메뉴 건너뛰기




Volumn 124, Issue 19, 2011, Pages 3332-3343

Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin

Author keywords

Bip; ERAD; FRAP; Huntingtin; UPR

Indexed keywords

DITHIOTHREITOL; GLUCOSE REGULATED PROTEIN 78; GLUTAMINE; HUNTINGTIN; HYBRID PROTEIN; MUTANT PROTEIN; SECRETORY PROTEIN; TUNICAMYCIN;

EID: 80054037000     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.087510     Document Type: Article
Times cited : (42)

References (67)
  • 2
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales, S., McDonald, K. L. and Walter, P. (2006). Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4, e423.
    • (2006) PLoS Biol , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 5
    • 63449090757 scopus 로고    scopus 로고
    • Huntingtin as an essential integrator of intracellular vesicular trafficking
    • Caviston, J. P. and Holzbaur, E. L. (2009). Huntingtin as an essential integrator of intracellular vesicular trafficking. Trends Cell Biol. 19, 147-155.
    • (2009) Trends Cell Biol , vol.19 , pp. 147-155
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 6
    • 0035800572 scopus 로고    scopus 로고
    • Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity
    • Chen, S., Berthelier, V., Yang, W. and Wetzel, R. (2001). Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity. J. Mol. Biol. 311, 173-182.
    • (2001) J. Mol. Biol. , vol.311 , pp. 173-182
    • Chen, S.1    Berthelier, V.2    Yang, W.3    Wetzel, R.4
  • 7
    • 76249091683 scopus 로고    scopus 로고
    • Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear huntingtin fragments in a mouse model of Huntington disease
    • Cho, K. J., Lee, B. I., Cheon, S. Y., Kim, H. W., Kim, H. J. and Kim, G. W. (2009). Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear huntingtin fragments in a mouse model of Huntington disease. Neuroscience 163, 1128-1134.
    • (2009) Neuroscience , vol.163 , pp. 1128-1134
    • Cho, K.J.1    Lee, B.I.2    Cheon, S.Y.3    Kim, H.W.4    Kim, H.J.5    Kim, G.W.6
  • 8
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J. C., Shaler, T. A., Tyler, R. E. and Kopito, R. R. (2008). OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat. Cell Biol. 10, 272-282.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 9
    • 73249116246 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB
    • Cunha, D. A., Ladriere, L., Ortis, F., Igoillo-Esteve, M., Gurzov, E. N., Lupi, R., Marchetti, P., Eizirik, D. L. and Cnop, M. (2009). Glucagon-like peptide-1 agonists protect pancreatic beta-cells from lipotoxic endoplasmic reticulum stress through upregulation of BiP and JunB. Diabetes 58, 2851-2862.
    • (2009) Diabetes , vol.58 , pp. 2851-2862
    • Cunha, D.A.1    Ladriere, L.2    Ortis, F.3    Igoillo-Esteve, M.4    Gurzov, E.N.5    Lupi, R.6    Marchetti, P.7    Eizirik, D.L.8    Cnop, M.9
  • 10
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes
    • de Silva, A., Braakman, I. and Helenius, A. (1993). Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes. J. Cell Biol. 120, 647-655.
    • (1993) J. Cell Biol. , vol.120 , pp. 647-655
    • de Silva, A.1    Braakman, I.2    Helenius, A.3
  • 11
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M. L. and Lindquist, S. (2008). Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 22, 3308-3319.
    • (2008) Genes Dev , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 13
    • 84977586068 scopus 로고
    • Über die von der molekularkinetischen Theorie der Wärme geforderte Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen
    • Einstein, A. (1905). Über die von der molekularkinetischen Theorie der Wärme geforderte Bewegung von in ruhenden Flüssigkeiten suspendierten Teilchen. Ann. Phys. 17, 549-560.
    • (1905) Ann. Phys. , vol.17 , pp. 549-560
    • Einstein, A.1
  • 14
    • 43449129732 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Huntington's disease
    • Finkbeiner, S. and Mitra, S. (2008). The ubiquitin-proteasome pathway in Huntington's disease. ScientificWorldJournal 8, 421-433.
    • (2008) ScientificWorldJournal , vol.8 , pp. 421-433
    • Finkbeiner, S.1    Mitra, S.2
  • 15
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R. and Morimoto, R. I. (2006). Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311, 1471-1474.
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 16
    • 77954886545 scopus 로고    scopus 로고
    • Mutant huntingtin-impaired degradation of beta-catenin causes neurotoxicity in Huntington's disease
    • Godin, J. D., Poizat, G., Hickey, M. A., Maschat, F. and Humbert, S. (2010). Mutant huntingtin-impaired degradation of beta-catenin causes neurotoxicity in Huntington's disease. EMBO J. 29, 2433-2445.
    • (2010) EMBO J , vol.29 , pp. 2433-2445
    • Godin, J.D.1    Poizat, G.2    Hickey, M.A.3    Maschat, F.4    Humbert, S.5
  • 17
    • 79952036205 scopus 로고    scopus 로고
    • Protein misfolding and cellular stress: an overview
    • Gregersen, N. and Bross, P. (2010). Protein misfolding and cellular stress: an overview. Methods Mol. Biol. 648, 3-23.
    • (2010) Methods Mol. Biol. , vol.648 , pp. 3-23
    • Gregersen, N.1    Bross, P.2
  • 18
    • 33747768203 scopus 로고    scopus 로고
    • Huntington's disease: seeing the pathogenic process through a genetic lens
    • Gusella, J. F. and MacDonald, M. E. (2006). Huntington's disease: seeing the pathogenic process through a genetic lens. Trends Biochem. Sci. 31, 533-540.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 533-540
    • Gusella, J.F.1    MacDonald, M.E.2
  • 19
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Zhang, Y. and Ron, D. (1999). Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 397, 271-274.
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 20
    • 0036385786 scopus 로고    scopus 로고
    • A genetic link between the unfolded protein response and vesicle formation from the endoplasmic reticulum
    • Higashio, H. and Kohno, K. (2002). A genetic link between the unfolded protein response and vesicle formation from the endoplasmic reticulum. Biochem. Biophys. Res. Commun. 296, 568-574.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 568-574
    • Higashio, H.1    Kohno, K.2
  • 21
    • 70549084746 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease: mechanisms and therapeutic opportunities
    • Hosoi, T. and Ozawa, K. (2010). Endoplasmic reticulum stress in disease: mechanisms and therapeutic opportunities. Clin. Sci. 118, 19-29.
    • (2010) Clin. Sci. , vol.118 , pp. 19-29
    • Hosoi, T.1    Ozawa, K.2
  • 22
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine lengthdependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
    • Jana, N. R., Tanaka, M., Wang, G. and Nukina, N. (2000). Polyglutamine lengthdependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Hum. Mol. Genet. 9, 2009-2018.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1    Tanaka, M.2    Wang, G.3    Nukina, N.4
  • 23
    • 2542436167 scopus 로고    scopus 로고
    • Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity
    • Kaytor, M. D., Wilkinson, K. D. and Warren, S. T. (2004). Modulating huntingtin half-life alters polyglutamine-dependent aggregate formation and cell toxicity. J. Neurochem. 89, 962-973.
    • (2004) J. Neurochem. , vol.89 , pp. 962-973
    • Kaytor, M.D.1    Wilkinson, K.D.2    Warren, S.T.3
  • 25
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. and Sambrook, J. (1988). The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 26
    • 77953501690 scopus 로고    scopus 로고
    • BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells
    • Lai, C. W., Aronson, D. E. and Snapp, E. L. (2010). BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells. Mol. Biol. Cell 21, 1909-1921.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1909-1921
    • Lai, C.W.1    Aronson, D.E.2    Snapp, E.L.3
  • 27
    • 78650811716 scopus 로고    scopus 로고
    • Formation and toxicity of soluble polyglutamine oligomers in living cells
    • Lajoie, P. and Snapp, E. L. (2010). Formation and toxicity of soluble polyglutamine oligomers in living cells. PLoS ONE 5, e15245.
    • (2010) PLoS ONE , vol.5
    • Lajoie, P.1    Snapp, E.L.2
  • 28
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A. H., Iwakoshi, N. N. and Glimcher, L. H. (2003). XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell. Biol. 23, 7448-7459.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 30
    • 0027250125 scopus 로고
    • The secretory pathway is normal in dithiothreitoltreated cells, but disulfide-bonded proteins are reduced and reversibly retained in the endoplasmic reticulum
    • Lodish, H. F. and Kong, N. (1993). The secretory pathway is normal in dithiothreitoltreated cells, but disulfide-bonded proteins are reduced and reversibly retained in the endoplasmic reticulum. J. Biol. Chem. 268, 20598-20605.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20598-20605
    • Lodish, H.F.1    Kong, N.2
  • 31
    • 0034039901 scopus 로고    scopus 로고
    • Degradation of unassembled soluble Ig subunits by cytosolic proteasomes: evidence that retrotranslocation and degradation are coupled events
    • Mancini, R., Fagioli, C., Fra, A. M., Maggioni, C. and Sitia, R. (2000). Degradation of unassembled soluble Ig subunits by cytosolic proteasomes: evidence that retrotranslocation and degradation are coupled events. FASEB J. 14, 769-778.
    • (2000) FASEB J , vol.14 , pp. 769-778
    • Mancini, R.1    Fagioli, C.2    Fra, A.M.3    Maggioni, C.4    Sitia, R.5
  • 33
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak, S. J. and Ron, D. (2006). Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133-1149.
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 34
    • 0037327305 scopus 로고    scopus 로고
    • Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes
    • Martinez, I. M. and Chrispeels, M. J. (2003). Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes. Plant Cell 15, 561-576.
    • (2003) Plant Cell , vol.15 , pp. 561-576
    • Martinez, I.M.1    Chrispeels, M.J.2
  • 35
  • 37
    • 0034682799 scopus 로고    scopus 로고
    • Regulation of connexin degradation as a mechanism to increase gap junction assembly and function
    • Musil, L. S., Le, A. C., VanSlyke, J. K. and Roberts, L. M. (2000). Regulation of connexin degradation as a mechanism to increase gap junction assembly and function. J. Biol. Chem. 275, 25207-25215.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25207-25215
    • Musil, L.S.1    Le, A.C.2    VanSlyke, J.K.3    Roberts, L.M.4
  • 38
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh, H., Matsuzawa, A., Tobiume, K., Saegusa, K., Takeda, K., Inoue, K., Hori, S., Kakizuka, A. and Ichijo, H. (2002). ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 16, 1345-1355.
    • (2002) Genes Dev , vol.16 , pp. 1345-1355
    • Nishitoh, H.1    Matsuzawa, A.2    Tobiume, K.3    Saegusa, K.4    Takeda, K.5    Inoue, K.6    Hori, S.7    Kakizuka, A.8    Ichijo, H.9
  • 39
    • 66449112462 scopus 로고    scopus 로고
    • SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded polyglutamine protein aggregates via endocytosis inhibition
    • Noh, J. Y., Lee, H., Song, S., Kim, N. S., Im, W., Kim, M., Seo, H., Chung, C. W., Chang, J. W., Ferrante, R. J. et al. (2009). SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded polyglutamine protein aggregates via endocytosis inhibition. J. Biol. Chem. 284, 11318-11325.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11318-11325
    • Noh, J.Y.1    Lee, H.2    Song, S.3    Kim, N.S.4    Im, W.5    Kim, M.6    Seo, H.7    Chung, C.W.8    Chang, J.W.9    Ferrante, R.J.10
  • 40
    • 77953302472 scopus 로고    scopus 로고
    • Nature and cause of mitochondrial dysfunction in Huntington's disease: focusing on huntingtin and the striatum
    • Oliveira, J. M. (2010). Nature and cause of mitochondrial dysfunction in Huntington's disease: focusing on huntingtin and the striatum. J. Neurochem. 114, 1-12.
    • (2010) J. Neurochem. , vol.114 , pp. 1-12
    • Oliveira, J.M.1
  • 43
    • 39649114320 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins
    • Reijonen, S., Putkonen, N., Norremolle, A., Lindholm, D. and Korhonen, L. (2008). Inhibition of endoplasmic reticulum stress counteracts neuronal cell death and protein aggregation caused by N-terminal mutant huntingtin proteins. Exp. Cell Res. 314, 950-960.
    • (2008) Exp. Cell Res. , vol.314 , pp. 950-960
    • Reijonen, S.1    Putkonen, N.2    Norremolle, A.3    Lindholm, D.4    Korhonen, L.5
  • 44
    • 33747359908 scopus 로고    scopus 로고
    • Polyglutamine neurodegenerative diseases and regulation of transcription: assembling the puzzle
    • Riley, B. E. and Orr, H. T. (2006). Polyglutamine neurodegenerative diseases and regulation of transcription: assembling the puzzle. Genes Dev. 20, 2183-2192.
    • (2006) Genes Dev , vol.20 , pp. 2183-2192
    • Riley, B.E.1    Orr, H.T.2
  • 45
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron, D. and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 46
    • 35348827324 scopus 로고    scopus 로고
    • That which does not kill me makes me stronger: adapting to chronic ER stress
    • Rutkowski, D. T. and Kaufman, R. J. (2007). That which does not kill me makes me stronger: adapting to chronic ER stress. Trends Biochem. Sci. 32, 469-476.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 469-476
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 48
    • 63149175877 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy
    • Scheper, W. and Hoozemans, J. J. (2009). Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy. Curr. Med. Chem. 16, 615-626.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 615-626
    • Scheper, W.1    Hoozemans, J.J.2
  • 50
    • 73349106233 scopus 로고    scopus 로고
    • Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response
    • Schuck, S., Prinz, W. A., Thorn, K. S., Voss, C. and Walter, P. (2009). Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response. J. Cell Biol. 187, 525-536.
    • (2009) J. Cell Biol. , vol.187 , pp. 525-536
    • Schuck, S.1    Prinz, W.A.2    Thorn, K.S.3    Voss, C.4    Walter, P.5
  • 51
    • 0033807598 scopus 로고    scopus 로고
    • Diffusion in inhomogeneous media: theory and simulations applied to whole cell photobleach recovery
    • Siggia, E. D., Lippincott-Schwartz, J. and Bekiranov, S. (2000). Diffusion in inhomogeneous media: theory and simulations applied to whole cell photobleach recovery. Biophys. J. 79, 1761-1770.
    • (2000) Biophys. J. , vol.79 , pp. 1761-1770
    • Siggia, E.D.1    Lippincott-Schwartz, J.2    Bekiranov, S.3
  • 52
    • 39049110236 scopus 로고    scopus 로고
    • Measuring protein mobility by photobleaching GFP chimeras in living cells
    • Chapter 21 Unit
    • Snapp, E. L., Altan, N. and Lippincott-Schwartz, J. (2003a). Measuring protein mobility by photobleaching GFP chimeras in living cells. Curr. Protoc. Cell Biol. Chapter 21, Unit 21 1.
    • (2003) Curr. Protoc. Cell Biol. , vol.21 , pp. 1
    • Snapp, E.L.1    Altan, N.2    Lippincott-Schwartz, J.3
  • 54
    • 33646238977 scopus 로고    scopus 로고
    • Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells
    • Snapp, E. L., Sharma, A., Lippincott-Schwartz, J. and Hegde, R. S. (2006). Monitoring chaperone engagement of substrates in the endoplasmic reticulum of live cells. Proc. Natl. Acad. Sci. USA 103, 6536-6541.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6536-6541
    • Snapp, E.L.1    Sharma, A.2    Lippincott-Schwartz, J.3    Hegde, R.S.4
  • 55
    • 78649262050 scopus 로고    scopus 로고
    • The clinical and genetic features of Huntington disease
    • Sturrock, A. and Leavitt, B. R. (2010). The clinical and genetic features of Huntington disease. J. Geriatr. Psychiatry Neurol. 23, 243-259.
    • (2010) J. Geriatr. Psychiatry Neurol. , vol.23 , pp. 243-259
    • Sturrock, A.1    Leavitt, B.R.2
  • 56
    • 4344568526 scopus 로고    scopus 로고
    • Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase
    • Svedine, S.,Wang, T., Halaban, R. and Hebert, D. N. (2004). Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. J. Cell Sci. 117, 2937-2949.
    • (2004) J. Cell Sci. , vol.117 , pp. 2937-2949
    • Svedine, S.1    Wang, T.2    Halaban, R.3    Hebert, D.N.4
  • 57
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I. and Ron, D. (2011). Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 13, 184-190.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 58
    • 0027174340 scopus 로고
    • Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells
    • Tatu, U., Braakman, I. and Helenius, A. (1993). Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells. EMBO J. 12, 2151-2157.
    • (1993) EMBO J , vol.12 , pp. 2151-2157
    • Tatu, U.1    Braakman, I.2    Helenius, A.3
  • 60
    • 20444378891 scopus 로고    scopus 로고
    • The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor
    • Thomas, M., Yu, Z., Dadgar, N., Varambally, S., Yu, J., Chinnaiyan, A. M. and Lieberman, A. P. (2005). The unfolded protein response modulates toxicity of the expanded glutamine androgen receptor. J. Biol. Chem. 280, 21264-21271.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21264-21271
    • Thomas, M.1    Yu, Z.2    Dadgar, N.3    Varambally, S.4    Yu, J.5    Chinnaiyan, A.M.6    Lieberman, A.P.7
  • 61
    • 0035844139 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits Involvement of ER-associated ubiquitinconjugating enzymes (E2s)
    • Tiwari, S. and Weissman, A. M. (2001). Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitinconjugating enzymes (E2s). J. Biol. Chem. 276, 16193-16200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16193-16200
    • Tiwari, S.1    Weissman, A.M.2
  • 63
    • 49349110821 scopus 로고    scopus 로고
    • Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases
    • Truant, R., Atwal, R. S., Desmond, C., Munsie, L. and Tran, T. (2008). Huntington's disease: revisiting the aggregation hypothesis in polyglutamine neurodegenerative diseases. FEBS J. 275, 4252-4262.
    • (2008) FEBS J , vol.275 , pp. 4252-4262
    • Truant, R.1    Atwal, R.S.2    Desmond, C.3    Munsie, L.4    Tran, T.5
  • 64
    • 58149380769 scopus 로고    scopus 로고
    • Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons
    • Tydlacka, S.,Wang, C. E., Wang, X., Li, S. and Li, X. J. (2008). Differential activities of the ubiquitin-proteasome system in neurons versus glia may account for the preferential accumulation of misfolded proteins in neurons. J. Neurosci. 28, 13285-13295.
    • (2008) J. Neurosci. , vol.28 , pp. 13285-13295
    • Tydlacka, S.1    Wang, C.E.2    Wang, X.3    Li, S.4    Li, X.J.5
  • 65
    • 0034047183 scopus 로고    scopus 로고
    • Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins
    • VanSlyke, J. K., Deschenes, S. M. and Musil, L. S. (2000). Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins. Mol. Biol. Cell 11, 1933-1946.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1933-1946
    • VanSlyke, J.K.1    Deschenes, S.M.2    Musil, L.S.3
  • 66
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang, H., Liu, C., Zhong, Y., Luo, S., Monteiro, M. J. and Fang, S. (2010). Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS ONE 5, e8905.
    • (2010) PLoS ONE , vol.5
    • Yang, H.1    Liu, C.2    Zhong, Y.3    Luo, S.4    Monteiro, M.J.5    Fang, S.6
  • 67
    • 33747891213 scopus 로고    scopus 로고
    • Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
    • Zhong, X. and Pittman, R. N. (2006). Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Hum. Mol. Genet. 15, 2409-2420.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2409-2420
    • Zhong, X.1    Pittman, R.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.