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Volumn 11, Issue 4, 2015, Pages

Beyond Glycolysis: GAPDHs Are Multi-functional Enzymes Involved in Regulation of ROS, Autophagy, and Plant Immune Responses

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; ELECTROLYTE; FLAGELLIN; FLUORESCENT DYE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GREEN FLUORESCENT PROTEIN; ISOPROTEIN; MULTIFUNCTIONAL ENZYME; PROTEIN GAPC1; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; WORTMANNIN; ARABIDOPSIS PROTEIN; GAPC1 PROTEIN, ARABIDOPSIS;

EID: 84930349982     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1005199     Document Type: Article
Times cited : (135)

References (92)
  • 1
    • 78449269327 scopus 로고    scopus 로고
    • Plant and animal sensors of conserved microbial signatures
    • Ronald PC, Beutler B, (2010) Plant and animal sensors of conserved microbial signatures. Science 330: 1061–1064. doi: 10.1126/science.1189468 21097929
    • (2010) Science , vol.330 , pp. 1061-1064
    • Ronald, P.C.1    Beutler, B.2
  • 2
    • 84856170491 scopus 로고    scopus 로고
    • How do plants achieve immunity? Defence without specialized immune cells
    • Spoel SH, Dong X, (2012) How do plants achieve immunity? Defence without specialized immune cells. Nat Rev Immunol 12: 89–100. doi: 10.1038/nri3141 22273771
    • (2012) Nat Rev Immunol , vol.12 , pp. 89-100
    • Spoel, S.H.1    Dong, X.2
  • 3
    • 84881235715 scopus 로고    scopus 로고
    • Recognition of bacterial plant pathogens: local, systemic and transgenerational immunity
    • Henry E, Yadeta KA, Coaker G, (2013) Recognition of bacterial plant pathogens: local, systemic and transgenerational immunity. New Phytol 199: 908–915. doi: 10.1111/nph.12214 23909802
    • (2013) New Phytol , vol.199 , pp. 908-915
    • Henry, E.1    Yadeta, K.A.2    Coaker, G.3
  • 4
    • 68149128399 scopus 로고    scopus 로고
    • Early molecular events in PAMP-triggered immunity
    • Zipfel C, (2009) Early molecular events in PAMP-triggered immunity. Curr Opin Plant Biol 12: 414–420. doi: 10.1016/j.pbi.2009.06.003 19608450
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 414-420
    • Zipfel, C.1
  • 5
    • 79952302258 scopus 로고    scopus 로고
    • Of PAMPs and Effectors: The Blurred PTI-ETI Dichotomy
    • Thomma BPHJ, Nürnberger T, Joosten MHAJ, (2011) Of PAMPs and Effectors: The Blurred PTI-ETI Dichotomy. The Plant Cell 23: 4–15. doi: 10.1105/tpc.110.082602 21278123
    • (2011) The Plant Cell , vol.23 , pp. 4-15
    • Thomma, B.P.H.J.1    Nürnberger, T.2    Joosten, M.H.A.J.3
  • 6
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 Is a Target of the Type III Virulence Effector AvrRpt2 and Modulates RPS2-Mediated Resistance
    • Mackey D, Belkhadir Y, Alonso JM, Ecker JR, Dangl JL, (2003) Arabidopsis RIN4 Is a Target of the Type III Virulence Effector AvrRpt2 and Modulates RPS2-Mediated Resistance. Cell 112: 379–389. 12581527
    • (2003) Cell , vol.112 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
  • 7
    • 34548676152 scopus 로고    scopus 로고
    • Autoimmune Response as a Mechanism for a Dobzhansky-Muller-Type Incompatibility Syndrome in Plants
    • Bomblies K, Lempe J, Epple P, Warthmann N, Lanz C, et al. (2007) Autoimmune Response as a Mechanism for a Dobzhansky-Muller-Type Incompatibility Syndrome in Plants. PLoS Biol 5: e236. 17803357
    • (2007) PLoS Biol , vol.5 , pp. e236
    • Bomblies, K.1    Lempe, J.2    Epple, P.3    Warthmann, N.4    Lanz, C.5
  • 8
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • Takahashi A, Casais C, Ichimura K, Shirasu K, (2003) HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc Natl Acad Sci U S A 100: 11777–11782. 14504384
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 9
    • 0036679001 scopus 로고    scopus 로고
    • Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants
    • Peart JR, Lu R, Sadanandom A, Malcuit I, Moffett P, et al. (2002) Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants. Proc Natl Acad Sci U S A 99: 10865–10869. 12119413
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10865-10869
    • Peart, J.R.1    Lu, R.2    Sadanandom, A.3    Malcuit, I.4    Moffett, P.5
  • 10
    • 40149092139 scopus 로고    scopus 로고
    • Tomato bushy stunt virus Co-Opts the RNA-Binding Function of a Host Metabolic Enzyme for Viral Genomic RNA Synthesis. Cell Host &
    • Wang RY-L, Nagy PD, (2008) Tomato bushy stunt virus Co-Opts the RNA-Binding Function of a Host Metabolic Enzyme for Viral Genomic RNA Synthesis. Cell Host & Microbe 3: 178–187.
    • (2008) Microbe , vol.3 , pp. 178-187
    • Wang, R.Y.-L.1    Nagy, P.D.2
  • 11
    • 84875222858 scopus 로고    scopus 로고
    • Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7
    • Nicaise V, Joe A, Jeong Br, Korneli C, Boutrot F, et al. (2013) Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7. EMBO J. 32: 701–712. doi: 10.1038/emboj.2013.15 23395902
    • (2013) EMBO J , vol.32 , pp. 701-712
    • Nicaise, V.1    Joe, A.2    Jeong, B.3    Korneli, C.4    Boutrot, F.5
  • 12
    • 78649842470 scopus 로고    scopus 로고
    • The diverse functions of GAPDH: views from different subcellular compartments
    • Tristan C, Shahani N, Sedlak TW, Sawa A, (2011) The diverse functions of GAPDH: views from different subcellular compartments. Cell Signal 23: 317–323. doi: 10.1016/j.cellsig.2010.08.003 20727968
    • (2011) Cell Signal , vol.23 , pp. 317-323
    • Tristan, C.1    Shahani, N.2    Sedlak, T.W.3    Sawa, A.4
  • 13
    • 70449712602 scopus 로고    scopus 로고
    • Novel roles for GAPDH in cell death and carcinogenesis
    • Colell A, Green DR, Ricci JE, (2009) Novel roles for GAPDH in cell death and carcinogenesis. Cell Death Differ 16: 1573–1581. doi: 10.1038/cdd.2009.137 19779498
    • (2009) Cell Death Differ , vol.16 , pp. 1573-1581
    • Colell, A.1    Green, D.R.2    Ricci, J.E.3
  • 14
    • 34249279169 scopus 로고    scopus 로고
    • GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation
    • Colell A, Ricci JE, Tait S, Milasta S, Maurer U, et al. (2007) GAPDH and autophagy preserve survival after apoptotic cytochrome c release in the absence of caspase activation. Cell 129: 983–997. 17540177
    • (2007) Cell , vol.129 , pp. 983-997
    • Colell, A.1    Ricci, J.E.2    Tait, S.3    Milasta, S.4    Maurer, U.5
  • 15
    • 84872566186 scopus 로고    scopus 로고
    • NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-kappaB activation. Cell Host &
    • Gao X, Wang X, Pham TH, Feuerbacher LA, Lubos ML, et al. (2013) NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-kappaB activation. Cell Host & Microbe 13: 87–99. doi: 10.1016/j.chom.2012.11.010 23332158
    • (2013) Microbe , vol.13 , pp. 87-99
    • Gao, X.1    Wang, X.2    Pham, T.H.3    Feuerbacher, L.A.4    Lubos, M.L.5
  • 16
    • 84907212907 scopus 로고    scopus 로고
    • Cell biology. Metabolic control of cell death
    • Green DR, Galluzzi L, Kroemer G, (2014) Cell biology. Metabolic control of cell death. Science 345: 1250256. doi: 10.1126/science.1250256 25237106
    • (2014) Science , vol.345 , pp. 1250256
    • Green, D.R.1    Galluzzi, L.2    Kroemer, G.3
  • 17
    • 84909578049 scopus 로고    scopus 로고
    • mTOR- and HIF-1alpha-mediated aerobic glycolysis as metabolic basis for trained immunity
    • Cheng SC, Quintin J, Cramer RA, Shepardson KM, Saeed S, et al. (2014) mTOR- and HIF-1alpha-mediated aerobic glycolysis as metabolic basis for trained immunity. Science 345: 1250684. doi: 10.1126/science.1250684 25258083
    • (2014) Science , vol.345 , pp. 1250684
    • Cheng, S.C.1    Quintin, J.2    Cramer, R.A.3    Shepardson, K.M.4    Saeed, S.5
  • 18
    • 84900868784 scopus 로고    scopus 로고
    • Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties
    • Zaffagnini M, Fermani S, Costa A, Lemaire SD, Trost P, (2013) Plant cytoplasmic GAPDH: redox post-translational modifications and moonlighting properties. Front Plant Sci 4: 450. doi: 10.3389/fpls.2013.00450 24282406
    • (2013) Front Plant Sci , vol.4 , pp. 450
    • Zaffagnini, M.1    Fermani, S.2    Costa, A.3    Lemaire, S.D.4    Trost, P.5
  • 19
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control
    • Sirover MA, (2011) On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim Biophys Acta 1810: 741–751. doi: 10.1016/j.bbagen.2011.05.010 21640161
    • (2011) Biochim Biophys Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 20
    • 84861065569 scopus 로고    scopus 로고
    • Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation
    • Sirover MA, (2012) Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J Cell Biochem 113: 2193–2200. doi: 10.1002/jcb.24113 22388977
    • (2012) J Cell Biochem , vol.113 , pp. 2193-2200
    • Sirover, M.A.1
  • 21
    • 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. 12962302
    • (2003) J Mol Evol , vol.57 , pp. 16-26
    • Petersen, J.1    Brinkmann, H.2    Cerff, R.3
  • 22
    • 57749121325 scopus 로고    scopus 로고
    • Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
    • Rius SP, Casati P, Iglesias AA, Gomez-Casati DF, (2008) Characterization of Arabidopsis lines deficient in GAPC-1, a cytosolic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. Plant Physiol 148: 1655–1667. doi: 10.1104/pp.108.128769 18820081
    • (2008) Plant Physiol , vol.148 , pp. 1655-1667
    • Rius, S.P.1    Casati, P.2    Iglesias, A.A.3    Gomez-Casati, D.F.4
  • 23
    • 0029583088 scopus 로고
    • Reductive modification and nonreductive activation of purified spinach chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
    • Baalmann E, Backhausen JE, Rak C, Vetter S, Scheibe R, (1995) Reductive modification and nonreductive activation of purified spinach chloroplast NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. Arch Biochem Biophys 324: 201–208. 8554310
    • (1995) Arch Biochem Biophys , vol.324 , pp. 201-208
    • Baalmann, E.1    Backhausen, J.E.2    Rak, C.3    Vetter, S.4    Scheibe, R.5
  • 24
    • 0029137802 scopus 로고
    • Specific reduction of chloroplast glyceraldehyde-3-phosphate dehydrogenase activity by antisense RNA reduces CO2 assimilation via a reduction in ribulose bisphosphate regeneration in transgenic tobacco plants
    • Price GD, Evans J, Caemmerer S, Yu J-W, Badger M, (1995) Specific reduction of chloroplast glyceraldehyde-3-phosphate dehydrogenase activity by antisense RNA reduces CO2 assimilation via a reduction in ribulose bisphosphate regeneration in transgenic tobacco plants. Planta 195: 369–378. 7766043
    • (1995) Planta , vol.195 , pp. 369-378
    • Price, G.D.1    Evans, J.2    Caemmerer, S.3    Yu, J.-W.4    Badger, M.5
  • 26
    • 39149095741 scopus 로고    scopus 로고
    • Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response
    • Romero-Puertas MC, Campostrini N, Matte A, Righetti PG, Perazzolli M, et al. (2008) Proteomic analysis of S-nitrosylated proteins in Arabidopsis thaliana undergoing hypersensitive response. Proteomics 8: 1459–1469. doi: 10.1002/pmic.200700536 18297659
    • (2008) Proteomics , vol.8 , pp. 1459-1469
    • Romero-Puertas, M.C.1    Campostrini, N.2    Matte, A.3    Righetti, P.G.4    Perazzolli, M.5
  • 27
    • 33845611917 scopus 로고    scopus 로고
    • The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation
    • Zaffagnini M, Michelet L, Marchand C, Sparla F, Decottignies P, et al. (2007) The thioredoxin-independent isoform of chloroplastic glyceraldehyde-3-phosphate dehydrogenase is selectively regulated by glutathionylation. FEBS J 274: 212–226. 17140414
    • (2007) FEBS J , vol.274 , pp. 212-226
    • Zaffagnini, M.1    Michelet, L.2    Marchand, C.3    Sparla, F.4    Decottignies, P.5
  • 28
    • 43149119739 scopus 로고    scopus 로고
    • Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications
    • Holtgrefe S, Gohlke J, Starmann J, Druce S, Klocke S, et al. (2008) Regulation of plant cytosolic glyceraldehyde 3-phosphate dehydrogenase isoforms by thiol modifications. Physiol Plant 133: 211–228. doi: 10.1111/j.1399-3054.2008.01066.x 18298409
    • (2008) Physiol Plant , vol.133 , pp. 211-228
    • Holtgrefe, S.1    Gohlke, J.2    Starmann, J.3    Druce, S.4    Klocke, S.5
  • 29
    • 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, et al. (2005) Proteomic identification of glyceraldehyde 3-phosphate dehydrogenase as an inhibitory target of hydrogen peroxide in Arabidopsis. Plant Physiol Biochem 43: 828–835. 16289945
    • (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
  • 30
    • 84863112816 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase Ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress
    • Guo L, Devaiah SP, Narasimhan R, Pan X, Zhang Y, et al. (2012) Cytosolic glyceraldehyde-3-phosphate dehydrogenases interact with phospholipase Ddelta to transduce hydrogen peroxide signals in the Arabidopsis response to stress. Plant Cell 24: 2200–2212. doi: 10.1105/tpc.111.094946 22589465
    • (2012) Plant Cell , vol.24 , pp. 2200-2212
    • Guo, L.1    Devaiah, S.P.2    Narasimhan, R.3    Pan, X.4    Zhang, Y.5
  • 31
    • 37549039041 scopus 로고    scopus 로고
    • Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase
    • Baek D, Jin Y, Jeong JC, Lee HJ, Moon H, et al. (2008) Suppression of reactive oxygen species by glyceraldehyde-3-phosphate dehydrogenase. Phytochemistry 69: 333–338. 17854848
    • (2008) Phytochemistry , vol.69 , pp. 333-338
    • Baek, D.1    Jin, Y.2    Jeong, J.C.3    Lee, H.J.4    Moon, H.5
  • 32
    • 84877044940 scopus 로고    scopus 로고
    • Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots
    • Vescovi M, Zaffagnini M, Festa M, Trost P, Lo Schiavo F, et al. (2013) Nuclear accumulation of cytosolic glyceraldehyde-3-phosphate dehydrogenase in cadmium-stressed Arabidopsis roots. Plant Physiol 162: 333–346. doi: 10.1104/pp.113.215194 23569110
    • (2013) Plant Physiol , vol.162 , pp. 333-346
    • Vescovi, M.1    Zaffagnini, M.2    Festa, M.3    Trost, P.4    Lo Schiavo, F.5
  • 33
    • 0000152747 scopus 로고    scopus 로고
    • Pseudomonas syringae pv. tomato: the right pathogen, of the right plant, at the right time
    • Preston GM, (2000) Pseudomonas syringae pv. tomato: the right pathogen, of the right plant, at the right time. Mol Plant Pathol 1: 263–275. doi: 10.1046/j.1364-3703.2000.00036.x 20572973
    • (2000) Mol Plant Pathol , vol.1 , pp. 263-275
    • Preston, G.M.1
  • 34
    • 70349643229 scopus 로고    scopus 로고
    • Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis
    • Munoz-Bertomeu J, Cascales-Minana B, Mulet JM, Baroja-Fernandez E, Pozueta-Romero J, et al. (2009) Plastidial glyceraldehyde-3-phosphate dehydrogenase deficiency leads to altered root development and affects the sugar and amino acid balance in Arabidopsis. Plant Physiol 151: 541–558. doi: 10.1104/pp.109.143701 19675149
    • (2009) Plant Physiol , vol.151 , pp. 541-558
    • Munoz-Bertomeu, J.1    Cascales-Minana, B.2    Mulet, J.M.3    Baroja-Fernandez, E.4    Pozueta-Romero, J.5
  • 35
    • 32944479048 scopus 로고    scopus 로고
    • Host-microbe interactions: shaping the evolution of the plant immune response
    • Chisholm ST, Coaker G, Day B, Staskawicz BJ, (2006) Host-microbe interactions: shaping the evolution of the plant immune response. Cell 124: 803–814. 16497589
    • (2006) Cell , vol.124 , pp. 803-814
    • Chisholm, S.T.1    Coaker, G.2    Day, B.3    Staskawicz, B.J.4
  • 36
    • 4744349055 scopus 로고    scopus 로고
    • Systemic acquired resistance
    • Durrant WE, Dong X, (2004) Systemic acquired resistance. Annu Rev Phytopathol 42: 185–209. 15283665
    • (2004) Annu Rev Phytopathol , vol.42 , pp. 185-209
    • Durrant, W.E.1    Dong, X.2
  • 37
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S, (2013) MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30: 2725–2729. doi: 10.1093/molbev/mst197 24132122
    • (2013) Mol Biol Evol , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 38
    • 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. 16927206
    • (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
  • 39
    • 77952191124 scopus 로고    scopus 로고
    • Salicylic acid antagonism of EDS1-driven cell death is important for immune and oxidative stress responses in Arabidopsis
    • Straus MR, Rietz S, Ver Loren van Themaat E, Bartsch M, Parker JE, (2010) Salicylic acid antagonism of EDS1-driven cell death is important for immune and oxidative stress responses in Arabidopsis. Plant J 62: 628–640. doi: 10.1111/j.1365-313X.2010.04178.x 20163553
    • (2010) Plant J , vol.62 , pp. 628-640
    • Straus, M.R.1    Rietz, S.2    Ver Loren van Themaat, E.3    Bartsch, M.4    Parker, J.E.5
  • 40
    • 84877095345 scopus 로고    scopus 로고
    • ROS-talk—how the apoplast, the chloroplast, and the nucleus get the message through
    • Shapiguzov A, Vainonen JP, Wrzaczek M, Kangasjarvi J, (2012) ROS-talk—how the apoplast, the chloroplast, and the nucleus get the message through. Front Plant Sci 3: 292. doi: 10.3389/fpls.2012.00292 23293644
    • (2012) Front Plant Sci , vol.3 , pp. 292
    • Shapiguzov, A.1    Vainonen, J.P.2    Wrzaczek, M.3    Kangasjarvi, J.4
  • 41
    • 0034321934 scopus 로고    scopus 로고
    • H2O2-induced block of glycolysis as an active ADP-ribosylation reaction protecting cells from apoptosis
    • Colussi C, Albertini MC, Coppola S, Rovidati S, Galli F, et al. (2000) H2O2-induced block of glycolysis as an active ADP-ribosylation reaction protecting cells from apoptosis. FASEB J 14: 2266–2276. 11053248
    • (2000) FASEB J , vol.14 , pp. 2266-2276
    • Colussi, C.1    Albertini, M.C.2    Coppola, S.3    Rovidati, S.4    Galli, F.5
  • 42
    • 0033634664 scopus 로고    scopus 로고
    • FLS2: An LRR Receptor—like Kinase Involved in the Perception of the Bacterial Elicitor Flagellin in Arabidopsis
    • Gómez-Gómez L, Boller T, (2000) FLS2: An LRR Receptor—like Kinase Involved in the Perception of the Bacterial Elicitor Flagellin in Arabidopsis. Molecular Cell 5: 1003–1011. 10911994
    • (2000) Molecular Cell , vol.5 , pp. 1003-1011
    • Gómez-Gómez, L.1    Boller, T.2
  • 43
    • 84985932198 scopus 로고
    • Antibodies—a Laboratory Manual—Harlow,E, Lane,D
    • Steiner L, (1989) Antibodies—a Laboratory Manual—Harlow,E, Lane,D. Nature 341: 32–32.
    • (1989) Nature , vol.341 , pp. 32
    • Steiner, L.1
  • 44
    • 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 MA, Dangl JL, Jones JD, (2002) 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: 517–522. 11756663
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 517-522
    • Torres, M.A.1    Dangl, J.L.2    Jones, J.D.3
  • 45
    • 33644860464 scopus 로고    scopus 로고
    • Light-dependent hypersensitive response and resistance signaling against Turnip Crinkle Virus in Arabidopsis
    • Chandra-Shekara AC, Gupte M, Navarre D, Raina S, Raina R, et al. (2006) Light-dependent hypersensitive response and resistance signaling against Turnip Crinkle Virus in Arabidopsis. Plant J 45: 320–334. 16412080
    • (2006) Plant J , vol.45 , pp. 320-334
    • Chandra-Shekara, A.C.1    Gupte, M.2    Navarre, D.3    Raina, S.4    Raina, R.5
  • 46
    • 25844468618 scopus 로고    scopus 로고
    • Redox Homeostasis and Antioxidant Signaling: A Metabolic Interface between Stress Perception and Physiological Responses
    • Foyer CH, Noctor G, (2005) Redox Homeostasis and Antioxidant Signaling: A Metabolic Interface between Stress Perception and Physiological Responses. The Plant Cell Online 17: 1866–1875.
    • (2005) The Plant Cell Online , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 47
    • 46449101370 scopus 로고    scopus 로고
    • Role of glyceraldehyde-3-phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum
    • Bryksin AV, Laktionov PP, (2008) Role of glyceraldehyde-3-phosphate dehydrogenase in vesicular transport from golgi apparatus to endoplasmic reticulum. Biochemistry (Mosc) 73: 619–625. 18620527
    • (2008) Biochemistry (Mosc) , vol.73 , pp. 619-625
    • Bryksin, A.V.1    Laktionov, P.P.2
  • 48
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms
    • Glaser PE, Gross RW, (1995) Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry 34: 12193–12203. 7547960
    • (1995) Biochemistry , vol.34 , pp. 12193-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 49
    • 0035951872 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway
    • Tisdale EJ, (2001) Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. J Biol Chem 276: 2480–2486. 11035021
    • (2001) J Biol Chem , vol.276 , pp. 2480-2486
    • Tisdale, E.J.1
  • 50
    • 84870663317 scopus 로고    scopus 로고
    • Spatio-temporal cellular dynamics of the Arabidopsis flagellin receptor reveal activation status-dependent endosomal sorting
    • Beck M, Zhou J, Faulkner C, MacLean D, Robatzek S, (2012) Spatio-temporal cellular dynamics of the Arabidopsis flagellin receptor reveal activation status-dependent endosomal sorting. Plant Cell 24: 4205–4219. doi: 10.1105/tpc.112.100263 23085733
    • (2012) Plant Cell , vol.24 , pp. 4205-4219
    • Beck, M.1    Zhou, J.2    Faulkner, C.3    MacLean, D.4    Robatzek, S.5
  • 51
    • 0036007915 scopus 로고    scopus 로고
    • Uptake of a fluorescent marker in plant cells is sensitive to brefeldin A and wortmannin
    • Emans N, Zimmermann S, Fischer R, (2002) Uptake of a fluorescent marker in plant cells is sensitive to brefeldin A and wortmannin. Plant Cell 14: 71–86. 11826300
    • (2002) Plant Cell , vol.14 , pp. 71-86
    • Emans, N.1    Zimmermann, S.2    Fischer, R.3
  • 52
    • 0036851186 scopus 로고    scopus 로고
    • Brefeldin A: Deciphering an Enigmatic Inhibitor of Secretion
    • Nebenführ A, Ritzenthaler C, Robinson DG, (2002) Brefeldin A: Deciphering an Enigmatic Inhibitor of Secretion. Plant Physiology 130: 1102–1108. 12427977
    • (2002) Plant Physiology , vol.130 , pp. 1102-1108
    • Nebenführ, A.1    Ritzenthaler, C.2    Robinson, D.G.3
  • 53
    • 1642372806 scopus 로고    scopus 로고
    • FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells
    • Bolte S, Talbot C, Boutte Y, Catrice O, Read ND, et al. (2004) FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells. J Microsc 214: 159–173. 15102063
    • (2004) J Microsc , vol.214 , pp. 159-173
    • Bolte, S.1    Talbot, C.2    Boutte, Y.3    Catrice, O.4    Read, N.D.5
  • 54
    • 20444414481 scopus 로고    scopus 로고
    • CtBP3/BARS drives membrane fission in dynamin-independent transport pathways
    • Bonazzi M, Spano S, Turacchio G, Cericola C, Valente C, et al. (2005) CtBP3/BARS drives membrane fission in dynamin-independent transport pathways. Nat Cell Biol 7: 570–580. 15880102
    • (2005) Nat Cell Biol , vol.7 , pp. 570-580
    • Bonazzi, M.1    Spano, S.2    Turacchio, G.3    Cericola, C.4    Valente, C.5
  • 56
    • 84892770734 scopus 로고    scopus 로고
    • ESCRT-I mediates FLS2 endosomal sorting and plant immunity
    • Spallek T, Beck M, Ben Khaled S, Salomon S, Bourdais G, et al. (2013) ESCRT-I mediates FLS2 endosomal sorting and plant immunity. PLoS Genet 9: e1004035. doi: 10.1371/journal.pgen.1004035 24385929
    • (2013) PLoS Genet , vol.9 , pp. e1004035
    • Spallek, T.1    Beck, M.2    Ben Khaled, S.3    Salomon, S.4    Bourdais, G.5
  • 57
    • 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. 15004741
    • (2004) Protoplasma , vol.223 , pp. 33-43
    • Anderson, L.E.1    Ringenberg, M.R.2    Carol, A.A.3
  • 58
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, et al. (2005) S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 7: 665–674. 15951807
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5
  • 59
    • 84865596150 scopus 로고    scopus 로고
    • Autophagy: a multifaceted intracellular system for bulk and selective recycling
    • Li F, Vierstra RD, (2012) Autophagy: a multifaceted intracellular system for bulk and selective recycling. Trends Plant Sci 17: 526–537. doi: 10.1016/j.tplants.2012.05.006 22694835
    • (2012) Trends Plant Sci , vol.17 , pp. 526-537
    • Li, F.1    Vierstra, R.D.2
  • 60
    • 84892563554 scopus 로고    scopus 로고
    • Differential processing of Arabidopsis ubiquitin-like Atg8 autophagy proteins by Atg4 cysteine proteases
    • Woo J, Park E, Dinesh-Kumar SP, (2014) Differential processing of Arabidopsis ubiquitin-like Atg8 autophagy proteins by Atg4 cysteine proteases. Proc Natl Acad Sci U S A 111: 863–868. doi: 10.1073/pnas.1318207111 24379391
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 863-868
    • Woo, J.1    Park, E.2    Dinesh-Kumar, S.P.3
  • 61
    • 84879047011 scopus 로고    scopus 로고
    • Cellular metabolic and autophagic pathways: traffic control by redox signaling
    • Dodson M, Darley-Usmar V, Zhang J, (2013) Cellular metabolic and autophagic pathways: traffic control by redox signaling. Free Radic Biol Med 63: 207–221. doi: 10.1016/j.freeradbiomed.2013.05.014 23702245
    • (2013) Free Radic Biol Med , vol.63 , pp. 207-221
    • Dodson, M.1    Darley-Usmar, V.2    Zhang, J.3
  • 62
    • 19444370899 scopus 로고    scopus 로고
    • Visualization of autophagy in Arabidopsis using the fluorescent dye monodansylcadaverine and a GFP-AtATG8e fusion protein
    • Contento AL, Xiong Y, Bassham DC, (2005) Visualization of autophagy in Arabidopsis using the fluorescent dye monodansylcadaverine and a GFP-AtATG8e fusion protein. The Plant Journal 42: 598–608. 15860017
    • (2005) The Plant Journal , vol.42 , pp. 598-608
    • Contento, A.L.1    Xiong, Y.2    Bassham, D.C.3
  • 63
    • 80054025654 scopus 로고    scopus 로고
    • The role of Atg proteins in autophagosome formation
    • Mizushima N, Yoshimori T, Ohsumi Y, (2011) The role of Atg proteins in autophagosome formation. Annu Rev Cell Dev Biol 27: 107–132. doi: 10.1146/annurev-cellbio-092910-154005 21801009
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 107-132
    • Mizushima, N.1    Yoshimori, T.2    Ohsumi, Y.3
  • 64
    • 84863115218 scopus 로고    scopus 로고
    • IRE1/bZIP60-mediated unfolded protein response plays distinct roles in plant immunity and abiotic stress responses
    • Moreno AA, Mukhtar MS, Blanco F, Boatwright JL, Moreno I, et al. (2012) IRE1/bZIP60-mediated unfolded protein response plays distinct roles in plant immunity and abiotic stress responses. PLoS One 7: e31944. doi: 10.1371/journal.pone.0031944 22359644
    • (2012) PLoS One , vol.7 , pp. e31944
    • Moreno, A.A.1    Mukhtar, M.S.2    Blanco, F.3    Boatwright, J.L.4    Moreno, I.5
  • 65
    • 79955556641 scopus 로고    scopus 로고
    • Heat induces the splicing by IRE1 of a mRNA encoding a transcription factor involved in the unfolded protein response in Arabidopsis
    • Deng Y, Humbert S, Liu JX, Srivastava R, Rothstein SJ, et al. (2011) Heat induces the splicing by IRE1 of a mRNA encoding a transcription factor involved in the unfolded protein response in Arabidopsis. Proc Natl Acad Sci U S A 108: 7247–7252. doi: 10.1073/pnas.1102117108 21482766
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7247-7252
    • Deng, Y.1    Humbert, S.2    Liu, J.X.3    Srivastava, R.4    Rothstein, S.J.5
  • 66
    • 34548845570 scopus 로고    scopus 로고
    • The Active Site Cysteine of the Proapoptotic Protein Glyceraldehyde-3-phosphate Dehydrogenase Is Essential in Oxidative Stress-induced Aggregation and Cell Death
    • Nakajima H, Amano W, Fujita A, Fukuhara A, Azuma Y-T, et al. (2007) The Active Site Cysteine of the Proapoptotic Protein Glyceraldehyde-3-phosphate Dehydrogenase Is Essential in Oxidative Stress-induced Aggregation and Cell Death. Journal of Biological Chemistry 282: 26562–26574. 17613523
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 26562-26574
    • Nakajima, H.1    Amano, W.2    Fujita, A.3    Fukuhara, A.4    Azuma, Y.-T.5
  • 67
    • 71749093538 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate Dehydrogenase Aggregate Formation Participates in Oxidative Stress-induced Cell Death
    • Nakajima H, Amano W, Kubo T, Fukuhara A, Ihara H, et al. (2009) Glyceraldehyde-3-phosphate Dehydrogenase Aggregate Formation Participates in Oxidative Stress-induced Cell Death. Journal of Biological Chemistry 284: 34331–34341. doi: 10.1074/jbc.M109.027698 19837666
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 34331-34341
    • Nakajima, H.1    Amano, W.2    Kubo, T.3    Fukuhara, A.4    Ihara, H.5
  • 68
    • 0027756183 scopus 로고
    • Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid
    • Chen Z, Silva H, Klessig DF, (1993) Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid. Science 262: 1883–1886. 8266079
    • (1993) Science , vol.262 , pp. 1883-1886
    • Chen, Z.1    Silva, H.2    Klessig, D.F.3
  • 69
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval R, Shvets E, Fass E, Shorer H, Gil L, et al. (2007) Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J 26: 1749–1760. 17347651
    • (2007) EMBO J , vol.26 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5
  • 70
    • 33846378524 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis
    • Xiong Y, Contento AL, Nguyen PQ, Bassham DC, (2007) Degradation of oxidized proteins by autophagy during oxidative stress in Arabidopsis. Plant Physiol 143: 291–299. 17098847
    • (2007) Plant Physiol , vol.143 , pp. 291-299
    • Xiong, Y.1    Contento, A.L.2    Nguyen, P.Q.3    Bassham, D.C.4
  • 71
    • 32644481938 scopus 로고    scopus 로고
    • Genome-wide identification and testing of superior reference genes for transcript normalization in Arabidopsis
    • Czechowski T, Stitt M, Altmann T, Udvardi MK, Scheible WR, (2005) Genome-wide identification and testing of superior reference genes for transcript normalization in Arabidopsis. Plant Physiol 139: 5–17. 16166256
    • (2005) Plant Physiol , vol.139 , pp. 5-17
    • Czechowski, T.1    Stitt, M.2    Altmann, T.3    Udvardi, M.K.4    Scheible, W.R.5
  • 72
    • 77954735369 scopus 로고    scopus 로고
    • Toll-like receptor-induced changes in glycolytic metabolism regulate dendritic cell activation
    • Krawczyk CM, Holowka T, Sun J, Blagih J, Amiel E, et al. (2010) Toll-like receptor-induced changes in glycolytic metabolism regulate dendritic cell activation. Blood 115: 4742–4749. doi: 10.1182/blood-2009-10-249540 20351312
    • (2010) Blood , vol.115 , pp. 4742-4749
    • Krawczyk, C.M.1    Holowka, T.2    Sun, J.3    Blagih, J.4    Amiel, E.5
  • 74
    • 84922937343 scopus 로고    scopus 로고
    • The growth-defense pivot: crisis management in plants mediated by LRR-RK surface receptors
    • Belkhadir Y, Yang L, Hetzel J, Dangl JL, Chory J, (2014) The growth-defense pivot: crisis management in plants mediated by LRR-RK surface receptors. Trends Biochem Sci 39: 447–456. doi: 10.1016/j.tibs.2014.06.006 25089011
    • (2014) Trends Biochem Sci , vol.39 , pp. 447-456
    • Belkhadir, Y.1    Yang, L.2    Hetzel, J.3    Dangl, J.L.4    Chory, J.5
  • 75
    • 84873323723 scopus 로고    scopus 로고
    • Vesicular glycolysis provides on-board energy for fast axonal transport
    • Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, et al. (2013) Vesicular glycolysis provides on-board energy for fast axonal transport. Cell 152: 479–491. doi: 10.1016/j.cell.2012.12.029 23374344
    • (2013) Cell , vol.152 , pp. 479-491
    • Zala, D.1    Hinckelmann, M.V.2    Yu, H.3    Lyra da Cunha, M.M.4    Liot, G.5
  • 76
    • 0037160071 scopus 로고    scopus 로고
    • The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide
    • Sparla F, Pupillo P, Trost P, (2002) The C-terminal extension of glyceraldehyde-3-phosphate dehydrogenase subunit B acts as an autoinhibitory domain regulated by thioredoxins and nicotinamide adenine dinucleotide. J Biol Chem 277: 44946–44952. 12270927
    • (2002) J Biol Chem , vol.277 , pp. 44946-44952
    • Sparla, F.1    Pupillo, P.2    Trost, P.3
  • 77
    • 20344377809 scopus 로고    scopus 로고
    • Proteomic identification of S-nitrosylated proteins in Arabidopsis
    • Lindermayr C, Saalbach G, Durner J, (2005) Proteomic identification of S-nitrosylated proteins in Arabidopsis. Plant Physiol 137: 921–930. 15734904
    • (2005) Plant Physiol , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 78
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu Y, Schiff M, Czymmek K, Talloczy Z, Levine B, et al. (2005) Autophagy regulates programmed cell death during the plant innate immune response. Cell 121: 567–577. 15907470
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Talloczy, Z.4    Levine, B.5
  • 79
    • 65549157489 scopus 로고    scopus 로고
    • Autophagic components contribute to hypersensitive cell death in Arabidopsis
    • Hofius D, Schultz-Larsen T, Joensen J, Tsitsigiannis DI, Petersen NH, et al. (2009) Autophagic components contribute to hypersensitive cell death in Arabidopsis. Cell 137: 773–783. doi: 10.1016/j.cell.2009.02.036 19450522
    • (2009) Cell , vol.137 , pp. 773-783
    • Hofius, D.1    Schultz-Larsen, T.2    Joensen, J.3    Tsitsigiannis, D.I.4    Petersen, N.H.5
  • 80
    • 0344668825 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis nuclear proteome and its response to cold stress
    • Bae MS, Cho EJ, Choi EY, Park OK, (2003) Analysis of the Arabidopsis nuclear proteome and its response to cold stress. Plant J 36: 652–663. 14617066
    • (2003) Plant J , vol.36 , pp. 652-663
    • Bae, M.S.1    Cho, E.J.2    Choi, E.Y.3    Park, O.K.4
  • 81
    • 84876581475 scopus 로고    scopus 로고
    • Transfer of a Redox-Signal through the Cytosol by Redox-Dependent Microcompartmentation of Glycolytic Enzymes at Mitochondria and Actin Cytoskeleton
    • Wojtera-Kwiczor J, Gross F, Leffers HM, Kang M, Schneider M, et al. (2012) Transfer of a Redox-Signal through the Cytosol by Redox-Dependent Microcompartmentation of Glycolytic Enzymes at Mitochondria and Actin Cytoskeleton. Front Plant Sci 3: 284. doi: 10.3389/fpls.2012.00284 23316205
    • (2012) Front Plant Sci , vol.3 , pp. 284
    • Wojtera-Kwiczor, J.1    Gross, F.2    Leffers, H.M.3    Kang, M.4    Schneider, M.5
  • 82
    • 0026070055 scopus 로고
    • A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase
    • Meyer-Siegler K, Mauro DJ, Seal G, Wurzer J, deRiel JK, et al. (1991) A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci U S A 88: 8460–8464. 1924305
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8460-8464
    • Meyer-Siegler, K.1    Mauro, D.J.2    Seal, G.3    Wurzer, J.4    deRiel, J.K.5
  • 83
    • 0033566144 scopus 로고    scopus 로고
    • Pea chloroplast glyceraldehyde-3-phosphate dehydrogenase has uracil glycosylase activity
    • Wang X, Sirover MA, Anderson LE, (1999) Pea chloroplast glyceraldehyde-3-phosphate dehydrogenase has uracil glycosylase activity. Arch Biochem Biophys 367: 348–353. 10395754
    • (1999) Arch Biochem Biophys , vol.367 , pp. 348-353
    • Wang, X.1    Sirover, M.A.2    Anderson, L.E.3
  • 84
    • 84876916661 scopus 로고    scopus 로고
    • Phosphatidic acid binds to cytosolic glyceraldehyde-3-phosphate dehydrogenase and promotes its cleavage in Arabidopsis
    • Kim SC, Guo L, Wang X, (2013) Phosphatidic acid binds to cytosolic glyceraldehyde-3-phosphate dehydrogenase and promotes its cleavage in Arabidopsis. J Biol Chem 288: 11834–11844. doi: 10.1074/jbc.M112.427229 23504314
    • (2013) J Biol Chem , vol.288 , pp. 11834-11844
    • Kim, S.C.1    Guo, L.2    Wang, X.3
  • 85
    • 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. 10069079
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 86
    • 34547677722 scopus 로고    scopus 로고
    • Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation
    • Nakagawa T, Kurose T, Hino T, Tanaka K, Kawamukai M, et al. (2007) Development of series of gateway binary vectors, pGWBs, for realizing efficient construction of fusion genes for plant transformation. J Biosci Bioeng 104: 34–41. 17697981
    • (2007) J Biosci Bioeng , vol.104 , pp. 34-41
    • Nakagawa, T.1    Kurose, T.2    Hino, T.3    Tanaka, K.4    Kawamukai, M.5
  • 87
    • 0033018269 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: demonstration of secretion and processing during bacterial pathogenesis
    • Mudgett MB, Staskawicz BJ, (1999) Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: demonstration of secretion and processing during bacterial pathogenesis. Mol Microbiol 32: 927–941. 10361296
    • (1999) Mol Microbiol , vol.32 , pp. 927-941
    • Mudgett, M.B.1    Staskawicz, B.J.2
  • 88
    • 20444369525 scopus 로고    scopus 로고
    • Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal defense in Arabidopsis
    • Kim MG, da Cunha L, McFall AJ, Belkhadir Y, DebRoy S, et al. (2005) Two Pseudomonas syringae type III effectors inhibit RIN4-regulated basal defense in Arabidopsis. Cell 121: 749–759. 15935761
    • (2005) Cell , vol.121 , pp. 749-759
    • Kim, M.G.1    da Cunha, L.2    McFall, A.J.3    Belkhadir, Y.4    DebRoy, S.5
  • 91
    • 68049143164 scopus 로고    scopus 로고
    • The FAST technique: a simplified Agrobacterium-based transformation method for transient gene expression analysis in seedlings of Arabidopsis and other plant species
    • Li JF, Park E, von Arnim AG, Nebenfuhr A, (2009) The FAST technique: a simplified Agrobacterium-based transformation method for transient gene expression analysis in seedlings of Arabidopsis and other plant species. Plant Methods 5: 6. doi: 10.1186/1746-4811-5-6 19457242
    • (2009) Plant Methods , vol.5 , pp. 6
    • Li, J.F.1    Park, E.2    von Arnim, A.G.3    Nebenfuhr, A.4
  • 92
    • 34548829882 scopus 로고    scopus 로고
    • Isolation of Arabidopsis nuclei and measurement of gene transcription rates using nuclear run-on assays
    • Folta KM, Kaufman LS, (2006) Isolation of Arabidopsis nuclei and measurement of gene transcription rates using nuclear run-on assays. Nat Protoc 1: 3094–3100. 17406505
    • (2006) Nat Protoc , vol.1 , pp. 3094-3100
    • Folta, K.M.1    Kaufman, L.S.2


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