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Volumn 72, Issue , 2014, Pages 134-148

Methylglyoxal induces endoplasmic reticulum stress and DNA demethylation in the Keap1 promoter of human lens epithelial cells and age-related cataracts

Author keywords

Cataracts; DNA methylation; ER stress; Free radicals; Keap1 promoter demethylation; Methylglyoxal; Nrf2 dependent antioxidant protection; Unfolded protein response

Indexed keywords

5 METHYLCYTOSINE; DNA; DNA METHYLTRANSFERASE; GENOMIC DNA; KELCH LIKE ECH ASSOCIATED PROTEIN 1; METHYLGLYOXAL; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR NRF2; KEAP1 PROTEIN, HUMAN; SIGNAL PEPTIDE;

EID: 84900490382     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2014.04.010     Document Type: Article
Times cited : (77)

References (78)
  • 1
    • 80051843990 scopus 로고    scopus 로고
    • Diabetic cataract-pathogenesis, epidemiology and treatment
    • A. Pollreisz, and U. Schmidt-Erfurth Diabetic cataract-pathogenesis, epidemiology and treatment J. Ophthalmol. 2010 2010 608751
    • (2010) J. Ophthalmol. , vol.2010 , pp. 608751
    • Pollreisz, A.1    Schmidt-Erfurth, U.2
  • 3
    • 33847723891 scopus 로고    scopus 로고
    • Prevalence and risk factors for cataracts in persons with type 2 diabetes mellitus
    • S.I. Kim, and S.J. Kim Prevalence and risk factors for cataracts in persons with type 2 diabetes mellitus Korean J. Ophthalmol. 20 2006 201 204
    • (2006) Korean J. Ophthalmol. , vol.20 , pp. 201-204
    • Kim, S.I.1    Kim, S.J.2
  • 5
    • 0042198801 scopus 로고    scopus 로고
    • Redox regulation in the lens
    • M.F. Lou Redox regulation in the lens Prog. Retinal Eye Res. 22 2003 657 682
    • (2003) Prog. Retinal Eye Res. , vol.22 , pp. 657-682
    • Lou, M.F.1
  • 8
    • 0029986646 scopus 로고    scopus 로고
    • Lens epithelial cell apoptosis is an early event in the development of UVB-induced cataract
    • W.C. Li, and A. Spector Lens epithelial cell apoptosis is an early event in the development of UVB-induced cataract Free Radic. Biol. Med. 20 1996 301 311
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 301-311
    • Li, W.C.1    Spector, A.2
  • 9
    • 0031457926 scopus 로고    scopus 로고
    • Lensification of the posterior corneal surface: An unusual proliferation of lens epithelial cells
    • T. Kohnen, D.D. Koch, and R.L. Font Lensification of the posterior corneal surface: an unusual proliferation of lens epithelial cells Ophthalmology 104 1997 1343 1347
    • (1997) Ophthalmology , vol.104 , pp. 1343-1347
    • Kohnen, T.1    Koch, D.D.2    Font, R.L.3
  • 10
    • 0036892845 scopus 로고    scopus 로고
    • Cataracts associated with systemic disorders and syndromes
    • K. Negahban, and K. Chern Cataracts associated with systemic disorders and syndromes Curr. Opin. Ophthalmol. 13 2002 419 422
    • (2002) Curr. Opin. Ophthalmol. , vol.13 , pp. 419-422
    • Negahban, K.1    Chern, K.2
  • 11
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • P.J. Thornalley, A. Langborg, and H.S. Minhas Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose Biochem. J. 344 1999 109 116
    • (1999) Biochem. J. , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 12
    • 0027396022 scopus 로고
    • The formation of methylglyoxal from triose phosphates: Investigation using a specific assay for methylglyoxal
    • S.A. Phillips, and P.J. Thornalley The formation of methylglyoxal from triose phosphates: investigation using a specific assay for methylglyoxal Eur. J. Biochem. 212 1993 101 105
    • (1993) Eur. J. Biochem. , vol.212 , pp. 101-105
    • Phillips, S.A.1    Thornalley, P.J.2
  • 14
    • 0037096983 scopus 로고    scopus 로고
    • Effects of modifications of alpha-crystallin on its chaperone and other properties
    • B.K. Derham, and J.J. Harding Effects of modifications of alpha-crystallin on its chaperone and other properties Biochem. J. 364 2002 711 717
    • (2002) Biochem. J. , vol.364 , pp. 711-717
    • Derham, B.K.1    Harding, J.J.2
  • 15
    • 2642538378 scopus 로고    scopus 로고
    • Carnosine disaggregates glycated α-crystallin: An in vitro study
    • N.W. Seidler, G.S. Yeargans, and T.G. Morgan Carnosine disaggregates glycated α-crystallin: an in vitro study Arch. Biochem. Biophys. 427 2004 110 115
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 110-115
    • Seidler, N.W.1    Yeargans, G.S.2    Morgan, T.G.3
  • 17
    • 61849093145 scopus 로고    scopus 로고
    • Mitochondrial function and redox control in the aging eye: Role of MsrA and other repair systems in cataract and macular degenerations
    • L.A. Brennan, and M. Kantorow Mitochondrial function and redox control in the aging eye: role of MsrA and other repair systems in cataract and macular degenerations Exp. Eye Res. 88 2009 195 203
    • (2009) Exp. Eye Res. , vol.88 , pp. 195-203
    • Brennan, L.A.1    Kantorow, M.2
  • 18
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: A new perspective on an old paradigm
    • J.W. Baynes, and S.R. Thorpe Role of oxidative stress in diabetic complications: a new perspective on an old paradigm Diabetes 48 1999 1 9
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 19
    • 71949098172 scopus 로고    scopus 로고
    • Signalling pathways in the unfolded protein response: Development from yeast to mammals
    • K. Mori Signalling pathways in the unfolded protein response: development from yeast to mammals J. Biochem. 146 2009 743 750
    • (2009) J. Biochem. , vol.146 , pp. 743-750
    • Mori, K.1
  • 21
    • 84872194492 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress, pancreatic beta-cell degeneration, and diabetes
    • F.R. Papa Endoplasmic reticulum stress, pancreatic beta-cell degeneration, and diabetes Cold Spring Harbor Perspect. Med. 2 2012 a007666
    • (2012) Cold Spring Harbor Perspect. Med. , vol.2 , pp. 007666
    • Papa, F.R.1
  • 22
    • 84861905329 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and type 2 diabetes
    • S.H. Back, and R.J. Kaufman Endoplasmic reticulum stress and type 2 diabetes Annu. Rev. Biochem. 81 2012 767 793
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 767-793
    • Back, S.H.1    Kaufman, R.J.2
  • 23
    • 0036676970 scopus 로고    scopus 로고
    • Stressful death of T-ALL tumor cells after treatment with the anti-tumor agent Tetrocarcin-A
    • I. Tinhofer, G. Anether, M. Senfter, K. Pfaller, D. Bernhard, M. Hara, and R. Greil Stressful death of T-ALL tumor cells after treatment with the anti-tumor agent Tetrocarcin-A FASEB J. 16 2002 1295 1297
    • (2002) FASEB J. , vol.16 , pp. 1295-1297
    • Tinhofer, I.1    Anether, G.2    Senfter, M.3    Pfaller, K.4    Bernhard, D.5    Hara, M.6    Greil, R.7
  • 24
    • 0036725164 scopus 로고    scopus 로고
    • Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation
    • Q. Xie, V.I. Khaoustov, C.C. Chung, J. Sohn, B. Krishnan, D.E. Lewis, and B. Yoffe Effect of tauroursodeoxycholic acid on endoplasmic reticulum stress-induced caspase-12 activation Hepatology 36 2002 592 601
    • (2002) Hepatology , vol.36 , pp. 592-601
    • Xie, Q.1    Khaoustov, V.I.2    Chung, C.C.3    Sohn, J.4    Krishnan, B.5    Lewis, D.E.6    Yoffe, B.7
  • 25
    • 2442542312 scopus 로고    scopus 로고
    • PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress
    • S.B. Cullinan, and J.A. Diehl PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress J. Biol. Chem. 279 2004 20108 20117
    • (2004) J. Biol. Chem. , vol.279 , pp. 20108-20117
    • Cullinan, S.B.1    Diehl, J.A.2
  • 26
    • 29244462498 scopus 로고    scopus 로고
    • Coordination of ER and oxidative stress signaling: The PERK/Nrf2 signaling pathway
    • S.B. Cullinan, and J.A. Diehl Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway Int. J. Biochem. Cell Biol. 38 2006 317 332
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 317-332
    • Cullinan, S.B.1    Diehl, J.A.2
  • 27
    • 18244377997 scopus 로고    scopus 로고
    • Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein
    • A.T. Dinkova-Kostova, W.D. Holtzclaw, and N. Wakabayashi Keap1, the sensor for electrophiles and oxidants that regulates the phase 2 response, is a zinc metalloprotein Biochemistry 44 2005 6889 6899
    • (2005) Biochemistry , vol.44 , pp. 6889-6899
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Wakabayashi, N.3
  • 28
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • T.W. Kensler, N. Wakabayashi, and S. Biswal Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway Annu. Rev. Pharmacol. Toxicol. 47 2007 89 116
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 29
    • 0025948113 scopus 로고
    • The antioxidant responsive element: Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • T.H. Rushmore, M.R. Morton, and C.B. Pickett The antioxidant responsive element: activation by oxidative stress and identification of the DNA consensus sequence required for functional activity J. Biol. Chem. 266 1991 11632 11639
    • (1991) J. Biol. Chem. , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 31
    • 63549121490 scopus 로고    scopus 로고
    • NRF2 and KEAP1 mutations: Permanent activation of an adaptive response in cancer
    • J.D. Hayes, and M. McMahon NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer Trends Biochem. Sci. 34 2009 176 188
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 176-188
    • Hayes, J.D.1    McMahon, M.2
  • 33
    • 0031126337 scopus 로고    scopus 로고
    • Activation of calpain in lens: A review and proposed mechanism
    • M. Azuma, C. Fukiage, L.L. David, and T.R. Shearer Activation of calpain in lens: a review and proposed mechanism Exp. Eye Res. 64 1997 529 538
    • (1997) Exp. Eye Res. , vol.64 , pp. 529-538
    • Azuma, M.1    Fukiage, C.2    David, L.L.3    Shearer, T.R.4
  • 34
    • 84861567265 scopus 로고    scopus 로고
    • Redox signaling loops in the unfolded protein response
    • A. Higa, and E. Chevet Redox signaling loops in the unfolded protein response Cell. Signalling 24 2012 1548 1555
    • (2012) Cell. Signalling , vol.24 , pp. 1548-1555
    • Higa, A.1    Chevet, E.2
  • 35
    • 0036862532 scopus 로고    scopus 로고
    • 2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum
    • 2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum Mol. Cell 10 2002 983 994
    • (2002) Mol. Cell , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 36
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
    • M. Pagani, M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N.J. Bulleid, A. Cabibbo, and R. Sitia Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response J. Biol. Chem. 275 2000 23685 23692
    • (2000) J. Biol. Chem. , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6    Cabibbo, A.7    Sitia, R.8
  • 37
    • 0036328026 scopus 로고    scopus 로고
    • Role of DNA methylation in the regulation of cell function: Autoimmunity, aging and cancer
    • B.C. Richardson Role of DNA methylation in the regulation of cell function: autoimmunity, aging and cancer J. Nutr. 132 2002 2401S 2405S
    • (2002) J. Nutr. , vol.132
    • Richardson, B.C.1
  • 38
    • 0035962631 scopus 로고    scopus 로고
    • DNA methylation, methyltransferases, and cancer
    • K.D. Robertson DNA methylation, methyltransferases, and cancer Oncogene 20 2001 3139 3155
    • (2001) Oncogene , vol.20 , pp. 3139-3155
    • Robertson, K.D.1
  • 39
    • 80052476744 scopus 로고    scopus 로고
    • Molecular biology: Demystifying DNA demethylation
    • C.S. Nabel, and R.M. Kohli Molecular biology: demystifying DNA demethylation Science 333 2011 1229 1230
    • (2011) Science , vol.333 , pp. 1229-1230
    • Nabel, C.S.1    Kohli, R.M.2
  • 40
    • 79955538247 scopus 로고    scopus 로고
    • Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain
    • J.U. Guo, Y. Su, C. Zhong, G.L. Ming, and H. Song Hydroxylation of 5-methylcytosine by TET1 promotes active DNA demethylation in the adult brain Cell 145 2011 423 434
    • (2011) Cell , vol.145 , pp. 423-434
    • Guo, J.U.1    Su, Y.2    Zhong, C.3    Ming, G.L.4    Song, H.5
  • 41
    • 84876946045 scopus 로고    scopus 로고
    • Genome-wide analysis reveals TET- and TDG-dependent 5-methylcytosine oxidation dynamics
    • L. Shen, H. Wu, D. Diep, S. Yamaguchi, A.C. D'Alessio, H.L. Fung, K. Zhang, and Y. Zhang Genome-wide analysis reveals TET- and TDG-dependent 5-methylcytosine oxidation dynamics Cell 153 2013 692 706
    • (2013) Cell , vol.153 , pp. 692-706
    • Shen, L.1    Wu, H.2    Diep, D.3    Yamaguchi, S.4    D'Alessio, A.C.5    Fung, H.L.6    Zhang, K.7    Zhang, Y.8
  • 44
  • 46
    • 84866867120 scopus 로고    scopus 로고
    • Age-related cataracts: Homocysteine coupled endoplasmic reticulum stress and suppression of Nrf2-dependent antioxidant protection
    • R. Elanchezhian, P. Palsamy, C.J. Madson, D.W. Lynch, and T. Shinohara Age-related cataracts: homocysteine coupled endoplasmic reticulum stress and suppression of Nrf2-dependent antioxidant protection Chem. Biol. Interact. 200 2012 1 10
    • (2012) Chem. Biol. Interact. , vol.200 , pp. 1-10
    • Elanchezhian, R.1    Palsamy, P.2    Madson, C.J.3    Lynch, D.W.4    Shinohara, T.5
  • 49
    • 77951850381 scopus 로고    scopus 로고
    • BISMA - Fast and accurate bisulfite sequencing data analysis of individual clones from unique and repetitive sequences
    • C. Rohde, Y. Zhang, R. Reinhardt, and A. Jeltsch BISMA - fast and accurate bisulfite sequencing data analysis of individual clones from unique and repetitive sequences BMC Bioinformatics 11 2010 230
    • (2010) BMC Bioinformatics , vol.11 , pp. 230
    • Rohde, C.1    Zhang, Y.2    Reinhardt, R.3    Jeltsch, A.4
  • 50
    • 0035910575 scopus 로고    scopus 로고
    • Yeast glyoxalase i is a monomeric enzyme with two active sites
    • E.M. Frickel, P. Jemth, M. Widersten, and B. Mannervik Yeast glyoxalase I is a monomeric enzyme with two active sites J. Biol. Chem. 276 2001 1845 1849
    • (2001) J. Biol. Chem. , vol.276 , pp. 1845-1849
    • Frickel, E.M.1    Jemth, P.2    Widersten, M.3    Mannervik, B.4
  • 51
    • 0029001483 scopus 로고
    • DNA adduct 8-hydroxyl-2′-deoxyguanosine (8-hydroxyguanine) affects function of human DNA methyltransferase
    • P.W. Turk, A. Laayoun, S.S. Smith, and S.A. Weitzman DNA adduct 8-hydroxyl-2′-deoxyguanosine (8-hydroxyguanine) affects function of human DNA methyltransferase Carcinogenesis 16 1995 1253 1255
    • (1995) Carcinogenesis , vol.16 , pp. 1253-1255
    • Turk, P.W.1    Laayoun, A.2    Smith, S.S.3    Weitzman, S.A.4
  • 53
    • 0018860957 scopus 로고
    • Cellular differentiation, cytidine analogs and DNA methylation
    • P.A. Jones, and S.M. Taylor Cellular differentiation, cytidine analogs and DNA methylation Cell 20 1980 85 93
    • (1980) Cell , vol.20 , pp. 85-93
    • Jones, P.A.1    Taylor, S.M.2
  • 54
    • 77955352128 scopus 로고    scopus 로고
    • Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy
    • W. Fan, Z. Tang, D. Chen, D. Moughon, X. Ding, S. Chen, M. Zhu, and Q. Zhong Keap1 facilitates p62-mediated ubiquitin aggregate clearance via autophagy Autophagy 6 2010 614 621
    • (2010) Autophagy , vol.6 , pp. 614-621
    • Fan, W.1    Tang, Z.2    Chen, D.3    Moughon, D.4    Ding, X.5    Chen, S.6    Zhu, M.7    Zhong, Q.8
  • 55
    • 77955238361 scopus 로고    scopus 로고
    • Targeting of 5-aza-2′-deoxycytidine residues by chromatin-associated DNMT1 induces proteasomal degradation of the free enzyme
    • K. Patel, J. Dickson, S. Din, K. Macleod, D. Jodrell, and B. Ramsahoye Targeting of 5-aza-2′-deoxycytidine residues by chromatin-associated DNMT1 induces proteasomal degradation of the free enzyme Nucleic Acids Res. 38 2010 4313 4324
    • (2010) Nucleic Acids Res. , vol.38 , pp. 4313-4324
    • Patel, K.1    Dickson, J.2    Din, S.3    Macleod, K.4    Jodrell, D.5    Ramsahoye, B.6
  • 56
    • 33745135040 scopus 로고    scopus 로고
    • Role of the unfolded protein response (UPR) in cataract formation
    • K. Ikesugi, R. Yamamoto, M.L. Mulhern, and T. Shinohara Role of the unfolded protein response (UPR) in cataract formation Exp. Eye Res. 83 2006 508 516
    • (2006) Exp. Eye Res. , vol.83 , pp. 508-516
    • Ikesugi, K.1    Yamamoto, R.2    Mulhern, M.L.3    Shinohara, T.4
  • 57
    • 0028019039 scopus 로고
    • Methylglyoxal concentration and glyoxalase activities in the human lens
    • G.M. Haik Jr, T.W. Lo, and P.J. Thornalley Methylglyoxal concentration and glyoxalase activities in the human lens Exp. Eye Res. 59 1994 497 500
    • (1994) Exp. Eye Res. , vol.59 , pp. 497-500
    • Haik, Jr.G.M.1    Lo, T.W.2    Thornalley, P.J.3
  • 58
    • 0028292698 scopus 로고
    • Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications
    • A.C. McLellan, P.J. Thornalley, J. Benn, and P.H. Sonksen Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications Clin. Sci. 87 1994 21 29
    • (1994) Clin. Sci. , vol.87 , pp. 21-29
    • McLellan, A.C.1    Thornalley, P.J.2    Benn, J.3    Sonksen, P.H.4
  • 59
    • 0036239372 scopus 로고    scopus 로고
    • Substrate-induced up-regulation of aldose reductase by methylglyoxal, a reactive oxoaldehyde elevated in diabetes
    • K.C. Chang, K.S. Paek, H.J. Kim, Y.S. Lee, C. Yabe-Nishimura, and H.G. Seo Substrate-induced up-regulation of aldose reductase by methylglyoxal, a reactive oxoaldehyde elevated in diabetes Mol. Pharmacol. 61 2002 1184 1191
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1184-1191
    • Chang, K.C.1    Paek, K.S.2    Kim, H.J.3    Lee, Y.S.4    Yabe-Nishimura, C.5    Seo, H.G.6
  • 61
    • 14244252567 scopus 로고    scopus 로고
    • Vitrectomy surgery increases oxygen exposure to the lens: A possible mechanism for nuclear cataract formation
    • N.M. Holekamp, Y.B. Shui, and D.C. Beebe Vitrectomy surgery increases oxygen exposure to the lens: a possible mechanism for nuclear cataract formation Am. J. Ophthalmol. 139 2005 302 310
    • (2005) Am. J. Ophthalmol. , vol.139 , pp. 302-310
    • Holekamp, N.M.1    Shui, Y.B.2    Beebe, D.C.3
  • 63
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis: Cytochrome c-independent activation of caspase-9 by caspase-12
    • N. Morishima, K. Nakanishi, H. Takenouchi, T. Shibata, and Y. Yasuhiko An endoplasmic reticulum stress-specific caspase cascade in apoptosis: cytochrome c-independent activation of caspase-9 by caspase-12 J. Biol. Chem. 277 2002 34287 34294
    • (2002) J. Biol. Chem. , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 65
    • 0035727359 scopus 로고    scopus 로고
    • Proteolysis by m-calpain enhances in vitro light scattering by crystallins from human and bovine lenses
    • M. Shih, L.L. David, K.J. Lampi, H. Ma, C. Fukiage, M. Azuma, and T.R. Shearer Proteolysis by m-calpain enhances in vitro light scattering by crystallins from human and bovine lenses Curr. Eye Res. 22 2001 458 469
    • (2001) Curr. Eye Res. , vol.22 , pp. 458-469
    • Shih, M.1    David, L.L.2    Lampi, K.J.3    Ma, H.4    Fukiage, C.5    Azuma, M.6    Shearer, T.R.7
  • 66
    • 0032829602 scopus 로고    scopus 로고
    • Identification of NRF2, a member of the NF-E2 family of transcription factors, as a substrate for caspase-3(-like) proteases
    • T. Ohtsubo, S. Kamada, T. Mikami, H. Murakami, and Y. Tsujimoto Identification of NRF2, a member of the NF-E2 family of transcription factors, as a substrate for caspase-3(-like) proteases Cell Death Differ. 6 1999 865 872
    • (1999) Cell Death Differ. , vol.6 , pp. 865-872
    • Ohtsubo, T.1    Kamada, S.2    Mikami, T.3    Murakami, H.4    Tsujimoto, Y.5
  • 68
    • 0031732522 scopus 로고    scopus 로고
    • Methylglyoxal-derived modifications in lens aging and cataract formation
    • F.A. Shamsi, K. Lin, C. Sady, and R.H. Nagaraj Methylglyoxal-derived modifications in lens aging and cataract formation Invest. Ophthalmol. Visual Sci. 39 1998 2355 2364
    • (1998) Invest. Ophthalmol. Visual Sci. , vol.39 , pp. 2355-2364
    • Shamsi, F.A.1    Lin, K.2    Sady, C.3    Nagaraj, R.H.4
  • 71
    • 84868363002 scopus 로고    scopus 로고
    • A possible gene silencing mechanism: Hypermethylation of the Keap1 promoter abrogates binding of the transcription factor Sp1 in lung cancer cells
    • D. Guo, B. Wu, J. Yan, X. Li, H. Sun, and D. Zhou A possible gene silencing mechanism: hypermethylation of the Keap1 promoter abrogates binding of the transcription factor Sp1 in lung cancer cells Biochem. Biophys. Res. Commun. 428 2012 80 85
    • (2012) Biochem. Biophys. Res. Commun. , vol.428 , pp. 80-85
    • Guo, D.1    Wu, B.2    Yan, J.3    Li, X.4    Sun, H.5    Zhou, D.6
  • 75
    • 45849133744 scopus 로고    scopus 로고
    • Hypermethylation of the Keap1 gene in human lung cancer cell lines and lung cancer tissues
    • R. Wang, J. An, F. Ji, H. Jiao, H. Sun, and D. Zhou Hypermethylation of the Keap1 gene in human lung cancer cell lines and lung cancer tissues Biochem. Biophys. Res. Commun. 373 2008 151 154
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 151-154
    • Wang, R.1    An, J.2    Ji, F.3    Jiao, H.4    Sun, H.5    Zhou, D.6
  • 76
    • 76649089973 scopus 로고    scopus 로고
    • Loss of Kelch-like ECH-associated protein 1 function in prostate cancer cells causes chemoresistance and radioresistance and promotes tumor growth
    • P. Zhang, A. Singh, S. Yegnasubramanian, D. Esopi, P. Kombairaju, M. Bodas, H. Wu, S.G. Bova, and S. Biswal Loss of Kelch-like ECH-associated protein 1 function in prostate cancer cells causes chemoresistance and radioresistance and promotes tumor growth Mol. Cancer Ther. 9 2010 336 346
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 336-346
    • Zhang, P.1    Singh, A.2    Yegnasubramanian, S.3    Esopi, D.4    Kombairaju, P.5    Bodas, M.6    Wu, H.7    Bova, S.G.8    Biswal, S.9


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