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Volumn 3, Issue , 2013, Pages

The membrane-topogenic vectorial behaviour of Nrf1 controls its post-translational modification and transactivation activity

Author keywords

[No Author keywords available]

Indexed keywords

NRF1 PROTEIN, MOUSE; NUCLEAR RESPIRATORY FACTOR 1;

EID: 84879628924     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep02006     Document Type: Article
Times cited : (39)

References (78)
  • 1
    • 77953012548 scopus 로고    scopus 로고
    • Stress-activated cap'n'collar transcription factors in aging and human disease
    • Sykiotis, G. P.& Bohmann, D. Stress-activated cap'n'collar transcription factors in aging and human disease. Sci. Signal. 3, re3 (2010).
    • (2010) Sci. Signal , vol.3
    • Sykiotis, G.P.1    Bohmann, D.2
  • 3
    • 0028795364 scopus 로고
    • Control of drosophila head segment identity by the bZIP homeotic gene cnc
    • Mohler, J., Mahaffey, J. W., Deutsch, E. & Vani, K. Control of Drosophila head segment identity by the bZIP homeotic gene cnc. Development 121, 237-47 (1995).
    • (1995) Development , vol.121 , pp. 237-247
    • Mohler, J.1    Mahaffey, J.W.2    Deutsch, E.3    Vani, K.4
  • 4
    • 0025868833 scopus 로고
    • Segmentally restricted, cephalic expression of a leucine zipper gene during Drosophila embryogenesis
    • Mohler, J., Vani, K., Leung, S. & Epstein, A. Segmentally restricted, cephalic expression of a leucine zipper gene during Drosophila embryogenesis. Mech. Dev. 34, 3-9 (1991).
    • (1991) Mech. Dev , vol.34 , pp. 3-9
    • Mohler, J.1    Vani, K.2    Leung, S.3    Epstein, A.4
  • 5
    • 0027209420 scopus 로고
    • The maternal gene skn-1 encodes a protein that is distributed unequally in early C. elegans embryos
    • Bowerman, B., Draper, B. W.,Mello, C. C. & Priess, J. R. The maternal gene skn-1 encodes a protein that is distributed unequally in early C. elegans embryos. Cell 74, 443-52 (1993). (Pubitemid 23244610)
    • (1993) Cell , vol.74 , Issue.3 , pp. 443-452
    • Bowerman, B.1    Draper, B.W.2    Mello, C.C.3    Priess, J.R.4
  • 6
    • 0026529831 scopus 로고
    • Skn-1 a maternally expressed gene required to specify the fate of ventral blastomeres in the early C. elegans embryo
    • Bowerman, B., Eaton, B. A. & Priess, J. R. Skn-1, a maternally expressed gene required to specify the fate of ventral blastomeres in the early C. elegans embryo. Cell 68, 1061-75 (1992).
    • (1992) Cell , vol.68 , pp. 1061-1075
    • Bowerman, B.1    Eaton, B.A.2    Priess, J.R.3
  • 7
    • 0027243681 scopus 로고
    • Erythroid transcription factor NF-E2 is a haematopoietic-specific basic-leucine zipper protein
    • DOI 10.1038/362722a0
    • Andrews, N. C., Erdjument-Bromage, H., Davidson, M. B., Tempst, P. & Orkin, S. H. Erythroid transcription factor NF-E2 is a haematopoietic-specific basicleucine zipper protein. Nature 362, 722-8 (1993). (Pubitemid 23125974)
    • (1993) Nature , vol.362 , Issue.6422 , pp. 722-728
    • Andrews, N.C.1    Erdjument-Bromage, H.2    Davidson, M.B.3    Tempst, P.4    Orkin, S.H.5
  • 9
    • 0028118492 scopus 로고
    • Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins
    • DOI 10.1038/367568a0
    • Igarashi, K. et al. Regulation of transcription by dimerization of erythroid factor NF-E2 p45 with small Maf proteins. Nature 367, 568-72 (1994). (Pubitemid 24055517)
    • (1994) Nature , vol.367 , Issue.6463 , pp. 568-572
    • Igarashi, K.1    Kataoka, K.2    Itoh, K.3    Hayashi, N.4    Nishizawa, M.5    Yamamoto, M.6
  • 12
    • 0029077801 scopus 로고
    • Structural organization and mapping of the human TCF11 gene
    • Luna, L. et al. Structural organization and mapping of the human TCF11 gene. Genomics 27, 237-44 (1995).
    • (1995) Genomics , vol.27 , pp. 237-244
    • Luna, L.1
  • 13
    • 0030995597 scopus 로고    scopus 로고
    • The bZIP transcription factor LCR-F1 is essential for mesoderm formation in mouse development
    • Farmer, S. C., Sun, C. W.,Winnier, G. E., Hogan, B. L. & Townes, T. M. The bZIP transcription factor LCR-F1 is essential for mesoderm formation in mouse development. Genes Dev. 11, 786-98 (1997). (Pubitemid 27157723)
    • (1997) Genes and Development , vol.11 , Issue.6 , pp. 786-798
    • Farmer, S.C.1    Sun, C.-W.2    Winnier, G.E.3    Hogan, B.L.M.4    Townes, T.M.5
  • 14
    • 0028247214 scopus 로고
    • Cloning and functional characterization of LCR-F1: A bZIP transcription factor that activates erythroid-specific, human globin gene expression
    • Caterina, J. J., Donze, D., Sun, C.W., Ciavatta, D. J. & Townes, T. M. Cloning and functional characterization of LCR-F1: a bZIP transcription factor that activates erythroid-specific, human globin gene expression. Nucleic Acids Res. 22, 2383-91 (1994). (Pubitemid 24209550)
    • (1994) Nucleic Acids Research , vol.22 , Issue.12 , pp. 2383-2391
    • Caterina, J.J.1    Donze, D.2    Sun, C.-W.3    Ciavatta, D.J.4    Townes, T.M.5
  • 15
    • 0028061444 scopus 로고
    • Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the β-globin locus control region
    • DOI 10.1073/pnas.91.21.9926
    • Moi, P., Chan, K., Asunis, I., Cao, A. & Kan, Y. W. Isolation of NF-E2-related factor 2 (Nrf2), a NF-E2-like basic leucine zipper transcriptional activator that binds to the tandem NF-E2/AP1 repeat of the beta-globin locus control region. Proc. Natl. Acad. Sci. USA 91, 9926-30 (1994). (Pubitemid 24311921)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.21 , pp. 9926-9930
    • Moi, P.1    Chan, K.2    Asunis, I.3    Cao, A.4    Kan, Y.W.5
  • 18
    • 2642683201 scopus 로고    scopus 로고
    • Isolation of the human BACH1 transcription regulator gene, which maps to chromosome 21q22.1
    • Blouin, J. L. et al. Isolation of the human BACH1 transcription regulator gene, which maps to chromosome 21q22.1. Hum. Genet. 102, 282-8 (1998).
    • (1998) Hum. Genet , vol.102 , pp. 282-288
    • Blouin, J.L.1
  • 19
    • 0032518256 scopus 로고    scopus 로고
    • Characterization of a human homolog (BACH1) of the mouse Bach1 gene encoding a BTB-basic leucine zipper transcription factor and its mapping to chromosome 21q22.1
    • DOI 10.1006/geno.1997.5080
    • Ohira, M. et al. Characterization of a human homolog (BACH1) of the mouse Bach1 gene encoding a BTB-basic leucine zipper transcription factor and its mapping to chromosome 21q22.1. Genomics 47, 300-6 (1998). (Pubitemid 28086856)
    • (1998) Genomics , vol.47 , Issue.2 , pp. 300-306
    • Ohira, M.1    Seki, N.2    Nagase, T.3    Ishikawa, K.-I.4    Nomura, N.5    Ohara, O.6
  • 22
    • 77957341511 scopus 로고    scopus 로고
    • Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop
    • Steffen, J., Seeger, M., Koch, A. & Kruger, E. Proteasomal degradation is transcriptionally controlled by TCF11 via an ERAD-dependent feedback loop. Mol. Cell 40, 147-58 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 147-158
    • Steffen, J.1    Seeger, M.2    Koch, A.3    Kruger, E.4
  • 23
    • 77950366349 scopus 로고    scopus 로고
    • Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells
    • Radhakrishnan, S. K. et al. Transcription factor Nrf1 mediates the proteasome recovery pathway after proteasome inhibition in mammalian cells. Mol. Cell 38, 17-28 (2010).
    • (2010) Mol. Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1
  • 24
    • 79251559085 scopus 로고    scopus 로고
    • Basic leucine zipper protein Cnc-C is a substrate and transcriptional regulator of the Drosophila 26S proteasome
    • Grimberg, K. B., Beskow, A., Lundin, D., Davis, M. M. & Young, P. Basic leucine zipper protein Cnc-C is a substrate and transcriptional regulator of the Drosophila 26S proteasome. Mol. Cell Biol. 31, 897-909 (2011).
    • (2011) Mol. Cell Biol , vol.31 , pp. 897-909
    • Grimberg, K.B.1    Beskow, A.2    Lundin, D.3    Davis, M.M.4    Young, P.5
  • 25
    • 79959823394 scopus 로고    scopus 로고
    • Specific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activity
    • Li, X. et al. Specific SKN-1/Nrf stress responses to perturbations in translation elongation and proteasome activity. PLoS Genet. 7, e1002119 (2011).
    • (2011) PLoS Genet , vol.7
    • Li, X.1
  • 26
    • 0032536783 scopus 로고    scopus 로고
    • Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice
    • DOI 10.1093/emboj/17.6.1779
    • Chan, J. Y. et al. Targeted disruption of the ubiquitous CNC-bZIP transcription factor, Nrf-1, results in anemia and embryonic lethality in mice. EMBO J. 17, 1779-87 (1998). (Pubitemid 28119131)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1779-1787
    • Chan, J.Y.1    Kwong, M.2    Lu, R.3    Chang, J.4    Wang, B.5    Yen, T.S.B.6    Kan, Y.W.7
  • 29
    • 57749120460 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes
    • Ohtsuji, M. et al. Nrf1 and Nrf2 play distinct roles in activation of antioxidant response element-dependent genes. J. Biol. Chem. 283, 33554-62 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 33554-33562
    • Ohtsuji, M.1
  • 30
    • 73949149483 scopus 로고    scopus 로고
    • Targeted disruption of nuclear factor erythroid-derived 2-like 1 in osteoblasts reduces bone size and bone formation in mice
    • Kim, J., Xing, W., Wergedal, J., Chan, J. Y. & Mohan, S. Targeted disruption of nuclear factor erythroid-derived 2-like 1 in osteoblasts reduces bone size and bone formation in mice. Physiol. Genomics 40, 100-10 (2010).
    • (2010) Physiol. Genomics , vol.40 , pp. 100-110
    • Kim, J.1    Xing, W.2    Wergedal, J.3    Chan, J.Y.4    Mohan, S.5
  • 31
    • 79956293008 scopus 로고    scopus 로고
    • Central nervous system-specific deletion of transcription factor Nrf1 causes progressive motor neuronal dysfunction
    • Kobayashi, A. et al. Central nervous system-specific deletion of transcription factor Nrf1 causes progressive motor neuronal dysfunction. Genes Cells 16, 692-703 (2011).
    • (2011) Genes Cells , vol.16 , pp. 692-703
    • Kobayashi, A.1
  • 32
    • 79957676924 scopus 로고    scopus 로고
    • Loss of nuclear factor E2-related factor 1 in the brain leads to dysregulation of proteasome gene expression and neurodegeneration
    • Lee, C. S. et al. Loss of nuclear factor E2-related factor 1 in the brain leads to dysregulation of proteasome gene expression and neurodegeneration. Proc. Natl. Acad. Sci. USA 108, 8408-13 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 8408-8413
    • Lee, C.S.1
  • 33
    • 0030451213 scopus 로고    scopus 로고
    • NRF2, a member of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development
    • DOI 10.1073/pnas.93.24.13943
    • Chan, K., Lu, R., Chang, J. C. & Kan, Y. W. NRF2, amember of the NFE2 family of transcription factors, is not essential for murine erythropoiesis, growth, and development. Proc. Natl. Acad. Sci. USA 93, 13943-8 (1996). (Pubitemid 26424225)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.24 , pp. 13943-13948
    • Chan, K.1    Lu, R.2    Chang, J.C.3    Kan, Y.W.4
  • 34
    • 0033616129 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: A complex multisubunit enzyme of the endoplasmic reticulum
    • DOI 10.1006/bbrc.1999.1886
    • Yan, Q. & Lennarz, W. J. Oligosaccharyltransferase: a complex multisubunit enzyme of the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 266, 684-9 (1999). (Pubitemid 30042493)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.3 , pp. 684-689
    • Yan, Q.1    Lennarz, W.J.2
  • 35
    • 17644366824 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
    • DOI 10.1021/bi047328f
    • Shibatani, T., David, L. L., McCormack, A. L., Frueh, K. & Skach,W. R. Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry 44, 5982-92 (2005). (Pubitemid 40570692)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 5982-5992
    • Shibatani, T.1    David, L.L.2    McCormack, A.L.3    Frueh, K.4    Skach, W.R.5
  • 36
    • 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
    • DOI 10.1042/BJ20060725
    • Zhang, Y., Crouch, D. H., Yamamoto, M. & Hayes, J. D. 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, 373-85 (2006). (Pubitemid 44672628)
    • (2006) Biochemical Journal , vol.399 , Issue.3 , pp. 373-385
    • Zhang, Y.1    Crouch, D.H.2    Yamamoto, M.3    Hayes, J.D.4
  • 37
    • 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
    • DOI 10.1074/jbc.M602802200
    • Wang, W. & Chan, J. Y. 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, 19676-87 (2006). (Pubitemid 44035470)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 38
    • 36749013169 scopus 로고    scopus 로고
    • The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation
    • DOI 10.1042/BJ20070761
    • Zhang, Y., Lucocq, J. M., Yamamoto, M. & Hayes, J. D. The NHB1 (N-terminal homology box 1) sequence in transcription factor Nrf1 is required to anchor it to the endoplasmic reticulum and also to enable its asparagine-glycosylation. Biochem. J. 408, 161-72 (2007). (Pubitemid 350206339)
    • (2007) Biochemical Journal , vol.408 , Issue.2 , pp. 161-172
    • Zhang, Y.1    Lucocq, J.M.2    Yamamoto, M.3    Hayes, J.D.4
  • 39
    • 61449180332 scopus 로고    scopus 로고
    • The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors
    • Zhang, Y., Lucocq, J. M. & Hayes, J. D. The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors. Biochem. J. 418, 293-310 (2009).
    • (2009) Biochem. J , vol.418 , pp. 293-310
    • Zhang, Y.1    Lucocq, J.M.2    Hayes, J.D.3
  • 40
    • 77956661152 scopus 로고    scopus 로고
    • Identification of topological determinants in the Nterminal domain of transcription factor Nrf1 that control its orientation in the endoplasmic reticulum membrane
    • Zhang, Y. & Hayes, J. D. Identification of topological determinants in the Nterminal domain of transcription factor Nrf1 that control its orientation in the endoplasmic reticulum membrane. Biochem. J. 430, 497-510 (2010).
    • (2010) Biochem. J , vol.430 , pp. 497-510
    • Zhang, Y.1    Hayes, J.D.2
  • 41
    • 59149089827 scopus 로고    scopus 로고
    • The Nrf3 transcription factor is a membrane-bound glycoprotein targeted to the endoplasmic reticulum through its N-terminal homology box 1 sequence
    • Zhang, Y., Kobayashi, A., Yamamoto, M. & Hayes, J. D. The Nrf3 transcription factor is a membrane-bound glycoprotein targeted to the endoplasmic reticulum through its N-terminal homology box 1 sequence. J. Biol. Chem. 284, 3195-210 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 3195-3210
    • Zhang, Y.1    Kobayashi, A.2    Yamamoto, M.3    Hayes, J.D.4
  • 42
    • 77956040144 scopus 로고    scopus 로고
    • Taurine reduces ER stress in C. elegans
    • Kim, H. M., Do, C. H. & Lee, D. H. Taurine reduces ER stress in C. elegans. J. Biomed. Sci. 17 Suppl 1, S26 (2010).
    • (2010) J. Biomed. Sci. , vol.17 , Issue.SUPPL. 1
    • Kim, H.M.1    Do, C.H.2    Lee, D.H.3
  • 43
    • 0030066709 scopus 로고    scopus 로고
    • Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis
    • DOI 10.1016/0021-9673(95)00502-1
    • O'Neill, R. A. Enzymatic release of oligosaccharides from glycoproteins for chromatographic and electrophoretic analysis. J. Chromatogr. A 720, 201-15 (1996). (Pubitemid 26037616)
    • (1996) Journal of Chromatography A , vol.720 , Issue.1-2 , pp. 201-215
    • O'Neill, R.A.1
  • 44
    • 0034057802 scopus 로고    scopus 로고
    • Membrane topology and insertion of membrane proteins: Search for topogenic signals
    • van Geest, M. & Lolkema, J. S. Membrane topology and insertion of membrane proteins: search for topogenic signals. Microbiol. Mol. Biol. Rev. 64, 13-33 (2000). (Pubitemid 30143838)
    • (2000) Microbiology and Molecular Biology Reviews , vol.64 , Issue.1 , pp. 13-33
    • Van Geest, M.1    Lolkema, J.S.2
  • 45
    • 84858698775 scopus 로고    scopus 로고
    • Induction of apoptosis by ribosome inactivating proteins: Importance of N-glycosidase activity
    • Das, M. K., Sharma, R. S. & Mishra, V. Induction of apoptosis by ribosome inactivating proteins: importance of N-glycosidase activity. Appl. Biochem. Biotechnol. 166, 1552-61 (2012).
    • (2012) Appl. Biochem. Biotechnol , vol.166 , pp. 1552-1561
    • Das, M.K.1    Sharma, R.S.2    Mishra, V.3
  • 46
    • 0026102843 scopus 로고
    • The structure and action of ricin, a cytotoxic N-glycosidase
    • Robertus, J. The structure and action of ricin, a cytotoxic N-glycosidase. Semin. Cell Biol. 2, 23-30 (1991).
    • (1991) Semin. Cell Biol , vol.2 , pp. 23-30
    • Robertus, J.1
  • 48
    • 83255185776 scopus 로고    scopus 로고
    • Dual Regulation of the Transcriptional Activity of Nrf1 by b-TrCP-and Hrd1-Dependent Degradation Mechanisms
    • Tsuchiya, Y. et al. Dual Regulation of the Transcriptional Activity of Nrf1 by b-TrCP-and Hrd1-Dependent Degradation Mechanisms. Mol. Cell Biol. 31, 4500-12 (2011).
    • (2011) Mol. Cell Biol , vol.31 , pp. 4500-4512
    • Tsuchiya, Y.1
  • 49
    • 80655128139 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor regulates nuclear factor E2 related factor 1 (Nrf1) transcription factor turnover through proteasome-mediated proteolysis
    • Biswas, M., Phan, D., Watanabe, M. & Chan, J. Y. The Fbw7 tumor suppressor regulates nuclear factor E2 related factor 1 (Nrf1) transcription factor turnover through proteasome-mediated proteolysis. J. Biol. Chem. 286, 39282-39289 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 39282-39289
    • Biswas, M.1    Phan, D.2    Watanabe, M.3    Chan, J.Y.4
  • 51
    • 0032403191 scopus 로고    scopus 로고
    • Nrf1 in a complex with fosB, c-jun, junD and ATF2 forms the AP1 component at the TNFα promoter in stimulated mast cells
    • Novotny, V., Prieschl, E. E., Csonga, R., Fabjani, G. & Baumruker, T. Nrf1 in a complex with fosB, c-jun, junD and ATF2 forms the AP1 component at the TNFa promoter in stimulated mast cells. Nucleic Acids Res. 26, 5480-5 (1998). (Pubitemid 28542751)
    • (1998) Nucleic Acids Research , vol.26 , Issue.23 , pp. 5480-5485
    • Novotny, V.1    Prieschl, E.E.2    Csonga, R.3    Fabjani, G.4    Baumruker, T.5
  • 53
    • 0032518185 scopus 로고    scopus 로고
    • Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG: Binding-site selection and regulation of transcription
    • DOI 10.1093/nar/26.2.512
    • Johnsen, O., Murphy, P., Prydz, H. & Kolsto, A. B. Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG: binding-site selection and regulation of transcription. Nucleic Acids Res. 26, 512-20 (1998). (Pubitemid 28291577)
    • (1998) Nucleic Acids Research , vol.26 , Issue.2 , pp. 512-520
    • Johnsen, O.1    Murphy, P.2    Prydz, H.3    Kolsto, A.-B.4
  • 54
    • 0031749528 scopus 로고    scopus 로고
    • A new DNA-binding motif in the Skn-1 binding domain-DNA complex
    • DOI 10.1038/nsb0698-484
    • Rupert, P. B., Daughdrill, G. W., Bowerman, B. & Matthews, B. W. A new DNA-binding motif in the Skn-1 binding domain-DNA complex. Nat. Struct. Biol. 5, 484-91 (1998). (Pubitemid 28265032)
    • (1998) Nature Structural Biology , vol.5 , Issue.6 , pp. 484-491
    • Rupert, P.B.1    Daughdrill, G.W.2    Bowerman, B.3    Matthews, B.W.4
  • 55
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanaseto probe its role in glycoprotein turnover
    • DOI 10.1016/j.chembiol.2004.11.010, PII S1074552104003345
    • Misaghi, S., Pacold, M. E., Blom, D., Ploegh, H. L. & Korbel, G. A. Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem. Biol. 11, 1677-87 (2004). (Pubitemid 39651302)
    • (2004) Chemistry and Biology , vol.11 , Issue.12 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 56
    • 0032727707 scopus 로고    scopus 로고
    • Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon
    • Goder, V., Bieri, C. & Spiess, M. Glycosylation can influence topogenesis of membrane proteins and reveals dynamic reorientation of nascent polypeptides within the translocon. J. Cell Biol. 147, 257-66 (1999).
    • (1999) J. Cell Biol , vol.147 , pp. 257-266
    • Goder, V.1    Bieri, C.2    Spiess, M.3
  • 57
    • 83755229096 scopus 로고    scopus 로고
    • The Nrf1 CNC-bZIP protein is regulated by the proteasome and activated by hypoxia
    • Chepelev, N. L., Bennitz, J. D.,Huang, T.,McBride, S.& Willmore, W. G. The Nrf1 CNC-bZIP protein is regulated by the proteasome and activated by hypoxia. PLoS One 6, e29167 (2011).
    • (2011) PLoS One , vol.6
    • Chepelev, N.L.1    Bennitz, J.D.2    Huang, T.3    McBride, S.4    Willmore, W.G.5
  • 59
    • 0035947639 scopus 로고    scopus 로고
    • Two domains of the human bZIP transcription factor TCF11 are necessary for transactivation
    • Husberg, C., Murphy, P., Martin, E. & Kolsto, A. B. Two domains of the human bZIP transcription factor TCF11 are necessary for transactivation. J. Biol. Chem. 276, 17641-52 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 17641-17652
    • Husberg, C.1    Murphy, P.2    Martin, E.3    Kolsto, A.B.4
  • 60
    • 67650069254 scopus 로고    scopus 로고
    • Interaction and conformational dynamics of membrane-spanning protein helices
    • Langosch, D. & Arkin, I. T. Interaction and conformational dynamics of membrane-spanning protein helices. Protein Sci. 18, 1343-58 (2009).
    • (2009) Protein Sci , vol.18 , pp. 1343-1358
    • Langosch, D.1    Arkin, I.T.2
  • 61
    • 34548337281 scopus 로고    scopus 로고
    • The p65 isoform of Nrf1 is a dominant negative inhibitor of ARE-mediated transcription
    • DOI 10.1074/jbc.M700159200
    • Wang, W., Kwok, A. M. & Chan, J. Y. The p65 isoform of Nrf1 is a dominant negative inhibitor of ARE-mediated transcription. J. Biol. Chem. 282, 24670-8 (2007). (Pubitemid 47347500)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24670-24678
    • Wang, W.1    Kwok, A.M.2    Chan, J.Y.3
  • 62
    • 77952952816 scopus 로고    scopus 로고
    • Enhanced expression of Nrf2 in mice attenuates the fatty liver produced by a methionine-and cholinedeficient diet
    • Zhang, Y. K., Yeager, R. L., Tanaka, Y. & Klaassen, C. D. Enhanced expression of Nrf2 in mice attenuates the fatty liver produced by a methionine-and cholinedeficient diet. Toxicol. Appl. Pharmacol. 245, 326-34 (2010).
    • (2010) Toxicol. Appl. Pharmacol , vol.245 , pp. 326-334
    • Zhang, Y.K.1    Yeager, R.L.2    Tanaka, Y.3    Klaassen, C.D.4
  • 63
    • 33646357780 scopus 로고    scopus 로고
    • Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization
    • Lorenz, H., Hailey, D. W. & Lippincott-Schwartz, J. Fluorescence protease protection of GFP chimeras to reveal protein topology and subcellular localization. Nat. Methods 3, 205-210 (2006).
    • (2006) Nat. Methods , vol.3 , pp. 205-210
    • Lorenz, H.1    Hailey, D.W.2    Lippincott-Schwartz, J.3
  • 64
    • 34250663574 scopus 로고    scopus 로고
    • The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology
    • Lorenz, H., Hailey, D. W.,Wunder, C. & Lippincott-Schwartz, J. The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology. Nat. Protoc. 1, 276-279 (2006).
    • (2006) Nat. Protoc , vol.1 , pp. 276-279
    • Lorenz, H.1    Hailey, D.W.2    Wunder, C.3    Lippincott-Schwartz, J.4
  • 66
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B. & Goldstein, J. L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-8 (2000).
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 67
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • DOI 10.1126/science.1096187
    • Wolfe, M. S. & Kopan, R. Intramembrane proteolysis: theme and variations. Science 305, 1119-23 (2004). (Pubitemid 39100316)
    • (2004) Science , vol.305 , Issue.5687 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2
  • 68
    • 33845343261 scopus 로고    scopus 로고
    • Membrane-protein topology
    • DOI 10.1038/nrm2063, PII NRM2063
    • von Heijne, G. Membrane-protein topology. Nat. Rev. Mol. Cell Biol. 7, 909-18 (2006). (Pubitemid 44871417)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.12 , pp. 909-918
    • Von Heijne, G.1
  • 69
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan, W. & Bogdanov, M. Lipid-dependent membrane protein topogenesis. Annu. Rev. Biochem. 78, 515-40 (2009).
    • (2009) Annu. Rev. Biochem , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 70
    • 66849131417 scopus 로고    scopus 로고
    • Cellular mechanisms ofmembrane protein folding
    • Skach,W. R. Cellular mechanisms ofmembrane protein folding. Nat. Struct. Mol. Biol. 16, 606-12 (2009).
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 606-612
    • Skach, W.R.1
  • 71
    • 14644393694 scopus 로고    scopus 로고
    • Lipid traffic: Floppy drives and a superhighway
    • DOI 10.1038/nrm1591
    • Holthuis, J. C. & Levine, T. P. Lipid traffic: floppy drives and a superhighway. Nat. Rev. Mol. Cell Biol. 6, 209-20 (2005). (Pubitemid 40314922)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 209-220
    • Holthuis, J.C.M.1    Levine, T.P.2
  • 72
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. & Simons, K. Lipid rafts as a membrane-organizing principle. Science 327, 46-50 (2010).
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 73
    • 33845297317 scopus 로고    scopus 로고
    • Generation of a stable antioxidant response element-driven reporter gene cell line and its use to show redox-dependent activation of Nrf2 by cancer chemotherapeutic agents
    • DOI 10.1158/0008-5472.CAN-06-2298
    • Wang, X. J., Hayes, J. D. & Wolf, C. R. Generation of a stable antioxidant response element-driven reporter gene cell line and its use to show redox-dependent activation of Nrf2 by cancer chemotherapeutic agents. Cancer Res. 66, 10983-94 (2006). (Pubitemid 44876998)
    • (2006) Cancer Research , vol.66 , Issue.22 , pp. 10983-10994
    • Xiu, J.W.1    Hayes, J.D.2    Wolf, C.R.3
  • 74
    • 35949003194 scopus 로고    scopus 로고
    • Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stress-regulated intramembrane proteolysis
    • DOI 10.1111/j.1600-0854.2007.00654.x
    • Bailey, D., Barreca, C. & O'Hare, P. Trafficking of the bZIP transmembrane transcription factor CREB-H into alternate pathways of ERAD and stressregulated intramembrane proteolysis. Traffic 8, 1796-814 (2007). (Pubitemid 350066690)
    • (2007) Traffic , vol.8 , Issue.12 , pp. 1796-1814
    • Bailey, D.1    Barreca, C.2    O'Hare, P.3
  • 75
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • DOI 10.1128/MCB.25.20.8844-8853.2005
    • Afshar, N., Black, B. E. & Paschal, B. M. Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell Biol. 25, 8844-53 (2005). (Pubitemid 41429076)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.20 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 76
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang, S. W. et al. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013 (2006).
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1
  • 77
    • 0028175016 scopus 로고
    • Topological frustration in multispanning E. coli inner membrane proteins
    • Gafvelin, G. & von Heijne, G. Topological "frustration" in multispanning E. coli inner membrane proteins. Cell 77, 401-12 (1994).
    • (1994) Cell , vol.77 , pp. 401-412
    • Gafvelin, G.1    Von Heijne, G.2
  • 78
    • 0035853751 scopus 로고    scopus 로고
    • Involvement of the acid sphingomyelinase pathway in UVAinduced apoptosis
    • Zhang, Y. et al. Involvement of the acid sphingomyelinase pathway in UVAinduced apoptosis. J. Biol. Chem. 276, 11775-82 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 11775-11782
    • Zhang, Y.1


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