메뉴 건너뛰기




Volumn 10, Issue 2, 2013, Pages 185-194

Computational insights into the role of glutathione in oxidative stress

Author keywords

Biotransport models; Glutathione peroxidase; Glutathione reductase; Hydrogen peroxide; Kinetic models; Nitrosylation; Protein s glutathionylation

Indexed keywords

GLUTATHIONE; HYDROGEN PEROXIDE; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE;

EID: 84879802374     PISSN: 15672026     EISSN: 18755739     Source Type: Journal    
DOI: 10.2174/1567202611310020011     Document Type: Review
Times cited : (56)

References (144)
  • 2
    • 39049169272 scopus 로고    scopus 로고
    • Modulation of neuro-inflammation and vascular response by oxidative stress following cerebral ischemia-reperfusion injury
    • Wong CH, Crack PJ. Modulation of neuro-inflammation and vascular response by oxidative stress following cerebral ischemia-reperfusion injury. Curr Med Chem. 2008;15(1):1-14.
    • (2008) Curr Med Chem. , vol.15 , Issue.1 , pp. 1-14
    • Wong, C.H.1    Crack, P.J.2
  • 3
    • 84873033865 scopus 로고    scopus 로고
    • Vascular factors and mitochondrial dysfunction: A central role in the pathogenesis of Alzheimer's disease
    • Nov 12
    • Orsucci D, Mancuso M, Ienco EC, Simoncini C, Siciliano G, Bonuccelli U. Vascular Factors and Mitochondrial Dysfunction: a Central Role in the Pathogenesis of Alzheimer's Disease. Curr Neurovasc Res. 2013 Nov 12;10(1):76-80
    • (2013) Curr Neurovasc Res. , vol.10 , Issue.1 , pp. 76-80
    • Orsucci, D.1    Mancuso, M.2    Ienco, E.C.3    Simoncini, C.4    Siciliano, G.5    Bonuccelli, U.6
  • 4
    • 33847146814 scopus 로고    scopus 로고
    • Oxidative stress biology and cell injury during type 1 and type 2 diabetes mellitus
    • Feb
    • Maiese K, Morhan SD, Chong ZZ. Oxidative stress biology and cell injury during type 1 and type 2 diabetes mellitus. Curr Neurovasc Res. 2007 Feb;4(1):63-71.
    • (2007) Curr Neurovasc Res. , vol.4 , Issue.1 , pp. 63-71
    • Maiese, K.1    Morhan, S.D.2    Chong, Z.Z.3
  • 5
    • 33645765312 scopus 로고    scopus 로고
    • Diabetes and mitochondrial function: Role of hyperglycemia and oxidative stress
    • Apr 15
    • Rolo AP, Palmeira CM. Diabetes and mitochondrial function: role of hyperglycemia and oxidative stress. Toxicol Appl Pharmacol. 2006 Apr 15;212(2):167-78.
    • (2006) Toxicol Appl Pharmacol. , vol.212 , Issue.2 , pp. 167-178
    • Rolo, A.P.1    Palmeira, C.M.2
  • 6
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • Jul
    • Trachootham D, Alexandre J, Huang P. Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat Rev Drug Discov. 2009 Jul;8(7):579-91.
    • (2009) Nat Rev Drug Discov. , vol.8 , Issue.7 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 8
    • 33745193908 scopus 로고    scopus 로고
    • Redox signaling in hypertension
    • Jul 15;
    • Paravicini TM, Touyz RM. Redox signaling in hypertension. Cardiovasc Res. 2006 Jul 15;71(2):247-58.
    • (2006) Cardiovasc Res. , vol.71 , Issue.2 , pp. 247-258
    • Paravicini, T.M.1    Touyz, R.M.2
  • 10
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: Overview of its protective roles, measurement, and biosynthesis
    • Feb-Apr
    • Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med. 2009 Feb-Apr;30(1-2):1- 12.
    • (2009) Mol Aspects Med. , vol.30 , Issue.1-2 , pp. 1-12
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 12
    • 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 , pp. 93-112
    • Jones, D.P.1
  • 13
    • 79851516092 scopus 로고    scopus 로고
    • Measurement of oxidized/reduced glutathione ratio
    • Owen JB, Butterfield DA. Measurement of oxidized/reduced glutathione ratio. Methods Mol Biol. 2010;648:269-77.
    • (2010) Methods Mol Biol. , vol.648 , pp. 269-277
    • Owen, J.B.1    Butterfield, D.A.2
  • 15
    • 80054938849 scopus 로고    scopus 로고
    • Gain and loss of function for glutathione syn thesis: Impact on advanced atherosclerosis in apolipoprotein E-deficient mice
    • Nov
    • Callegari A, Liu Y, White CC, Chait A, Gough P, Raines EW, et al. Gain and loss of function for glutathione synthesis: impact on advanced atherosclerosis in apolipoprotein E-deficient mice. Arterioscler Thromb Vasc Biol. 2011 Nov;31(11):2473-82.
    • (2011) Arterioscler Thromb Vasc Biol. , vol.31 , Issue.11 , pp. 2473-2482
    • Callegari, A.1    Liu, Y.2    White, C.C.3    Chait, A.4    Gough, P.5    Raines, E.W.6
  • 17
    • 84868107510 scopus 로고    scopus 로고
    • Dysregulation of glutathione homeostasis in neurodegenerative diseases
    • Johnson WM, Wilson-Delfosse AL, Mieyal JJ. Dysregulation of glutathione homeostasis in neurodegenerative diseases. Nutrients. 2012;4(10):1399-440.
    • (2012) Nutrients. , vol.4 , Issue.10 , pp. 1399-1440
    • Johnson, W.M.1    Wilson-Delfosse, A.L.2    Mieyal, J.J.3
  • 18
    • 79953715374 scopus 로고    scopus 로고
    • Glutathione in cancer cell death
    • Ortega AL, Mena S, Estrela JM. Glutathione in cancer cell death. Cancers. 2011;3(1):1285-310.
    • (2011) Cancers. , vol.3 , Issue.1 , pp. 1285-1310
    • Ortega, A.L.1    Mena, S.2    Estrela, J.M.3
  • 19
    • 51249104026 scopus 로고    scopus 로고
    • Pro-oxidant shift in glutathione redox state during aging
    • Oct-Nov
    • Rebrin I, Sohal RS. Pro-oxidant shift in glutathione redox state during aging. Adv Drug Deliv Rev. 2008 Oct-Nov;60(13-14):1545-52.
    • (2008) Adv Drug Deliv Rev. , vol.60 , Issue.13-14 , pp. 1545-1552
    • Rebrin, I.1    Sohal, R.S.2
  • 20
    • 80052000670 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 in health and disease: From molecular mechanisms to therapeutic opportunities
    • Oct 1
    • Lubos E, Loscalzo J, Handy DE. Glutathione peroxidase-1 in health and disease: from molecular mechanisms to therapeutic opportunities. Antioxid Redox Signal. 2011 Oct 1;15(7):1957-97.
    • (2011) Antioxid Redox Signal. , vol.15 , Issue.7 , pp. 1957-1997
    • Lubos, E.1    Loscalzo, J.2    Handy, D.E.3
  • 21
    • 79954599366 scopus 로고    scopus 로고
    • S-glutathionylation: From molecular mechanisms to health outcomes
    • Jul 1
    • Xiong Y, Uys JD, Tew KD, Townsend DM. S-glutathionylation: from molecular mechanisms to health outcomes. Antioxid Redox Signal. 2011 Jul 1;15(1):233-70.
    • (2011) Antioxid Redox Signal. , vol.15 , Issue.1 , pp. 233-270
    • Xiong, Y.1    Uys, J.D.2    Tew, K.D.3    Townsend, D.M.4
  • 22
    • 84862556342 scopus 로고    scopus 로고
    • Enzymatic mechanisms regulating protein S-nitrosylation: Implications in health and disease
    • Mar
    • Anand P, Stamler JS. Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease. J Mol Med (Berl). 2012 Mar;90(3):233-44.
    • (2012) J Mol Med (Berl). , vol.90 , Issue.3 , pp. 233-244
    • Anand, P.1    Stamler, J.S.2
  • 24
    • 84962420719 scopus 로고    scopus 로고
    • Glutathione radical: Intramolecular H abstraction by the thiyl radical
    • Rauk A, Armstrong DA, Berges J. Glutathione radical: Intramolecular H abstraction by the thiyl radical. Canadian Journal of Chemistry. 2001;79(4):405.
    • (2001) Canadian Journal of Chemistry. , vol.79 , Issue.4 , pp. 405
    • Rauk, A.1    Armstrong, D.A.2    Berges, J.3
  • 25
    • 84864022828 scopus 로고    scopus 로고
    • Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: An experimental-computational study
    • Jun
    • Aon MA, Stanley BA, Sivakumaran V, et al. Glutathione/thioredoxin systems modulate mitochondrial H2O2 emission: an experimental-computational study. J Gen Physiol. 2012 Jun;139(6):479-91.
    • (2012) J Gen Physiol. , vol.139 , Issue.6 , pp. 479-491
    • Aon, M.A.1    Stanley, B.A.2    Sivakumaran, V.3
  • 26
    • 77954935933 scopus 로고    scopus 로고
    • A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses
    • Sep 15
    • Adimora NJ, Jones DP, Kemp ML. A model of redox kinetics implicates the thiol proteome in cellular hydrogen peroxide responses. Antioxid Redox Signal. 2010 Sep 15;13(6):731-43.
    • (2010) Antioxid Redox Signal. , vol.13 , Issue.6 , pp. 731-743
    • Adimora, N.J.1    Jones, D.P.2    Kemp, M.L.3
  • 27
    • 33144490305 scopus 로고    scopus 로고
    • Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling
    • Hansen JM, Go YM, Jones DP. Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling. Annu Rev Pharmacol Toxicol. 2006;46:215-34.
    • (2006) Annu Rev Pharmacol Toxicol. , vol.46 , pp. 215-234
    • Hansen, J.M.1    Go, Y.M.2    Jones, D.P.3
  • 28
    • 0027274778 scopus 로고
    • Glutathione metabolism in primary astrocyte cultures: Flow cytometric evidence of heterogeneous distribution of GSH content
    • Aug 6
    • Devesa A, O'Connor JE, Garcia C, Puertes IR, Vina JR. Glutathione metabolism in primary astrocyte cultures: flow cytometric evidence of heterogeneous distribution of GSH content. Brain Res. 1993 Aug 6;618(2):181-9.
    • (1993) Brain Res. , vol.618 , Issue.2 , pp. 181-189
    • Devesa, A.1    O'Connor, J.E.2    Garcia, C.3    Puertes, I.R.4    Vina, J.R.5
  • 29
    • 84856086570 scopus 로고    scopus 로고
    • The contribution of oxidative stress to drug-induced organ toxicity and its detection in vitro and in vivo
    • Feb
    • Pereira CV, Nadanaciva S, Oliveira PJ, Will Y. The contribution of oxidative stress to drug-induced organ toxicity and its detection in vitro and in vivo. Expert Opin Drug Metab Toxicol. 2012 Feb;8(2):219-37.
    • (2012) Expert Opin Drug Metab Toxicol. , vol.8 , Issue.2 , pp. 219-237
    • Pereira, C.V.1    Nadanaciva, S.2    Oliveira, P.J.3    Will, Y.4
  • 30
    • 84555189342 scopus 로고    scopus 로고
    • Mathematical and computational models of oxidative and nitrosative stress
    • Kavdia M. Mathematical and computational models of oxidative and nitrosative stress. Crit Rev Biomed Eng. 2011;39(5):461-72.
    • (2011) Crit Rev Biomed Eng. , vol.39 , Issue.5 , pp. 461-472
    • Kavdia, M.1
  • 31
    • 57649183723 scopus 로고    scopus 로고
    • Impact of superoxide dismutase on nitric oxide and peroxynitrite levels in the microcirculation-a computational model
    • Chavez MD, Lakshmanan N, Kavdia M. Impact of superoxide dismutase on nitric oxide and peroxynitrite levels in the microcirculation-a computational model. Conf Proc IEEE Eng Med Biol Soc. 2007;2007:1022-6.
    • (2007) Conf Proc IEEE Eng Med Biol Soc. , vol.2007 , pp. 1022-1026
    • Chavez, M.D.1    Lakshmanan, N.2    Kavdia, M.3
  • 32
    • 33746853424 scopus 로고    scopus 로고
    • A computational model for free radicals transport in the microcirculation
    • Jul-Aug
    • Kavdia M. A computational model for free radicals transport in the microcirculation. Antioxid Redox Signal. 2006 Jul-Aug;8(7-8):1103-11.
    • (2006) Antioxid Redox Signal. , vol.8 , Issue.7-8 , pp. 1103-1111
    • Kavdia, M.1
  • 33
    • 0035990855 scopus 로고    scopus 로고
    • Free radical profiles in an encapsulated pancreatic cell matrix model
    • May
    • Kavdia M, Lewis RS. Free radical profiles in an encapsulated pancreatic cell matrix model. Ann Biomed Eng. 2002 May;30(5):721-30.
    • (2002) Ann Biomed Eng. , vol.30 , Issue.5 , pp. 721-730
    • Kavdia, M.1    Lewis, R.S.2
  • 34
    • 0033621724 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite effects on the insulin secretion and viability of betaTC3 cells
    • Jan
    • Kavdia M, Stanfield JL, Lewis RS. Nitric oxide, superoxide, and peroxynitrite effects on the insulin secretion and viability of betaTC3 cells. Ann Biomed Eng. 2000 Jan;28(1):102-9.
    • (2000) Ann Biomed Eng. , vol.28 , Issue.1 , pp. 102-109
    • Kavdia, M.1    Stanfield, J.L.2    Lewis, R.S.3
  • 35
    • 84868309300 scopus 로고    scopus 로고
    • Impact of SOD in eNOS uncoupling: A two-edged sword between hydrogen peroxide and peroxynitrite
    • Dec
    • Kar S, Bhandar B, Kavdia M. Impact of SOD in eNOS uncoupling: a two-edged sword between hydrogen peroxide and peroxynitrite. Free Radic Res. 2012 Dec;46(12):1496-513.
    • (2012) Free Radic Res. , vol.46 , Issue.12 , pp. 1496-1513
    • Kar, S.1    Bhandar, B.2    Kavdia, M.3
  • 36
    • 84878509841 scopus 로고    scopus 로고
    • Analysis of kinetics of dihydroethidium fluorescence with superoxide using xanthine oxidase and hypoxanthine assay
    • Sep 11
    • Chen J, Rogers SC, Kavdia M. Analysis of Kinetics of Dihydroethidium Fluorescence with Superoxide Using Xanthine Oxidase and Hypoxanthine Assay. Ann Biomed Eng. 2013 Sep 11;41(2):327-37.
    • (2013) Ann Biomed Eng. , vol.41 , Issue.2 , pp. 327-337
    • Chen, J.1    Rogers, S.C.2    Kavdia, M.3
  • 37
    • 84862255347 scopus 로고    scopus 로고
    • Local oxidative and nitrosative stress increases in the microcirculation during leukocytes-endothelial cell interactions
    • Kar S, Kavdia M. Local oxidative and nitrosative stress increases in the microcirculation during leukocytes-endothelial cell interactions. PLoS One. 2012;7(6):e38912.
    • (2012) PLoS One. , vol.7 , Issue.6
    • Kar, S.1    Kavdia, M.2
  • 38
    • 80052268768 scopus 로고    scopus 로고
    • Modeling of biopterin-dependent pathways of eNOS for nitric oxide and superoxide production
    • Oct 1
    • Kar S, Kavdia M. Modeling of biopterin-dependent pathways of eNOS for nitric oxide and superoxide production. Free Radic Biol Med. 2011 Oct 1;51(7):1411-27.
    • (2011) Free Radic Biol Med. , vol.51 , Issue.7 , pp. 1411-1427
    • Kar, S.1    Kavdia, M.2
  • 39
    • 68349135431 scopus 로고    scopus 로고
    • NO/peroxynitrite dynamics of high glucose-exposed HUVECs: Chemiluminescent measurement and computational model
    • Sep
    • Potdar S, Kavdia M. NO/peroxynitrite dynamics of high glucose-exposed HUVECs: chemiluminescent measurement and computational model. Microvasc Res. 2009 Sep;78(2):191-8.
    • (2009) Microvasc Res. , vol.78 , Issue.2 , pp. 191-198
    • Potdar, S.1    Kavdia, M.2
  • 40
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • Sep-Oct
    • Jones DP. Redefining oxidative stress. Antioxid Redox Signal. 2006 Sep-Oct;8(9-10):1865-79.
    • (2006) Antioxid Redox Signal. , vol.8 , Issue.9-10 , pp. 1865-1879
    • Jones, D.P.1
  • 42
    • 80052675856 scopus 로고    scopus 로고
    • Oxidative toxicity in neurodegenerative diseases: Role of mitochondrial dysfunction and therapeutic strategies
    • Facecchia K, Fochesato LA, Ray SD, Stohs SJ, Pandey S. Oxidative toxicity in neurodegenerative diseases: role of mitochondrial dysfunction and therapeutic strategies. J Toxicol. 2011;2011:683728.
    • (2011) J Toxicol. , vol.2011 , pp. 683728
    • Facecchia, K.1    Fochesato, L.A.2    Ray, S.D.3    Stohs, S.J.4    Pandey, S.5
  • 43
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Apr 13
    • Veal EA, Day AM, Morgan BA. Hydrogen peroxide sensing and signaling. Mol Cell. 2007 Apr 13;26(1):1-14.
    • (2007) Mol Cell. , vol.26 , Issue.1 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 44
    • 43749092334 scopus 로고    scopus 로고
    • Intracellular redox status and oxidative stress: Implications for cell proliferation, apoptosis, and carcinogenesis
    • May
    • Mates JM, Segura JA, Alonso FJ, Marquez J. Intracellular redox status and oxidative stress: implications for cell proliferation, apoptosis, and carcinogenesis. Arch Toxicol. 2008 May;82(5):273-99.
    • (2008) Arch Toxicol. , vol.82 , Issue.5 , pp. 273-299
    • Mates, J.M.1    Segura, J.A.2    Alonso, F.J.3    Marquez, J.4
  • 45
    • 77953434349 scopus 로고    scopus 로고
    • Transient glutathione depletion determines terminal differentiation in HL-60 cells
    • Jan-Feb
    • Krance SM, Keng PC, Palis J, Ballatori N. Transient glutathione depletion determines terminal differentiation in HL-60 cells. Oxid Med Cell Longev. 2010 Jan-Feb;3(1):53-60.
    • (2010) Oxid Med Cell Longev. , vol.3 , Issue.1 , pp. 53-60
    • Krance, S.M.1    Keng, P.C.2    Palis, J.3    Ballatori, N.4
  • 46
    • 70349172938 scopus 로고    scopus 로고
    • Apoptosis and glutathione: Beyond an antioxidant
    • Oct
    • Franco R, Cidlowski JA. Apoptosis and glutathione: beyond an antioxidant. Cell Death Differ. 2009 Oct;16(10):1303-14.
    • (2009) Cell Death Differ. , vol.16 , Issue.10 , pp. 1303-1314
    • Franco, R.1    Cidlowski, J.A.2
  • 47
    • 0242290219 scopus 로고    scopus 로고
    • Cellular redox: A modulator of intestinal epithelial cell proliferation
    • Oct
    • Aw TY. Cellular redox: a modulator of intestinal epithelial cell proliferation. News Physiol Sci. 2003 Oct;18:201-4.
    • (2003) News Physiol Sci. , vol.18 , pp. 201-204
    • Aw, T.Y.1
  • 48
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Nov
    • Griffith OW. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med. 1999 Nov;27(9-10):922-35.
    • (1999) Free Radic Biol Med. , vol.27 , Issue.9-10 , pp. 922-935
    • Griffith, O.W.1
  • 49
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Jun 1
    • 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 Jun 1;30(11):1191-212.
    • (2001) Free Radic Biol Med. , vol.30 , Issue.11 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 50
    • 77953809992 scopus 로고    scopus 로고
    • Redox-optimized ROS balance: A unifying hypothesis
    • Jun-Jul
    • Aon MA, Cortassa S, O'Rourke B. Redox-optimized ROS balance: a unifying hypothesis. Biochim Biophys Acta. 2010 Jun-Jul;1797(6-7):865-77.
    • (2010) Biochim Biophys Acta. , vol.1797 , Issue.6-7 , pp. 865-877
    • Aon, M.A.1    Cortassa, S.2    O'Rourke, B.3
  • 51
    • 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 , pp. 69-172
    • Gilbert, H.F.1
  • 52
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • Oct
    • D'Autreaux B, Toledano MB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol. 2007 Oct;8(10):813-24.
    • (2007) Nat Rev Mol Cell Biol. , vol.8 , Issue.10 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 53
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Aug
    • Gallogly MM, Mieyal JJ. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol. 2007 Aug;7(4):381-91.
    • (2007) Curr Opin Pharmacol. , vol.7 , Issue.4 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 54
    • 0030592716 scopus 로고    scopus 로고
    • Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione
    • Nov 18
    • MartinezChantar ML, Pajares MA. Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione. Febs Letters. 1996 Nov 18;397(2-3):293-7.
    • (1996) Febs Letters. , vol.397 , Issue.2-3 , pp. 293-297
    • Martinezchantar, M.L.1    Pajares, M.A.2
  • 55
    • 70350337363 scopus 로고    scopus 로고
    • Preservation of cellular glutathione status and mitochondrial membrane potential by N-acetylcysteine and insulin sensitizers prevent carbonyl stress-induced human brain endothelial cell apoptosis
    • Nov
    • Okouchi M, Okayama N, Aw TY. Preservation of cellular glutathione status and mitochondrial membrane potential by N-acetylcysteine and insulin sensitizers prevent carbonyl stress-induced human brain endothelial cell apoptosis. Curr Neurovasc Res. 2009 Nov;6(4):267-78.
    • (2009) Curr Neurovasc Res. , vol.6 , Issue.4 , pp. 267-278
    • Okouchi, M.1    Okayama, N.2    Aw, T.Y.3
  • 56
    • 0023084124 scopus 로고
    • Formation of disulfides with diamide
    • Kosower NS, Kosower EM. Formation of disulfides with diamide. Methods Enzymol. 1987;143:264-70.
    • (1987) Methods Enzymol. , vol.143 , pp. 264-270
    • Kosower, N.S.1    Kosower, E.M.2
  • 58
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Jun
    • Ghezzi P. Regulation of protein function by glutathionylation. Free Radic Res. 2005 Jun;39(6):573-80.
    • (2005) Free Radic Res. , vol.39 , Issue.6 , pp. 573-580
    • Ghezzi, P.1
  • 59
    • 14044257843 scopus 로고    scopus 로고
    • Glutaredoxin: Role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation
    • Mar-Apr
    • Shelton MD, Chock PB, Mieyal JJ. Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid Redox Signal. 2005 Mar-Apr;7(3-4):348-66.
    • (2005) Antioxid Redox Signal. , vol.7 , Issue.3-4 , pp. 348-366
    • Shelton, M.D.1    Chock, P.B.2    Mieyal, J.J.3
  • 61
    • 84879808307 scopus 로고    scopus 로고
    • The fairytale of the GSSG/GSH redox potential
    • 2012 Nov 2
    • Flohe L. The fairytale of the GSSG/GSH redox potential. Biochim Biophys Acta. 2012 Nov 2.
    • Biochim Biophys Acta
    • Flohe, L.1
  • 62
    • 39949085437 scopus 로고    scopus 로고
    • Nonequilibrium thermodynamics of thiol/disulfide redox systems: A perspective on redox systems biology
    • Mar 15
    • Kemp M, Go YM, Jones DP. Nonequilibrium thermodynamics of thiol/disulfide redox systems: a perspective on redox systems biology. Free Radic Biol Med. 2008 Mar 15;44(6):921-37.
    • (2008) Free Radic Biol Med. , vol.44 , Issue.6 , pp. 921-937
    • Kemp, M.1    Go, Y.M.2    Jones, D.P.3
  • 63
    • 29044434874 scopus 로고    scopus 로고
    • Hyperglycemia potentiates carbonyl stress-induced apoptosis in naive PC-12 cells: Relationship to cellular redox and activator protease factor-1 expression
    • Dec
    • Okouchi M, Okayama N, Aw TY. Hyperglycemia potentiates carbonyl stress-induced apoptosis in naive PC-12 cells: relationship to cellular redox and activator protease factor-1 expression. Curr Neurovasc Res. 2005 Dec;2(5):375-86.
    • (2005) Curr Neurovasc Res. , vol.2 , Issue.5 , pp. 375-386
    • Okouchi, M.1    Okayama, N.2    Aw, T.Y.3
  • 64
    • 34547105052 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-from oxidative stress to cellular functions and degenerative diseases
    • Ho HY, Cheng ML, Chiu DT. Glucose-6-phosphate dehydrogenase-from oxidative stress to cellular functions and degenerative diseases. Redox Rep. 2007;12(3):109-18.
    • (2007) Redox Rep. , vol.12 , Issue.3 , pp. 109-118
    • Ho, H.Y.1    Cheng, M.L.2    Chiu, D.T.3
  • 66
    • 81555215675 scopus 로고    scopus 로고
    • Predicting the kinetic properties associated with redox imbalance after oxidative crisis in G6PD-deficient erythrocytes: A simulation study
    • Shimo H, Nishino T, Tomita M. Predicting the Kinetic Properties Associated with Redox Imbalance after Oxidative Crisis in G6PD-Deficient Erythrocytes: A Simulation Study. Adv Hematol. 2011;2011:398945.
    • (2011) Adv Hematol. , vol.2011 , pp. 398945
    • Shimo, H.1    Nishino, T.2    Tomita, M.3
  • 67
    • 3042802690 scopus 로고    scopus 로고
    • Glutathione: An overview of biosynthesis and modulation
    • Apr 24
    • Anderson ME. Glutathione: an overview of biosynthesis and modulation. Chem Biol Interact. 1998 Apr 24;111-112:1-14.
    • (1998) Chem Biol Interact. , vol.111-112 , pp. 1-14
    • Anderson, M.E.1
  • 68
    • 0037653659 scopus 로고    scopus 로고
    • Gender difference in glutathione metabolism during aging in mice
    • May
    • Wang H, Liu H, Liu RM. Gender difference in glutathione metabolism during aging in mice. Exp Gerontol. 2003 May;38(5):507-17.
    • (2003) Exp Gerontol. , vol.38 , Issue.5 , pp. 507-517
    • Wang, H.1    Liu, H.2    Liu, R.M.3
  • 69
    • 3242686012 scopus 로고    scopus 로고
    • Glutathione metabolism during aging and in Alzheimer disease
    • Jun
    • Liu H, Wang H, Shenvi S, Hagen TM, Liu RM. Glutathione metabolism during aging and in Alzheimer disease. Ann N Y Acad Sci. 2004 Jun;1019:346-9.
    • (2004) Ann N y Acad Sci. , vol.1019 , pp. 346-349
    • Liu, H.1    Wang, H.2    Shenvi, S.3    Hagen, T.M.4    Liu, R.M.5
  • 70
    • 15844413589 scopus 로고    scopus 로고
    • Long exposure to high glucose concentration impairs the responsive expression of gamma-glutamylcysteine synthetase by interleukin-1beta and tumor necrosis factor-alpha in mouse endothelial cells
    • Jun 21
    • Urata Y, Yamamoto H, Goto S, et al. Long exposure to high glucose concentration impairs the responsive expression of gamma-glutamylcysteine synthetase by interleukin-1beta and tumor necrosis factor-alpha in mouse endothelial cells. J Biol Chem. 1996 Jun 21;271(25):15146-52.
    • (1996) J Biol Chem. , vol.271 , Issue.25 , pp. 15146-15152
    • Urata, Y.1    Yamamoto, H.2    Goto, S.3
  • 71
    • 33750734665 scopus 로고    scopus 로고
    • NRF2-dependent glutamate-L-cysteine ligase catalytic subunit expression mediates insulin protection against hyperglycemia-induced brain endothelial cell apoptosis
    • Nov
    • Okouchi M, Okayama N, Alexander JS, Aw TY. NRF2-dependent glutamate-L-cysteine ligase catalytic subunit expression mediates insulin protection against hyperglycemia-induced brain endothelial cell apoptosis. Curr Neurovasc Res. 2006 Nov;3(4):249-61.
    • (2006) Curr Neurovasc Res. , vol.3 , Issue.4 , pp. 249-261
    • Okouchi, M.1    Okayama, N.2    Alexander, J.S.3    Aw, T.Y.4
  • 72
    • 37549071817 scopus 로고    scopus 로고
    • Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: A potential role for Nrf2
    • Feb
    • Walters DM, Cho HY, Kleeberger SR. Oxidative stress and antioxidants in the pathogenesis of pulmonary fibrosis: a potential role for Nrf2. Antioxid Redox Signal. 2008 Feb;10(2):321-32.
    • (2008) Antioxid Redox Signal. , vol.10 , Issue.2 , pp. 321-332
    • Walters, D.M.1    Cho, H.Y.2    Kleeberger, S.R.3
  • 73
    • 77649341846 scopus 로고    scopus 로고
    • Decreased glutathione levels and altered antioxidant defense in an animal model of schizophrenia: Long-term effects of perinatal phencyclidine administration
    • Mar-Apr
    • Radonjic NV, Knezevic ID, Vilimanovich U, et al. Decreased glutathione levels and altered antioxidant defense in an animal model of schizophrenia: long-term effects of perinatal phencyclidine administration. Neuropharmacology. 2010 Mar-Apr;58(4-5):739-45.
    • (2010) Neuropharmacology. , vol.58 , Issue.4-5 , pp. 739-745
    • Radonjic, N.V.1    Knezevic, I.D.2    Vilimanovich, U.3
  • 74
    • 18744407864 scopus 로고    scopus 로고
    • Heme oxygenase-2 protects against glutathione depletion-induced neuronal apoptosis mediated by bilirubin and cyclic GMP
    • Apr
    • Chen J, Tu Y, Connolly EC, Ronnett GV. Heme oxygenase-2 protects against glutathione depletion-induced neuronal apoptosis mediated by bilirubin and cyclic GMP. Curr Neurovasc Res. 2005 Apr;2(2):121-31.
    • (2005) Curr Neurovasc Res. , vol.2 , Issue.2 , pp. 121-131
    • Chen, J.1    Tu, Y.2    Connolly, E.C.3    Ronnett, G.V.4
  • 75
    • 0025604921 scopus 로고
    • Importance and regulation of hepatic glutathione
    • Nov
    • DeLeve LD, Kaplowitz N. Importance and regulation of hepatic glutathione. Semin Liver Dis. 1990 Nov;10(4):251-66.
    • (1990) Semin Liver Dis. , vol.10 , Issue.4 , pp. 251-266
    • Deleve, L.D.1    Kaplowitz, N.2
  • 76
    • 0026387907 scopus 로고
    • Glutathione metabolism and its role in hepatotoxicity
    • Dec
    • DeLeve LD, Kaplowitz N. Glutathione metabolism and its role in hepatotoxicity. Pharmacol Ther. 1991 Dec;52(3):287-305.
    • (1991) Pharmacol Ther. , vol.52 , Issue.3 , pp. 287-305
    • Deleve, L.D.1    Kaplowitz, N.2
  • 78
    • 60149085253 scopus 로고    scopus 로고
    • Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases
    • Mar 6
    • Huang K, Wang YH, Brown A, Sun G. Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases. J Mol Biol. 2009 Mar 6;386(4):1066-77.
    • (2009) J Mol Biol. , vol.386 , Issue.4 , pp. 1066-1077
    • Huang, K.1    Wang, Y.H.2    Brown, A.3    Sun, G.4
  • 79
    • 0016635533 scopus 로고
    • Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione
    • Feb 25
    • Richman PG, Meister A. Regulation of gamma-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J Biol Chem. 1975 Feb 25;250(4):1422-6.
    • (1975) J Biol Chem. , vol.250 , Issue.4 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 80
    • 77954937495 scopus 로고    scopus 로고
    • Glutathione synthesis and turnover in the human erythrocyte: Alignment of a model based on detailed enzyme kinetics with experimental data
    • Jul 30
    • Raftos JE, Whillier S, Kuchel PW. Glutathione synthesis and turnover in the human erythrocyte: alignment of a model based on detailed enzyme kinetics with experimental data. J Biol Chem. 2010 Jul 30;285(31):23557-67.
    • (2010) J Biol Chem. , vol.285 , Issue.31 , pp. 23557-23567
    • Raftos, J.E.1    Whillier, S.2    Kuchel, P.W.3
  • 81
    • 0032872852 scopus 로고    scopus 로고
    • Regulation of gamma-glutamylcysteine synthetase expression in response to oxidative stress
    • Oct
    • Kondo T, Higashiyama Y, Goto S, Iida T, Cho S, Iwanaga M, et al. Regulation of gamma-glutamylcysteine synthetase expression in response to oxidative stress. Free Radic Res. 1999 Oct;31(4):325-34.
    • (1999) Free Radic Res. , vol.31 , Issue.4 , pp. 325-334
    • Kondo, T.1    Higashiyama, Y.2    Goto, S.3    Iida, T.4    Cho, S.5    Iwanaga, M.6
  • 82
    • 79960721951 scopus 로고    scopus 로고
    • Modulation of Nrf2 expression alters high glucose-induced oxidative stress and antioxidant gene expression in mouse mesangial cells
    • Oct
    • Li H, Wang F, Zhang L, Cao Y, Liu W, Hao J, et al. Modulation of Nrf2 expression alters high glucose-induced oxidative stress and antioxidant gene expression in mouse mesangial cells. Cell Signal. 2011 Oct;23(10):1625-32.
    • (2011) Cell Signal. , vol.23 , Issue.10 , pp. 1625-1632
    • Li, H.1    Wang, F.2    Zhang, L.3    Cao, Y.4    Liu, W.5    Hao, J.6
  • 83
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Feb-Apr
    • Lu SC. Regulation of glutathione synthesis. Mol Aspects Med. 2009 Feb-Apr;30(1-2):42-59.
    • (2009) Mol Aspects Med. , vol.30 , Issue.1-2 , pp. 42-59
    • Lu, S.C.1
  • 84
    • 0031846919 scopus 로고    scopus 로고
    • Surgical trauma decreases glutathione synthetic capacity in human skeletal muscle tissue
    • Aug
    • Luo JL, Hammarqvist F, Andersson K, Wernerman J. Surgical trauma decreases glutathione synthetic capacity in human skeletal muscle tissue. Am J Physiol. 1998 Aug;275(2 Pt 1):E359-65.
    • (1998) Am J Physiol. , vol.275 , Issue.2 PART 1
    • Luo, J.L.1    Hammarqvist, F.2    Andersson, K.3    Wernerman, J.4
  • 86
    • 0033067354 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis: Current concepts and controversies
    • Jul
    • Lu SC. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 1999 Jul;13(10):1169-83.
    • (1999) FASEB J. , vol.13 , Issue.10 , pp. 1169-1183
    • Lu, S.C.1
  • 87
    • 0032973861 scopus 로고    scopus 로고
    • Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis
    • Jun
    • Iwata-Ichikawa E, Kondo Y, Miyazaki I, Asanuma M, Ogawa N. Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis. J Neurochem. 1999 Jun;72(6):2334-44.
    • (1999) J Neurochem. , vol.72 , Issue.6 , pp. 2334-2344
    • Iwata-Ichikawa, E.1    Kondo, Y.2    Miyazaki, I.3    Asanuma, M.4    Ogawa, N.5
  • 88
    • 39749131628 scopus 로고    scopus 로고
    • Altered antioxidant capacity in human renal cell carcinoma: Role of glutathione associated enzymes
    • Mar-Apr
    • Pljesa-Ercegovac M, Mimic-Oka J, Dragicevic D, et al. Altered antioxidant capacity in human renal cell carcinoma: role of glutathione associated enzymes. Urol Oncol. 2008 Mar-Apr;26(2):175-81.
    • (2008) Urol Oncol. , vol.26 , Issue.2 , pp. 175-181
    • Pljesa-Ercegovac, M.1    Mimic-Oka, J.2    Dragicevic, D.3
  • 89
    • 0036231116 scopus 로고    scopus 로고
    • Oxidant stress induces gamma-glutamylcysteine synthetase and glutathione synthesis in human bronchial epithelial NCI-H292 cells
    • Apr
    • Ray S, Watkins DN, Misso NL, Thompson PJ. Oxidant stress induces gamma-glutamylcysteine synthetase and glutathione synthesis in human bronchial epithelial NCI-H292 cells. Clin Exp Allergy. 2002 Apr;32(4):571-7.
    • (2002) Clin Exp Allergy. , vol.32 , Issue.4 , pp. 571-577
    • Ray, S.1    Watkins, D.N.2    Misso, N.L.3    Thompson, P.J.4
  • 90
    • 0028075841 scopus 로고
    • Quinone-induced oxidative stress elevates glutathione and induces gamma-glutamylcysteine synthetase activity in rat lung epithelial L2 cells
    • Oct 21
    • Shi MM, Kugelman A, Iwamoto T, Tian L, Forman HJ. Quinone-induced oxidative stress elevates glutathione and induces gamma-glutamylcysteine synthetase activity in rat lung epithelial L2 cells. J Biol Chem. 1994 Oct 21;269(42):26512-7.
    • (1994) J Biol Chem. , vol.269 , Issue.42 , pp. 26512-26517
    • Shi, M.M.1    Kugelman, A.2    Iwamoto, T.3    Tian, L.4    Forman, H.J.5
  • 91
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress
    • Oct
    • Hayes JD, McLellan LI. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic Res. 1999 Oct;31(4):273-300.
    • (1999) Free Radic Res. , vol.31 , Issue.4 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 93
    • 84868328588 scopus 로고    scopus 로고
    • Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose
    • Nov 2
    • Du Y, Zhang H, Lu J, Holmgren A. Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose. J Biol Chem. 2012 Nov 2;287(45):38210-9.
    • (2012) J Biol Chem. , vol.287 , Issue.45 , pp. 38210-38219
    • Du, Y.1    Zhang, H.2    Lu, J.3    Holmgren, A.4
  • 94
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. in situ reduction of phospholipid and cholesterol hydroperoxides
    • Jan 5
    • Thomas JP, Maiorino M, Ursini F, Girotti AW. Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. In situ reduction of phospholipid and cholesterol hydroperoxides. J Biol Chem. 1990 Jan 5;265(1):454-61.
    • (1990) J Biol Chem. , vol.265 , Issue.1 , pp. 454-461
    • Thomas, J.P.1    Maiorino, M.2    Ursini, F.3    Girotti, A.W.4
  • 95
    • 34547578624 scopus 로고    scopus 로고
    • Sequential opening of mitochondrial ion channels as a function of glutathione redox thiol status
    • Jul 27
    • Aon MA, Cortassa S, Maack C, O'Rourke B. Sequential opening of mitochondrial ion channels as a function of glutathione redox thiol status. J Biol Chem. 2007 Jul 27;282(30):21889-900.
    • (2007) J Biol Chem. , vol.282 , Issue.30 , pp. 21889-21900
    • Aon, M.A.1    Cortassa, S.2    Maack, C.3    O'Rourke, B.4
  • 96
    • 0142210179 scopus 로고    scopus 로고
    • Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria
    • Nov
    • Han D, Canali R, Rettori D, Kaplowitz N. Effect of glutathione depletion on sites and topology of superoxide and hydrogen peroxide production in mitochondria. Mol Pharmacol. 2003 Nov;64(5): 1136-44.
    • (2003) Mol Pharmacol. , vol.64 , Issue.5 , pp. 1136-1144
    • Han, D.1    Canali, R.2    Rettori, D.3    Kaplowitz, N.4
  • 97
    • 80053034441 scopus 로고    scopus 로고
    • Thioredoxin reductase-2 is essential for keeping low levels of H(2)O(2) emission from isolated heart mitochondria
    • Sep 23
    • Stanley BA, Sivakumaran V, Shi S, McDonald I, Lloyd D, Watson WH, et al. Thioredoxin reductase-2 is essential for keeping low levels of H(2)O(2) emission from isolated heart mitochondria. J Biol Chem. 2011 Sep 23;286(38):33669-77.
    • (2011) J Biol Chem. , vol.286 , Issue.38 , pp. 33669-33677
    • Stanley, B.A.1    Sivakumaran, V.2    Shi, S.3    McDonald, I.4    Lloyd, D.5    Watson, W.H.6
  • 98
    • 0344603640 scopus 로고    scopus 로고
    • Glutathione depletion and neuronal cell death: The role of reactive oxygen intermediates and mitochondrial function
    • Apr 24
    • Wullner U, Seyfried J, Groscurth P, Beinroth S, Winter S, Gleichmann M, et al. Glutathione depletion and neuronal cell death: the role of reactive oxygen intermediates and mitochondrial function. Brain Res. 1999 Apr 24;826(1):53-62.
    • (1999) Brain Res. , vol.826 , Issue.1 , pp. 53-62
    • Wullner, U.1    Seyfried, J.2    Groscurth, P.3    Beinroth, S.4    Winter, S.5    Gleichmann, M.6
  • 100
    • 84255205291 scopus 로고    scopus 로고
    • Glutathione: Mechanism and kinetics of its non-enzymatic defense action against free radicals
    • Galano A, Alvarez-Idaboy JR. Glutathione: mechanism and kinetics of its non-enzymatic defense action against free radicals. RSC Advances. 2011;1(9):1763.
    • (2011) RSC Advances. , vol.1 , Issue.9 , pp. 1763
    • Galano, A.1    Alvarez-Idaboy, J.R.2
  • 102
    • 0028114890 scopus 로고
    • The reaction of superoxide with reduced glutathione
    • Nov 1
    • Winterbourn CC, Metodiewa D. The reaction of superoxide with reduced glutathione. Arch Biochem Biophys. 1994 Nov 1;314(2):284-90.
    • (1994) Arch Biochem Biophys. , vol.314 , Issue.2 , pp. 284-290
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 103
    • 0027390329 scopus 로고
    • Superoxide as an intracellular radical sink
    • Jan
    • Winterbourn CC. Superoxide as an intracellular radical sink. Free Radic Biol Med. 1993 Jan;14(1):85-90.
    • (1993) Free Radic Biol Med. , vol.14 , Issue.1 , pp. 85-90
    • Winterbourn, C.C.1
  • 104
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Aug
    • Winterbourn CC, Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med. 1999 Aug;27(3-4):322-8.
    • (1999) Free Radic Biol Med. , vol.27 , Issue.3-4 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 105
    • 77958092906 scopus 로고    scopus 로고
    • Hydrogen exchange equilibria in glutathione radicals: Rate constants
    • Oct 18
    • Hofstetter D, Nauser T, Koppenol WH. Hydrogen exchange equilibria in glutathione radicals: rate constants. Chem Res Toxicol. 2010 Oct 18;23(10):1596-600.
    • (2010) Chem Res Toxicol. , vol.23 , Issue.10 , pp. 1596-1600
    • Hofstetter, D.1    Nauser, T.2    Koppenol, W.H.3
  • 106
    • 84862059860 scopus 로고    scopus 로고
    • Phytochemical antioxidants modulate mammalian cellular epigenome: Implications in health and disease
    • Jul 15
    • Malireddy S, Kotha SR, Secor JD, Gurney TO, Abbott JL, Maulik G, et al. Phytochemical antioxidants modulate mammalian cellular epigenome: implications in health and disease. Antioxid Redox Signal. 2012 Jul 15;17(2):327-39.
    • (2012) Antioxid Redox Signal. , vol.17 , Issue.2 , pp. 327-339
    • Malireddy, S.1    Kotha, S.R.2    Secor, J.D.3    Gurney, T.O.4    Abbott, J.L.5    Maulik, G.6
  • 107
    • 0042357391 scopus 로고    scopus 로고
    • Effect of vitamin e on glutathione-dependent enzymes
    • May-Aug
    • van Haaften RI, Haenen GR, Evelo CT, Bast A. Effect of vitamin E on glutathione-dependent enzymes. Drug Metab Rev. 2003 May-Aug;35(2-3):215-53.
    • (2003) Drug Metab Rev. , vol.35 , Issue.2-3 , pp. 215-253
    • Van Haaften, R.I.1    Haenen, G.R.2    Evelo, C.T.3    Bast, A.4
  • 108
    • 14444271790 scopus 로고    scopus 로고
    • Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide
    • Aug 28
    • de Haan JB, Bladier C, Griffiths P, Kelner M, O'Shea RD, Cheung NS, et al. Mice with a homozygous null mutation for the most abundant glutathione peroxidase, Gpx1, show increased susceptibility to the oxidative stress-inducing agents paraquat and hydrogen peroxide. J Biol Chem. 1998 Aug 28;273(35):22528-36.
    • (1998) J Biol Chem. , vol.273 , Issue.35 , pp. 22528-22536
    • De Haan, J.B.1    Bladier, C.2    Griffiths, P.3    Kelner, M.4    O'Shea, R.D.5    Cheung, N.S.6
  • 109
    • 36549064271 scopus 로고    scopus 로고
    • Advanced glycation end products, oxidative stress and metalloproteinases are altered in the cerebral microvasculature during aging
    • Nov
    • Safciuc F, Constantin A, Manea A, Nicolae M, Popov D, Raicu M, et al. Advanced glycation end products, oxidative stress and metalloproteinases are altered in the cerebral microvasculature during aging. Curr Neurovasc Res. 2007 Nov;4(4):228-34.
    • (2007) Curr Neurovasc Res. , vol.4 , Issue.4 , pp. 228-234
    • Safciuc, F.1    Constantin, A.2    Manea, A.3    Nicolae, M.4    Popov, D.5    Raicu, M.6
  • 110
    • 75949121583 scopus 로고    scopus 로고
    • Oxidative stress in the progression of Alzheimer disease in the frontal cortex
    • Feb
    • Ansari MA, Scheff SW. Oxidative stress in the progression of Alzheimer disease in the frontal cortex. J Neuropathol Exp Neurol. 2010 Feb;69(2):155-67.
    • (2010) J Neuropathol Exp Neurol. , vol.69 , Issue.2 , pp. 155-167
    • Ansari, M.A.1    Scheff, S.W.2
  • 111
    • 0037104655 scopus 로고    scopus 로고
    • Kinetic studies on the hydrogen peroxide elimination by cultured PC12 cells: Rate limitation by glucose-6-phosphate dehydrogenase
    • Aug 15
    • Hashida K, Sakakura Y, Makino N. Kinetic studies on the hydrogen peroxide elimination by cultured PC12 cells: rate limitation by glucose-6-phosphate dehydrogenase. Biochim Biophys Acta. 2002 Aug 15;1572(1):85-90.
    • (2002) Biochim Biophys Acta. , vol.1572 , Issue.1 , pp. 85-90
    • Hashida, K.1    Sakakura, Y.2    Makino, N.3
  • 112
    • 43049159553 scopus 로고    scopus 로고
    • Kinetics of hydrogen peroxide elimination by astrocytes and C6 glioma cells analysis based on a mathematical model
    • Jun
    • Makino N, Mise T, Sagara J. Kinetics of hydrogen peroxide elimination by astrocytes and C6 glioma cells analysis based on a mathematical model. Biochim Biophys Acta. 2008 Jun;1780(6):927-36.
    • (2008) Biochim Biophys Acta. , vol.1780 , Issue.6 , pp. 927-936
    • Makino, N.1    Mise, T.2    Sagara, J.3
  • 113
    • 0032502995 scopus 로고    scopus 로고
    • Kinetics of hydrogen peroxide elimination by human umbilical vein endothelial cells in culture
    • Apr 10
    • Sasaki K, Bannai S, Makino N. Kinetics of hydrogen peroxide elimination by human umbilical vein endothelial cells in culture. Biochim Biophys Acta. 1998 Apr 10;1380(2):275-88.
    • (1998) Biochim Biophys Acta. , vol.1380 , Issue.2 , pp. 275-288
    • Sasaki, K.1    Bannai, S.2    Makino, N.3
  • 114
    • 0027972577 scopus 로고
    • Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts
    • Jan 14
    • Makino N, Mochizuki Y, Bannai S, Sugita Y. Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. J Biol Chem. 1994 Jan 14;269(2):1020-5.
    • (1994) J Biol Chem. , vol.269 , Issue.2 , pp. 1020-1025
    • Makino, N.1    Mochizuki, Y.2    Bannai, S.3    Sugita, Y.4
  • 115
    • 3242774397 scopus 로고    scopus 로고
    • A metabolic model describing the H2O2 elimination by mammalian cells including H2O2 permeation through cytoplasmic and peroxisomal membranes: Comparison with experimental data
    • Aug 4
    • Makino N, Sasaki K, Hashida K, Sakakura Y. A metabolic model describing the H2O2 elimination by mammalian cells including H2O2 permeation through cytoplasmic and peroxisomal membranes: comparison with experimental data. Biochim Biophys Acta. 2004 Aug 4;1673(3):149-59.
    • (2004) Biochim Biophys Acta. , vol.1673 , Issue.3 , pp. 149-159
    • Makino, N.1    Sasaki, K.2    Hashida, K.3    Sakakura, Y.4
  • 116
    • 36048938363 scopus 로고    scopus 로고
    • The rate of cellular hydrogen peroxide removal shows dependency on GSH: Mathematical insight into in vivo H2O2 and GPx concentrations
    • Nov
    • Ng CF, Schafer FQ, Buettner GR, Rodgers VG. The rate of cellular hydrogen peroxide removal shows dependency on GSH: mathematical insight into in vivo H2O2 and GPx concentrations. Free Radic Res. 2007 Nov;41(11):1201-11.
    • (2007) Free Radic Res. , vol.41 , Issue.11 , pp. 1201-1211
    • Ng, C.F.1    Schafer, F.Q.2    Buettner, G.R.3    Rodgers, V.G.4
  • 117
    • 0034660880 scopus 로고    scopus 로고
    • The role of cellular glutathione peroxidase redox regulation in the suppression of tumor cell growth by manganese superoxide dismutase
    • Jul 15
    • Li S, Yan T, Yang JQ, Oberley TD, Oberley LW. The role of cellular glutathione peroxidase redox regulation in the suppression of tumor cell growth by manganese superoxide dismutase. Cancer Res. 2000 Jul 15;60(14):3927-39.
    • (2000) Cancer Res. , vol.60 , Issue.14 , pp. 3927-3939
    • Li, S.1    Yan, T.2    Yang, J.Q.3    Oberley, T.D.4    Oberley, L.W.5
  • 118
    • 15444377306 scopus 로고    scopus 로고
    • Thioredoxin: A multifunctional antioxidant enzyme in kidney, heart and vessels
    • Mar
    • Yamawaki H, Berk BC. Thioredoxin: a multifunctional antioxidant enzyme in kidney, heart and vessels. Curr Opin Nephrol Hypertens. 2005 Mar;14(2):149-53.
    • (2005) Curr Opin Nephrol Hypertens. , vol.14 , Issue.2 , pp. 149-153
    • Yamawaki, H.1    Berk, B.C.2
  • 119
    • 12244263480 scopus 로고    scopus 로고
    • Nitric oxide delivery in stagnant systems via nitric oxide donors: A mathematical model
    • Jan
    • Kavdia M, Lewis RS. Nitric oxide delivery in stagnant systems via nitric oxide donors: a mathematical model. Chem Res Toxicol. 2003 Jan;16(1):7-14.
    • (2003) Chem Res Toxicol. , vol.16 , Issue.1 , pp. 7-14
    • Kavdia, M.1    Lewis, R.S.2
  • 120
    • 0031797336 scopus 로고    scopus 로고
    • Novel devices for the predictable delivery of nitric oxide to aqueous solutions
    • Nov
    • Kavdia M, Nagarajan S, Lewis RS. Novel devices for the predictable delivery of nitric oxide to aqueous solutions. Chem Res Toxicol. 1998 Nov;11(11):1346-51.
    • (1998) Chem Res Toxicol. , vol.11 , Issue.11 , pp. 1346-1351
    • Kavdia, M.1    Nagarajan, S.2    Lewis, R.S.3
  • 121
    • 84869382393 scopus 로고    scopus 로고
    • Contribution of membrane permeability and unstirred layer diffusion to nitric oxide-red blood cell interaction
    • Oct 29
    • Deonikar P, Kavdia M. Contribution of membrane permeability and unstirred layer diffusion to nitric oxide-red blood cell interaction. J Theor Biol. 2013 Oct 29;317:321-30.
    • (2013) J Theor Biol. , vol.317 , pp. 321-330
    • Deonikar, P.1    Kavdia, M.2
  • 122
    • 84860317131 scopus 로고    scopus 로고
    • Low micromolar intravascular cell-free hemoglobin concentration affects vascular NO bioavailability in sickle cell disease: A computational analysis
    • Apr
    • Deonikar P, Kavdia M. Low micromolar intravascular cell-free hemoglobin concentration affects vascular NO bioavailability in sickle cell disease: a computational analysis. J Appl Physiol. 2012 Apr;112(8):1383-92.
    • (2012) J Appl Physiol. , vol.112 , Issue.8 , pp. 1383-1392
    • Deonikar, P.1    Kavdia, M.2
  • 123
    • 78249266312 scopus 로고    scopus 로고
    • A computational model for nitric oxide, nitrite and nitrate biotransport in the microcirculation: Effect of reduced nitric oxide consumption by red blood cells and blood velocity
    • Dec
    • Deonikar P, Kavdia M. A computational model for nitric oxide, nitrite and nitrate biotransport in the microcirculation: effect of reduced nitric oxide consumption by red blood cells and blood velocity. Microvasc Res. 2010 Dec;80(3):464-76.
    • (2010) Microvasc Res. , vol.80 , Issue.3 , pp. 464-476
    • Deonikar, P.1    Kavdia, M.2
  • 124
    • 77249171159 scopus 로고    scopus 로고
    • An integrated computational and experimental model of nitric oxide-red blood cell interactions
    • Feb
    • Deonikar P, Kavdia M. An integrated computational and experimental model of nitric oxide-red blood cell interactions. Ann Biomed Eng. 2010 Feb;38(2):357-70.
    • (2010) Ann Biomed Eng. , vol.38 , Issue.2 , pp. 357-370
    • Deonikar, P.1    Kavdia, M.2
  • 125
    • 73449125764 scopus 로고    scopus 로고
    • Extracellular diffusion and permeability effects on NO-RBCs interactions using an experimental and theoretical model
    • Jan
    • Deonikar P, Kavdia M. Extracellular diffusion and permeability effects on NO-RBCs interactions using an experimental and theoretical model. Microvasc Res. 2010 Jan;79(1):47-55.
    • (2010) Microvasc Res. , vol.79 , Issue.1 , pp. 47-55
    • Deonikar, P.1    Kavdia, M.2
  • 126
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • Sep 23
    • Stamler JS. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell. 1994 Sep 23;78(6):931-6.
    • (1994) Cell. , vol.78 , Issue.6 , pp. 931-936
    • Stamler, J.S.1
  • 127
    • 0032921250 scopus 로고    scopus 로고
    • Nitric oxide and thiol groups
    • May 5
    • Gaston B. Nitric oxide and thiol groups. Biochim Biophys Acta. 1999 May 5;1411(2-3):323-33.
    • (1999) Biochim Biophys Acta. , vol.1411 , Issue.2-3 , pp. 323-333
    • Gaston, B.1
  • 128
    • 0034656848 scopus 로고    scopus 로고
    • Biological chemistry and clinical potential of S-nitrosothiols
    • May 15
    • Hogg N. Biological chemistry and clinical potential of S-nitrosothiols. Free Radic Biol Med. 2000 May 15;28(10):1478-86.
    • (2000) Free Radic Biol Med. , vol.28 , Issue.10 , pp. 1478-1486
    • Hogg, N.1
  • 129
    • 70349466515 scopus 로고    scopus 로고
    • Protein denitrosylation: Enzymatic mechanisms and cellular functions
    • Oct
    • Benhar M, Forrester MT, Stamler JS. Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat Rev Mol Cell Biol. 2009 Oct;10(10):721-32.
    • (2009) Nat Rev Mol Cell Biol. , vol.10 , Issue.10 , pp. 721-732
    • Benhar, M.1    Forrester, M.T.2    Stamler, J.S.3
  • 130
    • 48349131772 scopus 로고    scopus 로고
    • S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking
    • Aug 8
    • Ozawa K, Whalen EJ, Nelson CD, et al. S-nitrosylation of beta-arrestin regulates beta-adrenergic receptor trafficking. Mol Cell. 2008 Aug 8;31(3):395-405.
    • (2008) Mol Cell. , vol.31 , Issue.3 , pp. 395-405
    • Ozawa, K.1    Whalen, E.J.2    Nelson, C.D.3
  • 131
    • 34247470682 scopus 로고    scopus 로고
    • Regulation of beta-adrenergic receptor signaling by S-nitrosylation of G-protein-coupled receptor kinase 2
    • May 4
    • Whalen EJ, Foster MW, Matsumoto A, Ozawa K, Violin JD, Que LG, et al. Regulation of beta-adrenergic receptor signaling by S-nitrosylation of G-protein-coupled receptor kinase 2. Cell. 2007 May 4;129(3):511-22.
    • (2007) Cell. , vol.129 , Issue.3 , pp. 511-522
    • Whalen, E.J.1    Foster, M.W.2    Matsumoto, A.3    Ozawa, K.4    Violin, J.D.5    Que, L.G.6
  • 133
    • 48449104356 scopus 로고    scopus 로고
    • Computational insights on the competing effects of nitric oxide in regulating apoptosis
    • Bagci EZ, Vodovotz Y, Billiar TR, Ermentrout B, Bahar I. Computational insights on the competing effects of nitric oxide in regulating apoptosis. PLoS One. 2008;3(5):e2249.
    • (2008) PLoS One. , vol.3 , Issue.5
    • Bagci, E.Z.1    Vodovotz, Y.2    Billiar, T.R.3    Ermentrout, B.4    Bahar, I.5
  • 134
    • 33746927625 scopus 로고    scopus 로고
    • Kinetic modeling of nitric-oxide-associated reaction network
    • Aug
    • Hu TM, Hayton WL, Mallery SR. Kinetic modeling of nitric-oxide-associated reaction network. Pharm Res. 2006 Aug;23(8):1702-11.
    • (2006) Pharm Res. , vol.23 , Issue.8 , pp. 1702-1711
    • Hu, T.M.1    Hayton, W.L.2    Mallery, S.R.3
  • 136
    • 0028803686 scopus 로고
    • Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen
    • Nov 24
    • Kharitonov VG, Sundquist AR, Sharma VS. Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen. J Biol Chem. 1995 Nov 24;270(47):28158-64.
    • (1995) J Biol Chem. , vol.270 , Issue.47 , pp. 28158-28164
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 137
    • 74049084627 scopus 로고    scopus 로고
    • Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed?
    • Jan 1
    • Keszler A, Zhang Y, Hogg N. Reaction between nitric oxide, glutathione, and oxygen in the presence and absence of protein: How are S-nitrosothiols formed? Free Radic Biol Med. 2010 Jan 1;48(1):55-64.
    • (2010) Free Radic Biol Med. , vol.48 , Issue.1 , pp. 55-64
    • Keszler, A.1    Zhang, Y.2    Hogg, N.3
  • 138
    • 0036019494 scopus 로고    scopus 로고
    • Is N2O3 the main nitrosating intermediate in aerated nitric oxide (NO) solutions in vivo? if so, where, when, and which one?
    • Nedospasov AA. Is N2O3 the main nitrosating intermediate in aerated nitric oxide (NO) solutions in vivo? If so, where, when, and which one? J Biochem Mol Toxicol. 2002;16(3):109-20.
    • (2002) J Biochem Mol Toxicol. , vol.16 , Issue.3 , pp. 109-120
    • Nedospasov, A.A.1
  • 139
    • 0037446181 scopus 로고    scopus 로고
    • S-nitrosation of glutathione by nitric oxide, peroxynitrite, and (*) NO/O(2)(*-)
    • Apr 15
    • Schrammel A, Gorren AC, Schmidt K, Pfeiffer S, Mayer B. S-nitrosation of glutathione by nitric oxide, peroxynitrite, and (*)NO/O(2)(*-). Free Radic Biol Med. 2003 Apr 15;34(8):1078-88.
    • (2003) Free Radic Biol Med. , vol.34 , Issue.8 , pp. 1078-1088
    • Schrammel, A.1    Gorren, A.C.2    Schmidt, K.3    Pfeiffer, S.4    Mayer, B.5
  • 140
    • 15144349362 scopus 로고    scopus 로고
    • Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide
    • Nov 13
    • van der Vliet A, Hoen PA, Wong PS, Bast A, Cross CE. Formation of S-nitrosothiols via direct nucleophilic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide. J Biol Chem. 1998 Nov 13;273(46):30255-62.
    • (1998) J Biol Chem. , vol.273 , Issue.46 , pp. 30255-30262
    • Van Der Vliet, A.1    Hoen, P.A.2    Wong, P.S.3    Bast, A.4    Cross, C.E.5
  • 141
    • 0032488967 scopus 로고    scopus 로고
    • A new pathway of nitric oxide/cyclic GMP signaling involving S-nitrosoglutathione
    • Feb 6
    • Mayer B, Pfeiffer S, Schrammel A, Koesling D, Schmidt K, Brunner F. A new pathway of nitric oxide/cyclic GMP signaling involving S-nitrosoglutathione. J Biol Chem. 1998 Feb 6;273(6):3264-70.
    • (1998) J Biol Chem. , vol.273 , Issue.6 , pp. 3264-3270
    • Mayer, B.1    Pfeiffer, S.2    Schrammel, A.3    Koesling, D.4    Schmidt, K.5    Brunner, F.6
  • 142
    • 0031029150 scopus 로고    scopus 로고
    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
    • Jan 31
    • Gow AJ, Buerk DG, Ischiropoulos H. A novel reaction mechanism for the formation of S-nitrosothiol in vivo. J Biol Chem. 1997 Jan 31;272(5):2841-5.
    • (1997) J Biol Chem. , vol.272 , Issue.5 , pp. 2841-2845
    • Gow, A.J.1    Buerk, D.G.2    Ischiropoulos, H.3
  • 143
  • 144
    • 72649104434 scopus 로고    scopus 로고
    • A novel role for cytochrome c: Efficient catalysis of S-nitrosothiol formation
    • Jan 15
    • Basu S, Keszler A, Azarova NA, Nwanze N, Perlegas A, Shiva S, et al. A novel role for cytochrome c: Efficient catalysis of S-nitrosothiol formation. Free Radic Biol Med. 2010 Jan 15;48(2):255-63.
    • (2010) Free Radic Biol Med. , vol.48 , Issue.2 , pp. 255-263
    • Basu, S.1    Keszler, A.2    Azarova, N.A.3    Nwanze, N.4    Perlegas, A.5    Shiva, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.