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Volumn 148, Issue 3, 2008, Pages 1655-1667

Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 57749121325     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.108.128769     Document Type: Article
Times cited : (115)

References (65)
  • 1
    • 1242323413 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus
    • Anderson LE, Ringenberg MR, Carol AA (2004) Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus. Protoplasma 223: 33-43
    • (2004) Protoplasma , vol.223 , pp. 33-43
    • Anderson, L.E.1    Ringenberg, M.R.2    Carol, A.A.3
  • 4
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on bias and variance
    • Bolstad DM, Irizarry RA, Astrand M, Speed TP (2003) A comparison of normalization methods for high density oligonucleotide array data based on bias and variance. Bioinformatics 19: 185-193
    • (2003) Bioinformatics , vol.19 , pp. 185-193
    • Bolstad, D.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 5
    • 33646054582 scopus 로고    scopus 로고
    • Nuclear-encoded mitochondrial complex I gene expression is restored to normal levels by inhibition of unedited ATP9 transgene expression in Arabidopsis thaliana
    • Busi MV, Gomez-Casati DF, Perales M, Araya A, Zabaleta E (2006a) Nuclear-encoded mitochondrial complex I gene expression is restored to normal levels by inhibition of unedited ATP9 transgene expression in Arabidopsis thaliana. Plant Physiol Biochem 44: 1-6
    • (2006) Plant Physiol Biochem , vol.44 , pp. 1-6
    • Busi, M.V.1    Gomez-Casati, D.F.2    Perales, M.3    Araya, A.4    Zabaleta, E.5
  • 6
    • 33845520813 scopus 로고    scopus 로고
    • Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress
    • Busi MV, Maliandi MV, Valdez H, Clemente M, Zabaleta EJ, Araya A, Gomez-Casati DF (2006b) Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress. Plant J 48: 873-882
    • (2006) Plant J , vol.48 , pp. 873-882
    • Busi, M.V.1    Maliandi, M.V.2    Valdez, H.3    Clemente, M.4    Zabaleta, E.J.5    Araya, A.6    Gomez-Casati, D.F.7
  • 7
    • 0037163878 scopus 로고    scopus 로고
    • Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum)
    • Bustos DM, Iglesias AA (2002) Non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase is post-translationally phosphorylated in heterotrophic cells of wheat (Triticum aestivum). FEBS Lett 530: 169-173
    • (2002) FEBS Lett , vol.530 , pp. 169-173
    • Bustos, D.M.1    Iglesias, A.A.2
  • 8
    • 0347051814 scopus 로고    scopus 로고
    • Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins
    • Bustos DM, Iglesias AA (2003) Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins. Plant Physiol 133: 2081-2088
    • (2003) Plant Physiol , vol.133 , pp. 2081-2088
    • Bustos, D.M.1    Iglesias, A.A.2
  • 9
    • 0018786983 scopus 로고    scopus 로고
    • Cerff R, Chambers SE (1979) Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases (EC 1.2.1.12 and EC 1.2.1.13). J Biol Chem 254: 6094-6098
    • Cerff R, Chambers SE (1979) Subunit structure of higher plant glyceraldehyde-3-phosphate dehydrogenases (EC 1.2.1.12 and EC 1.2.1.13). J Biol Chem 254: 6094-6098
  • 10
    • 0036007901 scopus 로고    scopus 로고
    • A comparative study on diurnal changes in metabolite levels in the leaves of three crassulacean acid metabolism (CAM) species, Ananas comosus, Kalanchoe daigremontiana and K. pinnata
    • Chen LS, Lin Q, Nose A (2002) A comparative study on diurnal changes in metabolite levels in the leaves of three crassulacean acid metabolism (CAM) species, Ananas comosus, Kalanchoe daigremontiana and K. pinnata. J Exp Bot 53: 341-350
    • (2002) J Exp Bot , vol.53 , pp. 341-350
    • Chen, L.S.1    Lin, Q.2    Nose, A.3
  • 11
    • 6044241641 scopus 로고    scopus 로고
    • Large-scale identification of tubulin-binding proteins provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells
    • Chuong SD, Good AG, Taylor GJ, Freeman MC, Moorhead GB, Muench DG (2004) Large-scale identification of tubulin-binding proteins provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells. Mol Cell Proteomics 3: 970-983
    • (2004) Mol Cell Proteomics , vol.3 , pp. 970-983
    • Chuong, S.D.1    Good, A.G.2    Taylor, G.J.3    Freeman, M.C.4    Moorhead, G.B.5    Muench, D.G.6
  • 12
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 13
    • 0033080474 scopus 로고    scopus 로고
    • Mutations affecting induction of glycolytic and fermentative genes during germination and environmental stresses in Arabidopsis
    • Conley TR, Peng HP, Shih MC (1999) Mutations affecting induction of glycolytic and fermentative genes during germination and environmental stresses in Arabidopsis. Plant Physiol 119: 599-608
    • (1999) Plant Physiol , vol.119 , pp. 599-608
    • Conley, T.R.1    Peng, H.P.2    Shih, M.C.3
  • 16
    • 2442543417 scopus 로고    scopus 로고
    • Respiratory metabolism: Glycolysis, the TCA cycle and mitochondrial electron transport
    • Fernie AR, Carrari F, Sweetlove LJ (2004) Respiratory metabolism: glycolysis, the TCA cycle and mitochondrial electron transport. Curr Opin Plant Biol 7: 254-261
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 254-261
    • Fernie, A.R.1    Carrari, F.2    Sweetlove, L.J.3
  • 17
    • 0034640272 scopus 로고    scopus 로고
    • Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
    • Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275: 14031-14037
    • (2000) J Biol Chem , vol.275 , pp. 14031-14037
    • Fillinger, S.1    Boschi-Muller, S.2    Azza, S.3    Dervyn, E.4    Branlant, G.5    Aymerich, S.6
  • 20
    • 0343963061 scopus 로고    scopus 로고
    • Structural and kinetic characterization of NADP-dependent, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves
    • Gomez Casati DF, Sesma JI, Iglesias AA (2000) Structural and kinetic characterization of NADP-dependent, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves. Plant Sci 154: 107-115
    • (2000) Plant Sci , vol.154 , pp. 107-115
    • Gomez Casati, D.F.1    Sesma, J.I.2    Iglesias, A.A.3
  • 21
    • 37849026162 scopus 로고    scopus 로고
    • Glycolytic enzymes associate dynamically with mitochondria in response to respiratory demand and support substrate channeling
    • Graham JW, Williams TC, Morgan M, Fernie AR, Ratcliffe RG, Sweetlove LJ (2007) Glycolytic enzymes associate dynamically with mitochondria in response to respiratory demand and support substrate channeling. Plant Cell 19: 3723-3738
    • (2007) Plant Cell , vol.19 , pp. 3723-3738
    • Graham, J.W.1    Williams, T.C.2    Morgan, M.3    Fernie, A.R.4    Ratcliffe, R.G.5    Sweetlove, L.J.6
  • 23
    • 0031440371 scopus 로고    scopus 로고
    • The non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase: Biochemistry, structure, occurrence and evolution
    • Habenicht A (1997) The non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase: biochemistry, structure, occurrence and evolution. Biol Chem 378: 1413-1419
    • (1997) Biol Chem , vol.378 , pp. 1413-1419
    • Habenicht, A.1
  • 24
    • 0028330227 scopus 로고
    • Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH
    • Habenicht A, Hellman U, Cerff R (1994) Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH. JMol Biol 237: 165-171
    • (1994) JMol Biol , vol.237 , pp. 165-171
    • Habenicht, A.1    Hellman, U.2    Cerff, R.3
  • 25
    • 0028500170 scopus 로고
    • The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation
    • Hajdukiewiez P, Svab Z, Maliga P (1994) The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Mol Biol 25: 989-994
    • (1994) Plant Mol Biol , vol.25 , pp. 989-994
    • Hajdukiewiez, P.1    Svab, Z.2    Maliga, P.3
  • 26
    • 33747872541 scopus 로고    scopus 로고
    • The influence of cytosolic phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPC) on potato tuber metabolism
    • Hajirezaei MR, Biemelt S, Peisker M, Lytovchenko A, Fernie AR, Sonnewald U (2006) The influence of cytosolic phosphorylating glyceraldehyde 3-phosphate dehydrogenase (GAPC) on potato tuber metabolism. J Exp Bot 57: 2363-2377
    • (2006) J Exp Bot , vol.57 , pp. 2363-2377
    • Hajirezaei, M.R.1    Biemelt, S.2    Peisker, M.3    Lytovchenko, A.4    Fernie, A.R.5    Sonnewald, U.6
  • 27
    • 28444491773 scopus 로고    scopus 로고
    • Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis
    • Hancock JT, Henson D, Nyirenda M, Desikan R, Harrison J, Lewis M, Hughes J, Neill SJ (2005) Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis. Plant Physiol Biochem 43: 828-835
    • (2005) Plant Physiol Biochem , vol.43 , pp. 828-835
    • Hancock, J.T.1    Henson, D.2    Nyirenda, M.3    Desikan, R.4    Harrison, J.5    Lewis, M.6    Hughes, J.7    Neill, S.J.8
  • 28
    • 0030835681 scopus 로고    scopus 로고
    • Antisense repression of the mitochondrial NADH-binding subunit of complex I in transgenic potato plants induces male sterility
    • Heiser V, Rasmusson A, Thieck O, Brennicke A, Grohmann L (1997) Antisense repression of the mitochondrial NADH-binding subunit of complex I in transgenic potato plants induces male sterility. Plant Sci 127: 61-69
    • (1997) Plant Sci , vol.127 , pp. 61-69
    • Heiser, V.1    Rasmusson, A.2    Thieck, O.3    Brennicke, A.4    Grohmann, L.5
  • 29
    • 0032783532 scopus 로고    scopus 로고
    • Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: Comparison with 2′,7′-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123
    • Hempel SL, Buettner GR, O'Malley YQ, Wessels DA, Flaherty DM (1999) Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: comparison with 2′,7′-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2′,7′-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123. Free Radic Biol Med 27: 146-159
    • (1999) Free Radic Biol Med , vol.27 , pp. 146-159
    • Hempel, S.L.1    Buettner, G.R.2    O'Malley, Y.Q.3    Wessels, D.A.4    Flaherty, D.M.5
  • 30
    • 25144523910 scopus 로고    scopus 로고
    • Cytoskeleton-associated, carbohydrate-metabolizing enzymes in maize identified by yeast two-hybrid screening
    • Holtgrawe D, Scholz A, Altmann B, Scheibe R (2005) Cytoskeleton-associated, carbohydrate-metabolizing enzymes in maize identified by yeast two-hybrid screening. Physiol Plant 125: 141-156
    • (2005) Physiol Plant , vol.125 , pp. 141-156
    • Holtgrawe, D.1    Scholz, A.2    Altmann, B.3    Scheibe, R.4
  • 31
    • 0032434619 scopus 로고    scopus 로고
    • The role of mitochondrial electron transport during photosynthetic induction. A study with barley (Hordeum vulgare) protoplasts incubated with rotenone and oligomycin
    • Igamberdiev AU, Hurry V, Kromer S, Gardestrom P (1998) The role of mitochondrial electron transport during photosynthetic induction. A study with barley (Hordeum vulgare) protoplasts incubated with rotenone and oligomycin. Physiol Plant 104: 431-439
    • (1998) Physiol Plant , vol.104 , pp. 431-439
    • Igamberdiev, A.U.1    Hurry, V.2    Kromer, S.3    Gardestrom, P.4
  • 33
    • 0006196934 scopus 로고
    • A mechanism for the indirect transfer of photosynthetically reduced nicotinamide adenine dinucleotide phosphate from chloroplasts to the cytoplasm
    • Kelly GJ, Gibbs M (1973a) A mechanism for the indirect transfer of photosynthetically reduced nicotinamide adenine dinucleotide phosphate from chloroplasts to the cytoplasm. Plant Physiol 52: 674-676
    • (1973) Plant Physiol , vol.52 , pp. 674-676
    • Kelly, G.J.1    Gibbs, M.2
  • 34
    • 0002295359 scopus 로고
    • Nonreversible d-glyceraldehyde 3-phosphate dehydrogenase of plant tissues
    • Kelly GJ, Gibbs M (1973b) Nonreversible d-glyceraldehyde 3-phosphate dehydrogenase of plant tissues. Plant Physiol 52: 111-118
    • (1973) Plant Physiol , vol.52 , pp. 111-118
    • Kelly, G.J.1    Gibbs, M.2
  • 35
    • 0031909505 scopus 로고    scopus 로고
    • Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803
    • Koksharova O, Schubert M, Shestakov S, Cerff R (1998) Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 36: 183-194
    • (1998) Plant Mol Biol , vol.36 , pp. 183-194
    • Koksharova, O.1    Schubert, M.2    Shestakov, S.3    Cerff, R.4
  • 36
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li J, Kogan M, Knight SA, Pain D, Dancis A (1999) Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J Biol Chem 274: 33025-33034
    • (1999) J Biol Chem , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.3    Pain, D.4    Dancis, A.5
  • 37
    • 0001291049 scopus 로고
    • Occurrence of phosphorylating and non-phosphorylating NADP+-dependent gylceraldehyde 3-phosphate dehydrogenases in photosynthetic organisms
    • Mateos ML, Serrano A (1992) Occurrence of phosphorylating and non-phosphorylating NADP+-dependent gylceraldehyde 3-phosphate dehydrogenases in photosynthetic organisms. Plant Sci 84: 163-170
    • (1992) Plant Sci , vol.84 , pp. 163-170
    • Mateos, M.L.1    Serrano, A.2
  • 38
    • 0028316268 scopus 로고
    • Arguments against a close relationship between non-phosphorylating and phosphorylating glyceraldehyde-3-phosphate dehydrogenases
    • Michels S, Scagliarini S, Della Seta F, Carles C, Riva M, Trost P, Branlant G (1994) Arguments against a close relationship between non-phosphorylating and phosphorylating glyceraldehyde-3-phosphate dehydrogenases. FEBS Lett 339: 97-100
    • (1994) FEBS Lett , vol.339 , pp. 97-100
    • Michels, S.1    Scagliarini, S.2    Della Seta, F.3    Carles, C.4    Riva, M.5    Trost, P.6    Branlant, G.7
  • 39
    • 0034844069 scopus 로고    scopus 로고
    • Unravelling the role of mitochondria during oxidative stress in plants
    • Millar AH, Considine MJ, Day DA, Whelan J (2001) Unravelling the role of mitochondria during oxidative stress in plants. IUBMB Life 51: 201-205
    • (2001) IUBMB Life , vol.51 , pp. 201-205
    • Millar, A.H.1    Considine, M.J.2    Day, D.A.3    Whelan, J.4
  • 40
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Moller IM (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu Rev Plant Physiol Plant Mol Biol 52: 561-591
    • (2001) Annu Rev Plant Physiol Plant Mol Biol , vol.52 , pp. 561-591
    • Moller, I.M.1
  • 41
    • 3242749880 scopus 로고    scopus 로고
    • Protein oxidation in plant mitochondria as a stress indicator
    • Moller IM, Kristensen BK (2004) Protein oxidation in plant mitochondria as a stress indicator. Photochem Photobiol Sci 3: 730-735
    • (2004) Photochem Photobiol Sci , vol.3 , pp. 730-735
    • Moller, I.M.1    Kristensen, B.K.2
  • 43
    • 4644316529 scopus 로고    scopus 로고
    • Molecular evolution of the GapC gene family in Amsinckia spectabilis populations that differ in outcrossing rate
    • Perusse JR, Schoen DJ (2004) Molecular evolution of the GapC gene family in Amsinckia spectabilis populations that differ in outcrossing rate. J Mol Evol 59: 427-436
    • (2004) J Mol Evol , vol.59 , pp. 427-436
    • Perusse, J.R.1    Schoen, D.J.2
  • 44
    • 0042672742 scopus 로고    scopus 로고
    • Origin, evolution, and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids
    • Petersen J, Brinkmann H, Cerff R (2003) Origin, evolution, and metabolic role of a novel glycolytic GAPDH enzyme recruited by land plant plastids. J Mol Evol 57: 16-26
    • (2003) J Mol Evol , vol.57 , pp. 16-26
    • Petersen, J.1    Brinkmann, H.2    Cerff, R.3
  • 45
    • 0023056861 scopus 로고
    • Expression in plants of two bacterial antibiotic resistance genes after protoplast transformation with a new plant expression vector
    • Pietrzak M, Shillito RD, Hohn T, Potrykus I (1986) Expression in plants of two bacterial antibiotic resistance genes after protoplast transformation with a new plant expression vector. Nucleic Acids Res 14: 5857-5868
    • (1986) Nucleic Acids Res , vol.14 , pp. 5857-5868
    • Pietrzak, M.1    Shillito, R.D.2    Hohn, T.3    Potrykus, I.4
  • 46
    • 0024669157 scopus 로고
    • Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor oil endosperm and leaf
    • Plaxton WC (1989) Molecular and immunological characterization of plastid and cytosolic pyruvate kinase isozymes from castor oil endosperm and leaf. Eur J Biochem 181: 443-451
    • (1989) Eur J Biochem , vol.181 , pp. 443-451
    • Plaxton, W.C.1
  • 47
    • 0001259453 scopus 로고    scopus 로고
    • The organization and regulation of plant glycolysis
    • Plaxton WC (1996) The organization and regulation of plant glycolysis. Annu Rev Plant Physiol Plant Mol Biol 47: 185-214
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 185-214
    • Plaxton, W.C.1
  • 48
    • 33645536135 scopus 로고    scopus 로고
    • The functional organization and control of plant respiration
    • Plaxton WC, Podestá FE (2006) The functional organization and control of plant respiration. Crit Rev Plant Sci 25: 159-198
    • (2006) Crit Rev Plant Sci , vol.25 , pp. 159-198
    • Plaxton, W.C.1    Podestá, F.E.2
  • 49
    • 33747624376 scopus 로고    scopus 로고
    • Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
    • Rius SP, Casati P, Iglesias AA, Gomez-Casati DF (2006) Characterization of an Arabidopsis thaliana mutant lacking a cytosolic non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase. Plant Mol Biol 61: 945-957
    • (2006) Plant Mol Biol , vol.61 , pp. 945-957
    • Rius, S.P.1    Casati, P.2    Iglesias, A.A.3    Gomez-Casati, D.F.4
  • 50
    • 0000160467 scopus 로고
    • A pathway for photosynthetic carbon flow to mannitol in celery leaves: Activity and localization of key enzymes
    • Rumpho ME, Edwards GE, Loescher WH (1983) A pathway for photosynthetic carbon flow to mannitol in celery leaves: activity and localization of key enzymes. Plant Physiol 73: 869-873
    • (1983) Plant Physiol , vol.73 , pp. 869-873
    • Rumpho, M.E.1    Edwards, G.E.2    Loescher, W.H.3
  • 51
    • 0024707618 scopus 로고
    • Differential expression and sequence analysis of the maize glyceraldehyde-3-phosphate dehydrogenase gene family
    • Russell DA, Sachs MM (1989) Differential expression and sequence analysis of the maize glyceraldehyde-3-phosphate dehydrogenase gene family. Plant Cell 1: 793-803
    • (1989) Plant Cell , vol.1 , pp. 793-803
    • Russell, D.A.1    Sachs, M.M.2
  • 52
    • 0029201592 scopus 로고
    • Mechanisms of cadmium mobility and accumulation in Indian mustard
    • Salt DE, Prince RC, Pickering IJ, Raskin I (1995) Mechanisms of cadmium mobility and accumulation in Indian mustard. Plant Physiol 109: 1427-1433
    • (1995) Plant Physiol , vol.109 , pp. 1427-1433
    • Salt, D.E.1    Prince, R.C.2    Pickering, I.J.3    Raskin, I.4
  • 54
    • 33746917986 scopus 로고    scopus 로고
    • UDP-sugar pyrophosphorylase is essential for pollen development in Arabidopsis
    • Schnurr JA, Storey KK, Jung HJ, Somers DA, Gronwald JW (2006) UDP-sugar pyrophosphorylase is essential for pollen development in Arabidopsis. Planta 224: 520-532
    • (2006) Planta , vol.224 , pp. 520-532
    • Schnurr, J.A.1    Storey, K.K.2    Jung, H.J.3    Somers, D.A.4    Gronwald, J.W.5
  • 55
    • 2442675518 scopus 로고    scopus 로고
    • Effect of a pyruvate kinase (pykF-gene) knockout mutation on the control of gene expression and metabolic fluxes in Escherichia coli
    • Siddiquee KA, Arauzo-Bravo MJ, Shimizu K (2004) Effect of a pyruvate kinase (pykF-gene) knockout mutation on the control of gene expression and metabolic fluxes in Escherichia coli. FEMS Microbiol Lett 235: 25-33
    • (2004) FEMS Microbiol Lett , vol.235 , pp. 25-33
    • Siddiquee, K.A.1    Arauzo-Bravo, M.J.2    Shimizu, K.3
  • 56
    • 3242801382 scopus 로고    scopus 로고
    • Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited by oxidized thioredoxin
    • Sparla F, Fermani S, Falini G, Zaffagnini M, Ripamonti A, Sabatino P, Pupillo P, Trost P (2004) Coenzyme site-directed mutants of photosynthetic A4-GAPDH show selectively reduced NADPH-dependent catalysis, similar to regulatory AB-GAPDH inhibited by oxidized thioredoxin. J Mol Biol 340: 1025-1037
    • (2004) J Mol Biol , vol.340 , pp. 1025-1037
    • Sparla, F.1    Fermani, S.2    Falini, G.3    Zaffagnini, M.4    Ripamonti, A.5    Sabatino, P.6    Pupillo, P.7    Trost, P.8
  • 58
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher V, Tibshirani R, Chu G (2001) Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci USA 98: 5116-5121
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5116-5121
    • Tusher, V.1    Tibshirani, R.2    Chu, G.3
  • 59
    • 23944451857 scopus 로고    scopus 로고
    • Sugar-mediated transcriptional regulation of the Gap gene system and concerted photosystem II functional modulation in the microalga Scenedesmus vacuolatus
    • Valverde F, Ortega JM, Losada M, Serrano A (2005) Sugar-mediated transcriptional regulation of the Gap gene system and concerted photosystem II functional modulation in the microalga Scenedesmus vacuolatus. Planta 221: 937-952
    • (2005) Planta , vol.221 , pp. 937-952
    • Valverde, F.1    Ortega, J.M.2    Losada, M.3    Serrano, A.4
  • 60
    • 34547379957 scopus 로고    scopus 로고
    • Involvement of a cytoplasmic glyceraldehyde-3-phosphate dehydrogenase GapC-2 in low-phosphate-induced anthocyanin accumulation in Arabidopsis
    • Wang X, Chen Y, Zou J, Wu W (2007) Involvement of a cytoplasmic glyceraldehyde-3-phosphate dehydrogenase GapC-2 in low-phosphate-induced anthocyanin accumulation in Arabidopsis. Chin Sci Bull 52: 1764-1770
    • (2007) Chin Sci Bull , vol.52 , pp. 1764-1770
    • Wang, X.1    Chen, Y.2    Zou, J.3    Wu, W.4
  • 61
    • 57749116848 scopus 로고    scopus 로고
    • Transformation of Agrobacterium using the freeze-thaw method
    • doi/10.1101/pdb.prot4665
    • Weigel D, Glazebrook J (2006) Transformation of Agrobacterium using the freeze-thaw method. Cold Spring Harb Protoc doi/10.1101/pdb.prot4665
    • (2006) Cold Spring Harb Protoc
    • Weigel, D.1    Glazebrook, J.2
  • 62
    • 0000168597 scopus 로고
    • Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/ thioredoxin system
    • Wolosiuk RA, Buchanan BB (1978) Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/ thioredoxin system. Plant Physiol 61: 669-671
    • (1978) Plant Physiol , vol.61 , pp. 669-671
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 63
    • 0038038594 scopus 로고    scopus 로고
    • Phosphate starvation triggers distinct alterations of genome expression in Arabidopsis roots and leaves
    • Wu P, Ma L, Hou X, Wang M, Wu Y, Liu F, Deng XW (2003) Phosphate starvation triggers distinct alterations of genome expression in Arabidopsis roots and leaves. Plant Physiol 132: 1260-1271
    • (2003) Plant Physiol , vol.132 , pp. 1260-1271
    • Wu, P.1    Ma, L.2    Hou, X.3    Wang, M.4    Wu, Y.5    Liu, F.6    Deng, X.W.7
  • 64
    • 0000956444 scopus 로고
    • Luminometric method
    • HU Bergmeyer, ed, Verlag Chemie, Weinheim, Germany, pp
    • Wulff K, Döppen W (1985) Luminometric method. In HU Bergmeyer, ed, Methods of Enzymatic Analysis, Vol 7. Verlag Chemie, Weinheim, Germany, pp 357-364
    • (1985) Methods of Enzymatic Analysis , vol.7 , pp. 357-364
    • Wulff, K.1    Döppen, W.2
  • 65
    • 0027142302 scopus 로고
    • Stress responses and metabolic regulation of glyceraldehyde-3-phosphate dehydrogenase genes in Arabidopsis
    • Yang Y, Kwon HB, Peng HP, Shih MC (1993) Stress responses and metabolic regulation of glyceraldehyde-3-phosphate dehydrogenase genes in Arabidopsis. Plant Physiol 101: 209-216
    • (1993) Plant Physiol , vol.101 , pp. 209-216
    • Yang, Y.1    Kwon, H.B.2    Peng, H.P.3    Shih, M.C.4


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