메뉴 건너뛰기




Volumn 8, Issue 1, 2011, Pages

A direct way of redox sensing

Author keywords

Hypoxia; Oxidative stress; Redox sensing; Redox signaling; Redox switch; RNA binding proteins

Indexed keywords

REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RNA; RNA BINDING PROTEIN; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; CYSTEINE; DISULFIDE; HYDROGEN PEROXIDE; THIOL DERIVATIVE;

EID: 79952226736     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.8.1.13555     Document Type: Review
Times cited : (11)

References (68)
  • 1
    • 69849097192 scopus 로고    scopus 로고
    • Mitochondrial generation of free radicals and hypoxic signaling
    • Poyton RO, Ball KA, Castello PR. Mitochondrial generation of free radicals and hypoxic signaling. Trends Endocrinol Metab 2009; 20:332-40.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 332-340
    • Poyton, R.O.1    Ball, K.A.2    Castello, P.R.3
  • 2
    • 78650097292 scopus 로고    scopus 로고
    • Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation
    • Gianni D, Dermardirossian C, Bokoch GM. Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation. Eur J Cell Biol 2010.
    • (2010) Eur J Cell Biol
    • Gianni, D.1    Dermardirossian, C.2    Bokoch, G.M.3
  • 3
    • 75749123115 scopus 로고    scopus 로고
    • Orchestrating redox signaling networks through regulatory cysteine switches
    • Paulsen CE, Carroll KS. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol 2010; 5:47-62.
    • (2010) ACS Chem Biol , vol.5 , pp. 47-62
    • Paulsen, C.E.1    Carroll, K.S.2
  • 6
    • 37049198258 scopus 로고
    • Enzyme systems containing active sulfhydryl groups: The role of glutathione
    • Barron ES, Singer TP. Enzyme systems containing active sulfhydryl groups: The role of glutathione. Science 1943; 97:356-8.
    • (1943) Science , vol.97 , pp. 356-358
    • Barron, E.S.1    Singer, T.P.2
  • 7
    • 0017747006 scopus 로고
    • On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins
    • Fahey RC, Hunt JS, Windham GC. On the cysteine and cystine content of proteins. Differences between intracellular and extracellular proteins. J Mol Evol 1977; 10:155-60. (Pubitemid 8230959)
    • (1977) Journal of Molecular Evolution , vol.10 , Issue.2 , pp. 155-160
    • Fahey, R.C.1    Hunt, J.S.2    Windham, G.C.3
  • 8
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton JM. Disulphide bridges in globular proteins. J Mol Biol 1981; 151:261-87.
    • (1981) J Mol Biol , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 10
    • 77952077940 scopus 로고    scopus 로고
    • The redox switch: Dynamic regulation of protein function by cysteine modifications
    • Spadaro D, Yun BW, Spoel SH, Chu C, Wang YQ, Loake GJ. The redox switch: dynamic regulation of protein function by cysteine modifications. Physiol Plant 2010; 138:360-71.
    • (2010) Physiol Plant , vol.138 , pp. 360-371
    • Spadaro, D.1    Yun, B.W.2    Spoel, S.H.3    Chu, C.4    Wang, Y.Q.5    Loake, G.J.6
  • 11
    • 0032053707 scopus 로고    scopus 로고
    • Oxygen radicals and signaling
    • DOI 10.1016/S0955-0674(98)80147-6
    • Finkel T. Oxygen radicals and signaling. Curr Opin Cell Biol 1998; 10:248-53. (Pubitemid 28174767)
    • (1998) Current Opinion in Cell Biology , vol.10 , Issue.2 , pp. 248-253
    • Finkel, T.1
  • 13
    • 79960410407 scopus 로고    scopus 로고
    • Intermolecular disulfide bond to modulate protein function as a redox-sensing switch
    • In press
    • Nagahara N. Intermolecular disulfide bond to modulate protein function as a redox-sensing switch. Amino Acids 2010; In press.
    • (2010) Amino Acids
    • Nagahara, N.1
  • 14
    • 75749136883 scopus 로고    scopus 로고
    • Signaling functions of reactive oxygen species
    • Forman HJ, Maiorino M, Ursini F. Signaling functions of reactive oxygen species. Biochemistry 2010; 49:835-42.
    • (2010) Biochemistry , vol.49 , pp. 835-842
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 15
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems and apoptosis
    • Circu ML, Aw TY. Reactive oxygen species, cellular redox systems and apoptosis. Free Radic Biol Med 2010; 48:749-62.
    • (2010) Free Radic Biol Med , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 16
    • 0036775442 scopus 로고    scopus 로고
    • Redox signaling of angiogenesis
    • Maulik N. Redox signaling of angiogenesis. Antioxid Redox Signal 2002; 4:805-15. (Pubitemid 35246944)
    • (2002) Antioxidants and Redox Signaling , vol.4 , Issue.5 , pp. 805-815
    • Maulik, N.1
  • 17
    • 70349799010 scopus 로고    scopus 로고
    • The cell cycle is a redox cycle: Linking phase-specific targets to cell fate
    • Burhans WC, Heintz NH. The cell cycle is a redox cycle: linking phase-specific targets to cell fate. Free Radic Biol Med 2009; 47:1282-93.
    • (2009) Free Radic Biol Med , vol.47 , pp. 1282-1293
    • Burhans, W.C.1    Heintz, N.H.2
  • 18
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation, and a consensus motif
    • DOI 10.1016/S0896-6273(00)80310-4
    • Stamler JS, Toone EJ, Lipton SA, Sucher NJ. (S)NO signals: translocation, regulation and a consensus motif. Neuron 1997; 18:691-6. (Pubitemid 27232781)
    • (1997) Neuron , vol.18 , Issue.5 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 19
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • DOI 10.1016/j.sbi.2004.09.012, PII S0959440X04001769
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr Opin Struct Biol 2004; 14:679-86. (Pubitemid 39592578)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.6 , pp. 679-686
    • Barford, D.1
  • 20
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid
    • DOI 10.1110/ps.073096508
    • Salsbury FR Jr, Knutson ST, Poole LB, Fetrow JS. Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Protein Sci 2008; 17:299-312. (Pubitemid 351171842)
    • (2008) Protein Science , vol.17 , Issue.2 , pp. 299-312
    • Salsbury Jr., F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4
  • 21
    • 0027383705 scopus 로고
    • aof the active site cysteine and the function of the conserved histidine 402
    • a of the active site cysteine and the function of the conserved histidine 402. Biochemistry 1993; 32:9340-5.
    • (1993) Biochemistry , vol.32 , pp. 9340-9345
    • Zhang, Z.Y.1    Dixon, J.E.2
  • 22
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate C, Patel L, Rauscher FJ, III, Curran T. Redox regulation of fos and jun DNA-binding activity in vitro. Science 1990; 249:1157-61.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher III, F.J.3    Curran, T.4
  • 24
    • 76149146090 scopus 로고    scopus 로고
    • DNA-mediated charge transport in redox sensing and signaling
    • Genereux JC, Boal AK, Barton JK. DNA-mediated charge transport in redox sensing and signaling. J Am Chem Soc 2010; 132:891-905.
    • (2010) J Am Chem Soc , vol.132 , pp. 891-905
    • Genereux, J.C.1    Boal, A.K.2    Barton, J.K.3
  • 25
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: A signaling messenger
    • DOI 10.1089/ars.2006.8.243
    • Stone JR, Yang S. Hydrogen peroxide: a signaling messenger. Antioxid Redox Signal 2006; 8:243-70. (Pubitemid 43741296)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.3-4 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 27
    • 77951938957 scopus 로고    scopus 로고
    • Regulation of redox signaling by selenoproteins
    • Hawkes WC, Alkan Z. Regulation of redox signaling by selenoproteins. Biol Trace Elem Res 2010; 134:235-51.
    • (2010) Biol Trace Elem Res , vol.134 , pp. 235-251
    • Hawkes, W.C.1    Alkan, Z.2
  • 28
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Go YM, Jones DP. Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 2008; 1780:1273-90.
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 30
    • 65349157681 scopus 로고    scopus 로고
    • Compartmentalization of redox signaling through NADPH oxidase-derived ROS
    • Ushio-Fukai M. Compartmentalization of redox signaling through NADPH oxidase-derived ROS. Antioxid Redox Signal 2009; 11:1289-99.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1289-1299
    • Ushio-Fukai, M.1
  • 32
    • 0030746981 scopus 로고    scopus 로고
    • Redox state regulates binding of p53 to sequence-specific DNA, but not to non-specific or mismatched DNA
    • DOI 10.1093/nar/25.6.1289
    • Parks D, Bolinger R, Mann K. Redox state regulates binding of p53 to sequence-specific DNA, but not to non-specific or mismatched DNA. Nucleic Acids Res 1997; 25:1289-95. (Pubitemid 27303223)
    • (1997) Nucleic Acids Research , vol.25 , Issue.6 , pp. 1289-1295
    • Parks, D.1    Bolinger, R.2    Mann, K.3
  • 33
    • 74949091029 scopus 로고    scopus 로고
    • Oxidative stress drives disulfide bond formation between basic helix-loophelix transcription factors
    • Danciu TE, Whitman M. Oxidative stress drives disulfide bond formation between basic helix-loophelix transcription factors. J Cell Biochem 2010; 109:417-24.
    • (2010) J Cell Biochem , vol.109 , pp. 417-424
    • Danciu, T.E.1    Whitman, M.2
  • 34
    • 77957032845 scopus 로고    scopus 로고
    • Redox control of protein-DNA interactions: From molecular mechanisms to significance in signal transduction, gene expression, and DNA replication
    • Shlomai J. Redox control of protein-DNA interactions: from molecular mechanisms to significance in signal transduction, gene expression, and DNA replication. Antioxid. Redox Signal. 2010; 13:1429-1476.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1429-1476
    • Shlomai, J.1
  • 35
    • 16544369973 scopus 로고    scopus 로고
    • Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path
    • Lee C, Lee SM, Mukhopadhyay P, Kim SJ, Lee SC, Ahn WS, et al. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path. Nat Struct Mol Biol 2004; 11:1179-85.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1179-1185
    • Lee, C.1    Lee, S.M.2    Mukhopadhyay, P.3    Kim, S.J.4    Lee, S.C.5    Ahn, W.S.6
  • 36
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • DOI 10.1126/science.279.5357.1718
    • Zheng M, Aslund F, Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998; 279:1718-21. (Pubitemid 28164467)
    • (1998) Science , vol.279 , Issue.5357 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 37
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • DOI 10.1016/S0092-8674(01)00300-2
    • Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, Ryu SE. Structural basis of the redox switch in the OxyR transcription factor. Cell 2001; 105:103-13. (Pubitemid 32323920)
    • (2001) Cell , vol.105 , Issue.1 , pp. 103-113
    • Choi, H.-J.1    Kim, S.-J.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.-R.5    Storz, G.6    Ryu, S.-E.7
  • 39
    • 64649090344 scopus 로고    scopus 로고
    • Cysteine oxidation regulates the RNA-binding activity of iron regulatory protein 2
    • Zumbrennen KB, Wallander ML, Romney SJ, Leibold EA. Cysteine oxidation regulates the RNA-binding activity of iron regulatory protein 2. Mol Cell Biol 2009; 29:2219-29.
    • (2009) Mol Cell Biol , vol.29 , pp. 2219-2229
    • Zumbrennen, K.B.1    Wallander, M.L.2    Romney, S.J.3    Leibold, E.A.4
  • 40
    • 0034708674 scopus 로고    scopus 로고
    • Disulfide bond formation between RNA binding domains is used to regulate mRNA binding activity of the chloroplast poly(A)-binding protein
    • DOI 10.1074/jbc.275.12.8275
    • Fong CL, Lentz A, Mayfield SP. Disulfide bond formation between RNA binding domains is used to regulate mRNA binding activity of the chloroplast poly(A)-binding protein. J Biol Chem 2000; 275:8275-8. (Pubitemid 30180164)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.12 , pp. 8275-8278
    • Fong, C.L.1    Lentz, A.2    Mayfield, S.P.3
  • 41
    • 77950517022 scopus 로고    scopus 로고
    • The x-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible HuR redox sensing mechanism
    • Benoit RM, Meisner NC, Kallen J, Graff P, Hemmig R, Cebe R, et al. The x-ray crystal structure of the first RNA recognition motif and site-directed mutagenesis suggest a possible HuR redox sensing mechanism. J Mol Biol 2010; 397:1231-44.
    • (2010) J Mol Biol , vol.397 , pp. 1231-1244
    • Benoit, R.M.1    Meisner, N.C.2    Kallen, J.3    Graff, P.4    Hemmig, R.5    Cebe, R.6
  • 43
    • 28344450156 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein is a monomer
    • DOI 10.1261/rna.2214405
    • Monie TP, Hernandez H, Robinson CV, Simpson P, Matthews S, Curry S. The polypyrimidine tract binding protein is a monomer. RNA 2005; 11:1803-8. (Pubitemid 41720030)
    • (2005) RNA , vol.11 , Issue.12 , pp. 1803-1808
    • Monie, T.P.1    Hernandez, H.2    Robinson, C.V.3    Simpson, P.4    Matthews, S.5    Curry, S.6
  • 44
    • 72849111523 scopus 로고    scopus 로고
    • RNA-binding proteins implicated in the hypoxic response
    • Masuda K, Abdelmohsen K, Gorospe M. RNA-binding proteins implicated in the hypoxic response. J Cell Mol Med 2009; 13:2759-69.
    • (2009) J Cell Mol Med , vol.13 , pp. 2759-2769
    • Masuda, K.1    Abdelmohsen, K.2    Gorospe, M.3
  • 47
    • 28344435137 scopus 로고    scopus 로고
    • Role of elongin-binding domain of von hippel lindau gene product on HuR-mediated VPF/VEGF mRNA stability in renal cell carcinoma
    • DOI 10.1038/sj.onc.1208912, PII 1208912
    • Datta K, Mondal S, Sinha S, Li J, Wang E, Knebelmann B, et al. Role of elongin-binding domain of von Hippel Lindau gene product on HuR-mediated VPF/VEGF mRNA stability in renal cell carcinoma. Oncogene 2005; 24:7850-8. (Pubitemid 41715191)
    • (2005) Oncogene , vol.24 , Issue.53 , pp. 7850-7858
    • Datta, K.1    Mondal, S.2    Sinha, S.3    Li, J.4    Wang, E.5    Knebelmann, B.6    Karumanchi, S.A.7    Mukhopadhyay, D.8
  • 48
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-elonginC-elonginB complex: Implications for VHL tumor suppressor function
    • DOI 10.1126/science.284.5413.455
    • Stebbins CE, Kaelin WG Jr, Pavletich NP. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 1999; 284:455-61. (Pubitemid 29289612)
    • (1999) Science , vol.284 , Issue.5413 , pp. 455-461
    • Stebbins, C.E.1    Kaelin Jr., W.G.2    Pavletich, N.P.3
  • 50
    • 34250362729 scopus 로고    scopus 로고
    • Protein kinase Calpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: Implications for posttranscriptional regulation of cyclooxygenase-2
    • DOI 10.1091/mbc.E06-09-0850
    • Doller A, Huwiler A, Muller R, Radeke HH, Pfeilschifter J, Eberhardt W. Protein kinase Calpha-dependent phosphorylation of the mRNA-stabilizing factor HuR: implications for posttranscriptional regulation of cyclooxygenase-2. Mol Biol Cell 2007; 18:2137-48. (Pubitemid 46911365)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.6 , pp. 2137-2148
    • Doller, A.1    Huwiler, A.2    Muller, R.3    Radeke, H.H.4    Pfeilschifter, J.5    Eberhardt, W.6
  • 51
    • 77749334696 scopus 로고    scopus 로고
    • Tandem phosphorylation of serines 221 and 318 by protein kinase Cdelta coordinates mRNA binding and nucleocytoplasmic shuttling of HuR
    • Doller A, Schlepckow K, Schwalbe H, Pfeilschifter J, Eberhardt W. Tandem phosphorylation of serines 221 and 318 by protein kinase Cdelta coordinates mRNA binding and nucleocytoplasmic shuttling of HuR. Mol Cell Biol 2010; 30:1397-410.
    • (2010) Mol Cell Biol , vol.30 , pp. 1397-1410
    • Doller, A.1    Schlepckow, K.2    Schwalbe, H.3    Pfeilschifter, J.4    Eberhardt, W.5
  • 52
    • 28244496609 scopus 로고    scopus 로고
    • Hypoxia-induced phosphorylation of Chk2 in an ataxia telangiectasia mutated-dependent manner
    • Gibson SL, Bindra RS, Glazer P. M. Hypoxia-induced phosphorylation of Chk2 in an ataxia telangiectasia mutated-dependent manner. Cancer Res 2005; 65:10734-41.
    • (2005) Cancer Res , vol.65 , pp. 10734-10741
    • Gibson, S.L.1    Bindra, R.S.2    Glazer, P.M.3
  • 53
    • 0031427459 scopus 로고    scopus 로고
    • Chronic hypoxia induces proliferation of cultured mesangial cells: Role of calcium and protein kinase C
    • Sahai A, Mei C, Pattison TA, Tannen RL. Chronic hypoxia induces proliferation of cultured mesangial cells: role of calcium and protein kinase C. Am J Physiol 1997; 273:954-60.
    • (1997) Am J Physiol , vol.273 , pp. 954-960
    • Sahai, A.1    Mei, C.2    Pattison, T.A.3    Tannen, R.L.4
  • 55
    • 0038035142 scopus 로고    scopus 로고
    • Increased AMP:ATP ratio and AMP-activated protein kinase activity during cellular senescence linked to reduced HuR function
    • DOI 10.1074/jbc.M300318200
    • Wang W, Yang X, Lopez dSI, Carling D, Gorospe M. Increased AMP:ATP ratio and AMP-activated protein kinase activity during cellular senescence linked to reduced HuR function. J Biol Chem 2003; 278:27016-23. (Pubitemid 36876855)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 27016-27023
    • Wang, W.1    Yang, X.2    De, S.I.L.3    Carling, D.4    Gorospe, M.5
  • 56
    • 0141640857 scopus 로고    scopus 로고
    • Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2
    • DOI 10.1128/MCB.23.20.7177-7188.2003
    • Tran H, Maurer F, Nagamine Y. Stabilization of urokinase and urokinase receptor mRNAs by HuR is linked to its cytoplasmic accumulation induced by activated mitogen-activated protein kinase-activated protein kinase 2. Mol Cell Biol 2003; 23:7177-88. (Pubitemid 37211000)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.20 , pp. 7177-7188
    • Tran, H.1    Maurer, F.2    Nagamine, Y.3
  • 57
    • 0034907223 scopus 로고    scopus 로고
    • Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase
    • DOI 10.1128/MCB.21.17.5778-5789.2001
    • Ming XF, Stoecklin G, Lu M, Looser R, Moroni C. Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase. Mol Cell Biol 2001; 21:5778-89. (Pubitemid 32737795)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.17 , pp. 5778-5789
    • Ming, X.-F.1    Stoecklin, G.2    Lu, M.3    Looser, R.4    Moroni, C.5
  • 59
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • DOI 10.1038/nrm2256, PII NRM2256
    • D'Autreaux B, Toledano MB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007; 8:813-24. (Pubitemid 47462134)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 60
    • 3543095148 scopus 로고    scopus 로고
    • Monitoring disulfide bond formation in the eukaryotic cytosol
    • DOI 10.1083/jcb.200402120
    • Ostergaard H, Tachibana C, Winther JR. Monitoring disulfide bond formation in the eukaryotic cytosol. J Cell Biol 2004; 166:337-45. (Pubitemid 39031237)
    • (2004) Journal of Cell Biology , vol.166 , Issue.3 , pp. 337-345
    • Ostergaard, H.1    Tachibana, C.2    Winther, J.R.3
  • 61
    • 33646100778 scopus 로고    scopus 로고
    • A genetic redox sensor for mammalian cells
    • Weber W, Link N, Fussenegger M. A genetic redox sensor for mammalian cells. Metab Eng 2006; 8:273-80.
    • (2006) Metab Eng , vol.8 , pp. 273-280
    • Weber, W.1    Link, N.2    Fussenegger, M.3
  • 62
    • 77955301626 scopus 로고    scopus 로고
    • A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes
    • Yano T, Oku M, Akeyama N, Itoyama A, Yurimoto H, Kuge S, et al. A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes. Mol Cell Biol 2010; 30:3758-66.
    • (2010) Mol Cell Biol , vol.30 , pp. 3758-3766
    • Yano, T.1    Oku, M.2    Akeyama, N.3    Itoyama, A.4    Yurimoto, H.5    Kuge, S.6
  • 63
    • 79952214788 scopus 로고    scopus 로고
    • Quantitative Detection of the Cysteine Redox State in Vivo - The OxICAT Method
    • Das DK, ed(s). Mary Ann Liebert Inc
    • Leichert LI. Quantitative Detection of the Cysteine Redox State in Vivo - the OxICAT Method. In: Das DK, ed(s). Methods in Redox Signaling. Mary Ann Liebert Inc 2010; 63-70.
    • (2010) Methods in Redox Signaling , pp. 63-70
    • Leichert, L.I.1
  • 64
    • 58149105545 scopus 로고    scopus 로고
    • A new oxidative sensing and regulation pathway mediated by the MgrA homologue SarZ in Staphylococcus aureus
    • Chen PR, Nishida S, Poor CB, Cheng A, Bae T, Kuechenmeister L, et al. A new oxidative sensing and regulation pathway mediated by the MgrA homologue SarZ in Staphylococcus aureus. Mol Microbiol 2009; 71:198-211.
    • (2009) Mol Microbiol , vol.71 , pp. 198-211
    • Chen, P.R.1    Nishida, S.2    Poor, C.B.3    Cheng, A.4    Bae, T.5    Kuechenmeister, L.6
  • 65
    • 77950663504 scopus 로고    scopus 로고
    • Thioredoxin system modulation by plant and fungal secondary metabolites
    • Dal Piaz F, Braca A, Belisario MA, De TN. Thioredoxin system modulation by plant and fungal secondary metabolites. Curr Med Chem 2010; 17:479-94.
    • (2010) Curr Med Chem , vol.17 , pp. 479-494
    • Dal Piaz, F.1    Braca, A.2    Belisario, M.A.3    De, T.N.4
  • 66
    • 44149092895 scopus 로고    scopus 로고
    • Hypoxia in prostate cancer: A powerful shield against tumour destruction?
    • Marignol L, Coffey M, Lawler M, Hollywood D. Hypoxia in prostate cancer: a powerful shield against tumour destruction? Cancer Treat Rev 2008; 34:313-27.
    • (2008) Cancer Treat Rev , vol.34 , pp. 313-327
    • Marignol, L.1    Coffey, M.2    Lawler, M.3    Hollywood, D.4
  • 67
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Trachootham D, Alexandre J, Huang P. Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat Rev Drug Discov 2009; 8:579-91.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 68
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • Brandes N, Schmitt S, Jakob U. Thiol-based redox switches in eukaryotic proteins. Antioxid. Redox Signal. 2009; 11:997-1014.
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.