메뉴 건너뛰기




Volumn 185, Issue 7, 2015, Pages 1800-1808

Multiple Mechanisms of Unfolded Protein Response-Induced Cell Death

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PKR LIKE ENDOPLASMIC RETICULUM KINASE; PROTEIN BCL 2; PROTEIN IRE1; PROTEIN SERINE THREONINE KINASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; CHAPERONE; ERN1 PROTEIN, HUMAN; PERK KINASE; PROTEIN KINASE R; RIBONUCLEASE;

EID: 84931349200     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2015.03.009     Document Type: Review
Times cited : (164)

References (86)
  • 1
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome
    • C. Hetz, and L.H. Glimcher Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome Mol Cell 35 2009 551 561
    • (2009) Mol Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 2
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • J.S. Cox, C.E. Shamu, and P. Walter Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase Cell 73 1993 1197 1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 3
    • 0029903049 scopus 로고    scopus 로고
    • Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus
    • C.E. Shamu, and P. Walter Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus EMBO J 15 1996 3028 3039
    • (1996) EMBO J , vol.15 , pp. 3028-3039
    • Shamu, C.E.1    Walter, P.2
  • 5
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, and K. Mori XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor Cell 107 2001 881 891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 6
    • 84926106643 scopus 로고    scopus 로고
    • A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB
    • Y. Lu, F.X. Liang, and X. Wang A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB Mol Cell 55 2014 758 770
    • (2014) Mol Cell , vol.55 , pp. 758-770
    • Lu, Y.1    Liang, F.X.2    Wang, X.3
  • 9
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • A.H. Lee, N.N. Iwakoshi, and L.H. Glimcher XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response Mol Cell Biol 23 2003 7448 7459
    • (2003) Mol Cell Biol , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 11
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • K. Yamamoto, H. Yoshida, K. Kokame, R.J. Kaufman, and K. Mori Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II J Biochem 136 2004 343 350
    • (2004) J Biochem , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 12
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • K. Yamamoto, T. Sato, T. Matsui, M. Sato, T. Okada, H. Yoshida, A. Harada, and K. Mori Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1 Dev Cell 13 2007 365 376
    • (2007) Dev Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 15
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • H.P. Harding, Y. Zhang, and D. Ron Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature 397 1999 271 274
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 16
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • H.P. Harding, M. Calfon, F. Urano, I. Novoa, and D. Ron Transcriptional and translational control in the Mammalian unfolded protein response Annu Rev Cell Dev Biol 18 2002 575 599
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 17
    • 84870732594 scopus 로고    scopus 로고
    • Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation
    • pii: a013177
    • D. Ron, and H.P. Harding Protein-folding homeostasis in the endoplasmic reticulum and nutritional regulation Cold Spring Harb Perspect Biol 2012 4 pii: a013177
    • (2012) Cold Spring Harb Perspect Biol , pp. 4
    • Ron, D.1    Harding, H.P.2
  • 18
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • K. Haze, H. Yoshida, H. Yanagi, T. Yura, and K. Mori Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress Mol Biol Cell 10 1999 3787 3799
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 21
  • 23
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • H. Li, A.V. Korennykh, S.L. Behrman, and P. Walter Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering Proc Natl Acad Sci U S A 107 2010 16113 16118
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 25
    • 84919708686 scopus 로고    scopus 로고
    • Ire1 has distinct catalytic mechanisms for XBP1/HAC1 splicing and RIDD
    • A.B. Tam, A.C. Koong, and M. Niwa Ire1 has distinct catalytic mechanisms for XBP1/HAC1 splicing and RIDD Cell Rep 9 2014 850 858
    • (2014) Cell Rep , vol.9 , pp. 850-858
    • Tam, A.B.1    Koong, A.C.2    Niwa, M.3
  • 26
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • J. Hollien, and J.S. Weissman Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response Science 313 2006 104 107
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 28
    • 0035958913 scopus 로고    scopus 로고
    • Oxidative stress-induced phospholipase C-gamma 1 activation enhances cell survival
    • X.T. Wang, K.D. McCullough, X.J. Wang, G. Carpenter, and N.J. Holbrook Oxidative stress-induced phospholipase C-gamma 1 activation enhances cell survival J Biol Chem 276 2001 28364 28371
    • (2001) J Biol Chem , vol.276 , pp. 28364-28371
    • Wang, X.T.1    McCullough, K.D.2    Wang, X.J.3    Carpenter, G.4    Holbrook, N.J.5
  • 33
    • 0034312290 scopus 로고    scopus 로고
    • The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
    • W. Tirasophon, K. Lee, B. Callaghan, A. Welihinda, and R.J. Kaufman The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response Genes Dev 14 2000 2725 2736
    • (2000) Genes Dev , vol.14 , pp. 2725-2736
    • Tirasophon, W.1    Lee, K.2    Callaghan, B.3    Welihinda, A.4    Kaufman, R.J.5
  • 35
    • 84875857579 scopus 로고    scopus 로고
    • The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis
    • P. Kimmig, M. Diaz, J. Zheng, C.C. Williams, A. Lang, T. Aragon, H. Li, and P. Walter The unfolded protein response in fission yeast modulates stability of select mRNAs to maintain protein homeostasis Elife 1 2012 e00048
    • (2012) Elife , vol.1
    • Kimmig, P.1    Diaz, M.2    Zheng, J.3    Williams, C.C.4    Lang, A.5    Aragon, T.6    Li, H.7    Walter, P.8
  • 36
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • F. Urano, X. Wang, A. Bertolotti, Y. Zhang, P. Chung, H.P. Harding, and D. Ron Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1 Science 287 2000 664 666
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 37
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • H. Nishitoh, A. Matsuzawa, K. Tobiume, K. Saegusa, K. Takeda, K. Inoue, S. Hori, A. Kakizuka, and H. Ichijo ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats Genes Dev 16 2002 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
  • 42
    • 41449095062 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions
    • D. Zhou, L.R. Palam, L. Jiang, J. Narasimhan, K.A. Staschke, and R.C. Wek Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions J Biol Chem 283 2008 7064 7073
    • (2008) J Biol Chem , vol.283 , pp. 7064-7073
    • Zhou, D.1    Palam, L.R.2    Jiang, L.3    Narasimhan, J.4    Staschke, K.A.5    Wek, R.C.6
  • 43
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • H.P. Harding, I. Novoa, Y. Zhang, H. Zeng, R. Wek, M. Schapira, and D. Ron Regulated translation initiation controls stress-induced gene expression in mammalian cells Mol Cell 6 2000 1099 1108
    • (2000) Mol Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 44
    • 79953224498 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation
    • L.R. Palam, T.D. Baird, and R.C. Wek Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation J Biol Chem 286 2011 10939 10949
    • (2011) J Biol Chem , vol.286 , pp. 10939-10949
    • Palam, L.R.1    Baird, T.D.2    Wek, R.C.3
  • 48
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • I. Novoa, H. Zeng, H.P. Harding, and D. Ron Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha J Cell Biol 153 2001 1011 1022
    • (2001) J Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 50
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • P. Tsaytler, H.P. Harding, D. Ron, and A. Bertolotti Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis Science 332 2011 91 94
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 56
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • N. Ohoka, S. Yoshii, T. Hattori, K. Onozaki, and H. Hayashi TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death EMBO J 24 2005 1243 1255
    • (2005) EMBO J , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 57
    • 8544283103 scopus 로고    scopus 로고
    • CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells
    • H. Yamaguchi, and H.G. Wang CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells J Biol Chem 279 2004 45495 45502
    • (2004) J Biol Chem , vol.279 , pp. 45495-45502
    • Yamaguchi, H.1    Wang, H.G.2
  • 58
    • 84899672694 scopus 로고    scopus 로고
    • Translational and post-translational regulation of XIAP by eIF2α and ATF4 promotes ER stress-induced cell death during the unfolded protein response
    • N. Hiramatsu, C. Messah, J. Han, M.M. LaVail, R.J. Kaufman, and J.H. Lin Translational and post-translational regulation of XIAP by eIF2α and ATF4 promotes ER stress-induced cell death during the unfolded protein response Mol Biol Cell 25 2014 1411 1420
    • (2014) Mol Biol Cell , vol.25 , pp. 1411-1420
    • Hiramatsu, N.1    Messah, C.2    Han, J.3    Lavail, M.M.4    Kaufman, R.J.5    Lin, J.H.6
  • 59
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: blocking the road to death's door
    • G.S. Salvesen, and C.S. Duckett IAP proteins: blocking the road to death's door Nat Rev Mol Cell Biol 3 2002 401 410
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 60
    • 84871870648 scopus 로고    scopus 로고
    • Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation
    • W.C. Chiang, N. Hiramatsu, C. Messah, H. Kroeger, and J.H. Lin Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation Invest Ophthalmol Vis Sci 53 2012 7159 7166
    • (2012) Invest Ophthalmol Vis Sci , vol.53 , pp. 7159-7166
    • Chiang, W.C.1    Hiramatsu, N.2    Messah, C.3    Kroeger, H.4    Lin, J.H.5
  • 61
    • 79951648063 scopus 로고    scopus 로고
    • Monitoring and manipulating mammalian unfolded protein response
    • N. Hiramatsu, V.T. Joseph, and J.H. Lin Monitoring and manipulating mammalian unfolded protein response Methods Enzymol 491 2011 183 198
    • (2011) Methods Enzymol , vol.491 , pp. 183-198
    • Hiramatsu, N.1    Joseph, V.T.2    Lin, J.H.3
  • 62
    • 34447558382 scopus 로고    scopus 로고
    • Melatonin attenuates arsenite-induced apoptosis in rat brain: involvement of mitochondrial and endoplasmic reticulum pathways and aggregation of alpha-synuclein
    • A.M. Lin, S.F. Fang, P.L. Chao, and C.H. Yang Melatonin attenuates arsenite-induced apoptosis in rat brain: involvement of mitochondrial and endoplasmic reticulum pathways and aggregation of alpha-synuclein J Pineal Res 43 2007 163 171
    • (2007) J Pineal Res , vol.43 , pp. 163-171
    • Lin, A.M.1    Fang, S.F.2    Chao, P.L.3    Yang, C.H.4
  • 63
    • 58449084895 scopus 로고    scopus 로고
    • Divergent effects of PERK and IRE1 signaling on cell viability
    • J.H. Lin, H. Li, Y. Zhang, D. Ron, and P. Walter Divergent effects of PERK and IRE1 signaling on cell viability PLoS One 4 2009 e4170
    • (2009) PLoS One , vol.4
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 64
    • 33645535034 scopus 로고    scopus 로고
    • G protein-coupled receptor rhodopsin
    • K. Palczewski G protein-coupled receptor rhodopsin Annu Rev Biochem 75 2006 743 767
    • (2006) Annu Rev Biochem , vol.75 , pp. 743-767
    • Palczewski, K.1
  • 67
    • 0033399668 scopus 로고    scopus 로고
    • Molecular genetics of human retinal disease
    • A. Rattner, H. Sun, and J. Nathans Molecular genetics of human retinal disease Annu Rev Genet 33 1999 89 131
    • (1999) Annu Rev Genet , vol.33 , pp. 89-131
    • Rattner, A.1    Sun, H.2    Nathans, J.3
  • 68
    • 0037072934 scopus 로고    scopus 로고
    • A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
    • M.E. Illing, R.S. Rajan, N.F. Bence, and R.R. Kopito A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system J Biol Chem 277 2002 34150 34160
    • (2002) J Biol Chem , vol.277 , pp. 34150-34160
    • Illing, M.E.1    Rajan, R.S.2    Bence, N.F.3    Kopito, R.R.4
  • 69
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • C.H. Sung, B.G. Schneider, N. Agarwal, D.S. Papermaster, and J. Nathans Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa Proc Natl Acad Sci U S A 88 1991 8840 8844
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8840-8844
    • Sung, C.H.1    Schneider, B.G.2    Agarwal, N.3    Papermaster, D.S.4    Nathans, J.5
  • 70
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin, 7: point mutations associated with autosomal dominant retinitis pigmentosa
    • S. Kaushal, and H.G. Khorana Structure and function in rhodopsin, 7: point mutations associated with autosomal dominant retinitis pigmentosa Biochemistry 33 1994 6121 6128
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 71
    • 84863250283 scopus 로고    scopus 로고
    • IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin
    • W.C. Chiang, C. Messah, and J.H. Lin IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin Mol Biol Cell 23 2012 758 770
    • (2012) Mol Biol Cell , vol.23 , pp. 758-770
    • Chiang, W.C.1    Messah, C.2    Lin, J.H.3
  • 72
    • 79953181251 scopus 로고    scopus 로고
    • Probing mechanisms of photoreceptor degeneration in a new mouse model of the common form of autosomal dominant retinitis pigmentosa due to P23H opsin mutations
    • S. Sakami, T. Maeda, G. Bereta, K. Okano, M. Golczak, A. Sumaroka, A.J. Roman, A.V. Cideciyan, S.G. Jacobson, and K. Palczewski Probing mechanisms of photoreceptor degeneration in a new mouse model of the common form of autosomal dominant retinitis pigmentosa due to P23H opsin mutations J Biol Chem 286 2011 10551 10567
    • (2011) J Biol Chem , vol.286 , pp. 10551-10567
    • Sakami, S.1    Maeda, T.2    Bereta, G.3    Okano, K.4    Golczak, M.5    Sumaroka, A.6    Roman, A.J.7    Cideciyan, A.V.8    Jacobson, S.G.9    Palczewski, K.10
  • 74
    • 84877003413 scopus 로고    scopus 로고
    • Ablation of C/EBP homologous protein does not protect T17M RHO mice from retinal degeneration
    • S. Nashine, Y. Bhootada, A.S. Lewin, and M. Gorbatyuk Ablation of C/EBP homologous protein does not protect T17M RHO mice from retinal degeneration PLoS One 8 2013 e63205
    • (2013) PLoS One , vol.8
    • Nashine, S.1    Bhootada, Y.2    Lewin, A.S.3    Gorbatyuk, M.4
  • 75
    • 84895823108 scopus 로고    scopus 로고
    • Ablation of the proapoptotic genes chop or ask1 does not prevent or delay loss of visual function in a P23H transgenic mouse model of retinitis pigmentosa
    • A. Adekeye, M. Haeri, E. Solessio, and B.E. Knox Ablation of the proapoptotic genes chop or ask1 does not prevent or delay loss of visual function in a P23H transgenic mouse model of retinitis pigmentosa PLoS One 9 2014 e83871
    • (2014) PLoS One , vol.9
    • Adekeye, A.1    Haeri, M.2    Solessio, E.3    Knox, B.E.4
  • 78
    • 43149121009 scopus 로고    scopus 로고
    • The prion protein knockout mouse: a phenotype under challenge
    • A.D. Steele, S. Lindquist, and A. Aguzzi The prion protein knockout mouse: a phenotype under challenge Prion 1 2007 83 93
    • (2007) Prion , vol.1 , pp. 83-93
    • Steele, A.D.1    Lindquist, S.2    Aguzzi, A.3
  • 80
    • 34250351315 scopus 로고    scopus 로고
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication
    • C. Hetz, J. Castilla, and C. Soto Perturbation of endoplasmic reticulum homeostasis facilitates prion replication J Biol Chem 282 2007 12725 12733
    • (2007) J Biol Chem , vol.282 , pp. 12725-12733
    • Hetz, C.1    Castilla, J.2    Soto, C.3
  • 81
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • A. Orsi, L. Fioriti, R. Chiesa, and R. Sitia Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein J Biol Chem 281 2006 30431 30438
    • (2006) J Biol Chem , vol.281 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 82
    • 80053212141 scopus 로고    scopus 로고
    • Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein
    • M. Nunziante, K. Ackermann, K. Dietrich, H. Wolf, L. Gädtke, S. Gilch, I. Vorberg, M. Groschup, and H.M. Schätzl Proteasomal dysfunction and endoplasmic reticulum stress enhance trafficking of prion protein aggregates through the secretory pathway and increase accumulation of pathologic prion protein J Biol Chem 286 2011 33942 33953
    • (2011) J Biol Chem , vol.286 , pp. 33942-33953
    • Nunziante, M.1    Ackermann, K.2    Dietrich, K.3    Wolf, H.4    Gädtke, L.5    Gilch, S.6    Vorberg, I.7    Groschup, M.8    Schätzl, H.M.9
  • 83
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2[alpha]-P mediates prion neurodegeneration
    • J.A. Moreno Sustained translational repression by eIF2[alpha]-P mediates prion neurodegeneration Nature 485 2012 507 511
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1
  • 84
    • 84885463900 scopus 로고    scopus 로고
    • Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice
    • J.A. Moreno Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice Sci Transl Med 5 2013 206ra138
    • (2013) Sci Transl Med , vol.5 , pp. 206ra138
    • Moreno, J.A.1
  • 85
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • C. Hetz Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis Proc Natl Acad Sci U S A 105 2008 757 762
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 757-762
    • Hetz, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.