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Volumn 15, Issue 1, 1998, Pages 1-14

NADPH is a specific inhibitor of protein import into glyoxysomes

Author keywords

[No Author keywords available]

Indexed keywords

ASSAY; CELL ORGANELLE; GLYOXYSOME; IN VITRO STUDY; MEMBRANE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PEROXISOME; SENSITIVITY;

EID: 0032126744     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1998.00171.x     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 0026340914 scopus 로고
    • The carboxyl-terminal tripeptide Ala-Lys-IIe is essential for targeting Candida tropicalis trifunctional enzyme to yeast peroxisomes
    • Aitchison, J.D., Murray, W.W. and Rachubinski, R.A. (1991) The carboxyl-terminal tripeptide Ala-Lys-IIe is essential for targeting Candida tropicalis trifunctional enzyme to yeast peroxisomes. J. Biol. Chem. 266, 23197-23203.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23197-23203
    • Aitchison, J.D.1    Murray, W.W.2    Rachubinski, R.A.3
  • 2
    • 0020671498 scopus 로고
    • Preparation of a cell-free protein-synthesising system from wheat germ
    • Anderson, C.W., Straus, J.W. and Dudock, B.S. (1983) Preparation of a cell-free protein-synthesising system from wheat germ. Methods Enzymol. 101, 635-644.
    • (1983) Methods Enzymol. , vol.101 , pp. 635-644
    • Anderson, C.W.1    Straus, J.W.2    Dudock, B.S.3
  • 3
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris
    • Arnon, D.I. (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 4
    • 0027512241 scopus 로고
    • The carboxyl terminus of isocitrate lyase is not essential for import into glyoxysomes in an in vitro system
    • Behari, R. and Baker, A. (1993) The carboxyl terminus of isocitrate lyase is not essential for import into glyoxysomes in an in vitro system. J. Biol. Chem. 268, 7315-7322.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7315-7322
    • Behari, R.1    Baker, A.2
  • 5
    • 0014670256 scopus 로고
    • β-oxidation in glyoxysomes from castor bean endosperm
    • Cooper, T.G. and Beevers, H. (1969) β-oxidation in glyoxysomes from castor bean endosperm. J. Biol. Chem. 244, 3514-3520.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3514-3520
    • Cooper, T.G.1    Beevers, H.2
  • 7
    • 10144261887 scopus 로고    scopus 로고
    • A unified nomenclature for peroxisome biogensis factors
    • Distel, B., Erdmann, R., Gould, S.J. et al. (1996) A unified nomenclature for peroxisome biogensis factors. J. Cell Biol. 135, 1-3.
    • (1996) J. Cell Biol. , vol.135 , pp. 1-3
    • Distel, B.1    Erdmann, R.2    Gould, S.J.3
  • 8
    • 0020482990 scopus 로고
    • +) in glyoxysomes, mitochondria and plastids isolated from castor bean endosperm
    • +) in glyoxysomes, mitochondria and plastids isolated from castor bean endosperm. Arch. Biochem. Biophys. 215, 274-279.
    • (1982) Arch. Biochem. Biophys. , vol.215 , pp. 274-279
    • Donaldson, R.P.1
  • 9
    • 0002809161 scopus 로고
    • Electron transport in purified glyoxysomal membranes from castor-bean endosperm
    • Fang, T.K., Donaldson, R.P. and Vigil, E.L. (1987) Electron transport in purified glyoxysomal membranes from castor-bean endosperm. Planta, 172, 1-13.
    • (1987) Planta , vol.172 , pp. 1-13
    • Fang, T.K.1    Donaldson, R.P.2    Vigil, E.L.3
  • 10
    • 0030454683 scopus 로고    scopus 로고
    • Castor bean isocitrate lyase lacking the putative peroxisome targeting signal 1 ARM is imported into plant peroxisomes both in vitro and in vivo
    • Gao, X., Marrison, J.L., Pool, M.R., Leech, R.M. and Baker, A. (1996) Castor bean isocitrate lyase lacking the putative peroxisome targeting signal 1 ARM is imported into plant peroxisomes both in vitro and in vivo. Plant Physiol. 122, 1457-1464.
    • (1996) Plant Physiol. , vol.122 , pp. 1457-1464
    • Gao, X.1    Marrison, J.L.2    Pool, M.R.3    Leech, R.M.4    Baker, A.5
  • 11
    • 0028110118 scopus 로고
    • Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer
    • Glover, J.R., Andrews, D.W. and Rachubinski, R.A. (1994b) Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer. Proc. Natl Acad. Sci. USA, 91, 4908-4918.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4908-4918
    • Glover, J.R.1    Andrews, D.W.2    Rachubinski, R.A.3
  • 12
    • 0028278166 scopus 로고
    • Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo
    • Glover, J.R., Andrews, D.W., Subramani, S. and Rachubinski, R.A. (1994a) Mutagenesis of the amino targeting signal of Saccharomyces cerevisiae 3-ketoacyl-CoA thiolase reveals conserved amino acids required for import into peroxisomes in vivo. J. Biol. Chem. 269, 7558-7563.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7558-7563
    • Glover, J.R.1    Andrews, D.W.2    Subramani, S.3    Rachubinski, R.A.4
  • 13
    • 0030459304 scopus 로고    scopus 로고
    • Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p the PTS-1 receptor: Evidence that PTS-1 protein import is mediated by a cycling receptor
    • Gould, S.J. and Dodt, G. (1996) Multiple PEX genes are required for proper subcellular distribution and stability of Pex5p the PTS-1 receptor: evidence that PTS-1 protein import is mediated by a cycling receptor. J. Cell Biol. 135, 1763-1774.
    • (1996) J. Cell Biol. , vol.135 , pp. 1763-1774
    • Gould, S.J.1    Dodt, G.2
  • 15
    • 0028152032 scopus 로고
    • Carbon catabolite repression regulates glyoxylate cycle gene expression in cucumber
    • Graham, I.A., Denby, K.J. and Leaver, C.J. (1994) Carbon catabolite repression regulates glyoxylate cycle gene expression in cucumber. Plant Cell, 6, 761-772.
    • (1994) Plant Cell , vol.6 , pp. 761-772
    • Graham, I.A.1    Denby, K.J.2    Leaver, C.J.3
  • 16
    • 0000642178 scopus 로고
    • Apparent induction of key enzymes of the glyoxylic acid cycle in senescent barley leaves
    • Gut, H. and Matile, P. (1988) Apparent induction of key enzymes of the glyoxylic acid cycle in senescent barley leaves. Planta, 176, 548-550.
    • (1988) Planta , vol.176 , pp. 548-550
    • Gut, H.1    Matile, P.2
  • 17
    • 0030034571 scopus 로고    scopus 로고
    • Import of DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue, aminopterin
    • Häusler, T., Stierhof, Y., Wirtz, E. and Clayton, C. (1996) Import of DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue, aminopterin. J. Cell Biol. 132, 311-324.
    • (1996) J. Cell Biol. , vol.132 , pp. 311-324
    • Häusler, T.1    Stierhof, Y.2    Wirtz, E.3    Clayton, C.4
  • 18
    • 0030210553 scopus 로고    scopus 로고
    • Transport of chimeric proteins that contain a carboxyterminal targeting signal into plant microbodies
    • Hayashi, M., Aoki, M., Kato, A., Kondo, M. and Nishimura, M. (1996) Transport of chimeric proteins that contain a carboxyterminal targeting signal into plant microbodies. Plant. J. 10, 225-234.
    • (1996) Plant. J , vol.10 , pp. 225-234
    • Hayashi, M.1    Aoki, M.2    Kato, A.3    Kondo, M.4    Nishimura, M.5
  • 19
    • 0001560830 scopus 로고
    • Development and decline of the glyoxylate-cycle enzymes in watermelon seedlings (Citrullus vulgaris Schrad)
    • Hock, B. and Beevers, H. (1966) Development and decline of the glyoxylate-cycle enzymes in watermelon seedlings (Citrullus vulgaris Schrad). J. Pflanzenphysiol. 55, 405-414.
    • (1966) J. Pflanzenphysiol , vol.55 , pp. 405-414
    • Hock, B.1    Beevers, H.2
  • 20
    • 0023554848 scopus 로고
    • Control of flux through the citric acid cycle and the glyocylate bypass in Escherichia coli
    • Holms, W.H. (1989) Control of flux through the citric acid cycle and the glyocylate bypass in Escherichia coli. Biochem. Soc. Symp. 54, 17-31.
    • (1989) Biochem. Soc. Symp. , vol.54 , pp. 17-31
    • Holms, W.H.1
  • 21
    • 0011394066 scopus 로고
    • Light stimulated accumulation of the peroxisomal enzymes hydroxypyruvate reductase and serine:glyoxylate amino transferase and their translatable mRNAs in cotyledons of cucumber seedlings
    • Hondred, D., Wadle, D.M., Titus, D.E. and Becker, W.M. (1987) Light stimulated accumulation of the peroxisomal enzymes hydroxypyruvate reductase and serine:glyoxylate amino transferase and their translatable mRNAs in cotyledons of cucumber seedlings. Plant Mol. Biol. 9, 259-275.
    • (1987) Plant Mol. Biol. , vol.9 , pp. 259-275
    • Hondred, D.1    Wadle, D.M.2    Titus, D.E.3    Becker, W.M.4
  • 22
    • 0029054226 scopus 로고
    • Investigation of the energy requirement and targeting signal for the import of glycolate oxidase into glyoxysomes
    • Horng, J.T., Behari, R., Burke, L.E.C.-A. and Baker, A. (1995) Investigation of the energy requirement and targeting signal for the import of glycolate oxidase into glyoxysomes. Eur. J. Biochem. 230, 157-163.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 157-163
    • Horng, J.T.1    Behari, R.2    Burke, L.E.C.-A.3    Baker, A.4
  • 24
    • 0040557481 scopus 로고    scopus 로고
    • Evidence for the presence of the ascorbate glutathione cycle in mitochondria and peroxisomes of pea leaves
    • Jiménez, A., Hernández, J.A., del Rio, L.A. and Sevilla, F. (1997) Evidence for the presence of the ascorbate glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114, 275-284.
    • (1997) Plant Physiol. , vol.114 , pp. 275-284
    • Jiménez, A.1    Hernández, J.A.2    Del Rio, L.A.3    Sevilla, F.4
  • 25
    • 0030249391 scopus 로고    scopus 로고
    • Targeting and processing of a chimeric protein with the N-terminal presequence of the precursor to glyoxysomal citrate synthase
    • Kato, A., Hayashi, M., Kondo, M. and Nishimura, M. (1996) Targeting and processing of a chimeric protein with the N-terminal presequence of the precursor to glyoxysomal citrate synthase. Plant Cell, 8, 1601-1611.
    • (1996) Plant Cell , vol.8 , pp. 1601-1611
    • Kato, A.1    Hayashi, M.2    Kondo, M.3    Nishimura, M.4
  • 26
    • 0027483085 scopus 로고
    • Genetic approaches to studying peroxisome biogenesis
    • Lazarow, P.B. (1993) Genetic approaches to studying peroxisome biogenesis. Trends Cell Biol. 3, 89-93.
    • (1993) Trends Cell Biol. , vol.3 , pp. 89-93
    • Lazarow, P.B.1
  • 27
    • 0031080512 scopus 로고    scopus 로고
    • Oilseed isocitrate lyases lacking their essential type 1 peroxisome targeting signal are piggy backed to glyoxysomes
    • Lee, M.S., Mullen, R.T. and Trelease, R.N. (1997) Oilseed isocitrate lyases lacking their essential type 1 peroxisome targeting signal are piggy backed to glyoxysomes. Plant Cell, 9, 185-197.
    • (1997) Plant Cell , vol.9 , pp. 185-197
    • Lee, M.S.1    Mullen, R.T.2    Trelease, R.N.3
  • 29
    • 0028033934 scopus 로고
    • An oligomeric protein is imported into peroxisomes in vivo
    • McNew, J.A. and Goodman, J.M. (1994) An oligomeric protein is imported into peroxisomes in vivo. J. Cell Biol. 127, 1245-1257.
    • (1994) J. Cell Biol. , vol.127 , pp. 1245-1257
    • McNew, J.A.1    Goodman, J.M.2
  • 30
  • 32
    • 0027613630 scopus 로고
    • Targeting of castor bean glyoxysomal isocitrate lyase to tobacco leaf peroxisomes
    • Onyeocha, I., Behari, R., Hill, D. and Baker, A. (1993) Targeting of castor bean glyoxysomal isocitrate lyase to tobacco leaf peroxisomes. Plant Mol. Biol. 22, 385-396.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 385-396
    • Onyeocha, I.1    Behari, R.2    Hill, D.3    Baker, A.4
  • 34
    • 0028783455 scopus 로고    scopus 로고
    • How do proteins penetrate peroxisomes?
    • Rachubinski, R.A. and Subramani, S. (1996) How do proteins penetrate peroxisomes? Cell, 83, 525-528.
    • (1996) Cell , vol.83 , pp. 525-528
    • Rachubinski, R.A.1    Subramani, S.2
  • 35
    • 0031400792 scopus 로고    scopus 로고
    • Evidence for the presence of a porin in the membrane of glyoxysomes in castor bean
    • Reumann, S., Bettermann, M., Benz, R. and Heldt, H. (1997) Evidence for the presence of a porin in the membrane of glyoxysomes in castor bean. Plant Physiol. 115, 891-899.
    • (1997) Plant Physiol. , vol.115 , pp. 891-899
    • Reumann, S.1    Bettermann, M.2    Benz, R.3    Heldt, H.4
  • 36
    • 0028092345 scopus 로고
    • Compartmentation studies on spinach leaf peroxisomes. II. Evidence for the transfer of reductant from the cytosol to the peroxisomal compartment via a malate shuttle
    • Reumann, S., Heupel, R. and Heldt, H.W. (1994) Compartmentation studies on spinach leaf peroxisomes. II. Evidence for the transfer of reductant from the cytosol to the peroxisomal compartment via a malate shuttle. Planta, 193, 167-173.
    • (1994) Planta , vol.193 , pp. 167-173
    • Reumann, S.1    Heupel, R.2    Heldt, H.W.3
  • 37
    • 0029792163 scopus 로고    scopus 로고
    • A specific porin is involved in the malate shuttle of leaf peroxisomes
    • Reumann, S., Maier, E., Benz, R. and Heldt, H.W. (1996) A specific porin is involved in the malate shuttle of leaf peroxisomes. Biochem. Soc. Trans. 24, 754-757.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 754-757
    • Reumann, S.1    Maier, E.2    Benz, R.3    Heldt, H.W.4
  • 38
    • 0029064219 scopus 로고
    • The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions
    • van Roermund, C.W.T., Elgersma, Y., Singh, N., Wanders, R.J.A. and Tabak, H.F. (1995) The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions. EMBO J. 14, 3480-3486.
    • (1995) EMBO J , vol.14 , pp. 3480-3486
    • Van Roermund, C.W.T.1    Elgersma, Y.2    Singh, N.3    Wanders, R.J.A.4    Tabak, H.F.5
  • 39
    • 0032472937 scopus 로고    scopus 로고
    • Peroxisomal β-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: Isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions
    • van Roermund, C.W.T., Hettema, E., Kai, A.J., van den Berg, M., Tabak, H.F. and Wanders, R.J.A. (1998) Peroxisomal β-oxidation of polyunsaturated fatty acids in Saccharomyces cerevisiae: isocitrate dehydrogenase provides NADPH for reduction of double bonds at even positions. EMBO J. 17, 677-687.
    • (1998) EMBO J , vol.17 , pp. 677-687
    • Van Roermund, C.W.T.1    Hettema, E.2    Kai, A.J.3    Van den Berg, M.4    Tabak, H.F.5    Wanders, R.J.A.6
  • 40
    • 0030020584 scopus 로고    scopus 로고
    • Distinct cis-acting elements direct the germination and sugar responses of the cucumber malate synthase gene
    • Sarah, C.J., Graham, I.A., Reynolds, S.J., Leaver, C.J. and Smith, S.M. (1996) Distinct cis-acting elements direct the germination and sugar responses of the cucumber malate synthase gene. Mol. Gen. Genet. 250, 153-161.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 153-161
    • Sarah, C.J.1    Graham, I.A.2    Reynolds, S.J.3    Leaver, C.J.4    Smith, S.M.5
  • 41
    • 0000545202 scopus 로고
    • Purification of peroxisomes and mitochondria from spinach leaf by Percoll gradient centrifugation
    • Schwitzguebel, J.P. and Siegenthaler, P.A. (1984) Purification of peroxisomes and mitochondria from spinach leaf by Percoll gradient centrifugation. Plant Physiol. 75, 670-674.
    • (1984) Plant Physiol. , vol.75 , pp. 670-674
    • Schwitzguebel, J.P.1    Siegenthaler, P.A.2
  • 42
    • 0343042875 scopus 로고
    • Promoter analysis of a light regulated gene encoding hydroxypyruvate reductase, an enzyme of the photorespiratory glycolate pathway
    • Sloan, J.S., Schwartz, B.W. and Becker, W.M. (1993) Promoter analysis of a light regulated gene encoding hydroxypyruvate reductase, an enzyme of the photorespiratory glycolate pathway. Plant J. 3, 867-874.
    • (1993) Plant J. , vol.3 , pp. 867-874
    • Sloan, J.S.1    Schwartz, B.W.2    Becker, W.M.3
  • 43
    • 0025941962 scopus 로고
    • A novel cleavable peroxisomal targeting signal at the aminoterminus of rat 3-ketoacyl-CoA thiolase
    • Swinkels, B.W., Gould, S.J., Bodnar, A.G., Rachubinski, R.A. and Subramani, S. (1991) A novel cleavable peroxisomal targeting signal at the aminoterminus of rat 3-ketoacyl-CoA thiolase. EMBO J. 10, 3255-3262.
    • (1991) EMBO J. , vol.10 , pp. 3255-3262
    • Swinkels, B.W.1    Gould, S.J.2    Bodnar, A.G.3    Rachubinski, R.A.4    Subramani, S.5
  • 44
    • 0000770579 scopus 로고
    • The redox state of the NADP system in illuminated chloroplasts
    • Takahama, U., Shimizu-Takahama, M. and Heber, U. (1981) The redox state of the NADP system in illuminated chloroplasts. Biochim. Biophys. Acta, 637, 530-539.
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 530-539
    • Takahama, U.1    Shimizu-Takahama, M.2    Heber, U.3
  • 45
    • 0022395410 scopus 로고
    • Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double label immunoelectron microscopy
    • Titus, D.E. and Becker, W.M. (1985) Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double label immunoelectron microscopy. J. Cell Biol. 101, 1288-1299.
    • (1985) J. Cell Biol. , vol.101 , pp. 1288-1299
    • Titus, D.E.1    Becker, W.M.2
  • 46
    • 0016369244 scopus 로고
    • Isolation of subcellular organelles of metabolism on isopycnic sucrose gradients
    • Tolbert, N.E. (1974) Isolation of subcellular organelles of metabolism on isopycnic sucrose gradients. Methods Enzymol. 31A, 734-746.
    • (1974) Methods Enzymol. , vol.31 A , pp. 734-746
    • Tolbert, N.E.1
  • 47
    • 0019349080 scopus 로고
    • Metabolic pathways in glyoxysomes and peroxisomes
    • Tolbert, N.E. (1981) Metabolic pathways in glyoxysomes and peroxisomes. Annu. Rev. Biochem. 50, 133-157.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 133-157
    • Tolbert, N.E.1
  • 48
    • 0014409902 scopus 로고
    • Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism
    • Tolbert, N.E., Oeser, A., Kisaki, T., Hageman, R.H. and Yamazaki, R.K. (1968) Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism. J, Biol. Chem. 243, 5179-5184.
    • (1968) J Biol. Chem. , vol.243 , pp. 5179-5184
    • Tolbert, N.E.1    Oeser, A.2    Kisaki, T.3    Hageman, R.H.4    Yamazaki, R.K.5
  • 49
    • 0025954516 scopus 로고
    • NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids
    • Tserng, K.-Y. and Jin, S.-J. (1990) NADPH-dependent reductive metabolism of cis-5 unsaturated fatty acids. J Biol. Chem. 266, 11614-11620.
    • (1990) J Biol. Chem. , vol.266 , pp. 11614-11620
    • Tserng, K.-Y.1    Jin, S.-J.2
  • 50
    • 0028108279 scopus 로고
    • Characterisation of the signal peptide at the amino terminus of the rat peroxisomal 3-ketoacyl-CoA thiolase precursor
    • Tsukamoto, T., Hata, S., Yokota, S., Miura, S., Fujiki, Y., Hijikata, M., Miyazawa, S., Hashimoto, T. and Osumi, T. (1994) Characterisation of the signal peptide at the amino terminus of the rat peroxisomal 3-ketoacyl-CoA thiolase precursor. J. Biol. Chem. 269, 6001-6010.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6001-6010
    • Tsukamoto, T.1    Hata, S.2    Yokota, S.3    Miura, S.4    Fujiki, Y.5    Hijikata, M.6    Miyazawa, S.7    Hashimoto, T.8    Osumi, T.9
  • 51
    • 0026254622 scopus 로고
    • Thecarboxyl-terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes
    • Volokita, M. (1991) Thecarboxyl-terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes. Plant J. 1, 361-366.
    • (1991) Plant J , vol.1 , pp. 361-366
    • Volokita, M.1
  • 52
    • 0023665350 scopus 로고
    • The primary structure of spinach glycolate oxidase from the DNA sequence of a cDNA clone
    • Volokita, M. and Sommerville, C.R. (1987) The primary structure of spinach glycolate oxidase from the DNA sequence of a cDNA clone. J. Biol. Chem, 262, 15825-15828.
    • (1987) J. Biol. Chem , vol.262 , pp. 15825-15828
    • Volokita, M.1    Sommerville, C.R.2
  • 53
    • 0029010680 scopus 로고
    • Import of stably folded proteins into peroxisomes
    • Walton, P.A., Hill, P.E. and Subramani, S. (1995) Import of stably folded proteins into peroxisomes. Mol. Biol. Cell, 6, 675-683.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 675-683
    • Walton, P.A.1    Hill, P.E.2    Subramani, S.3
  • 54
    • 0026492912 scopus 로고
    • Protein A fusion vectors for use in combination with pEX vectors in the production and affinity purification of specific antibodies
    • Zueco, J. and Boyd, A. (1992) Protein A fusion vectors for use in combination with pEX vectors in the production and affinity purification of specific antibodies. Gene, 121, 181-182.
    • (1992) Gene , vol.121 , pp. 181-182
    • Zueco, J.1    Boyd, A.2


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