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Volumn 8, Issue 10, 2007, Pages 813-824

ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

DNA; REACTIVE OXYGEN METABOLITE;

EID: 34648813720     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2256     Document Type: Review
Times cited : (2856)

References (27)
  • 1
    • 0037365968 scopus 로고    scopus 로고
    • Nathan, C. Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling. J. Clin. Invest. 111, 769-778 (2003). An opinion paper that discusses the physiological and molecular basis of specificity in ROS and RNS signalling.
    • Nathan, C. Specificity of a third kind: reactive oxygen and nitrogen intermediates in cell signaling. J. Clin. Invest. 111, 769-778 (2003). An opinion paper that discusses the physiological and molecular basis of specificity in ROS and RNS signalling.
  • 3
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. Pathways of oxidative damage. Annu. Rev. Microbiol. 57, 395-418 (2003).
    • (2003) Annu. Rev. Microbiol , vol.57 , pp. 395-418
    • Imlay, J.A.1
  • 5
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn, C. C. & Metodiewa, D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic. Biol. Med. 27, 322-328 (1999).
    • (1999) Free Radic. Biol. Med , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 6
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert, H. F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63, 69-172 (1990).
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 7
  • 8
    • 0242668686 scopus 로고    scopus 로고
    • Wood, Z. A., Poole, L. B. & Karplus, P. A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653 (2003). Describes the structural basis of the sensitivity of a subgroup of peroxiredoxins to inactivation by overoxidation.
    • Wood, Z. A., Poole, L. B. & Karplus, P. A. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653 (2003). Describes the structural basis of the sensitivity of a subgroup of peroxiredoxins to inactivation by overoxidation.
  • 10
    • 33744543755 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae proteome of oxidized protein thiols: Contrasted functions for the thioredoxin and glutathione pathways
    • Le Moan, N., Clement, G., Le Maout, S., Tacnet, F. & Toledano, M. B. The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J. Biol. Chem. 281, 10420-10430 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 10420-10430
    • Le Moan, N.1    Clement, G.2    Le Maout, S.3    Tacnet, F.4    Toledano, M.B.5
  • 11
    • 33846813788 scopus 로고    scopus 로고
    • Reversible redox- and zinc-dependent dimerization of the Escherichia coli Fur protein
    • D'Autreaux, B. et al. Reversible redox- and zinc-dependent dimerization of the Escherichia coli Fur protein. Biochemistry 46, 1329-1342 (2007).
    • (2007) Biochemistry , vol.46 , pp. 1329-1342
    • D'Autreaux, B.1
  • 12
    • 33745865202 scopus 로고    scopus 로고
    • Zinc center as redox switch - new function for an old motif
    • Ilbert, M., Graf, P. C. & Jakob, U. Zinc center as redox switch - new function for an old motif. Antioxid. Redox Signal 8, 835-846 (2006).
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 835-846
    • Ilbert, M.1    Graf, P.C.2    Jakob, U.3
  • 13
    • 1642389890 scopus 로고    scopus 로고
    • Zinc and sulfur: A critical biological partnership
    • Maret, W. Zinc and sulfur: a critical biological partnership. Biochemistry 43, 3301-3309 (2004).
    • (2004) Biochemistry , vol.43 , pp. 3301-3309
    • Maret, W.1
  • 14
    • 23844508188 scopus 로고    scopus 로고
    • The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability
    • Conrad, M. et al. The nuclear form of phospholipid hydroperoxide glutathione peroxidase is a protein thiol peroxidase contributing to sperm chromatin stability. Mol. Cell Biol. 25, 7637-7644 (2005).
    • (2005) Mol. Cell Biol , vol.25 , pp. 7637-7644
    • Conrad, M.1
  • 15
    • 33644670813 scopus 로고    scopus 로고
    • Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase
    • Maiorino, M. et al. Functional interaction of phospholipid hydroperoxide glutathione peroxidase with sperm mitochondrion-associated cysteine-rich protein discloses the adjacent cysteine motif as a new substrate of the selenoperoxidase. J. Biol. Chem. 280, 38395-38402 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 38395-38402
    • Maiorino, M.1
  • 16
    • 0028049068 scopus 로고
    • An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein
    • Hidalgo, E. & Demple, B. An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein. EMBO J. 13, 138-146 (1994).
    • (1994) EMBO J , vol.13 , pp. 138-146
    • Hidalgo, E.1    Demple, B.2
  • 17
    • 1642514907 scopus 로고    scopus 로고
    • Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species
    • Mukhopadhyay, P., Zheng, M., Bedzyk, L. A., LaRossa, R. A. & Storz, G. Prominent roles of the NorR and Fur regulators in the Escherichia coli transcriptional response to reactive nitrogen species. Proc. Natl Acad. Sci. USA 101, 745-750 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 745-750
    • Mukhopadhyay, P.1    Zheng, M.2    Bedzyk, L.A.3    LaRossa, R.A.4    Storz, G.5
  • 18
    • 0026778382 scopus 로고
    • Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon
    • Liochev, S. I. & Fridovich, I. Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon. Proc. Natl Acad. Sci. USA 89, 5892-5896 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5892-5896
    • Liochev, S.I.1    Fridovich, I.2
  • 19
    • 0038540118 scopus 로고    scopus 로고
    • A reducing system of the superoxide sensor SoxR in Escherichia coli
    • Koo, M. S. et al. A reducing system of the superoxide sensor SoxR in Escherichia coli. EMBO J. 22, 2614-2622 (2003).
    • (2003) EMBO J , vol.22 , pp. 2614-2622
    • Koo, M.S.1
  • 20
    • 33847772498 scopus 로고    scopus 로고
    • Superoxide-mediated amplification of the oxygen-induced switch from [4Fe-4S] to [2Fe-2S] clusters in the transcriptional regulator FNR
    • Crack, J. C., Green, J., Cheesman, M. R., Le Brun, N. E. & Thomson, A. J. Superoxide-mediated amplification of the oxygen-induced switch from [4Fe-4S] to [2Fe-2S] clusters in the transcriptional regulator FNR. Proc. Natl Acad. Sci. USA 104, 2092-2097 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2092-2097
    • Crack, J.C.1    Green, J.2    Cheesman, M.R.3    Le Brun, N.E.4    Thomson, A.J.5
  • 22
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C. J. et al. IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc. Natl Acad. Sci. USA 98, 14895-14900 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1
  • 23
    • 33745187803 scopus 로고    scopus 로고
    • IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins
    • Yeo, W. S., Lee, J. H., Lee, K. C. & Roe, J. H. IscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins. Mol. Microbiol. 61, 206-218 (2006).
    • (2006) Mol. Microbiol , vol.61 , pp. 206-218
    • Yeo, W.S.1    Lee, J.H.2    Lee, K.C.3    Roe, J.H.4
  • 24
    • 1842608845 scopus 로고    scopus 로고
    • Iron metabolism and the IRE/IRP regulatory system: An update
    • Pantopoulos, K. Iron metabolism and the IRE/IRP regulatory system: an update. Ann. NY Acad. Sci. 1012, 1-13 (2004).
    • (2004) Ann. NY Acad. Sci , vol.1012 , pp. 1-13
    • Pantopoulos, K.1
  • 25
    • 0032513362 scopus 로고    scopus 로고
    • Zheng, M., Aslund, F. & Storz, G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721 (1998). Identification of the OxyR regulatory disulphide bond by mass spectrometry.
    • Zheng, M., Aslund, F. & Storz, G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721 (1998). Identification of the OxyR regulatory disulphide bond by mass spectrometry.
  • 26
    • 33645037891 scopus 로고    scopus 로고
    • 2.
    • 2.
  • 27
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S. & Helmann, J. D. OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J. Bacteriol. 183, 4134-4141 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.