메뉴 건너뛰기




Volumn 4, Issue 11, 2013, Pages

Erratum: Jun dimerization protein 2 is a critical component of the Nrf2/MafK complex regulating the response to ROS homeostasis (Cell Death and Disease (2013) 4 (e921) DOI: 10.1038/cddis.2013.448);Jun dimerization protein 2 is a critical component of the Nrf2/MafK complex regulating the response to ROS homeostasis

Author keywords

Antioxidant enzymes; Antioxidation; JDP2; Nrf2 MafK; ROS regulation

Indexed keywords

GLUTAMATE CYSTEINE LIGASE; HEME OXYGENASE 1; JAGGED1; JUN DIMERIZATION PROTEIN 2; LEUCINE ZIPPER PROTEIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR MAFK; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 84889583650     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.322     Document Type: Erratum
Times cited : (53)

References (53)
  • 1
    • 22344438250 scopus 로고    scopus 로고
    • Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice
    • Rangasamy T, Guo J, Mitzner WA, Roman J, Singh A, Fryer AD, et al. Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice. J Exp Med 2005; 202: 47-59
    • (2005) J Exp Med , vol.202 , pp. 47-59
    • Rangasamy, T.1    Guo, J.2    Mitzner, W.A.3    Roman, J.4    Singh, A.5    Fryer, A.D.6
  • 2
    • 33644501791 scopus 로고    scopus 로고
    • Activation of the Nrf2-ARE signaling pathway: A promising strategy in cancer prevention
    • Giudice A, Montella M. Activation of the Nrf2-ARE signaling pathway: A promising strategy in cancer prevention. BioEssays 2006; 28: 169-181
    • (2006) BioEssays , vol.28 , pp. 169-181
    • Giudice, A.1    Montella, M.2
  • 3
    • 33846264538 scopus 로고    scopus 로고
    • Nrf2-deficient mice have an increased susceptibility to dextran sulfate sodium-induced colitis
    • Khor TO, Huang MT, Kwon KH, Chan JY, Reddy BS, Kong AN. Nrf2-deficient mice have an increased susceptibility to dextran sulfate sodium-induced colitis. Cancer Res 2006; 66: 11580-11584
    • (2006) Cancer Res , vol.66 , pp. 11580-11584
    • Khor, T.O.1    Huang, M.T.2    Kwon, K.H.3    Chan, J.Y.4    Reddy, B.S.5    Kong, A.N.6
  • 4
    • 33646561819 scopus 로고    scopus 로고
    • Nrf transcription factors in keratinocytes are essential for skin tumor prevention but not for wound healing
    • Auf dem Keller U, Huber M, Beyer TA, Kumin A, Siemes C, Braun S, et al. Nrf transcription factors in keratinocytes are essential for skin tumor prevention but not for wound healing. Mol Cell Bio 2006; 26: 3773-3784
    • (2006) Mol Cell Bio , vol.26 , pp. 3773-3784
    • Auf Dem Keller, U.1    Huber, M.2    Beyer, T.A.3    Kumin, A.4    Siemes, C.5    Braun, S.6
  • 5
    • 0025368036 scopus 로고
    • Regulation of glutathione S-Transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds
    • Rushmore TH, King RG, Paulson KE, Pickett CB. Regulation of glutathione S-Transferase Ya subunit gene expression: Identification of a unique xenobiotic-responsive element controlling inducible expression by planar aromatic compounds. Proc Natl Acad Sci USA 1990; 87: 3826-3830
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3826-3830
    • Rushmore, T.H.1    King, R.G.2    Paulson, K.E.3    Pickett, C.B.4
  • 6
    • 0029000906 scopus 로고
    • Antitumor promotion by phenolic antioxidants: Inhibition of AP-1 activity through induction of Fra expression
    • Yoshioka K, Deng T, Cavigelli M, Karin M. Antitumor promotion by phenolic antioxidants: Inhibition of AP-1 activity through induction of Fra expression. Proc Natl Acad Sci USA 1995; 92: 4972-4976
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4972-4976
    • Yoshioka, K.1    Deng, T.2    Cavigelli, M.3    Karin, M.4
  • 7
    • 0029945755 scopus 로고    scopus 로고
    • The heme-responsive element of the mouse heme oxygenase-1 gene is an extended AP-1 binding site that resembles the recognition sequences for MAF and NF-E2 transcription factors
    • Inamdar NM, Ahn YI, Alam J. The heme-responsive element of the mouse heme oxygenase-1 gene is an extended AP-1 binding site that resembles the recognition sequences for MAF and NF-E2 transcription factors. Biochem Biophys Res Commum 1996; 221: 570-576
    • (1996) Biochem Biophys Res Commum , vol.221 , pp. 570-576
    • Inamdar, N.M.1    Ahn, Y.I.2    Alam, J.3
  • 8
    • 0035940984 scopus 로고    scopus 로고
    • Functional characterization of transcription regulators that interact with the electrophile response element
    • Zhu M, Fahl WE. Functional characterization of transcription regulators that interact with the electrophile response element. Biochem Biophys Res Commum 2001; 289: 212-219
    • (2001) Biochem Biophys Res Commum , vol.289 , pp. 212-219
    • Zhu, M.1    Fahl, W.E.2
  • 9
    • 0035374431 scopus 로고    scopus 로고
    • Fisetin induces transcription of NADPH:quinone oxidoreductase gene through an antioxidant responsive element-involved activation
    • Hou DX, Fukuda M, Johnson JA, Miyamori K, Ushikai M, Fujii M. Fisetin induces transcription of NADPH:quinone oxidoreductase gene through an antioxidant responsive element-involved activation. Int J Oncology 2001; 18: 1175-1179
    • (2001) Int J Oncology , vol.18 , pp. 1175-1179
    • Hou, D.X.1    Fukuda, M.2    Johnson, J.A.3    Miyamori, K.4    Ushikai, M.5    Fujii, M.6
  • 11
    • 0034685897 scopus 로고    scopus 로고
    • Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK
    • Nguyen T, Huang HC, Pickett CB. Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK. J Biol Chem 2000; 275: 15466-15473
    • (2000) J Biol Chem , vol.275 , pp. 15466-15473
    • Nguyen, T.1    Huang, H.C.2    Pickett, C.B.3
  • 12
    • 24344479164 scopus 로고    scopus 로고
    • Genetic evidence that small maf proteins are essential for the activation of antioxidant response elementdependent genes
    • Katsuoka F, Motohashi H, Ishii T, Aburatani H, Engel JD, Yamamoto M. Genetic evidence that small maf proteins are essential for the activation of antioxidant response elementdependent genes. Mol Cell Biol 2005; 25: 8044-8051
    • (2005) Mol Cell Biol , vol.25 , pp. 8044-8051
    • Katsuoka, F.1    Motohashi, H.2    Ishii, T.3    Aburatani, H.4    Engel, J.D.5    Yamamoto, M.6
  • 13
    • 39049129643 scopus 로고    scopus 로고
    • Small Maf proteins in mammalian gene control mere dimerization partners or dynamic transcriptional regulators
    • Blank V. Small Maf proteins in mammalian gene control: Mere dimerization partners or dynamic transcriptional regulators? J Mol Biol 2008; 376: 913-925
    • (2008) J Mol Biol , vol.376 , pp. 913-925
    • Blank, V.1
  • 14
    • 0030923133 scopus 로고    scopus 로고
    • Isolation of an ap-1 repressor by a novel method for detecting protein-protein interactions
    • Aronheim A, Zandi E, Hennemann H, Elledge SJ, Karin M. Isolation of an AP-1 repressor by a novel method for detecting protein-protein interactions. Mol Cell Biol 1997; 17: 3094-3102
    • (1997) Mol Cell Biol , vol.17 , pp. 3094-3102
    • Aronheim, A.1    Zandi, E.2    Hennemann, H.3    Elledge, S.J.4    Karin, M.5
  • 15
    • 0035951349 scopus 로고    scopus 로고
    • Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2
    • Jin C, Ugai H, Song J, Murata T, Nili F, Sun K, et al. Identification of mouse Jun dimerization protein 2 as a novel repressor of ATF-2. FEBS letters 2001; 489: 34-41
    • (2001) FEBS letters , vol.489 , pp. 34-41
    • Jin, C.1    Ugai, H.2    Song, J.3    Murata, T.4    Nili, F.5    Sun, K.6
  • 16
    • 78649517596 scopus 로고    scopus 로고
    • Suppression of cellcycle progression by Jun dimerization protein-2 (JDP2) involves downregulation of cyclin-A2
    • Pan J, Nakade K, Huang YC, Zhu ZW, Masuzaki S, Hasegawa H, et al. Suppression of cellcycle progression by Jun dimerization protein-2 (JDP2) involves downregulation of cyclin-A2. Oncogene 2010; 29: 6245-6256
    • (2010) Oncogene , vol.29 , pp. 6245-6256
    • Pan, J.1    Nakade, K.2    Huang, Y.C.3    Zhu, Z.W.4    Masuzaki, S.5    Hasegawa, H.6
  • 17
    • 0032497564 scopus 로고    scopus 로고
    • The ras recruitment system, a novel approach to the stuidy of protein-protein interascvtions
    • Broder YC, Katz S, Aronheim A. The ras recruitment system, a novel approach to the stuidy of protein-protein interascvtions. Curr Biol 1998; 8: 1121-1124
    • (1998) Curr Biol , vol.8 , pp. 1121-1124
    • Broder, Y.C.1    Katz, S.2    Aronheim, A.3
  • 19
    • 0036272787 scopus 로고    scopus 로고
    • JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells
    • Jin C, Li H, Murata T, Sun K, Horikoshi M, Chiu R, et al. JDP2, a repressor of AP-1, recruits a histone deacetylase 3 complex to inhibit the retinoic acid-induced differentiation of F9 cells. Mol Cell Biol 2002; 22: 4815-4826
    • (2002) Mol Cell Biol , vol.22 , pp. 4815-4826
    • Jin, C.1    Li, H.2    Murata, T.3    Sun, K.4    Horikoshi, M.5    Chiu, R.6
  • 20
    • 33745032887 scopus 로고    scopus 로고
    • Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2
    • Jin C, Kato K, Chimura T, Yamasaki T, Nakade K, Murata T, et al. Regulation of histone acetylation and nucleosome assembly by transcription factor JDP2. Nat Struc Mol Biol 2006; 13: 331-338
    • (2006) Nat Struc Mol Biol , vol.13 , pp. 331-338
    • Jin, C.1    Kato, K.2    Chimura, T.3    Yamasaki, T.4    Nakade, K.5    Murata, T.6
  • 21
    • 0035850831 scopus 로고    scopus 로고
    • The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-Terminal kinase
    • Katz S, Heinrich R, Aronheim A. The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-Terminal kinase. FEBS Lett 2001; 506: 196-200
    • (2001) FEBS Lett , vol.506 , pp. 196-200
    • Katz, S.1    Heinrich, R.2    Aronheim, A.3
  • 22
    • 34447648044 scopus 로고    scopus 로고
    • JDP2 suppresses adipocyte differentiation by regulating histone acetylation
    • Nakade K, Pan J, Yoshiki A, Ugai H, Kimura M, Li H, et al. JDP2 suppresses adipocyte differentiation by regulating histone acetylation. Cell Death Differ 2007; 14: 1398-1405
    • (2007) Cell Death Differ , vol.14 , pp. 1398-1405
    • Nakade, K.1    Pan, J.2    Yoshiki, A.3    Ugai, H.4    Kimura, M.5    Li, H.6
  • 23
    • 84870909437 scopus 로고    scopus 로고
    • The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteroclast and neutrophil differentiation
    • Maruyama K, Fukasaka M, Vandenbon A, Saitoh T, Kawasaki T, Kondo T, et al. The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteroclast and neutrophil differentiation. Immunity 2012; 37: 1024-1036
    • (2012) Immunity , vol.37 , pp. 1024-1036
    • Maruyama, K.1    Fukasaka, M.2    Vandenbon, A.3    Saitoh, T.4    Kawasaki, T.5    Kondo, T.6
  • 24
    • 67449100494 scopus 로고    scopus 로고
    • Jdp2 (jun dimerization protein 2)-deficient mouse embryonic fibroblasts are resistant to replicative senescence
    • Nakade K, Pan J, Yamasaki T, Murata T, Wasylyk B, Yokoyama KK. JDP2 (Jun dimerization protein 2)-deficient mouse embryonic fibroblasts are resistant to replicative senescence. J Biol Chem 2009; 284: 10808-10817
    • (2009) J Biol Chem , vol.284 , pp. 10808-10817
    • Nakade, K.1    Pan, J.2    Yamasaki, T.3    Murata, T.4    Wasylyk, B.5    Yokoyama, K.K.6
  • 26
    • 79960060305 scopus 로고    scopus 로고
    • Oncogeneinduced Nrf2 transcription promotes ROS detoxification and tumorigenesis
    • Nicola GM, Karreth FA, Humpton TJ, Gopinsthan A, Wei C, Frese K, et al. Oncogeneinduced Nrf2 transcription promotes ROS detoxification and tumorigenesis. Nature 2011; 475: 106-111
    • (2011) Nature , vol.475 , pp. 106-111
    • Nicola, G.M.1    Karreth, F.A.2    Humpton, T.J.3    Gopinsthan, A.4    Wei, C.5    Frese, K.6
  • 27
    • 33645784167 scopus 로고    scopus 로고
    • The role of glutathione in disulphide bind formation and endoplasmic-reticulum-generated oxodative stress
    • Chakravarthi S, Jessop CE, Bulleid NJ. The role of glutathione in disulphide bind formation and endoplasmic-reticulum-generated oxodative stress. EMBO Rep 2006; 7: 271-175
    • (2006) EMBO Rep , vol.7 , pp. 271-175
    • Chakravarthi, S.1    Jessop, C.E.2    Bulleid, N.J.3
  • 28
    • 0034162822 scopus 로고    scopus 로고
    • Sulforaphane, a naturally occurring isothiocyanate, induces cell cycle arrest and apoptosis in HT29 human colon cancer cells
    • Gamet-Payrastre L, Li P, Lumeau S, Cassar G, Dupont MA, Chevolleau S, et al. Sulforaphane, a naturally occurring isothiocyanate, induces cell cycle arrest and apoptosis in HT29 human colon cancer cells. Cancer Res 2000; 60: 1426-1433
    • (2000) Cancer Res , vol.60 , pp. 1426-1433
    • Gamet-Payrastre, L.1    Li, P.2    Lumeau, S.3    Cassar, G.4    Dupont, M.A.5    Chevolleau, S.6
  • 29
    • 34247606510 scopus 로고    scopus 로고
    • Molecular basis for chemoprevention by sulforaphane: A comprehensive review
    • Juge N, Mithen RF, Traka M. Molecular basis for chemoprevention by sulforaphane: A comprehensive review. Cell Mol Life Sci 2007; 64: 1105-1127
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1105-1127
    • Juge, N.1    Mithen, R.F.2    Traka, M.3
  • 30
    • 0023002670 scopus 로고
    • Toxicology of tert-butylhydroquinone (TBHQ
    • Vanesch G. Toxicology of tert-butylhydroquinone (TBHQ). Food Chem Toxicol 1986; 24: 1063-1065
    • (1986) Food Chem Toxicol , vol.24 , pp. 1063-1065
    • Vanesch, G.1
  • 31
    • 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. J Biol Chem 1999; 274: 26071-26078
    • (1999) J 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
  • 32
    • 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, et al. 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
  • 33
    • 0037648957 scopus 로고    scopus 로고
    • Regulation of Nrf2-mediated induction of glutamate cysteine ligase modulatory gene (GCLM) expression: Considerations for future studies
    • Walsh AC. Regulation of Nrf2-mediated induction of glutamate cysteine ligase modulatory gene (GCLM) expression: Considerations for future studies. Toxicol Sci 2003; 73: 1-3
    • (2003) Toxicol Sci , vol.73 , pp. 1-3
    • Walsh, A.C.1
  • 35
    • 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: 254-262
    • (2000) Free Radic Biol Med , vol.29 , pp. 254-262
    • Jaiswal, A.K.1
  • 36
    • 18244386712 scopus 로고    scopus 로고
    • Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF-E2-related factor-2
    • Sakurai A, Nishimoto M, Himeno S, Imura N, Tsujimoto M, Kunimoto M, et al. Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: Role of NF-E2-related factor-2. J Cell Physiol 2005; 203: 529-537
    • (2005) J Cell Physiol , vol.203 , pp. 529-537
    • Sakurai, A.1    Nishimoto, M.2    Himeno, S.3    Imura, N.4    Tsujimoto, M.5    Kunimoto, M.6
  • 37
    • 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 Commu 1997; 236: 313-322
    • (1997) Biochem Biophys Res Commu , vol.236 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3    Ishii, T.4    Igarashi, K.5    Katoh, Y.6
  • 39
    • 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 Bio 1994; 14: 700-712
    • (1994) Mol Cell Bio , vol.14 , pp. 700-712
    • Kataoka, K.1    Noda, M.2    Nishizawa, M.3
  • 40
    • 34247282872 scopus 로고    scopus 로고
    • Action of Nrf2 and Keap1 in ARE-mediated NQO1 expression by quercetin
    • Tanigawa S, Fujii M, Hou DX. Action of Nrf2 and Keap1 in ARE-mediated NQO1 expression by quercetin. Free Redic Biol Med 2007; 42: 1690-1703
    • (2007) Free Redic Biol Med , vol.42 , pp. 1690-1703
    • Tanigawa, S.1    Fujii, M.2    Hou, D.X.3
  • 41
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • Hayes JD, McMahon M. NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer. Trends Biochem Sci 2009; 34: 176-188
    • (2009) Trends Biochem Sci , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 42
    • 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: 2396-2402
    • (2003) J Biol Chem , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 43
    • 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. Gene Cell 2003; 8: 379-391
    • (2003) Gene 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
  • 44
    • 0034704137 scopus 로고    scopus 로고
    • Small maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:Quinone oxidoreductase1 gene
    • Dhakshinamoorthy S, Jaiswal AK. Small maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:Quinone oxidoreductase1 gene. J Biol Chem 2000; 275: 40134-40141
    • (2000) J Biol Chem , vol.275 , pp. 40134-40141
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 45
    • 84655169936 scopus 로고    scopus 로고
    • Tumor suppressor genes and ROS: Complex networks of interactions
    • Vurusaner B, Poli G, Basaga H. Tumor suppressor genes and ROS: Complex networks of interactions. Free Radic Biol Med 2012; 52: 7-18
    • (2012) Free Radic Biol Med , vol.52 , pp. 7-18
    • Vurusaner, B.1    Poli, G.2    Basaga, H.3
  • 46
    • 39749101693 scopus 로고    scopus 로고
    • Determination of cellular redox status by stable isotope dilution liquid chromatography/mass spectrometry analysis of glutathione and glutathione disulfide
    • Zhu P, Oe T, Blair IA. Determination of cellular redox status by stable isotope dilution liquid chromatography/mass spectrometry analysis of glutathione and glutathione disulfide. Rapid Comm Mass Spec 2008; 22: 432-440
    • (2008) Rapid Comm Mass Spec , vol.22 , pp. 432-440
    • Zhu, P.1    Oe, T.2    Blair, I.A.3
  • 47
    • 33644911742 scopus 로고    scopus 로고
    • Nuclear factor Nrf2 and antioxidant response element regulate NRH:quinone oxidoreductase 2 (NQO2) gene expression and antioxidant induction
    • Wang W, Jaiswal AK. Nuclear factor Nrf2 and antioxidant response element regulate NRH:quinone oxidoreductase 2 (NQO2) gene expression and antioxidant induction. Free Radic Biol Med 2006; 40: 1119-1130
    • (2006) Free Radic Biol Med , vol.40 , pp. 1119-1130
    • Wang, W.1    Jaiswal, A.K.2
  • 48
    • 0027249757 scopus 로고
    • Evaluation of 20, 70-dichlorofluoresein and dihydrorhodamine 123 as fluoresecent probes for intracellular H2O2 in culture endothelial cells
    • Royall JA, Ischiropoulos H. Evaluation of 20, 70-dichlorofluoresein and dihydrorhodamine 123 as fluoresecent probes for intracellular H2O2 in culture endothelial cells. Arch Biochem Biophy 1993; 302: 348-355
    • (1993) Arch Biochem Biophy , vol.302 , pp. 348-355
    • Royall, J.A.1    Ischiropoulos, H.2
  • 49
    • 44349169635 scopus 로고    scopus 로고
    • Evidence for the aldoketo reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells
    • Park JH, Mangal D, Tacka KA, Quinn AM, Harvey RG, Blair IA, et al. Evidence for the aldoketo reductase pathway of polycyclic aromatic trans-dihydrodiol activation in human lung A549 cells. Proc Natl Acad Sci USA 2008; 105: 6846-6851
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6846-6851
    • Park, J.H.1    Mangal, D.2    Tacka, K.A.3    Quinn, A.M.4    Harvey, R.G.5    Blair, I.A.6
  • 50
    • 0001037962 scopus 로고    scopus 로고
    • Probes for reactive oxygen species, including nitric oxide
    • Haugland RP, Spence MTZ (eds. Molecular Probes Inc.: Oregon
    • Hauglnd RP. Probes for reactive oxygen species, including nitric oxide. In: Haugland RP, Spence MTZ (eds) Handbook of Fluorescent Probes and Research Chemicals. Molecular Probes Inc.: Oregon, 1996. pp 483-502
    • (1996) Handbook of Fluorescent Probes and Research Chemicals , pp. 483-502
    • Hauglnd, R.P.1
  • 51
    • 84869043780 scopus 로고    scopus 로고
    • The predicted molecular weight of Nrf2: It is what it is not
    • Lau A, Tian W, Whitman SA, Zhang DD. The predicted molecular weight of Nrf2: It is what it is not. Antioxi Redox Signal 2013; 18: 91-93
    • (2013) Antioxi Redox Signal , vol.18 , pp. 91-93
    • Lau, A.1    Tian, W.2    Whitman, S.A.3    Zhang, D.D.4
  • 52
    • 33846148370 scopus 로고    scopus 로고
    • PRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene
    • Kotake Y, Cao R, Viatour P, Sage J, Zhang Y, Xiong Y. pRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene. Gene Dev 2007; 21: 49-54
    • (2007) Gene Dev , vol.21 , pp. 49-54
    • Kotake, Y.1    Cao, R.2    Viatour, P.3    Sage, J.4    Zhang, Y.5    Xiong, Y.6
  • 53
    • 63049123597 scopus 로고    scopus 로고
    • Nuclear localization of Src-family tyrosine kinases is required for growth factor-induced euchromatinization
    • Takahashi A, Obata Y, Fukumoto Y, Nakayama Y, Kasahara K, Kuga T, et al. Nuclear localization of Src-family tyrosine kinases is required for growth factor-induced euchromatinization. Exp Cell Res 2009; 315: 1117-1141
    • (2009) Exp Cell Res , vol.315 , pp. 1117-1141
    • Takahashi, A.1    Obata, Y.2    Fukumoto, Y.3    Nakayama, Y.4    Kasahara, K.5    Kuga, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.