메뉴 건너뛰기




Volumn 12, Issue 4, 1996, Pages 333-348

Candida maltosa NADPH-cytochrome P450 reductase: Cloning of a full-length cDNA, heterologous expression in Saccharomyces cerevisiae and function of the N-terminal region for membrane anchoring and proliferation of the endoplasmic reticulum

Author keywords

High level expression; Immunoelectron microscopy; Protein transport

Indexed keywords

COMPLEMENTARY DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE;

EID: 0029867362     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0061(19960330)12:4<333::aid-yea915>3.0.co;2-c     Document Type: Article
Times cited : (46)

References (59)
  • 1
    • 0027283562 scopus 로고
    • The amino-terminal amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum
    • Ahn, K., Szczesna-Skorupa, S. E. and Kemper, B. (1993). The amino-terminal amino acids of cytochrome P450 2C1 are sufficient for retention in the endoplasmic reticulum. J. Biol Chem. 268, 18726-18733.
    • (1993) J. Biol Chem. , vol.268 , pp. 18726-18733
    • Ahn, K.1    Szczesna-Skorupa, S.E.2    Kemper, B.3
  • 2
    • 0026569583 scopus 로고
    • Membrane topology of the mammalian P450 cytochromes
    • Black, S. D. (1992). Membrane topology of the mammalian P450 cytochromes. FASEB J. 6, 680-685.
    • (1992) FASEB J. , vol.6 , pp. 680-685
    • Black, S.D.1
  • 3
    • 0020490599 scopus 로고
    • Structural features of liver microsomal NADPH-cytochrome P450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region
    • Black, S. D. and Coon, M. J. (1982). Structural features of liver microsomal NADPH-cytochrome P450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region. J. Biol. Chem. 257, 5929-5938.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5929-5938
    • Black, S.D.1    Coon, M.J.2
  • 4
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M. S. and Munro, S. (1993). Cholesterol and the Golgi apparatus. Science 261, 1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 5
    • 0002830667 scopus 로고
    • Vectors for high level inducible expression of cloned genes in yeast
    • Inoye, M. (Ed.), Academic Press, New York
    • Broach, J. R., Li, Y.-Y, Wu, L.-C. C. and Jayaram, M. (1983). Vectors for high level inducible expression of cloned genes in yeast. In Inoye, M. (Ed.), Experimental Manipulation of Gene Expression. Academic Press, New York, pp. 83-117.
    • (1983) Experimental Manipulation of Gene Expression , pp. 83-117
    • Broach, J.R.1    Li, Y.-Y.2    Wu, L.-C.C.3    Jayaram, M.4
  • 6
    • 0141646834 scopus 로고
    • Appearance of crystalloid endoplasmic reticulum in compactin-resistant chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Chin, D. J., Luskey, K. L., Anderson, R. G. W., Faust, J. R., Goldstein, J. L. and Brown, M. S. (1982). Appearance of crystalloid endoplasmic reticulum in compactin-resistant chinese hamster cells with a 500-fold increase in 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc. Natl. Acad. Sci. USA 79, 1185-1189.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1185-1189
    • Chin, D.J.1    Luskey, K.L.2    Anderson, R.G.W.3    Faust, J.R.4    Goldstein, J.L.5    Brown, M.S.6
  • 7
    • 0025362658 scopus 로고
    • Recycling of proteins from the Golgi compartment to the ER in yeast
    • Dean, N. and Pelham, H. R. B. (1990). Recycling of proteins from the Golgi compartment to the ER in yeast. J. Cell Biol. 11, 369-377.
    • (1990) J. Cell Biol. , vol.11 , pp. 369-377
    • Dean, N.1    Pelham, H.R.B.2
  • 8
    • 0018801347 scopus 로고
    • 5 reduction by NADPH-cytochrome P450 reductase
    • 5 reduction by NADPH-cytochrome P450 reductase. J. Biol. Chem. 254, 8976-8981.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 9
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application on the endoplasmic reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S. and Lazarow, P. B. (1982). Isolation of intracellular membranes by means of sodium carbonate treatment: Application on the endoplasmic reticulum. J. Cell Biol 93, 97-102.
    • (1982) J. Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 10
    • 0016414490 scopus 로고
    • Beta-D-fructofuranoside fructohydrolase from yeast
    • Goldstein, A. and Lampen, J. O. (1975). Beta-D-fructofuranoside fructohydrolase from yeast. Meth. Enzymol. 42, 504-511.
    • (1975) Meth. Enzymol. , vol.42 , pp. 504-511
    • Goldstein, A.1    Lampen, J.O.2
  • 12
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., Rapoport, T. A. and Lodish, H. F (1989). Predicting the orientation of eukaryotic membrane-spanning proteins. Proc. Natl. Acad. Sci. USA 86, 5786-5790.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 13
    • 0020426041 scopus 로고
    • The cytochrome P-450 alkane monooxygenase system of Lodderomyces elongisporus: Purification and some properties of the NADPH-cytochrome P-450 reductase
    • Honeck, H., Schunck, W.-H., Riege, P. and Müller, H.-G. (1982). The cytochrome P-450 alkane monooxygenase system of Lodderomyces elongisporus: Purification and some properties of the NADPH-cytochrome P-450 reductase. Biochem. Biophys. Res. Commun. 106, 1318-1324.
    • (1982) Biochem. Biophys. Res. Commun. , vol.106 , pp. 1318-1324
    • Honeck, H.1    Schunck, W.-H.2    Riege, P.3    Müller, H.-G.4
  • 14
    • 0022254927 scopus 로고
    • Immunochemical analysis of rough and smooth microsomes from rat liver. Segregation of docking protein in rough membranes
    • Hortsch, M. and Meyer, D. I. (1985). Immunochemical analysis of rough and smooth microsomes from rat liver. Segregation of docking protein in rough membranes. Eur. J. Biochem. 150, 559-564.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 559-564
    • Hortsch, M.1    Meyer, D.I.2
  • 15
    • 0023202281 scopus 로고
    • Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum
    • Jingami, H., Brown, M. S., Goldstein, J. L., Anderson, R. G. W. and Luskey, K. L. (1987). Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum. J. Cell Biol. 104, 1693-1704.
    • (1987) J. Cell Biol. , vol.104 , pp. 1693-1704
    • Jingami, H.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.W.4    Luskey, K.L.5
  • 16
    • 0022938985 scopus 로고
    • Quantitative analysis of smooth and rough endoplasmic reticulum proliferation in differentiating hepatocytes of midpostnatal mice treated with phenobarbital
    • Kanai, K., Watanabe, J. and Kanamura, S. (1986). Quantitative analysis of smooth and rough endoplasmic reticulum proliferation in differentiating hepatocytes of midpostnatal mice treated with phenobarbital. J. Ultrastruct. Molec. Struct. Res. 97, 64-72.
    • (1986) J. Ultrastruct. Molec. Struct. Res. , vol.97 , pp. 64-72
    • Kanai, K.1    Watanabe, J.2    Kanamura, S.3
  • 17
    • 0022798555 scopus 로고
    • Molecular cloning and sequence analysis of full length cDNA for rabbit liver NADPH cytochrome P450 reductase mRNA
    • Katagiri, M., Murakami, H., Yabusaki, Y., Sugiyama, T., Okamoto, M., Yamano, T. and Ohkawa, H. (1986). Molecular cloning and sequence analysis of full length cDNA for rabbit liver NADPH cytochrome P450 reductase mRNA. J. Biochem. 100, 945-954.
    • (1986) J. Biochem. , vol.100 , pp. 945-954
    • Katagiri, M.1    Murakami, H.2    Yabusaki, Y.3    Sugiyama, T.4    Okamoto, M.5    Yamano, T.6    Ohkawa, H.7
  • 18
    • 0023832246 scopus 로고
    • A colony procedure for transformation of Saccharomyces cerevisiae
    • Keszenman-Peryra, D. and Hieda, K. (1988). A colony procedure for transformation of Saccharomyces cerevisiae. Curr. Genet. 13, 21-23.
    • (1988) Curr. Genet. , vol.13 , pp. 21-23
    • Keszenman-Peryra, D.1    Hieda, K.2
  • 19
    • 0021847027 scopus 로고
    • The detection and classification of membrane-spanning proteins
    • Klein, P., Kanehisa, M. and DeLisi, C. (1985). The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta 815, 468-476.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    DeLisi, C.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P450-containing hydroxytation system of liver microsomes into three components
    • Lu, A. Y. H., Junk, K. W. and Coon, M. J. (1969). Resolution of the cytochrome P450-containing hydroxytation system of liver microsomes into three components. J. Biol Chem. 244, 3714-3721.
    • (1969) J. Biol Chem. , vol.244 , pp. 3714-3721
    • Lu, A.Y.H.1    Junk, K.W.2    Coon, M.J.3
  • 23
    • 0021233394 scopus 로고
    • The induction of cytochrome P450 in the alkane-utilizing yeast Lodderomyces elongisporus: Alterations in the microsomal membrane fraction
    • Mauersberger, S., Schunck, W.-H. and Muller, H.-G. (1984). The induction of cytochrome P450 in the alkane-utilizing yeast Lodderomyces elongisporus: Alterations in the microsomal membrane fraction. Appl. Microbiol. Biotechnol. 19, 29-35.
    • (1984) Appl. Microbiol. Biotechnol. , vol.19 , pp. 29-35
    • Mauersberger, S.1    Schunck, W.-H.2    Muller, H.-G.3
  • 24
    • 0027630948 scopus 로고
    • Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase
    • Meijer, A. H., Lopes Cardoso, M. I., Voskuilen, J. T., de Waal, A., Verpoorte, R. and Hoge, J. H. C. (1993). Isolation and characterization of a cDNA clone from Catharanthus roseus encoding NADPH:cytochrome P-450 reductase. Plant J. 4, 47-60.
    • (1993) Plant J. , vol.4 , pp. 47-60
    • Meijer, A.H.1    Lopes Cardoso, M.I.2    Voskuilen, J.T.3    De Waal, A.4    Verpoorte, R.5    Hoge, J.H.C.6
  • 25
    • 0027929981 scopus 로고
    • The transmembrane region of microsomal cytochrome P450 identified as the endoplasmic reticulum retention signal
    • Murakami, K., Mihara, K. and Omura, T. (1994). The transmembrane region of microsomal cytochrome P450 identified as the endoplasmic reticulum retention signal. J. Biochem 116, 164-175.
    • (1994) J. Biochem , vol.116 , pp. 164-175
    • Murakami, K.1    Mihara, K.2    Omura, T.3
  • 26
    • 0027318045 scopus 로고
    • Kin recognition: A model for the retention of Golgi enzymes
    • Nilsson, T., Slusarewicz, P., Hoe, M. H. and Warren, G. (1993). Kin recognition: A model for the retention of Golgi enzymes. FEBS Lett. 330, 1-4.
    • (1993) FEBS Lett. , vol.330 , pp. 1-4
    • Nilsson, T.1    Slusarewicz, P.2    Hoe, M.H.3    Warren, G.4
  • 27
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus
    • Nilsson, T. and Warren, G. (1994). Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr Opin. Cell Biol. 6, 517-521.
    • (1994) Curr Opin. Cell Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 28
    • 0029337028 scopus 로고
    • Evidence that the expression of the gene for NADPH-cytochrome P450 reductase is n-alkane-inducible in Candida maltosa
    • Ohkuma, M., Masuda, Y., Park, S. M., Ohtomo, R., Ohta, A. and Takagi, M. (1995a). Evidence that the expression of the gene for NADPH-cytochrome P450 reductase is n-alkane-inducible in Candida maltosa. Biosci. Biotech. Biochem. 59, 1328-1330.
    • (1995) Biosci. Biotech. Biochem. , vol.59 , pp. 1328-1330
    • Ohkuma, M.1    Masuda, Y.2    Park, S.M.3    Ohtomo, R.4    Ohta, A.5    Takagi, M.6
  • 29
    • 0029061875 scopus 로고
    • Proliferation of intracellular membrane structures upon homologous overproduction of cytochrome P450 in Candida maltosa
    • Ohkuma, M., Park, S. M., Zimmer, T., Menzel., Vogel, F., Schunck, W.-H., Ohta, A. and Takagi, M. (1995b). Proliferation of intracellular membrane structures upon homologous overproduction of cytochrome P450 in Candida maltosa. Biochim. Biophys. Acta 1236, 163-169.
    • (1995) Biochim. Biophys. Acta , vol.1236 , pp. 163-169
    • Ohkuma, M.1    Park, S.M.2    Zimmer, T.3    Menzel4    Vogel, F.5    Schunck, W.-H.6    Ohta, A.7    Takagi, M.8
  • 30
    • 0017339034 scopus 로고
    • Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system
    • Ono, T., Ozasa, S., Hasegawa, F. and Imai, Y. (1977). Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system. Biochim. Biophys. Acta 486, 401-407.
    • (1977) Biochim. Biophys. Acta , vol.486 , pp. 401-407
    • Ono, T.1    Ozasa, S.2    Hasegawa, F.3    Imai, Y.4
  • 31
    • 0013785336 scopus 로고
    • Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes. A morphological and biochemical study
    • Orrenius, S., Ericson, J. L. E. and Ernster, L. (1965). Phenobarbital-induced synthesis of the microsomal drug-metabolizing enzyme system and its relationship to the proliferation of endoplasmic membranes. A morphological and biochemical study. J. Cell Biol. 25, 627-639.
    • (1965) J. Cell Biol. , vol.25 , pp. 627-639
    • Orrenius, S.1    Ericson, J.L.E.2    Ernster, L.3
  • 32
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H. R. B. (1989). Control of protein exit from the endoplasmic reticulum. Ann. Rev. Cell Biol. 5, 1-23.
    • (1989) Ann. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 33
    • 0025976756 scopus 로고
    • An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals
    • Porter, T. D. (1991). An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals. Trends Biochem. Sci. 16, 154-158.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 154-158
    • Porter, T.D.1
  • 34
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P450 oxidoreductase cDNA and identification of flavin-binding domains
    • Porter, T. D. and Kasper, C. B. (1985). Coding nucleotide sequence of rat NADPH-cytochrome P450 oxidoreductase cDNA and identification of flavin-binding domains. Proc. Natl. Acad. Sci. USA 82, 973-977.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 973-977
    • Porter, T.D.1    Kasper, C.B.2
  • 36
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C. J., Nothwehr, S. F. and Stevens, T. H. (1992). Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment. J. Cell Biol. 119, 69-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 39
    • 0024582440 scopus 로고
    • Characterization of the alkane-inducible cytochrome P-450 (P-450alk) gene from the yeast Candida tropicalis: Identification of a new P-450 gene family
    • Sanglard, D. and Loper, J. C. (1989). Characterization of the alkane-inducible cytochrome P-450 (P-450alk) gene from the yeast Candida tropicalis: Identification of a new P-450 gene family. Gene 76, 121-136.
    • (1989) Gene , vol.76 , pp. 121-136
    • Sanglard, D.1    Loper, J.C.2
  • 40
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter, B. A., Nelson, E. B., Marver, H. S. and Masters, B. S. S. (1972). Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J. Biol. Chem. 247, 3601-3607.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3601-3607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.S.4
  • 41
    • 3142575999 scopus 로고
    • Biochemical markers for yeast organelles
    • Strathern, J. N., Jones, E. W. and Broach, J. R. (Eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Schekman, R. (1982). Biochemical markers for yeast organelles. In Strathern, J. N., Jones, E. W. and Broach, J. R. (Eds), The Molecular Biology of the Yeast Saccharomyces cerevisiae. Metabolism and gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 651-652.
    • (1982) The Molecular Biology of the Yeast Saccharomyces Cerevisiae. Metabolism and Gene Expression , pp. 651-652
    • Schekman, R.1
  • 42
    • 0028298478 scopus 로고
    • Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3
    • Scheller, U., Kraft, R., Schröder, K.-L. and Schunck, W.-H. (1994). Generation of the soluble and functional cytosolic domain of microsomal cytochrome P450 52A3. J. Biol. Chem. 269, 12779-12783.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12779-12783
    • Scheller, U.1    Kraft, R.2    Schröder, K.-L.3    Schunck, W.-H.4
  • 44
    • 0025883783 scopus 로고
    • Comparison of two cytochromes P450 from Candida maltosa: Primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum
    • Schunck, W.-H., Vogel, F., Gross, B., Kärgel, E., Mauersberger, S., Köpke, K., Gengnagel, C. and Müller, H.-G. (1991). Comparison of two cytochromes P450 from Candida maltosa: Primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. Eur. J. Cell Biol. 55, 336-345.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 336-345
    • Schunck, W.-H.1    Vogel, F.2    Gross, B.3    Kärgel, E.4    Mauersberger, S.5    Köpke, K.6    Gengnagel, C.7    Müller, H.-G.8
  • 45
    • 0027406832 scopus 로고
    • Purification, characterization, and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean
    • Shet, M. S., Sathasivan, K., Arlotto, M. A., Mehdy, M. C. and Estabrook, R. W. (1993). Purification, characterization, and cDNA cloning of an NADPH-cytochrome P450 reductase from mung bean. Proc. Natl. Acad. Sci. USA 90, 2890-2894.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2890-2894
    • Shet, M.S.1    Sathasivan, K.2    Arlotto, M.A.3    Mehdy, M.C.4    Estabrook, R.W.5
  • 46
    • 0027169843 scopus 로고
    • Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae
    • Supply, P., Walch, A., Thinès-Sempoux, D. and Goffeau, A. (1993). Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae. J. Cell Biol. 268, 19744-19752.
    • (1993) J. Cell Biol. , vol.268 , pp. 19744-19752
    • Supply, P.1    Walch, A.2    Thinès-Sempoux, D.3    Goffeau, A.4
  • 47
    • 0024322441 scopus 로고
    • Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole
    • Sutter, T. R. and Loper, J. C. (1989). Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole. Biochem. Biophys. Res. Commun. 160, 1257-1266.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1257-1266
    • Sutter, T.R.1    Loper, J.C.2
  • 48
    • 0025043195 scopus 로고
    • Isolation and characterization of the alkane-inducible NADPH-cytochrome P450 oxidoreductase gene from Candida tropicalis
    • Sutter, T. R., Sanglard, D. and Loper, J. C. (1990). Isolation and characterization of the alkane-inducible NADPH-cytochrome P450 oxidoreductase gene from Candida tropicalis. J. Biol. Chem. 265, 16428-16436.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16428-16436
    • Sutter, T.R.1    Sanglard, D.2    Loper, J.C.3
  • 49
    • 0024318954 scopus 로고
    • Use of polyvinyl(pyrrolidone) and poly(vinylalcohol) for cryoultramicrotomy
    • Tokuyasu, K. T. (1989). Use of polyvinyl(pyrrolidone) and poly(vinylalcohol) for cryoultramicrotomy. Histochem. J 21, 163-171.
    • (1989) Histochem. J , vol.21 , pp. 163-171
    • Tokuyasu, K.T.1
  • 50
    • 0023137668 scopus 로고
    • Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase and carboxypeptidase Y in yeast cells at the ultrastructural level
    • Van Tuinen, E. and Riezman, H. (1987). Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase and carboxypeptidase Y in yeast cells at the ultrastructural level. J. Histochem. Cytochem. 35, 327-333.
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 327-333
    • Van Tuinen, E.1    Riezman, H.2
  • 52
    • 0016287623 scopus 로고
    • Highly purified detergent-solubilized NADPH-cytochrome P450 reductase from phenobarbital-induced rat liver microsomes
    • Vermilion, J. L. and Coon, M. J. (1974). Highly purified detergent-solubilized NADPH-cytochrome P450 reductase from phenobarbital-induced rat liver microsomes. Biochem. Biophys. Res. Commun. 60, 1315-1322.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 1315-1322
    • Vermilion, J.L.1    Coon, M.J.2
  • 53
    • 0025689948 scopus 로고
    • Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane
    • Vogel, F., Hartmann, E., Görlich, D. and Rapoport, T. A. (1990). Segregation of the signal sequence receptor protein in the rough endoplasmic reticulum membrane. Eur. J. Cell Biol. 53, 197-202.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 197-202
    • Vogel, F.1    Hartmann, E.2    Görlich, D.3    Rapoport, T.A.4
  • 54
    • 0026583004 scopus 로고
    • Immunocytochemical localization of alkane inducible cytochrome P-450 and its NADPH-dependent reductase in the yeast Candida maltosa
    • Vogel, F., Gengnagel, C., Kärgel, E., Müller, H.-G. and Schunck, W.-H. (1992). Immunocytochemical localization of alkane inducible cytochrome P-450 and its NADPH-dependent reductase in the yeast Candida maltosa. Eur. J. Cell Biol. 57, 285-291.
    • (1992) Eur. J. Cell Biol. , vol.57 , pp. 285-291
    • Vogel, F.1    Gengnagel, C.2    Kärgel, E.3    Müller, H.-G.4    Schunck, W.-H.5
  • 55
    • 0029108665 scopus 로고
    • Membrane protein assembly: Rules of the game
    • Von Heijne, G. (1995). Membrane protein assembly: Rules of the game. Bioessays 17, 25-30.
    • (1995) Bioessays , vol.17 , pp. 25-30
    • Von Heijne, G.1
  • 56
    • 0027732208 scopus 로고
    • Overexpression of ER-membrane protein P450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae
    • Wiedmann, B., Silver, P., Schunck, W.-H. and Wiedmann, M. (1993). Overexpression of ER-membrane protein P450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1153, 267-276.
    • (1993) Biochim. Biophys. Acta , vol.1153 , pp. 267-276
    • Wiedmann, B.1    Silver, P.2    Schunck, W.-H.3    Wiedmann, M.4
  • 57
    • 0023788653 scopus 로고
    • Increased amounts of HMG-CoA reductase induce 'karmellae': A proliferation of stacked membranes surrounding the yeast nucleus
    • Wright, R., Basson, M., D'Ari, L. and Rine, J. (1988). Increased amounts of HMG-CoA reductase induce 'karmellae': A proliferation of stacked membranes surrounding the yeast nucleus. J. Cell Biol 107, 101-114.
    • (1988) J. Cell Biol , vol.107 , pp. 101-114
    • Wright, R.1    Basson, M.2    D'Ari, L.3    Rine, J.4
  • 58
    • 0027141246 scopus 로고
    • Insights from inducible membranes
    • Wright, R. (1993). Insights from inducible membranes. Curr. Biol. 3, 870-873.
    • (1993) Curr. Biol. , vol.3 , pp. 870-873
    • Wright, R.1
  • 59
    • 0023899268 scopus 로고
    • Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene
    • Yabusaki, Y., Murakami, H. and Ohkawa, H. (1988). Primary structure of Saccharomyces cerevisiae NADPH-cytochrome P450 reductase deduced from nucleotide sequence of its cloned gene. J. Biochem. 103, 1004-1010.
    • (1988) J. Biochem. , vol.103 , pp. 1004-1010
    • Yabusaki, Y.1    Murakami, H.2    Ohkawa, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.