메뉴 건너뛰기




Volumn 72, Issue 3, 2009, Pages 475-483

Hunting for low abundant redox proteins in plant plasma membranes

Author keywords

In gel activity staining; Lipid rafts; Native PAGE; Plasma membrane proteome; Protein protein interactions; Redox systems

Indexed keywords

CELL MEMBRANE PROTEIN; LACTATE DEHYDROGENASE (CYTOCHROME); OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 63349101065     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.11.001     Document Type: Review
Times cited : (14)

References (94)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 28444437064 scopus 로고    scopus 로고
    • Membranes are more mosaic than fluid
    • Engelman D.M. Membranes are more mosaic than fluid. Nature 438 (2005) 578-580
    • (2005) Nature , vol.438 , pp. 578-580
    • Engelman, D.M.1
  • 3
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 4
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., and London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14 (1998) 111-136
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 5
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: heterogeneity on the high seas
    • Pike L.J. Lipid rafts: heterogeneity on the high seas. Biochem J 378 (2004) 281-292
    • (2004) Biochem J , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 6
    • 28444451916 scopus 로고    scopus 로고
    • Lipid rafts in plants
    • Bath R.A., and Panstruga R. Lipid rafts in plants. Planta 223 (2005) 5-19
    • (2005) Planta , vol.223 , pp. 5-19
    • Bath, R.A.1    Panstruga, R.2
  • 7
    • 20444426256 scopus 로고    scopus 로고
    • Lipid microdomains - plant membranes get organized
    • Martin S.W., Glover B.J., and Davies J.M. Lipid microdomains - plant membranes get organized. Trends Plant Sci 10 (2005) 263-265
    • (2005) Trends Plant Sci , vol.10 , pp. 263-265
    • Martin, S.W.1    Glover, B.J.2    Davies, J.M.3
  • 9
    • 33845885533 scopus 로고    scopus 로고
    • The proteomics of plant cell membranes
    • Komatsu S., Konishi H., and Hashimoto M. The proteomics of plant cell membranes. J Exp Bot 58 (2007) 103-112
    • (2007) J Exp Bot , vol.58 , pp. 103-112
    • Komatsu, S.1    Konishi, H.2    Hashimoto, M.3
  • 12
    • 33646227179 scopus 로고    scopus 로고
    • Methods of quantitative proteomics and their application to plant organelle characterization
    • Lilley K.S., and Dupree P. Methods of quantitative proteomics and their application to plant organelle characterization. J Exp Bot 57 (2005) 1493-1499
    • (2005) J Exp Bot , vol.57 , pp. 1493-1499
    • Lilley, K.S.1    Dupree, P.2
  • 13
    • 44449176711 scopus 로고    scopus 로고
    • Analysis of the Oryza sativa plasma membrane proteome using combined protein and peptide fractionation approaches in conjunction with mass spectrometry
    • Natera S.H.A., Ford K.L., Cassin A.M., Patterson J.H., Newbigin E.J., and Bacic A. Analysis of the Oryza sativa plasma membrane proteome using combined protein and peptide fractionation approaches in conjunction with mass spectrometry. J Proteome Res 7 (2008) 1159-1187
    • (2008) J Proteome Res , vol.7 , pp. 1159-1187
    • Natera, S.H.A.1    Ford, K.L.2    Cassin, A.M.3    Patterson, J.H.4    Newbigin, E.J.5    Bacic, A.6
  • 14
    • 38449119746 scopus 로고    scopus 로고
    • Identification of enzymes and activity from two-dimensional gel electrophoresis
    • Afjehi-Sadat L., and Lubec G. Identification of enzymes and activity from two-dimensional gel electrophoresis. Nat Protoc 2 (2007) 2318-2324
    • (2007) Nat Protoc , vol.2 , pp. 2318-2324
    • Afjehi-Sadat, L.1    Lubec, G.2
  • 15
    • 33744901613 scopus 로고    scopus 로고
    • Blue-native PAGE in plants: a tool in analysis of protein-protein interactions
    • 10.1186/1746-4811-1-11
    • Eubel H., Braun H.P., and Millar A.H. Blue-native PAGE in plants: a tool in analysis of protein-protein interactions. Plant Methods 1 (2005) 11 10.1186/1746-4811-1-11
    • (2005) Plant Methods , vol.1 , pp. 11
    • Eubel, H.1    Braun, H.P.2    Millar, A.H.3
  • 16
    • 34547138661 scopus 로고    scopus 로고
    • High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes
    • Wittig I., Karas M., and Schägger H. High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes. Mol Cell Proteomics 6 (2007) 1215-1225
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1215-1225
    • Wittig, I.1    Karas, M.2    Schägger, H.3
  • 17
    • 48849107198 scopus 로고    scopus 로고
    • Solubilization of membrane protein complexes for blue native PAGE
    • Reisinger V., and Eichacker L.A. Solubilization of membrane protein complexes for blue native PAGE. J Proteomics 71 (2008) 277-283
    • (2008) J Proteomics , vol.71 , pp. 277-283
    • Reisinger, V.1    Eichacker, L.A.2
  • 18
    • 0032409543 scopus 로고    scopus 로고
    • Use of a proteome strategy for tagging proteins present at the plasma membrane
    • Santoni V., Rouquie D., Doumas P., Mansion M., Boutry M., Degand H., et al. Use of a proteome strategy for tagging proteins present at the plasma membrane. Plant J 16 (1998) 633-641
    • (1998) Plant J , vol.16 , pp. 633-641
    • Santoni, V.1    Rouquie, D.2    Doumas, P.3    Mansion, M.4    Boutry, M.5    Degand, H.6
  • 19
    • 0033778077 scopus 로고    scopus 로고
    • Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties
    • Santoni V., Kieffer S., Desclaux D., Masson F., and Rabilloud T. Membrane proteomics: use of additive main effects with multiplicative interaction model to classify plasma membrane proteins according to their solubility and electrophoretic properties. Electrophoresis 21 (2000) 3329-3344
    • (2000) Electrophoresis , vol.21 , pp. 3329-3344
    • Santoni, V.1    Kieffer, S.2    Desclaux, D.3    Masson, F.4    Rabilloud, T.5
  • 21
    • 11144273935 scopus 로고    scopus 로고
    • Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking
    • Alexandersson E., Saalbach G., Karsson C., and Kjellbom P. Arabidopsis plasma membrane proteomics identifies components of transport, signal transduction and membrane trafficking. Plant Cell Physiol 45 (2004) 1543-1556
    • (2004) Plant Cell Physiol , vol.45 , pp. 1543-1556
    • Alexandersson, E.1    Saalbach, G.2    Karsson, C.3    Kjellbom, P.4
  • 22
    • 3142671423 scopus 로고    scopus 로고
    • Proteomics of the rice cell: systematic identification of the protein populations in subcellular compartments
    • Tanaka N., Fujita M., Handa H., Murayama S., Uemura M., Kawamura Y., et al. Proteomics of the rice cell: systematic identification of the protein populations in subcellular compartments. Mol Genet Genomics 271 (2004) 566-576
    • (2004) Mol Genet Genomics , vol.271 , pp. 566-576
    • Tanaka, N.1    Fujita, M.2    Handa, H.3    Murayama, S.4    Uemura, M.5    Kawamura, Y.6
  • 23
    • 36749034740 scopus 로고    scopus 로고
    • A high content in lipid-modified peripheral proteins and integral receptor kinases features in the Arabidopsis plasma membrane proteome
    • Marmagne A., Ferro M., Meinel T., Bruley C., Kuhn L., Garin J., et al. A high content in lipid-modified peripheral proteins and integral receptor kinases features in the Arabidopsis plasma membrane proteome. Mol Cell Proteomics 6 (2007) 1980-1996
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1980-1996
    • Marmagne, A.1    Ferro, M.2    Meinel, T.3    Bruley, C.4    Kuhn, L.5    Garin, J.6
  • 24
    • 52649124306 scopus 로고    scopus 로고
    • A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane
    • Whiteman S.A., Nühse T.S., Ashford D., Sanders D., and Maathuis F.J.M. A proteomic and phosphoproteomic analysis of Oryza sativa plasma membrane and vacuolar membrane. Plant J 56 (2008) 146-156
    • (2008) Plant J , vol.56 , pp. 146-156
    • Whiteman, S.A.1    Nühse, T.S.2    Ashford, D.3    Sanders, D.4    Maathuis, F.J.M.5
  • 25
    • 0034536003 scopus 로고    scopus 로고
    • Identification of low-density Triton X-100 insoluble plasma membrane microdomains in higher plants
    • Peskan T., Westermann M., and Oelmüller R. Identification of low-density Triton X-100 insoluble plasma membrane microdomains in higher plants. Eur J Biochem 267 (2000) 6989-6995
    • (2000) Eur J Biochem , vol.267 , pp. 6989-6995
    • Peskan, T.1    Westermann, M.2    Oelmüller, R.3
  • 26
    • 10944236307 scopus 로고    scopus 로고
    • Receptor kinases with leucine-rich repeats are enriched in Triton X-100 insoluble plasma membrane microdomains from plants
    • Shahollari B., Peskan-Berghöfer T., and Oelmüller R. Receptor kinases with leucine-rich repeats are enriched in Triton X-100 insoluble plasma membrane microdomains from plants. Physiol Plant 122 (2004) 397-403
    • (2004) Physiol Plant , vol.122 , pp. 397-403
    • Shahollari, B.1    Peskan-Berghöfer, T.2    Oelmüller, R.3
  • 27
    • 20844458248 scopus 로고    scopus 로고
    • Analysis of detergent-resistant membranes in Arabidopsis. Evidence for plasma membrane lipid rafts
    • Borner G.H.H., Sherrier D.J., Weimar T., Michaelson L.V., Hawkins N.D., MacAskill A., et al. Analysis of detergent-resistant membranes in Arabidopsis. Evidence for plasma membrane lipid rafts. Plant Physiol 137 (2005) 104-116
    • (2005) Plant Physiol , vol.137 , pp. 104-116
    • Borner, G.H.H.1    Sherrier, D.J.2    Weimar, T.3    Michaelson, L.V.4    Hawkins, N.D.5    MacAskill, A.6
  • 30
    • 34250677613 scopus 로고    scopus 로고
    • Characterization of lipid rafts from Medicago truncatula root plasma membranes: a proteomic study reveals the presence of a raft associated redox system
    • Lefevbre B., Furt F., Hartmann M.A., Michaelson L.V., Carde J.P., Rossignol M., et al. Characterization of lipid rafts from Medicago truncatula root plasma membranes: a proteomic study reveals the presence of a raft associated redox system. Plant Physiol 144 (2007) 402-418
    • (2007) Plant Physiol , vol.144 , pp. 402-418
    • Lefevbre, B.1    Furt, F.2    Hartmann, M.A.3    Michaelson, L.V.4    Carde, J.P.5    Rossignol, M.6
  • 31
    • 51649123620 scopus 로고    scopus 로고
    • Plasma membrane redox systems: lipid rafts and protein assemblies
    • Lüttge U., Beyschlag W., and Murata J. (Eds), Springer, Heidelberg
    • Lüthje S. Plasma membrane redox systems: lipid rafts and protein assemblies. In: Lüttge U., Beyschlag W., and Murata J. (Eds). Progress in botany vol. 69 (2008), Springer, Heidelberg 169-200
    • (2008) Progress in botany , vol.69 , pp. 169-200
    • Lüthje, S.1
  • 32
    • 0033039643 scopus 로고    scopus 로고
    • Mechanisms and regulation of reduction-based iron uptake in plants
    • Schmidt W. Mechanisms and regulation of reduction-based iron uptake in plants. New Phytol 141 (1999) 1-26
    • (1999) New Phytol , vol.141 , pp. 1-26
    • Schmidt, W.1
  • 33
    • 34248157691 scopus 로고    scopus 로고
    • Mining iron: iron uptake and transport in plants
    • Kim S.a., and Guerinot M.L. Mining iron: iron uptake and transport in plants. FESB Lett 581 (2007) 2273-2280
    • (2007) FESB Lett , vol.581 , pp. 2273-2280
    • Kim, S.a.1    Guerinot, M.L.2
  • 34
    • 0034542034 scopus 로고    scopus 로고
    • Redox enzymes in the plant plasma membrane and their possible roles
    • Bérczi A., and Møller I.M. Redox enzymes in the plant plasma membrane and their possible roles. Plant Cell Environ 23 (2000) 1287-1302
    • (2000) Plant Cell Environ , vol.23 , pp. 1287-1302
    • Bérczi, A.1    Møller, I.M.2
  • 35
    • 0028140643 scopus 로고
    • Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane
    • Serrano A., Córdoba F., Gonzáles-Reyes J.A., Navas P., and Villalba J.M. Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane. Plant Physiol 106 (1994) 87-96
    • (1994) Plant Physiol , vol.106 , pp. 87-96
    • Serrano, A.1    Córdoba, F.2    Gonzáles-Reyes, J.A.3    Navas, P.4    Villalba, J.M.5
  • 37
    • 0029169436 scopus 로고
    • NADH-specific dehydrogenase from onion root plasma membrane: purification and characterization
    • Serrano A., Cordoba F., González-Reyes J.A., Santos C., Navas P., and Villalba J.M. NADH-specific dehydrogenase from onion root plasma membrane: purification and characterization. Protoplasma 184 (1995) 133-139
    • (1995) Protoplasma , vol.184 , pp. 133-139
    • Serrano, A.1    Cordoba, F.2    González-Reyes, J.A.3    Santos, C.4    Navas, P.5    Villalba, J.M.6
  • 38
    • 0031397296 scopus 로고    scopus 로고
    • Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of zucchini plasma membrane
    • Trost P., Foscarini S., Preger S., Bonora P., Vitale L., and Pupillo P. Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of zucchini plasma membrane. Plant Physiol 114 (1997) 737-746
    • (1997) Plant Physiol , vol.114 , pp. 737-746
    • Trost, P.1    Foscarini, S.2    Preger, S.3    Bonora, P.4    Vitale, L.5    Pupillo, P.6
  • 39
    • 0001586031 scopus 로고
    • Purification and identification of plasma membrane associated electron transport protein from maize (Zea mays L.) roots
    • Luster D.G., and Buckhout T.J. Purification and identification of plasma membrane associated electron transport protein from maize (Zea mays L.) roots. Plant Physiol 91 (1989) 1014-1019
    • (1989) Plant Physiol , vol.91 , pp. 1014-1019
    • Luster, D.G.1    Buckhout, T.J.2
  • 41
    • 0038715037 scopus 로고    scopus 로고
    • Properties of guaiacol peroxidase activities isolated from corn root plasma membranes
    • Mika A., and Lüthje S. Properties of guaiacol peroxidase activities isolated from corn root plasma membranes. Plant Physiol 132 (2003) 1489-1498
    • (2003) Plant Physiol , vol.132 , pp. 1489-1498
    • Mika, A.1    Lüthje, S.2
  • 42
    • 51649084527 scopus 로고    scopus 로고
    • Membrane-bound class III peroxidases: identification, biochemical properties and sequence analysis of isoenzymes purified from maize (Zea mays L.) roots
    • Mika A., Buck F., and Lüthje S. Membrane-bound class III peroxidases: identification, biochemical properties and sequence analysis of isoenzymes purified from maize (Zea mays L.) roots. J Proteomics 71 (2008) 412-424
    • (2008) J Proteomics , vol.71 , pp. 412-424
    • Mika, A.1    Buck, F.2    Lüthje, S.3
  • 43
    • 0029136836 scopus 로고
    • The stereospecificity, purification and characterization of an NADH-ferricyanide reductase from spinach leaf plasma membrane
    • Møller I.M., Fredlund K.M., and Bérczi A. The stereospecificity, purification and characterization of an NADH-ferricyanide reductase from spinach leaf plasma membrane. Protoplasma 184 (1995) 124-132
    • (1995) Protoplasma , vol.184 , pp. 124-132
    • Møller, I.M.1    Fredlund, K.M.2    Bérczi, A.3
  • 44
    • 0542444213 scopus 로고    scopus 로고
    • NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes
    • Bérczi A., and Møller I.M. NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes. Plant Physiol 116 (1998) 1029-1036
    • (1998) Plant Physiol , vol.116 , pp. 1029-1036
    • Bérczi, A.1    Møller, I.M.2
  • 49
    • 0342844282 scopus 로고    scopus 로고
    • Purification of cytochrome b-561 from bean hypocotyls plasma membrane. Evidence for the presence of two heme centers
    • Trost P., Bérczi A., Sparla F., Sponza G., Marzadori B., Asard H., et al. Purification of cytochrome b-561 from bean hypocotyls plasma membrane. Evidence for the presence of two heme centers. Biochim Biophys Acta 1468 (2000) 1-5
    • (2000) Biochim Biophys Acta , vol.1468 , pp. 1-5
    • Trost, P.1    Bérczi, A.2    Sparla, F.3    Sponza, G.4    Marzadori, B.5    Asard, H.6
  • 50
    • 0038687192 scopus 로고    scopus 로고
    • Partial purification and characterization of an ascorbat-reducible b-type cytochrome from the plasma membrane of Arabidopsis thaliana leaves
    • Bérczi A., Caubergs R.J., and Asard H. Partial purification and characterization of an ascorbat-reducible b-type cytochrome from the plasma membrane of Arabidopsis thaliana leaves. Protoplasma 221 (2003) 47-56
    • (2003) Protoplasma , vol.221 , pp. 47-56
    • Bérczi, A.1    Caubergs, R.J.2    Asard, H.3
  • 51
    • 0033452469 scopus 로고    scopus 로고
    • Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase
    • Sparla F., Tedeschi G., Pupillo P., and Trost P. Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase. FEBS Lett 463 (1999) 382-386
    • (1999) FEBS Lett , vol.463 , pp. 382-386
    • Sparla, F.1    Tedeschi, G.2    Pupillo, P.3    Trost, P.4
  • 53
    • 0032424619 scopus 로고    scopus 로고
    • Initial purification study of the cytochrome b561 of bean hypocotyl plasma membrane
    • Scagliarini S., Rotino L., Bäurle I., Asard H., Pupillo P., and Trost P. Initial purification study of the cytochrome b561 of bean hypocotyl plasma membrane. Protoplasma 205 (1998) 66-73
    • (1998) Protoplasma , vol.205 , pp. 66-73
    • Scagliarini, S.1    Rotino, L.2    Bäurle, I.3    Asard, H.4    Pupillo, P.5    Trost, P.6
  • 54
    • 4243851669 scopus 로고    scopus 로고
    • Plasma membrane-bound nitrate reductase in algae and higher plants
    • Asard H., Bérczi A., and Caubergs R. (Eds), Kluwer Academic Publ, Dordrecht, NL
    • Stöhr C. Plasma membrane-bound nitrate reductase in algae and higher plants. In: Asard H., Bérczi A., and Caubergs R. (Eds). Plasma membrane redox systems and their role in biological stress and disease (1998), Kluwer Academic Publ, Dordrecht, NL 103-119
    • (1998) Plasma membrane redox systems and their role in biological stress and disease , pp. 103-119
    • Stöhr, C.1
  • 55
    • 0035037361 scopus 로고    scopus 로고
    • A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite
    • Stöhr C., Strube F., Marx G., Ulrich W.R., and Rockel P. A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite. Planta 212 (2001) 835-841
    • (2001) Planta , vol.212 , pp. 835-841
    • Stöhr, C.1    Strube, F.2    Marx, G.3    Ulrich, W.R.4    Rockel, P.5
  • 56
    • 0034948369 scopus 로고    scopus 로고
    • Different diurnal cycles of expression of two nitrate reductase transcripts in tobacco roots
    • Wienkoop S., Schlichting R., Ulrich E.R., and Stöhr C. Different diurnal cycles of expression of two nitrate reductase transcripts in tobacco roots. Protoplasma 217 (2001) 15-19
    • (2001) Protoplasma , vol.217 , pp. 15-19
    • Wienkoop, S.1    Schlichting, R.2    Ulrich, E.R.3    Stöhr, C.4
  • 57
    • 48249123929 scopus 로고    scopus 로고
    • Naphthoquinone-dependent generation of superoxide radicals by quinone reductase isolated from the plasma membrane of soybean
    • Schopfer P., Heyno E., Drepper F., and Krieger-Liszkay A. Naphthoquinone-dependent generation of superoxide radicals by quinone reductase isolated from the plasma membrane of soybean. Plant Physiol 147 (2008) 864-878
    • (2008) Plant Physiol , vol.147 , pp. 864-878
    • Schopfer, P.1    Heyno, E.2    Drepper, F.3    Krieger-Liszkay, A.4
  • 58
    • 0036323236 scopus 로고    scopus 로고
    • The plasma membrane oxidase NtrbohD is responsible for AOS production in elicited tobacco cells
    • Simon-Plas F., Elmayan T., and Blein J.P. The plasma membrane oxidase NtrbohD is responsible for AOS production in elicited tobacco cells. Plant J 31 (2002) 137-147
    • (2002) Plant J , vol.31 , pp. 137-147
    • Simon-Plas, F.1    Elmayan, T.2    Blein, J.P.3
  • 59
    • 0037039157 scopus 로고    scopus 로고
    • Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response
    • Torres M.A., Dangl J., and Jones J.D.G. Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response. Proc Natl Acad Sci U S A 99 (2002) 517-522
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 517-522
    • Torres, M.A.1    Dangl, J.2    Jones, J.D.G.3
  • 60
    • 0037039157 scopus 로고    scopus 로고
    • Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response
    • Torres M.A., Dangl J., and Jones J.D.G. Arabidopsis gp91phox homologues AtrbohD and AtrbohF are required for accumulation of reactive oxygen intermediates in the plant defense response. Proc Natl Acad Sci U S A 99 (2002) 517-522
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 517-522
    • Torres, M.A.1    Dangl, J.2    Jones, J.D.G.3
  • 61
    • 0037507299 scopus 로고    scopus 로고
    • NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signalling in Arabidopsis
    • Kwak J.M., Mori I.C., Pei Z.M., Leonhard N., Torres A.M., Dangl J.L., et al. NADPH oxidase AtrbohD and AtrbohF genes function in ROS-dependent ABA signalling in Arabidopsis. EMBO J 22 (2003) 2623-2633
    • (2003) EMBO J , vol.22 , pp. 2623-2633
    • Kwak, J.M.1    Mori, I.C.2    Pei, Z.M.3    Leonhard, N.4    Torres, A.M.5    Dangl, J.L.6
  • 63
    • 0035005480 scopus 로고    scopus 로고
    • Induction of plant gp91 phox homolog by fungal cell wall, arachidonic acid, and salicylic acid in potato
    • Yoshioka H., Sugie K., Park H.J., Maeda H., Tsuda N., Kawakita K., et al. Induction of plant gp91 phox homolog by fungal cell wall, arachidonic acid, and salicylic acid in potato. Mol Plant Microb Interact 14 (2001) 725-736
    • (2001) Mol Plant Microb Interact , vol.14 , pp. 725-736
    • Yoshioka, H.1    Sugie, K.2    Park, H.J.3    Maeda, H.4    Tsuda, N.5    Kawakita, K.6
  • 64
    • 20444458715 scopus 로고    scopus 로고
    • Functions of the respiratory burst oxidase in biotic interactions, abiotic stress and development
    • Torres M.A., and Dangl J.L. Functions of the respiratory burst oxidase in biotic interactions, abiotic stress and development. Curr Opin Plant Biol 8 (2005) 397-403
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 397-403
    • Torres, M.A.1    Dangl, J.L.2
  • 66
    • 3442888061 scopus 로고    scopus 로고
    • Isolation and characterization of Fe(III)-chelate reductase gene LeFRO1 in tomato
    • Li L., Cheng X., and Ling H.Q. Isolation and characterization of Fe(III)-chelate reductase gene LeFRO1 in tomato. Plant Mol Biol 54 (2004) 125-136
    • (2004) Plant Mol Biol , vol.54 , pp. 125-136
    • Li, L.1    Cheng, X.2    Ling, H.Q.3
  • 68
    • 0036000016 scopus 로고    scopus 로고
    • Characterization of FRO1, a pea ferric-chelate reductase involved in root iron acquisition
    • Waters B.M., Blevins D.G., and Eide D.J. Characterization of FRO1, a pea ferric-chelate reductase involved in root iron acquisition. Plant Physiol 19 (2002) 85-94
    • (2002) Plant Physiol , vol.19 , pp. 85-94
    • Waters, B.M.1    Blevins, D.G.2    Eide, D.J.3
  • 69
    • 0029830563 scopus 로고    scopus 로고
    • Molecular components and biochemistry of electron transport in plant plasma membranes
    • Döring O., and Lüthje S. Molecular components and biochemistry of electron transport in plant plasma membranes. Mol Membr Biol 13 (1996) 127-142
    • (1996) Mol Membr Biol , vol.13 , pp. 127-142
    • Döring, O.1    Lüthje, S.2
  • 71
    • 0001507812 scopus 로고
    • On the function of two systems that can transfer electrons across the plasma membrane
    • Bienfait F., and Lüttge U. On the function of two systems that can transfer electrons across the plasma membrane. Plant Physiol Biochem 26 (1988) 665-671
    • (1988) Plant Physiol Biochem , vol.26 , pp. 665-671
    • Bienfait, F.1    Lüttge, U.2
  • 72
  • 73
    • 39149121438 scopus 로고    scopus 로고
    • Regulation of rice NADPH oxidase by binding of Rac GTPase to its N-terminal extension
    • Wong H.L., Pinontoan R., Hayashi K., Tabata R., Yaeno T., Hasegawa K., et al. Regulation of rice NADPH oxidase by binding of Rac GTPase to its N-terminal extension. Plant Cell 19 (2007) 4022-4034
    • (2007) Plant Cell , vol.19 , pp. 4022-4034
    • Wong, H.L.1    Pinontoan, R.2    Hayashi, K.3    Tabata, R.4    Yaeno, T.5    Hasegawa, K.6
  • 74
    • 0001344391 scopus 로고
    • Cytochromes of plant plasma membranes. characterization by absorbance difference spectrophotometry and redox titration
    • Askerlund P., Larsson C., and Widell S. Cytochromes of plant plasma membranes. characterization by absorbance difference spectrophotometry and redox titration. Physiol Plant 76 (1989) 123-134
    • (1989) Physiol Plant , vol.76 , pp. 123-134
    • Askerlund, P.1    Larsson, C.2    Widell, S.3
  • 76
    • 84969769445 scopus 로고
    • b-Type cytochromes in higher plant plasma membranes
    • Asard H., Venken M Caubergs R., and De Greef J.A. b-Type cytochromes in higher plant plasma membranes. Plant Physiol 90 (1989) 1077-1083
    • (1989) Plant Physiol , vol.90 , pp. 1077-1083
    • Asard, H.1    Venken M Caubergs, R.2    De Greef, J.A.3
  • 77
    • 0034954412 scopus 로고    scopus 로고
    • b-Type cytochromes in plasma membranes of Phaseolus vulgaris hypocotyls, Arabidopsis thaliana leaves, and Zea mays roots
    • Bérczi A., Lüthje S., and Asard H. b-Type cytochromes in plasma membranes of Phaseolus vulgaris hypocotyls, Arabidopsis thaliana leaves, and Zea mays roots. Protoplasma 217 (2001) 50-55
    • (2001) Protoplasma , vol.217 , pp. 50-55
    • Bérczi, A.1    Lüthje, S.2    Asard, H.3
  • 78
    • 1342308497 scopus 로고    scopus 로고
    • Localization of an ascorbate-reducible cytochrome b561 in the plant tonoplast
    • Griesen D., Su D., Bérczi A., and Asard H. Localization of an ascorbate-reducible cytochrome b561 in the plant tonoplast. Plant Physiol 134 (2004) 726-734
    • (2004) Plant Physiol , vol.134 , pp. 726-734
    • Griesen, D.1    Su, D.2    Bérczi, A.3    Asard, H.4
  • 79
    • 14944360174 scopus 로고    scopus 로고
    • Identification of an ascorbate-dependent cytochrome b of tonoplast membrane sharing biochemical features with members of the cytochrome b561 family
    • Preger V., Scagliarini S., and Pupillo P. Identification of an ascorbate-dependent cytochrome b of tonoplast membrane sharing biochemical features with members of the cytochrome b561 family. Planta 220 (2005) 365-375
    • (2005) Planta , vol.220 , pp. 365-375
    • Preger, V.1    Scagliarini, S.2    Pupillo, P.3
  • 80
    • 1442291188 scopus 로고    scopus 로고
    • Analysis of an Arabidopsis thaliana protein family, structurally related to cytochrome b561 and potentially involved in catecholamine biochemistry in plants
    • Verelst W., and Asard H. Analysis of an Arabidopsis thaliana protein family, structurally related to cytochrome b561 and potentially involved in catecholamine biochemistry in plants. J Plant Physiol 161 (2004) 175-181
    • (2004) J Plant Physiol , vol.161 , pp. 175-181
    • Verelst, W.1    Asard, H.2
  • 81
    • 33846375045 scopus 로고    scopus 로고
    • Catecholamines are active compounds in plants
    • Kulma A., and Szopa J. Catecholamines are active compounds in plants. Plant Sci 172 (2007) 433-440
    • (2007) Plant Sci , vol.172 , pp. 433-440
    • Kulma, A.1    Szopa, J.2
  • 82
    • 0034948162 scopus 로고    scopus 로고
    • Higher-plant plasma membrane cytochrome b561: a protein in search of a function
    • Asard H., Kapila, Verelst W., and Bérczi A. Higher-plant plasma membrane cytochrome b561: a protein in search of a function. Protoplasma 217 (2001) 77-93
    • (2001) Protoplasma , vol.217 , pp. 77-93
    • Asard, H.1    Kapila2    Verelst, W.3    Bérczi, A.4
  • 83
    • 0038348700 scopus 로고    scopus 로고
    • Structure prediction for the di-heme cytochrome b561 protein family
    • Bashtovyy D., Bérczi A., Asard H., and Páli T. Structure prediction for the di-heme cytochrome b561 protein family. Protoplasma 221 (2003) 31-40
    • (2003) Protoplasma , vol.221 , pp. 31-40
    • Bashtovyy, D.1    Bérczi, A.2    Asard, H.3    Páli, T.4
  • 84
    • 33947422966 scopus 로고    scopus 로고
    • An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability
    • Bérczi A., Su D., and Asard H. An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability. FEBS Lett 581 (2007) 1505-1508
    • (2007) FEBS Lett , vol.581 , pp. 1505-1508
    • Bérczi, A.1    Su, D.2    Asard, H.3
  • 85
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: preparing the next generation of molecular biologists
    • Alberts B. The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92 (1998) 291-294
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 86
    • 4344627295 scopus 로고    scopus 로고
    • Protein complexes of the plant plasma membrane resolved by Blue Native PAGE
    • Kjell J., Rasmusson A.G., Larsson H., and Widell S. Protein complexes of the plant plasma membrane resolved by Blue Native PAGE. Physiol Plant 212 (2004) 546-555
    • (2004) Physiol Plant , vol.212 , pp. 546-555
    • Kjell, J.1    Rasmusson, A.G.2    Larsson, H.3    Widell, S.4
  • 87
    • 34848887433 scopus 로고    scopus 로고
    • Salt-induced changes in the plasma membrane proteome of the halotolerant alga Dunaliella salina as revealed by blue native gel electrophoresis and nano-LC-MS/Ms analysis
    • Katz A., Waridel P., Shevchenko A., and Pick U. Salt-induced changes in the plasma membrane proteome of the halotolerant alga Dunaliella salina as revealed by blue native gel electrophoresis and nano-LC-MS/Ms analysis. Mol Cell Proteomics 7 (2007) 1459-1472
    • (2007) Mol Cell Proteomics , vol.7 , pp. 1459-1472
    • Katz, A.1    Waridel, P.2    Shevchenko, A.3    Pick, U.4
  • 88
    • 34247884339 scopus 로고    scopus 로고
    • A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes
    • Paz Y., Katz A., and Pick U. A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes. J Biol Chem 282 (2007) 8658-8666
    • (2007) J Biol Chem , vol.282 , pp. 8658-8666
    • Paz, Y.1    Katz, A.2    Pick, U.3
  • 91
    • 25844503496 scopus 로고    scopus 로고
    • Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes
    • Singh R., Chénier D., Bériault R., Maillouc R., Hamel R.D., and Appanna V.D. Blue native polyacrylamide gel electrophoresis and the monitoring of malate- and oxaloacetate-producing enzymes. J Biochem Biophys Methods 64 (2005) 189-199
    • (2005) J Biochem Biophys Methods , vol.64 , pp. 189-199
    • Singh, R.1    Chénier, D.2    Bériault, R.3    Maillouc, R.4    Hamel, R.D.5    Appanna, V.D.6
  • 92
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas P.E., Ryan D., and Levin W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Ann Biochem 75 (1976) 168-176
    • (1976) Ann Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 93
    • 0021142747 scopus 로고
    • 2 staining is not specific for heme proteins separated by gel electrophoresis
    • 2 staining is not specific for heme proteins separated by gel electrophoresis. Anal Biochem 140 (1984) 577-580
    • (1984) Anal Biochem , vol.140 , pp. 577-580
    • Miller, D.J.1    Nicholas, D.J.D.2
  • 94
    • 0014200462 scopus 로고
    • Nuclear control of a cytoplasmic enzyme
    • Schweiger G., Master W.P., and Werz G. Nuclear control of a cytoplasmic enzyme. Nature 216 (1967) 554-557
    • (1967) Nature , vol.216 , pp. 554-557
    • Schweiger, G.1    Master, W.P.2    Werz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.