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Volumn 131, Issue 5, 2010, Pages 609-616

Possible involvement of granulocyte oxidative burst in Nrf2 signaling in cancer

Author keywords

Cancer; Granulocytes; Nrf2; Oxidative stress; Reactive oxygen species

Indexed keywords

GLYCOGEN SYNTHASE KINASE 3BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KELCH LIKE ECH ASSOCIATED PROTEIN 1; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NF E2; TRANSCRIPTION FACTOR NRF1; TRANSCRIPTION FACTOR NRF2;

EID: 77952373616     PISSN: 09715916     EISSN: 09715916     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (10)

References (105)
  • 1
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • Babior BM. Phagocytes and oxidative stress. Am J Med 2000; 109: 33-44.
    • (2000) Am J Med , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 3
    • 38349082455 scopus 로고    scopus 로고
    • The involvement of granulocytes in spontaneous regression of Walker 256 carcinoma
    • Jaganjac M, Poljak-Blazi M, Zarkovic K, Schaur RJ, Zarkovic N. The involvement of granulocytes in spontaneous regression of Walker 256 carcinoma. Cancer Lett 2008; 260: 180-6.
    • (2008) Cancer Lett , vol.260 , pp. 180-186
    • Jaganjac, M.1    Poljak-Blazi, M.2    Zarkovic, K.3    Schaur, R.J.4    Zarkovic, N.5
  • 5
    • 0000054142 scopus 로고
    • The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes
    • Sbarra AJ, Karnovsky ML. The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem 1959; 234: 1355-62.
    • (1959) J Biol Chem , vol.234 , pp. 1355-62
    • Sbarra, A.J.1    Karnovsky, M.L.2
  • 6
  • 7
    • 0024520513 scopus 로고
    • Central nervous system trauma and stroke. I. Biochemical considerations for oxygen radical formation and lipid peroxidation
    • Braughler JM, Hall ED. Central nervous system trauma and stroke. I. Biochemical considerations for oxygen radical formation and lipid peroxidation. Free Radic Biol Med 1989; 6: 289-301.
    • (1989) Free Radic Biol Med , vol.6 , pp. 289-301
    • Braughler, J.M.1    Hall, E.D.2
  • 8
    • 0024589421 scopus 로고
    • Central nervous system trauma and stroke. II. Physiological and pharmacological evidence for involvement of oxygen radicals and lipid peroxidation
    • Hall ED, Braughler JM. Central nervous system trauma and stroke. II. Physiological and pharmacological evidence for involvement of oxygen radicals and lipid peroxidation. Free Radic Biol Med 1989; 6: 303-13.
    • (1989) Free Radic Biol Med , vol.6 , pp. 303-13
    • Hall, E.D.1    Braughler, J.M.2
  • 9
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991; 11: 81-128.
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 10
    • 65949097061 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the pathogenesis of mitochondrial DNA (mtDNA) mutations in male infertility
    • Venkatesh S, Deecaraman M, Kumar R, Shamsi MB, Dada R. Role of reactive oxygen species in the pathogenesis of mitochondrial DNA (mtDNA) mutations in male infertility. Indian J Med Res 2009; 129: 127-37.
    • (2009) Indian J Med Res , vol.129 , pp. 127-37
    • Venkatesh, S.1    Deecaraman, M.2    Kumar, R.3    Shamsi, M.B.4    Dada, R.5
  • 11
    • 0028927261 scopus 로고
    • Reactions of oxyl radicals with DNA
    • Breen AP, Murphy JA. Reactions of oxyl radicals with DNA. Free Radic Biol Med 1995; 18: 1033-77.
    • (1995) Free Radic Biol Med , vol.18 , pp. 1033-77
    • Breen, A.P.1    Murphy, J.A.2
  • 12
    • 0038378322 scopus 로고    scopus 로고
    • Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis
    • Talalay P, Dinkova-Kostova AT, Holtzclaw WD. Importance of phase 2 gene regulation in protection against electrophile and reactive oxygen toxicity and carcinogenesis. Adv Enzyme Regul 2003; 43: 121-34.
    • (2003) Adv Enzyme Regul , vol.43 , pp. 121-34
    • Talalay, P.1    Dinkova-Kostova, A.T.2    Holtzclaw, W.D.3
  • 13
    • 0033800922 scopus 로고    scopus 로고
    • Regulation of genes encoding NAD(P)H: Quinone oxidoreductases
    • Jaiswal AK. Regulation of genes encoding NAD(P)H: quinone oxidoreductases. Free Radic Biol Med 2000; 29: 254-62.
    • (2000) Free Radic Biol Med , vol.29 , pp. 254-62
    • Jaiswal, A.K.1
  • 14
    • 0027243681 scopus 로고
    • Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein
    • Andrews NC, Erdjument-Bromage H, Davidson MB, Tempst P, Orkin SH. Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein. Nature 1993; 362: 722-8.
    • (1993) Nature , vol.362 , pp. 722-728
    • Andrews, N.C.1    Erdjument-Bromage, H.2    Davidson, M.B.3    Tempst, P.4    Orkin, S.H.5
  • 15
    • 0026516460 scopus 로고
    • Kan yW, Curtin PT. Dissection of the enhancer activity of beta-globin 5' DNase I-hypersensitive site 2 in transgenic mice
    • Liu D, Chang JC, Moi P, Liu W, Kan yW, Curtin PT. Dissection of the enhancer activity of beta-globin 5' DNase I-hypersensitive site 2 in transgenic mice. Proc Natl Acad Sci USA 1992; 89: 3899-903.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3899-903
    • Liu, D.1    Chang, J.C.2    Moi, P.3    Liu, W.4
  • 16
    • 0000976220 scopus 로고
    • Cis- and trans- acting elements involved in the regulation of the erythroid promoter of the human porphobilinogen deaminase gene
    • Mignotte V, Eleouet JF, Raich N, Romeo PH. Cis- and trans- acting elements involved in the regulation of the erythroid promoter of the human porphobilinogen deaminase gene. Proc Natl Acad Sci USA 1989; 86: 6548-52.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6548-52
    • Mignotte, V.1    Eleouet, J.F.2    Raich, N.3    Romeo, P.H.4
  • 17
    • 0028118492 scopus 로고
    • Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins
    • Igarashi K, Kataoka K, Itoh K, Hayashi N, Nishizawa M, yamamoto M. Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins. Nature 1994; 367: 568-72.
    • (1994) Nature , vol.367 , pp. 568-72
    • Igarashi, K.1    Kataoka, K.2    Itoh, K.3    Hayashi, N.4    Nishizawa, M.5    Yamamoto, M.6
  • 18
    • 0027532371 scopus 로고
    • Structure-function analysis of the maf oncogene product, a member of the b-Zip protein family
    • Kataoka K, Nishizawa M, Kawai S. Structure-function analysis of the maf oncogene product, a member of the b-Zip protein family. J Virol 1993; 67: 2133-41.
    • (1993) J Virol , vol.67 , pp. 2133-41
    • Kataoka, K.1    Nishizawa, M.2    Kawai, S.3
  • 19
    • 0027954409 scopus 로고
    • Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun
    • Kataoka K, Noda M, Nishizawa M. Maf nuclear oncoprotein recognizes sequences related to an AP-1 site and forms heterodimers with both Fos and Jun. Mol Cell Biol 1994; 14: 700-12.
    • (1994) Mol Cell Biol , vol.14 , pp. 700-12
    • Kataoka, K.1    Noda, M.2    Nishizawa, M.3
  • 20
    • 0030916735 scopus 로고    scopus 로고
    • Human MafG is a functional partner for p45 NF-E2 in activating globin gene expression
    • Blank V, Kim MJ, Andrews NC. Human MafG is a functional partner for p45 NF-E2 in activating globin gene expression. Blood 1997; 89: 3925-35.
    • (1997) Blood , vol.89 , pp. 3925-35
    • Blank, V.1    Kim, M.J.2    Andrews, N.C.3
  • 21
    • 0028061444 scopus 로고
    • 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
    • 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: 9926-30.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9926-30
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4
  • 22
    • 0037055265 scopus 로고    scopus 로고
    • Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors
    • Motohashi H, O'Connor T, Katsuoka F, Engel JD, yamamoto M. Integration and diversity of the regulatory network composed of Maf and CNC families of transcription factors. Gene 2002; 294: 1-12.
    • (2002) Gene , vol.294 , pp. 1-12
    • Motohashi, H.1    O'Connor, T.2    Katsuoka, F.3    Engel, J.D.4    Yamamoto, M.5
  • 23
    • 33845442925 scopus 로고    scopus 로고
    • Mechanistic studies of the Nrf2-Keap1 signaling pathway
    • Zhang DD. Mechanistic studies of the Nrf2-Keap1 signaling pathway. Drug Metab Rev 2006; 38: 769-89.
    • (2006) Drug Metab Rev , vol.38 , pp. 769-89
    • Zhang, D.D.1
  • 24
    • 40049088820 scopus 로고    scopus 로고
    • The Nrf2-Keap1 defence pathway: Role in protection against drug- induced toxicity
    • Copple IM, Goldring CE, Kitteringham NR, Park BK. The Nrf2-Keap1 defence pathway: role in protection against drug- induced toxicity. Toxicology 2008; 246: 24-33.
    • (2008) Toxicology , vol.246 , pp. 24-33
    • Copple, I.M.1    Goldring, C.E.2    Kitteringham, N.R.3    Park, B.K.4
  • 25
    • 23344452360 scopus 로고    scopus 로고
    • Nrf2 Possesses a redox-insensitive nuclear export signal overlapping with the leucine zipper motif
    • Li W, Jain MR, Chen C, yue X, Hebbar V, Zhou R, et al. Nrf2 Possesses a redox-insensitive nuclear export signal overlapping with the leucine zipper motif. J Biol Chem 2005; 280: 28430-8.
    • (2005) J Biol Chem , vol.280 , pp. 28430-28438
    • Li, W.1    Jain, M.R.2    Chen, C.3    Yue, X.4    Hebbar, V.5    Zhou, R.6
  • 26
    • 33748752586 scopus 로고    scopus 로고
    • Nrf2 possesses a redox-sensitive nuclear exporting signal in the Neh5 transactivation domain
    • Li W, yu SW, Kong AN. Nrf2 possesses a redox-sensitive nuclear exporting signal in the Neh5 transactivation domain. J Biol Chem 2006; 281: 27251-63.
    • (2006) J Biol Chem , vol.281 , pp. 27251-63
    • Li, W.1    Yu, S.W.2    Kong, A.N.3
  • 27
    • 23844475091 scopus 로고    scopus 로고
    • Nuclear import and export signals in control of Nrf2
    • Jain AK, Bloom DA, Jaiswal AK. Nuclear import and export signals in control of Nrf2. J Biol Chem 2005; 280: 29158-68.
    • (2005) J Biol Chem , vol.280 , pp. 29158-68
    • Jain, A.K.1    Bloom, D.A.2    Jaiswal, A.K.3
  • 28
    • 44049093741 scopus 로고    scopus 로고
    • Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2
    • Theodore M, Kawai Y, Yang J, Kleshchenko Y, Reddy SP, Villalta F, et al. Multiple nuclear localization signals function in the nuclear import of the transcription factor Nrf2. J Biol Chem 2008; 283: 8984-94.
    • (2008) J Biol Chem , vol.283 , pp. 8984-94
    • Theodore, M.1    Kawai, Y.2    Yang, J.3    Kleshchenko, Y.4    Reddy, S.P.5    Villalta, F.6
  • 29
    • 59849113546 scopus 로고    scopus 로고
    • Molecular mechanisms of Nrf2-mediated antioxidant response
    • Li W, Kong AN. Molecular mechanisms of Nrf2-mediated antioxidant response. Mol Carcinog 2009; 48: 91-104
    • (2009) Mol Carcinog , vol.48 , pp. 91-104
    • Li, W.1    Kong, A.N.2
  • 30
    • 2942568014 scopus 로고    scopus 로고
    • Dietary chemopreventive compounds and ARE/EpRE signaling
    • Chen C, Kong AN. Dietary chemopreventive compounds and ARE/EpRE signaling. Free Radic Biol Med 2004; 36: 1505-16.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1505-16
    • Chen, C.1    Kong, A.N.2
  • 31
    • 0035965945 scopus 로고    scopus 로고
    • Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention
    • Hayes JD, McMahon M. Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention. Cancer Lett 2001; 174: 103-13.
    • (2001) Cancer Lett , vol.174 , pp. 103-13
    • Hayes, J.D.1    McMahon, M.2
  • 32
    • 0025145723 scopus 로고
    • Tichauer y, Daniel V. Xenobiotic- inducible expression of murine glutathione S-transferase ya subunit gene is controlled by an electrophile-responsive element
    • Friling RS, Bensimon A, Tichauer y, Daniel V. Xenobiotic- inducible expression of murine glutathione S-transferase ya subunit gene is controlled by an electrophile-responsive element. Proc Natl Acad Sci USA 1990; 87: 6258-62.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6258-62
    • Friling, R.S.1    Bensimon, A.2
  • 33
    • 0037667901 scopus 로고    scopus 로고
    • Positive and negative regulation of prostaglandin E2 biosynthesis in human colorectal carcinoma cells by cancer chemopreventive agents
    • Sherratt PJ, McLellan LI, Hayes JD. Positive and negative regulation of prostaglandin E2 biosynthesis in human colorectal carcinoma cells by cancer chemopreventive agents. Biochem Pharmacol 2003; 66: 51-61.
    • (2003) Biochem Pharmacol , vol.66 , pp. 51-61
    • Sherratt, P.J.1    McLellan, L.I.2    Hayes, J.D.3
  • 34
    • 0037160092 scopus 로고    scopus 로고
    • Electrophile response element-mediated induction of the cystine/glutamate exchange transporter gene expression
    • Sasaki H, Sato H, Kuriyama-Matsumura K, Sato K, Maebara K, Wang H, et al. Electrophile response element-mediated induction of the cystine/glutamate exchange transporter gene expression. J Biol Chem 2002; 277: 44765-71.
    • (2002) J Biol Chem , vol.277 , pp. 44765-71
    • Sasaki, H.1    Sato, H.2    Kuriyama-Matsumura, K.3    Sato, K.4    Maebara, K.5    Wang, H.6
  • 35
    • 0035199904 scopus 로고    scopus 로고
    • Regulation of human apolipoprotein A-I gene expression by equine estrogens
    • Zhang X, Jiao JJ, Bhavnani BR, Tam SP. Regulation of human apolipoprotein A-I gene expression by equine estrogens. J Lipid Res 2001; 42: 1789-800.
    • (2001) J Lipid Res , vol.42 , pp. 1789-800
    • Zhang, X.1    Jiao, J.J.2    Bhavnani, B.R.3    Tam, S.P.4
  • 36
    • 0034333416 scopus 로고    scopus 로고
    • Profiles of antioxidant/electrophile response element (ARE/ EpRE) nuclear protein binding and c-Ha-ras transactivation in vascular smooth muscle cells treated with oxidative metabolites of benzo[a]pyrene
    • Miller KP, Chen YH, Hastings VL, Bral CM, Ramos KS. Profiles of antioxidant/electrophile response element (ARE/ EpRE) nuclear protein binding and c-Ha-ras transactivation in vascular smooth muscle cells treated with oxidative metabolites of benzo[a]pyrene. Biochem Pharmacol 2000; 60: 1285-96.
    • (2000) Biochem Pharmacol , vol.60 , pp. 1285-96
    • Miller, K.P.1    Chen, Y.H.2    Hastings, V.L.3    Bral, C.M.4    Ramos, K.S.5
  • 37
    • 0026755187 scopus 로고
    • Regulation of human NAD(P)H: Quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element
    • Li Y, Jaiswal AK. Regulation of human NAD(P)H: quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element. J Biol Chem 1992; 267: 15097-104.
    • (1992) J Biol Chem , vol.267 , pp. 15097-104
    • Li, Y.1    Jaiswal, A.K.2
  • 38
  • 39
    • 0031000208 scopus 로고    scopus 로고
    • Functional antioxidant responsive elements
    • Wasserman WW, Fahl WE. Functional antioxidant responsive elements. Proc Natl Acad Sci USA 1997; 94: 5361-6.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5361-5366
    • Wasserman, W.W.1    Fahl, W.E.2
  • 40
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii T, Itoh K, Takahashi S, Sato H, yanagawa T, Katoh Y, et al. Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J Biol Chem 2000; 275: 16023-9.
    • (2000) J Biol Chem , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6
  • 41
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • Itoh K, Chiba T, Takahashi S, Ishii T, Igarashi K, Katoh Y, et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem Biophys Res Commun 1997; 236: 313-22.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 313-22
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3    Ishii, T.4    Igarashi, K.5    Katoh, Y.6
  • 42
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J, Stewart D, Touchard C, Boinapally S, Choi AM, Cook JL. Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. Biol Chem 1999; 274: 26071-8.
    • (1999) Biol Chem , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 43
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of gamma- glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • Wild AC, Moinova HR, Mulcahy RT. Regulation of gamma- glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2. J Biol Chem 1999; 274: 33627-36.
    • (1999) J Biol Chem , vol.274 , pp. 33627-36
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 44
    • 0033525730 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of a new Cap'n' collar family transcription factor Nrf3
    • Kobayashi A, Ito E, Toki T, Kogame K, Takahashi S, Igarashi K, et al. Molecular cloning and functional characterization of a new Cap'n' collar family transcription factor Nrf3. J Biol Chem 1999; 274: 6443-52.
    • (1999) J Biol Chem , vol.274 , pp. 6443-52
    • Kobayashi, A.1    Ito, E.2    Toki, T.3    Kogame, K.4    Takahashi, S.5    Igarashi, K.6
  • 45
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino- terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, et al. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino- terminal Neh2 domain. Genes Dev 1999; 13: 76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6
  • 46
    • 0035963293 scopus 로고    scopus 로고
    • Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H: Quinone oxidoreductase1 gene
    • Dhakshinamoorthy S, Jaiswal AK. Functional characterization and role of INrf2 in antioxidant response element-mediated expression and antioxidant induction of NAD(P)H: quinone oxidoreductase1 gene. Oncogene 2001; 20: 3906-17
    • (2001) Oncogene , vol.20 , pp. 3906-17
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 47
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang MI, Kobayashi A, Wakabayashi N, Kim SG, yamamoto M. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc Natl Acad Sci USA 2004; 101: 2046-51.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2046-51
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 48
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang DD, Lo SC, Cross JV, Templeton DJ, Hannink M. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol Cell Biol 2004; 24: 10941-53.
    • (2004) Mol Cell Biol , vol.24 , pp. 10941-53
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 49
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang DD, Hannink M. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 2003; 23: 8137-51.
    • (2003) Mol Cell Biol , vol.23 , pp. 8137-51
    • Zhang, D.D.1    Hannink, M.2
  • 50
    • 42149196050 scopus 로고    scopus 로고
    • Physiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activity
    • yamamoto T, Suzuki T, Kobayashi A, Wakabayashi J, Maher J, Motohashi H, et al. Physiological significance of reactive cysteine residues of Keap1 in determining Nrf2 activity. Mol Cell Biol 2008; 28: 2758-70.
    • (2008) Mol Cell Biol , vol.28 , pp. 2758-70
    • Yamamoto, T.1    Suzuki, T.2    Kobayashi, A.3    Wakabayashi, J.4    Maher, J.5    Motohashi, H.6
  • 52
    • 67449128222 scopus 로고    scopus 로고
    • Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response
    • Chen W, Sun Z, Wang XJ, Jiang T, Huang Z, Fang D, et al. Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response. Mol Cell 2009; 34: 663-73.
    • (2009) Mol Cell , vol.34 , pp. 663-73
    • Chen, W.1    Sun, Z.2    Wang, X.J.3    Jiang, T.4    Huang, Z.5    Fang, D.6
  • 53
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D, Killeen E, Naquin R, Alam S, Alam J. Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J Biol Chem 2003; 278: 2396-402.
    • (2003) J Biol Chem , vol.278 , pp. 2396-402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 54
    • 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: 4536-41.
    • (2003) J Biol Chem , vol.278 , pp. 4536-41
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, C.B.5
  • 55
    • 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 Cells 2003; 8: 379-91.
    • (2003) Genes Cells , vol.8 , pp. 379-91
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 56
    • 0242666198 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/ accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H: Quinone oxidoreductase-1 gene expression
    • Bloom DA, Jaiswal AK. Phosphorylation of Nrf2 at Ser40 by protein kinase C in response to antioxidants leads to the release of Nrf2 from INrf2, but is not required for Nrf2 stabilization/ accumulation in the nucleus and transcriptional activation of antioxidant response element-mediated NAD(P)H: quinone oxidoreductase-1 gene expression. J Biol Chem 2003; 278: 44675-82.
    • (2003) J Biol Chem , vol.278 , pp. 44675-82
    • Bloom, D.A.1    Jaiswal, A.K.2
  • 57
    • 0037821802 scopus 로고    scopus 로고
    • Keap1- dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression
    • McMahon M, Itoh K, yamamoto M, Hayes JD. Keap1- dependent proteasomal degradation of transcription factor Nrf2 contributes to the negative regulation of antioxidant response element-driven gene expression. J Biol Chem 2003; 278: 21592-600.
    • (2003) J Biol Chem , vol.278 , pp. 21592-600
    • McMahon, M.1    Itoh, K.2    Yamamoto, M.3    Hayes, J.D.4
  • 58
    • 37549032763 scopus 로고    scopus 로고
    • An auto-regulatory loop between stress sensors INrf2 and Nrf2 controls their cellular abundance
    • Lee OH, Jain AK, Papusha V, Jaiswal AK. An auto-regulatory loop between stress sensors INrf2 and Nrf2 controls their cellular abundance. J Biol Chem 2007; 282: 36412-20.
    • (2007) J Biol Chem , vol.282 , pp. 36412-20
    • Lee, O.H.1    Jain, A.K.2    Papusha, V.3    Jaiswal, A.K.4
  • 60
    • 0034704079 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism
    • Yu R, Chen C, Mo YY, Hebbar V, Owuor ED, Tan TH, et al. Activation of mitogen-activated protein kinase pathways induces antioxidant response element-mediated gene expression via a Nrf2-dependent mechanism. J Biol Chem 2000; 275: 39907-13.
    • (2000) J Biol Chem , vol.275 , pp. 39907-13
    • Yu, R.1    Chen, C.2    Mo, Y.Y.3    Hebbar, V.4    Owuor, E.D.5    Tan, T.H.6
  • 61
    • 0038663090 scopus 로고    scopus 로고
    • Erk activation is required for Nrf2 nuclear localization during pyrrolidine dithiocarbamate induction of glutamate cysteine ligase modulatory gene expression in HepG2 cells
    • Zipper LM, Mulcahy RT. Erk activation is required for Nrf2 nuclear localization during pyrrolidine dithiocarbamate induction of glutamate cysteine ligase modulatory gene expression in HepG2 cells. Toxicol Sci 2003; 73: 124-34.
    • (2003) Toxicol Sci , vol.73 , pp. 124-34
    • Zipper, L.M.1    Mulcahy, R.T.2
  • 62
    • 41149177653 scopus 로고    scopus 로고
    • Suppression of Nrf2-driven heme oxygenase-1 enhances the chemosensitivity of lung cancer A549 cells toward cisplatin
    • Kim HR, Kim S, Kim EJ, Park JH, yang SH, Jeong ET, et al. Suppression of Nrf2-driven heme oxygenase-1 enhances the chemosensitivity of lung cancer A549 cells toward cisplatin. Lung Cancer 2008; 60: 47-56.
    • (2008) Lung Cancer , vol.60 , pp. 47-56
    • Kim, H.R.1    Kim, S.2    Kim, E.J.3    Park, J.H.4    Yang, S.H.5    Jeong, E.T.6
  • 63
    • 0033731182 scopus 로고    scopus 로고
    • Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2
    • Huang HC, Nguyen T, Pickett CB. Regulation of the antioxidant response element by protein kinase C-mediated phosphorylation of NF-E2-related factor 2. Proc Natl Acad Sci USA 2000; 97: 12475-80.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12475-80
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 64
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription
    • Huang HC, Nguyen T, Pickett CB. Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response element-mediated transcription. J Biol Chem 2002; 277: 42769-74.
    • (2002) J Biol Chem , vol.277 , pp. 42769-74
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 65
    • 0034805627 scopus 로고    scopus 로고
    • Nrf2- dependent activation of the antioxidant responsive element by tert-butylhydroquinone is independent of oxidative stress in IMR-32 human neuroblastoma cells
    • Lee JM, Moehlenkamp JD, Hanson JM, Johnson JA. Nrf2- dependent activation of the antioxidant responsive element by tert-butylhydroquinone is independent of oxidative stress in IMR-32 human neuroblastoma cells. Biochem Biophys Res Commun 2001; 280: 286-92.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 286-92
    • Lee, J.M.1    Moehlenkamp, J.D.2    Hanson, J.M.3    Johnson, J.A.4
  • 66
    • 0038537298 scopus 로고    scopus 로고
    • 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
    • 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: 181-4.
    • (2003) FEBS Lett , vol.546 , pp. 181-184
    • Nakaso, K.1    Yano, H.2
  • 67
    • 0036840585 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress
    • Kang KW, Lee SJ, Park JW, Kim SG. Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress. Mol Pharmacol 2002; 62: 1001-10.
    • (2002) Mol Pharmacol , vol.62 , pp. 1001-10
    • Kang, K.W.1    Lee, S.J.2    Park, J.W.3    Kim, S.G.4
  • 68
    • 34447526197 scopus 로고    scopus 로고
    • GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2
    • Jain AK, Jaiswal AK. GSK-3beta acts upstream of Fyn kinase in regulation of nuclear export and degradation of NF-E2 related factor 2. J Biol Chem 2007; 282: 16502-10.
    • (2007) J Biol Chem , vol.282 , pp. 16502-10
    • Jain, A.K.1    Jaiswal, A.K.2
  • 69
    • 41149134840 scopus 로고    scopus 로고
    • GSK-3beta down-regulates the transcription factor Nrf2 after oxidant damage: Relevance to exposure of neuronal cells to oxidative stress
    • Rojo AI, Sagarra MR, Cuadrado A. GSK-3beta down-regulates the transcription factor Nrf2 after oxidant damage: relevance to exposure of neuronal cells to oxidative stress. J Neurochem 2008; 105: 192-202.
    • (2008) J Neurochem , vol.105 , pp. 192-202
    • Rojo, A.I.1    Sagarra, M.R.2    Cuadrado, A.3
  • 70
    • 0037015035 scopus 로고    scopus 로고
    • Katoh y, et al. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova AT, Holtzclaw WD, Cole RN, Itoh K, Wakabayashi N, Katoh y, et al. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci USA 2002; 99: 11908-13.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11908-13
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5
  • 72
    • 0035853157 scopus 로고    scopus 로고
    • Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice
    • Ramos-Gomez M, Kwak MK, Dolan PM, Itoh K, yamamoto M, Talalay P, et al. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in nrf2 transcription factor-deficient mice. Proc Natl Acad Sci USA 2001; 98: 3410-5.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 3410-3415
    • Ramos-Gomez, M.1    Kwak, M.K.2    Dolan, P.M.3    Itoh, K.4    Yamamoto, M.5    Talalay, P.6
  • 73
    • 4644328941 scopus 로고    scopus 로고
    • Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesis
    • Iida K, Itoh K, Kumagai Y, Oyasu R, Hattori K, Kawai K, et al. Nrf2 is essential for the chemopreventive efficacy of oltipraz against urinary bladder carcinogenesis. Cancer Res 2004; 64: 6424-31.
    • (2004) Cancer Res , vol.64 , pp. 6424-31
    • Iida, K.1    Itoh, K.2    Kumagai, Y.3    Oyasu, R.4    Hattori, K.5    Kawai, K.6
  • 74
    • 36148977625 scopus 로고    scopus 로고
    • Nrf2 and p53 cooperatively protect against BBN-induced urinary bladder carcinogenesis
    • Iida K, Itoh K, Maher JM, Kumagai Y, Oyasu R, Mori Y, et al. Nrf2 and p53 cooperatively protect against BBN-induced urinary bladder carcinogenesis. Carcinogenesis 2007; 28: 2398-403.
    • (2007) Carcinogenesis , vol.28 , pp. 2398-403
    • Iida, K.1    Itoh, K.2    Maher, J.M.3    Kumagai, Y.4    Oyasu, R.5    Mori, Y.6
  • 75
    • 56249086316 scopus 로고    scopus 로고
    • Increased susceptibility of Nrf2 knockout mice to colitis- associated colorectal cancer
    • Khor TO, Huang MT, Prawan A, Liu Y, Hao X, Yu S, et al. Increased susceptibility of Nrf2 knockout mice to colitis- associated colorectal cancer. Cancer Prev Res (Phila Pa) 2008; 1: 187-91.
    • (2008) Cancer Prev Res (Phila Pa) , vol.1 , pp. 187-91
    • Khor, T.O.1    Huang, M.T.2    Prawan, A.3    Liu, Y.4    Hao, X.5    Yu, S.6
  • 76
    • 34648830424 scopus 로고    scopus 로고
    • Increased colonic inflammatory injury and formation of aberrant crypt foci in Nrf2-deficient mice upon dextran sulfate treatment
    • Osburn WO, Karim B, Dolan PM, Liu G, yamamoto M, Huso DL, et al. Increased colonic inflammatory injury and formation of aberrant crypt foci in Nrf2-deficient mice upon dextran sulfate treatment. Int J Cancer 2007; 121: 1883-91.
    • (2007) Int J Cancer , vol.121 , pp. 1883-91
    • Osburn, W.O.1    Karim, B.2    Dolan, P.M.3    Liu, G.4    Yamamoto, M.5    Huso, D.L.6
  • 77
    • 33748089664 scopus 로고    scopus 로고
    • Inhibition of 7,12-dimethylbenz(a)anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2
    • Xu C, Huang MT, Shen G, yuan X, Lin W, Khor TO, et al. Inhibition of 7,12-dimethylbenz(a)anthracene-induced skin tumorigenesis in C57BL/6 mice by sulforaphane is mediated by nuclear factor E2-related factor 2. Cancer Res 2006; 66: 8293-6.
    • (2006) Cancer Res , vol.66 , pp. 8293-8296
    • Xu, C.1    Huang, M.T.2    Shen, G.3    Yuan, X.4    Lin, W.5    Khor, T.O.6
  • 78
    • 77649270763 scopus 로고    scopus 로고
    • Targeting NRF2 signaling for cancer chemoprevention
    • Kwak MK, Kensler TW. Targeting NRF2 signaling for cancer chemoprevention. Toxicol Appl Pharmacol 2010; 244: 66-76.
    • (2010) Toxicol Appl Pharmacol , vol.244 , pp. 66-76
    • Kwak, M.K.1    Kensler, T.W.2
  • 79
    • 46949099638 scopus 로고    scopus 로고
    • Nrf2 enhances resistance of cancer cells to chemotherapeutic drugs, the dark side of Nrf2
    • Wang XJ, Sun Z, Villeneuve NF, Zhang S, Zhao F, Li Y, et al. Nrf2 enhances resistance of cancer cells to chemotherapeutic drugs, the dark side of Nrf2. Carcinogenesis 2008; 29: 1235-43.
    • (2008) Carcinogenesis , vol.29 , pp. 1235-43
    • Wang, X.J.1    Sun, Z.2    Villeneuve, N.F.3    Zhang, S.4    Zhao, F.5    Li, Y.6
  • 80
    • 2942746263 scopus 로고    scopus 로고
    • Transcription factor Nrf2/MafK regulates rat placental glutathione S-transferase gene during hepatocarcinogenesis
    • Ikeda H, Nishi S, Sakai M. Transcription factor Nrf2/MafK regulates rat placental glutathione S-transferase gene during hepatocarcinogenesis. Biochem J 2004; 380: 515-21.
    • (2004) Biochem J , vol.380 , pp. 515-21
    • Ikeda, H.1    Nishi, S.2    Sakai, M.3
  • 81
    • 33344456501 scopus 로고    scopus 로고
    • Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer
    • Padmanabhan B, Tong KI, Ohta T, Nakamura Y, Scharlock M, Ohtsuji M, et al. Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer. Mol Cell 2006; 21: 689-700.
    • (2006) Mol Cell , vol.21 , pp. 689-700
    • Padmanabhan, B.1    Tong, K.I.2    Ohta, T.3    Nakamura, Y.4    Scharlock, M.5    Ohtsuji, M.6
  • 82
    • 40449107193 scopus 로고    scopus 로고
    • Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth
    • Ohta T, Iijima K, Miyamoto M, Nakahara I, Tanaka H, Ohtsuji M, et al. Loss of Keap1 function activates Nrf2 and provides advantages for lung cancer cell growth. Cancer Res 2008; 68: 1303-9.
    • (2008) Cancer Res , vol.68 , pp. 1303-1309
    • Ohta, T.1    Iijima, K.2    Miyamoto, M.3    Nakahara, I.4    Tanaka, H.5    Ohtsuji, M.6
  • 84
    • 33644856080 scopus 로고    scopus 로고
    • The double-edged sword of Nrf2: Subversion of redox homeostasis during the evolution of cancer
    • Hayes JD, McMahon M. The double-edged sword of Nrf2: subversion of redox homeostasis during the evolution of cancer. Mol Cell 2006; 21: 732-4.
    • (2006) Mol Cell , vol.21 , pp. 732-734
    • Hayes, J.D.1    McMahon, M.2
  • 85
    • 53049105119 scopus 로고    scopus 로고
    • Genetic alteration of Keap1 confers constitutive Nrf2 activation and resistance to chemotherapy in gallbladder cancer
    • Shibata T, Kokubu A, Gotoh M, Ojima H, Ohta T, yamamoto M, et al. Genetic alteration of Keap1 confers constitutive Nrf2 activation and resistance to chemotherapy in gallbladder cancer. Gastroenterology 2008; 135: 1358-68.
    • (2008) Gastroenterology , vol.135 , pp. 1358-68
    • Shibata, T.1    Kokubu, A.2    Gotoh, M.3    Ojima, H.4    Ohta, T.5    Yamamoto, M.6
  • 86
    • 34548577395 scopus 로고    scopus 로고
    • A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity
    • Nioi P, Nguyen T. A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity. Biochem Biophys Res Commun 2007; 362: 816-21.
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 816-21
    • Nioi, P.1    Nguyen, T.2
  • 87
    • 68849092533 scopus 로고    scopus 로고
    • Cul3 overexpression depletes Nrf2 in breast cancer and is associated with sensitivity to carcinogens, to oxidative stress, and to chemotherapy
    • Loignon M, Miao W, Hu L, Bier A, Bismar TA, Scrivens PJ, et al. Cul3 overexpression depletes Nrf2 in breast cancer and is associated with sensitivity to carcinogens, to oxidative stress, and to chemotherapy. Mol Cancer Ther 2009; 8: 2432-40.
    • (2009) Mol Cancer Ther , vol.8 , pp. 2432-40
    • Loignon, M.1    Miao, W.2    Hu, L.3    Bier, A.4    Bismar, T.A.5    Scrivens, P.J.6
  • 92
    • 41949141296 scopus 로고    scopus 로고
    • NF-?B/p65 antagonizes Nrf2- ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK
    • Liu GH, Qu J, Shen X. NF-?B/p65 antagonizes Nrf2- ARE pathway by depriving CBP from Nrf2 and facilitating recruitment of HDAC3 to MafK. Biochim Biophys Acta 2008; 1783: 713-27.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 713-27
    • Liu, G.H.1    Qu, J.2    Shen, X.3
  • 93
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998; 16: 225-60.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-60
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 94
    • 46049090192 scopus 로고    scopus 로고
    • Tumor promoting or tumor suppressing of NF-kappa B, a matter of cell context dependency
    • Chen F, Beezhold K, Castranova V. Tumor promoting or tumor suppressing of NF-kappa B, a matter of cell context dependency. Int Rev Immunol 2008; 27: 183-204.
    • (2008) Int Rev Immunol , vol.27 , pp. 183-204
    • Chen, F.1    Beezhold, K.2    Castranova, V.3
  • 95
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic Biol Med 1991; 11: 81-128.
    • (1991) Free Radic Biol Med , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 96
    • 0033213329 scopus 로고    scopus 로고
    • Redl H, et al. 4-Hydroxynonenal as a second messenger of free radicals and growth modifying factor
    • Zarkovic N, Zarkovic K, Schaur RJ, Stolc S, Schlag G, Redl H, et al. 4-Hydroxynonenal as a second messenger of free radicals and growth modifying factor. Life Sci 1999; 65: 1901-4.
    • (1999) Life Sci , vol.65 , pp. 1901-1904
    • Zarkovic, N.1    Zarkovic, K.2    Schaur, R.J.3    Stolc, S.4    Schlag, G.5
  • 97
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: A product and mediator of oxidative stress
    • Uchida K. 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog Lipid Res 2003; 42: 318-43.
    • (2003) Prog Lipid Res , vol.42 , pp. 318-43
    • Uchida, K.1
  • 98
    • 0043172469 scopus 로고    scopus 로고
    • 4-hydroxynonenal as a bioactive marker of pathophysiological processes
    • Zarkovic N. 4-hydroxynonenal as a bioactive marker of pathophysiological processes. Mol Aspects Med 2003; 24: 281-91.
    • (2003) Mol Aspects Med , vol.24 , pp. 281-91
    • Zarkovic, N.1
  • 101
    • 28644440011 scopus 로고    scopus 로고
    • The influence of 4-hydroxy-2-nonenal on proliferation, differentiation and apoptosis of human osteosarcoma cells
    • Borovic Sunjic S, Cipak A, Rabuzin F, Wildburger R, Zarkovic N. The influence of 4-hydroxy-2-nonenal on proliferation, differentiation and apoptosis of human osteosarcoma cells. Biofactors 2005; 24: 141-8.
    • (2005) Biofactors , vol.24 , pp. 141-148
    • Borovic, S.S.1    Cipak, A.2    Rabuzin, F.3    Wildburger, R.4    Zarkovic, N.5
  • 104
    • 0034903730 scopus 로고    scopus 로고
    • The carcinostatic and proapoptotic potential of4-hydroxynonenal in HeLa cells is associated with its conjugation to cellular proteins
    • Sovic A, Borovic S, Loncaric I, Kreuzer T, Zarkovic K, Vukovic T, et al. The carcinostatic and proapoptotic potential of4-hydroxynonenal in HeLa cells is associated with its conjugation to cellular proteins. Anticancer Res 2001; 21: 1997-2004.
    • (2001) Anticancer Res , vol.21 , pp. 1997-2004
    • Sovic, A.1    Borovic, S.2    Loncaric, I.3    Kreuzer, T.4    Zarkovic, K.5    Vukovic, T.6
  • 105
    • 0041742490 scopus 로고    scopus 로고
    • Atypical protein kinase C mediates activation of NF-E2- related factor 2 in response to oxidative stress
    • Numazawa S, Ishikawa M, yoshida A, Tanaka S, yoshida T. Atypical protein kinase C mediates activation of NF-E2- related factor 2 in response to oxidative stress. Am J Physiol Cell Physiol 2003; 285: C334-42.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Numazawa, S.1    Ishikawa, M.2    Yoshida, A.3    Tanaka, S.4    Yoshida, T.5


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