메뉴 건너뛰기




Volumn 44, Issue 10, 2003, Pages 1002-1012

Novel Glyoxysomal Protein Kinase, GPK1, Identified by Proteomic Analysis of Glyoxysomes in Etiolated Cotyledons of Arabidopsis thaliana

Author keywords

Arabidopsis; Etiolated cotyledon; Glyoxysomes; Protein kinase; Protein phosphorylation; Proteome

Indexed keywords

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; COTYLEDON; DARKNESS; FREE RADICAL SCAVENGERS; GLYOXYSOMES; HYDROGEN PEROXIDE; MOLECULAR SEQUENCE DATA; PLANT LEAVES; PROTEIN KINASES; PROTEOME;

EID: 0242403025     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/pcg145     Document Type: Article
Times cited : (70)

References (71)
  • 1
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative, The (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408: 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 3
    • 0001124810 scopus 로고
    • Microbodies in higher plants
    • Beevers, H. (1979) Microbodies in higher plants. Annu. Rev. Plant Physiol. 30: 159-193.
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 159-193
    • Beevers, H.1
  • 4
    • 0014216690 scopus 로고
    • Association of the glyoxylate cycle enzymes in a novel subcellular particle from castor bean endosperm
    • Breidenbach, R. and Beevers, H. (1967) Association of the glyoxylate cycle enzymes in a novel subcellular particle from castor bean endosperm. Biochem. Biophys. Res. Commun. 27: 462-469.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 462-469
    • Breidenbach, R.1    Beevers, H.2
  • 5
    • 0004881952 scopus 로고
    • Chromatographic and immunological evidence that chloroplastic and cytosolic pea (Pisum sativum L.) NADP-isocitrate dehydrogenases are distinct isoenzymes
    • Chen, R., Bismuth, E., Champigny, M. and Gadal, P. (1989) Chromatographic and immunological evidence that chloroplastic and cytosolic pea (Pisum sativum L.) NADP-isocitrate dehydrogenases are distinct isoenzymes. Planta 178: 157-163.
    • (1989) Planta , vol.178 , pp. 157-163
    • Chen, R.1    Bismuth, E.2    Champigny, M.3    Gadal, P.4
  • 6
    • 0024288496 scopus 로고
    • Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum) roots and green leaves
    • Chen, R., Le Maréchal, P., Vidal, J., Jacquot, J. and Gadal, P. (1988) Purification and comparative properties of the cytosolic isocitrate dehydrogenases (NADP) from pea (Pisum sativum) roots and green leaves. Eur. J. Biochem. 175: 565-572.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 565-572
    • Chen, R.1    Le Maréchal, P.2    Vidal, J.3    Jacquot, J.4    Gadal, P.5
  • 7
    • 0002233189 scopus 로고
    • Cytochemical study of catalase and peroxidase in the mesophyll of Lolium rigidum plants treated with isoproturon
    • de Felipe, M.R., Lucas, M.M. and Pozuelo, J.M. (1988) Cytochemical study of catalase and peroxidase in the mesophyll of Lolium rigidum plants treated with isoproturon. J. Plant Physiol. 132: 67-73.
    • (1988) J. Plant Physiol. , vol.132 , pp. 67-73
    • De Felipe, M.R.1    Lucas, M.M.2    Pozuelo, J.M.3
  • 9
    • 0000002944 scopus 로고
    • Development of enzymes of the glyoxylate cycle during senescence of pumpkin cotyledons
    • De Bellis, L. and Nishimura, M. (1991) Development of enzymes of the glyoxylate cycle during senescence of pumpkin cotyledons. Plant Cell Physiol. 32: 555-561.
    • (1991) Plant Cell Physiol. , vol.32 , pp. 555-561
    • De Bellis, L.1    Nishimura, M.2
  • 10
    • 0020482990 scopus 로고
    • Nicotinamide cofactors (NAD and NADP) in glyoxysomes, mitochondria, and plastids isolated from castor bean endosperm
    • Donaldson, R. (1982) Nicotinamide cofactors (NAD and NADP) 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.1
  • 11
    • 0029879509 scopus 로고    scopus 로고
    • The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop
    • Dyer, J.M., McNew, J.A. and Goodman, J.M. (1996) The sorting sequence of the peroxisomal integral membrane protein PMP47 is contained within a short hydrophilic loop. J. Cell Biol. 133: 269-280.
    • (1996) J. Cell Biol. , vol.133 , pp. 269-280
    • Dyer, J.M.1    McNew, J.A.2    Goodman, J.M.3
  • 14
    • 0034838201 scopus 로고    scopus 로고
    • Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons
    • Fukao, Y., Hayashi, Y., Mano, S., Hayashi, M. and Nishimura, M. (2001) Developmental analysis of a putative ATP/ADP carrier protein localized on glyoxysomal membranes during the peroxisome transition in pumpkin cotyledons. Plant Cell Physiol. 42: 835-841.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 835-841
    • Fukao, Y.1    Hayashi, Y.2    Mano, S.3    Hayashi, M.4    Nishimura, M.5
  • 15
    • 0036346730 scopus 로고    scopus 로고
    • Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana
    • Fukao, Y., Hayashi, M. and Nishimura, M. (2002) Proteomic analysis of leaf peroxisomal proteins in greening cotyledons of Arabidopsis thaliana. Plant Cell Physiol. 43: 689-696.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 689-696
    • Fukao, Y.1    Hayashi, M.2    Nishimura, M.3
  • 16
    • 0027972175 scopus 로고
    • Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells
    • Gálvez, S., Bismuth, E., Sarda, C. and Gadal, P. (1994) Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mixotrophic tobacco cells. Plant Physiol. 105: 593-600.
    • (1994) Plant Physiol. , vol.105 , pp. 593-600
    • Gálvez, S.1    Bismuth, E.2    Sarda, C.3    Gadal, P.4
  • 17
    • 0021758408 scopus 로고
    • A comparison of the phosphorylated and unphosphorylated forms of isocitrate dehydrogenase from Escherichia coli ML308
    • Garland, D. and Nimmo, H. (1984) A comparison of the phosphorylated and unphosphorylated forms of isocitrate dehydrogenase from Escherichia coli ML308. FEBS Lett. 9: 259-264.
    • (1984) FEBS Lett. , vol.9 , pp. 259-264
    • Garland, D.1    Nimmo, H.2
  • 18
    • 0018696727 scopus 로고
    • Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli
    • Garnak, M. and Reeves, H.C. (1979) Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli. J. Biol. Chem. 254: 7915-7920.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7915-7920
    • Garnak, M.1    Reeves, H.C.2
  • 19
    • 0020536476 scopus 로고
    • Serological differences between the multiple amine oxidases of yeasts and comparison of the specificities of the purified enzymes from Candida utilis and Pichia pastoris
    • Green, J., Haywood, G.W. and Large, P.J. (1983) Serological differences between the multiple amine oxidases of yeasts and comparison of the specificities of the purified enzymes from Candida utilis and Pichia pastoris. Biochem. J. 211: 481-493.
    • (1983) Biochem. J. , vol.211 , pp. 481-493
    • Green, J.1    Haywood, G.W.2    Large, P.J.3
  • 20
    • 0031106374 scopus 로고    scopus 로고
    • A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons
    • Hatano, K., Shimada, T., Hiraiwa, N., Nishimura, M. and Hara-Nishimura, I. (1997) A rapid increase in the level of binding protein (BiP) is accompanied by synthesis and degradation of storage proteins in pumpkin cotyledons. Plant Cell Physiol. 38: 334-351.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 334-351
    • Hatano, K.1    Shimada, T.2    Hiraiwa, N.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 21
    • 0033617449 scopus 로고    scopus 로고
    • A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes
    • Hayashi, H., Bellis, L.D., Ciurli, A., Kondo, M., Hayashi, M. and Nishimura, M. (1999) A novel acyl-CoA oxidase that can oxidize short-chain acyl-CoA in plant peroxisomes. J. Biol. Chem. 274: 12715-12721.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12715-12721
    • Hayashi, H.1    Bellis, L.D.2    Ciurli, A.3    Kondo, M.4    Hayashi, M.5    Nishimura, M.6
  • 22
    • 0032478790 scopus 로고    scopus 로고
    • Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin
    • Hayashi, H., Bellis, L.D., Yamaguchi, K., Kato, A., Hayashi, M. and Nishimura, M. (1998) Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin. J. Biol. Chem. 273: 8301-8307.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8301-8307
    • Hayashi, H.1    Bellis, L.D.2    Yamaguchi, K.3    Kato, A.4    Hayashi, M.5    Nishimura, M.6
  • 23
    • 0029310672 scopus 로고
    • Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons
    • Hayashi, M., Bellis, L.D., Alpi, A. and Nishimura, M. (1995) Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons. Plant Cell Physiol. 36: 669-680.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 669-680
    • Hayashi, M.1    Bellis, L.D.2    Alpi, A.3    Nishimura, M.4
  • 24
    • 0034331230 scopus 로고    scopus 로고
    • AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes
    • Hayashi, M., Nito, K., Toriyama-Kato, K., Kondo, M., Yamaya, T. and Nishimura, M. (2000) AtPex14p maintains peroxisomal functions by determining protein targeting to three kinds of plant peroxisomes. EMBO J. 19: 5701-5710.
    • (2000) EMBO J. , vol.19 , pp. 5701-5710
    • Hayashi, M.1    Nito, K.2    Toriyama-Kato, K.3    Kondo, M.4    Yamaya, T.5    Nishimura, M.6
  • 25
    • 0028970515 scopus 로고
    • 2,4-Dienoyl- CoA isomerase and thus possess all enzymes required for the β-oxidation of unsaturated fatty acids by a novel reductase-dependent pathway
    • 2,4-Dienoyl- CoA isomerase and thus possess all enzymes required for the β-oxidation of unsaturated fatty acids by a novel reductase-dependent pathway. Biochem. Biophys. Res. Commun. 215: 15-22.
    • (1995) Biochem. Biophys. Res. Commun. , vol.215 , pp. 15-22
    • He, X.Y.1    Shoukry, K.2    Chu, C.3    Yang, J.4    Sprecher, H.5    Schultz, H.6
  • 28
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-Hydroxydopa at the active site of bovine serum amine oxidase
    • Janes, S.M., Mu, D., Wemmer, D., Smith, A.J., Kaur, S., Maltby, D., Burlingame, A.L. and Klinman, J.P. (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 248: 981-987.
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.J.4    Kaur, S.5    Maltby, D.6    Burlingame, A.L.7    Klinman, J.P.8
  • 30
    • 0029110307 scopus 로고
    • Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin
    • Kato, A., Hayashi, M., Mori, H. and Nishimura, M. (1995) Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin. Plant Mol. Biol. 27: 377-390.
    • (1995) Plant Mol. Biol. , vol.27 , pp. 377-390
    • Kato, A.1    Hayashi, M.2    Mori, H.3    Nishimura, M.4
  • 31
    • 0030199279 scopus 로고    scopus 로고
    • DNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons
    • Kato, A., Hayashi, M., Takeuchi, Y. and Nishimura, M. (1996) cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons. Plant Mol. Biol. 31: 843-852.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 843-852
    • Kato, A.1    Hayashi, M.2    Takeuchi, Y.3    Nishimura, M.4
  • 32
    • 0032005089 scopus 로고    scopus 로고
    • Glyoxysomal malate dehydrogenase in pumpkin: Cloning of a cDNA and functional analysis of its presequence
    • Kato, A., Takada-Yoshikawa, Y., Hayashi, M., Kondo, M., Hara-Nishimura, I. and Nishimura, M. (1998) Glyoxysomal malate dehydrogenase in pumpkin: cloning of a cDNA and functional analysis of its presequence. Plant Cell Physiol. 39: 186-195.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 186-195
    • Kato, A.1    Takada-Yoshikawa, Y.2    Hayashi, M.3    Kondo, M.4    Hara-Nishimura, I.5    Nishimura, M.6
  • 33
    • 0033553562 scopus 로고    scopus 로고
    • Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry
    • Kirkman, H.N., Rolfo, M., Ferraris, A.M. and Gaetani, G.F. (1999) Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. J. Biol. Chem. 274: 13908-13914.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13908-13914
    • Kirkman, H.N.1    Rolfo, M.2    Ferraris, A.M.3    Gaetani, G.F.4
  • 34
    • 0035839528 scopus 로고    scopus 로고
    • Chloroplasts have a novel Cpn10 in addition to Cpn20 as cochaperonins in Arabidopsis thaliana
    • Koumoto, Y., Shimada, T., Kondo, M., Nishimura, M. and Hara-Nishimura, I. (2001) Chloroplasts have a novel Cpn10 in addition to Cpn20 as cochaperonins in Arabidopsis thaliana. J. Biol. Chem. 276: 29688-29694.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29688-29694
    • Koumoto, Y.1    Shimada, T.2    Kondo, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 36
    • 0029416813 scopus 로고
    • β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: A century of continued progress
    • Kunau, W.H., Dommes, V. and Schultz, H. (1995) β-Oxidation of fatty acids in mitochondria, peroxisomes, and bacteria: a century of continued progress. Prog. Lipid Res. 34: 267-342.
    • (1995) Prog. Lipid Res. , vol.34 , pp. 267-342
    • Kunau, W.H.1    Dommes, V.2    Schultz, H.3
  • 37
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial proteins in Arabidopsis
    • Kruft, V., Eubel, H., Jänsch, L., Werhahn, W. and Braun, H.P. (2001) Proteomic approach to identify novel mitochondrial proteins in Arabidopsis. Plant Physiol. 127: 1711-1727.
    • (2001) Plant Physiol. , vol.127 , pp. 1711-1727
    • Kruft, V.1    Eubel, H.2    Jänsch, L.3    Werhahn, W.4    Braun, H.P.5
  • 38
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 39
    • 0028225390 scopus 로고
    • A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis
    • LaBrie, S.T. and Crawford, N.M. (1994) A glycine to aspartic acid change in the MoCo domain of nitrate reductase reduces both activity and phosphorylation levels in Arabidopsis. J. Biol. Chem. 269: 14497-14501.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14497-14501
    • LaBrie, S.T.1    Crawford, N.M.2
  • 40
    • 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
  • 41
    • 0002191974 scopus 로고
    • Catalase
    • Edited by Bergmeyer, H.U. New York: Academic Press
    • Lück, H. (1965) Catalase. In Methods of Enzymatic Analysis. Edited by Bergmeyer, H.U. pp. 885-894. New York: Academic Press.
    • (1965) Methods of Enzymatic Analysis , pp. 885-894
    • Lück, H.1
  • 42
    • 0000412469 scopus 로고
    • Evidence for no proteolytic processing during transport of isocitrate lyase into glyoxysomes in castor bean endosperm
    • Maeshima, M., Yokoi, H. and Asahi, T. (1988) Evidence for no proteolytic processing during transport of isocitrate lyase into glyoxysomes in castor bean endosperm. Plant Cell Physiol. 29: 381-384.
    • (1988) Plant Cell Physiol. , vol.29 , pp. 381-384
    • Maeshima, M.1    Yokoi, H.2    Asahi, T.3
  • 43
    • 0000239675 scopus 로고    scopus 로고
    • The dynamics of seedling and cotyledon cell development in Arabidopsis thaliana during reserve mobilization
    • Mansfield, S.G. and Briarty, L.G. (1996) The dynamics of seedling and cotyledon cell development in Arabidopsis thaliana during reserve mobilization. Int. J. Plant Sci. 157: 280-295.
    • (1996) Int. J. Plant Sci. , vol.157 , pp. 280-295
    • Mansfield, S.G.1    Briarty, L.G.2
  • 44
    • 0029046136 scopus 로고
    • On the role of the peroxisome in ontogeny, ageing and degenerative disease
    • Masters, C.J. and Crane, D.I. (1995) On the role of the peroxisome in ontogeny, ageing and degenerative disease. Mech. Ageing Dev. 80: 69-83.
    • (1995) Mech. Ageing Dev. , vol.80 , pp. 69-83
    • Masters, C.J.1    Crane, D.I.2
  • 46
    • 0012593920 scopus 로고
    • Enzymic mechanism of starch breakdown in germinating rice seeds
    • Miyata, S., Okamoto, K., Watanabe, A. and Akazawa, T. (1981) Enzymic mechanism of starch breakdown in germinating rice seeds. Plant Physiol. 68: 1314-1318.
    • (1981) Plant Physiol. , vol.68 , pp. 1314-1318
    • Miyata, S.1    Okamoto, K.2    Watanabe, A.3    Akazawa, T.4
  • 47
    • 0000224759 scopus 로고
    • Purification and characterization of glyoxysomal enzymes from germinating pumpkin cotyledons
    • Mori, H., Yokota, S., Akazawa, T. and Nishimura, M. (1988) Purification and characterization of glyoxysomal enzymes from germinating pumpkin cotyledons. Plant Cell Physiol. 29: 449-460.
    • (1988) Plant Cell Physiol. , vol.29 , pp. 449-460
    • Mori, H.1    Yokota, S.2    Akazawa, T.3    Nishimura, M.4
  • 49
    • 0034717248 scopus 로고    scopus 로고
    • The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail
    • Mullen, R.T. and Trelease, R.N. (2000) The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail. J. Biol. Chem. 275: 16337-16344.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16337-16344
    • Mullen, R.T.1    Trelease, R.N.2
  • 50
    • 0035987380 scopus 로고    scopus 로고
    • Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulfite oxidase family
    • Nakamura, T., Meyer, C. and Sano, H. (2002) Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulfite oxidase family. J. Exp. Bot. 53: 1833-1836.
    • (2002) J. Exp. Bot. , vol.53 , pp. 1833-1836
    • Nakamura, T.1    Meyer, C.2    Sano, H.3
  • 51
    • 0001188298 scopus 로고
    • Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons
    • Nishimura, M., Takeuchi, Y., Bellis, L.D. and Hara-Nishimura, I. (1993) Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma 175: 131-137.
    • (1993) Protoplasma , vol.175 , pp. 131-137
    • Nishimura, M.1    Takeuchi, Y.2    Bellis, L.D.3    Hara-Nishimura, I.4
  • 52
    • 0035129650 scopus 로고    scopus 로고
    • Pumpkin peroxisomal ascorbate peroxidase is localized on peroxisomal membranes and unknown membranous structures
    • Nito, K., Yamaguchi, K., Kondo, M., Hayashi, M. and Nishimura, M. (2001) Pumpkin peroxisomal ascorbate peroxidase is localized on peroxisomal membranes and unknown membranous structures. Plant Cell Physiol. 42: 20-27.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 20-27
    • Nito, K.1    Yamaguchi, K.2    Kondo, M.3    Hayashi, M.4    Nishimura, M.5
  • 53
    • 0025801196 scopus 로고
    • Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes
    • Palma, J.M., Garrido, M., Rodriguez-Garcia, M.I. and del Rio, L.A. (1991) Peroxisome proliferation and oxidative stress mediated by activated oxygen species in plant peroxisomes. Arch. Biochem. Biophys. 287: 68-74.
    • (1991) Arch. Biochem. Biophys. , vol.287 , pp. 68-74
    • Palma, J.M.1    Garrido, M.2    Rodriguez-Garcia, M.I.3    Del Rio, L.A.4
  • 54
    • 0030901644 scopus 로고    scopus 로고
    • Natural senescence of pea leaves - An activated oxygen-mediated function for peroxisomes
    • Pastori, G.M. and Barroso, J.B. (1997) Natural senescence of pea leaves - an activated oxygen-mediated function for peroxisomes. Plant Physiol. 113: 411-418.
    • (1997) Plant Physiol. , vol.113 , pp. 411-418
    • Pastori, G.M.1    Barroso, J.B.2
  • 55
    • 0033614781 scopus 로고    scopus 로고
    • An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha
    • Plastino, J., Green, E.L., Sanders-Loehr, J. and Klinman, J.P. (1999) An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha. Biochemistry 38: 8204-8216.
    • (1999) Biochemistry , vol.38 , pp. 8204-8216
    • Plastino, J.1    Green, E.L.2    Sanders-Loehr, J.3    Klinman, J.P.4
  • 57
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • Peltier, J.B., Friso, G., Kalume, D.E., Roepstorff, P., Nillson, F., Adamaska, I. and van Wijk, K.J. (2000) Proteomics of the chloroplast: Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins. Plant Cell 12: 319-342.
    • (2000) Plant Cell , vol.12 , pp. 319-342
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nillson, F.5    Adamaska, I.6    Van Wijk, K.J.7
  • 58
    • 0000171468 scopus 로고
    • NADP-utilizing enzymes in the matrix of plant mitochondria
    • Rasmusson, A. and Moller, M. (1990) NADP-utilizing enzymes in the matrix of plant mitochondria. Plant Physiol. 94: 1012-1018.
    • (1990) Plant Physiol. , vol.94 , pp. 1012-1018
    • Rasmusson, A.1    Moller, M.2
  • 60
    • 0026625826 scopus 로고
    • NADPH-dependent β-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms
    • Smeland, T.E., Nada, M., Cuebas, D. and Schultz, H. (1992) NADPH-dependent β-oxidation of unsaturated fatty acids with double bonds extending from odd-numbered carbon atoms. Proc. Natl Acad. Sci. USA 89: 6673-6677.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6673-6677
    • Smeland, T.E.1    Nada, M.2    Cuebas, D.3    Schultz, H.4
  • 62
    • 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
  • 63
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76: 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 64
    • 0014409902 scopus 로고
    • Peroxisomes from spinach leaves containing enzymes related to glycolate metabolism
    • Tolbert, N.B., 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.B.1    Oeser, A.2    Kisaki, T.3    Hageman, R.H.4    Yamazaki, R.K.5
  • 65
    • 0031414412 scopus 로고    scopus 로고
    • Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: Implications for the biogenesis of topaquinone
    • Wilce, M.C., Dooley, D.M., Freeman, H.C., Guss, J.M., Matsunami, H., McIntire, W.S., Ruggiero, C.E., Tanizawa, K. and Yamaguchi, H. (1997) Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone. Biochemistry 36: 16116-16133.
    • (1997) Biochemistry , vol.36 , pp. 16116-16133
    • Wilce, M.C.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Matsunami, H.5    McIntire, W.S.6    Ruggiero, C.E.7    Tanizawa, K.8    Yamaguchi, H.9
  • 67
    • 0000221387 scopus 로고
    • Purification of glyoxysomal catalase and immunochemical comparison of glyoxysomal and leaf peroxisomal catalase in germinating pumpkin cotyledons
    • Yamaguchi, J. and Nishimura, M. (1984) Purification of glyoxysomal catalase and immunochemical comparison of glyoxysomal and leaf peroxisomal catalase in germinating pumpkin cotyledons. Plant Physiol. 74: 261-267.
    • (1984) Plant Physiol. , vol.74 , pp. 261-267
    • Yamaguchi, J.1    Nishimura, M.2
  • 68
    • 0000733003 scopus 로고
    • Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons
    • Yamaguchi, J., Nishimura, M. and Akazawa, T. (1984) Maturation of catalase precursor proceeds to a different extent in glyoxysomes and leaf peroxisomes of pumpkin cotyledons. Proc. Natl Acad. Sci. USA 81: 4809-4813.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4809-4813
    • Yamaguchi, J.1    Nishimura, M.2    Akazawa, T.3
  • 69
    • 85047684006 scopus 로고    scopus 로고
    • A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves
    • Yamada, K., Matsushima, R., Nishimura, M. and Hara-Nishimura, I. (2001) A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves. Plant Physiol. 127: 1626-1634.
    • (2001) Plant Physiol. , vol.127 , pp. 1626-1634
    • Yamada, K.1    Matsushima, R.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 70
    • 0014940421 scopus 로고
    • Enzymatic characterization of leaf peroxisomes
    • Yamazaki, R. and Tolbert, N. (1970) Enzymatic characterization of leaf peroxisomes. J. Biol. Chem. 245: 5137-5144.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5137-5144
    • Yamazaki, R.1    Tolbert, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.