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Volumn 21, Issue 1, 2016, Pages 192-202

Nuclear factor erythroid-2 related factor 2 (Nrf2)-mediated Protein quality control in cardiomyocytes

Author keywords

Autophagy; Nuclear factor erythroid 2 related factor 2; Proteasome; Protein quality control

Indexed keywords

NFE2L2 PROTEIN, HUMAN; TRANSCRIPTION FACTOR NRF2;

EID: 85016151356     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4384     Document Type: Article
Times cited : (29)

References (71)
  • 1
    • 84919787042 scopus 로고    scopus 로고
    • The interplay between autophagy and the ubiquitin-proteasome system in cardiac proteotoxicity
    • C. Wang and X. Wang: The interplay between autophagy and the ubiquitin-proteasome system in cardiac proteotoxicity. Biochim Biophys Acta, 1852, 188-194 (2015) DOI: 10.1016/j.bbadis.2014.07.028
    • (2015) Biochim Biophys Acta , vol.1852 , pp. 188-194
    • Wang, C.1    Wang, X.2
  • 2
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • U. Schubert, L. C. Anton, J. Gibbs, C. C. Norbury, J. W. Yewdell and J. R. Bennink: Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature, 404, 770-774 (2000) DOI: 10.1038/35008096
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 3
    • 84892865694 scopus 로고    scopus 로고
    • Sorting out the trash: The spatial nature of eukaryotic protein quality control
    • E. M. Sontag, W. I. Vonk and J. Frydman: Sorting out the trash: the spatial nature of eukaryotic protein quality control. Curr Opin Cell Biol, 26, 139-146 (2014) DOI: 10.1016/j.ceb.2013.12.006
    • (2014) Curr Opin Cell Biol , vol.26 , pp. 139-146
    • Sontag, E.M.1    Vonk, W.I.2    Frydman, J.3
  • 5
    • 84872865382 scopus 로고    scopus 로고
    • Posttranslational modification and quality control
    • X. Wang, J. S. Pattison and H. Su: Posttranslational modification and quality control. Circ Res, 112, 367-381 (2013) DOI: 10.1161/CIRCRESAHA.112.268706
    • (2013) Circ Res , vol.112 , pp. 367-381
    • Wang, X.1    Pattison, J.S.2    Su, H.3
  • 6
    • 84890204277 scopus 로고    scopus 로고
    • Protein quality control and elimination of protein waste: The role of the ubiquitin-proteasome system
    • I. Amm, T. Sommer and D. H. Wolf: Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. Biochim Biophys Acta, 1843, 182-196 (2014) DOI: 10.1016/j.bbamcr.2013.06.031
    • (2014) Biochim Biophys Acta , vol.1843 , pp. 182-196
    • Amm, I.1    Sommer, T.2    Wolf, D.H.3
  • 7
    • 84899918569 scopus 로고    scopus 로고
    • Proteasomal and lysosomal protein degradation and heart disease
    • X. Wang and J. Robbins: Proteasomal and lysosomal protein degradation and heart disease. J Mol Cell Cardiol, 71, 16-24 (2014) DOI: 10.1016/j.yjmcc.2013.11.006
    • (2014) J Mol Cell Cardiol , vol.71 , pp. 16-24
    • Wang, X.1    Robbins, J.2
  • 8
    • 72949105329 scopus 로고    scopus 로고
    • Stressing the ubiquitin-proteasome system
    • N. P. Dantuma and K. Lindsten: Stressing the ubiquitin-proteasome system. Cardiovasc Res, 85, 263-271 (2010) DOI: 10.1093/cvr/cvp255
    • (2010) Cardiovasc Res , vol.85 , pp. 263-271
    • Dantuma, N.P.1    Lindsten, K.2
  • 9
    • 79954590790 scopus 로고    scopus 로고
    • Enhancement of proteasome function by PA28α overexpression protects against oxidative stress
    • J. Li, S. R. Powell and X. Wang: Enhancement of proteasome function by PA28α overexpression protects against oxidative stress. FASEB J, 25, 883-893 (2011) DOI: 10.1096/fj.10-160895
    • (2011) FASEB J , vol.25 , pp. 883-893
    • Li, J.1    Powell, S.R.2    Wang, X.3
  • 10
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • J. Li, K. M. Horak, H. Su, A. Sanbe, J. Robbins and X. Wang: Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J Clin Invest, 121, 3689-3700 (2011) DOI: 10.1172/JCI45709
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1    Horak, K.M.2    Su, H.3    Sanbe, A.4    Robbins, J.5    Wang, X.6
  • 11
    • 16744367068 scopus 로고
    • Introduction to the physiopathology of the lysosomes
    • C. de Duve: (Introduction to the physiopathology of the lysosomes). Brux Med, 46, 1087-1094 (1966)
    • (1966) Brux Med , vol.46 , pp. 1087-1094
    • De Duve, C.1
  • 13
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • A. Stolz, A. Ernst and I. Dikic: Cargo recognition and trafficking in selective autophagy. Nat Cell Biol, 16, 495-501 (2014) DOI: 10.1038/ncb2979
    • (2014) Nat Cell Biol , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 14
    • 84864318195 scopus 로고    scopus 로고
    • Chaperonemediated autophagy: A unique way to enter the lysosome world
    • S. Kaushik and A. M. Cuervo: Chaperonemediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol, 22, 407-417 (2012) DOI: 10.1016/j.tcb.2012.05.006
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 15
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy: The ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • M. S. Willis, W. H. Townley-Tilson, E. Y. Kang, J. W. Homeister and C. Patterson: Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease. Circ Res, 106, 463-478 (2010) DOI: 10.1161/CIRCRESAHA.109.208801
    • (2010) Circ Res , vol.106 , pp. 463-478
    • Willis, M.S.1    Townley-Tilson, W.H.2    Kang, E.Y.3    Homeister, J.W.4    Patterson, C.5
  • 16
    • 84899502960 scopus 로고    scopus 로고
    • Autophagy and cancer therapy
    • A. Thorburn, D. H. Thamm and D. L. Gustafson: Autophagy and cancer therapy. Mol Pharmacol, 85, 830-838 (2014) DOI: 10.1124/mol.114.091850
    • (2014) Mol Pharmacol , vol.85 , pp. 830-838
    • Thorburn, A.1    Thamm, D.H.2    Gustafson, D.L.3
  • 17
    • 84904230331 scopus 로고    scopus 로고
    • The regulation of the autophagic network and its implications for human disease
    • J. Yang, S. Carra, W. G. Zhu and H. H. Kampinga: The regulation of the autophagic network and its implications for human disease. Int J Biol Sci, 9, 1121-1133 (2013) DOI: 10.7150/ijbs.6666
    • (2013) Int J Biol Sci , vol.9 , pp. 1121-1133
    • Yang, J.1    Carra, S.2    Zhu, W.G.3    Kampinga, H.H.4
  • 18
    • 80052801111 scopus 로고    scopus 로고
    • Autophagy as a therapeutic target in cardiovascular disease
    • A. Nemchenko, M. Chiong, A. Turer, S. Lavandero and J. A. Hill: Autophagy as a therapeutic target in cardiovascular disease. J Mol Cell Cardiol, 51, 584-593 (2011) DOI: 10.1016/j.yjmcc.2011.06.010
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 584-593
    • Nemchenko, A.1    Chiong, M.2    Turer, A.3    Lavandero, S.4    Hill, J.A.5
  • 19
    • 82855181806 scopus 로고    scopus 로고
    • Proteasome malfunction activates macroautophagy in the heart
    • Q. Zheng, H. Su, Z. Tian and X. Wang: Proteasome malfunction activates macroautophagy in the heart. Am J Cardiovasc Dis, 1, 214-226 (2011)
    • (2011) Am J Cardiovasc Dis , vol.1 , pp. 214-226
    • Zheng, Q.1    Su, H.2    Tian, Z.3    Wang, X.4
  • 20
    • 79961022260 scopus 로고    scopus 로고
    • Autophagy and p62 in cardiac proteinopathy
    • Q. Zheng, H. Su, M. J. Ranek and X. Wang: Autophagy and p62 in cardiac proteinopathy. Circ Res, 109, 296-308 (2011) DOI: 10.1161/CIRCRESAHA.111.244707
    • (2011) Circ Res , vol.109 , pp. 296-308
    • Zheng, Q.1    Su, H.2    Ranek, M.J.3    Wang, X.4
  • 22
    • 84903520218 scopus 로고    scopus 로고
    • Autophagic-lysosomal inhibition compromises ubiquitin-proteasome system performance in a p62 dependent manner in cardiomyocytes
    • Z. Tian, C. Wang, C. Hu, Y. Tian, J. Liu and X. Wang: Autophagic-lysosomal inhibition compromises ubiquitin-proteasome system performance in a p62 dependent manner in cardiomyocytes. PLoS One, 9, e100715 (2014) DOI: 10.1371/journal.pone.0100715
    • (2014) PLoS One , vol.9 , pp. e100715
    • Tian, Z.1    Wang, C.2    Hu, C.3    Tian, Y.4    Liu, J.5    Wang, X.6
  • 23
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitinproteasome pathway substrates
    • V. I. Korolchuk, A. Mansilla, F. M. Menzies and D. C. Rubinsztein: Autophagy inhibition compromises degradation of ubiquitinproteasome pathway substrates. Mol Cell, 33, 517-527 (2009) DOI: 10.1016/j.molcel.2009.01.021
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 24
    • 14044254798 scopus 로고    scopus 로고
    • Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation
    • M. Kobayashi and M. Yamamoto: Molecular mechanisms activating the Nrf2-Keap1 pathway of antioxidant gene regulation. Antioxid Redox Signal, 7, 385-394 (2005) DOI: 10.1089/ars.2005.7.385
    • (2005) Antioxid Redox Signal , vol.7 , pp. 385-394
    • Kobayashi, M.1    Yamamoto, M.2
  • 25
    • 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, 89-116 (2007) DOI: 10.1146/annurev. pharmtox.46.120604. 141046
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 26
    • 67650453921 scopus 로고    scopus 로고
    • Targeting the Nrf2 pathway against cardiovascular disease
    • J. Li, T. Ichikawa, J. S. Janicki and T. Cui: Targeting the Nrf2 pathway against cardiovascular disease. Expert Opin Ther Targets, 13, 785-794 (2009) DOI: 10.1517/14728220903025762
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 785-794
    • Li, J.1    Ichikawa, T.2    Janicki, J.S.3    Cui, T.4
  • 27
    • 84878572136 scopus 로고    scopus 로고
    • Toward clinical application of the Keap1-Nrf2 pathway
    • T. Suzuki, H. Motohashi and M. Yamamoto: Toward clinical application of the Keap1-Nrf2 pathway. Trends Pharmacol Sci, 34, 340-346 (2013) DOI: 10.1016/j.tips.2013.04.005
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 340-346
    • Suzuki, T.1    Motohashi, H.2    Yamamoto, M.3
  • 28
    • 77649271223 scopus 로고    scopus 로고
    • The rise of antioxidant signaling-the evolution and hormetic actions of Nrf2
    • J. Maher and M. Yamamoto: The rise of antioxidant signaling-the evolution and hormetic actions of Nrf2. Toxicol Appl Pharmacol, 244, 4-15 (2010) DOI: 10.1016/j.taap. 2010.01.011
    • (2010) Toxicol Appl Pharmacol , vol.244 , pp. 4-15
    • Maher, J.1    Yamamoto, M.2
  • 29
    • 33750543308 scopus 로고    scopus 로고
    • Negative regulation of the Nrf1 transcription factor by its N-terminal domain is independent of Keap1: Nrf1, but not Nrf2, is targeted to the endoplasmic reticulum
    • Y. Zhang, D. H. Crouch, M. Yamamoto and J. D. Hayes: Negative regulation of the Nrf1 transcription factor by its N-terminal domain is independent of Keap1: Nrf1, but not Nrf2, is targeted to the endoplasmic reticulum. Biochem J, 399, 373-385 (2006) DOI: 10.1042/BJ20060725
    • (2006) Biochem J , vol.399 , pp. 373-385
    • Zhang, Y.1    Crouch, D.H.2    Yamamoto, M.3    Hayes, J.D.4
  • 30
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function
    • W. Wang and J. Y. Chan: Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain. Inhibition of nuclear translocation and transacting function. J Biol Chem, 281, 19676-19687 (2006) DOI: 10.1074/jbc. M602802200
    • (2006) J Biol Chem , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 31
    • 15244359632 scopus 로고    scopus 로고
    • Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia
    • Z. Xu, L. Chen, L. Leung, T. S. Yen, C. Lee and J. Y. Chan: Liver-specific inactivation of the Nrf1 gene in adult mouse leads to nonalcoholic steatohepatitis and hepatic neoplasia. Proc Natl Acad Sci U S A, 102, 4120-4125 (2005) DOI: 10.1073/pnas.0500660102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 4120-4125
    • Xu, Z.1    Chen, L.2    Leung, L.3    Yen, T.S.4    Lee, C.5    Chan, J.Y.6
  • 32
    • 10944235410 scopus 로고    scopus 로고
    • Nrf3 negatively regulates antioxidantresponse element-mediated expression and antioxidant induction of NAD (P) H:Quinone oxidoreductase1 gene
    • K. Sankaranarayanan and A. K. Jaiswal: Nrf3 negatively regulates antioxidantresponse element-mediated expression and antioxidant induction of NAD (P) H:quinone oxidoreductase1 gene. J Biol Chem, 279, 50810-50817 (2004) DOI: 10.1074/jbc. M404984200
    • (2004) J Biol Chem , vol.279 , pp. 50810-50817
    • Sankaranarayanan, K.1    Jaiswal, A.K.2
  • 33
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • M. K. Kwak, N. Wakabayashi, J. L. Greenlaw, M. Yamamoto and T. W. Kensler: Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol Cell Biol, 23, 8786-8794 (2003) DOI: 10.1128/MCB.23.23.8786-8794.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 34
    • 0037424262 scopus 로고    scopus 로고
    • Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival
    • M. K. Kwak, N. Wakabayashi, K. Itoh, H. Motohashi, M. Yamamoto and T. W. Kensler: Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J Biol Chem, 278, 8135-8145 (2003) DOI: 10.1074/jbc. M211898200
    • (2003) J Biol Chem , vol.278 , pp. 8135-8145
    • Kwak, M.K.1    Wakabayashi, N.2    Itoh, K.3    Motohashi, H.4    Yamamoto, M.5    Kensler, T.W.6
  • 35
    • 70449674487 scopus 로고    scopus 로고
    • Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2)
    • A. Arlt, I. Bauer, C. Schafmayer, J. Tepel, S. S. Muerkoster, M. Brosch, C. Roder, H. Kalthoff, J. Hampe, M. P. Moyer, U. R. Folsch and H. Schafer: Increased proteasome subunit protein expression and proteasome activity in colon cancer relate to an enhanced activation of nuclear factor E2-related factor 2 (Nrf2). Oncogene, 28, 3983-3996 (2009) DOI: 10.1038/onc.2009.264
    • (2009) Oncogene , vol.28 , pp. 3983-3996
    • Arlt, A.1    Bauer, I.2    Schafmayer, C.3    Tepel, J.4    Muerkoster, S.S.5    Brosch, M.6    Roder, C.7    Kalthoff, H.8    Hampe, J.9    Moyer, M.P.10    Folsch, U.R.11    Schafer, H.12
  • 36
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress
    • A. M. Pickering, R. A. Linder, H. Zhang, H. J. Forman and K. J. Davies: Nrf2-dependent induction of proteasome and Pa28alphabeta regulator are required for adaptation to oxidative stress. J Biol Chem, 287, 10021-10031 (2012) DOI: 10.1074/jbc. M111.277145
    • (2012) J Biol Chem , vol.287 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 37
    • 84899421127 scopus 로고    scopus 로고
    • Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington's disease
    • Y. Liu, C. L. Hettinger, D. Zhang, K. Rezvani, X. Wang and H. Wang: Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington's disease. J Neurochem, 129, 539-547 (2014) DOI: 10.1111/jnc.12647
    • (2014) J Neurochem , vol.129 , pp. 539-547
    • Liu, Y.1    Hettinger, C.L.2    Zhang, D.3    Rezvani, K.4    Wang, X.5    Wang, H.6
  • 38
    • 84908094625 scopus 로고    scopus 로고
    • Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells
    • J. Jang, Y. Wang, H. S. Kim, M. A. Lalli and K. S. Kosik: Nrf2, a regulator of the proteasome, controls self-renewal and pluripotency in human embryonic stem cells. Stem Cells, 32, 2616-2625 (2014) DOI: 10.1002/stem.1764
    • (2014) Stem Cells , vol.32 , pp. 2616-2625
    • Jang, J.1    Wang, Y.2    Kim, H.S.3    Lalli, M.A.4    Kosik, K.S.5
  • 41
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • S. K. Radhakrishnan, C. S. Lee, P. Young, A. Beskow, J. Y. Chan and R. J. Deshaies: Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol Cell, 38, 17-28 (2010) DOI: 10.1016/j.molcel.2010.02.029
    • (2010) Mol Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 42
    • 84904990897 scopus 로고    scopus 로고
    • Proteasomemediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97
    • Z. Sha and A. L. Goldberg: Proteasomemediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97. Curr Biol, 24, 1573-1583 (2014) DOI: 10.1016/j.cub.2014.06.004
    • (2014) Curr Biol , vol.24 , pp. 1573-1583
    • Sha, Z.1    Goldberg, A.L.2
  • 44
    • 78049398265 scopus 로고    scopus 로고
    • The antioxidant transcription factor Nrf2 negatively regulates autophagy and growth arrest induced by the anticancer redox agent mitoquinone
    • V. A. Rao, S. R. Klein, S. J. Bonar, J. Zielonka, N. Mizuno, J. S. Dickey, P. W. Keller, J. Joseph, B. Kalyanaraman and E. Shacter: The antioxidant transcription factor Nrf2 negatively regulates autophagy and growth arrest induced by the anticancer redox agent mitoquinone. J Biol Chem, 285, 34447-34459 (2010) DOI: 10.1074/jbc. M110.133579
    • (2010) J Biol Chem , vol.285 , pp. 34447-34459
    • Rao, V.A.1    Klein, S.R.2    Bonar, S.J.3    Zielonka, J.4    Mizuno, N.5    Dickey, J.S.6    Keller, P.W.7    Joseph, J.8    Kalyanaraman, B.9    Shacter, E.10
  • 45
    • 79952139698 scopus 로고    scopus 로고
    • Nrf2-mediated induction of p62 controls Toll-like receptor-4-driven aggresome-like induced structure formation and autophagic degradation
    • K. Fujita, D. Maeda, Q. Xiao and S. M. Srinivasula: Nrf2-mediated induction of p62 controls Toll-like receptor-4-driven aggresome-like induced structure formation and autophagic degradation. Proc Natl Acad Sci U S A, 108, 1427-1432 (2011) DOI: 10.1073/pnas.1014156108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1427-1432
    • Fujita, K.1    Maeda, D.2    Xiao, Q.3    Srinivasula, S.M.4
  • 47
    • 84876064507 scopus 로고    scopus 로고
    • Regulation of cigarette smoke (CS)-induced autophagy by Nrf2
    • L. Zhu, E. C. Barrett, Y. Xu, Z. Liu, A. Manoharan and Y. Chen: Regulation of Cigarette Smoke (CS)-Induced Autophagy by Nrf2. PLoS One, 8, e55695 (2013) DOI: 10.1371/journal.pone.0055695
    • (2013) PLoS One , vol.8 , pp. e55695
    • Zhu, L.1    Barrett, E.C.2    Xu, Y.3    Liu, Z.4    Manoharan, A.5    Chen, Y.6
  • 48
    • 84897093101 scopus 로고    scopus 로고
    • Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52
    • C. Jo, S. Gundemir, S. Pritchard, Y. N. Jin, I. Rahman and G. V. Johnson: Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52. Nat Commun, 5, 3496 (2014) DOI: 10.1038/ncomms4496
    • (2014) Nat Commun , vol.5 , pp. 3496
    • Jo, C.1    Gundemir, S.2    Pritchard, S.3    Jin, Y.N.4    Rahman, I.5    Johnson, G.V.6
  • 49
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • G. Kroemer, G. Marino and B. Levine: Autophagy and the integrated stress response. Mol Cell, 40, 280-293 (2010) DOI: 10.1016/j.molcel.2010.09.023
    • (2010) Mol Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 50
    • 84922489435 scopus 로고    scopus 로고
    • Oxidative stress and autophagy: The clash between damage and metabolic needs
    • G. Filomeni, D. De Zio and F. Cecconi: Oxidative stress and autophagy: the clash between damage and metabolic needs. Cell Death Differ, 22, 377-388 (2015) DOI: 10.1038/cdd.2014.150
    • (2015) Cell Death Differ , vol.22 , pp. 377-388
    • Filomeni, G.1    De Zio, D.2    Cecconi, F.3
  • 56
    • 79955418633 scopus 로고    scopus 로고
    • Up-regulation of p27 (kip1) contributes to Nrf2-mediated protection against angiotensin II-induced cardiac hypertrophy
    • J. Li, C. Zhang, Y. Xing, J. S. Janicki, M. Yamamoto, X. L. Wang, D. Q. Tang and T. Cui: Up-regulation of p27 (kip1) contributes to Nrf2-mediated protection against angiotensin II-induced cardiac hypertrophy. Cardiovasc Res, 90, 315-324 (2011) DOI: 10.1093/cvr/cvr010
    • (2011) Cardiovasc Res , vol.90 , pp. 315-324
    • Li, J.1    Zhang, C.2    Xing, Y.3    Janicki, J.S.4    Yamamoto, M.5    Wang, X.L.6    Tang, D.Q.7    Cui, T.8
  • 58
    • 79951918162 scopus 로고    scopus 로고
    • Sustained activation of nuclear erythroid 2-related factor 2/antioxidant response element signaling promotes reductive stress in the human mutant protein aggregation cardiomyopathy in mice
    • N. S. Rajasekaran, S. Varadharaj, G. D. Khanderao, C. J. Davidson, S. Kannan, M. A. Firpo, J. L. Zweier and I. J. Benjamin: Sustained activation of nuclear erythroid 2-related factor 2/antioxidant response element signaling promotes reductive stress in the human mutant protein aggregation cardiomyopathy in mice. Antioxid Redox Signal, 14, 957-971 (2011) DOI: 10.1089/ars.2010.3587
    • (2011) Antioxid Redox Signal , vol.14 , pp. 957-971
    • Rajasekaran, N.S.1    Varadharaj, S.2    Khanderao, G.D.3    Davidson, C.J.4    Kannan, S.5    Firpo, M.A.6    Zweier, J.L.7    Benjamin, I.J.8
  • 61
    • 84921752494 scopus 로고    scopus 로고
    • Sumo E2 enzyme UBC9 is required for efficient protein quality control in cardiomyocytes
    • M. K. Gupta, J. Gulick, R. Liu, X. Wang, J. D. Molkentin and J. Robbins: Sumo E2 enzyme UBC9 is required for efficient protein quality control in cardiomyocytes. Circ Res, 115, 721-729 (2014) DOI: 10.1161/CIRCRESAHA.115.304760
    • (2014) Circ Res , vol.115 , pp. 721-729
    • Gupta, M.K.1    Gulick, J.2    Liu, R.3    Wang, X.4    Molkentin, J.D.5    Robbins, J.6
  • 62
    • 27944450427 scopus 로고    scopus 로고
    • Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake
    • Q. Chen, J. B. Liu, K. M. Horak, H. Zheng, A. R. Kumarapeli, J. Li, F. Li, A. M. Gerdes, E. F. Wawrousek and X. Wang: Intrasarcoplasmic amyloidosis impairs proteolytic function of proteasomes in cardiomyocytes by compromising substrate uptake. Circ Res, 97, 1018-1026 (2005) DOI: 10.1161/01. RES.0000189262.92896.0b
    • (2005) Circ Res , vol.97 , pp. 1018-1026
    • Chen, Q.1    Liu, J.B.2    Horak, K.M.3    Zheng, H.4    Kumarapeli, A.R.5    Li, J.6    Li, F.7    Gerdes, A.M.8    Wawrousek, E.F.9    Wang, X.10
  • 63
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • X. Wang, R. Klevitsky, W. Huang, J. Glasford, F. Li and J. Robbins: AlphaB-crystallin modulates protein aggregation of abnormal desmin. Circ Res, 93, 998-1005 (2003) DOI: 10.1161/01. RES.0000102401.77712. ED
    • (2003) Circ Res , vol.93 , pp. 998-1005
    • Wang, X.1    Klevitsky, R.2    Huang, W.3    Glasford, J.4    Li, F.5    Robbins, J.6
  • 64
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-alphaBcrystallin causes aberrant desmin and alphaBcrystallin aggregation and cardiomyopathy in mice
    • X. Wang, H. Osinska, R. Klevitsky, A. M. Gerdes, M. Nieman, J. Lorenz, T. Hewett and J. Robbins: Expression of R120G-alphaBcrystallin causes aberrant desmin and alphaBcrystallin aggregation and cardiomyopathy in mice. Circ Res, 89, 84-91 (2001) DOI: 10.1161/hh1301.092688
    • (2001) Circ Res , vol.89 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8
  • 68
    • 79551575483 scopus 로고    scopus 로고
    • Diabetic downregulation of Nrf2 activity via ERK contributes to oxidative stress-induced insulin resistance in cardiac cells in vitro and in vivo
    • Y. Tan, T. Ichikawa, J. Li, Q. Si, H. Yang, X. Chen, C. S. Goldblatt, C. J. Meyer, X. Li, L. Cai and T. Cui: Diabetic downregulation of Nrf2 activity via ERK contributes to oxidative stress-induced insulin resistance in cardiac cells in vitro and in vivo. Diabetes, 60, 625-633 (2011) DOI: 10.2337/db10-1164
    • (2011) Diabetes , vol.60 , pp. 625-633
    • Tan, Y.1    Ichikawa, T.2    Li, J.3    Si, Q.4    Yang, H.5    Chen, X.6    Goldblatt, C.S.7    Meyer, C.J.8    Li, X.9    Cai, L.10    Cui, T.11
  • 70
    • 34247526984 scopus 로고    scopus 로고
    • Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer
    • K. T. Liby, M. M. Yore and M. B. Sporn: Triterpenoids and rexinoids as multifunctional agents for the prevention and treatment of cancer. Nat Rev Cancer, 7, 357-369 (2007) DOI: 10.1038/nrc2129
    • (2007) Nat Rev Cancer , vol.7 , pp. 357-369
    • Liby, K.T.1    Yore, M.M.2    Sporn, M.B.3
  • 71
    • 84890109914 scopus 로고    scopus 로고
    • Natural product-derived pharmacological modulators of Nrf2/ARE pathway for chronic diseases
    • H. Kumar, I. S. Kim, S. V. More, B. W. Kim and D. K. Choi: Natural product-derived pharmacological modulators of Nrf2/ARE pathway for chronic diseases. Nat Prod Rep, 31, 109-139 (2014) DOI: 10.1039/C3NP70065H
    • (2014) Nat Prod Rep , vol.31 , pp. 109-139
    • Kumar, H.1    Kim, I.S.2    More, S.V.3    Kim, B.W.4    Choi, D.K.5


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