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Volumn 57, Issue 4, 2009, Pages 399-411

Redox-sensitive signaling factors and antioxidants

Author keywords

Antioxidants; Gene expression; Glutathione; Oxidative stress; Thioredoxin; Transcription factors

Indexed keywords

ANTIOXIDANT; CATALASE; ERIOCALYXIN B; ESTROGEN RECEPTOR; GLUCOCORTICOID RECEPTOR; GLUTATHIONE PEROXIDASE; HELIX LOOP HELIX PROTEIN; HERBACEOUS AGENT; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; ISOFLAVONE; LEUCINE ZIPPER PROTEIN; METHYLGLYOXAL; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN P53; REACTIVE OXYGEN METABOLITE; REDOX EFFECTOR FACTOR 1; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; ZINC FINGER PROTEIN;

EID: 69249212488     PISSN: 00148237     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (21)

References (52)
  • 3
    • 1642422773 scopus 로고    scopus 로고
    • Mitochondrial free radical production and cell signaling
    • Cadenas E., Mitochondrial free radical production and cell signaling. Mol Asp Med. 2004, 25, 17-26.
    • (2004) Mol Asp Med , vol.25 , pp. 17-26
    • Cadenas, E.1
  • 4
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • Nathan C., Nitric oxide as a secretory product of mammalian cells. FASEB J. 1992, 6, 3051-3064.
    • (1992) FASEB J , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 6
    • 18244364147 scopus 로고    scopus 로고
    • Mendez J.I., Nicholson W.J., Taylorw.R., SOD Isoforms and Signaling in Blood Vessels: Evidence for the Importance of ROS Compartmentalization. Arterioscler. Thromb. Vasc. Biol. 2005, 25, 887-888.
    • Mendez J.I., Nicholson W.J., Taylorw.R., SOD Isoforms and Signaling in Blood Vessels: Evidence for the Importance of ROS Compartmentalization. Arterioscler. Thromb. Vasc. Biol. 2005, 25, 887-888.
  • 8
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W., Free radicals in the physiological control of cell function, Physiol Rev. 2002, 82, 47-95
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 9
    • 0037046214 scopus 로고    scopus 로고
    • Mechanisms of increased vascular superoxide production in human diabetes mellitus: Role of NAD(P)H oxidase and endothelial nitric oxide synthase
    • Guzik T.J., Mussa S., Gastaldi D., Sadowski J., Ratnatunga C., Pillai R., Channon K.M., Mechanisms of increased vascular superoxide production in human diabetes mellitus: role of NAD(P)H oxidase and endothelial nitric oxide synthase. Circulation. 2002, 105, 1656-1662.
    • (2002) Circulation , vol.105 , pp. 1656-1662
    • Guzik, T.J.1    Mussa, S.2    Gastaldi, D.3    Sadowski, J.4    Ratnatunga, C.5    Pillai, R.6    Channon, K.M.7
  • 10
    • 0035668056 scopus 로고    scopus 로고
    • Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA - transferase
    • Turko I.V., Marcondes S., Murad F., Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA - transferase. Am. J. Physiol. Heart Circ. Physiol, 2001, 281, 2289-2294.
    • (2001) Am. J. Physiol. Heart Circ. Physiol , vol.281 , pp. 2289-2294
    • Turko, I.V.1    Marcondes, S.2    Murad, F.3
  • 12
    • 25144482448 scopus 로고    scopus 로고
    • Novel mechanisms of natural antioxidant compounds in biological systems: Involvement of glutathione and glutathione related enzymes
    • Masella R., Benedetto R.D., Vari R., Filesi C., Giovannini C., Novel mechanisms of natural antioxidant compounds in biological systems: Involvement of glutathione and glutathione related enzymes. J. Nutr. Biochem. 2005, 16, 577-586.
    • (2005) J. Nutr. Biochem , vol.16 , pp. 577-586
    • Masella, R.1    Benedetto, R.D.2    Vari, R.3    Filesi, C.4    Giovannini, C.5
  • 16
    • 0029760957 scopus 로고    scopus 로고
    • Redox regulation of transcriptional activators
    • Sun Y., Oberley L.W., Redox regulation of transcriptional activators. Free Radic. Biol. Med. 1996, 21, 335-348.
    • (1996) Free Radic. Biol. Med , vol.21 , pp. 335-348
    • Sun, Y.1    Oberley, L.W.2
  • 17
    • 0031872331 scopus 로고    scopus 로고
    • Influence du stress oxydant sur la regulation des genes
    • Morel Y., Barouki R., Influence du stress oxydant sur la regulation des genes, Science, 1998, 14, 713-721
    • (1998) Science , vol.14 , pp. 713-721
    • Morel, Y.1    Barouki, R.2
  • 18
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen L.F., Greene W.C., Shaping the nuclear action of NF-kappaB. Nat.Rev.Mol.Cell Biol. 5, 392-40, 2004.
    • (2004) Nat.Rev.Mol.Cell Biol , vol.5 , pp. 392-440
    • Chen, L.F.1    Greene, W.C.2
  • 20
    • 0028170816 scopus 로고
    • Structure, regulation, and function of NF-kappa B
    • Siebenlist U., Franzoso G., Brown K., Structure, regulation, and function of NF-kappa B, Annu.Rev.Cell Biol. 1994, 10, 405-455.
    • (1994) Annu.Rev.Cell Biol , vol.10 , pp. 405-455
    • Siebenlist, U.1    Franzoso, G.2    Brown, K.3
  • 21
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF- kappa B signaling
    • Hayden M.S., Ghosh S., Shared principles in NF- kappa B signaling. Cell. 2008, 132, 344-362.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 22
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NFkappaB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y., Ando K., Hirao S., Yoshida M., and Handa H., Redox regulation of NFkappaB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid.Redox Signal. 2005, 7, 395-403.
    • (2005) Antioxid.Redox Signal , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 23
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • Perkins N.D., Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat.Rev.Mol. Cell Biol. 2007, 8, 49-62.
    • (2007) Nat.Rev.Mol. Cell Biol , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 24
    • 34848921787 scopus 로고    scopus 로고
    • Nuclear factor-kappaB activation via tyrosine phosphorylation of inhibitor kappaB-alpha is crucial for ciliary neurotrophic factor-promoted neurite growth from developing neurons
    • Gallagher D., Gutierrez H., Gavalda N., O'Keeffe G., Hay R., and Davies A.M., Nuclear factor-kappaB activation via tyrosine phosphorylation of inhibitor kappaB-alpha is crucial for ciliary neurotrophic factor-promoted neurite growth from developing neurons, J.Neurosci. 2007, 27, 9664-9669.
    • (2007) J.Neurosci , vol.27 , pp. 9664-9669
    • Gallagher, D.1    Gutierrez, H.2    Gavalda, N.3    O'Keeffe, G.4    Hay, R.5    Davies, A.M.6
  • 25
    • 33750523632 scopus 로고    scopus 로고
    • fifteen years later
    • NF-kappaB activation by reactive oxygen species
    • Gloire G., Legrand-Poels S., Piette J., NF-kappaB activation by reactive oxygen species: fifteen years later. Biochem Pharmacol 2006, 72, 1493-1505.
    • (2006) Biochem Pharmacol , vol.72 , pp. 1493-1505
    • Gloire, G.1    Legrand-Poels, S.2    Piette, J.3
  • 26
    • 0025852479 scopus 로고
    • Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro
    • Toledano M.B., Leonard W.J., Modulation of transcription factor NF-kappa B binding activity by oxidation-reduction in vitro. Proc.Natl.Acad. Sci. U S A. 1991, 88, 4328-4332.
    • (1991) Proc.Natl.Acad. Sci. U S A , vol.88 , pp. 4328-4332
    • Toledano, M.B.1    Leonard, W.J.2
  • 28
    • 0033600744 scopus 로고    scopus 로고
    • Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB
    • Hirota K., Murata M., Sachi Y., Nakamura H., Takeuchi J., Mori K., and Yodoi J., Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB. J.Biol.Chem. 1999, 274, 27891-27897.
    • (1999) J.Biol.Chem , vol.274 , pp. 27891-27897
    • Hirota, K.1    Murata, M.2    Sachi, Y.3    Nakamura, H.4    Takeuchi, J.5    Mori, K.6    Yodoi, J.7
  • 31
  • 32
    • 0034746311 scopus 로고    scopus 로고
    • NF-kB: Pivotal mediator or innocent bystander in atherogenesis ?
    • Collins T., Cybulsky M.I., NF-kB: pivotal mediator or innocent bystander in atherogenesis ? J.Clin.Invest. 2001, 197, 255-264.
    • (2001) J.Clin.Invest , vol.197 , pp. 255-264
    • Collins, T.1    Cybulsky, M.I.2
  • 33
    • 33751105546 scopus 로고    scopus 로고
    • Eriocalyxin B Inhibits Nuclear Factor-kB Activation by Interfering with the Binding of Both p65 and p50 to the Response Element in a Noncompetitive Manner
    • Leung C.H., Grill S.P., Wing Lam W., Gao W., Sun H.D., Cheng Y.C., Eriocalyxin B Inhibits Nuclear Factor-kB Activation by Interfering with the Binding of Both p65 and p50 to the Response Element in a Noncompetitive Manner. Mol.Pharmacol. 2006, 70, 1946-1955.
    • (2006) Mol.Pharmacol , vol.70 , pp. 1946-1955
    • Leung, C.H.1    Grill, S.P.2    Wing Lam, W.3    Gao, W.4    Sun, H.D.5    Cheng, Y.C.6
  • 34
    • 33947287291 scopus 로고    scopus 로고
    • Down-regulation of apurinic/apyrimidinic endonuclease 1/redox factor-1 expression by soy isoflavones enhances prostate cancer radiotherapy in vitro and in vivo
    • Raffoul J.J., Banerjee S., Singh-Gupta V., Knoll Z.E., Fite A., Zhang H., Abrams J., Sarkar F.H., and Hillman G.G., Down-regulation of apurinic/apyrimidinic endonuclease 1/redox factor-1 expression by soy isoflavones enhances prostate cancer radiotherapy in vitro and in vivo. Cancer Res. 2007, 67, 2141-2149.
    • (2007) Cancer Res , vol.67 , pp. 2141-2149
    • Raffoul, J.J.1    Banerjee, S.2    Singh-Gupta, V.3    Knoll, Z.E.4    Fite, A.5    Zhang, H.6    Abrams, J.7    Sarkar, F.H.8    Hillman, G.G.9
  • 37
    • 34047207337 scopus 로고    scopus 로고
    • TP53 mutations in human cancers: Functional selection and impact on cancer prognosis and outcomes
    • Petitjean A., Achatz M.I., Borresen-Dale A.L., Hainaut P., Olivier M., TP53 mutations in human cancers: functional selection and impact on cancer prognosis and outcomes. Oncogene. 2007, 26, 2157-2165.
    • (2007) Oncogene , vol.26 , pp. 2157-2165
    • Petitjean, A.1    Achatz, M.I.2    Borresen-Dale, A.L.3    Hainaut, P.4    Olivier, M.5
  • 39
    • 24644457314 scopus 로고    scopus 로고
    • Complicating the complexity of p53
    • Yee K.S., Vousden K.H., Complicating the complexity of p53, Carcinogenesis. 2005, 26, 1317-1322.
    • (2005) Carcinogenesis , vol.26 , pp. 1317-1322
    • Yee, K.S.1    Vousden, K.H.2
  • 40
    • 11144356558 scopus 로고    scopus 로고
    • p53-induced up-regulation of MnSOD and GPx but not catalase increases oxidative stress and apoptosis
    • Hussain S.P., Amstad P., He P. et al., p53-induced up-regulation of MnSOD and GPx but not catalase increases oxidative stress and apoptosis. Cancer Res. 2004, 64, 2350-2356.
    • (2004) Cancer Res , vol.64 , pp. 2350-2356
    • Hussain, S.P.1    Amstad, P.2    He, P.3
  • 41
    • 2142815107 scopus 로고    scopus 로고
    • Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD
    • Budanov A.V., Sablina A.A., Feinstein E., Koonin E.V., Chumakov P.M., Regeneration of peroxiredoxins by p53-regulated sestrins, homologs of bacterial AhpD. Science. 2004, 304, 596-600.
    • (2004) Science , vol.304 , pp. 596-600
    • Budanov, A.V.1    Sablina, A.A.2    Feinstein, E.3    Koonin, E.V.4    Chumakov, P.M.5
  • 42
    • 0037377060 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation and acetylation: The molecular basis for p53 regulation
    • Brooks C.L., Gu W., Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. Curr.Opin.Cell Biol. 2003, 15, 164-171.
    • (2003) Curr.Opin.Cell Biol , vol.15 , pp. 164-171
    • Brooks, C.L.1    Gu, W.2
  • 43
    • 59149085299 scopus 로고    scopus 로고
    • MSL2 promotes Mdm2-independent cytoplasmic localization of p53
    • Kruse J.P., Gu W., MSL2 promotes Mdm2-independent cytoplasmic localization of p53, J.Biol.Chem. 2009, 284, 3250-3263.
    • (2009) J.Biol.Chem , vol.284 , pp. 3250-3263
    • Kruse, J.P.1    Gu, W.2
  • 44
    • 0036606407 scopus 로고    scopus 로고
    • Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277
    • Buzek J., Latonen L., Kurki S., Peltonen K., Laiho M., Redox state of tumor suppressor p53 regulates its sequence-specific DNA binding in DNA-damaged cells by cysteine 277. Nucleic Acids Res. 2002, 30, 2340-2348.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2340-2348
    • Buzek, J.1    Latonen, L.2    Kurki, S.3    Peltonen, K.4    Laiho, M.5
  • 46
    • 33745170683 scopus 로고    scopus 로고
    • 2+ on DNA Recognition and Stability of the p53 DNA-Binding Domain
    • 2+ on DNA Recognition and Stability of the p53 DNA-Binding Domain. Biochemistry. 2006, 45, 7483-7492.
    • (2006) Biochemistry , vol.45 , pp. 7483-7492
    • Duan, J.1    Nilsson, L.2
  • 47
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y., Gorina S., Jeffrey P.D., Pavletich N.P., Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science. 1994, 265, 346-354.
    • (1994) Science , vol.265 , pp. 346-354
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 48
    • 0242552555 scopus 로고    scopus 로고
    • Influence of induced reactive oxygen species in p53-mediated cell fate decisions
    • Macip S., Igarashi M., Berggren P., Yu J., Lee S.W., Aaronson S.A., Influence of induced reactive oxygen species in p53-mediated cell fate decisions. Mol.Cell Biol. 2003, 23, 8576-8585.
    • (2003) Mol.Cell Biol , vol.23 , pp. 8576-8585
    • Macip, S.1    Igarashi, M.2    Berggren, P.3    Yu, J.4    Lee, S.W.5    Aaronson, S.A.6
  • 50
    • 57749193750 scopus 로고    scopus 로고
    • Vlad. Gruia, Andreea Arsene-Nitulescu, Mohora Maria, Niculina Mitrea, Daniela Gradinaru, Begona Y. Manuel, Correlations between some plasmatic redox parameters in diabetic pacients, Farmacia 2008, 56(6), 692-698
    • Vlad. Gruia, Andreea Arsene-Nitulescu, Mohora Maria, Niculina Mitrea, Daniela Gradinaru, Begona Y. Manuel, Correlations between some plasmatic redox parameters in diabetic pacients, Farmacia 2008, 56(6), 692-698
  • 51
    • 45949090990 scopus 로고    scopus 로고
    • Modifications of oxidative stress parameters in relationship with modifications of lipidic profile in arterial hypertension
    • Ioana Paduraru, Ofelia Paduraru, Luminita Jerca, Sanda Patrascanu, Modifications of oxidative stress parameters in relationship with modifications of lipidic profile in arterial hypertension, Farmacia 2008, 56(3), 261-266
    • (2008) Farmacia , vol.56 , Issue.3 , pp. 261-266
    • Paduraru, I.1    Paduraru, O.2    Jerca, L.3    Patrascanu, S.4
  • 52
    • 45949085677 scopus 로고    scopus 로고
    • Serum oxidative stress parameters and homocysteine levels in patients with renal transplant
    • Angela Antonescu, Mariana Mureşan, Otilia Micle, Liana Micle, Luciana Dobjanschi, Laura Vicaş, M. Dorofteiu, Serum oxidative stress parameters and homocysteine levels in patients with renal transplant, Farmacia 2008, 56(3), 352,358
    • (2008) Farmacia , vol.56 , Issue.3 , pp. 352-358
    • Antonescu, A.1    Mureşan, M.2    Micle, O.3    Micle, L.4    Dobjanschi, L.5    Laura Vicaş, M.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.