar R., Pavelka M. Catalase positive particles from pig lung. Biochemical preparations and morphological studies. Histochemistry 1978, 56:253-264.
    • (1978) Histochemistry , vol.56 , pp. 253-264
    • Goldenberg, H.1    Huttinger, M.2    Kollner, U.3    Kramar, R.4    Pavelka, M.5
  • 212
    • 51249112758 scopus 로고    scopus 로고
    • Peroxisomes in mouse and human lung: their involvement in pulmonary lipid metabolism
    • Karnati S., Baumgart-Vogt E. Peroxisomes in mouse and human lung: their involvement in pulmonary lipid metabolism. Histochem. Cell Biol. 2008, 130:719-740.
    • (2008) Histochem. Cell Biol. , vol.130 , pp. 719-740
    • Karnati, S.1    Baumgart-Vogt, E.2
  • 213
    • 64649099402 scopus 로고    scopus 로고
    • Peroxisomes in airway epithelia and future prospects of these organelles for pulmonary cell biology
    • Karnati S., Baumgart-Vogt E. Peroxisomes in airway epithelia and future prospects of these organelles for pulmonary cell biology. Histochem. Cell Biol. 2009, 131:447-454.
    • (2009) Histochem. Cell Biol. , vol.131 , pp. 447-454
    • Karnati, S.1    Baumgart-Vogt, E.2
  • 214
    • 0028597510 scopus 로고
    • Identification of the non-specific lipid-transfer protein (sterol carrier protein 2) in peroxisomes of lung type II cells
    • Ossendorp B.C., Voorhout W.F., van Golde L.M., Wirtz K.W., Batenburg J.J. Identification of the non-specific lipid-transfer protein (sterol carrier protein 2) in peroxisomes of lung type II cells. Biochem. Biophys. Res. Commun. 1994, 205:1581-1588.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1581-1588
    • Ossendorp, B.C.1    Voorhout, W.F.2    van Golde, L.M.3    Wirtz, K.W.4    Batenburg, J.J.5
  • 216
    • 68949151976 scopus 로고    scopus 로고
    • Peroxisomes, myelination, and axonal integrity in the CNS
    • Baes M., Aubourg P. Peroxisomes, myelination, and axonal integrity in the CNS. Neuroscientist 2009, 15:367-379.
    • (2009) Neuroscientist , vol.15 , pp. 367-379
    • Baes, M.1    Aubourg, P.2
  • 217
    • 0017106394 scopus 로고
    • Microperoxisome distribution in the central nervous system of the rat
    • McKenna O., Arnold G., Holtzman E. Microperoxisome distribution in the central nervous system of the rat. Brain Res. 1976, 117:181-194.
    • (1976) Brain Res. , vol.117 , pp. 181-194
    • McKenna, O.1    Arnold, G.2    Holtzman, E.3
  • 218
    • 0026099826 scopus 로고
    • Postnatal development and isolation of peroxisomes from brain
    • Lazo O., Singh A.K., Singh I. Postnatal development and isolation of peroxisomes from brain. J. Neurochem. 1991, 56:1343-1353.
    • (1991) J. Neurochem. , vol.56 , pp. 1343-1353
    • Lazo, O.1    Singh, A.K.2    Singh, I.3
  • 220
    • 0020002346 scopus 로고
    • Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway
    • Hajra A.K., Bishop J.E. Glycerolipid biosynthesis in peroxisomes via the acyl dihydroxyacetone phosphate pathway. Ann. N. Y. Acad. Sci. 1982, 386:170-182.
    • (1982) Ann. N. Y. Acad. Sci. , vol.386 , pp. 170-182
    • Hajra, A.K.1    Bishop, J.E.2
  • 221
    • 0020574070 scopus 로고
    • Severe plasmalogen deficiency in tissues of infants without peroxisomes (Zellweger syndrome)
    • Heymans H.S., Schutgens R.B., Tan R., van den Bosch H., Borst P. Severe plasmalogen deficiency in tissues of infants without peroxisomes (Zellweger syndrome). Nature 1983, 306:69-70.
    • (1983) Nature , vol.306 , pp. 69-70
    • Heymans, H.S.1    Schutgens, R.B.2    Tan, R.3    van den Bosch, H.4    Borst, P.5
  • 222
    • 0018118471 scopus 로고
    • Microperoxisomes in the central nervous system of the postnatal rat
    • Arnold G., Holtzman E. Microperoxisomes in the central nervous system of the postnatal rat. Brain Res. 1978, 155:1-17.
    • (1978) Brain Res. , vol.155 , pp. 1-17
    • Arnold, G.1    Holtzman, E.2
  • 223
    • 0028841708 scopus 로고
    • Immunocytochemical localization of catalase in the central nervous system of the rat
    • Moreno S., Mugnaini E., Ceru M.P. Immunocytochemical localization of catalase in the central nervous system of the rat. J. Histochem. Cytochem. 1995, 43:1253-1267.
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 1253-1267
    • Moreno, S.1    Mugnaini, E.2    Ceru, M.P.3
  • 224
    • 0038012896 scopus 로고    scopus 로고
    • Expression of catalase mRNA and protein in adult rat brain: detection by nonradioactive in situ hybridization with signal amplification by catalyzed reporter deposition (ISH-CARD) and immunohistochemistry (IHC)/immunofluorescence (IF)
    • Schad A., Fahimi H.D., Volkl A., Baumgart E. Expression of catalase mRNA and protein in adult rat brain: detection by nonradioactive in situ hybridization with signal amplification by catalyzed reporter deposition (ISH-CARD) and immunohistochemistry (IHC)/immunofluorescence (IF). J. Histochem. Cytochem. 2003, 51:751-760.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 751-760
    • Schad, A.1    Fahimi, H.D.2    Volkl, A.3    Baumgart, E.4
  • 225
  • 226
    • 0018763016 scopus 로고
    • Ultrastructural localization of d-amino acid oxidase in microperoxisomes of the rat nervous system
    • Arnold G., Liscum L., Holtzman E. Ultrastructural localization of d-amino acid oxidase in microperoxisomes of the rat nervous system. J. Histochem. Cytochem. 1979, 27:735-745.
    • (1979) J. Histochem. Cytochem. , vol.27 , pp. 735-745
    • Arnold, G.1    Liscum, L.2    Holtzman, E.3
  • 227
    • 0033499883 scopus 로고    scopus 로고
    • Immunocytochemical localization of d-amino acid oxidase in rat brain
    • Moreno S., Nardacci R., Cimini A., Ceru M.P. Immunocytochemical localization of d-amino acid oxidase in rat brain. J. Neurocytol. 1999, 28:169-185.
    • (1999) J. Neurocytol. , vol.28 , pp. 169-185
    • Moreno, S.1    Nardacci, R.2    Cimini, A.3    Ceru, M.P.4
  • 228
    • 0037179122 scopus 로고    scopus 로고
    • Cellular and subcellular distribution of d-aspartate oxidase in human and rat brain
    • Zaar K., Kost H.P., Schad A., Volkl A., Baumgart E., Fahimi H.D. Cellular and subcellular distribution of d-aspartate oxidase in human and rat brain. J. Comp. Neurol. 2002, 450:272-282.
    • (2002) J. Comp. Neurol. , vol.450 , pp. 272-282
    • Zaar, K.1    Kost, H.P.2    Schad, A.3    Volkl, A.4    Baumgart, E.5    Fahimi, H.D.6
  • 229
  • 230
    • 35948979696 scopus 로고    scopus 로고
    • Differential expression of peroxisomal matrix and membrane proteins during postnatal development of mouse brain
    • Ahlemeyer B., Neubert I., Kovacs W.J., Baumgart-Vogt E. Differential expression of peroxisomal matrix and membrane proteins during postnatal development of mouse brain. J. Comp. Neurol. 2007, 505:1-17.
    • (2007) J. Comp. Neurol. , vol.505 , pp. 1-17
    • Ahlemeyer, B.1    Neubert, I.2    Kovacs, W.J.3    Baumgart-Vogt, E.4
  • 231
    • 0027359303 scopus 로고
    • Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain
    • Singh I., Lazo O., Kremser K. Purification of peroxisomes and subcellular distribution of enzyme activities for activation and oxidation of very-long-chain fatty acids in rat brain. Biochim. Biophys. Acta 1993, 1170:44-52.
    • (1993) Biochim. Biophys. Acta , vol.1170 , pp. 44-52
    • Singh, I.1    Lazo, O.2    Kremser, K.3
  • 233
    • 0034797095 scopus 로고    scopus 로고
    • Purification of brain peroxisomes and localization of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Kovacs W.J., Faust P.L., Keller G.A., Krisans S.K. Purification of brain peroxisomes and localization of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Eur. J. Biochem. 2001, 268:4850-4859.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4850-4859
    • Kovacs, W.J.1    Faust, P.L.2    Keller, G.A.3    Krisans, S.K.4
  • 236
    • 0030830906 scopus 로고    scopus 로고
    • Targeted deletion of the PEX2 peroxisome assembly gene in mice provides a model for Zellweger syndrome, a human neuronal migration disorder
    • Faust P.L., Hatten M.E. Targeted deletion of the PEX2 peroxisome assembly gene in mice provides a model for Zellweger syndrome, a human neuronal migration disorder. J. Cell Biol. 1997, 139:1293-1305.
    • (1997) J. Cell Biol. , vol.139 , pp. 1293-1305
    • Faust, P.L.1    Hatten, M.E.2
  • 238
    • 0034914306 scopus 로고    scopus 로고
    • The peroxisome deficient PEX2 Zellweger mouse: pathologic and biochemical correlates of lipid dysfunction
    • discussion 317-221
    • Faust P.L., Su H.M., Moser A., Moser H.W. The peroxisome deficient PEX2 Zellweger mouse: pathologic and biochemical correlates of lipid dysfunction. J. Mol. Neurosci. 2001, 16:289-297. discussion 317-221.
    • (2001) J. Mol. Neurosci. , vol.16 , pp. 289-297
    • Faust, P.L.1    Su, H.M.2    Moser, A.3    Moser, H.W.4
  • 239
    • 70349325995 scopus 로고    scopus 로고
    • Docosahexaenoic acid promotes hippocampal neuronal development and synaptic function
    • Cao D., Kevala K., Kim J., Moon H.S., Jun S.B., Lovinger D., Kim H.Y. Docosahexaenoic acid promotes hippocampal neuronal development and synaptic function. J. Neurochem. 2009, 111:510-521.
    • (2009) J. Neurochem. , vol.111 , pp. 510-521
    • Cao, D.1    Kevala, K.2    Kim, J.3    Moon, H.S.4    Jun, S.B.5    Lovinger, D.6    Kim, H.Y.7
  • 240
    • 0030860131 scopus 로고    scopus 로고
    • Adrenoleukodystrophy: phenotype, genetics, pathogenesis and therapy
    • Moser H.W. Adrenoleukodystrophy: phenotype, genetics, pathogenesis and therapy. Brain 1997, 120(Pt 8):1485-1508.
    • (1997) Brain , vol.120 , Issue.PART 8 , pp. 1485-1508
    • Moser, H.W.1
  • 241
    • 33748594955 scopus 로고    scopus 로고
    • Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model
    • Huyghe S., Mannaerts G.P., Baes M., Van Veldhoven P.P. Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model. Biochim. Biophys. Acta 2006, 1761:973-994.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 973-994
    • Huyghe, S.1    Mannaerts, G.P.2    Baes, M.3    Van Veldhoven, P.P.4
  • 242
    • 0035658316 scopus 로고    scopus 로고
    • Identification of the peroxisomal beta-oxidation enzymes involved in the biosynthesis of docosahexaenoic acid
    • Ferdinandusse S., Denis S., Mooijer P.A., Zhang Z., Reddy J.K., Spector A.A., Wanders R.J. Identification of the peroxisomal beta-oxidation enzymes involved in the biosynthesis of docosahexaenoic acid. J. Lipid Res. 2001, 42:1987-1995.
    • (2001) J. Lipid Res. , vol.42 , pp. 1987-1995
    • Ferdinandusse, S.1    Denis, S.2    Mooijer, P.A.3    Zhang, Z.4    Reddy, J.K.5    Spector, A.A.6    Wanders, R.J.7
  • 243
    • 0035851141 scopus 로고    scopus 로고
    • Peroxisomal straight-chain Acyl-CoA oxidase and d-bifunctional protein are essential for the retroconversion step in docosahexaenoic acid synthesis
    • Su H.M., Moser A.B., Moser H.W., Watkins P.A. Peroxisomal straight-chain Acyl-CoA oxidase and d-bifunctional protein are essential for the retroconversion step in docosahexaenoic acid synthesis. J. Biol. Chem. 2001, 276:38115-38120.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38115-38120
    • Su, H.M.1    Moser, A.B.2    Moser, H.W.3    Watkins, P.A.4
  • 244
    • 60149094802 scopus 로고    scopus 로고
    • Plasmalogens participate in very-long-chain fatty acid-induced pathology
    • Brites P., Mooyer P.A., El Mrabet L., Waterham H.R., Wanders R.J. Plasmalogens participate in very-long-chain fatty acid-induced pathology. Brain 2009, 132:482-492.
    • (2009) Brain , vol.132 , pp. 482-492
    • Brites, P.1    Mooyer, P.A.2    El Mrabet, L.3    Waterham, H.R.4    Wanders, R.J.5
  • 246
    • 33846166061 scopus 로고    scopus 로고
    • Neocortical and cerebellar developmental abnormalities in conditions of selective elimination of peroxisomes from brain or from liver
    • Krysko O., Hulshagen L., Janssen A., Schutz G., Klein R., De Bruycker M., Espeel M., Gressens P., Baes M. Neocortical and cerebellar developmental abnormalities in conditions of selective elimination of peroxisomes from brain or from liver. J. Neurosci. Res. 2007, 85:58-72.
    • (2007) J. Neurosci. Res. , vol.85 , pp. 58-72
    • Krysko, O.1    Hulshagen, L.2    Janssen, A.3    Schutz, G.4    Klein, R.5    De Bruycker, M.6    Espeel, M.7    Gressens, P.8    Baes, M.9
  • 249
    • 74949133060 scopus 로고    scopus 로고
    • Early biochemical and morphological modifications in the brain of a transgenic mouse model of Alzheimer's disease: a role for peroxisomes, J. Alzheimers Dis. 18
    • A. Cimini, S. Moreno, M. D'Amelio, L. Cristiano, B. D'Angelo, S. Falone, E. Benedetti, P. Carrara, F. Fanelli, F. Cecconi, F. Amicarelli, M.P. Ceru, Early biochemical and morphological modifications in the brain of a transgenic mouse model of Alzheimer's disease: a role for peroxisomes, J. Alzheimers Dis. 18 (2009) 935-952.
    • (2009) , pp. 935-952
    • Cimini A1    Moreno S2    D'Amelio M3    Cristiano L4    D'Angelo B5    Falone S6    Benedetti E7    Carrara P8    Fanelli F9    Cecconi F10    Amicarelli F11    Ceru M.P12
  • 251
    • 21844461354 scopus 로고    scopus 로고
    • Peroxisomal participation in psychosine-mediated toxicity: implications for Krabbe's disease
    • Khan M., Haq E., Giri S., Singh I., Singh A.K. Peroxisomal participation in psychosine-mediated toxicity: implications for Krabbe's disease. J. Neurosci. Res. 2005, 80:845-854.
    • (2005) J. Neurosci. Res. , vol.80 , pp. 845-854
    • Khan, M.1    Haq, E.2    Giri, S.3    Singh, I.4    Singh, A.K.5
  • 252
    • 33645104535 scopus 로고    scopus 로고
    • Dysfunction of peroxisomes in twitcher mice brain: a possible mechanism of psychosine-induced disease
    • Haq E., Contreras M.A., Giri S., Singh I., Singh A.K. Dysfunction of peroxisomes in twitcher mice brain: a possible mechanism of psychosine-induced disease. Biochem. Biophys. Res. Commun. 2006, 343:229-238.
    • (2006) Biochem. Biophys. Res. Commun. , vol.343 , pp. 229-238
    • Haq, E.1    Contreras, M.A.2    Giri, S.3    Singh, I.4    Singh, A.K.5
  • 253
    • 66149173521 scopus 로고    scopus 로고
    • Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology
    • Palma J.M., Corpas F.J., del Rio L.A. Proteome of plant peroxisomes: new perspectives on the role of these organelles in cell biology. Proteomics 2009, 9:2301-2312.
    • (2009) Proteomics , vol.9 , pp. 2301-2312
    • Palma, J.M.1    Corpas, F.J.2    del Rio, L.A.3
  • 256
    • 0345791524 scopus 로고    scopus 로고
    • Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease
    • Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H. Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease. J. Biol. Chem. 2004, 279:421-428.
    • (2004) J. Biol. Chem. , vol.279 , pp. 421-428
    • Kikuchi, M.1    Hatano, N.2    Yokota, S.3    Shimozawa, N.4    Imanaka, T.5    Taniguchi, H.6
  • 257
    • 30744471923 scopus 로고    scopus 로고
    • Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity
    • Ofman R., Speijer D., Leen R., Wanders R.J. Proteomic analysis of mouse kidney peroxisomes: identification of RP2p as a peroxisomal nudix hydrolase with acyl-CoA diphosphatase activity. Biochem. J. 2006, 393:537-543.
    • (2006) Biochem. J. , vol.393 , pp. 537-543
    • Ofman, R.1    Speijer, D.2    Leen, R.3    Wanders, R.J.4
  • 258
    • 32944471823 scopus 로고    scopus 로고
    • Insights into the membrane proteome of rat liver peroxisomes: microsomal glutathione-S-transferase is shared by both subcellular compartments
    • Islinger M., Luers G.H., Zischka H., Ueffing M., Volkl A. Insights into the membrane proteome of rat liver peroxisomes: microsomal glutathione-S-transferase is shared by both subcellular compartments. Proteomics 2006, 6:804-816.
    • (2006) Proteomics , vol.6 , pp. 804-816
    • Islinger, M.1    Luers, G.H.2    Zischka, H.3    Ueffing, M.4    Volkl, A.5
  • 260
    • 0021838023 scopus 로고
    • Androgen regulation of MAK mRNAs in mouse kidney
    • Snider L.D., King D., Lingrel J.B. Androgen regulation of MAK mRNAs in mouse kidney. J. Biol. Chem. 1985, 260:9884-9893.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9884-9893
    • Snider, L.D.1    King, D.2    Lingrel, J.B.3
  • 261
    • 0035397652 scopus 로고    scopus 로고
    • The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives
    • Gasmi L., McLennan A.G. The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for coenzyme A and its derivatives. Biochem. J. 2001, 357:33-38.
    • (2001) Biochem. J. , vol.357 , pp. 33-38
    • Gasmi, L.1    McLennan, A.G.2
  • 265
    • 40949116751 scopus 로고    scopus 로고
    • RNAi-mediated silencing of ABCD3 gene expression in rat C6 glial cells: a model system to study PMP70 function
    • Di Benedetto R., Denti M.A., Salvati S., Sanchez M., Attorri L., David G., Di Biase A. RNAi-mediated silencing of ABCD3 gene expression in rat C6 glial cells: a model system to study PMP70 function. Neurochem. Int. 2008, 52:1106-1113.
    • (2008) Neurochem. Int. , vol.52 , pp. 1106-1113
    • Di Benedetto, R.1    Denti, M.A.2    Salvati, S.3    Sanchez, M.4    Attorri, L.5    David, G.6    Di Biase, A.7
  • 267
    • 34250336949 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of mouse peroxisomes from liver and kidney
    • Mi J., Kirchner E., Cristobal S. Quantitative proteomic comparison of mouse peroxisomes from liver and kidney. Proteomics 2007, 7:1916-1928.
    • (2007) Proteomics , vol.7 , pp. 1916-1928
    • Mi, J.1    Kirchner, E.2    Cristobal, S.3
  • 268
    • 0033544852 scopus 로고    scopus 로고
    • Aberrant oxidation of the cholesterol side chain in bile acid synthesis of sterol carrier protein-2/sterol carrier protein-x knockout mice
    • Kannenberg F., Ellinghaus P., Assmann G., Seedorf U. Aberrant oxidation of the cholesterol side chain in bile acid synthesis of sterol carrier protein-2/sterol carrier protein-x knockout mice. J. Biol. Chem. 1999, 274:35455-35460.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35455-35460
    • Kannenberg, F.1    Ellinghaus, P.2    Assmann, G.3    Seedorf, U.4
  • 270
    • 48649110209 scopus 로고    scopus 로고
    • Degradation of very long chain dicarboxylic polyunsaturated fatty acids in mouse hepatocytes, a peroxisomal process
    • Nguyen S.D., Baes M., Van Veldhoven P.P. Degradation of very long chain dicarboxylic polyunsaturated fatty acids in mouse hepatocytes, a peroxisomal process. Biochim. Biophys. Acta 2008, 1781:400-405.
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 400-405
    • Nguyen, S.D.1    Baes, M.2    Van Veldhoven, P.P.3
  • 271
    • 27144530363 scopus 로고    scopus 로고
    • Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment
    • Mi J., Orbea A., Syme N., Ahmed M., Cajaraville M.P., Cristobal S. Peroxisomal proteomics, a new tool for risk assessment of peroxisome proliferating pollutants in the marine environment. Proteomics 2005, 5:3954-3965.
    • (2005) Proteomics , vol.5 , pp. 3954-3965
    • Mi, J.1    Orbea, A.2    Syme, N.3    Ahmed, M.4    Cajaraville, M.P.5    Cristobal, S.6
  • 272
    • 34147139944 scopus 로고    scopus 로고
    • Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil
    • Mi J., Apraiz I., Cristobal S. Peroxisomal proteomic approach for protein profiling in blue mussels (Mytilus edulis) exposed to crude oil. Biomarkers 2007, 12:47-60.
    • (2007) Biomarkers , vol.12 , pp. 47-60
    • Mi, J.1    Apraiz, I.2    Cristobal, S.3
  • 275
    • 33846949331 scopus 로고    scopus 로고
    • Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing enzymes involved in beta-oxidation of fatty acids
    • Kurochkin I.V., Mizuno Y., Konagaya A., Sakaki Y., Schonbach C., Okazaki Y. Novel peroxisomal protease Tysnd1 processes PTS1- and PTS2-containing enzymes involved in beta-oxidation of fatty acids. Embo J. 2007, 26:835-845.
    • (2007) Embo J. , vol.26 , pp. 835-845
    • Kurochkin, I.V.1    Mizuno, Y.2    Konagaya, A.3    Sakaki, Y.4    Schonbach, C.5    Okazaki, Y.6
  • 276
    • 0037414458 scopus 로고    scopus 로고
    • Prediction of peroxisomal targeting signal 1 containing proteins from amino acid sequence
    • Neuberger G., Maurer-Stroh S., Eisenhaber B., Hartig A., Eisenhaber F. Prediction of peroxisomal targeting signal 1 containing proteins from amino acid sequence. J. Mol. Biol. 2003, 328:581-592.
    • (2003) J. Mol. Biol. , vol.328 , pp. 581-592
    • Neuberger, G.1    Maurer-Stroh, S.2    Eisenhaber, B.3    Hartig, A.4    Eisenhaber, F.5
  • 277
    • 0038122825 scopus 로고    scopus 로고
    • In silico prediction of the peroxisomal proteome in fungi, plants and animals
    • Emanuelsson O., Elofsson A., von Heijne G., Cristobal S. In silico prediction of the peroxisomal proteome in fungi, plants and animals. J. Mol. Biol. 2003, 330:443-456.
    • (2003) J. Mol. Biol. , vol.330 , pp. 443-456
    • Emanuelsson, O.1    Elofsson, A.2    von Heijne, G.3    Cristobal, S.4
  • 279
    • 57649201317 scopus 로고    scopus 로고
    • Predicted mouse peroxisome-targeted proteins and their actual subcellular locations
    • Mizuno Y., Kurochkin I.V., Herberth M., Okazaki Y., Schonbach C. Predicted mouse peroxisome-targeted proteins and their actual subcellular locations. BMC Bioinformatics 2008, 9(Suppl 12):S16.
    • (2008) BMC Bioinformatics , vol.9 , Issue.SUPPL 12
    • Mizuno, Y.1    Kurochkin, I.V.2    Herberth, M.3    Okazaki, Y.4    Schonbach, C.5
  • 280
    • 0025695105 scopus 로고
    • Changes in hepatic lipid metabolism associated with lipid accumulation and its reversal in rats given the peroxisome proliferator LY171883
    • Foxworthy P.S., Perry D.N., Hoover D.M., Eacho P.I. Changes in hepatic lipid metabolism associated with lipid accumulation and its reversal in rats given the peroxisome proliferator LY171883. Toxicol. Appl. Pharmacol. 1990, 106:375-383.
    • (1990) Toxicol. Appl. Pharmacol. , vol.106 , pp. 375-383
    • Foxworthy, P.S.1    Perry, D.N.2    Hoover, D.M.3    Eacho, P.I.4
  • 282
    • 0022924249 scopus 로고
    • Peroxisome proliferation due to di(2-ethylhexyl) phthalate (DEHP): species differences and possible mechanisms
    • Elcombe C.R., Mitchell A.M. Peroxisome proliferation due to di(2-ethylhexyl) phthalate (DEHP): species differences and possible mechanisms. Environ. Health Perspect. 1986, 70:211-219.
    • (1986) Environ. Health Perspect. , vol.70 , pp. 211-219
    • Elcombe, C.R.1    Mitchell, A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.