메뉴 건너뛰기




Volumn 172, Issue 6, 2008, Pages 1529-1541

Endogenous hydrogen peroxide regulates glutathione redox via nuclear factor erythroid 2-related factor 2 downstream of phosphatidylinositol 3-kinase during muscle differentiation

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; PHOSPHATIDYLINOSITOL 3 KINASE; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NRF2;

EID: 44849083150     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.2353/ajpath.2008.070429     Document Type: Article
Times cited : (52)

References (48)
  • 1
    • 33847685896 scopus 로고    scopus 로고
    • Therapeutic approaches for muscle wasting disorders
    • Lynch GS, Schertzer JD, Ryall JG: Therapeutic approaches for muscle wasting disorders. Pharmacol Ther 2007, 113:461-487
    • (2007) Pharmacol Ther , vol.113 , pp. 461-487
    • Lynch, G.S.1    Schertzer, J.D.2    Ryall, J.G.3
  • 2
    • 0034651562 scopus 로고    scopus 로고
    • A new look at the origin, function, and "stemcell" status of muscle satellite cells
    • Seale P, Rudnicki MA: A new look at the origin, function, and "stemcell" status of muscle satellite cells. Dev Biol 2000, 218:115-124
    • (2000) Dev Biol , vol.218 , pp. 115-124
    • Seale, P.1    Rudnicki, M.A.2
  • 4
    • 1942518724 scopus 로고    scopus 로고
    • Akt2, a novel functional link between p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways in myogenesis
    • Gonzalez I, Tripathi G, Carter EJ, Cobb LJ, Salih DA, Lovett FA, Holding C, Pell JM: Akt2, a novel functional link between p38 mitogen-activated protein kinase and phosphatidylinositol 3-kinase pathways in myogenesis. Mol Cell Biol 2004, 24:3607-3622
    • (2004) Mol Cell Biol , vol.24 , pp. 3607-3622
    • Gonzalez, I.1    Tripathi, G.2    Carter, E.J.3    Cobb, L.J.4    Salih, D.A.5    Lovett, F.A.6    Holding, C.7    Pell, J.M.8
  • 5
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E, Amini AR, Amini AA, Griffiths J, Martin FJ, Wei Y, Lin HC, Yancopoulos GD, Glass DJ: Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 2005, 280:2737-2744
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 7
    • 0030934472 scopus 로고    scopus 로고
    • The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways
    • Coolican SA, Samuel DS, Ewton DZ, McWade FJ, Florini JR: The mitogenic and myogenic actions of insulin-like growth factors utilize distinct signaling pathways. J Biol Chem 1997, 272:6653-6662
    • (1997) J Biol Chem , vol.272 , pp. 6653-6662
    • Coolican, S.A.1    Samuel, D.S.2    Ewton, D.Z.3    McWade, F.J.4    Florini, J.R.5
  • 11
    • 0033607784 scopus 로고    scopus 로고
    • Rommel C, Clarke BA, Zimmermann S, Nunez L, Rossman R, Reid K, Moelling K, Yancopoulos GD, Glass DJ: Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999, 286:1738-1741
    • Rommel C, Clarke BA, Zimmermann S, Nunez L, Rossman R, Reid K, Moelling K, Yancopoulos GD, Glass DJ: Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999, 286:1738-1741
  • 12
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers
    • Forman HJ, Fukuto JM, Torres M: Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol 2004, 287:C246-C256
    • (2004) Am J Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 13
    • 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 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 14
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Griffith OW: Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 1999, 27:922-935
    • (1999) Free Radic Biol Med , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 16
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region
    • Moi P, Chan K, Asunis I, Cao A, Kan YW: Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc Natl Acad Sci USA 1994, 91:9926-9930
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 17
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome
    • Nguyen T, Sherratt PJ, Huang HC, Yang CS, Pickett CB: Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome. J Biol Chem 2003, 278:4536-4541
    • (2003) J Biol Chem , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, C.B.5
  • 18
    • 33845759389 scopus 로고    scopus 로고
    • Induction of antioxidant and detoxification response by oxidants in cardiomyocytes: Evidence from gene expression profiling and activation of Nrf2 transcription factor
    • Purdom-Dickinson SE, Lin Y, Dedek M, Morrissy S, Johnson J, Chen QM: Induction of antioxidant and detoxification response by oxidants in cardiomyocytes: evidence from gene expression profiling and activation of Nrf2 transcription factor. J Mol Cell Cardiol 2007, 42:159-176
    • (2007) J Mol Cell Cardiol , vol.42 , pp. 159-176
    • Purdom-Dickinson, S.E.1    Lin, Y.2    Dedek, M.3    Morrissy, S.4    Johnson, J.5    Chen, Q.M.6
  • 19
    • 2642671110 scopus 로고    scopus 로고
    • An electrophile responsive element (EpRE) regulates beta-naphthoflavone induction of the human gamma-glutamylcysteine synthetase regulatory subunit gene. Constitutive expression is mediated by an adjacent AP-1 site
    • Moinova HR, Mulcahy RT: An electrophile responsive element (EpRE) regulates beta-naphthoflavone induction of the human gamma-glutamylcysteine synthetase regulatory subunit gene. Constitutive expression is mediated by an adjacent AP-1 site. J Biol Chem 1998, 273:14683-14689
    • (1998) J Biol Chem , vol.273 , pp. 14683-14689
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 20
    • 0036240610 scopus 로고    scopus 로고
    • Enhanced expression of the transcription factor Nrf2 by cancer chemopreventive agents: Role of antioxidant response element-like sequences in the nrf2 promoter
    • Kwak MK, Itoh K, Yamamoto M, Kensler TW: Enhanced expression of the transcription factor Nrf2 by cancer chemopreventive agents: role of antioxidant response element-like sequences in the nrf2 promoter. Mol Cell Biol 2002, 22:2883-2892
    • (2002) Mol Cell Biol , vol.22 , pp. 2883-2892
    • Kwak, M.K.1    Itoh, K.2    Yamamoto, M.3    Kensler, T.W.4
  • 21
    • 0038537298 scopus 로고    scopus 로고
    • PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells
    • Nakaso K, Yano H, Fukuhara Y, Takeshima T, Wada-Isoe K, Nakashima K: PI3K is a key molecule in the Nrf2-mediated regulation of antioxidative proteins by hemin in human neuroblastoma cells. FEBS Lett 2003, 546:181-184
    • (2003) FEBS Lett , vol.546 , pp. 181-184
    • Nakaso, K.1    Yano, H.2    Fukuhara, Y.3    Takeshima, T.4    Wada-Isoe, K.5    Nakashima, K.6
  • 22
    • 20444456655 scopus 로고    scopus 로고
    • Induction of heme oxygenase 1 by moderately oxidized low-density lipoproteins in human vascular smooth muscle cells: Role of mitogen-activated protein kinases and Nrf2
    • Anwar AA, Li FY, Leake DS, Ishii T, Mann GE, Siow RC: Induction of heme oxygenase 1 by moderately oxidized low-density lipoproteins in human vascular smooth muscle cells: role of mitogen-activated protein kinases and Nrf2. Free Radic Biol Med 2005, 39:227-236
    • (2005) Free Radic Biol Med , vol.39 , pp. 227-236
    • Anwar, A.A.1    Li, F.Y.2    Leake, D.S.3    Ishii, T.4    Mann, G.E.5    Siow, R.C.6
  • 23
    • 33748358379 scopus 로고    scopus 로고
    • Mechanism of action of isothiocyanates: The induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2
    • Xu C, Yuan X, Pan Z, Shen G, Kim JH, Yu S, Khor TO, Li W, Ma J, Kong AN: Mechanism of action of isothiocyanates: the induction of ARE-regulated genes is associated with activation of ERK and JNK and the phosphorylation and nuclear translocation of Nrf2. Mol Cancer Ther 2006, 5:1918-1926
    • (2006) Mol Cancer Ther , vol.5 , pp. 1918-1926
    • Xu, C.1    Yuan, X.2    Pan, Z.3    Shen, G.4    Kim, J.H.5    Yu, S.6    Khor, T.O.7    Li, W.8    Ma, J.9    Kong, A.N.10
  • 24
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S: Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 2000, 267:4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 25
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G: Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998, 279:1718-1721
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 26
    • 4344638224 scopus 로고    scopus 로고
    • Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-kappaB activation
    • Ardite E, Barbera JA, Roca J, Fernandez-Checa JC: Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-kappaB activation. Am J Pathol 2004, 165:719-728
    • (2004) Am J Pathol , vol.165 , pp. 719-728
    • Ardite, E.1    Barbera, J.A.2    Roca, J.3    Fernandez-Checa, J.C.4
  • 27
    • 10344243974 scopus 로고    scopus 로고
    • N-acetylcysteine amide, a novel cell-permeating thiol, restores cellular glutathione and protects human red blood cells from oxidative stress
    • Grinberg L, Fibach E, Am J, Atlas D: N-acetylcysteine amide, a novel cell-permeating thiol, restores cellular glutathione and protects human red blood cells from oxidative stress. Free Radic Biol Med 2005, 38:136-145
    • (2005) Free Radic Biol Med , vol.38 , pp. 136-145
    • Grinberg, L.1    Fibach, E.2    Am, J.3    Atlas, D.4
  • 28
    • 33644872102 scopus 로고    scopus 로고
    • The oxidation of 2′,7′-dichlorofluorescin to reactive oxygen species: A self-fulfilling prophesy?
    • Bonini MG, Rota C, Tomasi A, Mason RP: The oxidation of 2′,7′-dichlorofluorescin to reactive oxygen species: a self-fulfilling prophesy? Free Radic Biol Med 2006, 40:968-975
    • (2006) Free Radic Biol Med , vol.40 , pp. 968-975
    • Bonini, M.G.1    Rota, C.2    Tomasi, A.3    Mason, R.P.4
  • 29
    • 0036537035 scopus 로고    scopus 로고
    • In vitro pharmacokinetics and pharmacodynamics of 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)
    • Ueda-Kawamitsu H, Lawson TA, Gwilt PR: In vitro pharmacokinetics and pharmacodynamics of 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU). Biochem Pharmacol 2002, 63:1209-1218
    • (2002) Biochem Pharmacol , vol.63 , pp. 1209-1218
    • Ueda-Kawamitsu, H.1    Lawson, T.A.2    Gwilt, P.R.3
  • 30
    • 2442736665 scopus 로고    scopus 로고
    • Localization by in situ hybridization of gamma-glutamylcysteine synthetase mRNA expression in rat kidney following acute methylmercury treatment
    • Li S, Thompson SA, Kavanagh TJ, Woods JS: Localization by in situ hybridization of gamma-glutamylcysteine synthetase mRNA expression in rat kidney following acute methylmercury treatment. Toxicol Appl Pharmacol 1996, 141:59-67
    • (1996) Toxicol Appl Pharmacol , vol.141 , pp. 59-67
    • Li, S.1    Thompson, S.A.2    Kavanagh, T.J.3    Woods, J.S.4
  • 31
    • 25444449520 scopus 로고    scopus 로고
    • Nrf2 controls constitutive and inducible expression of ARE-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by Keap1
    • Nguyen T, Sherratt PJ, Nioi P, Yang CS, Pickett CB: Nrf2 controls constitutive and inducible expression of ARE-driven genes through a dynamic pathway involving nucleocytoplasmic shuttling by Keap1. J Biol Chem 2005, 280:32485-32492
    • (2005) J Biol Chem , vol.280 , pp. 32485-32492
    • Nguyen, T.1    Sherratt, P.J.2    Nioi, P.3    Yang, C.S.4    Pickett, C.B.5
  • 32
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, O'Connor T, Yamamoto M: Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles. Genes Cell 2003, 8:379-391
    • (2003) Genes Cell , vol.8 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 33
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1
    • Yang H, Magilnick N, Lee C, Kalmaz D, Ou X, Chan JY, Lu SC: Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1. Mol Cell Biol 2005, 25:5933-5946
    • (2005) Mol Cell Biol , vol.25 , pp. 5933-5946
    • Yang, H.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.5    Chan, J.Y.6    Lu, S.C.7
  • 34
    • 1642423481 scopus 로고    scopus 로고
    • p38 MAPK-induced nuclear factor-kappaB activity is required for skeletal muscle differentiation: Role of interleukin-6
    • Baeza-Raja B, Munoz-Canoves P: p38 MAPK-induced nuclear factor-kappaB activity is required for skeletal muscle differentiation: role of interleukin-6. Mol Biol Cell 2004, 15:2013-2026
    • (2004) Mol Biol Cell , vol.15 , pp. 2013-2026
    • Baeza-Raja, B.1    Munoz-Canoves, P.2
  • 35
    • 20444381360 scopus 로고    scopus 로고
    • Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: Protection against reactive oxygen and nitrogen species-induced cell injury
    • Zhu H, Itoh K, Yamamoto M, Zweier JL, Li Y: Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury. FEBS Lett 2005, 579:3029-3036
    • (2005) FEBS Lett , vol.579 , pp. 3029-3036
    • Zhu, H.1    Itoh, K.2    Yamamoto, M.3    Zweier, J.L.4    Li, Y.5
  • 36
    • 2342514015 scopus 로고    scopus 로고
    • An important role of Nrf2-ARE pathway in the cellular defense mechanism
    • Lee JM, Johnson JA: An important role of Nrf2-ARE pathway in the cellular defense mechanism. J Biochem Mol Biol 2004, 37:139-143
    • (2004) J Biochem Mol Biol , vol.37 , pp. 139-143
    • Lee, J.M.1    Johnson, J.A.2
  • 37
    • 2342451904 scopus 로고    scopus 로고
    • Targeting the FLICE inhibitory protein (FLIP) in cancer therapy
    • Wajant H: Targeting the FLICE inhibitory protein (FLIP) in cancer therapy. Mol Interv 2003, 3:124-127
    • (2003) Mol Interv , vol.3 , pp. 124-127
    • Wajant, H.1
  • 38
    • 0034617467 scopus 로고    scopus 로고
    • Role of reactive oxygen species and phosphatidylinositol 3-kinase in cardiomyocyte differentiation of embryonic stem cells
    • Sauer H, Rahimi G, Hescheler J, Wartenberg M: Role of reactive oxygen species and phosphatidylinositol 3-kinase in cardiomyocyte differentiation of embryonic stem cells. FEBS Lett 2000, 476:218-223
    • (2000) FEBS Lett , vol.476 , pp. 218-223
    • Sauer, H.1    Rahimi, G.2    Hescheler, J.3    Wartenberg, M.4
  • 39
    • 0034607872 scopus 로고    scopus 로고
    • Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species
    • Suzukawa K, Miura K, Mitsushita J, Resau J, Hirose K, Crystal R, Kamata T: Nerve growth factor-induced neuronal differentiation requires generation of Rac1-regulated reactive oxygen species. J Biol Chem 2000, 275:13175-13178
    • (2000) J Biol Chem , vol.275 , pp. 13175-13178
    • Suzukawa, K.1    Miura, K.2    Mitsushita, J.3    Resau, J.4    Hirose, K.5    Crystal, R.6    Kamata, T.7
  • 41
    • 33748333105 scopus 로고    scopus 로고
    • The NADPH oxidase NOX4 drives cardiac differentiation: Role in regulating cardiac transcription factors and MAP kinase activation
    • Li J, Stouffs M, Serrander L, Banfi B, Bettiol E, Charnay Y, Steger K, Krause KH, Jaconi ME: The NADPH oxidase NOX4 drives cardiac differentiation: role in regulating cardiac transcription factors and MAP kinase activation. Mol Biol Cell 2006, 17:3978-3988
    • (2006) Mol Biol Cell , vol.17 , pp. 3978-3988
    • Li, J.1    Stouffs, M.2    Serrander, L.3    Banfi, B.4    Bettiol, E.5    Charnay, Y.6    Steger, K.7    Krause, K.H.8    Jaconi, M.E.9
  • 42
    • 0036778387 scopus 로고    scopus 로고
    • Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: Cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity
    • Hong F, Lee J, Song JW, Lee SJ, Ahn H, Cho JJ, Ha J, Kim SS: Cyclosporin A blocks muscle differentiation by inducing oxidative stress and inhibiting the peptidyl-prolyl-cis-trans isomerase activity of cyclophilin A: cyclophilin A protects myoblasts from cyclosporin A-induced cytotoxicity. FASEB J 2002, 16:1633-1635
    • (2002) FASEB J , vol.16 , pp. 1633-1635
    • Hong, F.1    Lee, J.2    Song, J.W.3    Lee, S.J.4    Ahn, H.5    Cho, J.J.6    Ha, J.7    Kim, S.S.8
  • 43
    • 34247473444 scopus 로고    scopus 로고
    • A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle
    • Hansen JM, Klass M, Harris C, Csete M: A reducing redox environment promotes C2C12 myogenesis: implications for regeneration in aged muscle. Cell Biol Int 2007, 31:546-553
    • (2007) Cell Biol Int , vol.31 , pp. 546-553
    • Hansen, J.M.1    Klass, M.2    Harris, C.3    Csete, M.4
  • 45
    • 0033602762 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha and basic fibroblast growth factor differentially inhibit the insulin-like growth factor-I induced expression of myogenin in C2C12 myoblasts
    • Layne MD, Farmer SR: Tumor necrosis factor-alpha and basic fibroblast growth factor differentially inhibit the insulin-like growth factor-I induced expression of myogenin in C2C12 myoblasts. Exp Cell Res 1999, 249:177-187
    • (1999) Exp Cell Res , vol.249 , pp. 177-187
    • Layne, M.D.1    Farmer, S.R.2
  • 46
    • 0036089571 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure
    • Sorescu D, Griendling KK: Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure. Congest Heart Fail 2002, 8:132-140
    • (2002) Congest Heart Fail , vol.8 , pp. 132-140
    • Sorescu, D.1    Griendling, K.K.2
  • 47
    • 0042831502 scopus 로고    scopus 로고
    • Regulation of glutathione in cardiac myocytes
    • Li S, Li X, Rozanski GJ: Regulation of glutathione in cardiac myocytes. J Mol Cell Cardiol 2003, 35:1145-1152
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 1145-1152
    • Li, S.1    Li, X.2    Rozanski, G.J.3
  • 48
    • 0035827505 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase, not extracellular signal-regulated kinase, regulates activation of the antioxidant-responsive element in IMR-32 human neuroblastoma cells
    • Lee JM, Hanson JM, Chu WA, Johnson JA: Phosphatidylinositol 3-kinase, not extracellular signal-regulated kinase, regulates activation of the antioxidant-responsive element in IMR-32 human neuroblastoma cells. J Biol Chem 2001, 276:20011-20016
    • (2001) J Biol Chem , vol.276 , pp. 20011-20016
    • Lee, J.M.1    Hanson, J.M.2    Chu, W.A.3    Johnson, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.