메뉴 건너뛰기




Volumn 12, Issue SUPPL. 2, 2010, Pages 116-125

Redox compartmentalization and cellular stress

Author keywords

Cysteine; Glutathione; Oxidative stress; Redox signalling; Thioredoxin

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; ARSENIC; CADMIUM; CESIUM; COPPER; CYSTEINE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEIN; IRON; MERCURY; NICKEL; PEROXIREDOXIN; PROTEIN DISULFIDE REDUCTASE (GLUTATHIONE); REACTIVE OXYGEN METABOLITE; THIOREDOXIN; THIOREDOXIN REDUCTASE; TRANSITION ELEMENT; ZINC;

EID: 77957315403     PISSN: 14628902     EISSN: 14631326     Source Type: Journal    
DOI: 10.1111/j.1463-1326.2010.01266.x     Document Type: Article
Times cited : (204)

References (75)
  • 2
    • 0036829579 scopus 로고    scopus 로고
    • Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses.
    • Jones DP, Mody VC, Carlson JL, Lynn MJ, Sternberg P. Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses. Free Radic Biol Med 2002, 33:1290-1300..
    • (2002) Free Radic Biol Med , vol.33
    • Jones, D.P.1    Mody, V.C.2    Carlson, J.L.3    Lynn, M.J.4    Sternberg, P.5
  • 3
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress.
    • Jones DP. Redefining oxidative stress. Antioxid Redox Signal 2006, 8:1865-1879..
    • (2006) Antioxid Redox Signal , vol.8
    • Jones, D.P.1
  • 4
    • 84882816411 scopus 로고    scopus 로고
    • Oxidative Stress in Encyclopedia of Stress, 2nd edn., San Diego: Elsevier
    • Sies H, Jones D. 2007, 45-48. Oxidative Stress in Encyclopedia of Stress, 2nd edn., San Diego: Elsevier
    • (2007) , pp. 45-48
    • Sies, H.1    Jones, D.2
  • 5
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells.
    • Go YM, Jones DP. Redox compartmentalization in eukaryotic cells. Biochim Biophys Acta 2008, 1780:1273-1290..
    • (2008) Biochim Biophys Acta , vol.1780
    • Go, Y.M.1    Jones, D.P.2
  • 6
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/ disulfide redox systems: a perspective on redox systems biology.
    • Kemp M, Go YM, Jones DP. Nonequilibrium thermodynamics of thiol/ disulfide redox systems: a perspective on redox systems biology. Free Radic Biol Med 2008, 44:921-937..
    • (2008) Free Radic Biol Med , vol.44
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 7
    • 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, 49:835-842..
    • (2010) Biochemistry , vol.49
    • Forman, H.J.1    Maiorino, M.2    Ursini, F.3
  • 8
    • 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. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001, 30:1191-1212..
    • (2001) Free Radic Biol Med , vol.30
    • Schafer, F.Q.1    Buettner, G.R.2
  • 9
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress.
    • Jones DP. Radical-free biology of oxidative stress. Am J Physiol Cell Physiol 2008, 295:C849-C868..
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Jones, D.P.1
  • 10
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis.
    • D'Autreaux B, Toledano MB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007, 8:813-824..
    • (2007) Nat Rev Mol Cell Biol , vol.8
    • D'Autreaux, B.1    Toledano, M.B.2
  • 11
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation.
    • Ziegler DM. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 1985, 54:305-329..
    • (1985) Annu Rev Biochem , vol.54
    • Ziegler, D.M.1
  • 12
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory.
    • Sitia R, Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 2003, 426:891-894..
    • (2003) Nature , vol.426
    • Sitia, R.1    Braakman, I.2
  • 13
    • 0016811224 scopus 로고
    • Hydroperoxide-metabolizing systems in rat liver.
    • Sies H, Summer KH. Hydroperoxide-metabolizing systems in rat liver. Eur J Biochem 1975, 57:503-512..
    • (1975) Eur J Biochem , vol.57
    • Sies, H.1    Summer, K.H.2
  • 14
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange.
    • Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 1990, 63:69-172..
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63
    • Gilbert, H.F.1
  • 16
    • 70350036051 scopus 로고    scopus 로고
    • Measuring the poise of thiol/disulfide couples in vivo.
    • Jones DP, Liang Y. Measuring the poise of thiol/disulfide couples in vivo. Free Radic Biol Med 2009, 47:1329-1338..
    • (2009) Free Radic Biol Med , vol.47
    • Jones, D.P.1    Liang, Y.2
  • 17
    • 0036372619 scopus 로고    scopus 로고
    • Redox potential of GSH/GSSG couple: assay and biological significance.
    • Jones DP. Redox potential of GSH/GSSG couple: assay and biological significance. Methods Enzymol 2002, 348:93-112..
    • (2002) Methods Enzymol , vol.348
    • Jones, D.P.1
  • 18
    • 33845936364 scopus 로고    scopus 로고
    • Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells.
    • Go YM, Ziegler TR, Johnson JM, Gu L, Hansen JM, Jones DP. Selective protection of nuclear thioredoxin-1 and glutathione redox systems against oxidation during glucose and glutamine deficiency in human colonic epithelial cells. Free Radic Biol Med 2007, 42:363-370..
    • (2007) Free Radic Biol Med , vol.42
    • Go, Y.M.1    Ziegler, T.R.2    Johnson, J.M.3    Gu, L.4    Hansen, J.M.5    Jones, D.P.6
  • 19
    • 44449090114 scopus 로고    scopus 로고
    • Real-time imaging of the intracellular glutathione redox potential.
    • Gutscher M, Pauleau AL, Marty L. Real-time imaging of the intracellular glutathione redox potential. Nat Methods 2008, 5:553-559..
    • (2008) Nat Methods , vol.5
    • Gutscher, M.1    Pauleau, A.L.2    Marty, L.3    et al4
  • 20
    • 33751509841 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin in regulation of oxidant-induced cell death.
    • Chen Y, Cai J, Jones DP. Mitochondrial thioredoxin in regulation of oxidant-induced cell death. FEBS Lett 2006, 580:6596-6602..
    • (2006) FEBS Lett , vol.580
    • Chen, Y.1    Cai, J.2    Jones, D.P.3
  • 21
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells.
    • Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 2001, 20:6288-6296..
    • (2001) EMBO J , vol.20
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 22
    • 0029006074 scopus 로고
    • Measurement of glutathione redox state in cytosol and secretory pathway of cultured cells.
    • Hwang C, Lodish HF, Sinskey AJ. Measurement of glutathione redox state in cytosol and secretory pathway of cultured cells. Methods Enzymol 1995, 251:212-221..
    • (1995) Methods Enzymol , vol.251
    • Hwang, C.1    Lodish, H.F.2    Sinskey, A.J.3
  • 23
    • 0038393058 scopus 로고    scopus 로고
    • Oxidation of nuclear thioredoxin during oxidative stress.
    • Watson WH, Jones DP. Oxidation of nuclear thioredoxin during oxidative stress. FEBS Lett 2003, 543:144-147..
    • (2003) FEBS Lett , vol.543
    • Watson, W.H.1    Jones, D.P.2
  • 24
    • 72649107557 scopus 로고    scopus 로고
    • A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential.
    • Go YM, Park H, Koval M. A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential. Free Radic Biol Med 2010, 48:275-283..
    • (2010) Free Radic Biol Med , vol.48
    • Go, Y.M.1    Park, H.2    Koval, M.3    et al4
  • 25
    • 60349113228 scopus 로고    scopus 로고
    • Quantification of redox conditions in the nucleus.
    • Go YM, Pohl J, Jones DP. Quantification of redox conditions in the nucleus. Methods Mol Biol 2009, 464:303-317..
    • (2009) Methods Mol Biol , vol.464
    • Go, Y.M.1    Pohl, J.2    Jones, D.P.3
  • 26
    • 46149125288 scopus 로고    scopus 로고
    • Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.
    • Leichert LI, Gehrke F, Gudiseva HV. Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc Natl Acad Sci U S A 2008, 105:8197-8202..
    • (2008) Proc Natl Acad Sci U S A , vol.105
    • Leichert, L.I.1    Gehrke, F.2    Gudiseva, H.V.3    et al4
  • 27
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity.
    • Xanthoudakis S, Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J 1992, 11:653-665..
    • (1992) EMBO J , vol.11
    • Xanthoudakis, S.1    Curran, T.2
  • 28
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen.
    • Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev 2004, 4:181-189..
    • (2004) Nat Rev , vol.4
    • Lambeth, J.D.1
  • 29
    • 1242316987 scopus 로고    scopus 로고
    • H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1.
    • Go YM, Gipp JJ, Mulcahy RT, Jones DP. H2O2-dependent activation of GCLC-ARE4 reporter occurs by mitogen-activated protein kinase pathways without oxidation of cellular glutathione or thioredoxin-1. J Biol Chem 2004, 279:5837-5845..
    • (2004) J Biol Chem , vol.279
    • Go, Y.M.1    Gipp, J.J.2    Mulcahy, R.T.3    Jones, D.P.4
  • 30
    • 14844298802 scopus 로고    scopus 로고
    • Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling.
    • Halvey PJ, Watson WH, Hansen JM, Go YM, Samali A, Jones DP. Compartmental oxidation of thiol-disulphide redox couples during epidermal growth factor signalling. Biochem J 2005, 386:215-219..
    • (2005) Biochem J , vol.386
    • Halvey, P.J.1    Watson, W.H.2    Hansen, J.M.3    Go, Y.M.4    Samali, A.5    Jones, D.P.6
  • 31
    • 8444228527 scopus 로고    scopus 로고
    • Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1.
    • Hansen JM, Watson WH, Jones DP. Compartmentation of Nrf-2 redox control: regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol Sci 2004, 82:308-317..
    • (2004) Toxicol Sci , vol.82
    • Hansen, J.M.1    Watson, W.H.2    Jones, D.P.3
  • 32
    • 33744809562 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-alpha-induced reactive oxygen species generation, NF-kappaB activation, and apoptosis.
    • Hansen JM, Zhang H, Jones DP. Mitochondrial thioredoxin-2 has a key role in determining tumor necrosis factor-alpha-induced reactive oxygen species generation, NF-kappaB activation, and apoptosis. Toxicol Sci 2006, 91:643-650..
    • (2006) Toxicol Sci , vol.91
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 33
    • 29144496897 scopus 로고    scopus 로고
    • Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfide-based antibody-drug conjugates.
    • Austin CD, Wen X, Gazzard L, Nelson C, Scheller RH, Scales SJ. Oxidizing potential of endosomes and lysosomes limits intracellular cleavage of disulfide-based antibody-drug conjugates. Proceedings Natl Acad Sci U S A 2005, 102:17987-17992..
    • (2005) Proceedings Natl Acad Sci U S A , vol.102
    • Austin, C.D.1    Wen, X.2    Gazzard, L.3    Nelson, C.4    Scheller, R.H.5    Scales, S.J.6
  • 34
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum.
    • Hwang C, Sinskey AJ, Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 1992, 257:1496-1502..
    • (1992) Science , vol.257
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 35
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.
    • Chakravarthi S, Jessop CE, Bulleid NJ. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep 2006, 7:271-275..
    • (2006) EMBO Rep , vol.7
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 36
    • 9444243245 scopus 로고    scopus 로고
    • Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control.
    • Jones DP, Go YM, Anderson CL, Ziegler TR, Kinkade JM, Kirlin WG. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J 2004, 18:1246-1248..
    • (2004) FASEB J , vol.18
    • Jones, D.P.1    Go, Y.M.2    Anderson, C.L.3    Ziegler, T.R.4    Kinkade, J.M.5    Kirlin, W.G.6
  • 37
    • 0023274831 scopus 로고
    • Effect of chronic ethanol feeding on rat hepatocytic glutathione. Compartmentation, efflux, and response to incubation with ethanol.
    • Fernandez-Checa JC, Ookhtens M, Kaplowitz N. Effect of chronic ethanol feeding on rat hepatocytic glutathione. Compartmentation, efflux, and response to incubation with ethanol. J Clin Invest 1987, 80:57-62..
    • (1987) J Clin Invest , vol.80
    • Fernandez-Checa, J.C.1    Ookhtens, M.2    Kaplowitz, N.3
  • 39
    • 0037031939 scopus 로고    scopus 로고
    • Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells.
    • Chen Y, Cai J, Murphy TJ, Jones DP. Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J Biol Chem 2002, 277:33242-33248..
    • (2002) J Biol Chem , vol.277
    • Chen, Y.1    Cai, J.2    Murphy, T.J.3    Jones, D.P.4
  • 41
    • 0034544555 scopus 로고    scopus 로고
    • Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation.
    • Wei SJ, Botero A, Hirota K. Thioredoxin nuclear translocation and interaction with redox factor-1 activates the activator protein-1 transcription factor in response to ionizing radiation. Cancer Res 2000, 60:6688-6695..
    • (2000) Cancer Res , vol.60
    • Wei, S.J.1    Botero, A.2    Hirota, K.3    et al4
  • 42
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling.
    • Rhee SG, Chae HZ, Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 2005, 38:1543-1552..
    • (2005) Free Radic Biol Med , vol.38
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 44
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions.
    • Hansen JM, Zhang H, Jones DP. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 2006, 40:138-145..
    • (2006) Free Radic Biol Med , vol.40
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 45
    • 2942696470 scopus 로고    scopus 로고
    • Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner.
    • Zhang R, Al-Lamki R, Bai L. Thioredoxin-2 inhibits mitochondria-located ASK1-mediated apoptosis in a JNK-independent manner. Circ Res 2004, 94:1483-1491..
    • (2004) Circ Res , vol.94
    • Zhang, R.1    Al-Lamki, R.2    Bai, L.3    et al4
  • 46
    • 0032521155 scopus 로고    scopus 로고
    • Glutathione in human plasma: decline in association with aging, age-related macular degeneration, and diabetes.
    • Samiec PS, Drews-Botsch C, Flagg EW. Glutathione in human plasma: decline in association with aging, age-related macular degeneration, and diabetes. Free Radic Biol Med 1998, 24:699-704..
    • (1998) Free Radic Biol Med , vol.24
    • Samiec, P.S.1    Drews-Botsch, C.2    Flagg, E.W.3    et al4
  • 47
    • 77957297487 scopus 로고    scopus 로고
    • Redox clamp model for study of extracellular thiols and disulfides in redox signaling.
    • Go Y-M, Jones DP. Redox clamp model for study of extracellular thiols and disulfides in redox signaling. Methods Enzymol 2010, 474:165-179.
    • (2010) Methods Enzymol , vol.474 , pp. 165-179
    • Go, Y.-.M.1    Jones, D.P.2
  • 48
    • 20444499841 scopus 로고    scopus 로고
    • Intracellular proatherogenic events and cell adhesion modulated by extracellular thiol/disulfide redox state.
    • Go YM, Jones DP. Intracellular proatherogenic events and cell adhesion modulated by extracellular thiol/disulfide redox state. Circulation 2005, 111:2973-2980..
    • (2005) Circulation , vol.111
    • Go, Y.M.1    Jones, D.P.2
  • 49
    • 74949087000 scopus 로고    scopus 로고
    • Gene and protein responses of human monocytes to extracellular cysteine redox potential.
    • Go YM, Craige SE, Orr M, Gernert KM, Jones DP. Gene and protein responses of human monocytes to extracellular cysteine redox potential. Toxicol Sci 2009, 112:354-362..
    • (2009) Toxicol Sci , vol.112
    • Go, Y.M.1    Craige, S.E.2    Orr, M.3    Gernert, K.M.4    Jones, D.P.5
  • 50
    • 63449096561 scopus 로고    scopus 로고
    • Cysteine redox potential determines pro-inflammatory IL-1beta levels.
    • Iyer SS, Accardi CJ, Ziegler TR. Cysteine redox potential determines pro-inflammatory IL-1beta levels. PLoS One 2009, 4:e5017..
    • (2009) PLoS One , vol.4
    • Iyer, S.S.1    Accardi, C.J.2    Ziegler, T.R.3    et al4
  • 52
    • 35348921812 scopus 로고    scopus 로고
    • Extracellular cysteine/cystine redox potential controls lung fibroblast proliferation and matrix expression through upregulation of transforming growth factor-beta.
    • Ramirez A, Ramadan B, Ritzenthaler JD, Rivera HN, Jones DP, Roman J. Extracellular cysteine/cystine redox potential controls lung fibroblast proliferation and matrix expression through upregulation of transforming growth factor-beta. Am J Physiol Lung Cell Mol Physiol 2007, 293:L972-L981..
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.293
    • Ramirez, A.1    Ramadan, B.2    Ritzenthaler, J.D.3    Rivera, H.N.4    Jones, D.P.5    Roman, J.6
  • 53
    • 67650936587 scopus 로고    scopus 로고
    • Reductive stress on life span extension in C. elegans.
    • Ralser M, Benjamin IJ. Reductive stress on life span extension in C. elegans. BMC Res Notes 2008, 1:19..
    • (2008) BMC Res Notes , vol.1
    • Ralser, M.1    Benjamin, I.J.2
  • 54
    • 0035036447 scopus 로고    scopus 로고
    • Electrophilic methyl groups present in the diet ameliorate pathological states induced by reductive and oxidative stress: a hypothesis.
    • Ghyczy M, Boros M. Electrophilic methyl groups present in the diet ameliorate pathological states induced by reductive and oxidative stress: a hypothesis. Br J Nutr 2001, 85:409-414..
    • (2001) Br J Nutr , vol.85
    • Ghyczy, M.1    Boros, M.2
  • 55
    • 34547681313 scopus 로고    scopus 로고
    • Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice.
    • Rajasekaran NS, Connell P, Christians ES. Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in mice. Cell 2007, 130:427-439..
    • (2007) Cell , vol.130
    • Rajasekaran, N.S.1    Connell, P.2    Christians, E.S.3    et al4
  • 56
    • 37549072681 scopus 로고    scopus 로고
    • Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress.
    • Ralser M, Wamelink MM, Kowald A. Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. J Biol 2007, 6:10..
    • (2007) J Biol , vol.6
    • Ralser, M.1    Wamelink, M.M.2    Kowald, A.3    et al4
  • 57
    • 0000862210 scopus 로고
    • Cellular oxygen requirements.
    • Chance B. Cellular oxygen requirements. Fed Proc 1957, 16:671-680..
    • (1957) Fed Proc , vol.16
    • Chance, B.1
  • 58
    • 0021325445 scopus 로고
    • The crucial role of hypoxia in halothane-induced lipid peroxidation.
    • de Groot H, Noll T. The crucial role of hypoxia in halothane-induced lipid peroxidation. Biochem Biophys Res Commun 1984, 119:139-143..
    • (1984) Biochem Biophys Res Commun , vol.119
    • de Groot, H.1    Noll, T.2
  • 60
    • 0019956167 scopus 로고
    • Nitroimidazoles as anaerobic electron acceptors for xanthine oxidase.
    • Clarke ED, Goulding KH, Wardman P. Nitroimidazoles as anaerobic electron acceptors for xanthine oxidase. Biochem Pharmacol 1982, 31:3237-3242..
    • (1982) Biochem Pharmacol , vol.31
    • Clarke, E.D.1    Goulding, K.H.2    Wardman, P.3
  • 62
    • 0344851909 scopus 로고    scopus 로고
    • Glutamine and KGF each regulate extracellular thiol/disulfide redox and enhance proliferation in Caco-2 cells.
    • Jonas CR, Gu LH, Nkabyo YS. Glutamine and KGF each regulate extracellular thiol/disulfide redox and enhance proliferation in Caco-2 cells. Am J Physiol 2003, 285:R1421-R1429..
    • (2003) Am J Physiol , vol.285
    • Jonas, C.R.1    Gu, L.H.2    Nkabyo, Y.S.3    et al4
  • 63
    • 0036890251 scopus 로고    scopus 로고
    • Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line.
    • Jonas CR, Ziegler TR, Gu LH, Jones DP. Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line. Free Radic Biol Med 2002, 33:1499-1506..
    • (2002) Free Radic Biol Med , vol.33
    • Jonas, C.R.1    Ziegler, T.R.2    Gu, L.H.3    Jones, D.P.4
  • 64
    • 21744459518 scopus 로고    scopus 로고
    • Extracellular cysteine/cystine redox regulates the p44/p42 MAPK pathway by metalloproteinase-dependent epidermal growth factor receptor signaling.
    • Nkabyo YS, Go YM, Ziegler TR, Jones DP. Extracellular cysteine/cystine redox regulates the p44/p42 MAPK pathway by metalloproteinase-dependent epidermal growth factor receptor signaling. Am J Physiol Gastrointest Liver Physiol 2005, 289:G70-G78..
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.289
    • Nkabyo, Y.S.1    Go, Y.M.2    Ziegler, T.R.3    Jones, D.P.4
  • 66
    • 0032882988 scopus 로고    scopus 로고
    • Dietary compounds that induce cancer preventive phase 2 enzymes activate apoptosis at comparable doses in HT29 colon carcinoma cells.
    • Kirlin WG, Cai J, DeLong MJ, Patten EJ, Jones DP. Dietary compounds that induce cancer preventive phase 2 enzymes activate apoptosis at comparable doses in HT29 colon carcinoma cells. J Nutr 1999, 129:1827-1835..
    • (1999) J Nutr , vol.129
    • Kirlin, W.G.1    Cai, J.2    DeLong, M.J.3    Patten, E.J.4    Jones, D.P.5
  • 67
    • 0026564310 scopus 로고
    • Bidirectional mechanism of plasma membrane transport of reduced glutathione in intact rat hepatocytes and membrane vesicles.
    • Garcia-Ruiz C, Fernandez-Checa JC, Kaplowitz N. Bidirectional mechanism of plasma membrane transport of reduced glutathione in intact rat hepatocytes and membrane vesicles. J Biol Chem 1992, 267:22256-22264..
    • (1992) J Biol Chem , vol.267
    • Garcia-Ruiz, C.1    Fernandez-Checa, J.C.2    Kaplowitz, N.3
  • 68
    • 33750011601 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport: physiological, pathological and toxicological implications.
    • Lash LH. Mitochondrial glutathione transport: physiological, pathological and toxicological implications. Chem-Biol Interact 2006, 163:54-67..
    • (2006) Chem-Biol Interact , vol.163
    • Lash, L.H.1
  • 70
    • 0029912351 scopus 로고    scopus 로고
    • ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump.
    • Leier I, Jedlitschky G, Buchholz U. ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump. Biochem J 1996, 314:433-437..
    • (1996) Biochem J , vol.314
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    et al4
  • 71
    • 0021288857 scopus 로고
    • Glutathione disulfide (GSSG) efflux from cells and tissues.
    • Sies H, Akerboom TP. Glutathione disulfide (GSSG) efflux from cells and tissues. Methods Enzymol 1984, 105:445-451..
    • (1984) Methods Enzymol , vol.105
    • Sies, H.1    Akerboom, T.P.2
  • 73
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells.
    • Bannai S. Transport of cystine and cysteine in mammalian cells. Biochim Biophys Acta 1984, 779:289-306..
    • (1984) Biochim Biophys Acta , vol.779
    • Bannai, S.1
  • 74
    • 43449106831 scopus 로고    scopus 로고
    • Redox proteomics: understanding oxidative stress in the progression of age-related neurodegenerative disorders.
    • Butterfield DA, Sultana R. Redox proteomics: understanding oxidative stress in the progression of age-related neurodegenerative disorders. Expert Rev Proteomics 2008, 5:157-160..
    • (2008) Expert Rev Proteomics , vol.5
    • Butterfield, D.A.1    Sultana, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.