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Volumn 1486, Issue 1, 2000, Pages 45-54

Sterol carrier protein-2

Author keywords

Acyl coenzyme A; Cholesterol; Peroxisome; Sterol carrier protein 2; Oxidation

Indexed keywords

PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR; STEROL CARRIER PROTEIN 2;

EID: 0034717891     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(00)00047-0     Document Type: Review
Times cited : (106)

References (64)
  • 1
    • 0017286759 scopus 로고
    • Asymmetry and transposition rates of phosphatidylcholine in rat erythrocyte ghosts
    • Bloj B., Zilversmit D.B. Asymmetry and transposition rates of phosphatidylcholine in rat erythrocyte ghosts. Biochemistry. 15:1976;1277-1283.
    • (1976) Biochemistry , vol.15 , pp. 1277-1283
    • Bloj, B.1    Zilversmit, D.B.2
  • 5
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler K., Parton R.G., Kellner R., Etzold T., Simons K. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J. 13:1994;1729-1740.
    • (1994) EMBO J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 6
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes
    • Hanada K., Nishijima M., Akamatsu Y., Pagano R.E. Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J. Biol. Chem. 270:1995;6254-6260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 7
    • 0028032064 scopus 로고
    • VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol-anchored proteins in epithelial cells
    • Zurzolo C., van't-Hof W., van Meer G., Rodriguez B.E. VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol-anchored proteins in epithelial cells. EMBO J. 13:1994;42-53.
    • (1994) EMBO J. , vol.13 , pp. 42-53
    • Zurzolo, C.1    Van't-Hof, W.2    Van Meer, G.3    Rodriguez, B.E.4
  • 12
    • 0025142335 scopus 로고
    • Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane
    • Urbani L., Simoni R.D. Cholesterol and vesicular stomatitis virus G protein take separate routes from the endoplasmic reticulum to the plasma membrane. J. Biol. Chem. 265:1990;1919-1923.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1919-1923
    • Urbani, L.1    Simoni, R.D.2
  • 15
    • 0029101538 scopus 로고
    • Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic-reticulum to the plasma-membrane in human fibroblasts
    • Puglielli L., Rigotti A., Greco A.V., Santos M.J., Nervi F. Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic-reticulum to the plasma-membrane in human fibroblasts. J. Biol. Chem. 270:1995;18723-18726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18723-18726
    • Puglielli, L.1    Rigotti, A.2    Greco, A.V.3    Santos, M.J.4    Nervi, F.5
  • 16
    • 0030972973 scopus 로고    scopus 로고
    • Sterol carrier protein-2 overexpression enhances sterol cycling and inhibits cholesterol ester synthesis and high density lipoprotein cholesterol secretion
    • Baum C.L., Reschly E.J., Gayen A.K., Groh M.E., Schadick K. Sterol carrier protein-2 overexpression enhances sterol cycling and inhibits cholesterol ester synthesis and high density lipoprotein cholesterol secretion. J. Biol. Chem. 272:1997;6490-6498.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6490-6498
    • Baum, C.L.1    Reschly, E.J.2    Gayen, A.K.3    Groh, M.E.4    Schadick, K.5
  • 19
    • 0029838510 scopus 로고    scopus 로고
    • Structure and chromosomal assignment of the murine sterol carrier protein-2 gene (Scp2) and two related pseudogenes by in situ hybridization
    • Raabe M., Seedorf U., Hameister H., Ellinghaus P., Assmann G. Structure and chromosomal assignment of the murine sterol carrier protein-2 gene (Scp2) and two related pseudogenes by in situ hybridization. Cytogenet. Cell Genet. 73:1996;279-281.
    • (1996) Cytogenet. Cell Genet. , vol.73 , pp. 279-281
    • Raabe, M.1    Seedorf, U.2    Hameister, H.3    Ellinghaus, P.4    Assmann, G.5
  • 21
    • 0029128887 scopus 로고
    • Human sterol carrier protein-x/sterol carrier protein-2 gene has two promoters
    • Ohba T., Holt J.A., Billheimer J.T., Strauss J.F. Human sterol carrier protein-x/sterol carrier protein-2 gene has two promoters. Biochemistry. 34:1995;10660-10668.
    • (1995) Biochemistry , vol.34 , pp. 10660-10668
    • Ohba, T.1    Holt, J.A.2    Billheimer, J.T.3    Strauss, J.F.4
  • 22
    • 0025330098 scopus 로고
    • The amino-acid-sequence of rat-liver nonspecific lipid transfer protein (sterol carrier protein-2) is present in a high-molecular-weight protein - evidence from cDNA analysis
    • Ossendorp B.C., van Heusden G.P.H., Wirtz K.W.A. The amino-acid-sequence of rat-liver nonspecific lipid transfer protein (sterol carrier protein-2) is present in a high-molecular-weight protein - evidence from cDNA analysis. Biochem. Biophys. Res. Commun. 168:1990;631-636.
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 631-636
    • Ossendorp, B.C.1    Van Heusden, G.P.H.2    Wirtz, K.W.A.3
  • 23
    • 0026018481 scopus 로고
    • Cloning, expression, and nucleotide-sequence of rat-liver sterol carrier protein-2 cDNAs
    • Seedorf U., Assmann G. Cloning, expression, and nucleotide-sequence of rat-liver sterol carrier protein-2 cDNAs. J. Biol. Chem. 266:1991;630-636.
    • (1991) J. Biol. Chem. , vol.266 , pp. 630-636
    • Seedorf, U.1    Assmann, G.2
  • 24
    • 0027194338 scopus 로고
    • Chicken sterol carrier protein-2/sterol carrier protein-x - cDNA cloning reveals evolutionary conservation of structure and regulated expression
    • Pfeifer S.M., Sakuragi N., Ryan A., Johnson A.L., Deeley R.G., Billheimer J.T., Baker M.E., Strauss J.F. Chicken sterol carrier protein-2/sterol carrier protein-x - cDNA cloning reveals evolutionary conservation of structure and regulated expression. Arch. Biochem. Biophys. 304:1993;287-293.
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 287-293
    • Pfeifer, S.M.1    Sakuragi, N.2    Ryan, A.3    Johnson, A.L.4    Deeley, R.G.5    Billheimer, J.T.6    Baker, M.E.7    Strauss, J.F.8
  • 25
    • 0030950139 scopus 로고    scopus 로고
    • A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein-x but lacks the sequence of sterol carrier protein-2
    • Bunya M., Maebuchi M., Hashimoto T., Yokota S., Kamiryo T. A second isoform of 3-ketoacyl-CoA thiolase found in Caenorhabditis elegans, which is similar to sterol carrier protein-x but lacks the sequence of sterol carrier protein-2. Eur. J. Biochem. 245:1997;252-259.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 252-259
    • Bunya, M.1    Maebuchi, M.2    Hashimoto, T.3    Yokota, S.4    Kamiryo, T.5
  • 26
    • 0025376437 scopus 로고
    • A novel peroxisomal nonspecific lipid-transfer protein from Candida tropicalis - gene structure, purification and possible role in β-oxidation
    • Tan H., Okazaki K., Kubota I., Kamiryo T., Utiyama H. A novel peroxisomal nonspecific lipid-transfer protein from Candida tropicalis - gene structure, purification and possible role in β-oxidation. Eur. J. Biochem. 190:1990;107-112.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 107-112
    • Tan, H.1    Okazaki, K.2    Kubota, I.3    Kamiryo, T.4    Utiyama, H.5
  • 29
    • 0028123083 scopus 로고
    • Sterol carrier protein-x is peroxisomal 3-oxoacyl coenzyme-A thiolase with intrinsic sterol carrier and lipid transfer activity
    • Seedorf U., Brysch P., Engel T., Schrage K., Assmann G. Sterol carrier protein-x is peroxisomal 3-oxoacyl coenzyme-A thiolase with intrinsic sterol carrier and lipid transfer activity. J. Biol. Chem. 269:1994;21277-21283.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21277-21283
    • Seedorf, U.1    Brysch, P.2    Engel, T.3    Schrage, K.4    Assmann, G.5
  • 30
    • 0031591658 scopus 로고    scopus 로고
    • Sterol carrier protein-x (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: A new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes
    • Wanders R.A., Denis S., Wouters F., Wirtz K.A., Seedorf U. Sterol carrier protein-x (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochem. Biophys. Res. Commun. 236:1997;565-569.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 565-569
    • Wanders, R.A.1    Denis, S.2    Wouters, F.3    Wirtz, K.A.4    Seedorf, U.5
  • 31
    • 0031879234 scopus 로고    scopus 로고
    • Identification of the newly discovered 58 kDa peroxisomal thiolase SCPx as the main thiolase involved in both pristanic acid and trihydroxycholestanoic acid oxidation: Implications for peroxisomal β-oxidation disorders
    • Wanders R.J.A., Denis S., van Berkel E., Wouters F., Wirtz K.A., Seedorf U. Identification of the newly discovered 58 kDa peroxisomal thiolase SCPx as the main thiolase involved in both pristanic acid and trihydroxycholestanoic acid oxidation: implications for peroxisomal β-oxidation disorders. J. Inherit. Metab. Dis. 21:1998;302-305.
    • (1998) J. Inherit. Metab. Dis. , vol.21 , pp. 302-305
    • Wanders, R.J.A.1    Denis, S.2    Van Berkel, E.3    Wouters, F.4    Wirtz, K.A.5    Seedorf, U.6
  • 32
    • 0023655257 scopus 로고
    • Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase
    • Hijikata M., Ishii N., Kagamiyama H., Osumi T., Hashimoto T. Structural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase. J. Biol. Chem. 262:1987;8151-8158.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8151-8158
    • Hijikata, M.1    Ishii, N.2    Kagamiyama, H.3    Osumi, T.4    Hashimoto, T.5
  • 34
    • 0027980260 scopus 로고
    • The sequence of porcine 80 kDa 17 β-estradiol dehydrogenase reveals similarities to the short chain alcohol dehydrogenase family, to actin binding motifs and to sterol carrier protein-2
    • Leenders F., Husen B., Thole H.H., Adamski J. The sequence of porcine 80 kDa 17 β-estradiol dehydrogenase reveals similarities to the short chain alcohol dehydrogenase family, to actin binding motifs and to sterol carrier protein-2. Mol. Cell. Endocrinol. 104:1994;127-131.
    • (1994) Mol. Cell. Endocrinol. , vol.104 , pp. 127-131
    • Leenders, F.1    Husen, B.2    Thole, H.H.3    Adamski, J.4
  • 35
    • 0029866529 scopus 로고    scopus 로고
    • Porcine 80-kDa protein reveals intrinsic 17β-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities
    • Leenders F., Tesdorpf J.G., Markus M., Engel T., Seedorf U., Adamski J. Porcine 80-kDa protein reveals intrinsic 17β-hydroxysteroid dehydrogenase, fatty acyl-CoA-hydratase/dehydrogenase, and sterol transfer activities. J. Biol. Chem. 271:1996;5438-5442.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5438-5442
    • Leenders, F.1    Tesdorpf, J.G.2    Markus, M.3    Engel, T.4    Seedorf, U.5    Adamski, J.6
  • 36
    • 0030454449 scopus 로고    scopus 로고
    • Peroxisomes contain an enzyme with 17β-estradiol dehydrogenase, fatty acid hydratase/dehydrogenase, and sterol carrier activity
    • Markus M., Husen B., Leenders F., Seedorf U., Jungblut P.W., Hall P.H., Adamski J. Peroxisomes contain an enzyme with 17β-estradiol dehydrogenase, fatty acid hydratase/dehydrogenase, and sterol carrier activity. Ann. NY Acad. Sci. 804:1996;691-693.
    • (1996) Ann. NY Acad. Sci. , vol.804 , pp. 691-693
    • Markus, M.1    Husen, B.2    Leenders, F.3    Seedorf, U.4    Jungblut, P.W.5    Hall, P.H.6    Adamski, J.7
  • 37
    • 0029566261 scopus 로고
    • Intrinsic sterol- And phosphatidylcholine transfer activities of 17 β-hydroxysteroid dehydrogenase type IV
    • Seedorf U., Engel T., Assmann G., Leenders F., Adamski J. Intrinsic sterol- and phosphatidylcholine transfer activities of 17 β-hydroxysteroid dehydrogenase type IV. J. Steroid Biochem. Mol. Biol. 55:1995;549-553.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 549-553
    • Seedorf, U.1    Engel, T.2    Assmann, G.3    Leenders, F.4    Adamski, J.5
  • 38
    • 0019028350 scopus 로고
    • Purification and properties of acyl-CoA oxidase from rat liver
    • Osumi T., Hashimoto T., Ui N. Purification and properties of acyl-CoA oxidase from rat liver. J. Biochem. 87:1980;1735-1746.
    • (1980) J. Biochem. , vol.87 , pp. 1735-1746
    • Osumi, T.1    Hashimoto, T.2    Ui, N.3
  • 39
    • 0029771659 scopus 로고    scopus 로고
    • Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: Medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase
    • Jiang L.L., Kobayashi A., Matsuura H., Fukushima H., Hashimoto T. Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase. J. Biochem. 120:1996;624-632.
    • (1996) J. Biochem. , vol.120 , pp. 624-632
    • Jiang, L.L.1    Kobayashi, A.2    Matsuura, H.3    Fukushima, H.4    Hashimoto, T.5
  • 40
    • 0031003977 scopus 로고    scopus 로고
    • Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein
    • Jiang L.L., Kurosawa T., Sato M., Suzuki Y., Hashimoto T. Physiological role of D-3-hydroxyacyl-CoA dehydratase/D-3-hydroxyacyl-CoA dehydrogenase bifunctional protein. J. Biochem. 121:1997;506-513.
    • (1997) J. Biochem. , vol.121 , pp. 506-513
    • Jiang, L.L.1    Kurosawa, T.2    Sato, M.3    Suzuki, Y.4    Hashimoto, T.5
  • 41
    • 0029766087 scopus 로고    scopus 로고
    • Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- And tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins
    • Dieuaide N.M., Novikov D., Baumgart E., Vanhooren J.C., Fransen M., Goethals M., Vandekerckhove J., van Veldhoven P.P., Mannaerts G.P. Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins. Eur. J. Biochem. 240:1996;660-666.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 660-666
    • Dieuaide, N.M.1    Novikov, D.2    Baumgart, E.3    Vanhooren, J.C.4    Fransen, M.5    Goethals, M.6    Vandekerckhove, J.7    Van Veldhoven, P.P.8    Mannaerts, G.P.9
  • 42
    • 0031018720 scopus 로고    scopus 로고
    • Peroxisomal multifunctional enzyme of β-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: Molecular cloning, expression and characterization
    • Qin Y.M., Poutanen M.H., Helander H.M., Kvist A.P., Siivari K.M., Schmitz W., Conzelmann E., Hellman U., Hiltunen J.K. Peroxisomal multifunctional enzyme of β-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization. Biochem. J. 321:1997;21-28.
    • (1997) Biochem. J. , vol.321 , pp. 21-28
    • Qin, Y.M.1    Poutanen, M.H.2    Helander, H.M.3    Kvist, A.P.4    Siivari, K.M.5    Schmitz, W.6    Conzelmann, E.7    Hellman, U.8    Hiltunen, J.K.9
  • 44
    • 0029886763 scopus 로고    scopus 로고
    • The Caenorhabditis elegans behavioral gene unc-24 encodes a novel bipartite protein similar to both erythrocyte band 7.2 (stomatin) and nonspecific lipid transfer protein
    • Barnes T.M., Jin Y., Horvitz H.R., Ruvkun G., Hekimi S. The Caenorhabditis elegans behavioral gene unc-24 encodes a novel bipartite protein similar to both erythrocyte band 7.2 (stomatin) and nonspecific lipid transfer protein. J. Neurochem. 67:1996;46-57.
    • (1996) J. Neurochem. , vol.67 , pp. 46-57
    • Barnes, T.M.1    Jin, Y.2    Horvitz, H.R.3    Ruvkun, G.4    Hekimi, S.5
  • 45
    • 0032576593 scopus 로고    scopus 로고
    • Molecular cloning of hSLP-1, a novel human brain-specific member of the band 7/MEC-2 family similar to Caenorhabditis elegans UNC-24
    • Seidel G., Prohaska R. Molecular cloning of hSLP-1, a novel human brain-specific member of the band 7/MEC-2 family similar to Caenorhabditis elegans UNC-24. Gene. 225:1998;23-29.
    • (1998) Gene , vol.225 , pp. 23-29
    • Seidel, G.1    Prohaska, R.2
  • 46
    • 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
    • in press
    • F. Kannenberg, P. Ellinghaus, G. Assmann, U. Seedorf, 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) in press.
    • (1999) J. Biol. Chem.
    • Kannenberg, F.1    Ellinghaus, P.2    Assmann, G.3    Seedorf, U.4
  • 47
    • 0033613869 scopus 로고    scopus 로고
    • Phytanic acid activates the peroxisome proliferator-activated receptor-α (PPARα) in sterol carrier protein-2/sterol carrier protein x-deficient mice
    • Ellinghaus P., Wolfrum C., Assmann G., Spener F., Seedorf U. Phytanic acid activates the peroxisome proliferator-activated receptor-α (PPARα) in sterol carrier protein-2/sterol carrier protein x-deficient mice. J. Biol. Chem. 274:1999;2766-2772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2766-2772
    • Ellinghaus, P.1    Wolfrum, C.2    Assmann, G.3    Spener, F.4    Seedorf, U.5
  • 48
    • 10144234128 scopus 로고    scopus 로고
    • Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene
    • Fan C.Y., Pan J., Chu R., Lee D., Kluckman K.D., Usuda N., Singh I., Yeldandi A.V., Rao M.S., Maeda N., et al. Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene. J. Biol. Chem. 271:1996;24698-24710.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24698-24710
    • Fan, C.Y.1    Pan, J.2    Chu, R.3    Lee, D.4    Kluckman, K.D.5    Usuda, N.6    Singh, I.7    Yeldandi, A.V.8    Rao, M.S.9    Maeda, N.10
  • 49
    • 0032546929 scopus 로고    scopus 로고
    • Steatohepatitis, spontaneous peroxisome proliferation and liver tumors in mice lacking peroxisomal fatty acyl-CoA oxidase. Implications for peroxisome proliferator-activated receptor-α natural ligand metabolism
    • Fan C.Y., Pan J., Usuda N., Yeldandi A.V., Rao M.S., Reddy J.K. Steatohepatitis, spontaneous peroxisome proliferation and liver tumors in mice lacking peroxisomal fatty acyl-CoA oxidase. Implications for peroxisome proliferator-activated receptor-α natural ligand metabolism. J. Biol. Chem. 273:1998;15639-15645.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15639-15645
    • Fan, C.Y.1    Pan, J.2    Usuda, N.3    Yeldandi, A.V.4    Rao, M.S.5    Reddy, J.K.6
  • 50
    • 0022346124 scopus 로고
    • Correlation between the cellular level of long-chain acyl-CoA, peroxisomal β-oxidation, and palmitoyl-CoA hydrolase activity in rat liver. Are the two enzyme systems regulated by a substrate-induced mechanism?
    • Berge R.K., Aarsland A. Correlation between the cellular level of long-chain acyl-CoA, peroxisomal β-oxidation, and palmitoyl-CoA hydrolase activity in rat liver. Are the two enzyme systems regulated by a substrate-induced mechanism? Biochim. Biophys. Acta. 837:1985;141-151.
    • (1985) Biochim. Biophys. Acta , vol.837 , pp. 141-151
    • Berge, R.K.1    Aarsland, A.2
  • 51
    • 0027139208 scopus 로고
    • Structural and metabolic requirements for activators of the peroxisome proliferator-activated receptor
    • Gottlicher M., Demoz A., Svensson D., Tollet P., Berge R.K., Gustafsson J.A. Structural and metabolic requirements for activators of the peroxisome proliferator-activated receptor. Biochem. Pharmacol. 46:1993;2177-2184.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 2177-2184
    • Gottlicher, M.1    Demoz, A.2    Svensson, D.3    Tollet, P.4    Berge, R.K.5    Gustafsson, J.A.6
  • 52
    • 0026074550 scopus 로고
    • Peroxisome proliferating sulphur- And oxy-substituted fatty acid analogues are activated to acyl coenzyme A thioesters
    • Aarsland A., Berge R.K. Peroxisome proliferating sulphur- and oxy-substituted fatty acid analogues are activated to acyl coenzyme A thioesters. Biochem. Pharmacol. 41:1991;53-61.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 53-61
    • Aarsland, A.1    Berge, R.K.2
  • 53
    • 0000228425 scopus 로고
    • Disorders of peroxisome biogenesis
    • in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), McGraw-Hill, New York
    • P.B. Lazarow, H.W. Moser, Disorders of peroxisome biogenesis, in: C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle (Eds.), The Metabolic and Molecular Bases of Inherited Disease, 7th edn., McGraw-Hill, New York, 1995, pp. 2287-2324.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, 7th Edn. , pp. 2287-2324
    • Lazarow, P.B.1    Moser, H.W.2
  • 56
    • 0031587790 scopus 로고    scopus 로고
    • Adrenoleukodystrophy protein-deficient mice represent abnormality of very long chain fatty acid metabolism
    • Kobayashi T., Shinnoh N., Kondo A., Yamada T. Adrenoleukodystrophy protein-deficient mice represent abnormality of very long chain fatty acid metabolism. Biochem. Biophys. Res. Commun. 232:1997;631-636.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 631-636
    • Kobayashi, T.1    Shinnoh, N.2    Kondo, A.3    Yamada, T.4
  • 57
    • 0030952937 scopus 로고    scopus 로고
    • Hypolipidemic drugs, polyunsaturated fatty acids, and eicasanoids are ligands for peroxisome proliferator-activated receptors
    • Forman B.M., Chen J., Evans R.M. Hypolipidemic drugs, polyunsaturated fatty acids, and eicasanoids are ligands for peroxisome proliferator-activated receptors. Proc. Natl. Acad. Sci. USA. 94:1997;4312-4317.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4312-4317
    • Forman, B.M.1    Chen, J.2    Evans, R.M.3
  • 58
    • 0030783119 scopus 로고    scopus 로고
    • Polyunsaturated fatty acid suppression of hepatic fatty acid synthase and S14 gene expression does not require peroxisome proliferator-activated receptor alpha
    • Ren B., Thelen A.P., Peters J.M., Gonzalez F.J., Jump D.B. Polyunsaturated fatty acid suppression of hepatic fatty acid synthase and S14 gene expression does not require peroxisome proliferator-activated receptor alpha. J. Biol. Chem. 272:1997;26827-26832.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26827-26832
    • Ren, B.1    Thelen, A.P.2    Peters, J.M.3    Gonzalez, F.J.4    Jump, D.B.5
  • 59
    • 0026045925 scopus 로고
    • Characterization of an 8-lipoxygenase activity induced by the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate in mouse skin in vivo
    • Furstenberger G., Hagedorn H., Jacobi T., Besemfelder E., Stephan M., Lehmann W.D., Marks F. Characterization of an 8-lipoxygenase activity induced by the phorbol ester tumor promoter 12-O-tetradecanoylphorbol-13-acetate in mouse skin in vivo. J. Biol. Chem. 266:1991;15738-15745.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15738-15745
    • Furstenberger, G.1    Hagedorn, H.2    Jacobi, T.3    Besemfelder, E.4    Stephan, M.5    Lehmann, W.D.6    Marks, F.7
  • 61
  • 62
    • 0031719295 scopus 로고    scopus 로고
    • The non-specific lipid transfer protein (sterol carrier protein 2) acts as a peroxisomal fatty acyl-CoA binding protein
    • Wirtz K.W., Wouters F.S., Bastiaens P.H., Wanders R.J., Seedorf U., Jovin T.M. The non-specific lipid transfer protein (sterol carrier protein 2) acts as a peroxisomal fatty acyl-CoA binding protein. Biochem. Soc. Trans. 26:1998;374-378.
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 374-378
    • Wirtz, K.W.1    Wouters, F.S.2    Bastiaens, P.H.3    Wanders, R.J.4    Seedorf, U.5    Jovin, T.M.6
  • 63
    • 0032535138 scopus 로고    scopus 로고
    • FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes
    • Wouters F.S., Bastiaens P.I., Wirtz K.W., Jovin T.M. FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J. 17:1998;7179-7189.
    • (1998) EMBO J. , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.2    Wirtz, K.W.3    Jovin, T.M.4


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