메뉴 건너뛰기




Volumn 37, Issue 8, 2017, Pages

p97 negatively regulates NRF2 by extracting ubiquitylated NRF2 from the KEAP1-CUL3 E3 complex

Author keywords

Autophagy; Cancer chemoresistance; KEAP1; NRF2; Oxidative stress; P97; Proteasome; Protein quality control; Ubiquitylation

Indexed keywords

ADENOSINE TRIPHOSPHATE; CUL3 E3 PROTEIN; HETERODIMER; KELCH LIKE ECH ASSOCIATED PROTEIN 1; PROTEASOME; PROTEIN P97; TRANSCRIPTION FACTOR NRF2; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UBXN7 PROTEIN; UFD1 PROTEIN; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATASE; CARRIER PROTEIN; CDC48 PROTEIN; CELL CYCLE PROTEIN; CUL3 PROTEIN, HUMAN; CULLIN; KEAP1 PROTEIN, HUMAN; PROTEIN BINDING; RBX1 PROTEIN, HUMAN;

EID: 85017152943     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00660-16     Document Type: Article
Times cited : (84)

References (56)
  • 1
    • 84969900554 scopus 로고    scopus 로고
    • Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease
    • Tebay LE, Robertson H, Durant ST, Vitale SR, Penning TM, Dinkova-Kostova AT, Hayes JD. 2015. Mechanisms of activation of the transcription factor Nrf2 by redox stressors, nutrient cues, and energy status and the pathways through which it attenuates degenerative disease. Free Radic Biol Med 88:108-146. https://doi.org/10.1016/j.freeradbiomed.2015.06.021.
    • (2015) Free Radic Biol Med , vol.88 , pp. 108-146
    • Tebay, L.E.1    Robertson, H.2    Durant, S.T.3    Vitale, S.R.4    Penning, T.M.5    Dinkova-Kostova, A.T.6    Hayes, J.D.7
  • 2
    • 0029043995 scopus 로고
    • Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins
    • Itoh K, Igarashi K, Hayashi N, Nishizawa M, Yamamoto M. 1995. Cloning and characterization of a novel erythroid cell-derived CNC family transcription factor heterodimerizing with the small Maf family proteins. Mol Cell Biol 15:4184-4193. https://doi.org/10.1128/MCB.15.8.4184.
    • (1995) Mol Cell Biol , vol.15 , pp. 4184-4193
    • Itoh, K.1    Igarashi, K.2    Hayashi, N.3    Nishizawa, M.4    Yamamoto, M.5
  • 3
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, Yamamoto M. 1999. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev 13:76-86. https://doi.org/10.1101/gad.13.1.76.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 4
    • 3543008924 scopus 로고    scopus 로고
    • Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2
    • Kobayashi A, Kang MI, Okawa H, Ohtsuji M, Zenke Y, Chiba T, Igarashi K, Yamamoto M. 2004. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate proteasomal degradation of Nrf2. Mol Cell Biol 24:7130-7139. https://doi.org/10.1128/MCB.24.16.7130-7139.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 7130-7139
    • Kobayashi, A.1    Kang, M.I.2    Okawa, H.3    Ohtsuji, M.4    Zenke, Y.5    Chiba, T.6    Igarashi, K.7    Yamamoto, M.8
  • 5
    • 10044228504 scopus 로고    scopus 로고
    • Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex
    • Zhang DD, Lo SC, Cross JV, Templeton DJ, Hannink M. 2004. Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex. Mol Cell Biol 24:10941-10953. https://doi.org/10.1128/MCB.24.24.10941-10953.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 10941-10953
    • Zhang, D.D.1    Lo, S.C.2    Cross, J.V.3    Templeton, D.J.4    Hannink, M.5
  • 6
    • 0037015035 scopus 로고    scopus 로고
    • Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants
    • Dinkova-Kostova AT, Holtzclaw WD, Cole RN, Itoh K, Wakabayashi N, Katoh Y, Yamamoto M, Talalay P. 2002. Direct evidence that sulfhydryl groups of Keap1 are the sensors regulating induction of phase 2 enzymes that protect against carcinogens and oxidants. Proc Natl Acad Sci U S A 99:11908-11913. https://doi.org/10.1073/pnas.172398899.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11908-11913
    • Dinkova-Kostova, A.T.1    Holtzclaw, W.D.2    Cole, R.N.3    Itoh, K.4    Wakabayashi, N.5    Katoh, Y.6    Yamamoto, M.7    Talalay, P.8
  • 7
    • 0242580049 scopus 로고    scopus 로고
    • Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress
    • Zhang DD, Hannink M. 2003. Distinct cysteine residues in Keap1 are required for Keap1-dependent ubiquitination of Nrf2 and for stabilization of Nrf2 by chemopreventive agents and oxidative stress. Mol Cell Biol 23:8137-8151. https://doi.org/10.1128/MCB.23.22.8137-8151.2003.
    • (2003) Mol Cell Biol , vol.23 , pp. 8137-8151
    • Zhang, D.D.1    Hannink, M.2
  • 8
    • 84884338770 scopus 로고    scopus 로고
    • Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex
    • Baird L, Lleres D, Swift S, Dinkova-Kostova AT. 2013. Regulatory flexibility in the Nrf2-mediated stress response is conferred by conformational cycling of the Keap1-Nrf2 protein complex. Proc Natl Acad Sci U S A 110:15259-15264. https://doi.org/10.1073/pnas.1305687110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 15259-15264
    • Baird, L.1    Lleres, D.2    Swift, S.3    Dinkova-Kostova, A.T.4
  • 10
    • 84964238183 scopus 로고    scopus 로고
    • Small Maf proteins (MafF, MafG, MafK): history, structure and function
    • Katsuoka F, Yamamoto M. 2016. Small Maf proteins (MafF, MafG, MafK): history, structure and function. Gene 586:197-205. https://doi.org/10.1016/j.gene.2016.03.058.
    • (2016) Gene , vol.586 , pp. 197-205
    • Katsuoka, F.1    Yamamoto, M.2
  • 11
    • 84969983910 scopus 로고    scopus 로고
    • The emerging role of Nrf2 in mitochondrial function
    • Dinkova-Kostova AT, Abramov AY. 2015. The emerging role of Nrf2 in mitochondrial function. Free Radic Biol Med 88:179-188. https://doi.org/10.1016/j.freeradbiomed.2015.04.036.
    • (2015) Free Radic Biol Med , vol.88 , pp. 179-188
    • Dinkova-Kostova, A.T.1    Abramov, A.Y.2
  • 12
    • 84938694329 scopus 로고    scopus 로고
    • Molecular mechanisms of Nrf2 regulation and how these influence chemical modulation for disease intervention
    • Harder B, Jiang T, Wu T, Tao S, Rojo de la Vega M, Tian W, Chapman E, Zhang DD. 2015. Molecular mechanisms of Nrf2 regulation and how these influence chemical modulation for disease intervention. Biochem Soc Trans 43:680-686. https://doi.org/10.1042/BST20150020.
    • (2015) Biochem Soc Trans , vol.43 , pp. 680-686
    • Harder, B.1    Jiang, T.2    Wu, T.3    Tao, S.4    Rojo de la Vega, M.5    Tian, W.6    Chapman, E.7    Zhang, D.D.8
  • 13
    • 33644856080 scopus 로고    scopus 로고
    • The double-edged sword of Nrf2: subversion of redox homeostasis during the evolution of cancer
    • Hayes JD, McMahon M. 2006. The double-edged sword of Nrf2: subversion of redox homeostasis during the evolution of cancer. Mol Cell 21:732-734. https://doi.org/10.1016/j.molcel.2006.03.004.
    • (2006) Mol Cell , vol.21 , pp. 732-734
    • Hayes, J.D.1    McMahon, M.2
  • 18
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62
    • Lau A, Wang XJ, Zhao F, Villeneuve NF, Wu T, Jiang T, Sun Z, White E, Zhang DD. 2010. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol Cell Biol 30:3275-3285. https://doi.org/10.1128/MCB.00248-10.
    • (2010) Mol Cell Biol , vol.30 , pp. 3275-3285
    • Lau, A.1    Wang, X.J.2    Zhao, F.3    Villeneuve, N.F.4    Wu, T.5    Jiang, T.6    Sun, Z.7    White, E.8    Zhang, D.D.9
  • 20
    • 77954599053 scopus 로고    scopus 로고
    • p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription
    • Jain A, Lamark T, Sjottem E, Larsen KB, Awuh JA, Overvatn A, McMahon M, Hayes JD, Johansen T. 2010. p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. J Biol Chem 285:22576-22591. https://doi.org/10.1074/jbc.M110.118976.
    • (2010) J Biol Chem , vol.285 , pp. 22576-22591
    • Jain, A.1    Lamark, T.2    Sjottem, E.3    Larsen, K.B.4    Awuh, J.A.5    Overvatn, A.6    McMahon, M.7    Hayes, J.D.8    Johansen, T.9
  • 21
    • 34548772935 scopus 로고    scopus 로고
    • Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2
    • Sun Z, Zhang S, Chan JY, Zhang DD. 2007. Keap1 controls postinduction repression of the Nrf2-mediated antioxidant response by escorting nuclear export of Nrf2. Mol Cell Biol 27:6334-6349. https://doi.org/10.1128/MCB.00630-07.
    • (2007) Mol Cell Biol , vol.27 , pp. 6334-6349
    • Sun, Z.1    Zhang, S.2    Chan, J.Y.3    Zhang, D.D.4
  • 22
    • 79955442831 scopus 로고    scopus 로고
    • KPNA6 (importin +7)-mediated nuclear import of Keap1 represses the Nrf2-dependent antioxidant response
    • Sun Z, Wu T, Zhao F, Lau A, Birch CM, Zhang DD. 2011. KPNA6 (importin +7)-mediated nuclear import of Keap1 represses the Nrf2-dependent antioxidant response. Mol Cell Biol 31:1800-1811. https://doi.org/10.1128/MCB.05036-11.
    • (2011) Mol Cell Biol , vol.31 , pp. 1800-1811
    • Sun, Z.1    Wu, T.2    Zhao, F.3    Lau, A.4    Birch, C.M.5    Zhang, D.D.6
  • 24
    • 84878963658 scopus 로고    scopus 로고
    • Arsenic inhibits autophagic flux, activating the Nrf2-Keap1 pathway in a p62-dependent manner
    • Lau A, Zheng Y, Tao S, Wang H, Whitman SA, White E, Zhang DD. 2013. Arsenic inhibits autophagic flux, activating the Nrf2-Keap1 pathway in a p62-dependent manner. Mol Cell Biol 33:2436-2446. https://doi.org/10.1128/MCB.01748-12.
    • (2013) Mol Cell Biol , vol.33 , pp. 2436-2446
    • Lau, A.1    Zheng, Y.2    Tao, S.3    Wang, H.4    Whitman, S.A.5    White, E.6    Zhang, D.D.7
  • 25
    • 84906315540 scopus 로고    scopus 로고
    • Nrf2 promotes the development of fibrosis and tumorigenesis in mice with defective hepatic autophagy
    • Ni HM, Woolbright BL, Williams J, Copple B, Cui W, Luyendyk JP, Jaeschke H, Ding WX. 2014. Nrf2 promotes the development of fibrosis and tumorigenesis in mice with defective hepatic autophagy. J Hepatol 61:617-625. https://doi.org/10.1016/j.jhep.2014.04.043.
    • (2014) J Hepatol , vol.61 , pp. 617-625
    • Ni, H.M.1    Woolbright, B.L.2    Williams, J.3    Copple, B.4    Cui, W.5    Luyendyk, J.P.6    Jaeschke, H.7    Ding, W.X.8
  • 27
    • 84856474838 scopus 로고    scopus 로고
    • Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system
    • Meyer H, Bug M, Bremer S. 2012. Emerging functions of the VCP/p97 AAA-ATPase in the ubiquitin system. Nat Cell Biol 14:117-123. https://doi.org/10.1038/ncb2407.
    • (2012) Nat Cell Biol , vol.14 , pp. 117-123
    • Meyer, H.1    Bug, M.2    Bremer, S.3
  • 28
    • 84963617847 scopus 로고    scopus 로고
    • Structure and function of the AAA+ ATPase p97/Cdc48p
    • Xia D, Tang WK, Ye Y. 2016. Structure and function of the AAA+ ATPase p97/Cdc48p. Gene 583:64-77. https://doi.org/10.1016/j.gene.2016.02.042.
    • (2016) Gene , vol.583 , pp. 64-77
    • Xia, D.1    Tang, W.K.2    Ye, Y.3
  • 29
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. 2001. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107:667-677. https://doi.org/10.1016/S0092-8674(01)00595-5.
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 30
    • 77952533111 scopus 로고    scopus 로고
    • VCP/p97 is essential for maturation of ubiquitincontaining autophagosomes and this function is impaired by mutations that cause IBMPFD
    • Tresse E, Salomons FA, Vesa J, Bott LC, Kimonis V, Yao TP, Dantuma NP, Taylor JP. 2010. VCP/p97 is essential for maturation of ubiquitincontaining autophagosomes and this function is impaired by mutations that cause IBMPFD. Autophagy 6:217-227. https://doi.org/10.4161/auto.6.2.11014.
    • (2010) Autophagy , vol.6 , pp. 217-227
    • Tresse, E.1    Salomons, F.A.2    Vesa, J.3    Bott, L.C.4    Kimonis, V.5    Yao, T.P.6    Dantuma, N.P.7    Taylor, J.P.8
  • 31
    • 84896393480 scopus 로고    scopus 로고
    • Ubiquitin signals proteolysisindependent stripping of transcription factors
    • Ndoja A, Cohen RE, Yao T. 2014. Ubiquitin signals proteolysisindependent stripping of transcription factors. Mol Cell 53:893-903. https://doi.org/10.1016/j.molcel.2014.02.002.
    • (2014) Mol Cell , vol.53 , pp. 893-903
    • Ndoja, A.1    Cohen, R.E.2    Yao, T.3
  • 32
    • 84904990897 scopus 로고    scopus 로고
    • Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97
    • Sha Z, Goldberg AL. 2014. Proteasome-mediated processing of Nrf1 is essential for coordinate induction of all proteasome subunits and p97. Curr Biol 24:1573-1583. https://doi.org/10.1016/j.cub.2014.06.004.
    • (2014) Curr Biol , vol.24 , pp. 1573-1583
    • Sha, Z.1    Goldberg, A.L.2
  • 33
    • 84939170347 scopus 로고    scopus 로고
    • The transitional endoplasmic reticulum ATPase p97 regulates the alternative nuclear factor NF-kappaB signaling via partial degradation of the NF-kappaB subunit p100
    • Zhang Z, Wang Y, Li C, Shi Z, Hao Q, Wang W, Song X, Zhao Y, Jiao S, Zhou Z. 2015. The transitional endoplasmic reticulum ATPase p97 regulates the alternative nuclear factor NF-kappaB signaling via partial degradation of the NF-kappaB subunit p100. J Biol Chem 290: 19558-19568. https://doi.org/10.1074/jbc.M114.630061.
    • (2015) J Biol Chem , vol.290 , pp. 19558-19568
    • Zhang, Z.1    Wang, Y.2    Li, C.3    Shi, Z.4    Hao, Q.5    Wang, W.6    Song, X.7    Zhao, Y.8    Jiao, S.9    Zhou, Z.10
  • 36
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H, Rape M, Braun S, Rumpf S, Hoege C, Jentsch S. 2005. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120:73-84. https://doi.org/10.1016/j.cell.2004.11.013.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 37
    • 84860120476 scopus 로고    scopus 로고
    • UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation
    • Bandau S, Knebel A, Gage ZO, Wood NT, Alexandru G. 2012. UBXN7 docks on neddylated cullin complexes using its UIM motif and causes HIF1alpha accumulation. BMC Biol 10:36. https://doi.org/10.1186/1741-7007-10-36.
    • (2012) BMC Biol , vol.10 , pp. 36
    • Bandau, S.1    Knebel, A.2    Gage, Z.O.3    Wood, N.T.4    Alexandru, G.5
  • 38
    • 84860773994 scopus 로고    scopus 로고
    • NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway
    • den Besten W, Verma R, Kleiger G, Oania RS, Deshaies RJ. 2012. NEDD8 links cullin-RING ubiquitin ligase function to the p97 pathway. Nat Struct Mol Biol 19:511-516. https://doi.org/10.1038/nsmb.2269.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 511-516
    • den Besten, W.1    Verma, R.2    Kleiger, G.3    Oania, R.S.4    Deshaies, R.J.5
  • 39
    • 31544441350 scopus 로고    scopus 로고
    • Redox-sensitive transcription factors as prime targets for chemoprevention with anti-inflammatory and antioxidative phytochemicals
    • Surh YJ, Kundu JK, Na HK, Lee JS. 2005. Redox-sensitive transcription factors as prime targets for chemoprevention with anti-inflammatory and antioxidative phytochemicals. J Nutr 135:2993S-3001S.
    • (2005) J Nutr , vol.135 , pp. 2993S-3001S
    • Surh, Y.J.1    Kundu, J.K.2    Na, H.K.3    Lee, J.S.4
  • 40
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • Kensler TW, Wakabayashi N, Biswal S. 2007. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol 47:89-116. https://doi.org/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
  • 41
    • 84874459340 scopus 로고    scopus 로고
    • A perspective on dietary phytochemicals and cancer chemoprevention: oxidative stress, nrf2, and epigenomics
    • Su ZY, Shu L, Khor TO, Lee JH, Fuentes F, Kong AN. 2013. A perspective on dietary phytochemicals and cancer chemoprevention: oxidative stress, nrf2, and epigenomics. Top Curr Chem 329:133-162. https://doi.org/10.1007/128_2012_340.
    • (2013) Top Curr Chem , vol.329 , pp. 133-162
    • Su, Z.Y.1    Shu, L.2    Khor, T.O.3    Lee, J.H.4    Fuentes, F.5    Kong, A.N.6
  • 43
    • 84885944468 scopus 로고    scopus 로고
    • The emerging role of the Nrf2-Keap1 signaling pathway in cancer
    • Jaramillo MC, Zhang DD. 2013. The emerging role of the Nrf2-Keap1 signaling pathway in cancer. Genes Dev 27:2179-2191. https://doi.org/10.1101/gad.225680.113.
    • (2013) Genes Dev , vol.27 , pp. 2179-2191
    • Jaramillo, M.C.1    Zhang, D.D.2
  • 45
    • 79952122321 scopus 로고    scopus 로고
    • Brusatol enhances the efficacy of chemotherapy by inhibiting the Nrf2-mediated defense mechanism
    • Ren D, Villeneuve NF, Jiang T, Wu T, Lau A, Toppin HA, Zhang DD. 2011. Brusatol enhances the efficacy of chemotherapy by inhibiting the Nrf2-mediated defense mechanism. Proc Natl Acad Sci U S A 108:1433-1438. https://doi.org/10.1073/pnas.1014275108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1433-1438
    • Ren, D.1    Villeneuve, N.F.2    Jiang, T.3    Wu, T.4    Lau, A.5    Toppin, H.A.6    Zhang, D.D.7
  • 46
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase
    • Ye Y. 2006. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J Struct Biol 156:29-40. https://doi.org/10.1016/j.jsb.2006.01.005.
    • (2006) J Struct Biol , vol.156 , pp. 29-40
    • Ye, Y.1
  • 47
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru G, Graumann J, Smith GT, Kolawa NJ, Fang R, Deshaies RJ. 2008 UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134:804-816. https://doi.org/10.1016/j.cell.2008.06.048.
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 48
    • 79952256187 scopus 로고    scopus 로고
    • SCF/β-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner
    • Rada P, Rojo AI, Chowdhry S, McMahon M, Hayes JD, Cuadrado A. 2011. SCF/β-TrCP promotes glycogen synthase kinase 3-dependent degradation of the Nrf2 transcription factor in a Keap1-independent manner. Mol Cell Biol 31:1121-1133. https://doi.org/10.1128/MCB.01204-10.
    • (2011) Mol Cell Biol , vol.31 , pp. 1121-1133
    • Rada, P.1    Rojo, A.I.2    Chowdhry, S.3    McMahon, M.4    Hayes, J.D.5    Cuadrado, A.6
  • 49
    • 84881476323 scopus 로고    scopus 로고
    • Nrf2 is controlled by two distinct beta-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity
    • Chowdhry S, Zhang Y, McMahon M, Sutherland C, Cuadrado A, Hayes JD. 2013 Nrf2 is controlled by two distinct beta-TrCP recognition motifs in its Neh6 domain, one of which can be modulated by GSK-3 activity. Oncogene 32:3765-3781. https://doi.org/10.1038/onc.2012.388.
    • (2013) Oncogene , vol.32 , pp. 3765-3781
    • Chowdhry, S.1    Zhang, Y.2    McMahon, M.3    Sutherland, C.4    Cuadrado, A.5    Hayes, J.D.6
  • 51
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, Pestronk A, Whyte MP, Kimonis VE. 2004. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 36:377-381. https://doi.org/10.1038/ng1332.
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6    Pestronk, A.7    Whyte, M.P.8    Kimonis, V.E.9
  • 52
    • 79951625225 scopus 로고    scopus 로고
    • The complexities of p97 function in health and disease
    • Chapman E, Fry AN, Kang M. 2011. The complexities of p97 function in health and disease. Mol Biosyst 7:700-710. https://doi.org/10.1039/C0MB00176G.
    • (2011) Mol Biosyst , vol.7 , pp. 700-710
    • Chapman, E.1    Fry, A.N.2    Kang, M.3
  • 53
    • 84969944644 scopus 로고    scopus 로고
    • Proteasome inhibitor-adapted myeloma cells are largely independent from proteasome activity and show complex proteomic changes, in particular in redox and energy metabolism
    • Soriano GP, Besse L, Li N, Kraus M, Besse A, Meeuwenoord N, Bader J, Everts B, den Dulk H, Overkleeft HS, Florea BI, Driessen C. 2016. Proteasome inhibitor-adapted myeloma cells are largely independent from proteasome activity and show complex proteomic changes, in particular in redox and energy metabolism. Leukemia 30:2198-2207. https://doi.org/10.1038/leu.2016.102.
    • (2016) Leukemia , vol.30 , pp. 2198-2207
    • Soriano, G.P.1    Besse, L.2    Li, N.3    Kraus, M.4    Besse, A.5    Meeuwenoord, N.6    Bader, J.7    Everts, B.8    den Dulk, H.9    Overkleeft, H.S.10    Florea, B.I.11    Driessen, C.12
  • 54
    • 84927610137 scopus 로고    scopus 로고
    • Regulation of the expression of renal drug transporters in KEAP1-knockdown human tubular cells
    • Jeong HS, Ryoo IG, Kwak MK. 2015. Regulation of the expression of renal drug transporters in KEAP1-knockdown human tubular cells. Toxicol In Vitro 29:884-892. https://doi.org/10.1016/j.tiv.2015.03.013.
    • (2015) Toxicol In Vitro , vol.29 , pp. 884-892
    • Jeong, H.S.1    Ryoo, I.G.2    Kwak, M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.