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Volumn 11, Issue 7, 2011, Pages 1346-1350

Redox-regulatory mechanisms induced by oxidative stress in Brassica juncea roots monitored by 2-DE proteomics

Author keywords

2 DE; Buthionine sulfoximine; Hydrogen peroxide; Oxidative stress; Plant proteomics

Indexed keywords

BUTHIONINE SULFOXIMINE; GLUTATHIONE; HYDROGEN PEROXIDE;

EID: 79953058655     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000450     Document Type: Article
Times cited : (13)

References (20)
  • 2
    • 0021284165 scopus 로고
    • Redox control of enzyme activities by thiol/disulfide exchange
    • Gilbert, H. F., Redox control of enzyme activities by thiol/disulfide exchange. Meth. Enzym. 1984, 107, 330-351.
    • (1984) Meth. Enzym. , vol.107 , pp. 330-351
    • Gilbert, H.F.1
  • 3
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler, D. M., Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu. Rev. Biochem. 1985, 54, 305-329.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 305-329
    • Ziegler, D.M.1
  • 4
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocystein sulfoxime)
    • Griffith, O. W., Meister, A., Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocystein sulfoxime). J. Biol. Chem. 1979, 254, 7558-7560.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 5
    • 35348880995 scopus 로고    scopus 로고
    • Thiol-based regulation of redox-active glutamate-cysteine ligase from Arabidopsis thaliana
    • Hicks, L. M., Cahoon, R. E., Bonner, E. R., Rivard, R. S. et al., Thiol-based regulation of redox-active glutamate-cysteine ligase from Arabidopsis thaliana. Plant Cell 2007, 19, 2653-2661.
    • (2007) Plant Cell , vol.19 , pp. 2653-2661
    • Hicks, L.M.1    Cahoon, R.E.2    Bonner, E.R.3    Rivard, R.S.4
  • 6
    • 66149160358 scopus 로고    scopus 로고
    • Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches
    • Alvarez, S., Berla, B. M., Sheffield, J., Cahoon, R. E. et al., Comprehensive analysis of the Brassica juncea root proteome in response to cadmium exposure by complementary proteomic approaches. Proteomics 2009, 9, 2419-2431.
    • (2009) Proteomics , vol.9 , pp. 2419-2431
    • Alvarez, S.1    Berla, B.M.2    Sheffield, J.3    Cahoon, R.E.4
  • 7
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain, M. A., Asada, K., Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant Cell Physiol. 1984, 25, 85-92.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 8
    • 5144234728 scopus 로고    scopus 로고
    • A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase
    • Gelhaye, E., Rouhier, N., Gerard, J., Jolivet, Y. et al., A specific form of thioredoxin h occurs in plant mitochondria and regulates the alternative oxidase. Proc. Natl. Acad. Sci. USA 2004, 101, 14545-14550.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14545-14550
    • Gelhaye, E.1    Rouhier, N.2    Gerard, J.3    Jolivet, Y.4
  • 9
    • 33846368170 scopus 로고    scopus 로고
    • PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances
    • Traverso, J. A., Vignols, F., Cazalis, R., Pulido, A. et al., PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances. Plant Physiol. 2007, 143, 300-311.
    • (2007) Plant Physiol. , vol.143 , pp. 300-311
    • Traverso, J.A.1    Vignols, F.2    Cazalis, R.3    Pulido, A.4
  • 10
    • 0043199342 scopus 로고    scopus 로고
    • The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione
    • Ito, H., Iwabuchi, M., Ogawa, K., The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione. Plant Cell Physiol. 2003, 44, 655-660.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 655-660
    • Ito, H.1    Iwabuchi, M.2    Ogawa, K.3
  • 11
    • 0037628370 scopus 로고    scopus 로고
    • Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics
    • Wong, J. H., Balmer, Y., Cai, N., Tanaka, C. K. et al., Unraveling thioredoxin-linked metabolic processes of cereal starchy endosperm using proteomics. FEBS Lett. 2003, 547, 151-156.
    • (2003) FEBS Lett. , vol.547 , pp. 151-156
    • Wong, J.H.1    Balmer, Y.2    Cai, N.3    Tanaka, C.K.4
  • 12
    • 34447130271 scopus 로고    scopus 로고
    • Thioredoxin-linked proteins are reduced during germination of Medicago truncatula seeds
    • Alkhalfioui, F., Renard, M., Vensel, W. H., Wong, J. et al., Thioredoxin-linked proteins are reduced during germination of Medicago truncatula seeds. Plant Physiol. 2007, 144, 1559-1579.
    • (2007) Plant Physiol. , vol.144 , pp. 1559-1579
    • Alkhalfioui, F.1    Renard, M.2    Vensel, W.H.3    Wong, J.4
  • 13
    • 57549086038 scopus 로고    scopus 로고
    • Determination of in vivo disulfide-bonded proteins in Arabidopsis
    • Alvarez, S., Wilson, G. H., Chen, S., Determination of in vivo disulfide-bonded proteins in Arabidopsis. J. Chromatogr. B 2009, 877, 101-104.
    • (2009) J. Chromatogr. B , vol.877 , pp. 101-104
    • Alvarez, S.1    Wilson, G.H.2    Chen, S.3
  • 14
    • 70349983351 scopus 로고    scopus 로고
    • Proteomics of Arabidopsis redox proteins in response to methyl jasmonate
    • Alvarez, S., Zhu, M., Chen, S., Proteomics of Arabidopsis redox proteins in response to methyl jasmonate. J. Proteomics 2009, 73, 30-40.
    • (2009) J. Proteomics , vol.73 , pp. 30-40
    • Alvarez, S.1    Zhu, M.2    Chen, S.3
  • 15
    • 10744230621 scopus 로고    scopus 로고
    • Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria
    • Balmer, Y., Vensel, W. H., Tanaka, C. K., Hurkman, W. J. et al., Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proc. Natl. Acad. Sci. USA 2004, 101, 2642-2647.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2642-2647
    • Balmer, Y.1    Vensel, W.H.2    Tanaka, C.K.3    Hurkman, W.J.4
  • 16
    • 33644682396 scopus 로고    scopus 로고
    • Stress-induced protein S-glutathionylation in Arabidopsis
    • Dixon, D. P., Skipsey, M., Grundy, N. M., Edwards, R., Stress-induced protein S-glutathionylation in Arabidopsis. Plant Physiol. 2005, 138, 2233-2244.
    • (2005) Plant Physiol. , vol.138 , pp. 2233-2244
    • Dixon, D.P.1    Skipsey, M.2    Grundy, N.M.3    Edwards, R.4
  • 17
    • 0034969736 scopus 로고    scopus 로고
    • The Arabidopsis 14-3-3 family of signaling regulators
    • DeLille, J. M., Sehnke, P. C., Ferl, R. J., The Arabidopsis 14-3-3 family of signaling regulators. Plant Physiol. 2001, 126, 35-38.
    • (2001) Plant Physiol. , vol.126 , pp. 35-38
    • DeLille, J.M.1    Sehnke, P.C.2    Ferl, R.J.3
  • 18
    • 33845911220 scopus 로고    scopus 로고
    • Brassinosteroid confers tolerance in Arabidopsis thaliana and Brassica napus to a range of abiotic stresses
    • Kagale, S., Divi, U. K., Krochko, J. E., Keller, W. A., Krishna, P., Brassinosteroid confers tolerance in Arabidopsis thaliana and Brassica napus to a range of abiotic stresses. Planta 2007, 225, 353-364.
    • (2007) Planta , vol.225 , pp. 353-364
    • Kagale, S.1    Divi, U.K.2    Krochko, J.E.3    Keller, W.A.4    Krishna, P.5
  • 19
    • 0242500944 scopus 로고    scopus 로고
    • Brassinosteroid functions in a broad range of disease resistance in tobacco and rice
    • Nakashita, H., Yasuda, M., Nitta, T., Asami, T. et al., Brassinosteroid functions in a broad range of disease resistance in tobacco and rice. Plant J. 2003, 33, 887-898.
    • (2003) Plant J. , vol.33 , pp. 887-898
    • Nakashita, H.1    Yasuda, M.2    Nitta, T.3    Asami, T.4
  • 20
    • 66649105761 scopus 로고    scopus 로고
    • Reactive oxygen species are involved in brassinosteroid-induced stress tolerance in cucumber
    • Xia, X. J., Wang, Y. J., Zhou, Y. H., Tao, Y. et al., Reactive oxygen species are involved in brassinosteroid-induced stress tolerance in cucumber. Plant Physiol. 2009, 150, 801-814.
    • (2009) Plant Physiol. , vol.150 , pp. 801-814
    • Xia, X.J.1    Wang, Y.J.2    Zhou, Y.H.3    Tao, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.