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Volumn 370, Issue 1, 2003, Pages 223-231

The liver isoform of carnitine palmitoyltransferase 1 is not targeted to the endoplasmic reticulum

Author keywords

Carnitine acyltransferase; Malonyl CoA; Mitochondria; Peroxisomes

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; MICROSCOPIC EXAMINATION; PROTEINS;

EID: 0037442828     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021269     Document Type: Article
Times cited : (10)

References (47)
  • 1
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis
    • McGarry, J. D. and Brown, N. F. (1997) The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis. Eur. J. Biochem. 244, 1-14
    • (1997) Eur. J. Biochem. , vol.244 , pp. 1-14
    • McGarry, J.D.1    Brown, N.F.2
  • 2
    • 0032518861 scopus 로고    scopus 로고
    • Enrichment of carnitine palmitoyltransferases I and II in the contact sites of rat liver mitochondria
    • Fraser, F. and Zammit, V. A. (1998) Enrichment of carnitine palmitoyltransferases I and II in the contact sites of rat liver mitochondria. Biochem. J. 329, 225-229
    • (1998) Biochem. J. , vol.329 , pp. 225-229
    • Fraser, F.1    Zammit, V.A.2
  • 3
    • 0032483331 scopus 로고    scopus 로고
    • The malonyl-CoA-sensitive form of carnitine palmitoyltransferase is not localized exclusively in the outer membrane of rat liver mitochondria
    • Hoppel, C. L., Kerner, J., Turkaly, P., Turkaly, J. and Tandler, B. (1998) The malonyl-CoA-sensitive form of carnitine palmitoyltransferase is not localized exclusively in the outer membrane of rat liver mitochondria. J. Biol. Chem. 273, 23495-23503
    • (1998) J. Biol. Chem. , vol.273 , pp. 23495-23503
    • Hoppel, C.L.1    Kerner, J.2    Turkaly, P.3    Turkaly, J.4    Tandler, B.5
  • 4
    • 0035881548 scopus 로고    scopus 로고
    • Rat liver mitochondrial contact sites and carnitine palmitoyltransferase-I
    • Hoppel, C., Kerner, J., Turkaly, P. and Tandler, B. (2001) Rat liver mitochondrial contact sites and carnitine palmitoyltransferase-I. Arch. Biochem. Biophys. 392, 321-325
    • (2001) Arch. Biochem. Biophys. , vol.392 , pp. 321-325
    • Hoppel, C.1    Kerner, J.2    Turkaly, P.3    Tandler, B.4
  • 5
    • 0035827646 scopus 로고    scopus 로고
    • Distinct kinetics of carnitine palmitoyltransferase 1 in contact sites and outer membranes of rat liver mitochondria
    • Fraser, F., Padovese, R. and Zammit, V. A. (2001) Distinct kinetics of carnitine palmitoyltransferase 1 in contact sites and outer membranes of rat liver mitochondria. J. Biol. Chem. 276, 20182-20185
    • (2001) J. Biol. Chem. , vol.276 , pp. 20182-20185
    • Fraser, F.1    Padovese, R.2    Zammit, V.A.3
  • 6
    • 0028792529 scopus 로고
    • Molecular cloning and sequence analysis of the rat liver carnitine octanoyltransferase cDNA, its natural gene and the gene promoter
    • Ohoi, S. J., Oh, D. H., Song, C. S., Roy, A. K. and Chatterjee, B. (1995) Molecular cloning and sequence analysis of the rat liver carnitine octanoyltransferase cDNA, its natural gene and the gene promoter. Biochim. Biophys. Acta 1264, 215-222
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 215-222
    • Ohoi, S.J.1    Oh, D.H.2    Song, C.S.3    Roy, A.K.4    Chatterjee, B.5
  • 7
    • 0030837072 scopus 로고    scopus 로고
    • cDNA cloning, recombinant expression, and site-directed mutagenesis of bovine liver carnitine octanoyltransferase-Arg505 binds the carboxylate group of carnitine
    • Cronin, C. N. (1997) cDNA cloning, recombinant expression, and site-directed mutagenesis of bovine liver carnitine octanoyltransferase-Arg505 binds the carboxylate group of carnitine. Eur. J. Biochem. 247, 1029-1037
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1029-1037
    • Cronin, C.N.1
  • 8
    • 0033032120 scopus 로고    scopus 로고
    • Submitochondriai and subcellular distributions of the carnitine-acylcarnitine carrier
    • Fraser, F. and Zammit, V. A. (1999) Submitochondriai and subcellular distributions of the carnitine-acylcarnitine carrier. FEBS Lett. 445, 41-44
    • (1999) FEBS Lett. , vol.445 , pp. 41-44
    • Fraser, F.1    Zammit, V.A.2
  • 9
    • 0030466735 scopus 로고    scopus 로고
    • Evidence of two catalytically active carnitine medium/long chain acyltransferases in rat liver peroxisomes
    • Singh, H., Beckman, K. and Poulos, A. (1996) Evidence of two catalytically active carnitine medium/long chain acyltransferases in rat liver peroxisomes. J. Lipid Res. 37, 2616-2626
    • (1996) J. Lipid Res. , vol.37 , pp. 2616-2626
    • Singh, H.1    Beckman, K.2    Poulos, A.3
  • 10
    • 0001324755 scopus 로고    scopus 로고
    • The malonyl-CoA sensitive carnitine palmitoyltransferase (CPT) of peroxisomes resembles the mitochondrial outer CPT but is a distinct protein
    • Murthy, M. S. R., Esser, V., McGarry, J. D. and Pande, S. V. (1996) The malonyl-CoA sensitive carnitine palmitoyltransferase (CPT) of peroxisomes resembles the mitochondrial outer CPT but is a distinct protein. FASEB J. 10, A506-A506
    • (1996) FASEB J. , vol.10
    • Murthy, M.S.R.1    Esser, V.2    McGarry, J.D.3    Pande, S.V.4
  • 11
    • 0033062413 scopus 로고    scopus 로고
    • Evidence that carnitine palmitoyltransferase I (CPT I) is expressed in microsomes and peroxisomes of rat liver. Distinct immunoreactivity of the N-terminal domain of the microsomal protein
    • Fraser, F., Corstorphine, C. G., Price, N. T. and Zammit, V. A. (1999) Evidence that carnitine palmitoyltransferase I (CPT I) is expressed in microsomes and peroxisomes of rat liver. Distinct immunoreactivity of the N-terminal domain of the microsomal protein. FEBS Lett. 446, 69-74
    • (1999) FEBS Lett. , vol.446 , pp. 69-74
    • Fraser, F.1    Corstorphine, C.G.2    Price, N.T.3    Zammit, V.A.4
  • 12
    • 0028225358 scopus 로고
    • Malonyl-CoA-sensitive and -insensitive carnitine palmitoyltransferase activities of microsomes are due to different proteins
    • Murthy, M. S. and Pande, S. V. (1994) Malonyl-CoA-sensitive and -insensitive carnitine palmitoyltransferase activities of microsomes are due to different proteins. J. Biol. Chem. 269, 18283-18286
    • (1994) J. Biol. Chem. , vol.269 , pp. 18283-18286
    • Murthy, M.S.1    Pande, S.V.2
  • 13
    • 0029118186 scopus 로고
    • Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: Characterization of the malonyl-CoA-sensitive enzyme
    • Broadway, N. M. and Saggerson, E. D. (1995) Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme. Biochem. J. 310, 989-995
    • (1995) Biochem. J. , vol.310 , pp. 989-995
    • Broadway, N.M.1    Saggerson, E.D.2
  • 14
    • 0026819717 scopus 로고
    • Purification of the medium-chain/long-chain (COT/CPT) carnitine acyltransferase of rat liver microsomes
    • Murthy, M. S. and Bieber, L. L. (1992) Purification of the medium-chain/long-chain (COT/CPT) carnitine acyltransferase of rat liver microsomes. Protein Expr. Purif. 3, 75-79
    • (1992) Protein Expr. Purif. , vol.3 , pp. 75-79
    • Murthy, M.S.1    Bieber, L.L.2
  • 15
    • 0027417408 scopus 로고
    • Properties of the medium chain/long chain carnitine acyltransferase purified from rat liver microsomes
    • Chung, C. D. and Bieber, L. L. (1993) Properties of the medium chain/long chain carnitine acyltransferase purified from rat liver microsomes. J. Biol. Chem. 268, 4519-4524
    • (1993) J. Biol. Chem. , vol.268 , pp. 4519-4524
    • Chung, C.D.1    Bieber, L.L.2
  • 16
    • 0029156130 scopus 로고
    • Inhibition of liver microsomal carnitine acyltransferases by sulphonylurea drugs
    • Broadway, N. M. and Saggerson, E. D. (1995) Inhibition of liver microsomal carnitine acyltransferases by sulphonylurea drugs. FEBS Lett. 371, 137-139
    • (1995) FEBS Lett. , vol.371 , pp. 137-139
    • Broadway, N.M.1    Saggerson, E.D.2
  • 17
    • 0031057110 scopus 로고    scopus 로고
    • Effect of membrane environment on the activity and inhibitability by malonyl-CoA of the carnitine acyltransferase of hepatic microsomal membranes
    • Broadway, N. M. and Saggerson, E. D. (1997) Effect of membrane environment on the activity and inhibitability by malonyl-CoA of the carnitine acyltransferase of hepatic microsomal membranes. Biochem. J, 322, 435-440
    • (1997) Biochem. J. , vol.322 , pp. 435-440
    • Broadway, N.M.1    Saggerson, E.D.2
  • 18
    • 0034466558 scopus 로고    scopus 로고
    • Carnitine acyltransferases and associated transport processes in the endoplasmic reticulum. Missing links in the VLDL story?
    • Broadway, N. M., Gooding, J. M. and Saggerson, E. D. (1999) Carnitine acyltransferases and associated transport processes in the endoplasmic reticulum. Missing links in the VLDL story? Adv. Exp. Med. Biol. 466, 59-67
    • (1999) Adv. Exp. Med. Biol. , vol.466 , pp. 59-67
    • Broadway, N.M.1    Gooding, J.M.2    Saggerson, E.D.3
  • 19
    • 0033544873 scopus 로고    scopus 로고
    • Evidence for triacylglycerol synthesis in the lumen of microsomes via a lipolysis-esterification pathway involving carnitine acyltransferases
    • Abo-Hashema, K. A., Cake, M. H., Power, G. W. and Clarke, D. (1999) Evidence for triacylglycerol synthesis in the lumen of microsomes via a lipolysis-esterification pathway involving carnitine acyltransferases. J. Biol. Chem. 274, 35577-35582
    • (1999) J. Biol. Chem. , vol.274 , pp. 35577-35582
    • Abo-Hashema, K.A.1    Cake, M.H.2    Power, G.W.3    Clarke, D.4
  • 20
    • 0030957455 scopus 로고    scopus 로고
    • Overt and latent activities of diacylglycerol acytransferase in rat liver microsomes: Possible roles in very-low-density lipoprotein triacylglycerol secretion
    • Owen, M. R., Corstorphine, C. C. and Zammit, V. A. (1997) Overt and latent activities of diacylglycerol acytransferase in rat liver microsomes: possible roles in very-low-density lipoprotein triacylglycerol secretion. Biochem. J. 323, 17-21
    • (1997) Biochem. J. , vol.323 , pp. 17-21
    • Owen, M.R.1    Corstorphine, C.C.2    Zammit, V.A.3
  • 21
    • 0032777703 scopus 로고    scopus 로고
    • Carnitine acyltransferases: Functional significance of subcellular distribution and membrane topology
    • Zammit, V. A. (1999) Carnitine acyltransferases: functional significance of subcellular distribution and membrane topology. Prog. Lipid Res. 38, 199-224
    • (1999) Prog. Lipid Res. , vol.38 , pp. 199-224
    • Zammit, V.A.1
  • 22
    • 0031006933 scopus 로고    scopus 로고
    • Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane
    • Fraser, F., Corstorphine, C. G. and Zammit, V. A. (1997) Topology of carnitine palmitoyltransferase I in the mitochondrial outer membrane. Biochem. J. 323, 711-718
    • (1997) Biochem. J. , vol.323 , pp. 711-718
    • Fraser, F.1    Corstorphine, C.G.2    Zammit, V.A.3
  • 23
    • 0025708373 scopus 로고
    • The relationship of rat liver overt carnitine palmitoyltransferase to the mitochondrial malonyl-CoA binding entity and to the latent palmitoyltransferase
    • Ghadiminejad, I. and Saggerson, E. D. (1990) The relationship of rat liver overt carnitine palmitoyltransferase to the mitochondrial malonyl-CoA binding entity and to the latent palmitoyltransferase. Biochem. J. 270, 787-794
    • (1990) Biochem. J. , vol.270 , pp. 787-794
    • Ghadiminejad, I.1    Saggerson, E.D.2
  • 26
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., Yuan, L. C., Bonifacino, J. S. and Klausner, R. D. (1989) Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56, 801-813
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 27
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter, P. and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84-93
    • (1983) Methods Enzymol. , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 28
    • 0035895945 scopus 로고    scopus 로고
    • The N-terminal domain of rat liver carnitine palmitoyltransferase 1 contains an internal mitochondrial import signal and residues essential for folding of its C-terminal catalytic domain
    • Cohen, I., Guillerault, F., Girard, J. and Prip-Buus, C. (2001) The N-terminal domain of rat liver carnitine palmitoyltransferase 1 contains an internal mitochondrial import signal and residues essential for folding of its C-terminal catalytic domain. J. Biol. Chem. 276, 5403-5411
    • (2001) J. Biol. Chem. , vol.276 , pp. 5403-5411
    • Cohen, I.1    Guillerault, F.2    Girard, J.3    Prip-Buus, C.4
  • 29
    • 0032491604 scopus 로고    scopus 로고
    • The N-terminal domain of rat liver carnitine palmitoyltransferase 1 mediates import into the outer mitochondrial membrane and is essential for activity and malonyl-CoA sensitivity
    • Cohen, I., Kohl, C., McGarry, J. D., Girard, J. and Prip-Buus, C. (1998) The N-terminal domain of rat liver carnitine palmitoyltransferase 1 mediates import into the outer mitochondrial membrane and is essential for activity and malonyl-CoA sensitivity. J. Biol. Chem. 273, 29896-29904
    • (1998) J. Biol. Chem. , vol.273 , pp. 29896-29904
    • Cohen, I.1    Kohl, C.2    McGarry, J.D.3    Girard, J.4    Prip-Buus, C.5
  • 30
    • 0020039867 scopus 로고
    • Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: Comparison with endoplasmic reticulum and mitochondrial membranes
    • Fujiki, Y., Fowler, S., Shio, H., Hubbard, A. L. and Lazarow, P. B. (1982) Polypeptide and phospholipid composition of the membrane of rat liver peroxisomes: comparison with endoplasmic reticulum and mitochondrial membranes. J. Cell Biol. 93, 103-110
    • (1982) J. Cell Biol. , vol.93 , pp. 103-110
    • Fujiki, Y.1    Fowler, S.2    Shio, H.3    Hubbard, A.L.4    Lazarow, P.B.5
  • 31
    • 0023642635 scopus 로고
    • Integration of porin synthesized in vitro into outer mitochondrial membranes Eur
    • Ono, H. and Tuboi, S. (1987) Integration of porin synthesized in vitro into outer mitochondrial membranes Eur. J. Biochem. 168, 509-514
    • (1987) J. Biochem. , vol.168 , pp. 509-514
    • Ono, H.1    Tuboi, S.2
  • 32
    • 0027049521 scopus 로고
    • A signal-anchor sequence selective for the mitochondrial outer membrane
    • McBride, H. M., Millar, D. G., Li, J. M. and Shore, G. C. (1992) A signal-anchor sequence selective for the mitochondrial outer membrane. J. Cell Biol. 119, 1451-1457
    • (1992) J. Cell Biol. , vol.119 , pp. 1451-1457
    • McBride, H.M.1    Millar, D.G.2    Li, J.M.3    Shore, G.C.4
  • 33
    • 0033178350 scopus 로고    scopus 로고
    • Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane
    • van der Leij, F. R., Kram, A. M., Bartelds, B., Roelofsen, H., Smid, G. B., Takens, J., Zammit, V. A. and Kuipers, J. R. (1999) Cytological evidence that the C-terminus of carnitine palmitoyltransferase I is on the cytosolic face of the mitochondrial outer membrane. Biochem. J. 341, 777-784
    • (1999) Biochem. J. , vol.341 , pp. 777-784
    • Van Der Leij, F.R.1    Kram, A.M.2    Bartelds, B.3    Roelofsen, H.4    Smid, G.B.5    Takens, J.6    Zammit, V.A.7    Kuipers, J.R.8
  • 34
    • 0027456595 scopus 로고
    • Inhibitors of mitochondrial carnitine palmitoyltransferase I limit the action of proteases on the enzyme. Isolation and partial amino acid analysis of a truncated form of the rat liver isozyme
    • Esser, V., Kuwajima, M., Britton, C. H., Krishnan, K., Foster, D. W. and McGarry, J. D. (1993) Inhibitors of mitochondrial carnitine palmitoyltransferase I limit the action of proteases on the enzyme. Isolation and partial amino acid analysis of a truncated form of the rat liver isozyme. J. Biol. Chem. 268, 5810-5816
    • (1993) J. Biol. Chem. , vol.268 , pp. 5810-5816
    • Esser, V.1    Kuwajima, M.2    Britton, C.H.3    Krishnan, K.4    Foster, D.W.5    McGarry, J.D.6
  • 35
    • 0027943519 scopus 로고
    • Some properties of the malonyl-CoA sensitive carnitine long/medium chain acyltransferase activities of peroxisomes and microsomes of rat liver
    • Bhuiyan, A. K., Murthy, M. S. and Pande, S. V. (1994) Some properties of the malonyl-CoA sensitive carnitine long/medium chain acyltransferase activities of peroxisomes and microsomes of rat liver. Biochem. Mol. Biol. Int. 34, 493-503
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 493-503
    • Bhuiyan, A.K.1    Murthy, M.S.2    Pande, S.V.3
  • 36
    • 0025345433 scopus 로고
    • The medium-chain carnitine acyltransferase activity associated with rat liver microsomes is malonyl-CoA sensitive
    • Lilly, K, Bugaisky, G. E., Umeda, P. K. and Bieber, L. L. (1990) The medium-chain carnitine acyltransferase activity associated with rat liver microsomes is malonyl-CoA sensitive. Arch. Biochem. Biophys. 280, 167-174
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 167-174
    • Lilly, K.1    Bugaisky, G.E.2    Umeda, P.K.3    Bieber, L.L.4
  • 37
    • 0000936031 scopus 로고
    • A comparison of the malonyl-CoA sensitive carnitine palmitoyltransferase activities acting on cytoplasmic substrates and their distribution in mitochondria, peroxisomes and microsomes
    • Ramsay, R. R. (1993) A comparison of the malonyl-CoA sensitive carnitine palmitoyltransferase activities acting on cytoplasmic substrates and their distribution in mitochondria, peroxisomes and microsomes. Biochem. Life Sci. Adv. 12, 23-29
    • (1993) Biochem. Life Sci. Adv. , vol.12 , pp. 23-29
    • Ramsay, R.R.1
  • 38
    • 0027377058 scopus 로고
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes
    • Ardail, D., Gasnier, F., Lerme, F., Simonot, C., Louisot, P. and Gateau-Roesch, O. (1993) Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes. J. Biol. Chem. 268, 25985-25992
    • (1993) J. Biol. Chem. , vol.268 , pp. 25985-25992
    • Ardail, D.1    Gasnier, F.2    Lerme, F.3    Simonot, C.4    Louisot, P.5    Gateau-Roesch, O.6
  • 39
    • 0026079408 scopus 로고
    • Contact sites between mitochondrial envelope membranes. Structure and function in energy- and protein-transfer
    • Brdiczka, D. (1991) Contact sites between mitochondrial envelope membranes. Structure and function in energy- and protein-transfer. Biochim. Biophys. Acta 1071, 291-312
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 291-312
    • Brdiczka, D.1
  • 40
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton, M. (2000) Mitochondrial intermembrane junctional complexes and their role in cell death. J. Physiol. (Cambridge, U.K.) 529, 11-21
    • (2000) J. Physiol. (Cambridge, U.K.) , vol.529 , pp. 11-21
    • Crompton, M.1
  • 42
    • 0020464225 scopus 로고
    • In vitro synthesis and integration into mitochondria of porin, a major protein of the outer mitochondrial membrane of Saccharomyces cerevisiae
    • Mihara, K., Blobel, G. and Sato, R. (1982) In vitro synthesis and integration into mitochondria of porin, a major protein of the outer mitochondrial membrane of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 79, 7102-7106
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 7102-7106
    • Mihara, K.1    Blobel, G.2    Sato, R.3
  • 43
    • 0026675770 scopus 로고
    • Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes
    • Sakaguchi, M., Hachiya, N., Mihara, K. and Omura, T. (1992) Mitochondrial porin can be translocated across both endoplasmic reticulum and mitochondrial membranes. J. Biochem. (Tokyo) 112, 243-248
    • (1992) J. Biochem. (Tokyo) , vol.112 , pp. 243-248
    • Sakaguchi, M.1    Hachiya, N.2    Mihara, K.3    Omura, T.4
  • 44
    • 0034468456 scopus 로고    scopus 로고
    • Subcellular distribution of mitochondrial carnitine palmitoyltransferase I in rat liver. Evidence for a distinctive N- terminal structure of the microsomal but not the peroxisomal enzyme
    • Fraser, F., Corstorphine, C. G. and Zammit, V. A. (1999) Subcellular distribution of mitochondrial carnitine palmitoyltransferase I in rat liver. Evidence for a distinctive N- terminal structure of the microsomal but not the peroxisomal enzyme. Adv. Exp. Med. Biol. 466, 17-25
    • (1999) Adv. Exp. Med. Biol. , vol.466 , pp. 17-25
    • Fraser, F.1    Corstorphine, C.G.2    Zammit, V.A.3
  • 45
    • 0032511158 scopus 로고    scopus 로고
    • Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae
    • Prip-Buus, C., Cohen, I., Kohl, C., Esser, V., McGarry, J. D. and Girard, J. (1998) Topological and functional analysis of the rat liver carnitine palmitoyltransferase 1 expressed in Saccharomyces cerevisiae. FEBS Lett. 429, 173-178
    • (1998) FEBS Lett. , vol.429 , pp. 173-178
    • Prip-Buus, C.1    Cohen, I.2    Kohl, C.3    Esser, V.4    McGarry, J.D.5    Girard, J.6
  • 46
    • 0031448780 scopus 로고    scopus 로고
    • Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane
    • Elgersma, Y., Kwast, L., van den Berg, M., Snyder, W. B., Distel, B., Subramani, S. and Tabak, H. F. (1997) Overexpression of Pex15p, a phosphorylated peroxisomal integral membrane protein required for peroxisome assembly in S. cerevisiae, causes proliferation of the endoplasmic reticulum membrane. EMBO J. 16, 7326-7341
    • (1997) EMBO J. , vol.16 , pp. 7326-7341
    • Elgersma, Y.1    Kwast, L.2    Van Den Berg, M.3    Snyder, W.B.4    Distel, B.5    Subramani, S.6    Tabak, H.F.7
  • 47
    • 0033739779 scopus 로고    scopus 로고
    • ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membrane
    • Joyce, C. W., Shelness, G. S., Davis, M. A., Lee, R. G., Skinner, K., Anderson, R. A. and Rudel, L. L. (2000) ACAT1 and ACAT2 membrane topology segregates a serine residue essential for activity to opposite sides of the endoplasmic reticulum membrane. Mol. Biol. Cell 11, 3675-3687
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3675-3687
    • Joyce, C.W.1    Shelness, G.S.2    Davis, M.A.3    Lee, R.G.4    Skinner, K.5    Anderson, R.A.6    Rudel, L.L.7


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