메뉴 건너뛰기




Volumn 39, Issue 6, 2016, Pages 394-404

Emerging Roles for the Unfolded Protein Response in the Developing Nervous System

Author keywords

[No Author keywords available]

Indexed keywords

REELIN;

EID: 84964617549     PISSN: 01662236     EISSN: 1878108X     Source Type: Journal    
DOI: 10.1016/j.tins.2016.04.002     Document Type: Review
Times cited : (58)

References (86)
  • 1
    • 32344431637 scopus 로고    scopus 로고
    • Area and layer patterning in the developing cerebral cortex
    • Rash B.G., Grove E.A. Area and layer patterning in the developing cerebral cortex. Curr. Opin. Neurobiol. 2006, 16:25-34.
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 25-34
    • Rash, B.G.1    Grove, E.A.2
  • 2
    • 0036250810 scopus 로고    scopus 로고
    • Life is a journey: a genetic look at neocortical development
    • Gupta A., et al. Life is a journey: a genetic look at neocortical development. Nat. Rev. Genet. 2002, 3:342-355.
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 342-355
    • Gupta, A.1
  • 3
    • 67651177570 scopus 로고    scopus 로고
    • The embryonic preoptic area is a novel source of cortical GABAergic interneurons
    • Gelman D.M., et al. The embryonic preoptic area is a novel source of cortical GABAergic interneurons. J. Neurosci. 2009, 29:9380-9389.
    • (2009) J. Neurosci. , vol.29 , pp. 9380-9389
    • Gelman, D.M.1
  • 4
    • 33747614577 scopus 로고    scopus 로고
    • The origin and specification of cortical interneurons
    • Wonders C.P., Anderson S.A. The origin and specification of cortical interneurons. Nat. Rev. Neurosci. 2006, 7:687-696.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 687-696
    • Wonders, C.P.1    Anderson, S.A.2
  • 5
    • 33644751622 scopus 로고    scopus 로고
    • Cell and molecular mechanisms involved in the migration of cortical interneurons
    • Metin C., et al. Cell and molecular mechanisms involved in the migration of cortical interneurons. Eur. J. Neurosci. 2006, 23:894-900.
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 894-900
    • Metin, C.1
  • 6
    • 70349554367 scopus 로고    scopus 로고
    • EFHC1 interacts with microtubules to regulate cell division and cortical development
    • de Nijs L., et al. EFHC1 interacts with microtubules to regulate cell division and cortical development. Nat. Neurosci. 2009, 12:1266-1274.
    • (2009) Nat. Neurosci. , vol.12 , pp. 1266-1274
    • de Nijs, L.1
  • 7
    • 80053540965 scopus 로고    scopus 로고
    • Absence of CNTNAP2 leads to epilepsy, neuronal migration abnormalities, and core autism-related deficits
    • Penagarikano O., et al. Absence of CNTNAP2 leads to epilepsy, neuronal migration abnormalities, and core autism-related deficits. Cell 2011, 147:235-246.
    • (2011) Cell , vol.147 , pp. 235-246
    • Penagarikano, O.1
  • 8
    • 84878717611 scopus 로고    scopus 로고
    • Mutations in TUBG1, DYNC1H1, KIF5 C and KIF2A cause malformations of cortical development and microcephaly
    • Poirier K., et al. Mutations in TUBG1, DYNC1H1, KIF5 C and KIF2A cause malformations of cortical development and microcephaly. Nat. Genet. 2013, 45:639-647.
    • (2013) Nat. Genet. , vol.45 , pp. 639-647
    • Poirier, K.1
  • 9
    • 84906712846 scopus 로고    scopus 로고
    • The impact of the endoplasmic reticulum protein-folding environment on cancer development
    • Wang M., Kaufman R.J. The impact of the endoplasmic reticulum protein-folding environment on cancer development. Nat. Rev. Cancer 2014, 14:581-597.
    • (2014) Nat. Rev. Cancer , vol.14 , pp. 581-597
    • Wang, M.1    Kaufman, R.J.2
  • 10
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T., Sitia R. Protein quality control in the early secretory pathway. EMBO J. 2008, 27:315-327.
    • (2008) EMBO J. , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 11
    • 84921901605 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in human pathology
    • Oakes S.A., Papa F.R. The role of endoplasmic reticulum stress in human pathology. Annu. Rev. Pathol. 2015, 10:173-194.
    • (2015) Annu. Rev. Pathol. , vol.10 , pp. 173-194
    • Oakes, S.A.1    Papa, F.R.2
  • 12
    • 23144451257 scopus 로고    scopus 로고
    • ERAD: the long road to destruction
    • Meusser B., et al. ERAD: the long road to destruction. Nat. Cell Biol. 2005, 7:766-772.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 766-772
    • Meusser, B.1
  • 13
    • 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
  • 14
    • 72149134488 scopus 로고    scopus 로고
    • Abnormal expression of collagen IV in lens activates unfolded protein response resulting in cataract
    • Firtina Z., et al. Abnormal expression of collagen IV in lens activates unfolded protein response resulting in cataract. J. Biol. Chem. 2009, 284:35872-35884.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35872-35884
    • Firtina, Z.1
  • 15
    • 79951671303 scopus 로고    scopus 로고
    • Unfolded protein response (UPR) is activated during normal lens development
    • Firtina Z., Duncan M.K. Unfolded protein response (UPR) is activated during normal lens development. Gene Expr. Patterns 2011, 11:135-143.
    • (2011) Gene Expr. Patterns , vol.11 , pp. 135-143
    • Firtina, Z.1    Duncan, M.K.2
  • 16
    • 77958457920 scopus 로고    scopus 로고
    • Control of activating transcription factor 4 (ATF4) persistence by multisite phosphorylation impacts cell cycle progression and neurogenesis
    • Frank C.L., et al. Control of activating transcription factor 4 (ATF4) persistence by multisite phosphorylation impacts cell cycle progression and neurogenesis. J. Biol. Chem. 2010, 285:33324-33337.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33324-33337
    • Frank, C.L.1
  • 17
    • 36348930605 scopus 로고    scopus 로고
    • The role of brain-derived neurotrophic factor (BDNF)-induced XBP1 splicing during brain development
    • Hayashi A., et al. The role of brain-derived neurotrophic factor (BDNF)-induced XBP1 splicing during brain development. J. Biol. Chem. 2007, 282:34525-34534.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34525-34534
    • Hayashi, A.1
  • 18
    • 84961576051 scopus 로고    scopus 로고
    • A dynamic unfolded protein response contributes to the control of cortical neurogenesis
    • Laguesse S., et al. A dynamic unfolded protein response contributes to the control of cortical neurogenesis. Dev. Cell 2015, 35:553-567.
    • (2015) Dev. Cell , vol.35 , pp. 553-567
    • Laguesse, S.1
  • 19
    • 37549015265 scopus 로고    scopus 로고
    • Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP
    • Mimura N., et al. Altered quality control in the endoplasmic reticulum causes cortical dysplasia in knock-in mice expressing a mutant BiP. Mol. Cell. Biol. 2008, 28:293-301.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 293-301
    • Mimura, N.1
  • 20
    • 6344225824 scopus 로고    scopus 로고
    • The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum
    • Shim J., et al. The unfolded protein response regulates glutamate receptor export from the endoplasmic reticulum. Mol. Biol. Cell 2004, 15:4818-4828.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4818-4828
    • Shim, J.1
  • 21
    • 84898681415 scopus 로고    scopus 로고
    • Initiation and developmental dynamics of Wfs1 expression in the context of neural differentiation and ER stress in mouse forebrain
    • Tekko T., et al. Initiation and developmental dynamics of Wfs1 expression in the context of neural differentiation and ER stress in mouse forebrain. Int. J. Dev. Neurosci. 2014, 35:80-88.
    • (2014) Int. J. Dev. Neurosci. , vol.35 , pp. 80-88
    • Tekko, T.1
  • 22
    • 67649661636 scopus 로고    scopus 로고
    • Induction of unfolded protein response during neuronal induction of rat bone marrow stromal cells and mouse embryonic stem cells
    • Cho Y.M., et al. Induction of unfolded protein response during neuronal induction of rat bone marrow stromal cells and mouse embryonic stem cells. Exp. Mol. Med. 2009, 41:440-452.
    • (2009) Exp. Mol. Med. , vol.41 , pp. 440-452
    • Cho, Y.M.1
  • 23
    • 84904365695 scopus 로고    scopus 로고
    • Aberrant neuronal differentiation and inhibition of dendrite outgrowth resulting from endoplasmic reticulum stress
    • Kawada K., et al. Aberrant neuronal differentiation and inhibition of dendrite outgrowth resulting from endoplasmic reticulum stress. J. Neurosci. Res. 2014, 92:1122-1133.
    • (2014) J. Neurosci. Res. , vol.92 , pp. 1122-1133
    • Kawada, K.1
  • 24
    • 84855453212 scopus 로고    scopus 로고
    • Deficient Notch signaling associated with neurogenic pecanex is compensated for by the unfolded protein response in Drosophila
    • Yamakawa T., et al. Deficient Notch signaling associated with neurogenic pecanex is compensated for by the unfolded protein response in Drosophila. Development 2012, 139:558-567.
    • (2012) Development , vol.139 , pp. 558-567
    • Yamakawa, T.1
  • 25
    • 54949151933 scopus 로고    scopus 로고
    • Dynamic Notch signaling in neural progenitor cells and a revised view of lateral inhibition
    • Kageyama R., et al. Dynamic Notch signaling in neural progenitor cells and a revised view of lateral inhibition. Nat. Neurosci. 2008, 11:1247-1251.
    • (2008) Nat. Neurosci. , vol.11 , pp. 1247-1251
    • Kageyama, R.1
  • 26
    • 1642458489 scopus 로고    scopus 로고
    • Cortical neurons arise in symmetric and asymmetric division zones and migrate through specific phases
    • Noctor S.C., et al. Cortical neurons arise in symmetric and asymmetric division zones and migrate through specific phases. Nat. Neurosci. 2004, 7:136-144.
    • (2004) Nat. Neurosci. , vol.7 , pp. 136-144
    • Noctor, S.C.1
  • 28
    • 84931576485 scopus 로고    scopus 로고
    • Optimization of codon translation rates via tRNA modifications maintains proteome integrity
    • Nedialkova D.D., Leidel S.A. Optimization of codon translation rates via tRNA modifications maintains proteome integrity. Cell 2015, 161:1606-1618.
    • (2015) Cell , vol.161 , pp. 1606-1618
    • Nedialkova, D.D.1    Leidel, S.A.2
  • 29
    • 0033739622 scopus 로고    scopus 로고
    • PERK mediates cell-cycle exit during the mammalian unfolded protein response
    • Brewer J.W., Diehl J.A. PERK mediates cell-cycle exit during the mammalian unfolded protein response. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:12625-12630.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12625-12630
    • Brewer, J.W.1    Diehl, J.A.2
  • 30
    • 84885667446 scopus 로고    scopus 로고
    • Co-opting the unfolded protein response to elicit olfactory receptor feedback
    • Dalton R.P., et al. Co-opting the unfolded protein response to elicit olfactory receptor feedback. Cell 2013, 155:321-332.
    • (2013) Cell , vol.155 , pp. 321-332
    • Dalton, R.P.1
  • 31
    • 84937047237 scopus 로고    scopus 로고
    • The unfolded protein response is required for dendrite morphogenesis
    • Wei X., et al. The unfolded protein response is required for dendrite morphogenesis. Elife 2015, 4:e06963.
    • (2015) Elife , vol.4 , pp. e06963
    • Wei, X.1
  • 32
    • 84864603834 scopus 로고    scopus 로고
    • Drosophila fatty acid transport protein regulates rhodopsin-1 metabolism and is required for photoreceptor neuron survival
    • Dourlen P., et al. Drosophila fatty acid transport protein regulates rhodopsin-1 metabolism and is required for photoreceptor neuron survival. PLoS Genet. 2012, 8:e1002833.
    • (2012) PLoS Genet. , vol.8 , pp. e1002833
    • Dourlen, P.1
  • 33
    • 84887609926 scopus 로고    scopus 로고
    • Xbp1-independent Ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila
    • Coelho D.S., et al. Xbp1-independent Ire1 signaling is required for photoreceptor differentiation and rhabdomere morphogenesis in Drosophila. Cell Rep. 2013, 5:791-801.
    • (2013) Cell Rep. , vol.5 , pp. 791-801
    • Coelho, D.S.1
  • 34
    • 84929353109 scopus 로고    scopus 로고
    • A Drosophila reporter for the translational activation of ATF4 marks stressed cells during development
    • Kang K., et al. A Drosophila reporter for the translational activation of ATF4 marks stressed cells during development. PLoS ONE 2015, 10:e0126795.
    • (2015) PLoS ONE , vol.10 , pp. e0126795
    • Kang, K.1
  • 35
    • 79955520100 scopus 로고    scopus 로고
    • A CHOP-regulated microRNA controls rhodopsin expression
    • Behrman S., et al. A CHOP-regulated microRNA controls rhodopsin expression. J. Cell Biol. 2011, 192:919-927.
    • (2011) J. Cell Biol. , vol.192 , pp. 919-927
    • Behrman, S.1
  • 36
    • 84960336177 scopus 로고    scopus 로고
    • Ire1 supports normal ER differentiation in developing Drosophila photoreceptors
    • Xu Z., et al. Ire1 supports normal ER differentiation in developing Drosophila photoreceptors. J. Cell Sci. 2016, 129:921-929.
    • (2016) J. Cell Sci. , vol.129 , pp. 921-929
    • Xu, Z.1
  • 37
    • 4644247806 scopus 로고    scopus 로고
    • Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice
    • Zuber C., et al. Misfolded proinsulin accumulates in expanded pre-Golgi intermediates and endoplasmic reticulum subdomains in pancreatic beta cells of Akita mice. FASEB J. 2004, 18:917-919.
    • (2004) FASEB J. , vol.18 , pp. 917-919
    • Zuber, C.1
  • 38
    • 0025995535 scopus 로고
    • The cyclophilin homolog ninaA is required in the secretory pathway
    • Colley N.J., et al. The cyclophilin homolog ninaA is required in the secretory pathway. Cell 1991, 67:255-263.
    • (1991) Cell , vol.67 , pp. 255-263
    • Colley, N.J.1
  • 39
    • 0018244387 scopus 로고
    • Mechanisms of cortical development: a view from mutations in mice
    • Caviness V.S., Rakic P. Mechanisms of cortical development: a view from mutations in mice. Annu. Rev. Neurosci. 1978, 1:297-326.
    • (1978) Annu. Rev. Neurosci. , vol.1 , pp. 297-326
    • Caviness, V.S.1    Rakic, P.2
  • 40
    • 0034682554 scopus 로고    scopus 로고
    • Reelin controls position of autonomic neurons in the spinal cord
    • Yip J.W., et al. Reelin controls position of autonomic neurons in the spinal cord. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:8612-8616.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8612-8616
    • Yip, J.W.1
  • 41
    • 0036534443 scopus 로고    scopus 로고
    • Evidence for a cell-specific action of Reelin in the spinal cord
    • Phelps P.E., et al. Evidence for a cell-specific action of Reelin in the spinal cord. Dev. Biol. 2002, 244:180-198.
    • (2002) Dev. Biol. , vol.244 , pp. 180-198
    • Phelps, P.E.1
  • 42
    • 84877833331 scopus 로고    scopus 로고
    • A modified UPR stress sensing system reveals a novel tissue distribution of IRE1/XBP1 activity during normal Drosophila development
    • Sone M., et al. A modified UPR stress sensing system reveals a novel tissue distribution of IRE1/XBP1 activity during normal Drosophila development. Cell Stress Chaperones 2013, 18:307-319.
    • (2013) Cell Stress Chaperones , vol.18 , pp. 307-319
    • Sone, M.1
  • 43
    • 84864835211 scopus 로고    scopus 로고
    • Unfolded protein response, activated by OASIS family transcription factors, promotes astrocyte differentiation
    • Saito A., et al. Unfolded protein response, activated by OASIS family transcription factors, promotes astrocyte differentiation. Nat. Commun. 2012, 3:967.
    • (2012) Nat. Commun. , vol.3 , pp. 967
    • Saito, A.1
  • 44
    • 84949096300 scopus 로고    scopus 로고
    • Differential activation of ER stress pathways in myelinating cerebellar tracts
    • Naughton M.C., et al. Differential activation of ER stress pathways in myelinating cerebellar tracts. Int. J. Dev. Neurosci. 2015, 47:347-360.
    • (2015) Int. J. Dev. Neurosci. , vol.47 , pp. 347-360
    • Naughton, M.C.1
  • 45
    • 84896319455 scopus 로고    scopus 로고
    • Genetic inactivation of PERK signaling in mouse oligodendrocytes: normal developmental myelination with increased susceptibility to inflammatory demyelination
    • Hussien Y., et al. Genetic inactivation of PERK signaling in mouse oligodendrocytes: normal developmental myelination with increased susceptibility to inflammatory demyelination. Glia 2014, 62:680-691.
    • (2014) Glia , vol.62 , pp. 680-691
    • Hussien, Y.1
  • 46
    • 84921448756 scopus 로고    scopus 로고
    • Deletion of Atf6alpha impairs astroglial activation and enhances neuronal death following brain ischemia in mice
    • Yoshikawa A., et al. Deletion of Atf6alpha impairs astroglial activation and enhances neuronal death following brain ischemia in mice. J. Neurochem. 2015, 132:342-353.
    • (2015) J. Neurochem. , vol.132 , pp. 342-353
    • Yoshikawa, A.1
  • 47
    • 33747816491 scopus 로고    scopus 로고
    • Glia-specific activation of all pathways of the unfolded protein response in vanishing white matter disease
    • van Kollenburg B., et al. Glia-specific activation of all pathways of the unfolded protein response in vanishing white matter disease. J. Neuropathol. Exp. Neurol. 2006, 65:707-715.
    • (2006) J. Neuropathol. Exp. Neurol. , vol.65 , pp. 707-715
    • van Kollenburg, B.1
  • 48
    • 84875722407 scopus 로고    scopus 로고
    • The unfolded protein response to endoplasmic reticulum stress in cultured astrocytes and rat brain during experimental diabetes
    • Lind K.R., et al. The unfolded protein response to endoplasmic reticulum stress in cultured astrocytes and rat brain during experimental diabetes. Neurochem. Int. 2013, 62:784-795.
    • (2013) Neurochem. Int. , vol.62 , pp. 784-795
    • Lind, K.R.1
  • 49
    • 34247152063 scopus 로고    scopus 로고
    • A novel ER stress transducer, OASIS, expressed in astrocytes
    • Saito A., et al. A novel ER stress transducer, OASIS, expressed in astrocytes. Antioxid. Redox Signal. 2007, 9:563-571.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 563-571
    • Saito, A.1
  • 50
    • 13944263299 scopus 로고    scopus 로고
    • OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes
    • Kondo S., et al. OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes. Nat. Cell. Biol. 2005, 7:186-194.
    • (2005) Nat. Cell. Biol. , vol.7 , pp. 186-194
    • Kondo, S.1
  • 51
    • 84870735655 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress sensing in the unfolded protein response
    • Gardner B.M., et al. Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb. Perspect. Biol. 2013, 5:a013169.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a013169
    • Gardner, B.M.1
  • 52
    • 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
  • 53
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon M., 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
  • 54
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • Hollien J., Weissman J.S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 2006, 313:104-107.
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 55
    • 0034515724 scopus 로고    scopus 로고
    • ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs
    • Ye J., 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
  • 56
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N., Hinnebusch A.G. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 57
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz C., et al. Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 2013, 12:703-719.
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 703-719
    • Hetz, C.1
  • 58
    • 84925662746 scopus 로고    scopus 로고
    • Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis
    • Zhu G., Lee A.S. Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis. J. Cell Physiol. 2015, 230:1413-1420.
    • (2015) J. Cell Physiol. , vol.230 , pp. 1413-1420
    • Zhu, G.1    Lee, A.S.2
  • 59
    • 15944366885 scopus 로고    scopus 로고
    • The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
    • Lee A.S. The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress. Methods 2005, 35:373-381.
    • (2005) Methods , vol.35 , pp. 373-381
    • Lee, A.S.1
  • 60
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z., Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 2003, 22:2309-2317.
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 61
    • 70349777048 scopus 로고    scopus 로고
    • Regulation of apoptosis by the unfolded protein response
    • Fribley A., et al. Regulation of apoptosis by the unfolded protein response. Methods Mol. Biol. 2009, 559:191-204.
    • (2009) Methods Mol. Biol. , vol.559 , pp. 191-204
    • Fribley, A.1
  • 62
    • 63649109017 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disorders of myelinating cells
    • Lin W., Popko B. Endoplasmic reticulum stress in disorders of myelinating cells. Nat. Neurosci. 2009, 12:379-385.
    • (2009) Nat. Neurosci. , vol.12 , pp. 379-385
    • Lin, W.1    Popko, B.2
  • 63
    • 84947867559 scopus 로고    scopus 로고
    • Genome-wide RNA-seq of human motor neurons implicates selective ER stress activation in spinal muscular atrophy
    • Ng S.Y., et al. Genome-wide RNA-seq of human motor neurons implicates selective ER stress activation in spinal muscular atrophy. Cell Stem Cell 2015, 17:569-584.
    • (2015) Cell Stem Cell , vol.17 , pp. 569-584
    • Ng, S.Y.1
  • 64
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10(Suppl):S10-S17.
    • (2004) Nat. Med. , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 65
    • 0038143287 scopus 로고    scopus 로고
    • Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons
    • Holtz W.A., O'Malley K.L. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons. J. Biol. Chem. 2003, 278:19367-19377.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19367-19377
    • Holtz, W.A.1    O'Malley, K.L.2
  • 66
    • 24344489466 scopus 로고    scopus 로고
    • The unfolded protein response is activated in Alzheimer's disease
    • Hoozemans J.J., et al. The unfolded protein response is activated in Alzheimer's disease. Acta Neuropathol. 2005, 110:165-172.
    • (2005) Acta Neuropathol. , vol.110 , pp. 165-172
    • Hoozemans, J.J.1
  • 67
    • 33645798615 scopus 로고    scopus 로고
    • Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model
    • Kikuchi H., et al. Spinal cord endoplasmic reticulum stress associated with a microsomal accumulation of mutant superoxide dismutase-1 in an ALS model. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:6025-6030.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6025-6030
    • Kikuchi, H.1
  • 68
    • 0036606540 scopus 로고    scopus 로고
    • ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats
    • Nishitoh H., et al. ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats. Genes Dev. 2002, 16:1345-1355.
    • (2002) Genes Dev. , vol.16 , pp. 1345-1355
    • Nishitoh, H.1
  • 69
    • 84883453343 scopus 로고    scopus 로고
    • Suppression of eIF2alpha kinases alleviates Alzheimer's disease-related plasticity and memory deficits
    • Ma T., et al. Suppression of eIF2alpha kinases alleviates Alzheimer's disease-related plasticity and memory deficits. Nat. Neurosci. 2013, 16:1299-1305.
    • (2013) Nat. Neurosci. , vol.16 , pp. 1299-1305
    • Ma, T.1
  • 70
    • 84887226564 scopus 로고    scopus 로고
    • Expression of autophagy and UPR genes in the developing brain during ethanol-sensitive and resistant periods
    • Alimov A., et al. Expression of autophagy and UPR genes in the developing brain during ethanol-sensitive and resistant periods. Metab. Brain Dis. 2013, 28:667-676.
    • (2013) Metab. Brain Dis. , vol.28 , pp. 667-676
    • Alimov, A.1
  • 71
    • 84867837982 scopus 로고    scopus 로고
    • Inherited genetic variants in autism-related CNTNAP2 show perturbed trafficking and ATF6 activation
    • Falivelli G., et al. Inherited genetic variants in autism-related CNTNAP2 show perturbed trafficking and ATF6 activation. Hum. Mol. Genet. 2012, 21:4761-4773.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4761-4773
    • Falivelli, G.1
  • 72
    • 84863818278 scopus 로고    scopus 로고
    • Early brain vulnerability in Wolfram syndrome
    • Hershey T., et al. Early brain vulnerability in Wolfram syndrome. PLoS ONE 2012, 7:e40604.
    • (2012) PLoS ONE , vol.7 , pp. e40604
    • Hershey, T.1
  • 73
    • 80051617030 scopus 로고    scopus 로고
    • Sequencing of DISC1 pathway genes reveals increased burden of rare missense variants in schizophrenia patients from a northern Swedish population
    • Moens L.N., et al. Sequencing of DISC1 pathway genes reveals increased burden of rare missense variants in schizophrenia patients from a northern Swedish population. PLoS ONE 2011, 6:e23450.
    • (2011) PLoS ONE , vol.6 , pp. e23450
    • Moens, L.N.1
  • 74
    • 84861731674 scopus 로고    scopus 로고
    • DISC1 variants 37 W and 607F disrupt its nuclear targeting and regulatory role in ATF4-mediated transcription
    • Malavasi E.L., et al. DISC1 variants 37 W and 607F disrupt its nuclear targeting and regulatory role in ATF4-mediated transcription. Hum. Mol. Genet. 2012, 21:2779-2792.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2779-2792
    • Malavasi, E.L.1
  • 75
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K., Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response. Nature 2008, 454:455-462.
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 76
    • 0037079142 scopus 로고    scopus 로고
    • The unfolded protein response modulates disease severity in Pelizaeus-Merzbacher disease
    • Southwood C.M., et al. The unfolded protein response modulates disease severity in Pelizaeus-Merzbacher disease. Neuron 2002, 36:585-596.
    • (2002) Neuron , vol.36 , pp. 585-596
    • Southwood, C.M.1
  • 77
    • 0030036917 scopus 로고    scopus 로고
    • A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease
    • Gow A., Lazzarini R.A. A cellular mechanism governing the severity of Pelizaeus-Merzbacher disease. Nat. Genet. 1996, 13:422-428.
    • (1996) Nat. Genet. , vol.13 , pp. 422-428
    • Gow, A.1    Lazzarini, R.A.2
  • 78
    • 18344386777 scopus 로고    scopus 로고
    • Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter
    • Leegwater P.A., et al. Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter. Nat. Genet. 2001, 29:383-388.
    • (2001) Nat. Genet. , vol.29 , pp. 383-388
    • Leegwater, P.A.1
  • 79
    • 36049023510 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress during the embryonic development of the central nervous system in the mouse
    • Zhang X., et al. Endoplasmic reticulum stress during the embryonic development of the central nervous system in the mouse. Int. J. Dev. Neurosci. 2007, 25:455-463.
    • (2007) Int. J. Dev. Neurosci. , vol.25 , pp. 455-463
    • Zhang, X.1
  • 80
    • 10744233077 scopus 로고    scopus 로고
    • ORP150/HSP12A regulates Purkinje cell survival: a role for endoplasmic reticulum stress in cerebellar development
    • Kitao Y., et al. ORP150/HSP12A regulates Purkinje cell survival: a role for endoplasmic reticulum stress in cerebellar development. J. Neurosci. 2004, 24:1486-1496.
    • (2004) J. Neurosci. , vol.24 , pp. 1486-1496
    • Kitao, Y.1
  • 81
    • 84885758467 scopus 로고    scopus 로고
    • Deficiency of asparagine synthetase causes congenital microcephaly and a progressive form of encephalopathy
    • Ruzzo E.K., et al. Deficiency of asparagine synthetase causes congenital microcephaly and a progressive form of encephalopathy. Neuron 2013, 80:429-441.
    • (2013) Neuron , vol.80 , pp. 429-441
    • Ruzzo, E.K.1
  • 82
    • 80052021823 scopus 로고    scopus 로고
    • Ethanol induces endoplasmic reticulum stress in the developing brain
    • Ke Z., et al. Ethanol induces endoplasmic reticulum stress in the developing brain. Alcohol Clin. Exp. Res. 2011, 35:1574-1583.
    • (2011) Alcohol Clin. Exp. Res. , vol.35 , pp. 1574-1583
    • Ke, Z.1
  • 83
    • 84898642148 scopus 로고    scopus 로고
    • Neurogenesis during development of the vertebrate central nervous system
    • Paridaen J.T., Huttner W.B. Neurogenesis during development of the vertebrate central nervous system. EMBO Rep. 2014, 15:351-364.
    • (2014) EMBO Rep. , vol.15 , pp. 351-364
    • Paridaen, J.T.1    Huttner, W.B.2
  • 84
    • 65249141717 scopus 로고    scopus 로고
    • Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels
    • Raghu P., et al. Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels. J. Cell Biol. 2009, 185:129-145.
    • (2009) J. Cell Biol. , vol.185 , pp. 129-145
    • Raghu, P.1
  • 85
    • 5444222234 scopus 로고    scopus 로고
    • XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum
    • Sriburi R., et al. XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J. Cell Biol. 2004, 167:35-41.
    • (2004) J. Cell Biol. , vol.167 , pp. 35-41
    • Sriburi, R.1
  • 86
    • 29244448729 scopus 로고    scopus 로고
    • XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands
    • Lee A.H., et al. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J. 2005, 24:4368-4380.
    • (2005) EMBO J. , vol.24 , pp. 4368-4380
    • Lee, A.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.