메뉴 건너뛰기




Volumn 53, Issue 11, 2012, Pages 7159-7166

Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; GLUCOSE REGULATED PROTEIN 78; PROTEIN KINASE R; PROTEIN KINASE RNA LIKE ENDOPLASMIC RETICULUM KINASE; RHODOPSIN; UNCLASSIFIED DRUG; ATF6 PROTEIN, HUMAN; ERN2 PROTEIN, HUMAN; MEMBRANE PROTEIN; PERK KINASE; PROTEIN SERINE THREONINE KINASE; RIBONUCLEASE;

EID: 84871870648     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.12-10222     Document Type: Article
Times cited : (68)

References (53)
  • 1
    • 0019994808 scopus 로고
    • Visual field changes in cone-rod degenerations
    • Krauss HR, Heckenlively JR. Visual field changes in cone-rod degenerations. Arch Ophthalmol. 1982;100:1784-1790.
    • (1982) Arch Ophthalmol. , vol.100 , pp. 1784-1790
    • Krauss, H.R.1    Heckenlively, J.R.2
  • 2
    • 0027537949 scopus 로고
    • Retinitis pigmentosa. The Friedenwald Lecture
    • Berson EL. Retinitis pigmentosa. The Friedenwald Lecture. Invest Ophthalmol Vis Sci. 1993;34:1659-1676.
    • (1993) Invest Ophthalmol Vis Sci. , vol.34 , pp. 1659-1676
    • Berson, E.L.1
  • 3
    • 41149137801 scopus 로고    scopus 로고
    • Activation of G protein-coupled receptors: Beyond two-state models and tertiary conformational changes
    • Park PS, Lodowski DT, Palczewski K. Activation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes. Annu Rev Pharmacol Toxicol. 2008;48:107-141.
    • (2008) Annu Rev Pharmacol Toxicol. , vol.48 , pp. 107-141
    • Park, P.S.1    Lodowski, D.T.2    Palczewski, K.3
  • 4
    • 0026058548 scopus 로고
    • Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa
    • Sung CH, Schneider BG, Agarwal N, Papermaster DS, Nathans J. Functional heterogeneity of mutant rhodopsins responsible for autosomal dominant retinitis pigmentosa. Proc Natl Acad Sci U S A. 1991;88:8840-8844.
    • (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
  • 5
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa
    • Kaushal S, Khorana HG. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry. 1994;33:6121-6128.
    • (1994) Biochemistry. , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 6
    • 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
    • Illing ME, Rajan RS, Bence NF, Kopito RR. A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system. J Biol Chem. 2002; 277:34150-34160.
    • (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
  • 7
    • 0037099080 scopus 로고    scopus 로고
    • The cellular fate of mutant rhodopsin: Quality control, degradation and aggresome formation
    • Saliba RS, Munro PM, Luthert PJ, Cheetham ME. The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation. J Cell Sci. 2002;115:2907-2918.
    • (2002) J Cell Sci. , vol.115 , pp. 2907-2918
    • Saliba, R.S.1    Munro, P.M.2    Luthert, P.J.3    Cheetham, M.E.4
  • 8
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • Lin JH, Li H, Yasumura D, et al. IRE1 signaling affects cell fate during the unfolded protein response. Science. 2007;318:944-949.
    • (2007) Science. , vol.318 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3
  • 9
    • 77950532428 scopus 로고    scopus 로고
    • Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78
    • Gorbatyuk MS, Knox T, LaVail MM, et al. Restoration of visual function in P23H rhodopsin transgenic rats by gene delivery of BiP/Grp78. Proc Natl Acad Sci U S A. 2010;107:5961-5966.
    • (2010) Proc Natl Acad Sci U S A. , vol.107 , pp. 5961-5966
    • Gorbatyuk, M.S.1    Knox, T.2    LaVail, M.M.3
  • 10
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter P, Ron D. The unfolded protein response: from stress pathway to homeostatic regulation. Science. 2011;334:1081-1086.
    • (2011) Science. , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 11
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J, Rawson RB, Komuro R, et al. ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell. 2000;6:1355-1364.
    • (2000) Mol Cell. , vol.6 , pp. 1355-1364
    • Ye, J.1    Rawson, R.B.2    Komuro, R.3
  • 12
    • 0041731803 scopus 로고    scopus 로고
    • A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6
    • Okada T, Haze K, Nadanaka S, et al. A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6. J Biol Chem. 2003;278:31024-31032.
    • (2003) J Biol Chem. , vol.278 , pp. 31024-31032
    • Okada, T.1    Haze, K.2    Nadanaka, S.3
  • 13
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell. 2002;3:99-111.
    • (2002) Dev Cell. , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 14
    • 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
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell. 1999;10:3787-3799.
    • (1999) Mol Biol Cell. , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 15
    • 34548189283 scopus 로고    scopus 로고
    • ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress
    • Wu J, Rutkowski DT, Dubois M, et al. ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress. Dev Cell. 2007;13:351-364.
    • (2007) Dev Cell. , vol.13 , pp. 351-364
    • Wu, J.1    Rutkowski, D.T.2    Dubois, M.3
  • 16
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto K, Sato T, Matsui T, et al. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell. 2007;13:365-376.
    • (2007) Dev Cell. , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3
  • 17
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 1999; 397:271-274.
    • (1999) Nature. , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 18
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resistance to oxidative stress
    • Harding HP, Zhang Y, Zeng H, et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol Cell. 2003;11:619-633.
    • (2003) Mol Cell. , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3
  • 19
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M, Zeng H, Urano F, et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature. 2002;415:92-96.
    • (2002) Nature. , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3
  • 20
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell. 1993;73:1197-1206.
    • (1993) Cell. , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 21
    • 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
    • Yoshida H, Matsui T, Yamamoto A, Okada T, Mori K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell. 2001;107:881-891.
    • (2001) Cell. , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 22
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee AH, Iwakoshi NN, Glimcher LH. XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol. 2003;23:7448-7459.
    • (2003) Mol Cell Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 23
    • 84863250283 scopus 로고    scopus 로고
    • IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin
    • Chiang WC, Messah C, Lin JH. IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin. Mol Biol Cell. 2012;23:758-770.
    • (2012) Mol Biol Cell. , vol.23 , pp. 758-770
    • Chiang, W.C.1    Messah, C.2    Lin, J.H.3
  • 24
    • 58449084895 scopus 로고    scopus 로고
    • Divergent effects of PERK and IRE1 signaling on cell viability
    • Lin JH, Li H, Zhang Y, Ron D, Walter P. Divergent effects of PERK and IRE1 signaling on cell viability. PLoS One. 2009;4:e4170.
    • (2009) PLoS One. , vol.4
    • Lin, J.H.1    Li, H.2    Zhang, Y.3    Ron, D.4    Walter, P.5
  • 25
    • 0034699382 scopus 로고    scopus 로고
    • A chemical switch for inhibitor-sensitive alleles of any protein kinase
    • Bishop AC, Ubersax JA, Petsch DT, et al. A chemical switch for inhibitor-sensitive alleles of any protein kinase. Nature. 2000;407: 395-401.
    • (2000) Nature. , vol.407 , pp. 395-401
    • Bishop, A.C.1    Ubersax, J.A.2    Petsch, D.T.3
  • 26
    • 79951648063 scopus 로고    scopus 로고
    • Monitoring and manipulating mammalian unfolded protein response
    • Hiramatsu N, Joseph VT, Lin JH. Monitoring and manipulating mammalian unfolded protein response. Methods Enzymol. 2011; 491:183-198.
    • (2011) Methods Enzymol. , vol.491 , pp. 183-198
    • Hiramatsu, N.1    Joseph, V.T.2    Lin, J.H.3
  • 27
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 2007;8:519-529.
    • (2007) Nat Rev Mol Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 28
    • 77449113158 scopus 로고    scopus 로고
    • Severe retinal degeneration caused by a novel rhodopsin mutation
    • Liu H, Wang M, Xia CH, et al. Severe retinal degeneration caused by a novel rhodopsin mutation. Invest Ophthalmol Vis Sci. 2010;51:1059-1065.
    • (2010) Invest Ophthalmol Vis Sci. , vol.51 , pp. 1059-1065
    • Liu, H.1    Wang, M.2    Xia, C.H.3
  • 29
    • 17044363529 scopus 로고    scopus 로고
    • Mechanisms of cell death in rhodopsin retinitis pigmentosa: Implications for therapy
    • Mendes HF, van der Spuy J, Chapple JP, Cheetham ME. Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy. Trends Mol Med. 2005;11:177-185.
    • (2005) Trends Mol Med. , vol.11 , pp. 177-185
    • Mendes, H.F.1    van der Spuy, J.2    Chapple, J.P.3    Cheetham, M.E.4
  • 30
    • 78650855405 scopus 로고    scopus 로고
    • Analysis of disease-linked rhodopsin mutations based on structure, function, and protein stability calculations
    • Rakoczy EP, Kiel C, McKeone R, Stricher F, Serrano L. Analysis of disease-linked rhodopsin mutations based on structure, function, and protein stability calculations. J Mol Biol. 2011;405:584-606.
    • (2011) J Mol Biol. , vol.405 , pp. 584-606
    • Rakoczy, E.P.1    Kiel, C.2    McKeone, R.3    Stricher, F.4    Serrano, L.5
  • 31
    • 0346902097 scopus 로고    scopus 로고
    • Photoreceptor degeneration in Pro23His and S334ter transgenic rats
    • Lee D, Geller S, Walsh N, et al. Photoreceptor degeneration in Pro23His and S334ter transgenic rats. Adv Exp Med Biol. 2003;533: 297-302.
    • (2003) Adv Exp Med Biol. , vol.533 , pp. 297-302
    • Lee, D.1    Geller, S.2    Walsh, N.3
  • 32
    • 5144234438 scopus 로고    scopus 로고
    • Photoreceptor preservation in the S334ter model of retinitis pigmentosa by a novel estradiol analog
    • Dykens JA, Carroll AK, Wiley S, et al. Photoreceptor preservation in the S334ter model of retinitis pigmentosa by a novel estradiol analog. Biochem Pharmacol. 2004;68:1971-1984.
    • (2004) Biochem Pharmacol. , vol.68 , pp. 1971-1984
    • Dykens, J.A.1    Carroll, A.K.2    Wiley, S.3
  • 33
    • 0036974437 scopus 로고    scopus 로고
    • Low docosahexaenoic acid levels in rod outer segments of rats with P23H and S334ter rhodopsin mutations
    • Anderson RE, Maude MB, McClellan M, Matthes MT, Yasumura D, LaVail MM. Low docosahexaenoic acid levels in rod outer segments of rats with P23H and S334ter rhodopsin mutations. Mol Vis. 2002;8: 351-358.
    • (2002) Mol Vis. , vol.8 , pp. 351-358
    • Anderson, R.E.1    Maude, M.B.2    McClellan, M.3    Matthes, M.T.4    Yasumura, D.5    LaVail, M.M.6
  • 35
    • 56349134417 scopus 로고    scopus 로고
    • The relationship of photoreceptor degeneration to retinal vascular development and loss in mutant rhodopsin transgenic and RCS rats
    • Pennesi ME, Nishikawa S, Matthes MT, Yasumura D, LaVail MM. The relationship of photoreceptor degeneration to retinal vascular development and loss in mutant rhodopsin transgenic and RCS rats. Exp Eye Res. 2008;87:561-570.
    • (2008) Exp Eye Res. , vol.87 , pp. 561-570
    • Pennesi, M.E.1    Nishikawa, S.2    Matthes, M.T.3    Yasumura, D.4    LaVail, M.M.5
  • 36
    • 0036183677 scopus 로고    scopus 로고
    • The carboxyl-terminal domain is essential for rhodopsin transport in rod photoreceptors
    • Concepcion F, Mendez A, Chen J. The carboxyl-terminal domain is essential for rhodopsin transport in rod photoreceptors. Vision Res. 2002;42:417-426.
    • (2002) Vision Res. , vol.42 , pp. 417-426
    • Concepcion, F.1    Mendez, A.2    Chen, J.3
  • 37
    • 0034015064 scopus 로고    scopus 로고
    • Characterization of rhodopsin mis-sorting and constitutive activation in a transgenic rat model of retinitis pigmentosa
    • Green ES, Menz MD, LaVail MM, Flannery JG. Characterization of rhodopsin mis-sorting and constitutive activation in a transgenic rat model of retinitis pigmentosa. Invest Ophthalmol Vis Sci. 2000;41: 1546-1553.
    • (2000) Invest Ophthalmol Vis Sci. , vol.41 , pp. 1546-1553
    • Green, E.S.1    Menz, M.D.2    LaVail, M.M.3    Flannery, J.G.4
  • 38
    • 34347204136 scopus 로고    scopus 로고
    • Transport of truncated rhodopsin and its effects on rod function and degeneration
    • Lee ES, Flannery JG. Transport of truncated rhodopsin and its effects on rod function and degeneration. Invest Ophthalmol Vis Sci. 2007; 48:2868-2876.
    • (2007) Invest Ophthalmol Vis Sci. , vol.48 , pp. 2868-2876
    • Lee, E.S.1    Flannery, J.G.2
  • 39
    • 0027348403 scopus 로고
    • High-mannose chains of mammalian glycoproteins
    • Sherblom AP, Smagula RM. High-mannose chains of mammalian glycoproteins. Methods Mol Biol. 1993;14:143-149.
    • (1993) Methods Mol Biol. , vol.14 , pp. 143-149
    • Sherblom, A.P.1    Smagula, R.M.2
  • 40
    • 0021485787 scopus 로고
    • Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-beta-N-acetylglucosaminidase H
    • Trimble RB, Maley F. Optimizing hydrolysis of N-linked high-mannose oligosaccharides by endo-beta-N-acetylglucosaminidase H. Anal Biochem. 1984;141:515-522.
    • (1984) Anal Biochem. , vol.141 , pp. 515-522
    • Trimble, R.B.1    Maley, F.2
  • 41
    • 0038529723 scopus 로고    scopus 로고
    • Pharmacological chaperonemediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa
    • Noorwez SM, Kuksa V, Imanishi Y, et al. Pharmacological chaperonemediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa. J Biol Chem. 2003;278:14442-14450.
    • (2003) J Biol Chem. , vol.278 , pp. 14442-14450
    • Noorwez, S.M.1    Kuksa, V.2    Imanishi, Y.3
  • 42
    • 1942469395 scopus 로고    scopus 로고
    • Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H
    • Noorwez SM, Malhotra R, McDowell JH, Smith KA, Krebs MP, Kaushal S. Retinoids assist the cellular folding of the autosomal dominant retinitis pigmentosa opsin mutant P23H. J Biol Chem. 2004;279: 16278-16284.
    • (2004) J Biol Chem. , vol.279 , pp. 16278-16284
    • Noorwez, S.M.1    Malhotra, R.2    McDowell, J.H.3    Smith, K.A.4    Krebs, M.P.5    Kaushal, S.6
  • 44
    • 52949134162 scopus 로고    scopus 로고
    • Pharmacological manipulation of gain-offunction and dominant-negative mechanisms in rhodopsin retinitis pigmentosa
    • Mendes HF, Cheetham ME. Pharmacological manipulation of gain-offunction and dominant-negative mechanisms in rhodopsin retinitis pigmentosa. Hum Mol Genet. 2008;17:3043-3054.
    • (2008) Hum Mol Genet. , vol.17 , pp. 3043-3054
    • Mendes, H.F.1    Cheetham, M.E.2
  • 45
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol. 2004;167:27-33.
    • (2004) J Cell Biol. , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 46
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • Lu PD, Jousse C, Marciniak SJ, et al. Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J. 2004;23:169-179.
    • (2004) EMBO J. , vol.23 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3
  • 48
    • 44449101173 scopus 로고    scopus 로고
    • ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum
    • Adachi Y, Yamamoto K, Okada T, Yoshida H, Harada A, Mori K. ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum. Cell Struct Funct. 2008;33:75-89.
    • (2008) Cell Struct Funct. , vol.33 , pp. 75-89
    • Adachi, Y.1    Yamamoto, K.2    Okada, T.3    Yoshida, H.4    Harada, A.5    Mori, K.6
  • 49
    • 82355184462 scopus 로고    scopus 로고
    • Activating transcription factor 6 limits intracellular accumulation of mutant alpha(1)-antitrypsin Z and mitochondrial damage in hepatoma cells
    • Smith SE, Granell S, Salcedo-Sicilia L, Baldini G, Egea G, Teckman JH. Activating transcription factor 6 limits intracellular accumulation of mutant alpha(1)-antitrypsin Z and mitochondrial damage in hepatoma cells. J Biol Chem. 2011;286:41563-41577.
    • (2011) J Biol Chem. , vol.286 , pp. 41563-41577
    • Smith, S.E.1    Granell, S.2    Salcedo-Sicilia, L.3    Baldini, G.4    Egea, G.5    Teckman, J.H.6
  • 50
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation
    • Kaneko M, Koike H, Saito R, Kitamura Y, Okuma Y, Nomura Y. Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J Neurosci. 2010;30:3924-3932.
    • (2010) J Neurosci. , vol.30 , pp. 3924-3932
    • Kaneko, M.1    Koike, H.2    Saito, R.3    Kitamura, Y.4    Okuma, Y.5    Nomura, Y.6
  • 51
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding HP, Novoa I, Zhang Y, et al. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell. 2000;6:1099-1108.
    • (2000) Mol Cell. , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3
  • 52
    • 41449095062 scopus 로고    scopus 로고
    • Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions
    • Zhou D, Palam LR, Jiang L, Narasimhan J, Staschke KA, Wek RC. Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions. J Biol Chem. 2008;283:7064-7073.
    • (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
  • 53
    • 58249093962 scopus 로고    scopus 로고
    • Effect of an inducer of BiP, a molecular chaperone, on endoplasmic reticulum (ER) stress-induced retinal cell death
    • Inokuchi Y, Nakajima Y, Shimazawa M, et al. Effect of an inducer of BiP, a molecular chaperone, on endoplasmic reticulum (ER) stress-induced retinal cell death. Invest Ophthalmol Vis Sci. 2009;50:334-344.
    • (2009) Invest Ophthalmol Vis Sci. , vol.50 , pp. 334-344
    • Inokuchi, Y.1    Nakajima, Y.2    Shimazawa, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.