메뉴 건너뛰기




Volumn 191, Issue 1-3, 2011, Pages 239-249

Proteasome inhibitors MG-132 and bortezomib induce AKR1C1, AKR1C3, AKR1B1, and AKR1B10 in human colon cancer cell lines SW-480 and HT-29

Author keywords

Aldo keto reductase; Colon cells; Proteasome inhibitors

Indexed keywords

ALDO KETO REDUCTASE 1B1; ALDO KETO REDUCTASE 1B10; ALDO KETO REDUCTASE 1C1; ALDO KETO REDUCTASE 1C2; ALDO KETO REDUCTASE 1C3; ALDO KETO REDUCTASE 1C4; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BETA ACTIN; BORTEZOMIB; CYCLOOXYGENASE 2; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; MULTIDRUG RESISTANCE PROTEIN 2; PS 431; STEROID REDUCTASE; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG;

EID: 79957569340     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.12.026     Document Type: Conference Paper
Times cited : (46)

References (47)
  • 1
    • 0034287545 scopus 로고    scopus 로고
    • Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: Functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones
    • T.M. Penning, M.E. Burczynski, J.M. Jez, C.F. Hung, H.K. Lin, H. Ma, M. Moore, N. Palackal, K. Ratnam, Human 3alpha-hydroxysteroid dehydrogenase isoforms (AKR1C1-AKR1C4) of the aldo-keto reductase superfamily: functional plasticity and tissue distribution reveals roles in the inactivation and formation of male and female sex hormones, Biochem. J. 351 (Pt 1) (2000) 67-77.
    • (2000) Biochem. J. , vol.351 , Issue.PART 1 , pp. 67-77
    • Penning, T.M.1    Burczynski, M.E.2    Jez, J.M.3    Hung, C.F.4    Lin, H.K.5    Ma, H.6    Moore, M.7    Palackal, N.8    Ratnam, K.9
  • 2
    • 1642305724 scopus 로고    scopus 로고
    • Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: Implications for steroid hormone metabolism and action
    • S. Steckelbroeck, Y. Jin, S. Gopishetty, B. Oyesanmi, T.M. Penning, Human cytosolic 3alpha-hydroxysteroid dehydrogenases of the aldo-keto reductase superfamily display significant 3beta-hydroxysteroid dehydrogenase activity: implications for steroid hormone metabolism and action, J. Biol. Chem. 279 (11) (2004) 10784-10795.
    • (2004) J. Biol. Chem. , vol.279 , Issue.11 , pp. 10784-10795
    • Steckelbroeck, S.1    Jin, Y.2    Gopishetty, S.3    Oyesanmi, B.4    Penning, T.M.5
  • 3
    • 33847021147 scopus 로고    scopus 로고
    • Aldo-keto reductases and bioactivation/detoxication
    • Y. Jin, T.M. Penning, Aldo-keto reductases and bioactivation/ detoxication, Annu. Rev. Pharmacol. Toxicol. 47 (2007) 263-292.
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 263-292
    • Jin, Y.1    Penning, T.M.2
  • 4
    • 34547679864 scopus 로고    scopus 로고
    • Increased resistance of tumor cells to daunorubicin after transfection of cDNAs coding for anthracycline inactivating enzymes
    • DOI 10.1016/j.canlet.2007.03.018, PII S0304383507001565
    • M. Plebuch, M. Soldan, C. Hungerer, L. Koch, E. Maser, Increased resistance of tumor cells to daunorubicin after transfection of cDNAs coding for anthracycline inactivating enzymes, Cancer Lett. 255 (1) (2007) 49-56. (Pubitemid 47212606)
    • (2007) Cancer Letters , vol.255 , Issue.1 , pp. 49-56
    • Plebuch, M.1    Soldan, M.2    Hungerer, C.3    Koch, L.4    Maser, E.5
  • 5
    • 0033852886 scopus 로고    scopus 로고
    • Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)- 1-butanone (NNK) in human liver cytosol
    • A. Atalla, U. Breyer-Pfaff, E. Maser, Purification and characterization of oxidoreductases-catalyzing carbonyl reduction of the tobacco-specific nitrosamine 4-methylnitrosamino-1-(3-pyridyl)-1-butanone (NNK) in human liver cytosol, Xenobiotica 30 (8) (2000) 755-769.
    • (2000) Xenobiotica , vol.30 , Issue.8 , pp. 755-769
    • Atalla, A.1    Breyer-Pfaff, U.2    Maser, E.3
  • 6
    • 0032937593 scopus 로고    scopus 로고
    • Dihydrodiol dehydrogenases and polycyclic aromatic hydrocarbon activation: Generation of reactive and redox active o-quinones
    • DOI 10.1021/tx980143n
    • T.M. Penning, M.E. Burczynski, C.F. Hung, K.D. McCoull, N.T. Palackal, L.S. Tsuruda, Dihydrodiol dehydrogenases and polycyclic aromatic hydrocarbon activation: generation of reactive and redox active o-quinones, Chem. Res. Toxicol. 12 (1) (1999) 1-18. (Pubitemid 29048827)
    • (1999) Chemical Research in Toxicology , vol.12 , Issue.1 , pp. 1-18
    • Penning, T.M.1    Burczynski, M.E.2    Hung, C.-F.3    McCoull, K.D.4    Palackal, N.T.5    Tsuruda, L.S.6
  • 8
    • 60449106323 scopus 로고    scopus 로고
    • The aldo-keto reductase AKR1C3 contributes to 7,12-dimethylbenz(a) anthracene-3,4-dihydrodiol mediated oxidative DNA damage in myeloid cells: Implications for leukemogenesis
    • J. Birtwistle, R.E. Hayden, F.L. Khanim, R.M. Green, C. Pearce, N.J. Davies, N. Wake, H. Schrewe, J.P. Ride, J.K. Chipman, C.M. Bunce, The aldo-keto reductase AKR1C3 contributes to 7,12-dimethylbenz(a)anthracene-3,4-dihydrodiol mediated oxidative DNA damage in myeloid cells: implications for leukemogenesis, Mutat. Res. 662 (1-2) (2009) 67-74.
    • (2009) Mutat. Res. , vol.662 , Issue.1-2 , pp. 67-74
    • Birtwistle, J.1    Hayden, R.E.2    Khanim, F.L.3    Green, R.M.4    Pearce, C.5    Davies, N.J.6    Wake, N.7    Schrewe, H.8    Ride, J.P.9    Chipman, J.K.10    Bunce, C.M.11
  • 9
    • 0037025386 scopus 로고    scopus 로고
    • Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate carcinogens by human aldo-keto reductase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells
    • N.T. Palackal, S.H. Lee, R.G. Harvey, I.A. Blair, T.M. Penning, Activation of polycyclic aromatic hydrocarbon trans-dihydrodiol proximate carcinogens by human aldo-keto reductase (AKR1C) enzymes and their functional overexpression in human lung carcinoma (A549) cells, J. Biol. Chem. 277 (27) (2002) 24799-24808.
    • (2002) J. Biol. Chem. , vol.277 , Issue.27 , pp. 24799-24808
    • Palackal, N.T.1    Lee, S.H.2    Harvey, R.G.3    Blair, I.A.4    Penning, T.M.5
  • 10
    • 74449092601 scopus 로고    scopus 로고
    • Aldo-keto reductase 1C3 expression in MCF-7 cells reveals roles in steroid hormone and prostaglandin metabolism that may explain its over-expression in breast cancer
    • M.C. Byrns, L. Duan, S.H. Lee, I.A. Blair, T.M. Penning, Aldo-keto reductase 1C3 expression in MCF-7 cells reveals roles in steroid hormone and prostaglandin metabolism that may explain its over-expression in breast cancer, J. Steroid Biochem. Mol. Biol. 118 (3) (2010) 177-187.
    • (2010) J. Steroid Biochem. Mol. Biol. , vol.118 , Issue.3 , pp. 177-187
    • Byrns, M.C.1    Duan, L.2    Lee, S.H.3    Blair, I.A.4    Penning, T.M.5
  • 11
    • 61649103983 scopus 로고    scopus 로고
    • Steroid hormone transforming aldo-keto reductases and cancer
    • T.M. Penning, M.C. Byrns, Steroid hormone transforming aldo-keto reductases and cancer, Ann. N.Y. Acad. Sci. 1155 (2009) 33-42.
    • (2009) Ann. N.Y. Acad. Sci. , vol.1155 , pp. 33-42
    • Penning, T.M.1    Byrns, M.C.2
  • 12
    • 59049086019 scopus 로고    scopus 로고
    • Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes
    • H.J. Martin, E. Maser, Role of human aldo-keto-reductase AKR1B10 in the protection against toxic aldehydes, Chem. Biol. Interact. 178 (1-3) (2009) 145-150.
    • (2009) Chem. Biol. Interact. , vol.178 , Issue.1-3 , pp. 145-150
    • Martin, H.J.1    Maser, E.2
  • 13
    • 77952403264 scopus 로고    scopus 로고
    • Aldose reductase and cardiovascular diseases, creating human-like diabetic complications in an experimental model
    • R. Ramasamy, I.J. Goldberg, Aldose reductase and cardiovascular diseases, creating human-like diabetic complications in an experimental model, Circ. Res. 106 (9) (2010) 1449-1458.
    • (2010) Circ. Res. , vol.106 , Issue.9 , pp. 1449-1458
    • Ramasamy, R.1    Goldberg, I.J.2
  • 14
    • 58149141588 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: Medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism
    • X. Pares, J. Farres, N. Kedishvili, G. Duester, Medium- and short-chain dehydrogenase/reductase gene and protein families: medium-chain and short-chain dehydrogenases/reductases in retinoid metabolism, Cell. Mol. Life Sci. 65 (24) (2008) 3936-3949.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.24 , pp. 3936-3949
    • Pares, X.1    Farres, J.2    Kedishvili, N.3    Duester, G.4
  • 15
    • 0043069767 scopus 로고    scopus 로고
    • Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: Consequences for retinoid metabolism
    • DOI 10.1042/BJ20021818
    • B. Crosas, D.J. Hyndman, O. Gallego, S. Martras, X. Pares, T.G. Flynn, J. Farres, Human aldose reductase and human small intestine aldose reductase are efficient retinal reductases: consequences for retinoid metabolism, Biochem. J. 373 (Pt 3) (2003) 973-979. (Pubitemid 36981109)
    • (2003) Biochemical Journal , vol.373 , Issue.3 , pp. 973-979
    • Crosas, B.1    Hyndman, D.J.2    Gallego, O.3    Martras, S.4    Pares, X.5    Flynn, T.G.6    Farres, J.7
  • 17
    • 75349086165 scopus 로고    scopus 로고
    • Identification and expression analysis of the aldo-ketoreductase1-B10 gene in primary malignant liver tumours
    • S. Heringlake, M. Hofdmann, A. Fiebeler, M.P. Manns, W. Schmiegel, A. Tannapfel, Identification and expression analysis of the aldo-ketoreductase1-B10 gene in primary malignant liver tumours, J. Hepatol. 52 (2) (2010) 220-227.
    • (2010) J. Hepatol. , vol.52 , Issue.2 , pp. 220-227
    • Heringlake, S.1    Hofdmann, M.2    Fiebeler, A.3    Manns, M.P.4    Schmiegel, W.5    Tannapfel, A.6
  • 19
    • 35348887886 scopus 로고    scopus 로고
    • Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: Implication for cancer intervention
    • DOI 10.1002/ijc.22933
    • R. Yan, X. Zu, J. Ma, Z. Liu, M. Adeyanju, D. Cao, Aldo-keto reductase family 1 B10 gene silencing results in growth inhibition of colorectal cancer cells: implication for cancer intervention, Int. J. Cancer 121 (10) (2007) 2301-2306. (Pubitemid 47585613)
    • (2007) International Journal of Cancer , vol.121 , Issue.10 , pp. 2301-2306
    • Yan, R.1    Zu, X.2    Ma, J.3    Liu, Z.4    Adeyanju, M.5    Cao, D.6
  • 20
    • 41249090769 scopus 로고    scopus 로고
    • Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells
    • J. Ma, R. Yan, X. Zu, J.M. Cheng, K. Rao, D.F. Liao, D. Cao, Aldo-keto reductase family 1 B10 affects fatty acid synthesis by regulating the stability of acetyl-CoA carboxylase-alpha in breast cancer cells, J. Biol. Chem. 283 (6) (2008) 3418-3423.
    • (2008) J. Biol. Chem. , vol.283 , Issue.6 , pp. 3418-3423
    • Ma, J.1    Yan, R.2    Zu, X.3    Cheng, J.M.4    Rao, K.5    Liao, D.F.6    Cao, D.7
  • 21
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • C. Naujokat, S. Hoffmann, Role and function of the 26S proteasome in proliferation and apoptosis, Lab. Invest. 82 (8) (2002) 965-980.
    • (2002) Lab. Invest. , vol.82 , Issue.8 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 22
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • D.H. Wolf, W. Hilt, The proteasome: a proteolytic nanomachine of cell regulation and waste disposal, Biochim. Biophys. Acta 1695 (1-3) (2004) 19-31.
    • (2004) Biochim. Biophys. Acta , vol.1695 , Issue.1-3 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 23
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • DOI 10.1038/nrm1049
    • M. Muratani, W.P. Tansey,Howthe ubiquitin-proteasome system controls transcription, Nat. Rev. Mol. Cell Biol. 4 (3) (2003) 192-201. (Pubitemid 36288041)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.3 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 24
    • 5344234076 scopus 로고    scopus 로고
    • The ubiquitin-mediated protein degradation pathway in cancer: Therapeutic implications
    • DOI 10.1016/j.ejca.2004.07.006, PII S0959804904005660
    • A.M. Burger, A.K. Seth, The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications, Eur. J. Cancer 40 (15) (2004) 2217-2229. (Pubitemid 39348871)
    • (2004) European Journal of Cancer , vol.40 , Issue.15 , pp. 2217-2229
    • Burger, A.M.1    Seth, A.K.2
  • 25
    • 0035328584 scopus 로고    scopus 로고
    • Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: Implications for systemic nuclear factor-kappaB inhibition
    • J.C. Cusack Jr., R. Liu, M. Houston, K. Abendroth, P.J. Elliott, J. Adams, A.S. Baldwin Jr., Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition, Cancer Res. 61 (9) (2001) 3535-3540. (Pubitemid 32694955)
    • (2001) Cancer Research , vol.61 , Issue.9 , pp. 3535-3540
    • Cusack Jr., J.C.1    Liu, R.2    Houston, M.3    Abendroth, K.4    Elliott, P.J.5    Adams, J.6    Baldwin Jr., A.S.7
  • 27
    • 0037514596 scopus 로고    scopus 로고
    • Clinical update: Proteasome inhibitors in solid tumors
    • H.J. Lenz, Clinical update: proteasome inhibitors in solid tumors, Cancer Treat. Rev. 29 (Suppl. 1) (2003) 41-48.
    • (2003) Cancer Treat. Rev. , vol.29 , Issue.SUPPL. 1 , pp. 41-48
    • Lenz, H.J.1
  • 28
    • 0141706672 scopus 로고    scopus 로고
    • Reactive Oxygen Species Generation and Mitochondrial Dysfunction in the Apoptotic Response to Bortezomib, a Novel Proteasome Inhibitor, in Human H460 Non-small Cell Lung Cancer Cells
    • DOI 10.1074/jbc.M302559200
    • Y.H. Ling, L. Liebes, Y. Zou, R. Perez-Soler, Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells, J. Biol. Chem. 278 (36) (2003) 33714-33723. (Pubitemid 37553204)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 33714-33723
    • Ling, Y.-H.1    Liebes, L.2    Zou, Y.3    Perez-Soler, R.4
  • 29
    • 64749106188 scopus 로고    scopus 로고
    • Role of oxidative stress and intracellular glutathione in the sensitivity to apoptosis induced by proteasome inhibitor in thyroid cancer cells
    • Z.X. Du, H.Y. Zhang, X. Meng, Y. Guan, H.Q. Wang, Role of oxidative stress and intracellular glutathione in the sensitivity to apoptosis induced by proteasome inhibitor in thyroid cancer cells, BMC Cancer 9 (2009) 56.
    • (2009) BMC Cancer , vol.9 , pp. 56
    • Du, Z.X.1    Zhang, H.Y.2    Meng, X.3    Guan, Y.4    Wang, H.Q.5
  • 30
    • 12444257799 scopus 로고    scopus 로고
    • Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles
    • DOI 10.1046/j.1365-2443.2003.00640.x
    • K. Itoh, N. Wakabayashi, Y. Katoh, T. Ishii, T. O'Connor, M. Yamamoto, Keap1 regulates both cytoplasmic-nuclear shuttling and degradation of Nrf2 in response to electrophiles, Genes Cells 8 (4) (2003) 379-391. (Pubitemid 36504013)
    • (2003) Genes to Cells , vol.8 , Issue.4 , pp. 379-391
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    O'Connor, T.5    Yamamoto, M.6
  • 31
    • 67650229881 scopus 로고    scopus 로고
    • Nrf2-dependent upregulation of antioxidative enzymes: A novel path way for proteasome inhibitor-mediated cardioprotection
    • H. Dreger, K. Westphal, A. Weller, G. Baumann, V. Stangl, S. Meiners, K. Stangl, Nrf2-dependent upregulation of antioxidative enzymes: a novel path way for proteasome inhibitor-mediated cardioprotection, Cardiovasc. Res. 83 (2) (2009) 354-361.
    • (2009) Cardiovasc. Res. , vol.83 , Issue.2 , pp. 354-361
    • Dreger, H.1    Westphal, K.2    Weller, A.3    Baumann, G.4    Stangl, V.5    Meiners, S.6    Stangl, K.7
  • 33
    • 34547692874 scopus 로고    scopus 로고
    • Human aldo-keto reductases: Function, gene regulation, and single nucleotide polymorphisms
    • T.M. Penning, J.E. Drury, Human aldo-keto reductases: function, gene regulation, and single nucleotide polymorphisms, Arch. Biochem. Biophys. 464 (2) (2007) 241-250.
    • (2007) Arch. Biochem. Biophys. , vol.464 , Issue.2 , pp. 241-250
    • Penning, T.M.1    Drury, J.E.2
  • 34
    • 77957288996 scopus 로고    scopus 로고
    • Regulation of human carbonyl reductase 3 (CBR3; SDR21C2) expression by Nrf2 in cultured cancer cells
    • B. Ebert, M. Kisiela, P. Malatkova, Y. El-Hawari, E. Maser, Regulation of human carbonyl reductase 3 (CBR3; SDR21C2) expression by Nrf2 in cultured cancer cells, Biochemistry 49 (39) (2010) 8499-8511.
    • (2010) Biochemistry , vol.49 , Issue.39 , pp. 8499-8511
    • Ebert, B.1    Kisiela, M.2    Malatkova, P.3    El-Hawari, Y.4    Maser, E.5
  • 36
    • 0032510704 scopus 로고    scopus 로고
    • Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: Oxidation of trans-7,8-dihydroxy-7,8-dihydrobenzo[a] pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione
    • M.E. Burczynski, R.G. Harvey, T.M. Penning, Expression and characterization of four recombinant human dihydrodiol dehydrogenase isoforms: oxidation of trans-7,8-dihydroxy-7,8-dihydrobenzo[a]pyrene to the activated o-quinone metabolite benzo[a]pyrene-7,8-dione, Biochemistry 37 (19) (1998) 6781-6790.
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6781-6790
    • Burczynski, M.E.1    Harvey, R.G.2    Penning, T.M.3
  • 37
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • I.J. Hidalgo, T.J. Raub, R.T. Borchardt, Characterization of the human colon carcinoma cell line (Caco-2) as amodel system for intestinal epithelial permeability, Gastroenterology 96 (3) (1989) 736-749. (Pubitemid 19057595)
    • (1989) Gastroenterology , vol.96 , Issue.3 , pp. 736-749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 39
    • 33645893202 scopus 로고    scopus 로고
    • Induction of AKR1C2 by phase II inducers: Identification of a distal consensus antioxidant response element regulated by NRF2
    • H. Lou, S. Du, Q. Ji, A. Stolz, Induction of AKR1C2 by phase II inducers: identification of a distal consensus antioxidant response element regulated by NRF2, Mol. Pharmacol. 69 (5) (2006) 1662-1672.
    • (2006) Mol. Pharmacol. , vol.69 , Issue.5 , pp. 1662-1672
    • Lou, H.1    Du, S.2    Ji, Q.3    Stolz, A.4
  • 41
    • 49649120671 scopus 로고    scopus 로고
    • Intestinal efflux transporters and drug absorption
    • T. Murakami, M. Takano, Intestinal efflux transporters and drug absorption, Expert Opin. Drug Metab. Toxicol. 4 (7) (2008) 923-939.
    • (2008) Expert Opin. Drug Metab. Toxicol. , vol.4 , Issue.7 , pp. 923-939
    • Murakami, T.1    Takano, M.2
  • 43
    • 63349102182 scopus 로고    scopus 로고
    • Comparison of the effects of phenethyl isothiocyanate and sulforaphane on gene expression in breast cancer and normal mammary epithelial cells
    • Maywood
    • U. Telang, D.A. Brazeau, M.E. Morris, Comparison of the effects of phenethyl isothiocyanate and sulforaphane on gene expression in breast cancer and normal mammary epithelial cells, Exp. Biol. Med. (Maywood) 234 (3) (2009) 287-295.
    • (2009) Exp. Biol. Med. , vol.234 , Issue.3 , pp. 287-295
    • Telang, U.1    Brazeau, D.A.2    Morris, M.E.3
  • 44
    • 0032875364 scopus 로고    scopus 로고
    • An autoregulatory loop controlling CYP1A1 gene expression: Role of H(2)O(2) and NFI
    • Y. Morel, N. Mermod, R. Barouki, An autoregulatory loop controlling CYP1A1 gene expression: role of H(2)O(2) and NFI, Mol. Cell. Biol. 19 (10) (1999) 6825-6832.
    • (1999) Mol. Cell. Biol. , vol.19 , Issue.10 , pp. 6825-6832
    • Morel, Y.1    Mermod, N.2    Barouki, R.3
  • 45
    • 0021842504 scopus 로고
    • Transient depletion of lung glutathione by diethylmaleate enhances oxygen toxicity
    • S.M. Deneke, B.A. Lynch, B.L. Fanburg, Transient depletion of lung glutathione by diethylmaleate enhances oxygen toxicity, J. Appl. Physiol. 58 (2) (1985) 571-574.
    • (1985) J. Appl. Physiol. , vol.58 , Issue.2 , pp. 571-574
    • Deneke, S.M.1    Lynch, B.A.2    Fanburg, B.L.3
  • 46
    • 33744477355 scopus 로고    scopus 로고
    • Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts
    • DOI 10.1196/annals.1354.060
    • D.C. Kraft, C.C. Deocaris, R. Wadhwa, S.I. Rattan, Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aginghumanskin fibroblasts, Ann. N. Y. Acad. Sci. 1067 (2006) 420-424. (Pubitemid 43806354)
    • (2006) Annals of the New York Academy of Sciences , vol.1067 , Issue.1 , pp. 420-424
    • Kraft, D.C.1    Deocaris, C.C.2    Wadhwa, R.3    Rattan, S.I.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.