메뉴 건너뛰기




Volumn 4, Issue 2, 2009, Pages 142-153

Hydrogen peroxide-induced response in E. coli and S. cerevisiae: Different stages of the flow of the genetic information

Author keywords

E. coli; Enzyme activity; Hydrogen peroxide; mRNA level; Protein synthesis; S. cerevisiae

Indexed keywords

ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA; SACCHAROMYCES CEREVISIAE;

EID: 67349187753     PISSN: 1895104X     EISSN: 16443632     Source Type: Journal    
DOI: 10.2478/s11535-009-0005-5     Document Type: Article
Times cited : (26)

References (92)
  • 1
    • 0026335852 scopus 로고
    • Regulation of bacterial oxidative stress genes
    • B. Demple 1991 Regulation of bacterial oxidative stress genes Annu. Rev. Genet. 25 315 337 (Pubitemid 21903724)
    • (1991) Annual Review of Genetics , vol.25 , Issue.1 , pp. 315-337
    • Demple, B.1
  • 2
    • 0035773684 scopus 로고    scopus 로고
    • Oxidative stress and mechanisms of protection against it in bacteria
    • V.I. Lushchak 2001 Oxidative stress and mechanisms of protection against it in bacteria Biochemistry (Mosc.) 66 592 609 (Pubitemid 35207961)
    • (2001) Biokhimiya , vol.66 , Issue.5 , pp. 592-609
    • Lushchak, V.I.1
  • 3
    • 0036728274 scopus 로고    scopus 로고
    • The genomics of yeast responses to environmental stress and starvation
    • DOI 10.1007/s10142-002-0058-2
    • A.P. Gasch M. Werner-Washburne 2002 The genomic of yeast responses to environmental stress and starvation Funct. Integ. Genomics 2 181 192 (Pubitemid 41449152)
    • (2002) Functional and Integrative Genomics , vol.2 , Issue.4-5 , pp. 181-192
    • Gasch, A.P.1    Werner-Washburne, M.2
  • 4
    • 34250011458 scopus 로고    scopus 로고
    • Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast
    • DOI 10.1016/j.freeradbiomed.2007.04.007, PII S0891584907002560
    • M. Molin J.P. Renault G. Lagniel S. Pin M. Toledano J. Labarre 2007 Ionizing radiation induces a Yap1-dependent peroxide stress response in yeast Free Radic. Biol. Med. 43 136 144 (Pubitemid 46881218)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.1 , pp. 136-144
    • Molin, M.1    Renault, J.-P.2    Lagniel, G.3    Pin, S.4    Toledano, M.5    Labarre, J.6
  • 5
    • 0031025115 scopus 로고    scopus 로고
    • Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli
    • B. Gonzalez-Flecha B. Demple 1997 Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli J. Bacteriol. 179 382 388 (Pubitemid 27030390)
    • (1997) Journal of Bacteriology , vol.179 , Issue.2 , pp. 382-388
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 6
    • 1342325429 scopus 로고    scopus 로고
    • Decrease of H2O2 plasma membrane permeability during adaptation to H2O2 in Saccharomyces cerevisiae
    • M.R. Branco H.S. Marinho L. Cyrne F. Antunes 2004 Decrease of H2O2 plasma membrane permeability during adaptation to H2O2 in Saccharomyces cerevisiae J. Biol. Chem. 279 6501 6506
    • (2004) J. Biol. Chem. , vol.279 , pp. 6501-6506
    • Branco, M.R.1    Marinho, H.S.2    Cyrne, L.3    Antunes, F.4
  • 8
    • 0035985625 scopus 로고    scopus 로고
    • Global adjustment of microbial physiology during free radical stress
    • DOI 10.1016/S0065-2911(02)46007-9
    • P.J. Pomposiello B. Demple 2002 Global adjustment of microbial physiology during free radical stress Adv. Microb. Physiol. 46 319 341 (Pubitemid 34602245)
    • (2002) Advances in Microbial Physiology , vol.46 , pp. 319-341
    • Pomposiello, P.J.1    Demple, B.2
  • 10
    • 0033673079 scopus 로고    scopus 로고
    • Sensing and protecting against superoxide stress in Escherichia coli - How many ways are there to trigger soxRS response?
    • D. Touati 2000 Sensing and protecting against superoxide stress in Escherichia coli - how many ways are there to trigger soxRS response? Redox Rep. 5 287 293
    • (2000) Redox Rep. , vol.5 , pp. 287-293
    • Touati, D.1
  • 11
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • DOI 10.1128/JB.183.13.3890-3902.2001
    • P.J. Pomposiello M.H. Bennik B. Demple 2001 Genomewide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate J. Bacteriol. 183 3890 3902 (Pubitemid 32565468)
    • (2001) Journal of Bacteriology , vol.183 , Issue.13 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.J.2    Demple, B.3
  • 12
    • 43149105201 scopus 로고    scopus 로고
    • Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and independent transcriptional networks
    • J.L. Blanchard W.Y. Wholey E.M. Conlon P.J. Pomposiello 2007 Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and independent transcriptional networks PLoS ONE 2 e1186
    • (2007) PLoS ONE , vol.2 , pp. 1186
    • Blanchard, J.L.1    Wholey, W.Y.2    Conlon, E.M.3    Pomposiello, P.J.4
  • 14
    • 0034020742 scopus 로고    scopus 로고
    • Flavodoxin mutants of Escherichia coli K-12
    • DOI 10.1128/JB.182.7.1788-1793.2000
    • P. Gaudu B. Weiss 2000 Flavodoxin mutants of Escherichia coli K-12 J. Bacteriol. 182 1788 1793 (Pubitemid 30165363)
    • (2000) Journal of Bacteriology , vol.182 , Issue.7 , pp. 1788-1793
    • Gaudu, P.1    Weiss, B.2
  • 15
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • M. Zheng G. Storz 2000 Redox sensing by prokaryotic transcription factors Biochem. Pharmacol. 59 1 6
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 16
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers SoxR transcription activator
    • DOI 10.1073/pnas.97.10.5146
    • H. Ding B. Demple 2000 Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator Proc. Natl. Acad. Sci. USA 97 5146 5150 (Pubitemid 30313686)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.10 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 17
    • 0034461245 scopus 로고    scopus 로고
    • Hydrogen peroxide activates the SoxRS regulon in vivo
    • DOI 10.1128/JB.182.23.6842-6844.2000
    • M. Manchado K. Micha C. Pueyo 2000 Hydrogen peroxide activates the soxRS regulon in vivo J. Bacteriol. 182 6842 6844 (Pubitemid 32249272)
    • (2000) Journal of Bacteriology , vol.182 , Issue.23 , pp. 6842-6844
    • Manchado, M.1    Michan, C.2    Pueyo, C.3
  • 18
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • DOI 10.1128/JB.183.15.4562-4570.2001
    • M. Zheng X. Wang L.J. Templeton D.R. Smulski R.A. LaRossa G. Storz 2001 DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide J. Bacteriol. 183 4562 4570 (Pubitemid 32646006)
    • (2001) Journal of Bacteriology , vol.183 , Issue.15 , pp. 4562-4570
    • Zheng, M.1    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6
  • 19
    • 27844581259 scopus 로고    scopus 로고
    • Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli
    • DOI 10.1016/j.cellbi.2005.08.002, PII S1065699505001915
    • H.M. Semchyshyn T.V. Bagnyukova K.B. Storey V.I. Lushchak 2005 Hydrogen peroxide increases the activities of soxRS regulon enzymes and the levels of oxidized proteins and lipids in Escherichia coli Cell Biol. Int. 29 898 902 (Pubitemid 41654793)
    • (2005) Cell Biology International , vol.29 , Issue.11 , pp. 898-902
    • Semchyshyn, H.1    Bagnyukova, T.2    Storey, K.3    Lushchak, V.4
  • 20
    • 29144465668 scopus 로고    scopus 로고
    • Involvement of soxRS regulon in response of Escherichia coli to oxidative stress induced by hydrogen peroxide
    • H.M. Semchyshyn T.V. Bagnyukova V.I. Lushchak 2005 Involvement of soxRS regulon in response of Escherichia coli to oxidative stress induced by hydrogen peroxide Biochemistry (Mosc.) 70 1238 1244
    • (2005) Biochemistry (Mosc.) , vol.70 , pp. 1238-1244
    • Semchyshyn, H.M.1    Bagnyukova, T.V.2    Lushchak, V.I.3
  • 21
    • 0142211218 scopus 로고    scopus 로고
    • Effects of Hydrogen Peroxide upon Nicotinamide Nucleotide Metabolism in Escherichia coli: Changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III)
    • DOI 10.1074/jbc.M306251200
    • J.L. Brumaghim Y. Li E. Henle S. Linn 2003 Effects of hydrogen peroxide upon nicotinamide nucleotide metabolism in Escherichia coli: changes in enzyme levels and nicotinamide nucleotide pools and studies of the oxidation of NAD(P)H by Fe(III) J. Biol. Chem. 278 42495 42504 (Pubitemid 37310522)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42495-42504
    • Brumaghim, J.L.1    Li, Y.2    Henle, E.3    Linn, S.4
  • 22
    • 14044259281 scopus 로고    scopus 로고
    • Exploiting thiol modifications
    • DOI 10.1371/journal.pbio.0020400
    • P.J. Kiley G. Storz 2004 Exploiting thiol modifications PLoS Biol. 2 1714 1717 (Pubitemid 40280470)
    • (2004) PLoS Biology , vol.2 , Issue.11
    • Kiley, P.J.1    Storz, G.2
  • 23
    • 39949084153 scopus 로고    scopus 로고
    • Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor
    • C.H. Ng S.X. Tan G.G. Perrone G.W. Thorpe V.J. Higgins I.W. Dawes 2008 Adaptation to hydrogen peroxide in Saccharomyces cerevisiae: The role of NADPH-generating systems and the SKN7 transcription factor Free Radic. Biol. Med. 44 1131 1145
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1131-1145
    • Ng, C.H.1    Tan, S.X.2    Perrone, G.G.3    Thorpe, G.W.4    Higgins, V.J.5    Dawes, I.W.6
  • 24
    • 0034008694 scopus 로고    scopus 로고
    • Activation of SoxR by overproduction of desulfoferrodoxin: Multiple ways to induce the soxRS regulon
    • DOI 10.1128/JB.182.6.1761-1763.2000
    • P. Gaudu S. Dubrac D. Touati 2000 Activation of SoxR by overproduction of desulfoferredoxin: multiple ways to induce the soxRS regulon J. Bacteriol. 182 1761 1763 (Pubitemid 30121144)
    • (2000) Journal of Bacteriology , vol.182 , Issue.6 , pp. 1761-1763
    • Gaudu, P.1    Dubrac, S.2    Touati, D.3
  • 25
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • DOI 10.1126/science.279.5357.1718
    • M. Zheng F. Aslund G. Storz 1998 Activation of the OxyR transcription factor by reversible disulfide bond formation Science 279 1718 1721 (Pubitemid 28164467)
    • (1998) Science , vol.279 , Issue.5357 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 26
    • 34447518686 scopus 로고    scopus 로고
    • The system biology of thiol redox system in Escherichia coli and yeast: Differential functions in oxidative stress, iron metabolism and DNA synthesis
    • DOI 10.1016/j.febslet.2007.07.002, PII S0014579307007557, Cellular Stress
    • M.B. Toledano C. Kumar N. Le Moan D. Spector F. Tacnet 2007 The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis FEBS Lett. 581 3598 3607 (Pubitemid 47081012)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3598-3607
    • Toledano, M.B.1    Kumar, C.2    Le Moan, N.3    Spector, D.4    Tacnet, F.5
  • 28
    • 0000291637 scopus 로고    scopus 로고
    • The general stress response in Escherichia coli
    • ASM Press Washington, D.C.
    • Hengge-Aronis R., The general stress response in Escherichia coli, In: Storz G., Hengge-Aronis R. (Eds.), Bacterial stress response, ASM Press, Washington, D.C., 2000, 161-178
    • (2000) Bacterial Stress Response , pp. 161-178
    • Hengge-Aronis, R.1    Storz, G.2    Hengge-Aronis, R.3
  • 29
    • 28844501851 scopus 로고    scopus 로고
    • Oxidant-specific folding of Yap1p regulates both transcriptional activation and nuclear localization
    • DOI 10.1074/jbc.M504716200
    • K. Gulshan S.A. Rovinsky S.T. Coleman W.S. Moye-Rowley 2005 Oxidant-specific folding of Yap1p regulates both transcriptional activation and nuclear localization J. Biol. Chem. 280 40524 40533 (Pubitemid 41780541)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40524-40533
    • Gulshan, K.1    Rovinsky, S.A.2    Coleman, S.T.3    Moye-Rowley, W.S.4
  • 30
    • 33751001337 scopus 로고    scopus 로고
    • Thermodynamic basis for redox regulation of the Yap1 signal transduction pathway
    • J.T. Mason S.K. Kim D.B. Knaff M.J. Wood 2006 Thermodynamic basis for redox regulation of the Yap1 signal transduction pathway Biochemistry 45 13409 13417
    • (2006) Biochemistry , vol.45 , pp. 13409-13417
    • Mason, J.T.1    Kim, S.K.2    Knaff, D.B.3    Wood, M.J.4
  • 32
    • 0033646709 scopus 로고    scopus 로고
    • Adaptive response of the yeast Saccharomyces cerevisiae to reactive oxygen species: Defences, damage and death
    • P. Moradas-Ferreira V. Costa 2000 Adaptive response of the yeast Saccharomyces cerevisiae to reactive oxygen species: defences, damage and death Redox Rep. 5 277 285
    • (2000) Redox Rep. , vol.5 , pp. 277-285
    • Moradas-Ferreira, P.1    Costa, V.2
  • 33
  • 34
    • 0026640235 scopus 로고
    • Saccharomyces cerevisiae has distinct adaptive responses to both hydrogen peroxide and menadione
    • D.J. Jamieson 1992 Saccharomyces cerevisiae has distinct adaptive responses to both hydrogen peroxide and menadione J. Bacteriol. 174 6678 6681
    • (1992) J. Bacteriol. , vol.174 , pp. 6678-6681
    • Jamieson, D.J.1
  • 35
    • 0027483385 scopus 로고
    • Saccharomyces cerevisiae has an inducible response to menadione which differs from that to hydrogen peroxide
    • J. Flattery-O'Brien L.P. Collinson I.W. Dawes 1993 Saccharomyces cerevisiae has an inducible response to menadione which differs that to hydrogen peroxide J. Gen. Microbiol. 139 501 507 (Pubitemid 23101156)
    • (1993) Journal of General Microbiology , vol.139 , Issue.3 , pp. 501-507
    • Flattery-O'Brien, J.1    Collinson, L.P.2    Dawes, I.W.3
  • 37
    • 0028597439 scopus 로고
    • Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress
    • D.J. Jamieson S.L. Rivers D.W.S. Stephen 1994 Analysis of Saccharomyces cerevisiae proteins induced by peroxide and superoxide stress Microbiology 140 3277 3283
    • (1994) Microbiology , vol.140 , pp. 3277-3283
    • Jamieson, D.J.1    Rivers, S.L.2    Stephen, D.W.S.3
  • 39
    • 0027529748 scopus 로고
    • Regulation of Cu,Zn- and Mn-superoxide dismutase transcription in Saccharomyces cerevisiae
    • DOI 10.1016/0014-5793(93)81162-S
    • F. Galiazzo R. Labbe-Bois 1993 Regulation of Cu,Zn-and Mn-superoxide dismutase transcription in Saccharomyces cerevisiae FEBS Lett. 315 197 200 (Pubitemid 23015884)
    • (1993) FEBS Letters , vol.315 , Issue.2 , pp. 197-200
    • Galiazzo, F.1    Labbe-Bois, R.2
  • 40
    • 15844429977 scopus 로고    scopus 로고
    • Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae
    • V.D. Longo E.B. Gralla J.S. Valentine 1996 Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae J. Biol. Chem. 271 12275 12280
    • (1996) J. Biol. Chem. , vol.271 , pp. 12275-12280
    • Longo, V.D.1    Gralla, E.B.2    Valentine, J.S.3
  • 42
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria
    • L.A. Sturz K. Diekert L.T. Jensen R. Lill V.C. Cullota 2001 A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria J. Biol. Chem. 276 38084 38089
    • (2001) J. Biol. Chem. , vol.276 , pp. 38084-38089
    • Sturz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Cullota, V.C.5
  • 43
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase
    • R.A. Weisinger I. Fridovich 1973 Mitochondrial superoxide dismutase J. Biol. Chem. 248 4793 4796
    • (1973) J. Biol. Chem. , vol.248 , pp. 4793-4796
    • Weisinger, R.A.1    Fridovich, I.2
  • 44
    • 0034703101 scopus 로고    scopus 로고
    • Yeast lacking superoxide dismutase(s) show elevated levels of free iron as measured by whole cell electron paramagnetic resonance
    • DOI 10.1074/jbc.M004239200
    • C. Srinivasan A. Liba J.A. Imlay J.S. Valentine E.B. Gralla 2000 Yeast lacking superoxide dismutase(s) show elevated levels of "free iron" as measured by whole cell electron paramagnetic resonance J. Biol. Chem. 275 29187 29192 (Pubitemid 32043786)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29187-29192
    • Srinivasan, C.1    Liba, A.2    Imlay, J.A.3    Valentine, J.S.4    Gralla, E.B.5
  • 45
    • 0032483373 scopus 로고    scopus 로고
    • The cytoplasmic Cu,Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress
    • J.-I. Park C.M. Grant M.J. Davies I.W. Dawes 1998 The cytoplasmic Cu,Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress J. Biol. Chem. 273 22921 22928
    • (1998) J. Biol. Chem. , vol.273 , pp. 22921-22928
    • Park, J.-I.1    Grant, C.M.2    Davies, M.J.3    Dawes, I.W.4
  • 46
    • 27844572415 scopus 로고    scopus 로고
    • Diethyldithiocarbamate inhibits in vivo Cu,Zn-superoxide dismutase and perturbs free radical processes in the yeast Saccharomyces cerevisiae cells
    • DOI 10.1016/j.bbrc.2005.10.147, PII S0006291X05024381
    • V. Lushchak H. Semchyshyn S. Mandryk O. Lushchak 2005 Diethyldithiocarbamate inhibits in vivo Cu,Zn-superoxide dismutase and perturbs free radical processes in the yeast Saccharomyces cerevisiae cells Biochem. Biophys. Res. Commun. 338 1739 1744 (Pubitemid 41643084)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.4 , pp. 1739-1744
    • Lushchak, V.1    Semchyshyn, H.2    Lushchak, O.3    Mandryk, S.4
  • 47
    • 23944451104 scopus 로고    scopus 로고
    • Possible role of superoxide dismutases in the yeast Saccharomyces cerevisiae under respiratory conditions
    • DOI 10.1016/j.abb.2005.06.010, PII S0003986105002572
    • V. Lushchak H. Semchyshyn S. Mandryk O. Lushchak 2005 Possible role of superoxide dismutases in the yeast Saccharomyces cerevisiae under respiratory conditions Arch. Biochem. Biophys. 441 35 40 (Pubitemid 41188350)
    • (2005) Archives of Biochemistry and Biophysics , vol.441 , Issue.1 , pp. 35-40
    • Lushchak, V.1    Semchyshyn, H.2    Mandryk, S.3    Lushchak, O.4
  • 48
    • 35548933327 scopus 로고    scopus 로고
    • Growth on ethanol results in co-ordinated Saccharomyces cerevisiae response to inactivation of genes encoding superoxide dismutases
    • DOI 10.1179/135100007X200263
    • O. Lushchak H. Semchyshyn V. Lushchak 2007 Growth on ethanol results in coordinated S. cerevisiae response to inactivation of gene encoding superoxide dismutases Redox Rep. 4 181 188 (Pubitemid 350065113)
    • (2007) Redox Report , vol.12 , Issue.4 , pp. 181-188
    • Lushchak, O.V.1    Semchyshyn, H.M.2    Lushchak, V.I.3
  • 49
    • 0033655897 scopus 로고    scopus 로고
    • Superoxide dismutase, oxidative stress, and cell metabolism
    • V.C. Culotta 2000 Superoxide dismutase, oxidative stress, and cell metabolism Curr. Top. Cell. Regul. 36 117 132
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 117-132
    • Culotta, V.C.1
  • 51
    • 18044363639 scopus 로고    scopus 로고
    • SOD, oxidative stress and human pathologies: A brief history and a future vision
    • DOI 10.1016/j.biopha.2005.03.005
    • J.M. McCord M.A. Edeas 2005 SOD, oxidative stress and human pathologies: a brief history and a future vision Biomed. Pharmacother 59 139 142 (Pubitemid 40603324)
    • (2005) Biomedicine and Pharmacotherapy , vol.59 , Issue.4 , pp. 139-142
    • McCord, J.M.1    Edeas, M.A.2
  • 52
    • 0034042319 scopus 로고    scopus 로고
    • The pro-oxidative activity of SOD and nitroxide SOD mimics
    • T. Offer A. Russo A. Samuni 2000 The pro-oxidative activity of SOD and nitroxide SOD mimics FASEB J. 14 1215 1223 (Pubitemid 30350403)
    • (2000) FASEB Journal , vol.14 , Issue.9 , pp. 1215-1223
    • Offer, T.1    Russo, A.2    Samuni, A.3
  • 53
    • 0029844594 scopus 로고    scopus 로고
    • Importance of catalase in the adaptive response to hydrogen peroxide: Analysis of acatalasaemic Saccharomyces cerevisiae
    • S. Izawa Y. Inoue A. Kimura 1996 Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae Biochem. J. 320 61 67 (Pubitemid 26400161)
    • (1996) Biochemical Journal , vol.320 , Issue.1 , pp. 61-67
    • Izawa, S.1    Inoue, Y.2    Kimura, A.3
  • 55
    • 0031048280 scopus 로고    scopus 로고
    • The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae
    • DOI 10.1093/emboj/16.5.1035
    • B.A. Morgan G.R. Banks W.M. Toone D. Raitt S. Kuge L.H. Johnston 1997 The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae EMBO J. 16 1035 1044 (Pubitemid 27113182)
    • (1997) EMBO Journal , vol.16 , Issue.5 , pp. 1035-1044
    • Morgan, B.A.1    Banks, G.R.2    Mark Toone, W.3    Raitt, D.4    Kuge, S.5    Johnston, L.H.6
  • 57
    • 0033916138 scopus 로고    scopus 로고
    • The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsf1 in vivo and is required for the induction of heat shock genes by oxidative stress
    • D.C. Raitt A.L. Johnson A.M. Erkine K. Makino B. Morgan D.S. Gross 2000 The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsf1 in vivo and is required for the induction of heat shock genes by oxidative stress Mol. Cell. Biol. 11 2335 2347 (Pubitemid 30489918)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.7 , pp. 2335-2347
    • Raitt, D.C.1    Johnson, A.L.2    Erkine, A.M.3    Makino, K.4    Morgan, B.5    Gross, D.S.6    Johnston, L.H.7
  • 61
    • 0036187717 scopus 로고    scopus 로고
    • The adaptive response of Saccharomyces cerevisiae to mercury exposure
    • DOI 10.1002/yea.835
    • J. Westwater N.F. McLaren U.H. Dormer D.J. Jamieson 2002 The adaptive response of Saccharomyces cerevisiae to mercury exposure Yeast 19 233 239 (Pubitemid 34189561)
    • (2002) Yeast , vol.19 , Issue.3 , pp. 233-239
    • Westwater, J.1    McLaren, N.F.2    Dormer, U.H.3    Jamieson, D.J.4
  • 62
    • 33645120423 scopus 로고    scopus 로고
    • Cell wall assembly in Saccharomyces cerevisiae
    • DOI 10.1128/MMBR.00038-05
    • G. Lesage H. Bussey 2006 Cell wall assembly in Saccharomyces cerevisiae Microbiol. Mol. Biol. Rev. 70 317 343 (Pubitemid 43895030)
    • (2006) Microbiology and Molecular Biology Reviews , vol.70 , Issue.2 , pp. 317-343
    • Lesage, G.1    Bussey, H.2
  • 63
    • 19544370016 scopus 로고    scopus 로고
    • RGD1, encoding a RhoGAP involved in low-pH survival, is an Msn2p/Msn4p regulated gene in Saccharomyces cerevisiae
    • DOI 10.1016/j.gene.2005.03.034, PII S0378111905001812
    • X. Gatti G. de Bettignies S. Claret F. Doignon M. Crouzet D. Thoraval 2005 RGD1, encoding a RhoGAP involved in low-pH survival, is an Msn2p/Msn4p regulated gene in Saccharomyces cerevisiae Gene 351 159 169 (Pubitemid 40732628)
    • (2005) Gene , vol.351 , pp. 159-169
    • Gatti, X.1    De Bettignies, G.2    Claret, S.3    Doignon, F.4    Crouzet, M.5    Thoraval, D.6
  • 64
    • 33751069252 scopus 로고    scopus 로고
    • High hydrostatic pressure activates gene expression through Msn2/4 stress transcription factors which are involved in the acquired tolerance by mild pressure precondition in Saccharomyces cerevisiae
    • T. Domitrovic C.M. Fernandes E. Boy-Marcotte E. Kurtenbach 2006 High hydrostatic pressure activates gene expression through Msn2/4 stress transcription factors which are involved in the acquired tolerance by mild pressure precondition in Saccharomyces cerevisiae FEBS Lett. 580 6033 6038
    • (2006) FEBS Lett. , vol.580 , pp. 6033-6038
    • Domitrovic, T.1    Fernandes, C.M.2    Boy-Marcotte, E.3    Kurtenbach, E.4
  • 65
    • 33845298638 scopus 로고    scopus 로고
    • Msn2p/Msn4p-activation is essential for the recovery from freezing stress in yeast
    • S. Izawa K. Ikeda T. Ohdate Y. Inoue 2007 Msn2p/Msn4p-activation is essential for the recovery from freezing stress in yeast Biochem. Biophys. Res. Commun. 352 750 755
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 750-755
    • Izawa, S.1    Ikeda, K.2    Ohdate, T.3    Inoue, Y.4
  • 66
    • 0035726624 scopus 로고    scopus 로고
    • Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation
    • DOI 10.1128/MCB.21.18.6139-6150.2001
    • S. Kuge M. Arita A. Murayama K. Maeta S. Izawa Y. Inoue 2001 Regulation of the yeast Yap1p nuclear export signal is mediated by redox signalinduced reversible disulfide bond formation Mol. Cell. Biol. 21 6139 6150 (Pubitemid 34263514)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.18 , pp. 6139-6150
    • Kuge, S.1    Arita, M.2    Murayama, A.3    Maeta, K.4    Izawa, S.5    Inoue, Y.6    Nomoto, A.7
  • 67
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen Peroxide Sensing and Signaling
    • DOI 10.1016/j.molcel.2007.03.016, PII S1097276507001864
    • E.A. Veal A.M. Day B.A. Morgan 2007 Hydrogen peroxide sensing and signaling Mol. Cell 26 1 14 (Pubitemid 46578115)
    • (2007) Molecular Cell , vol.26 , Issue.1 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 68
    • 0037110454 scopus 로고    scopus 로고
    • A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation
    • A. Delaunay D. Pflieger M.B. Barrault J. Vinh M.B. Toledano 2002 A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation Cell 111 471 481
    • (2002) Cell , vol.111 , pp. 471-481
    • Delaunay, A.1    Pflieger, D.2    Barrault, M.B.3    Vinh, J.4    Toledano, M.B.5
  • 69
    • 0030942294 scopus 로고    scopus 로고
    • Regulation of yAP-1 nuclear localization in response to oxidative stress
    • DOI 10.1093/emboj/16.7.1710
    • S. Kuge N. Jones A. Nomoto 1997 Regulation of yAP-1 nuclear localization in response to oxidative stress EMBO J. 16 1710 1720 (Pubitemid 27151965)
    • (1997) EMBO Journal , vol.16 , Issue.7 , pp. 1710-1720
    • Kuge, S.1    Jones, N.2    Nomoto, A.3
  • 70
    • 0034597012 scopus 로고    scopus 로고
    • H2O2 sensing through oxidation of the Yap1 transcription factor
    • A. Delaunay A.D. Isnard M.B. Toledano 2000 H2O2 sensing through oxidation of the Yap1 transcription factor EMBO J. 19 5157 5166
    • (2000) EMBO J. , vol.19 , pp. 5157-5166
    • Delaunay, A.1    Isnard, A.D.2    Toledano, M.B.3
  • 71
    • 11244327652 scopus 로고    scopus 로고
    • Nuclear localization destabilizes the stress-regulated transcription factor Msn2
    • DOI 10.1074/jbc.M407264200
    • E. Durchschlag W. Reiter G. Ammerer C. Schuller 2004 Nuclear localization destabilizes the stress-regulated transcription factor Msn2 J. Biol. Chem. 279 55425 55432 (Pubitemid 40066543)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55425-55432
    • Durchschlag, E.1    Reiter, W.2    Ammerer, G.3    Schuller, C.4
  • 72
    • 33644821383 scopus 로고    scopus 로고
    • The transcriptional activation region of Msn2p, in Saccharomyces cerevisiae, is regulated by stress but is insensitive to the cAMP signalling pathway
    • DOI 10.1007/s00438-005-0017-4
    • E. Boy-Marcotte C. Garmendia H. Garreau S. Lallet L. Mallet M. Jacquet 2006 The transcriptional activation region of Msn2p, in Saccharomyces cerevisiae, is regulated by stress but is insensitive to the cAMP signalling pathway Mol. Genet. Genomics 275 277 287 (Pubitemid 43357664)
    • (2006) Molecular Genetics and Genomics , vol.275 , Issue.3 , pp. 277-287
    • Boy-Marcotte, E.1    Garmendia, C.2    Garreau, H.3    Lallet, S.4    Mallet, L.5    Jacquet, M.6
  • 73
    • 0029879360 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress-response element (STRE)
    • M.T. Martinez-Pastor G. Marchler C. Schüller A. Marchler-Bauer H. Ruis F. Estruch 1996 The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE) EMBO J. 15 2227 2235 (Pubitemid 26141139)
    • (1996) EMBO Journal , vol.15 , Issue.9 , pp. 2227-2235
    • Martinez-Pastor, M.T.1    Marchler, G.2    Schuller, C.3    Marchler-Bauer, A.4    Ruis, H.5    Estruch, F.6
  • 75
    • 0033828333 scopus 로고    scopus 로고
    • Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae
    • H. Garreau R.N. Hasan G. Renault F. Estruch E. Boy-Marcotte M. Jacquet 2000 Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae Microbiology 146 2113 2120
    • (2000) Microbiology , vol.146 , pp. 2113-2120
    • Garreau, H.1    Hasan, R.N.2    Renault, G.3    Estruch, F.4    Boy-Marcotte, E.5    Jacquet, M.6
  • 76
    • 0037080980 scopus 로고    scopus 로고
    • Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor
    • W. Görner E. Durchschlag J. Wolf E.L. Brown G. Ammerer H. Ruis C. Schüller 2002 Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor EMBO J. 21 135 144
    • (2002) EMBO J. , vol.21 , pp. 135-144
    • Görner, W.1    Durchschlag, E.2    Wolf, J.3    Brown, E.L.4    Ammerer, G.5    Ruis, H.6    Schüller, C.7
  • 77
    • 19944399062 scopus 로고    scopus 로고
    • The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation via a newly identified Glc7/Bud14 type i protein phosphatase module and TFIID promoter distribution
    • E. Lenssen N. James I. Pedruzzi F. Dubouloz E. Cameroni R. Bisig 2005 The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation via a newly identified Glc7/Bud14 type I protein phosphatase module and TFIID promoter distribution Mol. Cell. Biol. 25 488 498
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 488-498
    • Lenssen, E.1    James, N.2    Pedruzzi, I.3    Dubouloz, F.4    Cameroni, E.5    Bisig, R.6
  • 78
    • 0346433720 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p
    • J.M. Lu R.J. Deschenes J.S. Fassler 2003 Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p Eukaryot. Cell 2 1304 1314
    • (2003) Eukaryot. Cell , vol.2 , pp. 1304-1314
    • Lu, J.M.1    Deschenes, R.J.2    Fassler, J.S.3
  • 79
    • 0036179410 scopus 로고    scopus 로고
    • The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p
    • S. Li S. Dean Z. Li J. Horecka R.J. Deschenes J.S. Fassler 2002 The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p Mol. Biol. Cell. 13 412 424
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 412-424
    • Li, S.1    Dean, S.2    Li, Z.3    Horecka, J.4    Deschenes, R.J.5    Fassler, J.S.6
  • 83
    • 0037301640 scopus 로고    scopus 로고
    • Regulation of antioxidant enzymes gene expression in the yeast Saccharomyces cerevisiae during stationary phase
    • DOI 10.1016/S0891-5849(02)01300-X
    • L. Cyrne L. Martins L. Fernandes H.S. Marinho 2003 Regulation of antioxidant enzymes gene expression in the yeast Saccharomyces cerevisiae during stationary phase Free Radic. Biol. Med. 34 385 393 (Pubitemid 36120754)
    • (2003) Free Radical Biology and Medicine , vol.34 , Issue.3 , pp. 385-393
    • Cyrne, L.1    Martins, L.2    Fernandes, L.3    Marinho, H.S.4
  • 85
    • 34547837362 scopus 로고    scopus 로고
    • Possible accumulation of non-active molecules of catalase and superoxide dismutase in S. cerevisiae cells under hydrogen peroxide induced stress
    • DOI 10.2478/s11535-007-0021-2
    • M. Bayliak H. Semchyshyn V. Lushchak 2007 Possible accumulation of non-active molecules of catalase and superoxide dismutase in S. cerevisiae cells under hydrogen peroxide induced stress Cent. Eur. J. Biol. 2 326 336 (Pubitemid 47245950)
    • (2007) Central European Journal of Biology , vol.2 , Issue.3 , pp. 326-336
    • Bayliak, M.M.1    Semchyshyn, H.M.2    Lushchak, V.I.3
  • 86
    • 21144433999 scopus 로고    scopus 로고
    • Possible reasons for difference in sensitivity to oxygen of two Escherichia coli strains
    • H.M. Semchyshyn V.I. Lushchak K. Storey 2005 Possible reasons for difference in sensitivity to oxygen of two Escherichia coli strains Biochemistry (Mosc.) 70 424 431
    • (2005) Biochemistry (Mosc.) , vol.70 , pp. 424-431
    • Semchyshyn, H.M.1    Lushchak, V.I.2    Storey, K.3
  • 87
    • 39049186021 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide on antioxidant enzyme activities in Saccharomyces cerevisiae is strain-specific
    • M. Bayliak H. Semchyshyn V. Lushchak 2006 Effect of hydrogen peroxide on antioxidant enzyme activities in Saccharomyces cerevisiae is strain-specific Biochemistry (Mosc.) 71 1243 1252
    • (2006) Biochemistry (Mosc.) , vol.71 , pp. 1243-1252
    • Bayliak, M.1    Semchyshyn, H.2    Lushchak, V.3
  • 91
    • 33847660853 scopus 로고    scopus 로고
    • Use and abuse of exogenous H2O2 in studies of signal transduction
    • H.J. Forman 2007 Use and abuse of exogenous H2O2 in studies of signal transduction Free Radic. Biol. Med. 42 926 932
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 926-932
    • Forman, H.J.1
  • 92
    • 0026513954 scopus 로고
    • Inducibility of the response of yeast cells to peroxide stress
    • L.P. Collinson I.W. Dawes 1992 Inducibility of the response of yeast cells to peroxide stress J. Gen. Microbiol. 138 329 335
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 329-335
    • Collinson, L.P.1    Dawes, I.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.