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Volumn 56, Issue 6, 2008, Pages 1963-1976

Proteome changes in leaves of Brassica napus L. as a result of Sclerotinia sclerotiorum challenge

Author keywords

Biotic stress; Brassica napus; Glyoxalase; Peroxidase; Sclerotinia sclerotiorum

Indexed keywords

ANTIOXIDANT; PROTEOME;

EID: 41849098566     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf073012d     Document Type: Article
Times cited : (58)

References (70)
  • 2
    • 0038597601 scopus 로고
    • Index of plant hosts of Sclerotinia sclerotiorum
    • Boland, G. J.; Hall, R. Index of plant hosts of Sclerotinia sclerotiorum. Can. J. Plant Pathol. 1994, 16, 93-108.
    • (1994) Can. J. Plant Pathol , vol.16 , pp. 93-108
    • Boland, G.J.1    Hall, R.2
  • 3
    • 41849124448 scopus 로고    scopus 로고
    • Rimmer, S. R.; Kutcher, H. R.; Morrall, R. A. A. Diseases of canola and mustard. In Diseases of Field Crops in Canada; Bailey, K. L. ,Gossen, B. D., Gugel, R. K., Morrall, R. A. A., Eds.; Canadian Phytopathology Society:Saskatoon, SK, Canada, 2003; pp 129-146.
    • Rimmer, S. R.; Kutcher, H. R.; Morrall, R. A. A. Diseases of canola and mustard. In Diseases of Field Crops in Canada; Bailey, K. L. ,Gossen, B. D., Gugel, R. K., Morrall, R. A. A., Eds.; Canadian Phytopathology Society:Saskatoon, SK, Canada, 2003; pp 129-146.
  • 4
    • 0031020876 scopus 로고    scopus 로고
    • Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi
    • Annis, S. L.; Goodwin, P. H. Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi. Eur. J. Plant Pathol. 1997, 103, 1-14.
    • (1997) Eur. J. Plant Pathol , vol.103 , pp. 1-14
    • Annis, S.L.1    Goodwin, P.H.2
  • 5
    • 0142226991 scopus 로고    scopus 로고
    • Ambient pH controls the expression of endopolygalacturonase genes in the necrotrophic fungus Sclerotinia sclerotiorum
    • Cotton, P.; Kasza, Z.; Bruel, C.; Rascle, C.; Fèvre, M. Ambient pH controls the expression of endopolygalacturonase genes in the necrotrophic fungus Sclerotinia sclerotiorum. FEMS Microbiol. Lett. 2003, 227, 163-169.
    • (2003) FEMS Microbiol. Lett , vol.227 , pp. 163-169
    • Cotton, P.1    Kasza, Z.2    Bruel, C.3    Rascle, C.4    Fèvre, M.5
  • 6
    • 0001467680 scopus 로고
    • Use of mutants to demonstrate the role of oxalic acid in pathogenicity of Sclerotinia sclerotiorum on Phaseolus vulgaris
    • Godoy, G.; Steadman, J. R.; Dickman, M. B.; Dam, R. Use of mutants to demonstrate the role of oxalic acid in pathogenicity of Sclerotinia sclerotiorum on Phaseolus vulgaris. Physiol. Mol. Plant Pathol. 1990, 37, 179-191.
    • (1990) Physiol. Mol. Plant Pathol , vol.37 , pp. 179-191
    • Godoy, G.1    Steadman, J.R.2    Dickman, M.B.3    Dam, R.4
  • 7
    • 16544377400 scopus 로고    scopus 로고
    • Oxalate production by Sclerotinia sclerotiorum deregulates guard cells during infection
    • Guimarães, R. L.; Stotz, H. U. Oxalate production by Sclerotinia sclerotiorum deregulates guard cells during infection. Plant Physiol. 2004, 136, 3703-3711.
    • (2004) Plant Physiol , vol.136 , pp. 3703-3711
    • Guimarães, R.L.1    Stotz, H.U.2
  • 8
    • 0025774855 scopus 로고
    • Production of cell wall-degrading enzymes by the phytopathogenic fungus Sclerotinia sclerotiorum
    • Riou, C.; Freyssinet, G.; Fevre, M. Production of cell wall-degrading enzymes by the phytopathogenic fungus Sclerotinia sclerotiorum. Appl. Environ. Microbiol. 1991, 57, 1478-1484.
    • (1991) Appl. Environ. Microbiol , vol.57 , pp. 1478-1484
    • Riou, C.1    Freyssinet, G.2    Fevre, M.3
  • 9
    • 33645102390 scopus 로고    scopus 로고
    • Sclerotinia sclerotiorum (Lib.) de Bary: Biology and molecular traits of a cosmopolitan pathogen
    • Bolton, M. D.; Thomma, B. P. H. J.; Nelson, B. D. Sclerotinia sclerotiorum (Lib.) de Bary: biology and molecular traits of a cosmopolitan pathogen. Mol. Plant Pathol. 2006, 7, 1-16.
    • (2006) Mol. Plant Pathol , vol.7 , pp. 1-16
    • Bolton, M.D.1    Thomma, B.P.H.J.2    Nelson, B.D.3
  • 10
    • 33845232009 scopus 로고    scopus 로고
    • The proteome of the phytopathogenic fungus Sclerotinia sclerotiorum
    • Yajima, W.; Kav, N. N. V. The proteome of the phytopathogenic fungus Sclerotinia sclerotiorum. Proteomics 2006, 6, 5995-6007.
    • (2006) Proteomics , vol.6 , pp. 5995-6007
    • Yajima, W.1    Kav, N.N.V.2
  • 11
    • 3042544371 scopus 로고    scopus 로고
    • Interaction of Sclerotinia sclerotiorum with a resistant Brassica napus cultivar: Expressed sequence tag analysis identifies genes associated with fungal pathogenesis
    • Li, R.; Rimmer, R.; Buchwaldt, L.; Sharpe, A. G.; Séguin-Swartz, G.; Coutu, C.; Hegedus, D. D. Interaction of Sclerotinia sclerotiorum with a resistant Brassica napus cultivar: expressed sequence tag analysis identifies genes associated with fungal pathogenesis. Fungal Genet. Biol. 2004, 41, 735-753.
    • (2004) Fungal Genet. Biol , vol.41 , pp. 735-753
    • Li, R.1    Rimmer, R.2    Buchwaldt, L.3    Sharpe, A.G.4    Séguin-Swartz, G.5    Coutu, C.6    Hegedus, D.D.7
  • 12
    • 33751340782 scopus 로고    scopus 로고
    • Identification of prior candidate genes for Sclerotinia local resistance in Brassica napus using Arabidopsis cDNA microarray and Brassica-Arabidopsis comparative mapping
    • Liu, R.; Zhao, J.; Xiao, Y.; Meng, J. Identification of prior candidate genes for Sclerotinia local resistance in Brassica napus using Arabidopsis cDNA microarray and Brassica-Arabidopsis comparative mapping. Sci. China Ser. C: Life Sci. 2005, 48, 460-470.
    • (2005) Sci. China Ser. C: Life Sci , vol.48 , pp. 460-470
    • Liu, R.1    Zhao, J.2    Xiao, Y.3    Meng, J.4
  • 13
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P.; Rochon, Y.; Franza, B. R.; Aebersold, R. Correlation between protein and mRNA abundance in yeast. Mol. Cell. Biol. 1999, 19, 1720-1730.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 14
    • 7944235545 scopus 로고    scopus 로고
    • Proteome-level changes in the roots of Pisum sativum in response to salinity
    • Kav, N. N. V.; Srivastava, S.; Goonewardene, L.; Blade, S. F. Proteome-level changes in the roots of Pisum sativum in response to salinity. Ann. Appl. Biol. 2004, 145, 217-230.
    • (2004) Ann. Appl. Biol , vol.145 , pp. 217-230
    • Kav, N.N.V.1    Srivastava, S.2    Goonewardene, L.3    Blade, S.F.4
  • 15
    • 12344268211 scopus 로고    scopus 로고
    • Proteome-level investigation of Brassica carinata derived resistance to Leptosphaeria maculans
    • Subramanian, S.; Bansal, V. K.; Kav, N. N. V. Proteome-level investigation of Brassica carinata derived resistance to Leptosphaeria maculans. J. Agric. Food Chem. 2005, 53, 313-324.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 313-324
    • Subramanian, S.1    Bansal, V.K.2    Kav, N.N.V.3
  • 16
    • 33750701783 scopus 로고    scopus 로고
    • Proteome-level changes in two Brassica napus lines exhibiting differential responses to the fungal pathogen Alternaria brassicae
    • Sharma, N.; Rahman, M. H.; Strelkov, S. E.; Thiagarajah, M.; Bansal, V. K.; Kav, N. N. V. Proteome-level changes in two Brassica napus lines exhibiting differential responses to the fungal pathogen Alternaria brassicae. Plant Sci. 2006, 172, 95-110.
    • (2006) Plant Sci , vol.172 , pp. 95-110
    • Sharma, N.1    Rahman, M.H.2    Strelkov, S.E.3    Thiagarajah, M.4    Bansal, V.K.5    Kav, N.N.V.6
  • 17
    • 33745287881 scopus 로고    scopus 로고
    • Proteomics reveals elevated levels of PR 10 proteins in saline-tolerant peanut (Arachis hypogaea) calli
    • Jain, S.; Srivastava, S.; Sarin, N. B.; Kav, N. N. V. Proteomics reveals elevated levels of PR 10 proteins in saline-tolerant peanut (Arachis hypogaea) calli. Plant Physiol. Biochem. 2006, 44, 253-259.
    • (2006) Plant Physiol. Biochem , vol.44 , pp. 253-259
    • Jain, S.1    Srivastava, S.2    Sarin, N.B.3    Kav, N.N.V.4
  • 18
    • 33748344060 scopus 로고    scopus 로고
    • Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host Triticum aestivum
    • Zhou, W.; Eudes, F.; Laroche, A. Identification of differentially regulated proteins in response to a compatible interaction between the pathogen Fusarium graminearum and its host Triticum aestivum. Proteomics 2006, 6, 4599-4609.
    • (2006) Proteomics , vol.6 , pp. 4599-4609
    • Zhou, W.1    Eudes, F.2    Laroche, A.3
  • 20
    • 0004254020 scopus 로고
    • 4th ed, George, C, Ed, William and Wilkins: Baltimore, MD
    • Dougherty, W. J. In Staining Procedures, 4th ed.; George, C., Ed.; William and Wilkins: Baltimore, MD, 1981; pp 27-38.
    • (1981) Staining Procedures , pp. 27-38
    • Dougherty, W.J.1
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1967, 72, 248-254.
    • (1967) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 33947536792 scopus 로고    scopus 로고
    • A crucial role for cytokinins in pea ABR17-mediated enhanced germination and early seedling growth of Arabidopsis thaliana under saline and low-temperature stresses
    • Srivastava, S.; Emery, R. J. N.; Rahman, M. H.; Kav, N. N. V. A crucial role for cytokinins in pea ABR17-mediated enhanced germination and early seedling growth of Arabidopsis thaliana under saline and low-temperature stresses. J. Plant Growth Regul. 2007, 26, 26-37.
    • (2007) J. Plant Growth Regul , vol.26 , pp. 26-37
    • Srivastava, S.1    Emery, R.J.N.2    Rahman, M.H.3    Kav, N.N.V.4
  • 24
    • 34047244162 scopus 로고    scopus 로고
    • Chilling effect on soluble sugars, respiration rate, total phenolics, peroxidase activity and dormancy of onion bulbs
    • Benkeblia, N.; Shiomi, N. Chilling effect on soluble sugars, respiration rate, total phenolics, peroxidase activity and dormancy of onion bulbs. Sci. Agric. 2004, 61, 281-285.
    • (2004) Sci. Agric , vol.61 , pp. 281-285
    • Benkeblia, N.1    Shiomi, N.2
  • 25
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • Beauchamp, C.; Fridovich, I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971, 44, 276-287.
    • (1971) Anal. Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 26
    • 0000597483 scopus 로고
    • Superoxide dismutases: I. Occurrence in higher plants
    • Giannopolitis, C. N.; Ries, S. K. Superoxide dismutases: I. Occurrence in higher plants. Plant Physiol. 1977, 59, 309-314.
    • (1977) Plant Physiol , vol.59 , pp. 309-314
    • Giannopolitis, C.N.1    Ries, S.K.2
  • 27
    • 0036678462 scopus 로고    scopus 로고
    • Differential induction of superoxide dismutase in downy mildew-resistant and -susceptible genotypes of pearl millet
    • Babitha, M. P.; Bhat, S. G.; Prakash, H. S.; Shetty, H. S. Differential induction of superoxide dismutase in downy mildew-resistant and -susceptible genotypes of pearl millet. Plant Pathol. 2002, 51, 480-486.
    • (2002) Plant Pathol , vol.51 , pp. 480-486
    • Babitha, M.P.1    Bhat, S.G.2    Prakash, H.S.3    Shetty, H.S.4
  • 28
    • 0000760905 scopus 로고
    • Histopathology of Sclerotinia sclerotiorum infection of bean
    • Lumsden, D. R.; Dow, R. L. Histopathology of Sclerotinia sclerotiorum infection of bean. Phytopathology 1973, 63, 708-715.
    • (1973) Phytopathology , vol.63 , pp. 708-715
    • Lumsden, D.R.1    Dow, R.L.2
  • 29
    • 0024755607 scopus 로고
    • Rubisco assembly: A model system for studying the mechanism of chaperonin action
    • Roy, H. Rubisco assembly: a model system for studying the mechanism of chaperonin action. Plant Cell 1989, 1, 1035-1042.
    • (1989) Plant Cell , vol.1 , pp. 1035-1042
    • Roy, H.1
  • 30
    • 0035836695 scopus 로고    scopus 로고
    • A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress
    • Hanson, T. E.; Tabita, F. R. A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 2001, 98, 4397-4402.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 31
    • 0028836508 scopus 로고
    • Characterization of chilling effects on photosynthetic performance of maize crops during early season growth using chlorophyll fluorescence
    • Andrews, J. R.; Fryer, M. J.; Baker, N. R. Characterization of chilling effects on photosynthetic performance of maize crops during early season growth using chlorophyll fluorescence. J. Exp. Bot. 1995, 46, 1195-1203.
    • (1995) J. Exp. Bot , vol.46 , pp. 1195-1203
    • Andrews, J.R.1    Fryer, M.J.2    Baker, N.R.3
  • 32
    • 0029178064 scopus 로고
    • Subsaturating ribulose-1,5-bisphosphate concentration promotes inactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) (studies using continuous substrate addition in the presence and absence of rubisco activase)
    • Portis, A. R., Jr.; Lilley, R. M.; Andrews, T. J. Subsaturating ribulose-1,5-bisphosphate concentration promotes inactivation of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) (studies using continuous substrate addition in the presence and absence of rubisco activase). Plant Physiol. 1995, 109, 1441-1451.
    • (1995) Plant Physiol , vol.109 , pp. 1441-1451
    • Portis Jr., A.R.1    Lilley, R.M.2    Andrews, T.J.3
  • 33
    • 0033989946 scopus 로고    scopus 로고
    • Kleczkowski, L. A. Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme. Biochim. Biophys. Acta 2000, 1476, 103-108.
    • Kleczkowski, L. A. Is leaf ADP-glucose pyrophosphorylase an allosteric enzyme. Biochim. Biophys. Acta 2000, 1476, 103-108.
  • 34
    • 0014267264 scopus 로고
    • Regulation of starch biosynthesis in plant leaves: Activation and inhibition of ADPglucose pyrophosphorylase
    • Sanwal, G. G.; Greenberg, E.; Hardie, J.; Cameron, E. C.; Preiss, J. Regulation of starch biosynthesis in plant leaves: activation and inhibition of ADPglucose pyrophosphorylase. Plant Physiol. 1968, 43, 417-427.
    • (1968) Plant Physiol , vol.43 , pp. 417-427
    • Sanwal, G.G.1    Greenberg, E.2    Hardie, J.3    Cameron, E.C.4    Preiss, J.5
  • 35
    • 0033548217 scopus 로고    scopus 로고
    • Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus
    • Mock, H. P.; Heller, W.; Molina, A.; Neubohn, B.; Sandermann, H., Jr.; Grimm, B. Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus. J. Biol. Chem. 1999, 274, 4231-4238.
    • (1999) J. Biol. Chem , vol.274 , pp. 4231-4238
    • Mock, H.P.1    Heller, W.2    Molina, A.3    Neubohn, B.4    Sandermann Jr., H.5    Grimm, B.6
  • 36
    • 31544446625 scopus 로고    scopus 로고
    • The two senescence-related markers, GS1 (cytosolic glutamine synthetase) and GDH (glutamate dehydrogenase), involved in nitrogen mobilization, are differentially regulated during pathogen attack and by stress hormones and reactive oxygen species in Nicotiana tabacum L. leaves
    • Pageau, K.; Reisdorf-Cren, M.; Morot-Gaudry, J. F.; Masclaux-Daubresse, C. The two senescence-related markers, GS1 (cytosolic glutamine synthetase) and GDH (glutamate dehydrogenase), involved in nitrogen mobilization, are differentially regulated during pathogen attack and by stress hormones and reactive oxygen species in Nicotiana tabacum L. leaves. J. Exp. Bot. 2006, 57, 547-557.
    • (2006) J. Exp. Bot , vol.57 , pp. 547-557
    • Pageau, K.1    Reisdorf-Cren, M.2    Morot-Gaudry, J.F.3    Masclaux-Daubresse, C.4
  • 37
    • 2442614109 scopus 로고    scopus 로고
    • The biochemical reaction of maize (Zea mays L.) to salt stress is characterized by a mitigation of symptoms and not by a specific adaptation
    • Zörb, C.; Schmitt, S.; Neeb, A.; Karl, S.; Linder, M.; Schubert, S. The biochemical reaction of maize (Zea mays L.) to salt stress is characterized by a mitigation of symptoms and not by a specific adaptation. Plant Sci. 2004, 167, 91-100.
    • (2004) Plant Sci , vol.167 , pp. 91-100
    • Zörb, C.1    Schmitt, S.2    Neeb, A.3    Karl, S.4    Linder, M.5    Schubert, S.6
  • 38
    • 0030916512 scopus 로고    scopus 로고
    • Cloning and characterisation of glutamine synthetase from Colletotrichum gloeosporioides and demonstration of elevated expression during pathogenesis on Stylosanthes guianensis
    • Stephenson, S. A.; Green, J. R.; Manners, J. M.; Maclean, D. J. Cloning and characterisation of glutamine synthetase from Colletotrichum gloeosporioides and demonstration of elevated expression during pathogenesis on Stylosanthes guianensis. Curr. Genet. 1997, 31, 447-454.
    • (1997) Curr. Genet , vol.31 , pp. 447-454
    • Stephenson, S.A.1    Green, J.R.2    Manners, J.M.3    Maclean, D.J.4
  • 39
    • 33645470420 scopus 로고    scopus 로고
    • Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction
    • Rampitsch, C.; Bykova, N. V.; McCallum, B.; Beimcik, E.; Ens, W. Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction. Proteomics 2006, 6, 1897-1907.
    • (2006) Proteomics , vol.6 , pp. 1897-1907
    • Rampitsch, C.1    Bykova, N.V.2    McCallum, B.3    Beimcik, E.4    Ens, W.5
  • 40
    • 0023644520 scopus 로고
    • Inactivation of pea seed glutamine synthetase by the toxin, tabtoxinine-β- lactam
    • Langston-Unkefer, P. J.; Robinson, A. C.; Knight, T. J.; Durbin, R. D. Inactivation of pea seed glutamine synthetase by the toxin, tabtoxinine-β- lactam. J. Biol. Chem. 1987, 262, 1608-1613.
    • (1987) J. Biol. Chem , vol.262 , pp. 1608-1613
    • Langston-Unkefer, P.J.1    Robinson, A.C.2    Knight, T.J.3    Durbin, R.D.4
  • 41
    • 0033083976 scopus 로고    scopus 로고
    • Complexity and expression of the glutamine synthetase multigene family in the amphidiploid crop Brassica napus
    • Ochs, G.; Schock, G.; Trischler, M.; Kosemund, K.; Wild, A. Complexity and expression of the glutamine synthetase multigene family in the amphidiploid crop Brassica napus. Plant Mol. Biol. 1999, 39, 395-405.
    • (1999) Plant Mol. Biol , vol.39 , pp. 395-405
    • Ochs, G.1    Schock, G.2    Trischler, M.3    Kosemund, K.4    Wild, A.5
  • 42
    • 0024314918 scopus 로고
    • Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
    • Ellis, R. J.; Hemmingsen, S. M. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 1989, 14, 339-342.
    • (1989) Trends Biochem. Sci , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 44
    • 33747838884 scopus 로고    scopus 로고
    • Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function
    • Schultz-Norton, J. R.; McDonald, W. H.; Yates, J. R.; Nardulli, A. M. Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function. Mol. Endocrinol. 2006, 20, 1982-1995.
    • (2006) Mol. Endocrinol , vol.20 , pp. 1982-1995
    • Schultz-Norton, J.R.1    McDonald, W.H.2    Yates, J.R.3    Nardulli, A.M.4
  • 45
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai, A.; Rudd, M. A.; Scribner, A. W.; Loscalzo, J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J. Clin. Invest. 1999, 103, 393-399.
    • (1999) J. Clin. Invest , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4
  • 46
    • 1942474533 scopus 로고    scopus 로고
    • Rapid induction of a protein disulfide isomerase and defense-related genes in wheat in response to the hemibiotrophic fungal pathogen Mycosphaerella graminicola
    • Ray, S.; Anderson, J. M.; Urmeev, F. I.; Goodwin, S. B. Rapid induction of a protein disulfide isomerase and defense-related genes in wheat in response to the hemibiotrophic fungal pathogen Mycosphaerella graminicola. Plant Mol. Biol. 2003, 53, 741-754.
    • (2003) Plant Mol. Biol , vol.53 , pp. 741-754
    • Ray, S.1    Anderson, J.M.2    Urmeev, F.I.3    Goodwin, S.B.4
  • 47
    • 0034809742 scopus 로고    scopus 로고
    • Arabidopsis thaliana type I and II chaperonins
    • Hill, J. E.; Hemmingsen, S. M. Arabidopsis thaliana type I and II chaperonins. Cell Stress Chaperon. 2001, 6, 190-200.
    • (2001) Cell Stress Chaperon , vol.6 , pp. 190-200
    • Hill, J.E.1    Hemmingsen, S.M.2
  • 48
    • 0037401446 scopus 로고    scopus 로고
    • Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: Towards the characterization of "plant defense proteasomes
    • Suty, L.; Lequeu, J.; Lancon, A.; Etienne, P.; Petitot, A. S.; Blein, J. P. Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of "plant defense proteasomes". Int. J. Biochem. Cell Biol. 2003, 35, 637-650.
    • (2003) Int. J. Biochem. Cell Biol , vol.35 , pp. 637-650
    • Suty, L.1    Lequeu, J.2    Lancon, A.3    Etienne, P.4    Petitot, A.S.5    Blein, J.P.6
  • 49
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W.; Walz, J.; Zuhl, F.; Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 1998, 92, 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 50
    • 0031823438 scopus 로고    scopus 로고
    • Tobacco plants perturbed in the ubiquitin-dependent protein degradation system accumulate callose, salicylic acid, and pathogenesis-related protein 1
    • Conrath, U.; Klessig, D. F.; Bachmair, A. Tobacco plants perturbed in the ubiquitin-dependent protein degradation system accumulate callose, salicylic acid, and pathogenesis-related protein 1. Plant Cell Rep. 1998, 17, 876-880.
    • (1998) Plant Cell Rep , vol.17 , pp. 876-880
    • Conrath, U.1    Klessig, D.F.2    Bachmair, A.3
  • 51
    • 0032912334 scopus 로고    scopus 로고
    • Involvement of proteasome-ubiquitin system in wound-signaling in tobacco plants
    • Ito, N.; Seo, S.; Ohtsubo, N.; Nakagawa, H.; Ohashi, Y. Involvement of proteasome-ubiquitin system in wound-signaling in tobacco plants. Plant Cell Physiol. 1999, 40, 355-360.
    • (1999) Plant Cell Physiol , vol.40 , pp. 355-360
    • Ito, N.1    Seo, S.2    Ohtsubo, N.3    Nakagawa, H.4    Ohashi, Y.5
  • 52
    • 0034808429 scopus 로고    scopus 로고
    • Isolation of the first putative peroxidase cDNA from a conifer and the local and systemic accumulation of related proteins upon pathogen infection
    • Fossdal, C. G.; Sharma, P.; Lonneborg, A. Isolation of the first putative peroxidase cDNA from a conifer and the local and systemic accumulation of related proteins upon pathogen infection. Plant Mol. Biol. 2001, 47, 423-435.
    • (2001) Plant Mol. Biol , vol.47 , pp. 423-435
    • Fossdal, C.G.1    Sharma, P.2    Lonneborg, A.3
  • 54
    • 0031128103 scopus 로고    scopus 로고
    • A peroxidase gene promoter induced by phytopathogens and methyl jasmonate in transgenic plants
    • Curtis, M. D.; Rae, A. L.; Rusu, A. G.; Harrison, S. J.; Manners, J. M. A peroxidase gene promoter induced by phytopathogens and methyl jasmonate in transgenic plants. Mol. Plant Microbe. Interact. 1997, 10, 326-338.
    • (1997) Mol. Plant Microbe. Interact , vol.10 , pp. 326-338
    • Curtis, M.D.1    Rae, A.L.2    Rusu, A.G.3    Harrison, S.J.4    Manners, J.M.5
  • 56
    • 0025298551 scopus 로고
    • The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley, P. J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 1990, 269, 1-11.
    • (1990) Biochem. J , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 57
    • 0025787465 scopus 로고
    • Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance
    • Richard, J. P. Kinetic parameters for the elimination reaction catalyzed by triosephosphate isomerase and an estimation of the reaction's physiological significance. Biochemistry 1991, 30, 4581-4585.
    • (1991) Biochemistry , vol.30 , pp. 4581-4585
    • Richard, J.P.1
  • 58
    • 0035876322 scopus 로고    scopus 로고
    • In situ kinetic analysis of glyoxalase I and glyoxalase II in Saccharomyces cerevisiae
    • Martins, A. M. T. B. S.; Cordeiro, C. A. A.; Freire, A. M. J. P. In situ kinetic analysis of glyoxalase I and glyoxalase II in Saccharomyces cerevisiae. FEBS Lett. 2001, 499, 41-44.
    • (2001) FEBS Lett , vol.499 , pp. 41-44
    • Martins, A.M.T.B.S.1    Cordeiro, C.A.A.2    Freire, A.M.J.P.3
  • 60
    • 4344630443 scopus 로고    scopus 로고
    • Identification of a maize kernel stress-related protein and its effects on aflatoxin accumulation
    • Chen, Z. Y.; Brown, R. L.; Damann, K. E.; Cleveland, T. E. Identification of a maize kernel stress-related protein and its effects on aflatoxin accumulation. Phytopathology 2004, 94, 938-945.
    • (2004) Phytopathology , vol.94 , pp. 938-945
    • Chen, Z.Y.1    Brown, R.L.2    Damann, K.E.3    Cleveland, T.E.4
  • 61
    • 41049106186 scopus 로고    scopus 로고
    • Enhancing salt tolerance in a crop plant by overexpression of glyoxalase II
    • DOI 10.1007/s11248-007-9082-2
    • Singla-Pareek, S. L.; Yadav, S. K.; Pareek, A.; Reddy, M. K.; Sopory, S. K. Enhancing salt tolerance in a crop plant by overexpression of glyoxalase II. Transgenic Res. 2007,DOI 10.1007/s11248-007-9082-2.
    • (2007) Transgenic Res
    • Singla-Pareek, S.L.1    Yadav, S.K.2    Pareek, A.3    Reddy, M.K.4    Sopory, S.K.5
  • 62
    • 0033082685 scopus 로고    scopus 로고
    • Glyoxalase I from Brassica juncea: Molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress
    • Veena; Reddy, V. S.; Sopory, S. K. Glyoxalase I from Brassica juncea: molecular cloning, regulation and its over-expression confer tolerance in transgenic tobacco under stress. Plant J. 1999, 17, 385-395.
    • (1999) Plant J , vol.17 , pp. 385-395
    • Veena1    Reddy, V.S.2    Sopory, S.K.3
  • 63
    • 0032129686 scopus 로고    scopus 로고
    • Dong, X. SA, JA, ethylene, and disease resistance in plants. Curr. Opin. Plant Biol. 1998, 1, 316-323.
    • Dong, X. SA, JA, ethylene, and disease resistance in plants. Curr. Opin. Plant Biol. 1998, 1, 316-323.
  • 64
    • 0032490943 scopus 로고    scopus 로고
    • Nitric oxide functions as a signal in plant disease resistance
    • Delledonne, M.; Xia, Y.; Dixon, R. A.; Lamb, C. Nitric oxide functions as a signal in plant disease resistance. Nature 1998, 394, 585-588.
    • (1998) Nature , vol.394 , pp. 585-588
    • Delledonne, M.1    Xia, Y.2    Dixon, R.A.3    Lamb, C.4
  • 65
    • 33645240777 scopus 로고    scopus 로고
    • Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation
    • Lindermayr, C.; Saalbach, G.; Bahnweg, G.; Durner, J. Differential inhibition of Arabidopsis methionine adenosyltransferases by protein S-nitrosylation. J. Biol. Chem. 2006, 281, 4285-4291.
    • (2006) J. Biol. Chem , vol.281 , pp. 4285-4291
    • Lindermayr, C.1    Saalbach, G.2    Bahnweg, G.3    Durner, J.4
  • 66
    • 33745601651 scopus 로고    scopus 로고
    • S-Nitrosylation: An emerging redox-based post-translational modification in plants
    • Wang, Y.; Yun, B. W.; Kwon, E.; Hong, J. K.; Yoon, J.; Loake, G. J. S-Nitrosylation: an emerging redox-based post-translational modification in plants. J. Exp. Bot. 2006, 57, 1777-1784.
    • (2006) J. Exp. Bot , vol.57 , pp. 1777-1784
    • Wang, Y.1    Yun, B.W.2    Kwon, E.3    Hong, J.K.4    Yoon, J.5    Loake, G.J.6
  • 69
    • 34250855797 scopus 로고    scopus 로고
    • Transcriptional profiling of canola (Brassica napus L.) responses to the fungal pathogen Sclerotinia sclerotiorum
    • Yang, B.; Srivastava, S.; Deyholos, M. K.; Kav, N. N. V. Transcriptional profiling of canola (Brassica napus L.) responses to the fungal pathogen Sclerotinia sclerotiorum. Plant Sci. 2007, 173, 156-171.
    • (2007) Plant Sci , vol.173 , pp. 156-171
    • Yang, B.1    Srivastava, S.2    Deyholos, M.K.3    Kav, N.N.V.4
  • 70
    • 0141920354 scopus 로고    scopus 로고
    • Comparing protein abundance and mRNA expression levels on a genomic scale
    • Greenbaum, D.; Colangelo, C.; Williams, K.; Gerstein, M. Comparing protein abundance and mRNA expression levels on a genomic scale. Genome Biol. 2003, 4, 117124.
    • (2003) Genome Biol , vol.4 , pp. 117124
    • Greenbaum, D.1    Colangelo, C.2    Williams, K.3    Gerstein, M.4


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