메뉴 건너뛰기




Volumn 1648, Issue , 2016, Pages 658-666

Protein aggregation and ER stress

Author keywords

Alzheimer's disease; Huntington's disease; Neurodegenerative disease; Parkinson's disease; Protein misfolding; Unfolded protein response

Indexed keywords

PROTEASOME; UBIQUITIN;

EID: 84961918756     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2016.03.044     Document Type: Review
Times cited : (77)

References (216)
  • 1
    • 84954535655 scopus 로고    scopus 로고
    • A missense mutation in PPP1R15B causes a syndrome including diabetes, short stature, and microcephaly
    • Abdulkarim, B., et al. A missense mutation in PPP1R15B causes a syndrome including diabetes, short stature, and microcephaly. Diabetes 64 (2015), 3951–3962.
    • (2015) Diabetes , vol.64 , pp. 3951-3962
    • Abdulkarim, B.1
  • 2
    • 84878333056 scopus 로고    scopus 로고
    • Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation
    • Abisambra, J.F., et al. Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation. J. Neurosci. 33 (2013), 9498–9507.
    • (2013) J. Neurosci. , vol.33 , pp. 9498-9507
    • Abisambra, J.F.1
  • 3
    • 84941954604 scopus 로고    scopus 로고
    • A Huntingtin-based peptide inhibitor of caspase-6 provides protection from mutant Huntingtin-induced motor and behavioral deficits
    • Aharony, I., et al. A Huntingtin-based peptide inhibitor of caspase-6 provides protection from mutant Huntingtin-induced motor and behavioral deficits. Hum. Mol. Genet. 24 (2015), 2604–2614.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 2604-2614
    • Aharony, I.1
  • 4
    • 84155163741 scopus 로고    scopus 로고
    • A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis
    • Al-Saif, A., Al-Mohanna, F., Bohlega, S., A mutation in sigma-1 receptor causes juvenile amyotrophic lateral sclerosis. Ann. Neurol. 70 (2011), 913–919.
    • (2011) Ann. Neurol. , vol.70 , pp. 913-919
    • Al-Saif, A.1    Al-Mohanna, F.2    Bohlega, S.3
  • 5
    • 33749563294 scopus 로고    scopus 로고
    • Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1
    • Atkin, J.D., et al. Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1. J. Biol. Chem. 281 (2006), 30152–30165.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30152-30165
    • Atkin, J.D.1
  • 6
    • 85056070270 scopus 로고    scopus 로고
    • Rapamycin improves motor function, reduces 4-hydroxynonenal adducted protein in brain, and attenuates synaptic injury in a mouse model of synucleinopathy
    • Bai, X., et al. Rapamycin improves motor function, reduces 4-hydroxynonenal adducted protein in brain, and attenuates synaptic injury in a mouse model of synucleinopathy. Pathobiol. Aging Age Relat. Dis., 5, 2015, 28743.
    • (2015) Pathobiol. Aging Age Relat. Dis. , vol.5 , pp. 28743
    • Bai, X.1
  • 7
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W.E., et al. Adapting proteostasis for disease intervention. Science 319 (2008), 916–919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1
  • 8
    • 33748561495 scopus 로고    scopus 로고
    • Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers
    • Behrends, C., et al. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol. Cell 23 (2006), 887–897.
    • (2006) Mol. Cell , vol.23 , pp. 887-897
    • Behrends, C.1
  • 9
    • 79551647443 scopus 로고    scopus 로고
    • Induction of the unfolded protein response by alpha-synuclein in experimental models of Parkinson's disease
    • Bellucci, A., et al. Induction of the unfolded protein response by alpha-synuclein in experimental models of Parkinson's disease. J. Neurochem. 116 (2011), 588–605.
    • (2011) J. Neurochem. , vol.116 , pp. 588-605
    • Bellucci, A.1
  • 10
    • 34547807613 scopus 로고    scopus 로고
    • Global changes to the ubiquitin system in Huntington's disease
    • Bennett, E.J., et al. Global changes to the ubiquitin system in Huntington's disease. Nature 448 (2007), 704–708.
    • (2007) Nature , vol.448 , pp. 704-708
    • Bennett, E.J.1
  • 11
    • 84920946243 scopus 로고    scopus 로고
    • Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates
    • Benyair, R., et al. Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates. Mol. Biol. Cell 26 (2015), 172–184.
    • (2015) Mol. Biol. Cell , vol.26 , pp. 172-184
    • Benyair, R.1
  • 12
    • 80855139444 scopus 로고    scopus 로고
    • Protein quality control, retention, and degradation at the endoplasmic reticulum
    • Benyair, R., Ron, E., Lederkremer, G.Z., Protein quality control, retention, and degradation at the endoplasmic reticulum. Int. Rev. Cell Mol. Biol. 292 (2011), 197–280.
    • (2011) Int. Rev. Cell Mol. Biol. , vol.292 , pp. 197-280
    • Benyair, R.1    Ron, E.2    Lederkremer, G.Z.3
  • 13
    • 84931571933 scopus 로고    scopus 로고
    • Glycan regulation of ER-associated degradation through compartmentalization
    • Benyair, R., Ogen-Shtern, N., Lederkremer, G.Z., Glycan regulation of ER-associated degradation through compartmentalization. Semin. Cell Dev. Biol. 41 (2015), 99–109.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 99-109
    • Benyair, R.1    Ogen-Shtern, N.2    Lederkremer, G.Z.3
  • 14
    • 84890954073 scopus 로고    scopus 로고
    • Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial
    • Berk, J.L., et al. Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial. JAMA 310 (2013), 2658–2667.
    • (2013) JAMA , vol.310 , pp. 2658-2667
    • Berk, J.L.1
  • 15
    • 84929069085 scopus 로고    scopus 로고
    • Dysfunction in endoplasmic reticulum-mitochondria crosstalk underlies SIGMAR1 loss of function mediated motor neuron degeneration
    • Bernard-Marissal, N., et al. Dysfunction in endoplasmic reticulum-mitochondria crosstalk underlies SIGMAR1 loss of function mediated motor neuron degeneration. Brain 138 (2015), 875–890.
    • (2015) Brain , vol.138 , pp. 875-890
    • Bernard-Marissal, N.1
  • 16
    • 65249181587 scopus 로고    scopus 로고
    • The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease
    • Bett, J.S., et al. The ubiquitin-proteasome reporter GFPu does not accumulate in neurons of the R6/2 transgenic mouse model of Huntington's disease. PLoS One, 4, 2009, e5128.
    • (2009) PLoS One , vol.4 , pp. e5128
    • Bett, J.S.1
  • 17
    • 0036307333 scopus 로고    scopus 로고
    • Loss of kinase activity in a patient with Wolcott-Rallison syndrome caused by a novel mutation in the EIF2AK3 gene
    • Biason-Lauber, A., et al. Loss of kinase activity in a patient with Wolcott-Rallison syndrome caused by a novel mutation in the EIF2AK3 gene. Diabetes 51 (2002), 2301–2305.
    • (2002) Diabetes , vol.51 , pp. 2301-2305
    • Biason-Lauber, A.1
  • 18
    • 84864742403 scopus 로고    scopus 로고
    • Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis
    • Bosco, D.A., et al. Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis. Cold Spring Harb. Perspect. Biol., 3, 2011, a007500.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a007500
    • Bosco, D.A.1
  • 20
    • 83455202793 scopus 로고    scopus 로고
    • Alpha-synuclein misfolding and Parkinson's disease
    • Breydo, L., Wu, J.W., Uversky, V.N., Alpha-synuclein misfolding and Parkinson's disease. Biochim. Biophys. Acta 1822 (2012), 261–285.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 261-285
    • Breydo, L.1    Wu, J.W.2    Uversky, V.N.3
  • 21
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning Up: ER-Associated Degradation to the Rescue
    • Brodsky, J.L., Cleaning Up: ER-Associated Degradation to the Rescue. Cell 151 (2012), 1163–1167.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 22
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows, J.A., Willis, L.K., Perlmutter, D.H., Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc. Natl. Acad. Sci. USA 97 (2000), 1796–1801.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 23
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo, J.J., Parodi, A.J., Getting in and out from calnexin/calreticulin cycles. J. Biol. Chem. 283 (2008), 10221–10225.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 24
    • 84946491193 scopus 로고    scopus 로고
    • A sweet code for glycoprotein folding
    • Caramelo, J.J., Parodi, A.J., A sweet code for glycoprotein folding. FEBS Lett. 589 (2015), 3379–3387.
    • (2015) FEBS Lett. , vol.589 , pp. 3379-3387
    • Caramelo, J.J.1    Parodi, A.J.2
  • 25
    • 67650566385 scopus 로고    scopus 로고
    • Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease
    • Carnemolla, A., et al. Rrs1 is involved in endoplasmic reticulum stress response in Huntington disease. J. Biol. Chem. 284 (2009), 18167–18173.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18167-18173
    • Carnemolla, A.1
  • 26
    • 79956036398 scopus 로고    scopus 로고
    • The ER stress factor XBP1s prevents amyloid-β neurotoxicity
    • Casas-Tinto, S., et al. The ER stress factor XBP1s prevents amyloid-β neurotoxicity. Hum. Mol. Genet. 20 (2011), 2144–2160.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2144-2160
    • Casas-Tinto, S.1
  • 27
    • 84871870648 scopus 로고    scopus 로고
    • Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation
    • Chiang, W.C., et al. Selective activation of ATF6 and PERK endoplasmic reticulum stress signaling pathways prevent mutant rhodopsin accumulation. Investig. Ophthalmol. Vis. Sci. 53 (2012), 7159–7166.
    • (2012) Investig. Ophthalmol. Vis. Sci. , vol.53 , pp. 7159-7166
    • Chiang, W.C.1
  • 28
    • 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., et al. Inhibition of apoptosis signal-regulating kinase 1 reduces endoplasmic reticulum stress and nuclear huntingtin fragments in a mouse model of Huntington disease. Neuroscience 163 (2009), 1128–1134.
    • (2009) Neuroscience , vol.163 , pp. 1128-1134
    • Cho, K.J.1
  • 29
    • 16644379264 scopus 로고    scopus 로고
    • Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function
    • Cleary, J.P., et al. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat. Neurosci. 8 (2005), 79–84.
    • (2005) Nat. Neurosci. , vol.8 , pp. 79-84
    • Cleary, J.P.1
  • 30
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of alpha-synucleinopathy in vivo
    • Colla, E., et al. Endoplasmic reticulum stress is important for the manifestations of alpha-synucleinopathy in vivo. J. Neurosci. 32 (2012), 3306–3320.
    • (2012) J. Neurosci. , vol.32 , pp. 3306-3320
    • Colla, E.1
  • 31
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla, E., et al. Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J. Neurosci. 32 (2012), 3301–3305.
    • (2012) J. Neurosci. , vol.32 , pp. 3301-3305
    • Colla, E.1
  • 32
    • 0030866540 scopus 로고    scopus 로고
    • Human prion diseases and bovine spongiform encephalopathy (BSE)
    • Collinge, J., Human prion diseases and bovine spongiform encephalopathy (BSE). Hum. Mol. Genet. 6 (1997), 1699–1705.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1699-1705
    • Collinge, J.1
  • 33
    • 84906993311 scopus 로고    scopus 로고
    • Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain
    • Cooley, C.B., et al. Unfolded protein response activation reduces secretion and extracellular aggregation of amyloidogenic immunoglobulin light chain. Proc. Natl. Acad. Sci. USA 111 (2014), 13046–13051.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 13046-13051
    • Cooley, C.B.1
  • 34
    • 33947719749 scopus 로고    scopus 로고
    • eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory
    • Costa-Mattioli, M., et al. eIF2alpha phosphorylation bidirectionally regulates the switch from short- to long-term synaptic plasticity and memory. Cell 129 (2007), 195–206.
    • (2007) Cell , vol.129 , pp. 195-206
    • Costa-Mattioli, M.1
  • 35
    • 84923871028 scopus 로고    scopus 로고
    • alpha-Synuclein-mediated inhibition of ATF6 processing into COPII vesicles disrupts UPR signaling in Parkinson's disease
    • Credle, J.J., et al. alpha-Synuclein-mediated inhibition of ATF6 processing into COPII vesicles disrupts UPR signaling in Parkinson's disease. Neurobiol. Dis. 76 (2015), 112–125.
    • (2015) Neurobiol. Dis. , vol.76 , pp. 112-125
    • Credle, J.J.1
  • 36
    • 84927619395 scopus 로고    scopus 로고
    • Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit
    • Das, I., et al. Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit. Science 348 (2015), 239–242.
    • (2015) Science , vol.348 , pp. 239-242
    • Das, I.1
  • 37
    • 0034425698 scopus 로고    scopus 로고
    • EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome
    • Delepine, M., et al. EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome. Nat. Genet. 25 (2000), 406–409.
    • (2000) Nat. Genet. , vol.25 , pp. 406-409
    • Delepine, M.1
  • 38
    • 0037457966 scopus 로고    scopus 로고
    • Chaperones increase association of tau protein with microtubules
    • Dou, F., et al. Chaperones increase association of tau protein with microtubules. Proc. Natl. Acad. Sci. 100 (2003), 721–726.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 721-726
    • Dou, F.1
  • 39
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M.L., Lindquist, S., Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes. Dev. 22 (2008), 3308–3319.
    • (2008) Genes. Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 40
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D., Jucker, M., The amyloid state of proteins in human diseases. Cell 148 (2012), 1188–1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 41
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., Helenius, A., Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4 (2003), 181–191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 42
    • 84923233765 scopus 로고    scopus 로고
    • Legal but lethal: functional protein aggregation at the verge of toxicity
    • Falsone, A., Falsone, S.F., Legal but lethal: functional protein aggregation at the verge of toxicity. Front. Cell. Neurosci., 9, 2015, 45.
    • (2015) Front. Cell. Neurosci. , vol.9 , pp. 45
    • Falsone, A.1    Falsone, S.F.2
  • 43
    • 84961288468 scopus 로고    scopus 로고
    • Mitochondrial function in neuronal cells depends on p97/VCP/Cdc48-mediated quality control
    • Fang, L., et al. Mitochondrial function in neuronal cells depends on p97/VCP/Cdc48-mediated quality control. Front. Cell. Neurosci., 9, 2015, 16.
    • (2015) Front. Cell. Neurosci. , vol.9 , pp. 16
    • Fang, L.1
  • 44
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang, S., et al. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 98 (2001), 14422–14427.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.1
  • 45
    • 84940185085 scopus 로고    scopus 로고
    • Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions
    • Farrawell, N.E., et al. Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions. Sci. Rep., 5, 2015, 13416.
    • (2015) Sci. Rep. , vol.5 , pp. 13416
    • Farrawell, N.E.1
  • 46
    • 0142157600 scopus 로고    scopus 로고
    • Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice
    • Ferrante, R.J., et al. Histone deacetylase inhibition by sodium butyrate chemotherapy ameliorates the neurodegenerative phenotype in Huntington's disease mice. J. Neurosci. 23 (2003), 9418–9427.
    • (2003) J. Neurosci. , vol.23 , pp. 9418-9427
    • Ferrante, R.J.1
  • 47
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro, E., et al. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol. Dis. 23 (2006), 669–678.
    • (2006) Neurobiol. Dis. , vol.23 , pp. 669-678
    • Ferreiro, E.1
  • 49
    • 43449129732 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Huntington's disease
    • Finkbeiner, S., Mitra, S., The ubiquitin-proteasome pathway in Huntington's disease. Sci. World J. 8 (2008), 421–433.
    • (2008) Sci. World J. , vol.8 , pp. 421-433
    • Finkbeiner, S.1    Mitra, S.2
  • 50
    • 0041315902 scopus 로고    scopus 로고
    • Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane
    • Flierman, D., et al. Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane. J. Biol. Chem. 278 (2003), 34774–34782.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34774-34782
    • Flierman, D.1
  • 51
    • 84896111540 scopus 로고    scopus 로고
    • Loss of proteostasis induced by amyloid beta peptide in brain endothelial cells
    • Fonseca, A.C., et al. Loss of proteostasis induced by amyloid beta peptide in brain endothelial cells. Biochim. Biophys. Acta 1843 (2014), 1150–1161.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 1150-1161
    • Fonseca, A.C.1
  • 52
    • 84939989763 scopus 로고    scopus 로고
    • Cellular factors modulating the mechanism of tau protein aggregation
    • Fontaine, S.N., et al. Cellular factors modulating the mechanism of tau protein aggregation. Cell. Mol. Life Sci. 72 (2015), 1863–1879.
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 1863-1879
    • Fontaine, S.N.1
  • 53
    • 84862303631 scopus 로고    scopus 로고
    • ER stress inhibits neuronal death by promoting autophagy
    • Fouillet, A., et al. ER stress inhibits neuronal death by promoting autophagy. Autophagy 8 (2012), 915–926.
    • (2012) Autophagy , vol.8 , pp. 915-926
    • Fouillet, A.1
  • 54
    • 84903529679 scopus 로고    scopus 로고
    • Pharmacological stimulation of sigma-1 receptors has neurorestorative effects in experimental parkinsonism
    • Francardo, V., et al. Pharmacological stimulation of sigma-1 receptors has neurorestorative effects in experimental parkinsonism. Brain 137 (2014), 1998–2014.
    • (2014) Brain , vol.137 , pp. 1998-2014
    • Francardo, V.1
  • 55
    • 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., 5, 2013, a013169.
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5 , pp. a013169
    • Gardner, B.M.1
  • 56
    • 84954204422 scopus 로고    scopus 로고
    • Regulating extracellular proteostasis capacity through the unfolded protein response
    • Genereux, J.C., Wiseman, R.L., Regulating extracellular proteostasis capacity through the unfolded protein response. Prion 9 (2015), 10–21.
    • (2015) Prion , vol.9 , pp. 10-21
    • Genereux, J.C.1    Wiseman, R.L.2
  • 57
    • 84922460332 scopus 로고    scopus 로고
    • Delivering a disease-modifying treatment for Huntington's disease
    • Godinho, B.M.D.C., et al. Delivering a disease-modifying treatment for Huntington's disease. Drug. Discov. Today 20 (2015), 50–64.
    • (2015) Drug. Discov. Today , vol.20 , pp. 50-64
    • Godinho, B.M.D.C.1
  • 58
    • 84927566116 scopus 로고    scopus 로고
    • A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease
    • Gonzalez, M.A., et al. A novel mutation in VCP causes Charcot-Marie-Tooth Type 2 disease. Brain 137 (2014), 2897–2902.
    • (2014) Brain , vol.137 , pp. 2897-2902
    • Gonzalez, M.A.1
  • 59
    • 84863498486 scopus 로고    scopus 로고
    • Glucose regulated protein 78 diminishes alpha-synuclein neurotoxicity in a rat model of Parkinson disease
    • Gorbatyuk, M.S., et al. Glucose regulated protein 78 diminishes alpha-synuclein neurotoxicity in a rat model of Parkinson disease. Mol. Ther. 20 (2012), 1327–1337.
    • (2012) Mol. Ther. , vol.20 , pp. 1327-1337
    • Gorbatyuk, M.S.1
  • 60
    • 0037073748 scopus 로고    scopus 로고
    • Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion
    • Gosavi, N., et al. Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion. J. Biol. Chem. 277 (2002), 48984–48992.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48984-48992
    • Gosavi, N.1
  • 62
    • 0028979993 scopus 로고
    • Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro
    • Gregori, L., et al. Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro. J. Biol. Chem. 270 (1995), 19702–19708.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19702-19708
    • Gregori, L.1
  • 63
    • 78651394090 scopus 로고    scopus 로고
    • Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps
    • Groisman, B., et al. Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. J. Biol. Chem. 286 (2011), 1292–1300.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1292-1300
    • Groisman, B.1
  • 64
    • 84941139665 scopus 로고    scopus 로고
    • HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons
    • Guedes-Dias, P., et al. HDAC6 inhibition induces mitochondrial fusion, autophagic flux and reduces diffuse mutant huntingtin in striatal neurons. Biochim. Biophys. Acta 1852 (2015), 2484–2493.
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 2484-2493
    • Guedes-Dias, P.1
  • 65
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella, J.F., MacDonald, M.E., Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci. 1 (2000), 109–115.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 109-115
    • Gusella, J.F.1    MacDonald, M.E.2
  • 66
    • 66249137770 scopus 로고    scopus 로고
    • Sigma receptors suppress multiple aspects of microglial activation
    • Hall, A.A., et al. Sigma receptors suppress multiple aspects of microglial activation. Glia 57 (2009), 744–754.
    • (2009) Glia , vol.57 , pp. 744-754
    • Hall, A.A.1
  • 67
    • 84988811921 scopus 로고    scopus 로고
    • Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity
    • Halliday, M., et al. Partial restoration of protein synthesis rates by the small molecule ISRIB prevents neurodegeneration without pancreatic toxicity. Cell Death Dis., 6, 2015, e1672.
    • (2015) Cell Death Dis. , vol.6 , pp. e1672
    • Halliday, M.1
  • 68
    • 0028076031 scopus 로고
    • Folding of VSV G protein: sequential interaction with BiP and calnexin
    • Hammond, C., Helenius, A., Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266 (1994), 456–458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 69
    • 36849026845 scopus 로고    scopus 로고
    • A kinase inhibitor activates the IRE1alpha RNase to confer cytoprotection against ER stress
    • Han, D., et al. A kinase inhibitor activates the IRE1alpha RNase to confer cytoprotection against ER stress. Biochem. Biophys. Res. Commun. 365 (2008), 777–783.
    • (2008) Biochem. Biophys. Res. Commun. , vol.365 , pp. 777-783
    • Han, D.1
  • 70
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response
    • Harding, H.P., et al. 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
  • 71
    • 33749177143 scopus 로고    scopus 로고
    • A hundred years of Alzheimer's disease research
    • Hardy, J., A hundred years of Alzheimer's disease research. Neuron 52 (2006), 3–13.
    • (2006) Neuron , vol.52 , pp. 3-13
    • Hardy, J.1
  • 72
    • 84870937818 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperone and brain-derived neurotrophic factor: emerging links between cardiovascular disease and depression
    • Hashimoto, K., Sigma-1 receptor chaperone and brain-derived neurotrophic factor: emerging links between cardiovascular disease and depression. Prog. Neurobiol. 100 (2013), 15–29.
    • (2013) Prog. Neurobiol. , vol.100 , pp. 15-29
    • Hashimoto, K.1
  • 73
    • 20544440605 scopus 로고    scopus 로고
    • TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum
    • Hassink, G., et al. TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum. Biochem. J. 388 (2005), 647–655.
    • (2005) Biochem. J. , vol.388 , pp. 647-655
    • Hassink, G.1
  • 74
    • 84874872486 scopus 로고    scopus 로고
    • Putting huntingtin “aggregation” in view with windows into the cellular milieu
    • Hatters, D.M., Putting huntingtin “aggregation” in view with windows into the cellular milieu. Curr. Top. Med. Chem. 12 (2012), 2611–2622.
    • (2012) Curr. Top. Med. Chem. , vol.12 , pp. 2611-2622
    • Hatters, D.M.1
  • 75
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi, T., Su, T.P., Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 131 (2007), 596–610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.P.2
  • 76
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: protein folding, quality control, degradation, and related human diseases
    • Hebert, D.N., Molinari, M., In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol. Rev. 87 (2007), 1377–1408.
    • (2007) Physiol. Rev. , vol.87 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 77
    • 84866322000 scopus 로고    scopus 로고
    • Visualization of cell-to-cell transmission of mutant huntingtin oligomers
    • Herrera, F., et al. Visualization of cell-to-cell transmission of mutant huntingtin oligomers. PLoS Curr., 3, 2011, RRN1210.
    • (2011) PLoS Curr. , vol.3 , pp. RRN1210
    • Herrera, F.1
  • 78
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz, C., et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes. Dev. 23 (2009), 2294–2306.
    • (2009) Genes. Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1
  • 79
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C., Mollereau, B., Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15 (2014), 233–249.
    • (2014) Nat. Rev. Neurosci. , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 80
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz, C., Chevet, E., Harding, H.P., Targeting the unfolded protein response in disease. Nat. Rev. Drug. Discov. 12 (2013), 703–719.
    • (2013) Nat. Rev. Drug. Discov. , vol.12 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 81
    • 28244499949 scopus 로고    scopus 로고
    • Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response
    • Hidvegi, T., et al. Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response. J. Biol. Chem. 280 (2005), 39002–39015.
    • (2005) J. Biol. Chem. , vol.280 , pp. 39002-39015
    • Hidvegi, T.1
  • 82
    • 84859983420 scopus 로고    scopus 로고
    • Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease
    • Hipp, M.S., et al. Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease. J. Cell Biol. 196 (2012), 573–587.
    • (2012) J. Cell Biol. , vol.196 , pp. 573-587
    • Hipp, M.S.1
  • 83
    • 84906794886 scopus 로고    scopus 로고
    • Proteostasis impairment in protein-misfolding and -aggregation diseases
    • Hipp, M.S., Park, S.H., Hartl, F.U., Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol. 24 (2014), 506–514.
    • (2014) Trends Cell Biol. , vol.24 , pp. 506-514
    • Hipp, M.S.1    Park, S.H.2    Hartl, F.U.3
  • 84
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch, C., et al. The ubiquitylation machinery of the endoplasmic reticulum. Nature 458 (2009), 453–460.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1
  • 85
    • 9144223729 scopus 로고    scopus 로고
    • Inefficient degradation of truncated polyglutamine proteins by the proteasome
    • Holmberg, C.I., et al. Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J. 23 (2004), 4307–4318.
    • (2004) EMBO J. , vol.23 , pp. 4307-4318
    • Holmberg, C.I.1
  • 86
    • 33646188838 scopus 로고    scopus 로고
    • The unfolded protein response affects neuronal cell cycle protein expression: implications for Alzheimer's disease pathogenesis
    • Hoozemans, J.J., et al. The unfolded protein response affects neuronal cell cycle protein expression: implications for Alzheimer's disease pathogenesis. Exp. Gerontol. 41 (2006), 380–386.
    • (2006) Exp. Gerontol. , vol.41 , pp. 380-386
    • Hoozemans, J.J.1
  • 87
    • 33846605587 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in Parkinson's disease
    • Hoozemans, J.J., et al. Activation of the unfolded protein response in Parkinson's disease. Biochem. Biophys. Res. Commun. 354 (2007), 707–711.
    • (2007) Biochem. Biophys. Res. Commun. , vol.354 , pp. 707-711
    • Hoozemans, J.J.1
  • 88
    • 65349093893 scopus 로고    scopus 로고
    • The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus
    • Hoozemans, J.J., et al. The unfolded protein response is activated in pretangle neurons in Alzheimer's disease hippocampus. Am. J. Pathol. 174 (2009), 1241–1251.
    • (2009) Am. J. Pathol. , vol.174 , pp. 1241-1251
    • Hoozemans, J.J.1
  • 89
    • 77952811195 scopus 로고    scopus 로고
    • EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
    • Hosokawa, N., et al. EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans. Glycobiology 20 (2010), 567–575.
    • (2010) Glycobiology , vol.20 , pp. 567-575
    • Hosokawa, N.1
  • 90
    • 84929709547 scopus 로고    scopus 로고
    • Quantitative interaction proteomics of neurodegenerative disease proteins
    • Hosp, F., et al. Quantitative interaction proteomics of neurodegenerative disease proteins. Cell Rep. 11 (2015), 1134–1146.
    • (2015) Cell Rep. , vol.11 , pp. 1134-1146
    • Hosp, F.1
  • 91
    • 84879392732 scopus 로고    scopus 로고
    • Sigma-1 receptor agonist PRE084 is protective against mutant huntingtin-induced cell degeneration: involvement of calpastatin and the NF-kappaB pathway
    • Hyrskyluoto, A., et al. Sigma-1 receptor agonist PRE084 is protective against mutant huntingtin-induced cell degeneration: involvement of calpastatin and the NF-kappaB pathway. Cell Death Dis., 4, 2013, e646.
    • (2013) Cell Death Dis. , vol.4 , pp. e646
    • Hyrskyluoto, A.1
  • 92
    • 2542448088 scopus 로고    scopus 로고
    • Infiltration of the brain by pathogens causes Alzheimer's disease
    • Itzhaki, R.F., et al. Infiltration of the brain by pathogens causes Alzheimer's disease. Neurobiol. Aging 25 (2004), 619–627.
    • (2004) Neurobiol. Aging , vol.25 , pp. 619-627
    • Itzhaki, R.F.1
  • 93
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn, T.R., Radford, S.E., The Yin and Yang of protein folding. FEBS J. 272 (2005), 5962–5970.
    • (2005) FEBS J. , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 94
    • 84941198850 scopus 로고    scopus 로고
    • Evidence for human transmission of amyloid-beta pathology and cerebral amyloid angiopathy
    • Jaunmuktane, Z., et al. Evidence for human transmission of amyloid-beta pathology and cerebral amyloid angiopathy. Nature 525 (2015), 247–250.
    • (2015) Nature , vol.525 , pp. 247-250
    • Jaunmuktane, Z.1
  • 95
    • 84938212067 scopus 로고    scopus 로고
    • Targeting the IRE1alpha-XBP1 branch of the unfolded protein response in human diseases
    • Jiang, D., Niwa, M., Koong, A.C., Targeting the IRE1alpha-XBP1 branch of the unfolded protein response in human diseases. Semin. Cancer Biol. 33 (2015), 48–56.
    • (2015) Semin. Cancer Biol. , vol.33 , pp. 48-56
    • Jiang, D.1    Niwa, M.2    Koong, A.C.3
  • 97
    • 0035162691 scopus 로고    scopus 로고
    • A novel quality control compartment derived from the endoplasmic reticulum
    • Kamhi-Nesher, S., et al. A novel quality control compartment derived from the endoplasmic reticulum. Mol. Biol. Cell 12 (2001), 1711–1723.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1711-1723
    • Kamhi-Nesher, S.1
  • 98
    • 77949764687 scopus 로고    scopus 로고
    • Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation
    • Kaneko, M., et al. Loss of HRD1-mediated protein degradation causes amyloid precursor protein accumulation and amyloid-beta generation. J. Neurosci. 30 (2010), 3924–3932.
    • (2010) J. Neurosci. , vol.30 , pp. 3924-3932
    • Kaneko, M.1
  • 99
    • 84896837095 scopus 로고    scopus 로고
    • Hsp90-tau complex reveals molecular basis for specificity in chaperone action
    • Karagöz, G.E., et al. Hsp90-tau complex reveals molecular basis for specificity in chaperone action. Cell 156 (2014), 963–974.
    • (2014) Cell , vol.156 , pp. 963-974
    • Karagöz, G.E.1
  • 100
    • 84948717105 scopus 로고    scopus 로고
    • Huntingtin haplotypes provide prioritized target panels for allele-specific silencing in huntington disease patients of european ancestry
    • Kay, C., et al. Huntingtin haplotypes provide prioritized target panels for allele-specific silencing in huntington disease patients of european ancestry. Mol. Ther. 23 (2015), 1759–1771.
    • (2015) Mol. Ther. , vol.23 , pp. 1759-1771
    • Kay, C.1
  • 101
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003), 486–489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1
  • 102
    • 0036677435 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease
    • Keene, C.D., et al. Tauroursodeoxycholic acid, a bile acid, is neuroprotective in a transgenic animal model of Huntington's disease. Proc. Natl. Acad. Sci. USA 99 (2002), 10671–10676.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10671-10676
    • Keene, C.D.1
  • 103
    • 84927626719 scopus 로고    scopus 로고
    • PINK1-induced mitophagy promotes neuroprotection in Huntington's disease
    • Khalil, B., et al. PINK1-induced mitophagy promotes neuroprotection in Huntington's disease. Cell Death Dis., 6, 2015, e1617.
    • (2015) Cell Death Dis. , vol.6 , pp. e1617
    • Khalil, B.1
  • 104
    • 78049383942 scopus 로고    scopus 로고
    • Protein homeostasis in models of aging and age-related conformational disease
    • Kikis, E.A., Gidalevitz, T., Morimoto, R.I., Protein homeostasis in models of aging and age-related conformational disease. Adv. Exp. Med. Biol. 694 (2010), 138–159.
    • (2010) Adv. Exp. Med. Biol. , vol.694 , pp. 138-159
    • Kikis, E.A.1    Gidalevitz, T.2    Morimoto, R.I.3
  • 105
    • 9144239817 scopus 로고    scopus 로고
    • Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
    • Kikkert, M., et al. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J. Biol. Chem. 279 (2004), 3525–3534.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3525-3534
    • Kikkert, M.1
  • 106
    • 84906777179 scopus 로고    scopus 로고
    • Granulovacuolar degeneration and unfolded protein response in mouse models of tauopathy and Abeta amyloidosis
    • Kohler, C., Dinekov, M., Gotz, J., Granulovacuolar degeneration and unfolded protein response in mouse models of tauopathy and Abeta amyloidosis. Neurobiol. Dis. 71 (2014), 169–179.
    • (2014) Neurobiol. Dis. , vol.71 , pp. 169-179
    • Kohler, C.1    Dinekov, M.2    Gotz, J.3
  • 107
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame, K., et al. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol. Chem. 275 (2000), 32846–32853.
    • (2000) J Biol. Chem. , vol.275 , pp. 32846-32853
    • Kokame, K.1
  • 108
    • 34548651757 scopus 로고    scopus 로고
    • PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress
    • Kondratyev, M., et al. PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress. Exp. Cell Res. 313 (2007), 3395–3407.
    • (2007) Exp. Cell Res. , vol.313 , pp. 3395-3407
    • Kondratyev, M.1
  • 109
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • Kopito, R.R., Ron, D., Conformational disease. Nat. Cell Biol. 2 (2000), E207–E209.
    • (2000) Nat. Cell Biol. , vol.2 , pp. E207-E209
    • Kopito, R.R.1    Ron, D.2
  • 110
    • 84856958110 scopus 로고    scopus 로고
    • VCP mutations in familial and sporadic amyotrophic lateral sclerosis
    • 837
    • Koppers, M., et al. VCP mutations in familial and sporadic amyotrophic lateral sclerosis. Neurobiol. Aging 33 (2012), e7–13 837.
    • (2012) Neurobiol. Aging , vol.33 , pp. e7-13
    • Koppers, M.1
  • 111
    • 33646185061 scopus 로고    scopus 로고
    • Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)
    • Kreft, S.G., Wang, L., Hochstrasser, M., Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J. Biol. Chem. 281 (2006), 4646–4653.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4646-4653
    • Kreft, S.G.1    Wang, L.2    Hochstrasser, M.3
  • 112
    • 79961013560 scopus 로고    scopus 로고
    • Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease
    • Labbadia, J., et al. Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease. J. Clin. Investig. 121 (2011), 3306–3319.
    • (2011) J. Clin. Investig. , vol.121 , pp. 3306-3319
    • Labbadia, J.1
  • 113
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia, J., Morimoto, R.I., The biology of proteostasis in aging and disease. Annu. Rev. Biochem. 84 (2015), 435–464.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 435-464
    • Labbadia, J.1    Morimoto, R.I.2
  • 114
    • 78650811716 scopus 로고    scopus 로고
    • Formation and toxicity of soluble polyglutamine oligomers in living cells
    • Lajoie, P., Snapp, E.L., Formation and toxicity of soluble polyglutamine oligomers in living cells. PLoS One, 5, 2010, e15245.
    • (2010) PLoS One , vol.5 , pp. e15245
    • Lajoie, P.1    Snapp, E.L.2
  • 115
    • 0034730172 scopus 로고    scopus 로고
    • Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
    • Lam, Y.A., et al. Inhibition of the ubiquitin-proteasome system in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 97 (2000), 9902–9906.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9902-9906
    • Lam, Y.A.1
  • 116
    • 84962570989 scopus 로고    scopus 로고
    • N-Glycan-based ER molecular chaperone and protein quality control system: the calnexin binding cycle
    • Lamriben, L., et al. N-Glycan-based ER molecular chaperone and protein quality control system: the calnexin binding cycle. Traffic 17 (2016), 308–326.
    • (2016) Traffic , vol.17 , pp. 308-326
    • Lamriben, L.1
  • 117
    • 34948838383 scopus 로고    scopus 로고
    • Riluzole in Huntington's disease: a 3-year, randomized controlled study
    • Landwehrmeyer, G.B., et al. Riluzole in Huntington's disease: a 3-year, randomized controlled study. Ann. Neurol. 62 (2007), 262–272.
    • (2007) Ann. Neurol. , vol.62 , pp. 262-272
    • Landwehrmeyer, G.B.1
  • 118
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer, G.Z., Glycoprotein folding, quality control and ER-associated degradation. Curr. Opin. Struct. Biol. 19 (2009), 515–523.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 119
    • 83455169115 scopus 로고    scopus 로고
    • IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux
    • Lee, H., et al. IRE1 plays an essential role in ER stress-mediated aggregation of mutant huntingtin via the inhibition of autophagy flux. Hum. Mol. Genet. 21 (2012), 101–114.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 101-114
    • Lee, H.1
  • 120
    • 77956288847 scopus 로고    scopus 로고
    • Activation of PERK signaling attenuates Abeta-mediated ER stress
    • Lee do, Y., et al. Activation of PERK signaling attenuates Abeta-mediated ER stress. PLoS One, 5, 2010, e10489.
    • (2010) PLoS One , vol.5 , pp. e10489
    • Lee do, Y.1
  • 121
    • 84873027092 scopus 로고    scopus 로고
    • Compartmentalization of endoplasmic reticulum quality control and ER-associated degradation factors
    • Leitman, J., et al. Compartmentalization of endoplasmic reticulum quality control and ER-associated degradation factors. DNA Cell Biol. 32 (2013), 2–7.
    • (2013) DNA Cell Biol. , vol.32 , pp. 2-7
    • Leitman, J.1
  • 122
    • 84897002606 scopus 로고    scopus 로고
    • ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin
    • Leitman, J., et al. ER stress-induced eIF2-alpha phosphorylation underlies sensitivity of striatal neurons to pathogenic huntingtin. PLoS One, 9, 2014, e90803.
    • (2014) PLoS One , vol.9 , pp. e90803
    • Leitman, J.1
  • 123
    • 84898754350 scopus 로고    scopus 로고
    • Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD
    • Leitman, J., et al. Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD. Mol. Biol. Cell 25 (2014), 1050–1060.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 1050-1060
    • Leitman, J.1
  • 124
    • 84887792874 scopus 로고    scopus 로고
    • Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress
    • Leitman, J., Ulrich Hartl, F., Lederkremer, G.Z., Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress. Nat. Commun., 4, 2013, 2753.
    • (2013) Nat. Commun. , vol.4 , pp. 2753
    • Leitman, J.1    Ulrich Hartl, F.2    Lederkremer, G.Z.3
  • 125
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • Lin, J.H., et al. IRE1 signaling affects cell fate during the unfolded protein response. Science 318 (2007), 944–949.
    • (2007) Science , vol.318 , pp. 944-949
    • Lin, J.H.1
  • 126
    • 84876032962 scopus 로고    scopus 로고
    • New directions in ER stress-induced cell death
    • Logue, S.E., et al. New directions in ER stress-induced cell death. Apoptosis 18 (2013), 537–546.
    • (2013) Apoptosis , vol.18 , pp. 537-546
    • Logue, S.E.1
  • 127
    • 84946925426 scopus 로고    scopus 로고
    • Long term aggresome accumulation leads to dna damage, p53-dependent cell cycle arrest, and steric interference in mitosis
    • Lu, M., Boschetti, C., Tunnacliffe, A., Long term aggresome accumulation leads to dna damage, p53-dependent cell cycle arrest, and steric interference in mitosis. J. Biol. Chem. 290 (2015), 27986–28000.
    • (2015) J. Biol. Chem. , vol.290 , pp. 27986-28000
    • Lu, M.1    Boschetti, C.2    Tunnacliffe, A.3
  • 128
    • 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. 16 (2013), 1299–1305.
    • (2013) Nat. Neurosci. , vol.16 , pp. 1299-1305
    • Ma, T.1
  • 129
    • 77952583297 scopus 로고    scopus 로고
    • Protein quality control in the ER: the recognition of misfolded proteins
    • Maattanen, P., et al. Protein quality control in the ER: the recognition of misfolded proteins. Semin. Cell Dev. Biol. 21 (2010), 500–511.
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 500-511
    • Maattanen, P.1
  • 130
    • 85018400910 scopus 로고    scopus 로고
    • Neurodegenerative disease: VCP mutations lead to defects in mitochondrial dynamics
    • Malpass, K., Neurodegenerative disease: VCP mutations lead to defects in mitochondrial dynamics. Nat. Rev. Neurol., 9, 2013, 239.
    • (2013) Nat. Rev. Neurol. , vol.9 , pp. 239
    • Malpass, K.1
  • 131
    • 23044437134 scopus 로고    scopus 로고
    • Neuroprotective effects of sigma-1 receptor agonists against beta-amyloid-induced toxicity
    • Marrazzo, A., et al. Neuroprotective effects of sigma-1 receptor agonists against beta-amyloid-induced toxicity. Neuroreport 16 (2005), 1223–1226.
    • (2005) Neuroreport , vol.16 , pp. 1223-1226
    • Marrazzo, A.1
  • 132
    • 26444471905 scopus 로고    scopus 로고
    • Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates
    • Matsumoto, G., et al. Structural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates. J. Cell Biol. 171 (2005), 75–85.
    • (2005) J. Cell Biol. , vol.171 , pp. 75-85
    • Matsumoto, G.1
  • 133
    • 0035660075 scopus 로고    scopus 로고
    • The interaction between neuroactive steroids and the sigma1 receptor function: behavioral consequences and therapeutic opportunities
    • Maurice, T., et al. The interaction between neuroactive steroids and the sigma1 receptor function: behavioral consequences and therapeutic opportunities. Brain Res. Brain Res. Rev. 37 (2001), 116–132.
    • (2001) Brain Res. Brain Res. Rev. , vol.37 , pp. 116-132
    • Maurice, T.1
  • 134
    • 84885191322 scopus 로고    scopus 로고
    • Respiratory infection promotes T cell infiltration and amyloid-beta deposition in APP/PS1 mice
    • McManus, R.M., et al. Respiratory infection promotes T cell infiltration and amyloid-beta deposition in APP/PS1 mice. Neurobiol. Aging 35 (2014), 109–121.
    • (2014) Neurobiol. Aging , vol.35 , pp. 109-121
    • McManus, R.M.1
  • 135
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught, K.S., Jenner, P., Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297 (2001), 191–194.
    • (2001) Neurosci. Lett. , vol.297 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 136
    • 67349104211 scopus 로고    scopus 로고
    • Molecular mechanisms underlying polyalanine diseases
    • Messaed, C., Rouleau, G.A., Molecular mechanisms underlying polyalanine diseases. Neurobiol. Dis. 34 (2009), 397–405.
    • (2009) Neurobiol. Dis. , vol.34 , pp. 397-405
    • Messaed, C.1    Rouleau, G.A.2
  • 137
    • 84911862220 scopus 로고    scopus 로고
    • Sigma-1 receptor is involved in degradation of intranuclear inclusions in a cellular model of Huntington's disease
    • Miki, Y., et al. Sigma-1 receptor is involved in degradation of intranuclear inclusions in a cellular model of Huntington's disease. Neurobiol. Dis. 74 (2015), 25–31.
    • (2015) Neurobiol. Dis. , vol.74 , pp. 25-31
    • Miki, Y.1
  • 138
    • 3142582012 scopus 로고    scopus 로고
    • Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum
    • Miranda, E., Romisch, K., Lomas, D.A., Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum. J. Biol. Chem. 279 (2004), 28283–28291.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28283-28291
    • Miranda, E.1    Romisch, K.2    Lomas, D.A.3
  • 139
    • 63249135140 scopus 로고    scopus 로고
    • Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease
    • Mitra, S., Tsvetkov, A.S., Finkbeiner, S., Single neuron ubiquitin-proteasome dynamics accompanying inclusion body formation in huntington disease. J. Biol. Chem. 284 (2009), 4398–4403.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4398-4403
    • Mitra, S.1    Tsvetkov, A.S.2    Finkbeiner, S.3
  • 140
    • 84861450392 scopus 로고    scopus 로고
    • Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration
    • Moreno, J.A., et al. Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration. Nature 485 (2012), 507–511.
    • (2012) Nature , vol.485 , pp. 507-511
    • Moreno, J.A.1
  • 141
    • 84901317040 scopus 로고    scopus 로고
    • Recent technical developments in the study of ER-associated degradation
    • Nakatsukasa, K., Kamura, T., Brodsky, J.L., Recent technical developments in the study of ER-associated degradation. Curr. Opin. Cell Biol. 29c (2014), 82–91.
    • (2014) Curr. Opin. Cell Biol. , vol.29c , pp. 82-91
    • Nakatsukasa, K.1    Kamura, T.2    Brodsky, J.L.3
  • 142
    • 84923260646 scopus 로고    scopus 로고
    • Targeted excision of VCP R155H mutation by Cre-LoxP technology as a promising therapeutic strategy for valosin-containing protein disease
    • Nalbandian, A., et al. Targeted excision of VCP R155H mutation by Cre-LoxP technology as a promising therapeutic strategy for valosin-containing protein disease. Hum. Gene. Ther. Methods 26 (2015), 13–24.
    • (2015) Hum. Gene. Ther. Methods , vol.26 , pp. 13-24
    • Nalbandian, A.1
  • 143
    • 84929121456 scopus 로고    scopus 로고
    • Sigma-1 receptor directly interacts with Rac1-GTPase in the brain mitochondria
    • Natsvlishvili, N., et al. Sigma-1 receptor directly interacts with Rac1-GTPase in the brain mitochondria. BMC Biochem., 16, 2015, 11.
    • (2015) BMC Biochem. , vol.16 , pp. 11
    • Natsvlishvili, N.1
  • 144
    • 75649105019 scopus 로고    scopus 로고
    • Current treatment and recent clinical research in Alzheimer's disease
    • Neugroschl, J., Sano, M., Current treatment and recent clinical research in Alzheimer's disease. Mt. Sinai J. Med. 77 (2010), 3–16.
    • (2010) Mt. Sinai J. Med. , vol.77 , pp. 3-16
    • Neugroschl, J.1    Sano, M.2
  • 145
    • 84924047943 scopus 로고    scopus 로고
    • Role of sigma-1 receptors in neurodegenerative diseases
    • Nguyen, L., et al. Role of sigma-1 receptors in neurodegenerative diseases. J. Pharmacol. Sci. 127 (2015), 17–29.
    • (2015) J. Pharmacol. Sci. , vol.127 , pp. 17-29
    • Nguyen, L.1
  • 146
    • 84905987689 scopus 로고    scopus 로고
    • EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step
    • Ninagawa, S., et al. EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step. J. Cell Biol. 206 (2014), 347–356.
    • (2014) J. Cell Biol. , vol.206 , pp. 347-356
    • Ninagawa, S.1
  • 147
    • 44849124411 scopus 로고    scopus 로고
    • ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1
    • Nishitoh, H., et al. ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1. Genes. Dev. 22 (2008), 1451–1464.
    • (2008) Genes. Dev. , vol.22 , pp. 1451-1464
    • Nishitoh, H.1
  • 148
    • 84867485621 scopus 로고    scopus 로고
    • TUDCA, a bile acid, attenuates amyloid precursor protein processing and amyloid-beta deposition in APP/PS1 mice
    • Nunes, A.F., et al. TUDCA, a bile acid, attenuates amyloid precursor protein processing and amyloid-beta deposition in APP/PS1 mice. Mol. Neurobiol. 45 (2012), 440–454.
    • (2012) Mol. Neurobiol. , vol.45 , pp. 440-454
    • Nunes, A.F.1
  • 149
    • 57649245230 scopus 로고    scopus 로고
    • Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis
    • O'Connor, T., et al. Phosphorylation of the translation initiation factor eIF2alpha increases BACE1 levels and promotes amyloidogenesis. Neuron 60 (2008), 988–1009.
    • (2008) Neuron , vol.60 , pp. 988-1009
    • O'Connor, T.1
  • 150
    • 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. 10 (2015), 173–194.
    • (2015) Annu. Rev. Pathol. , vol.10 , pp. 173-194
    • Oakes, S.A.1    Papa, F.R.2
  • 151
    • 33748795800 scopus 로고    scopus 로고
    • EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
    • Olivari, S., et al. EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem. Biophys. Res. Commun. 349 (2006), 1278–1284.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1278-1284
    • Olivari, S.1
  • 152
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha, H., et al. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144 (2011), 67–78.
    • (2011) Cell , vol.144 , pp. 67-78
    • Olzscha, H.1
  • 153
    • 34548331451 scopus 로고    scopus 로고
    • Is the ubiquitin-proteasome system impaired in Huntington's disease?
    • Ortega, Z., Diaz-Hernandez, M., Lucas, J.J., Is the ubiquitin-proteasome system impaired in Huntington's disease?. Cell. Mol. Life Sci. 64 (2007), 2245–2257.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 2245-2257
    • Ortega, Z.1    Diaz-Hernandez, M.2    Lucas, J.J.3
  • 154
    • 84881478531 scopus 로고    scopus 로고
    • Potential for therapeutic manipulation of the UPR in disease
    • Park, S.W., Ozcan, U., Potential for therapeutic manipulation of the UPR in disease. Semin. Immunopathol. 35 (2013), 351–373.
    • (2013) Semin. Immunopathol. , vol.35 , pp. 351-373
    • Park, S.W.1    Ozcan, U.2
  • 155
    • 0020957538 scopus 로고
    • Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins
    • Parodi, A.J., Mendelzon, D.H., Lederkremer, G.Z., Transient glucosylation of protein-bound Man9GlcNAc2, Man8GlcNAc2, and Man7GlcNAc2 in calf thyroid cells. A possible recognition signal in the processing of glycoproteins. J. Biol. Chem. 258 (1983), 8260–8265.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8260-8265
    • Parodi, A.J.1    Mendelzon, D.H.2    Lederkremer, G.Z.3
  • 156
    • 84927949614 scopus 로고    scopus 로고
    • Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain
    • Pearce, M.M., et al. Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain. Nat. Commun., 6, 2015, 6768.
    • (2015) Nat. Commun. , vol.6 , pp. 6768
    • Pearce, M.M.1
  • 157
    • 84947474720 scopus 로고    scopus 로고
    • Comparative incidence of conformational, neurodegenerative disorders
    • de Pedro-Cuesta, J., et al. Comparative incidence of conformational, neurodegenerative disorders. PLoS One, 10, 2015, e0137342.
    • (2015) PLoS One , vol.10 , pp. e0137342
    • de Pedro-Cuesta, J.1
  • 158
    • 79551604651 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates
    • Perlmutter, D.H., Alpha-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates. Annu. Rev. Med. 62 (2011), 333–345.
    • (2011) Annu. Rev. Med. , vol.62 , pp. 333-345
    • Perlmutter, D.H.1
  • 159
    • 11144356089 scopus 로고    scopus 로고
    • CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli, L., et al. CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum. Mol. Genet. 13 (2004), 703–714.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 703-714
    • Petrucelli, L.1
  • 160
    • 84949511959 scopus 로고    scopus 로고
    • Polyalanine expansions drive a shift into alpha-helical clusters without amyloid-fibril formation
    • Polling, S., et al. Polyalanine expansions drive a shift into alpha-helical clusters without amyloid-fibril formation. Nat. Struct. Mol. Biol. 22 (2015), 1008–1015.
    • (2015) Nat. Struct. Mol. Biol. , vol.22 , pp. 1008-1015
    • Polling, S.1
  • 161
    • 84857953079 scopus 로고    scopus 로고
    • The unfolded protein response in models of human mutant G93A amyotrophic lateral sclerosis
    • Prell, T., et al. The unfolded protein response in models of human mutant G93A amyotrophic lateral sclerosis. Eur. J. Neurosci. 35 (2012), 652–660.
    • (2012) Eur. J. Neurosci. , vol.35 , pp. 652-660
    • Prell, T.1
  • 162
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., et al. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell Biol. 22 (2002), 626–634.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1
  • 163
    • 84942082866 scopus 로고    scopus 로고
    • Neurobiology of Alzheimer's disease: integrated molecular, physiological, anatomical, biomarker, and cognitive dimensions
    • Raskin, J., et al. Neurobiology of Alzheimer's disease: integrated molecular, physiological, anatomical, biomarker, and cognitive dimensions. Curr. Alzheimer Res. 12 (2015), 712–722.
    • (2015) Curr. Alzheimer Res. , vol.12 , pp. 712-722
    • Raskin, J.1
  • 164
    • 80655144729 scopus 로고    scopus 로고
    • Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1
    • Ron, E., et al. Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1. Mol. Biol. Cell 22 (2011), 3945–3954.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3945-3954
    • Ron, E.1
  • 165
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Suppl, S10-7
    • Ross, C.A., Poirier, M.A., Protein aggregation and neurodegenerative disease. Nat. Med., 10, 2004 Suppl, S10-7.
    • (2004) Nat. Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 166
    • 84912572110 scopus 로고    scopus 로고
    • Modulation of the maladaptive stress response to manage diseases of protein folding
    • Roth, D.M., et al. Modulation of the maladaptive stress response to manage diseases of protein folding. PLoS Biol., 12, 2014, e1001998.
    • (2014) PLoS Biol. , vol.12 , pp. e1001998
    • Roth, D.M.1
  • 167
    • 60849093466 scopus 로고    scopus 로고
    • Current hypotheses for the underlying biology of amyotrophic lateral sclerosis
    • Rothstein, J.D., Current hypotheses for the underlying biology of amyotrophic lateral sclerosis. Ann. Neurol. 65:Suppl 1 (2009), S3–S9.
    • (2009) Ann. Neurol. , vol.65 , pp. S3-S9
    • Rothstein, J.D.1
  • 168
    • 80053603907 scopus 로고    scopus 로고
    • Unravelling the twists and turns of the serpinopathies
    • Roussel, B.D., et al. Unravelling the twists and turns of the serpinopathies. FEBS J. 278 (2011), 3859–3867.
    • (2011) FEBS J. , vol.278 , pp. 3859-3867
    • Roussel, B.D.1
  • 169
    • 84870838478 scopus 로고    scopus 로고
    • Endoplasmic reticulum dysfunction in neurological disease
    • Roussel, B.D., et al. Endoplasmic reticulum dysfunction in neurological disease. Lancet Neurol. 12 (2013), 105–118.
    • (2013) Lancet Neurol. , vol.12 , pp. 105-118
    • Roussel, B.D.1
  • 170
    • 63349104307 scopus 로고    scopus 로고
    • Protective effect against Parkinson's disease-related insults through the activation of XBP1
    • Sado, M., et al. Protective effect against Parkinson's disease-related insults through the activation of XBP1. Brain Res. 1257 (2009), 16–24.
    • (2009) Brain Res. , vol.1257 , pp. 16-24
    • Sado, M.1
  • 171
    • 77950853379 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis
    • Sasaki, S., Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J. Neuropathol. Exp. Neurol. 69 (2010), 346–355.
    • (2010) J. Neuropathol. Exp. Neurol. , vol.69 , pp. 346-355
    • Sasaki, S.1
  • 172
    • 3042717240 scopus 로고    scopus 로고
    • Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation
    • Schaffar, G., et al. Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol. Cell 15 (2004), 95–105.
    • (2004) Mol. Cell , vol.15 , pp. 95-105
    • Schaffar, G.1
  • 173
    • 84939562716 scopus 로고    scopus 로고
    • The unfolded protein response in neurodegenerative diseases: a neuropathological perspective
    • Scheper, W., Hoozemans, J.J., The unfolded protein response in neurodegenerative diseases: a neuropathological perspective. Acta Neuropathol. 130 (2015), 315–331.
    • (2015) Acta Neuropathol. , vol.130 , pp. 315-331
    • Scheper, W.1    Hoozemans, J.J.2
  • 174
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder, M., Kaufman, R.J., The mammalian unfolded protein response. Annu. Rev. Biochem. 74 (2005), 739–789.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 175
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway
    • Schulze, A., et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J. Mol. Biol. 354 (2005), 1021–1027.
    • (2005) J. Mol. Biol. , vol.354 , pp. 1021-1027
    • Schulze, A.1
  • 176
    • 84990896014 scopus 로고    scopus 로고
    • Polyglutamine aggregation in Huntington's disease and spinocerebellar ataxia type 3: similar mechanisms in aggregate formation
    • Seidel, K., et al. Polyglutamine aggregation in Huntington's disease and spinocerebellar ataxia type 3: similar mechanisms in aggregate formation. Neuropathol. Appl. Neurobiol., 2015.
    • (2015) Neuropathol. Appl. Neurobiol.
    • Seidel, K.1
  • 177
    • 37849030901 scopus 로고    scopus 로고
    • Polyglutamine diseases: emerging concepts in pathogenesis and therapy
    • Spec No. 2
    • Shao, J., Diamond, M.I., Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum. Mol. Genet. 16 (2007), R115–R123 Spec No. 2.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. R115-R123
    • Shao, J.1    Diamond, M.I.2
  • 178
    • 84991007871 scopus 로고    scopus 로고
    • Genesis of ER stress in huntington's disease
    • Shenkman, M., Eiger, H., Lederkremer, G.Z., Genesis of ER stress in huntington's disease. ER Stress Dis. 2 (2015), 94–106.
    • (2015) ER Stress Dis. , vol.2 , pp. 94-106
    • Shenkman, M.1    Eiger, H.2    Lederkremer, G.Z.3
  • 179
    • 84876991539 scopus 로고    scopus 로고
    • Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments
    • Shoulders, M.D., et al. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep. 3 (2013), 1279–1292.
    • (2013) Cell Rep. , vol.3 , pp. 1279-1292
    • Shoulders, M.D.1
  • 180
    • 84881530677 scopus 로고    scopus 로고
    • Pharmacological brake-release of mRNA translation enhances cognitive memory
    • Sidrauski, C., et al. Pharmacological brake-release of mRNA translation enhances cognitive memory. Elife, 2, 2013, e00498.
    • (2013) Elife , vol.2 , pp. e00498
    • Sidrauski, C.1
  • 181
    • 28244466782 scopus 로고    scopus 로고
    • CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism
    • Silva, R.M., et al. CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism. J. Neurochem. 95 (2005), 974–986.
    • (2005) J. Neurochem. , vol.95 , pp. 974-986
    • Silva, R.M.1
  • 182
    • 84880606810 scopus 로고    scopus 로고
    • Disorders of protein misfolding: alpha-1-antitrypsin deficiency as prototype
    • Silverman, G.A., Pak, S.C., Perlmutter, D.H., Disorders of protein misfolding: alpha-1-antitrypsin deficiency as prototype. J. Pediatr. 163 (2013), 320–326.
    • (2013) J. Pediatr. , vol.163 , pp. 320-326
    • Silverman, G.A.1    Pak, S.C.2    Perlmutter, D.H.3
  • 183
    • 20144385980 scopus 로고    scopus 로고
    • PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis
    • Simmen, T., et al. PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis. EMBO J. 24 (2005), 717–729.
    • (2005) EMBO J. , vol.24 , pp. 717-729
    • Simmen, T.1
  • 184
    • 84929274276 scopus 로고    scopus 로고
    • Molecular chaperones and neuronal proteostasis
    • Smith, H.L., Li, W., Cheetham, M.E., Molecular chaperones and neuronal proteostasis. Semin. Cell Dev. Biol. 40 (2015), 142–152.
    • (2015) Semin. Cell Dev. Biol. , vol.40 , pp. 142-152
    • Smith, H.L.1    Li, W.2    Cheetham, M.E.3
  • 185
    • 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, S.E., et al. Activating transcription factor 6 limits intracellular accumulation of mutant alpha(1)-antitrypsin Z and mitochondrial damage in hepatoma cells. J. Biol. Chem. 286 (2011), 41563–41577.
    • (2011) J. Biol. Chem. , vol.286 , pp. 41563-41577
    • Smith, S.E.1
  • 186
    • 84881426112 scopus 로고    scopus 로고
    • Intracellular accumulation of toxic turn amyloid-beta is associated with endoplasmic reticulum stress in Alzheimer's disease
    • Soejima, N., et al. Intracellular accumulation of toxic turn amyloid-beta is associated with endoplasmic reticulum stress in Alzheimer's disease. Curr. Alzheimer Res. 10 (2013), 11–20.
    • (2013) Curr. Alzheimer Res. , vol.10 , pp. 11-20
    • Soejima, N.1
  • 188
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003), 49–60.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 189
    • 84944750508 scopus 로고    scopus 로고
    • beta-Amyloid: the key peptide in the pathogenesis of Alzheimer's disease
    • Sun, X., Chen, W.D., Wang, Y.D., beta-Amyloid: the key peptide in the pathogenesis of Alzheimer's disease. Front. Pharmacol., 6, 2015, 221.
    • (2015) Front. Pharmacol. , vol.6 , pp. 221
    • Sun, X.1    Chen, W.D.2    Wang, Y.D.3
  • 190
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas, I., Ron, D., Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 13 (2011), 184–190.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 191
    • 38349158062 scopus 로고    scopus 로고
    • Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic
    • Takahashi, T., et al. Soluble polyglutamine oligomers formed prior to inclusion body formation are cytotoxic. Hum. Mol. Genet. 17 (2008), 345–356.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 345-356
    • Takahashi, T.1
  • 192
    • 84931565973 scopus 로고    scopus 로고
    • N-linked sugar-regulated protein folding and quality control in the ER
    • Tannous, A., et al. N-linked sugar-regulated protein folding and quality control in the ER. Semin. Cell Dev. Biol. 41 (2015), 79–89.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 79-89
    • Tannous, A.1
  • 193
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J.P., Hardy, J., Fischbeck, K.H., Toxic proteins in neurodegenerative disease. Science 296 (2002), 1991–1995.
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 194
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler, P., et al. 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
  • 195
    • 77956254963 scopus 로고    scopus 로고
    • Parkin directly modulates 26S proteasome activity
    • Um, J.W., et al. Parkin directly modulates 26S proteasome activity. J. Neurosci. 30 (2010), 11805–11814.
    • (2010) J. Neurosci. , vol.30 , pp. 11805-11814
    • Um, J.W.1
  • 196
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • Urano, F., et al. 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
  • 197
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy
    • Vidal, R.L., et al. Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy. Hum. Mol. Genet. 21 (2012), 2245–2262.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2245-2262
    • Vidal, R.L.1
  • 198
    • 84942615942 scopus 로고    scopus 로고
    • Guanabenz treatment accelerates disease in a mutant SOD1 mouse model of ALS
    • Vieira, F.G., et al. Guanabenz treatment accelerates disease in a mutant SOD1 mouse model of ALS. PLoS One, 10, 2015, e0135570.
    • (2015) PLoS One , vol.10 , pp. e0135570
    • Vieira, F.G.1
  • 199
    • 84937392013 scopus 로고    scopus 로고
    • Neurodegenerative diseases: expanding the prion concept
    • Walker, L.C., Jucker, M., Neurodegenerative diseases: expanding the prion concept. Annu. Rev. Neurosci. 38 (2015), 87–103.
    • (2015) Annu. Rev. Neurosci. , vol.38 , pp. 87-103
    • Walker, L.C.1    Jucker, M.2
  • 200
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh, D.M., et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002), 535–539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 201
    • 84928963751 scopus 로고    scopus 로고
    • Widespread Proteome Remodeling and Aggregation in Aging C. elegans
    • Walther, D.M., et al. Widespread Proteome Remodeling and Aggregation in Aging C. elegans. Cell 161 (2015), 919–932.
    • (2015) Cell , vol.161 , pp. 919-932
    • Walther, D.M.1
  • 202
    • 84943339574 scopus 로고    scopus 로고
    • Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates
    • Wear, M.P., et al. Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates. PLS One, 10, 2015, e0136362.
    • (2015) PLS One , vol.10 , pp. e0136362
    • Wear, M.P.1
  • 203
    • 38849146956 scopus 로고    scopus 로고
    • ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones
    • Wei, H., et al. ER and oxidative stresses are common mediators of apoptosis in both neurodegenerative and non-neurodegenerative lysosomal storage disorders and are alleviated by chemical chaperones. Hum. Mol. Genet. 17 (2008), 469–477.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 469-477
    • Wei, H.1
  • 204
    • 31144470450 scopus 로고    scopus 로고
    • Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation
    • Weihl, C.C., et al. Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation. Hum. Mol. Genet. 15 (2006), 189–199.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 189-199
    • Weihl, C.C.1
  • 205
    • 79955979595 scopus 로고    scopus 로고
    • Phenylbutyric acid reduces amyloid plaques and rescues cognitive behavior in AD transgenic mice
    • Wiley, J.C., Pettan-Brewer, C., Ladiges, W.C., Phenylbutyric acid reduces amyloid plaques and rescues cognitive behavior in AD transgenic mice. Aging Cell 10 (2011), 418–428.
    • (2011) Aging Cell , vol.10 , pp. 418-428
    • Wiley, J.C.1    Pettan-Brewer, C.2    Ladiges, W.C.3
  • 206
    • 84955098544 scopus 로고    scopus 로고
    • Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA
    • Woerner, A.C., et al. Cytoplasmic protein aggregates interfere with nucleocytoplasmic transport of protein and RNA. Science 351 (2016), 173–176.
    • (2016) Science , vol.351 , pp. 173-176
    • Woerner, A.C.1
  • 207
    • 80053564708 scopus 로고    scopus 로고
    • Amyloid in neurodegenerative diseases: friend or foe?
    • Wolfe, K.J., Cyr, D.M., Amyloid in neurodegenerative diseases: friend or foe?. Semin. Cell Dev. Biol. 22 (2011), 476–481.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 476-481
    • Wolfe, K.J.1    Cyr, D.M.2
  • 208
    • 77749270634 scopus 로고    scopus 로고
    • Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP
    • Yang, H., et al. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP. PLoS One, 5, 2010, e8905.
    • (2010) PLoS One , vol.5 , pp. e8905
    • Yang, H.1
  • 209
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H.H., Rapoport, T.A., Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162 (2003), 71–84.
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 210
    • 33745019916 scopus 로고    scopus 로고
    • Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses
    • Yu, M.S., et al. Beta-amyloid peptides induces neuronal apoptosis via a mechanism independent of unfolded protein responses. Apoptosis 11 (2006), 687–700.
    • (2006) Apoptosis , vol.11 , pp. 687-700
    • Yu, M.S.1
  • 211
    • 84862209309 scopus 로고    scopus 로고
    • A BAX/BAK and cyclophilin D-independent intrinsic apoptosis pathway
    • Zamorano, S., et al. A BAX/BAK and cyclophilin D-independent intrinsic apoptosis pathway. PLoS One, 7, 2012, e37782.
    • (2012) PLoS One , vol.7 , pp. e37782
    • Zamorano, S.1
  • 212
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun, A., et al. Conformation-independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88 (1997), 29–38.
    • (1997) Cell , vol.88 , pp. 29-38
    • Zapun, A.1
  • 213
    • 84859609686 scopus 로고    scopus 로고
    • Huntington disease and the huntingtin protein
    • Zheng, Z., Diamond, M.I., Huntington disease and the huntingtin protein. Prog. Mol. Biol. Transl. Sci. 107 (2012), 189–214.
    • (2012) Prog. Mol. Biol. Transl. Sci. , vol.107 , pp. 189-214
    • Zheng, Z.1    Diamond, M.I.2
  • 214
    • 84923225433 scopus 로고    scopus 로고
    • Update on Huntington's disease: advances in care and emerging therapeutic options
    • Zielonka, D., Mielcarek, M., Landwehrmeyer, G.B., Update on Huntington's disease: advances in care and emerging therapeutic options. Park. Relat. Disord. 21 (2015), 169–178.
    • (2015) Park. Relat. Disord. , vol.21 , pp. 169-178
    • Zielonka, D.1    Mielcarek, M.2    Landwehrmeyer, G.B.3
  • 215
    • 0032054744 scopus 로고    scopus 로고
    • CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum
    • Zinszner, H., et al. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes. Dev. 12 (1998), 982–995.
    • (1998) Genes. Dev. , vol.12 , pp. 982-995
    • Zinszner, H.1
  • 216
    • 84859577308 scopus 로고    scopus 로고
    • AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington's disease
    • Zuleta, A., et al. AAV-mediated delivery of the transcription factor XBP1s into the striatum reduces mutant Huntingtin aggregation in a mouse model of Huntington's disease. Biochem. Biophys. Res. Commun. 420 (2012), 558–563.
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 558-563
    • Zuleta, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.