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Volumn 7, Issue 6, 2012, Pages

Glycolate oxidase isozymes are coordinately controlled by GLO1 and GLO4 in rice

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXY ACID OXIDASE A; HYDROXY ACID OXIDASE A 1; HYDROXY ACID OXIDASE A 3; HYDROXY ACID OXIDASE A 4; HYDROXY ACID OXIDASE A 5; HYDROXY ACID OXIDASE A 6; UNCLASSIFIED DRUG;

EID: 84862734160     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039658     Document Type: Article
Times cited : (33)

References (50)
  • 1
    • 67651049051 scopus 로고    scopus 로고
    • Photorespiratory Metabolism: Genes, Mutants, Energetics, and Redox Signaling
    • Foyer CH, Bloom AJ, Queval G, Noctor G, (2009) Photorespiratory Metabolism: Genes, Mutants, Energetics, and Redox Signaling. Annu Rev Plant Biol 60: 455-484.
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 455-484
    • Foyer, C.H.1    Bloom, A.J.2    Queval, G.3    Noctor, G.4
  • 2
    • 0036593051 scopus 로고    scopus 로고
    • Drought and Oxidative Load in the Leaves of C3 Plants: a Predominant Role for Photorespiration
    • Noctor G, Veljovic JS, Driscoll S, Novitskaya L, Foyer CH, (2002) Drought and Oxidative Load in the Leaves of C3 Plants: a Predominant Role for Photorespiration. Ann Bot 89: 841-850.
    • (2002) Ann Bot , vol.89 , pp. 841-850
    • Noctor, G.1    Veljovic, J.S.2    Driscoll, S.3    Novitskaya, L.4    Foyer, C.H.5
  • 3
    • 85032070722 scopus 로고
    • Implications of water stress-induced changes in the levels of endogenous ascorbic acid and hydrogen peroxide in Vigna seedlings
    • Mukherjee SP, Choudhuri MA, (1983) Implications of water stress-induced changes in the levels of endogenous ascorbic acid and hydrogen peroxide in Vigna seedlings. Physiol Plant 58: 166-170.
    • (1983) Physiol Plant , vol.58 , pp. 166-170
    • Mukherjee, S.P.1    Choudhuri, M.A.2
  • 4
    • 0028385024 scopus 로고
    • Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought stress and following recovery from drought
    • Mittler R, Zilinskas BA, (1994) Regulation of pea cytosolic ascorbate peroxidase and other antioxidant enzymes during the progression of drought stress and following recovery from drought. Plant J 5: 397-405.
    • (1994) Plant J , vol.5 , pp. 397-405
    • Mittler, R.1    Zilinskas, B.A.2
  • 5
    • 0036853024 scopus 로고    scopus 로고
    • The Combined Effect of Drought Stress and Heat Shock on Gene Expression in Tobacco
    • Rizhsky L, Liang HJ, Mittler R, (2002) The Combined Effect of Drought Stress and Heat Shock on Gene Expression in Tobacco. Plant Physiol 130: 1143-1151.
    • (2002) Plant Physiol , vol.130 , pp. 1143-1151
    • Rizhsky, L.1    Liang, H.J.2    Mittler, R.3
  • 6
    • 0036923909 scopus 로고    scopus 로고
    • Arabidopsis thaliana derived resistance against Leptosphaeria maculans in a Brassica napus genomic background
    • Bohman S, Wang M, Dixelius C, (2002) Arabidopsis thaliana derived resistance against Leptosphaeria maculans in a Brassica napus genomic background. Theor Appl Genet 105: 498-504.
    • (2002) Theor Appl Genet , vol.105 , pp. 498-504
    • Bohman, S.1    Wang, M.2    Dixelius, C.3
  • 7
    • 1642423636 scopus 로고    scopus 로고
    • The white barley mutant Albostrians shows a supersusceptible but symptomless interaction phenotype with the hemibiotrophic fungus Bipolaris sorokiniana
    • Schäfer P, Huckelhoven R, Kogel KH, (2004) The white barley mutant Albostrians shows a supersusceptible but symptomless interaction phenotype with the hemibiotrophic fungus Bipolaris sorokiniana. Mol Plant Microbe Interact 17: 366-373.
    • (2004) Mol Plant Microbe Interact , vol.17 , pp. 366-373
    • Schäfer, P.1    Huckelhoven, R.2    Kogel, K.H.3
  • 8
    • 0842270049 scopus 로고    scopus 로고
    • Plant eR genes that encode photorespiratory enzymes confer resistance against disease
    • Taler D, Galperin M, Benjamin I, Cohen Y, Kenigsbuch D, (2004) Plant eR genes that encode photorespiratory enzymes confer resistance against disease. Plant Cell 16: 172-184.
    • (2004) Plant Cell , vol.16 , pp. 172-184
    • Taler, D.1    Galperin, M.2    Benjamin, I.3    Cohen, Y.4    Kenigsbuch, D.5
  • 9
    • 84863230574 scopus 로고    scopus 로고
    • Glycolate Oxidase Modulates Reactive Oxygen Species-Mediated Signal Transduction during Nonhost Resistance in Nicotiana benthamiana and Arabidopsis
    • Rojas CM, Senthil-Kumar M, Wang K, Ryu CM, Kaundal A, et al. (2012) Glycolate Oxidase Modulates Reactive Oxygen Species-Mediated Signal Transduction during Nonhost Resistance in Nicotiana benthamiana and Arabidopsis. Plant Cell 24: 1336-352.
    • (2012) Plant Cell , vol.24 , pp. 1336-1352
    • Rojas, C.M.1    Senthil-Kumar, M.2    Wang, K.3    Ryu, C.M.4    Kaundal, A.5
  • 10
    • 0005741867 scopus 로고
    • Chemical Inhibition of the Glycolate Pathway in Soybean Leaf Cells
    • Servaites JC, Ogren WL, (1977) Chemical Inhibition of the Glycolate Pathway in Soybean Leaf Cells. Plant Physiol 60: 461-466.
    • (1977) Plant Physiol , vol.60 , pp. 461-466
    • Servaites, J.C.1    Ogren, W.L.2
  • 11
    • 49049131273 scopus 로고
    • Glycollate oxidase inhibition and its effect on photosynthesis and pigment formation in Hordeum vulgare
    • Jenkins CLD, Rogers LJ, Kerr MW, (1982) Glycollate oxidase inhibition and its effect on photosynthesis and pigment formation in Hordeum vulgare. Phytochemistry 21: 1849-1858.
    • (1982) Phytochemistry , vol.21 , pp. 1849-1858
    • Jenkins, C.L.D.1    Rogers, L.J.2    Kerr, M.W.3
  • 12
    • 0035146277 scopus 로고    scopus 로고
    • An Early Arabidopsis Demonstration. Resolving a Few Issues Concerning Photorespiration
    • Somerville CR, (2001) An Early Arabidopsis Demonstration. Resolving a Few Issues Concerning Photorespiration. Plant Physiol 125: 20-24.
    • (2001) Plant Physiol , vol.125 , pp. 20-24
    • Somerville, C.R.1
  • 13
    • 0034489711 scopus 로고    scopus 로고
    • Reduction to below Threshold Levels of Glycolate Oxidase Activities in Transgenic Tobacco Enhances Photoinhibition during Irradiation
    • Yamaguchi K, Nishimura M, (2000) Reduction to below Threshold Levels of Glycolate Oxidase Activities in Transgenic Tobacco Enhances Photoinhibition during Irradiation. Plant Cell Physiol 41: 1397-1406.
    • (2000) Plant Cell Physiol , vol.41 , pp. 1397-1406
    • Yamaguchi, K.1    Nishimura, M.2
  • 14
    • 58449134896 scopus 로고    scopus 로고
    • High Glycolate Oxidase Activity is Required for Survival of Maize in Normal Air
    • Zelitch I, Schultes NP, Peterson RB, Brown P, Brutnell TP, (2009) High Glycolate Oxidase Activity is Required for Survival of Maize in Normal Air. Plant Physiol 149: 195-204.
    • (2009) Plant Physiol , vol.149 , pp. 195-204
    • Zelitch, I.1    Schultes, N.P.2    Peterson, R.B.3    Brown, P.4    Brutnell, T.P.5
  • 15
    • 65349195082 scopus 로고    scopus 로고
    • Inducible antisense suppression of glycolate oxidase reveals its strong regulation over photosynthesis in rice
    • Xu HW, Zhang JJ, Zeng JW, Jiang LR, Liu E, et al. (2009) Inducible antisense suppression of glycolate oxidase reveals its strong regulation over photosynthesis in rice. J Exp Bot 60: 1799-1809.
    • (2009) J Exp Bot , vol.60 , pp. 1799-1809
    • Xu, H.W.1    Zhang, J.J.2    Zeng, J.W.3    Jiang, L.R.4    Liu, E.5
  • 16
    • 27744454005 scopus 로고    scopus 로고
    • D-Glycerate 3-kinase, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family
    • Boldt R, Edner C, Kolukisaoglu Ü, Hagemann M, Weckwerth W, et al. (2005) D-Glycerate 3-kinase, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family. Plant Cell 17: 2413-2420.
    • (2005) Plant Cell , vol.17 , pp. 2413-2420
    • Boldt, R.1    Edner, C.2    Kolukisaoglu, Ü.3    Hagemann, M.4    Weckwerth, W.5
  • 17
    • 0000044510 scopus 로고
    • Genetic modification of photorespiration
    • Somerville CR, Ogren WL, (1982) Genetic modification of photorespiration. Trends biochem sci 7: 171-174.
    • (1982) Trends Biochem Sci , vol.7 , pp. 171-174
    • Somerville, C.R.1    Ogren, W.L.2
  • 18
    • 0000463899 scopus 로고
    • Preparation and some properties of crystalline glycolic acid oxidase of spinach
    • Frigerio NA, Harbury HA, (1958) Preparation and some properties of crystalline glycolic acid oxidase of spinach. J Biol Chem 231: 135-158.
    • (1958) J Biol Chem , vol.231 , pp. 135-158
    • Frigerio, N.A.1    Harbury, H.A.2
  • 19
    • 0001745167 scopus 로고
    • Purification and properties of glycollate oxidase from Pisum sativum leaves
    • Kerr MW, Groves D, (1975) Purification and properties of glycollate oxidase from Pisum sativum leaves. Phytochemistry 14: 359-362.
    • (1975) Phytochemistry , vol.14 , pp. 359-362
    • Kerr, M.W.1    Groves, D.2
  • 20
    • 0007909813 scopus 로고
    • Purification of glycollate oxidase from greening cucumber cotyledons
    • Behrends W, Rausch U, Löffler HG, Kindl H, (1982) Purification of glycollate oxidase from greening cucumber cotyledons. Planta 156: 566-571.
    • (1982) Planta , vol.156 , pp. 566-571
    • Behrends, W.1    Rausch, U.2    Löffler, H.G.3    Kindl, H.4
  • 22
    • 0007914255 scopus 로고
    • Purification and properties of glycollate oxidase from Lemna minor L
    • Emes MJ, Erismann KH, (1984) Purification and properties of glycollate oxidase from Lemna minor L. Int J Biochem 16: 1373-1378.
    • (1984) Int J Biochem , vol.16 , pp. 1373-1378
    • Emes, M.J.1    Erismann, K.H.2
  • 23
    • 0013038907 scopus 로고
    • Structure of glycolate oxidase from spinach
    • Lindqvist Y, Brändén CI, (1985) Structure of glycolate oxidase from spinach. Proc Natl Acad Sci USA 82: 6855-6859.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6855-6859
    • Lindqvist, Y.1    Brändén, C.I.2
  • 24
    • 0042710528 scopus 로고
    • Molecular weights of glycollate oxidase from C3 and C4 plants determined during early stages of purification
    • Hall NP, Reggiani R, Lea PJ, (1985) Molecular weights of glycollate oxidase from C3 and C4 plants determined during early stages of purification. Phytochemistry 24: 1645-1648.
    • (1985) Phytochemistry , vol.24 , pp. 1645-1648
    • Hall, N.P.1    Reggiani, R.2    Lea, P.J.3
  • 25
    • 0029788277 scopus 로고    scopus 로고
    • Purification and properties of glycolate oxidase from plants with different photosynthetic pathways: Distinctness of C4 enzyme from that of a C3 species and a C3-C4 intermediate
    • Devi MT, Rajagopalan AV, Raghavendara AS, (1996) Purification and properties of glycolate oxidase from plants with different photosynthetic pathways: Distinctness of C4 enzyme from that of a C3 species and a C3-C4 intermediate. Photosynth Res 47: 231-238.
    • (1996) Photosynth Res , vol.47 , pp. 231-238
    • Devi, M.T.1    Rajagopalan, A.V.2    Raghavendara, A.S.3
  • 26
    • 0343737503 scopus 로고    scopus 로고
    • Glycolate metabolism and subcellular distribution of glycolate oxidase in Spatoglossum pacificum (Phaeophyceae, Chromophyta)
    • Iwamoto K, Ikawa T, (1997) Glycolate metabolism and subcellular distribution of glycolate oxidase in Spatoglossum pacificum (Phaeophyceae, Chromophyta). Phycol Res 45: 77-83.
    • (1997) Phycol Res , vol.45 , pp. 77-83
    • Iwamoto, K.1    Ikawa, T.2
  • 27
    • 0033811956 scopus 로고    scopus 로고
    • A Novel Glycolate Oxidase Requiring Flavin Mononucleotide as the Cofactor in the Prasinophycean Alga Mesostigma viride
    • Iwamoto K, Ikawa T, (2000) A Novel Glycolate Oxidase Requiring Flavin Mononucleotide as the Cofactor in the Prasinophycean Alga Mesostigma viride. Plant Cell Physiol 41: 988-991.
    • (2000) Plant Cell Physiol , vol.41 , pp. 988-991
    • Iwamoto, K.1    Ikawa, T.2
  • 28
    • 0009948056 scopus 로고
    • Evidence for the Presence in Tobacco Leaves of Multiple Enzymes for the Oxidation of Glycolate and Glyoxylate
    • Havir EA, (1983) Evidence for the Presence in Tobacco Leaves of Multiple Enzymes for the Oxidation of Glycolate and Glyoxylate. Plant Physiol 71: 874-878.
    • (1983) Plant Physiol , vol.71 , pp. 874-878
    • Havir, E.A.1
  • 29
    • 0041427694 scopus 로고    scopus 로고
    • Glycolate oxidase isoforms are distributed between the bundle sheath and mesophyll tissues of maize leaves
    • Popov VN, Dmitrieva EA, Eprintsev AT, Igamberdiev AU, (2003) Glycolate oxidase isoforms are distributed between the bundle sheath and mesophyll tissues of maize leaves. J Plant Physiol 160: 851-857.
    • (2003) J Plant Physiol , vol.160 , pp. 851-857
    • Popov, V.N.1    Dmitrieva, E.A.2    Eprintsev, A.T.3    Igamberdiev, A.U.4
  • 30
    • 0031277483 scopus 로고    scopus 로고
    • Diverse Amino Acid Residues Function within the Type 1 Peroxisomal Targeting Signal (Implications for the Role of Accessory Residues Upstream of the Type 1 Peroxisomal Targeting Signal)
    • Mullen RT, Lee MS, Flynn CR, Trelease RN, (1997) Diverse Amino Acid Residues Function within the Type 1 Peroxisomal Targeting Signal (Implications for the Role of Accessory Residues Upstream of the Type 1 Peroxisomal Targeting Signal). Plant Physiol 115: 881-889.
    • (1997) Plant Physiol , vol.115 , pp. 881-889
    • Mullen, R.T.1    Lee, M.S.2    Flynn, C.R.3    Trelease, R.N.4
  • 31
    • 3042586212 scopus 로고    scopus 로고
    • Specification of the Peroxisome Targeting Signals Type 1 and Type 2 of Plant Peroxisomes by Bioinformatics Analyses
    • Sigrun Reumann, (2004) Specification of the Peroxisome Targeting Signals Type 1 and Type 2 of Plant Peroxisomes by Bioinformatics Analyses. Plant Physiol 135: 783-800.
    • (2004) Plant Physiol , vol.135 , pp. 783-800
    • Sigrun, R.1
  • 32
    • 0023665350 scopus 로고
    • The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone
    • Volokita M, Somerville CR, (1987) The primary structure of spinach glycolate oxidase deduced 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    Somerville, C.R.2
  • 33
    • 0005089898 scopus 로고
    • Characterization of a cDNA Encoding Lens culinaris Glycolate Oxidase and Developmental Expression of Glycolate Oxidase mRNA in Cotyledons and Leaves
    • Ludt C, Kindl H, (1990) Characterization of a cDNA Encoding Lens culinaris Glycolate Oxidase and Developmental Expression of Glycolate Oxidase mRNA in Cotyledons and Leaves. Plant Physiol 94: 1193-1198.
    • (1990) Plant Physiol , vol.94 , pp. 1193-1198
    • Ludt, C.1    Kindl, H.2
  • 34
    • 0027341713 scopus 로고
    • Cloning and Sequencing of cDNA for Glycolate Oxidase from Pumpkin Cotyledons and Northern Blot Analysis
    • Tsugeki R, Nishimura IH, Mori H, Nishimura M, (1993) Cloning and Sequencing of cDNA for Glycolate Oxidase from Pumpkin Cotyledons and Northern Blot Analysis. Plant Cell Physiol 34: 51-57.
    • (1993) Plant Cell Physiol , vol.34 , pp. 51-57
    • Tsugeki, R.1    Nishimura, I.H.2    Mori, H.3    Nishimura, M.4
  • 35
    • 57749111568 scopus 로고    scopus 로고
    • Generation of Hydrogen Peroxide in Chloroplasts of Arabidopsis Overexpressing Glycolate Oxidase as an Inducible System to Study Oxidative Stress
    • Fahnenstich H, Scarpeci TE, Valle EM, Flügge UI, Maurino VG, (2008) Generation of Hydrogen Peroxide in Chloroplasts of Arabidopsis Overexpressing Glycolate Oxidase as an Inducible System to Study Oxidative Stress. Plant Physiol 148: 719-729.
    • (2008) Plant Physiol , vol.148 , pp. 719-729
    • Fahnenstich, H.1    Scarpeci, T.E.2    Valle, E.M.3    Flügge, U.I.4    Maurino, V.G.5
  • 36
    • 0000377424 scopus 로고
    • Induction of Lactate Dehydrogenase Isozymes by Oxygen Deficit in Barley Root Tissue
    • Hoffman NE, Bent AF, Hanson AD, (1986) Induction of Lactate Dehydrogenase Isozymes by Oxygen Deficit in Barley Root Tissue. Plant Physiol 82: 658-663.
    • (1986) Plant Physiol , vol.82 , pp. 658-663
    • Hoffman, N.E.1    Bent, A.F.2    Hanson, A.D.3
  • 37
    • 0000183066 scopus 로고
    • Tissue-Specific Expression and Anaerobically Induced Posttranscriptional Modulation of Sucrose Synthase Genes in Sorghum bicolor M
    • Chourey PS, Taliercio EW, Kane EJ, (1991) Tissue-Specific Expression and Anaerobically Induced Posttranscriptional Modulation of Sucrose Synthase Genes in Sorghum bicolor M. Plant Physiol 96: 485-490.
    • (1991) Plant Physiol , vol.96 , pp. 485-490
    • Chourey, P.S.1    Taliercio, E.W.2    Kane, E.J.3
  • 38
    • 33645700621 scopus 로고    scopus 로고
    • Control of the Synthesis and Subcellular Targeting of the Two GDH Genes Products in Leaves and Stems of Nicotiana plumbaginifolia and Arabidopsis thaliana
    • Fontaine JX, Saladino F, Agrimonti C, Bedu M, Tercé-Laforgue T, et al. (2006) Control of the Synthesis and Subcellular Targeting of the Two GDH Genes Products in Leaves and Stems of Nicotiana plumbaginifolia and Arabidopsis thaliana. Plant Cell Physiol 47: 410-418.
    • (2006) Plant Cell Physiol , vol.47 , pp. 410-418
    • Fontaine, J.X.1    Saladino, F.2    Agrimonti, C.3    Bedu, M.4    Tercé-Laforgue, T.5
  • 39
    • 0035657169 scopus 로고    scopus 로고
    • Changes in the turnover of Rubisco and levels of mRNAs of rbcL and rbcS in rice leaves from emergence to senescence
    • Suzuki Y, Makino A, Mae T, (2001) Changes in the turnover of Rubisco and levels of mRNAs of rbcL and rbcS in rice leaves from emergence to senescence. Plant Cell Environ 24: 1353-1360.
    • (2001) Plant Cell Environ , vol.24 , pp. 1353-1360
    • Suzuki, Y.1    Makino, A.2    Mae, T.3
  • 40
    • 84855981107 scopus 로고    scopus 로고
    • Effect of individual suppression of RBCS multigene family on Rubisco contents in rice leaves
    • Ogawa S, Suzuki Y, Yoshizawa R, Kanno K, Makino A, (2012) Effect of individual suppression of RBCS multigene family on Rubisco contents in rice leaves. Plant Cell Environ 35: 546-553.
    • (2012) Plant Cell Environ , vol.35 , pp. 546-553
    • Ogawa, S.1    Suzuki, Y.2    Yoshizawa, R.3    Kanno, K.4    Makino, A.5
  • 41
    • 0030007956 scopus 로고    scopus 로고
    • Association of glycolate oxidation with photosynthetic electron transport in plant and algal chloroplasts
    • Goyal A, Tolbert NE, (1996) Association of glycolate oxidation with photosynthetic electron transport in plant and algal chloroplasts. Proc Natl Acad Sci USA 93: 3319-3324.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3319-3324
    • Goyal, A.1    Tolbert, N.E.2
  • 43
    • 0035983929 scopus 로고    scopus 로고
    • Distinct Physiological Roles of Fructokinase Isozymes Revealed by Gene-Specific Suppression of Frk1 and Frk2 Expression in Tomato
    • Odanaka S, Bennett AB, Kanayama Y, (2002) Distinct Physiological Roles of Fructokinase Isozymes Revealed by Gene-Specific Suppression of Frk1 and Frk2 Expression in Tomato. Plant Physiol 129: 1119-1126.
    • (2002) Plant Physiol , vol.129 , pp. 1119-1126
    • Odanaka, S.1    Bennett, A.B.2    Kanayama, Y.3
  • 45
    • 0020198680 scopus 로고
    • Electrophoresis buffers for polyacrylamide gels at various pH
    • McLellan T, (1982) Electrophoresis buffers for polyacrylamide gels at various pH. Anal Biochem 126: 94-99.
    • (1982) Anal Biochem , vol.126 , pp. 94-99
    • McLellan, T.1
  • 46
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (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
  • 47
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl RH, Gietz RD, (1989) High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genet 16: 339-346.
    • (1989) Curr Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 48
    • 33745605163 scopus 로고    scopus 로고
    • Oxalate accumulation and regulation is independent of glycolate oxidase in rice leaves
    • Xu HW, Ji XM, He ZH, Shi WP, Zhu GH, et al. (2006) Oxalate accumulation and regulation is independent of glycolate oxidase in rice leaves. J Exp Bot 57: 1899-1908.
    • (2006) J Exp Bot , vol.57 , pp. 1899-1908
    • Xu, H.W.1    Ji, X.M.2    He, Z.H.3    Shi, W.P.4    Zhu, G.H.5
  • 49
    • 7044239645 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in plants using bimolecular fluorescence complementation
    • Bracha-Drori K, Shichrur K, Katz A, Oliva M, Angelovici R, et al. (2004) Detection of protein-protein interactions in plants using bimolecular fluorescence complementation. Plant J 40: 419-427.
    • (2004) Plant J , vol.40 , pp. 419-427
    • Bracha-Drori, K.1    Shichrur, K.2    Katz, A.3    Oliva, M.4    Angelovici, R.5
  • 50
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


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