메뉴 건너뛰기




Volumn 138, Issue 4, 2005, Pages 2233-2244

Stress-induced protein S-glutathionylation in arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; MIXTURES; OXIDATION; PROTEINS;

EID: 33644682396     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.058917     Document Type: Article
Times cited : (261)

References (40)
  • 3
    • 0036745407 scopus 로고    scopus 로고
    • Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis
    • Baty JW, Hampton MB, Winterbourn CC (2002) Detection of oxidant sensitive thiol proteins by fluorescence labeling and two-dimensional electrophoresis. Proteomics 2: 1261-1266
    • (2002) Proteomics , vol.2 , pp. 1261-1266
    • Baty, J.W.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 4
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan BB, Balmer Y (2005) Redox regulation: a broadening horizon. Annu Rev Plant Biol 56: 187-220
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 5
    • 0042974241 scopus 로고    scopus 로고
    • Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite
    • Carballal S, Radi R, Kirk MC, Barnes S, Freeman BA, Alvarez B (2003) Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry 42: 9906-9914
    • (2003) Biochemistry , vol.42 , pp. 9906-9914
    • Carballal, S.1    Radi, R.2    Kirk, M.C.3    Barnes, S.4    Freeman, B.A.5    Alvarez, B.6
  • 7
    • 0029845410 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding IMP dehydrogenase from Arabidopsis thaliana
    • Collart FR, Osipiuk J, Trent J, Olsen GJ, Huberman E (1996) Cloning and characterization of the gene encoding IMP dehydrogenase from Arabidopsis thaliana. Gene 174: 217-220
    • (1996) Gene , vol.174 , pp. 217-220
    • Collart, F.R.1    Osipiuk, J.2    Trent, J.3    Olsen, G.J.4    Huberman, E.5
  • 8
    • 0030817825 scopus 로고    scopus 로고
    • Glutathione transferases in herbicide-resistant and herbicide-susceptible black grass (Alopecurus myosuroides)
    • Cummins I, Moss S, Cole DJ, Edwards R (1997) Glutathione transferases in herbicide-resistant and herbicide-susceptible black grass (Alopecurus myosuroides). Pestic Sci 51: 244-250
    • (1997) Pestic Sci , vol.51 , pp. 244-250
    • Cummins, I.1    Moss, S.2    Cole, D.J.3    Edwards, R.4
  • 9
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi M, Shringarpure R, Davies KJA (2001) Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch Biochem Biophys 389: 254-263
    • (2001) Arch Biochem Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.A.3
  • 10
    • 0037414784 scopus 로고    scopus 로고
    • 20S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated
    • Demasi M, Silva GM, Netto LES (2003) 20S proteasome from Saccharomyces cerevisiae is responsive to redox modifications and is S-glutathionylated. J Biol Chem 278: 679-685
    • (2003) J Biol Chem , vol.278 , pp. 679-685
    • Demasi, M.1    Silva, G.M.2    Netto, L.E.S.3
  • 12
    • 0034672089 scopus 로고    scopus 로고
    • Characterisation of a zeta class glutathione transferase from Arabidopsis thaliana with a putative role in tyrosine catabolism
    • Dixon DP, Cole DJ, Edwards R (2000) Characterisation of a zeta class glutathione transferase from Arabidopsis thaliana with a putative role in tyrosine catabolism. Arch Biochem Biophys 384: 407-412
    • (2000) Arch Biochem Biophys , vol.384 , pp. 407-412
    • Dixon, D.P.1    Cole, D.J.2    Edwards, R.3
  • 13
    • 0037163126 scopus 로고    scopus 로고
    • Functional divergence in the glutathione transferase superfamily in plants: Identification of two dasses with putative functions in redox homeostasis in Arabidopsis thaliana
    • Dixon DP, Davis BG, Edwards R (2002) Functional divergence in the glutathione transferase superfamily in plants: identification of two dasses with putative functions in redox homeostasis in Arabidopsis thaliana. J Biol Chem 277: 30859-30869
    • (2002) J Biol Chem , vol.277 , pp. 30859-30869
    • Dixon, D.P.1    Davis, B.G.2    Edwards, R.3
  • 14
    • 7244220083 scopus 로고    scopus 로고
    • Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate
    • Ferrer J-L, Ravanel S, Robert M, Dumas R (2004) Crystal structures of cobalamin-independent methionine synthase complexed with zinc, homocysteine, and methyltetrahydrofolate. J Biol Chem 279: 44235-44238
    • (2004) J Biol Chem , vol.279 , pp. 44235-44238
    • Ferrer, J.-L.1    Ravanel, S.2    Robert, M.3    Dumas, R.4
  • 16
    • 33646146488 scopus 로고    scopus 로고
    • Redox proteomics: Identification and functional role of glutathionylated proteins
    • Fratelli M, Gianazza E, Ghezzi P (2004) Redox proteomics: identification and functional role of glutathionylated proteins. Expert Rev Proteomics 1: 365-376
    • (2004) Expert Rev Proteomics , vol.1 , pp. 365-376
    • Fratelli, M.1    Gianazza, E.2    Ghezzi, P.3
  • 18
    • 14044271464 scopus 로고    scopus 로고
    • Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli
    • Hondorp ER, Matthews RG (2004) oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli. PLoS Biol 2: 1738-1753
    • (2004) PLoS Biol , vol.2 , pp. 1738-1753
    • Hondorp, E.R.1    Matthews, R.G.2
  • 19
    • 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 (2003) The sugar-metabolic enzymes aldolase and triose-phosphate isomerase are targets of glutathionylation in Arabidopsis thaliana: detection using biotinylated glutathione. Plant Cell Physiol 44: 655-660
    • (2003) Plant Cell Physiol , vol.44 , pp. 655-660
    • Ito, H.1    Iwabuchi, M.2    Ogawa, K.3
  • 20
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S (2000) Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267: 4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 21
    • 0032187235 scopus 로고    scopus 로고
    • Superoxide dismutase in Arabidopsis: An eclectic enzyme family with disparate regulation and protein localization
    • Kliebenstein DJ, Monde R-A, Last RL (1998) Superoxide dismutase in Arabidopsis: an eclectic enzyme family with disparate regulation and protein localization. Plant Physiol 118: 637-650
    • (1998) Plant Physiol , vol.118 , pp. 637-650
    • Kliebenstein, D.J.1    Monde, R.-A.2    Last, R.L.3
  • 22
    • 0031105944 scopus 로고    scopus 로고
    • Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: Cloning, expression and phylogenetic relationships
    • Lacombe E, Hawkins S, Van Doorsselaere J, Piquemal J, Goffner D, Poeydomenge O, Boudet A-M, Grima-Pettenati J (1997) Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: cloning, expression and phylogenetic relationships. Plant J 11: 429-441
    • (1997) Plant J , vol.11 , pp. 429-441
    • Lacombe, E.1    Hawkins, S.2    Van Doorsselaere, J.3    Piquemal, J.4    Goffner, D.5    Poeydomenge, O.6    Boudet, A.-M.7    Grima-Pettenati, J.8
  • 24
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert LI, Jakob U (2004) Protein thiol modifications visualized in vivo. PLoS Biol 2: 1723-1737
    • (2004) PLoS Biol , vol.2 , pp. 1723-1737
    • Leichert, L.I.1    Jakob, U.2
  • 25
    • 0032543374 scopus 로고    scopus 로고
    • Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin
    • Lind C, Gerdes R, Schuppe-Koistinen I, Cotgreave IA (1998) Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: catalysis by glutaredoxin. Biochem Biophys Res Commun 247: 431-436
    • (1998) Biochem Biophys Res Commun , vol.247 , pp. 431-436
    • Lind, C.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Cotgreave, I.A.4
  • 26
    • 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
    • (2005) Plant Physiol , vol.137 , pp. 921-930
    • Lindermayr, C.1    Saalbach, G.2    Durner, J.3
  • 27
    • 0037517067 scopus 로고    scopus 로고
    • Isolation of a glucosyltransferase from Arabidopsis thaliana active in the metabolism of the persistent pollutant 3,4-dichluroaniline
    • Loutre C, Dixon DP, Brazier M, Slater M, Cole DJ, Edwards R (2003) Isolation of a glucosyltransferase from Arabidopsis thaliana active in the metabolism of the persistent pollutant 3,4-dichluroaniline. Plant J 34: 435-493
    • (2003) Plant J , vol.34 , pp. 435-493
    • Loutre, C.1    Dixon, D.P.2    Brazier, M.3    Slater, M.4    Cole, D.J.5    Edwards, R.6
  • 29
    • 0027143463 scopus 로고
    • Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension cultures
    • May MJ, Leaver CJ (1993) Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension cultures. Plant Physiol 103: 621-627
    • (1993) Plant Physiol , vol.103 , pp. 621-627
    • May, M.J.1    Leaver, C.J.2
  • 30
    • 0035949574 scopus 로고    scopus 로고
    • Comprehensive survey of proteins targeted by chloroplast thioredoxin
    • Motohashi K, Kondoh A, Stumpp MT, Hisabori T (2001) Comprehensive survey of proteins targeted by chloroplast thioredoxin. Proc Natl Acad Sci USA 98: 11224-11229
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11224-11229
    • Motohashi, K.1    Kondoh, A.2    Stumpp, M.T.3    Hisabori, T.4
  • 31
    • 0035114118 scopus 로고    scopus 로고
    • The nitrilase superfamily: Classification, structure and function
    • REVIEWS0001
    • Pace HC, Brenner C (2001) The nitrilase superfamily: classification, structure and function. Genome Biol 2: REVIEWS0001
    • (2001) Genome Biol , vol.2
    • Pace, H.C.1    Brenner, C.2
  • 32
    • 0030699351 scopus 로고    scopus 로고
    • The 20S proteasome gene family in Arabidopsis thaliana
    • Parmentier Y, Bouchez D, Fleck J, Genschlik P (1997) The 20S proteasome gene family in Arabidopsis thaliana. FEBS Lett 416: 281-285
    • (1997) FEBS Lett , vol.416 , pp. 281-285
    • Parmentier, Y.1    Bouchez, D.2    Fleck, J.3    Genschlik, P.4
  • 33
    • 0032533445 scopus 로고    scopus 로고
    • Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase: Explanations for the selectivity of the enzyme in plants
    • Prade L, Huber R, Bieseler B (1998) Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase: explanations for the selectivity of the enzyme in plants. Structure 6: 1445-1452
    • (1998) Structure , vol.6 , pp. 1445-1452
    • Prade, L.1    Huber, R.2    Bieseler, B.3
  • 34
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 35
    • 0042261992 scopus 로고    scopus 로고
    • Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae
    • Shenton D, Grant CM (2003) Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 374: 513-519
    • (2003) Biochem J , vol.374 , pp. 513-519
    • Shenton, D.1    Grant, C.M.2
  • 36
    • 0037018936 scopus 로고    scopus 로고
    • Structure of a tau dass glutathione S-transferase from wheat active in herbicide detoxification
    • Thom R, Cummins I, Dixon DP, Edwards R, Cole DJ, Lapthorn AJ (2002) Structure of a tau dass glutathione S-transferase from wheat active in herbicide detoxification. Biochemistry 41: 7008-7020
    • (2002) Biochemistry , vol.41 , pp. 7008-7020
    • Thom, R.1    Cummins, I.2    Dixon, D.P.3    Edwards, R.4    Cole, D.J.5    Lapthorn, A.J.6
  • 37
    • 0003143549 scopus 로고    scopus 로고
    • Structure determination of zeta dass glutathione transferase from Arobidopsis thaliana
    • Thom R, Dixon D, Edwards R, Cole D, Lapthorn A (2001) Structure determination of zeta dass glutathione transferase from Arobidopsis thaliana. Chem Biol Interact 133: 53-54
    • (2001) Chem Biol Interact , vol.133 , pp. 53-54
    • Thom, R.1    Dixon, D.2    Edwards, R.3    Cole, D.4    Lapthorn, A.5
  • 38
    • 0037127295 scopus 로고    scopus 로고
    • Thiol oxidase activity of copper, zinc superoxide dismutase
    • Winterbourn CC, Peskin AV, Parsons-Mair HN (2002) Thiol oxidase activity of copper, zinc superoxide dismutase. J Biol Chem 277: 1906-1911
    • (2002) J Biol Chem , vol.277 , pp. 1906-1911
    • Winterbourn, C.C.1    Peskin, A.V.2    Parsons-Mair, H.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.