메뉴 건너뛰기




Volumn 1820, Issue 6, 2012, Pages 770-776

Synthesis of and signalling by small, redox active molecules in the plant immune response

Author keywords

Nitric oxide; Plant defence; Reactive nitrogen intermediates; Reactive oxygen intermediates; Redox signalling; S nitrosylation

Indexed keywords

CARBONATE DEHYDRATASE; CYSTEINE; NITRATE REDUCTASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PEROXIREDOXIN 2; PEROXIREDOXIN IIE; PROTEIN NPR1; PROTEIN SABP3; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; S NITROSOGLUTATHIONE; THIOREDOXIN REDUCTASE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84860495899     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.06.015     Document Type: Review
Times cited : (30)

References (82)
  • 1
    • 20444493980 scopus 로고    scopus 로고
    • Plants and animals: A different taste for microbes?
    • DOI 10.1016/j.pbi.2005.05.004, PII S1369526605000658, Biotic Interactions
    • C. Zipfel, and G. Felix Plants and animals: a different taste for microbes? Curr. Opin. Plant Biol. 8 2005 353 360 (Pubitemid 40817376)
    • (2005) Current Opinion in Plant Biology , vol.8 , Issue.4 , pp. 353-360
    • Zipfel, C.1    Felix, G.2
  • 2
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • DOI 10.1038/35081161
    • J.L. Dangl, and J.D.G. Jones Plant pathogens and integrated defence responses to infection Nature 411 2001 826 833 (Pubitemid 32588110)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.G.2
  • 3
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • DOI 10.1016/j.jmb.2004.08.023, PII S0022283604010010
    • D.D. Leipe, E.V. Koonin, and L. Aravind STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer J. Mol. Biol. 343 2004 1 28 (Pubitemid 39294573)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.1 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 5
    • 27644498442 scopus 로고    scopus 로고
    • A direct role for dual oxidase in Drosophila gut immunity
    • DOI 10.1126/science.1117311
    • E.M. Ha, C.T. Oh, Y.S. Bae, and W.J. Lee A direct role for dual oxidase in Drosophila gut immunity Science 310 2005 847 850 (Pubitemid 41567342)
    • (2005) Science , vol.310 , Issue.5749 , pp. 847-850
    • Ha, E.-M.1    Oh, C.-T.2    Bae, Y.S.3    Lee, W.-J.4
  • 6
    • 0032490943 scopus 로고    scopus 로고
    • Nitric oxide functions as a signal in plant disease resistance
    • DOI 10.1038/29087
    • M. Delledonne, Y. Xia, R.A. Dixon, and C. Lamb Nitric oxide functions as a signal in plant disease resistance Nature 394 1998 585 588 (Pubitemid 28366834)
    • (1998) Nature , vol.394 , Issue.6693 , pp. 585-588
    • Delledonne, M.1    Xia, Y.2    Dixon, R.A.3    Lamb, C.4
  • 8
    • 0033826053 scopus 로고    scopus 로고
    • Role of reactive oxygen intermediates and cognate redox signalling in disease resistance
    • J.J. Grant, and G.J. Loake Role of reactive oxygen intermediates and cognate redox signalling in disease resistance Plant Physiol. 124 2000 21 29
    • (2000) Plant Physiol. , vol.124 , pp. 21-29
    • Grant, J.J.1    Loake, G.J.2
  • 12
    • 35248829013 scopus 로고    scopus 로고
    • Identification of loci controlling non-host disease resistance in Arabidopsis against the leaf rust pathogen Puccinia triticina
    • DOI 10.1111/j.1364-3703.2007.00431.x
    • R. Shafiei, C. Hang, J.G. Kang, and G.J. Loake Identification of loci controlling non-host disease resistance in Arabidopsis against the leaf rust pathogen Puccinia triticina Mol. Plant Pathol. 8 2007 773 784 (Pubitemid 47568898)
    • (2007) Molecular Plant Pathology , vol.8 , Issue.6 , pp. 773-784
    • Shafiei, R.1    Hang, C.2    Kang, J.-G.3    Loake, G.J.4
  • 13
    • 33644655397 scopus 로고    scopus 로고
    • Cauliflower mosaic virus, a compatible pathogen of Arabidopsis, engages three distinct defence signalling pathways and activates rapid systemic generation of reactive oxygen species
    • A.J. Love, B.-Y. Yun, V. Laval, G.J. Loake, and J.J. Milner Cauliflower mosaic virus, a compatible pathogen of Arabidopsis, engages three distinct defence signalling pathways and activates rapid systemic generation of reactive oxygen species Plant Physiol. 139 2007 1 14
    • (2007) Plant Physiol. , vol.139 , pp. 1-14
    • Love, A.J.1    Yun, B.-Y.2    Laval, V.3    Loake, G.J.4    Milner, J.J.5
  • 14
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • J.D. Lambeth NOX enzymes and the biology of reactive oxygen Nat. Rev. Immunol. 4 2004 181 189 (Pubitemid 38339084)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.3 , pp. 181-189
    • Lambeth, J.D.1
  • 17
    • 44049090117 scopus 로고    scopus 로고
    • 2+ and phosphorylation
    • 2+ and phosphorylation J. Biol. Chem. 283 2008 8885 8892
    • (2008) J. Biol. Chem. , vol.283 , pp. 8885-8892
    • Ogasawara1
  • 21
    • 36248980473 scopus 로고    scopus 로고
    • Hydrogen peroxidase generation by the pepper extracellular peroxidase CaPO2 activates local and systemic cell death and defence response to bacterial pathogens
    • H.W. Choi, Y.J. Kim, S.C. Lee, J.K. Hong, and B.K. Hwang Hydrogen peroxidase generation by the pepper extracellular peroxidase CaPO2 activates local and systemic cell death and defence response to bacterial pathogens Plant Physiol. 145 2007 890 904
    • (2007) Plant Physiol. , vol.145 , pp. 890-904
    • Choi, H.W.1    Kim, Y.J.2    Lee, S.C.3    Hong, J.K.4    Hwang, B.K.5
  • 22
    • 0031448239 scopus 로고    scopus 로고
    • Mechanisms for the generation of reactive oxygen species in plant defence - A broad perspective
    • DOI 10.1006/pmpp.1997.0129
    • G.P. Bolwell, and P. Wojitaszek Mechanisms for the generation of reactive oxygen species in plant defense: a broad perspective Physiol. Mol. Plant Pathol. 51 1997 347 366 (Pubitemid 28228945)
    • (1997) Physiological and Molecular Plant Pathology , vol.51 , Issue.6 , pp. 347-366
    • Bolwell, G.P.1    Wojtaszek, P.2
  • 24
    • 43149090294 scopus 로고    scopus 로고
    • The hypersensitive response; The centenary is upon us but how much do we know?
    • DOI 10.1093/jxb/erm239
    • L.A.J. Mur, P. Kenton, A.J. Lloyd, H. Ougham, and E. Prats The hypersensitive response; the century is upon us but how much do we know? J. Exp. Bot. 59 2008 501 520 (Pubitemid 351640730)
    • (2008) Journal of Experimental Botany , vol.59 , Issue.3 , pp. 501-520
    • Mur, L.A.J.1    Kenton, P.2    Lloyd, A.J.3    Ougham, H.4    Prats, E.5
  • 25
    • 20044375371 scopus 로고    scopus 로고
    • Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis
    • DOI 10.1105/tpc.104.026971
    • S. Davletova, L. Rizhsky, H. Liang, Z. Shengqiang, D.J. Oliver, J. Coutu, V. Shulaev, K. Schlauch, and R. Mittler Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis Plant Cell 17 2005 268 281 (Pubitemid 41673002)
    • (2005) Plant Cell , vol.17 , Issue.1 , pp. 268-281
    • Davletova, S.1    Rizhsky, L.2    Liang, H.3    Shengqiang, Z.4    Oliver, D.J.5    Coutu, J.6    Shulaev, V.7    Schlauch, K.8    Mittler, R.9
  • 26
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses
    • C.H. Foyer, and G. Noctor Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses Plant Cell 17 2005 1866 1875
    • (2005) Plant Cell , vol.17 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 28
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • DOI 10.1042/0264-6021:3570593
    • W.K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615 (Pubitemid 32735142)
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 29
    • 33744950512 scopus 로고    scopus 로고
    • Constitutive arginine-dependent nitric oxide synthase activity in different organs of pea seedlings during plant development
    • DOI 10.1007/s00425-005-0205-9
    • F.J. Corpas, J.B. Barroso, A. Carreras, R. Valderrama, J.M. Palma, A.M. Leon, L.M. Sandalio, and L.A. del Rio Constitutive arginine-dependent nitric oxide synthase activity in different organs of pea seedlings during plant development Planta 224 2006 246 254 (Pubitemid 43946044)
    • (2006) Planta , vol.224 , Issue.2 , pp. 246-254
    • Corpas, F.J.1    Barroso, J.B.2    Carreras, A.3    Valderrama, R.4    Palma, J.M.5    Leon, A.M.6    Sandalio, L.M.7    Del Rio, L.A.8
  • 31
    • 0038740645 scopus 로고    scopus 로고
    • The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex
    • DOI 10.1016/S0092-8674(03)00350-7
    • M.R. Chandok, A.J. Ytterberg, K.J. van Wijk, and D.F. Klessig The pathogen-inducible nitric oxide synthase (iNOS) in plants is a variant of the P protein of the glycine decarboxylase complex Cell 113 2003 469 482 (Pubitemid 36588750)
    • (2003) Cell , vol.113 , Issue.4 , pp. 469-482
    • Chandok, M.R.1    Ytterberg, A.J.2    Van Wijk, K.J.3    Klessig, D.F.4
  • 32
    • 0141531067 scopus 로고    scopus 로고
    • Identification of a plant nitric oxide synthase gene involved in hormonal signaling
    • DOI 10.1126/science.1086770
    • F.Q. Guo, M. Okamoto, and N.M. Crawford Identification of a plant nitric oxide synthase gene involved in hormonal signaling Science 302 2003 100 103 (Pubitemid 37210696)
    • (2003) Science , vol.302 , Issue.5642 , pp. 100-103
    • Guo, F.-Q.1    Okamoto, M.2    Crawford, N.M.3
  • 33
    • 33750362866 scopus 로고    scopus 로고
    • Response to Zemojtel et al: Plant nitric oxide synthase: back to square one
    • DOI 10.1016/j.tplants.2006.09.007, PII S1360138506002524
    • N.M. Crawford, M. Galli, R. Tischner, Y.M. Heimer, M. Okamoto, and A. Mack Plant nitric oxide synthase: back to square one - response Trends Plant Sci. 11 2006 526 527 (Pubitemid 44636299)
    • (2006) Trends in Plant Science , vol.11 , Issue.11 , pp. 526-527
    • Crawford, N.M.1    Galli, M.2    Tischner, R.3    Heimer, Y.M.4    Okamoto, M.5    Mack, A.6
  • 35
    • 57749108288 scopus 로고    scopus 로고
    • AtNOS/AtNOA1 is a functional Arabidopsis thaliana cGTPase and not a nitric-oxide synthase
    • M. Moreau, G.I. Lee, Y. Wang, B.R. Crane, and D.F. Klessig AtNOS/AtNOA1 is a functional Arabidopsis thaliana cGTPase and not a nitric-oxide synthase J. Biol. Chem. 283 2008 32957 32967
    • (2008) J. Biol. Chem. , vol.283 , pp. 32957-32967
    • Moreau, M.1    Lee, G.I.2    Wang, Y.3    Crane, B.R.4    Klessig, D.F.5
  • 37
    • 56049097303 scopus 로고    scopus 로고
    • MAPK signaling regulates nitric oxide and NADPH oxidase-dependent oxidative bursts in Nicotiana benthamiana
    • DOI 10.1105/tpc.107.055855
    • S. Asai, K. Ohta, and H. Yoshioka MAPK signaling regulates nitric oxide and NADPH oxidase-dependent oxidative bursts in Nicotiana benthamiana Plant Cell 20 2008 1390 1406 (Pubitemid 352844190)
    • (2008) Plant Cell , vol.20 , Issue.5 , pp. 1390-1406
    • Asai, S.1    Ohta, K.2    Yoshioka, H.3
  • 38
    • 33747667570 scopus 로고    scopus 로고
    • An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression
    • DOI 10.1074/jbc.M602135200
    • N. Arnaud, I. Murgia, J. Boucherez, J.F. Briat, F. Cellier, and F. Gaymard An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression J. Biol. Chem. 281 2006 23579 23588 (Pubitemid 44274132)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.33 , pp. 23579-23588
    • Arnaud, N.1    Murgia, I.2    Boucherez, J.3    Briat, J.-F.4    Cellier, F.5    Gaymard, F.6
  • 39
    • 43149119873 scopus 로고    scopus 로고
    • Exogenous auxin-induced NO synthesis is nitrate reductase-associated in Arabidopsis thaliana root primordia
    • DOI 10.1016/j.jplph.2007.07.019, PII S0176161707002295
    • Z. Kolbert, B. Bartha, and L. Erdei Exogenous auxin-induced NO synthesis is nitrate reductase-associated in Arabidopsis thaliana root primordial J. Plant Physiol. 165 2008 967 975 (Pubitemid 351718468)
    • (2008) Journal of Plant Physiology , vol.165 , Issue.9 , pp. 967-975
    • Kolbert, Zs.1    Bartha, B.2    Erdei, L.3
  • 40
    • 42249086477 scopus 로고    scopus 로고
    • Zeatin-induced nitric oxide (NO) biosynthesis in Arabidopsis thaliana mutants of NO biosynthesis and of two-component signaling genes
    • DOI 10.1111/j.1469-8137.2008.02383.x
    • N.N. Tun, M. Livaja, J.J. Kieber, and G.F. Scherer Zeatin-induced nitric oxide (NO) biosynthesis in Arabidopsis thaliana mutants of NO biosynthesis and of two-component signaling genes New Phytol. 178 2008 515 531 (Pubitemid 351550564)
    • (2008) New Phytologist , vol.178 , Issue.3 , pp. 515-531
    • Tun, N.N.1    Livaja, M.2    Kieber, J.J.3    Scherer, G.F.E.4
  • 41
    • 56549123692 scopus 로고    scopus 로고
    • A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids
    • DOI 10.1105/tpc.108.058768
    • U. Flores-Perez, S. Sauret-Gueto, E. Gas, P. Jarvis, and M. Rodriguez-Concepcion A mutant impaired in the production of plastome-encoded proteins uncovers a mechanism for the homeostasis of isoprenoid biosynthetic enzymes in Arabidopsis plastids Plant Cell 20 2008 1303 1315 (Pubitemid 352844184)
    • (2008) Plant Cell , vol.20 , Issue.5 , pp. 1303-1315
    • Flores-Perez, U.1    Sauret-Gueto, S.2    Gas, E.3    Jarvis, P.4    Rodriguez-Concepciona, M.5
  • 42
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • DOI 10.1006/jmbi.2001.5378
    • D.D. Leipe, Y.I. Wolf, E.V. Koonin, and L. Aravind Classification and evolution of P-loop GTPases and related ATPases J. Mol. Biol. 317 2002 41 72 (Pubitemid 34722199)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.1 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 43
    • 78650891858 scopus 로고    scopus 로고
    • Characterization of a nitric oxide synthase from the plant kingdom: NO generation from the green alga Ostreococcus tauri is light irradiance and growth phase dependent
    • N. Foresi, N. Correa-Aragunde, G. Parisi, G. Calo, G. Salerno, and L. Lamattina Characterization of a nitric oxide synthase from the plant kingdom: NO generation from the green alga Ostreococcus tauri is light irradiance and growth phase dependent Plant Cell 22 2010 3816 3830
    • (2010) Plant Cell , vol.22 , pp. 3816-3830
    • Foresi, N.1    Correa-Aragunde, N.2    Parisi, G.3    Calo, G.4    Salerno, G.5    Lamattina, L.6
  • 44
    • 0026150937 scopus 로고
    • Identification of the Arabidopsis CHL3 gene as the nitrate reductase structural gene NIA2
    • J.Q. Wilkinson, and N.M. Crawford Identification of the Arabidopsis CHL3 gene as the nitrate reductase structural gene NIA2 Plant Cell 3 1991 461 471 (Pubitemid 21913712)
    • (1991) Plant Cell , vol.3 , Issue.5 , pp. 461-471
    • Wilkinson, J.Q.1    Crawford, N.M.2
  • 45
    • 0036006867 scopus 로고    scopus 로고
    • Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro
    • P. Rockel, F. Strube, A. Rockel, J. Wildt, and W.M. Kaiser Regulation of nitric oxide (NO) production by plant nitrate reductase in vivo and in vitro J. Exp. Bot. 53 2002 103 110 (Pubitemid 34043147)
    • (2002) Journal of Experimental Botany , vol.53 , Issue.366 , pp. 103-110
    • Rockel, P.1    Strube, F.2    Rockel, A.3    Wildt, J.4    Kaiser, W.M.5
  • 46
    • 0033952545 scopus 로고    scopus 로고
    • Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: In vitro evidence for the NR-dependent formation of active nitrogen species
    • DOI 10.1016/S0014-5793(00)01203-5, PII S0014579300012035
    • H. Yamasaki, and Y. Sakihama Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species FEBS Lett. 468 2000 89 92 (Pubitemid 30101688)
    • (2000) FEBS Letters , vol.468 , Issue.1 , pp. 89-92
    • Yamasaki, H.1    Sakihama, Y.2
  • 47
    • 39049084257 scopus 로고    scopus 로고
    • Verticillium dahliae toxins-induced nitric oxide production in Arabidopsis is major dependent on nitrate reductase
    • F.M. Shi, and Y.Z. Li Verticillium dahliae toxins-induced nitric oxide production in Arabidopsis is major dependent on nitrate reductase BMB Rep. 41 2008 79 85
    • (2008) BMB Rep. , vol.41 , pp. 79-85
    • Shi, F.M.1    Li, Y.Z.2
  • 48
    • 61349183750 scopus 로고    scopus 로고
    • Nitric oxide production occurs downstream of reactive oxygen species in guard cells during stomatal closure induced by chitosan in abaxial epidermis of Pisum sativum
    • N. Srivastava, V.K. Gonugunta, M.R. Puli, and A.S. Raghavendra Nitric oxide production occurs downstream of reactive oxygen species in guard cells during stomatal closure induced by chitosan in abaxial epidermis of Pisum sativum Planta 229 2009 757 765
    • (2009) Planta , vol.229 , pp. 757-765
    • Srivastava, N.1    Gonugunta, V.K.2    Puli, M.R.3    Raghavendra, A.S.4
  • 49
    • 4243223355 scopus 로고
    • Nitrate reductase of nitrate respiration type from E. coli. I. solubilization and purification from the particulate system with molecular characterization as a metalloprotein
    • S. Taniguchi, and E. Itagaki Nitrate reductase of nitrate respiration type from E. coli. I. solubilization and purification from the particulate system with molecular characterization as a metalloprotein Biochim. Biophys. Acta 44 1960 263 279
    • (1960) Biochim. Biophys. Acta , vol.44 , pp. 263-279
    • Taniguchi, S.1    Itagaki, E.2
  • 51
    • 33745396481 scopus 로고    scopus 로고
    • Nitrate reductase is responsible for elicitin-induced nitric oxide production in Nicotiana benthamiana
    • DOI 10.1093/pcp/pcj044
    • A. Yamamoto-Katou, S. Katou, H. Yoshioka, N. Doke, and K. Kawakita Nitrate reductase is responsible for elicitin-induced nitric oxide production in Nicotiana benthamiana Plant Cell Physiol. 47 2006 726 735 (Pubitemid 43946301)
    • (2006) Plant and Cell Physiology , vol.47 , Issue.6 , pp. 726-735
    • Yamamoto-Katou, A.1    Katou, S.2    Yoshioka, H.3    Doke, N.4    Kawakita, K.5
  • 52
    • 33747429121 scopus 로고    scopus 로고
    • Decreased arginine and nitrite levels in nitrate reductase-deficient Arabidopsis thaliana plants impair nitric oxide synthesis and the hypersensitive response to Pseudomonas syringae
    • DOI 10.1016/j.plantsci.2006.02.010, PII S0168945206000598
    • L.V. Modolo, O. Augusto, I.M.G. Almeida, C.A.F. Pinto-Maglio, H.C. Oliveira, K. Seligman, and I. Salgado Decreased arginine and nitrite levels in nitrate reductase-deficient Arabidopsis thaliana plants impair nitric oxide synthesis and the hypersensitive response to Pseudomonas syringae Plant Sci. 171 2006 34 40 (Pubitemid 44251004)
    • (2006) Plant Science , vol.171 , Issue.1 , pp. 34-40
    • Modolo, L.V.1    Augusto, O.2    Almeida, I.M.G.3    Pinto-Maglio, C.A.F.4    Oliveira, H.C.5    Seligman, K.6    Salgado, I.7
  • 53
    • 56049109730 scopus 로고    scopus 로고
    • Amino acid recovery does not prevent susceptibility to Pseudomonas syringae in nitrate reductase double-deficient Arabidopsis thaliana plants
    • H.C. Oliveira, G.C. Justino, L. Sodek, and I. Salgado Amino acid recovery does not prevent susceptibility to Pseudomonas syringae in nitrate reductase double-deficient Arabidopsis thaliana plants Plant Sci. 176 2009 105 111
    • (2009) Plant Sci. , vol.176 , pp. 105-111
    • Oliveira, H.C.1    Justino, G.C.2    Sodek, L.3    Salgado, I.4
  • 54
    • 0037059014 scopus 로고    scopus 로고
    • A new role for an old enzyme: Nitrate reductase-mediated nitric oxide generation is required for abscisic acid-induced stomatal closure in Arabidopsis thaliana
    • DOI 10.1073/pnas.252461999
    • R. Desikan, R. Griffiths, J. Hancock, and S. Neill A new role for an old enzyme: nitrate reductase-mediated nitric oxide generation is required for abscisic acid-induced stomatal closure in Arabidopsis thaliana Proc. Natl. Acad. Sci. USA 99 2002 16314 16318 (Pubitemid 35462792)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.25 , pp. 16314-16318
    • Desikan, R.1    Griffiths, R.2    Hancock, J.3    Neill, S.4
  • 55
    • 78049481933 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated activation of MAP Kinase 6 modulates nitric oxide biosynthesis and signal transduction in Arabidopsis
    • P. Wang, Y. Du, Y. Li, D. Ren, and C.-P. Song Hydrogen peroxide-mediated activation of MAP Kinase 6 modulates nitric oxide biosynthesis and signal transduction in Arabidopsis Plant Cell 22 2010 2981 2998
    • (2010) Plant Cell , vol.22 , pp. 2981-2998
    • Wang, P.1    Du, Y.2    Li, Y.3    Ren, D.4    Song, C.-P.5
  • 56
    • 0037365968 scopus 로고    scopus 로고
    • Specificity of a third kind: Reactive oxygen and nitrogen intermediates in cell signaling
    • DOI 10.1172/JCI200318174
    • C. Nathan Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling J. Clin. Invest. 111 2003 769 778 (Pubitemid 37074948)
    • (2003) Journal of Clinical Investigation , vol.111 , Issue.6 , pp. 769-778
    • Nathan, C.1
  • 57
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • DOI 10.1016/S1097-2765(02)00445-8
    • T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of tyrosine phosphatases in vivo Mol. Cell 9 2002 387 399 (Pubitemid 34195563)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 387-399
    • Meng, T.-C.1    Fukada, T.2    Tonks, N.K.3
  • 58
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signaling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autŕeaux, and M.B. Toledano ROS as signaling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell Biol. 8 2007 813 823
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-823
    • D'Autŕeaux, B.1    Toledano, M.B.2
  • 59
    • 77952077940 scopus 로고    scopus 로고
    • The redox switch: Dynamic regulation of protein function by cysteine modifications
    • D. Spadaroa, B.-Y. Yun, S.H. Spoel, C. Chuc, Y.-Q. Wang, and G.J. Loake The redox switch: dynamic regulation of protein function by cysteine modifications Physiol. Plant. 138 2010 360 371
    • (2010) Physiol. Plant. , vol.138 , pp. 360-371
    • Spadaroa, D.1    Yun, B.-Y.2    Spoel, S.H.3    Chuc, C.4    Wang, Y.-Q.5    Loake, G.J.6
  • 60
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • DOI 10.1126/science.1158265
    • M. Benhar, M.T. Forrester, D.T. Hess, and J.S. Stamler Regulated protein denitsoylation by cytosolic and mitochondrial thioredoxins Science 320 2008 1050 1054 (Pubitemid 351929542)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 62
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation and a consensus motif
    • J.S. Stamler, E.J. Toone, S.A. Lipton, and N.J. Sucher (S)NO signals: translocation, regulation and a consensus motif Neuron 18 1997 691 696
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 65
    • 77955283497 scopus 로고    scopus 로고
    • GPS-SNO: Computational prediction of protein S-Nitrosylation sites with a modified GPS algorithm
    • Y. Xue, Z. Liu, X. Gao, C. Jin, L. Wen, X. Yao, and J. Ren GPS-SNO: computational prediction of protein S-Nitrosylation sites with a modified GPS algorithm PLoS One 5 2010 e11290
    • (2010) PLoS One , vol.5 , pp. 11290
    • Xue, Y.1    Liu, Z.2    Gao, X.3    Jin, C.4    Wen, L.5    Yao, X.6    Ren, J.7
  • 66
    • 33846635882 scopus 로고    scopus 로고
    • High-throughput identification of catalytic redox-active cystein residues
    • DOI 10.1126/science.1133114
    • D.E. Fomenko, W. Xing, B.M. Adair, D.J. Thomas, and V.N. Gladyshev High throughput identification of catalytic redox-active cysteine residues Science 315 2007 387 389 (Pubitemid 46175521)
    • (2007) Science , vol.315 , Issue.5810 , pp. 387-389
    • Fomenko, D.E.1    Xing, W.2    Adair, B.M.3    Thomas, D.J.4    Gladyshev, V.N.5
  • 68
    • 0028191408 scopus 로고
    • Characterization of an Arabidopsis mutant that is nonresponsive to inducers of systemic acquired resistance
    • H. Cao, S.A. Bowling, A.S. Gordon, and X.N. Dong Characterisation of an Arabidopsis mutant that is nonresponsive to inducers of systemic acquired resistance Plant Cell 6 1994 1583 1592 (Pubitemid 24986212)
    • (1994) Plant Cell , vol.6 , Issue.11 , pp. 1583-1592
    • Cao, H.1    Bowling, S.A.2    Gordon, A.S.3    Dong, X.4
  • 69
    • 0038826955 scopus 로고    scopus 로고
    • Inducers of plant systemic acquired resistance Regulate NPR1 function through redox changes
    • DOI 10.1016/S0092-8674(03)00429-X
    • Z. Mou, W.H. Fan, and X.N. Dong Inducers of plant systemic acquired resistance regulate NPR1 function through redox changes Cell 113 2003 935 944 (Pubitemid 36792035)
    • (2003) Cell , vol.113 , Issue.7 , pp. 935-944
    • Mou, Z.1    Fan, W.2    Dong, X.3
  • 70
    • 65849096454 scopus 로고    scopus 로고
    • Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity
    • S.H. Spoel, Z.L. Mou, Y. Tada, N.W. Spivey, P. Genschik, and X. Dong Proteasome-mediated turnover of the transcription coactivator NPR1 plays dual roles in regulating plant immunity Cell 137 2009 860 872
    • (2009) Cell , vol.137 , pp. 860-872
    • Spoel, S.H.1    Mou, Z.L.2    Tada, Y.3    Spivey, N.W.4    Genschik, P.5    Dong, X.6
  • 71
    • 0141746099 scopus 로고    scopus 로고
    • The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domain/Leucine Zipper transcription factor TGA1
    • DOI 10.1105/tpc.012849
    • C. Després, C. Chubak, A. Rochon, R. Clark, T. Bethune, D. Desveaux, and P.R. Fobert The Arabidopsis NPR1 disease resistance protein is a novel cofactor that confers redox regulation of DNA binding activity to the basic domainleucine zipper transcription factor TGA1 Plant Cell 15 2003 2181 2191 (Pubitemid 37144069)
    • (2003) Plant Cell , vol.15 , Issue.9 , pp. 2181-2191
    • Despres, C.1    Chubak, C.2    Rochon, A.3    Clark, R.4    Bethune, T.5    Desveaux, D.6    Fobert, P.R.7
  • 72
    • 77957824005 scopus 로고    scopus 로고
    • Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide
    • C. Lindermayr, S. Sell, B. Müller, D. Leister, and J. Durner Redox regulation of the NPR1-TGA1 system of Arabidopsis thaliana by nitric oxide Plant Cell 22 2010 2894 2907
    • (2010) Plant Cell , vol.22 , pp. 2894-2907
    • Lindermayr, C.1    Sell, S.2    Müller, B.3    Leister, D.4    Durner, J.5
  • 74
    • 0027756183 scopus 로고
    • Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid
    • Z. Chen, H. Silva, and D.F. Klessig Active oxygen species in the induction of plant systemic acquired-resistance by salicylic acid Science 262 1993 1883 1886 (Pubitemid 24041861)
    • (1993) Science , vol.262 , Issue.5141 , pp. 1883-1886
    • Chen, Z.1    Silva, H.2    Klessig, D.F.3
  • 75
    • 0347364622 scopus 로고    scopus 로고
    • High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity
    • DOI 10.1073/pnas.0307162100
    • D. Kumar, and D.F. Klessig High-affinity salicylic acid-binding protein 2 is required for plant innate immunity and has salicylic acid-stimulated lipase activity Proc. Natl. Acad. Sci. USA 100 2003 16101 16106 (Pubitemid 38021121)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.26 , pp. 16101-16106
    • Kumar, D.1    Klessig, D.F.2
  • 77
    • 0036010675 scopus 로고    scopus 로고
    • Biochemical and molecular inhibition of plastidial carbonic anhydrase reduces the incorporation of acetate into lipids in cotton embryos and tobacco cell suspensions and leaves
    • DOI 10.1104/pp.010879
    • C.V. Hoang, and K.D. Chapman Biochemical and molecular inhibition of plastidial carbonic anhydrase reduces the incorporation of acetate into lipids in cotton embryos and tobacco cell suspensions and leaves Plant Physiol. 128 2002 1417 1427 (Pubitemid 34305793)
    • (2002) Plant Physiology , vol.128 , Issue.4 , pp. 1417-1427
    • Hoang, C.V.1    Chapman, K.D.2
  • 81
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • DOI 10.1126/science.1158265
    • M. Benhar, M.T. Forrester, D.T. Hess, and J.S. Stamler Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins Science 320 2008 1050 1054 (Pubitemid 351929542)
    • (2008) Science , vol.320 , Issue.5879 , pp. 1050-1054
    • Benhar, M.1    Forrester, M.T.2    Hess, D.T.3    Stamler, J.S.4
  • 82
    • 0035252076 scopus 로고    scopus 로고
    • Export by red blood cells of nitric oxide bioactivity
    • DOI 10.1038/35054560
    • J.R. Pawloski, D.T. Hess, and J.S. Stamler Export by red blood cells of nitric oxide bioactivity Nature 409 2001 622 626 (Pubitemid 32154814)
    • (2001) Nature , vol.409 , Issue.6820 , pp. 622-626
    • Pawloski, J.R.1    Hes, D.T.2    Stamler, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.