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Volumn 1648, Issue , 2016, Pages 561-570

Gene therapy to target ER stress in brain diseases

Author keywords

Alzheimer's disease; Amyotrophic lateral sclerosis; Endoplasmic reticulum stress; Gene therapy; Parkinson's disease; Unfolded protein response

Indexed keywords

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; BRAIN DISEASE; DEGENERATIVE DISEASE; ENDOPLASMIC RETICULUM STRESS; GENE THERAPY; HUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN HOMEOSTASIS; REVIEW; ANIMAL; DEPENDOPARVOVIRUS; GENETICS; PHYSIOLOGY; PROCEDURES; UNFOLDED PROTEIN RESPONSE;

EID: 84966708289     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2016.04.064     Document Type: Review
Times cited : (32)

References (144)
  • 2
    • 33847134439 scopus 로고    scopus 로고
    • Neuronal polarity: from extracellular signals to intracellular mechanisms
    • Arimura, N., Kaibuchi, K., Neuronal polarity: from extracellular signals to intracellular mechanisms. Nat. Rev. Neurosci. 8 (2007), 194–205.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 194-205
    • Arimura, N.1    Kaibuchi, K.2
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W.E., Morimoto, R.I., Dillin, A., Kelly, J.W., Adapting proteostasis for disease intervention. Science 319 (2008), 916–919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 7
    • 84990948204 scopus 로고    scopus 로고
    • Calreticulin levels determine onset of early muscle denervation by fast motoneurons of ALS model mice
    • Bernard-Marissal, N., Sunyach, C., Marissal, T., Raoul, C., Pettmann, B., Calreticulin levels determine onset of early muscle denervation by fast motoneurons of ALS model mice. Neurobiol. Dis., 2014.
    • (2014) Neurobiol. Dis.
    • Bernard-Marissal, N.1    Sunyach, C.2    Marissal, T.3    Raoul, C.4    Pettmann, B.5
  • 9
    • 84901832947 scopus 로고    scopus 로고
    • Systemic gene delivery to the central nervous system using Adeno-associated virus
    • Bourdenx, M., Dutheil, N., Bezard, E., Dehay, B., Systemic gene delivery to the central nervous system using Adeno-associated virus. Front. Mol. Neurosci., 7, 2014, 50.
    • (2014) Front. Mol. Neurosci. , vol.7 , pp. 50
    • Bourdenx, M.1    Dutheil, N.2    Bezard, E.3    Dehay, B.4
  • 10
    • 77955790177 scopus 로고    scopus 로고
    • Protein homeostasis and synaptic plasticity
    • Cajigas, I.J., Will, T., Schuman, E.M., Protein homeostasis and synaptic plasticity. EMBO J. 29 (2010), 2746–2752.
    • (2010) EMBO J. , vol.29 , pp. 2746-2752
    • Cajigas, I.J.1    Will, T.2    Schuman, E.M.3
  • 12
    • 84938262536 scopus 로고    scopus 로고
    • Gene therapy in Parkinson's disease: targeting the endplasmic reticulum proteostasis network
    • Castillo, V., Mercado, G., Hetz, C., Gene therapy in Parkinson's disease: targeting the endplasmic reticulum proteostasis network. Neural Regen. Res. 10 (2015), 1053–1054.
    • (2015) Neural Regen. Res. , vol.10 , pp. 1053-1054
    • Castillo, V.1    Mercado, G.2    Hetz, C.3
  • 16
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla, E., Jensen, P.H., Pletnikova, O., Troncoso, J.C., Glabe, C., Lee, M.K., Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J. Neurosci.: Off. J. Soc. Neurosci. 32 (2012), 3301–3305.
    • (2012) J. Neurosci.: Off. J. Soc. Neurosci. , vol.32 , pp. 3301-3305
    • Colla, E.1    Jensen, P.H.2    Pletnikova, O.3    Troncoso, J.C.4    Glabe, C.5    Lee, M.K.6
  • 17
    • 4444237848 scopus 로고    scopus 로고
    • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology
    • Conn, K.J., Gao, W., McKee, A., Lan, M.S., Ullman, M.D., Eisenhauer, P.B., Fine, R.E., Wells, J.M., Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. Brain Res. 1022 (2004), 164–172.
    • (2004) Brain Res. , vol.1022 , pp. 164-172
    • Conn, K.J.1    Gao, W.2    McKee, A.3    Lan, M.S.4    Ullman, M.D.5    Eisenhauer, P.B.6    Fine, R.E.7    Wells, J.M.8
  • 19
    • 84881479630 scopus 로고    scopus 로고
    • The unfolded protein response in Alzheimer's disease
    • Cornejo, V.H., Hetz, C., The unfolded protein response in Alzheimer's disease. Semin. Immunopathol. 35 (2013), 277–292.
    • (2013) Semin. Immunopathol. , vol.35 , pp. 277-292
    • Cornejo, V.H.1    Hetz, C.2
  • 21
    • 58149469090 scopus 로고    scopus 로고
    • Translational control of long-lasting synaptic plasticity and memory
    • Costa-Mattioli, M., Sossin, W.S., Klann, E., Sonenberg, N., Translational control of long-lasting synaptic plasticity and memory. Neuron 61 (2009), 10–26.
    • (2009) Neuron , vol.61 , pp. 10-26
    • Costa-Mattioli, M.1    Sossin, W.S.2    Klann, E.3    Sonenberg, N.4
  • 22
    • 84857834456 scopus 로고    scopus 로고
    • Rab1A over-expression prevents Golgi apparatus fragmentation and partially corrects motor deficits in an alpha-synuclein based rat model of Parkinson's disease
    • Coune, P.G., Bensadoun, J.C., Aebischer, P., Schneider, B.L., Rab1A over-expression prevents Golgi apparatus fragmentation and partially corrects motor deficits in an alpha-synuclein based rat model of Parkinson's disease. J. Parkinson's Dis. 1 (2011), 373–387.
    • (2011) J. Parkinson's Dis. , vol.1 , pp. 373-387
    • Coune, P.G.1    Bensadoun, J.C.2    Aebischer, P.3    Schneider, B.L.4
  • 24
    • 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., Forcelli, P.A., Delannoy, M., Oaks, A.W., Permaul, E., Berry, D.L., Duka, V., Wills, J., Sidhu, A., 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    Forcelli, P.A.2    Delannoy, M.3    Oaks, A.W.4    Permaul, E.5    Berry, D.L.6    Duka, V.7    Wills, J.8    Sidhu, A.9
  • 29
    • 84885398154 scopus 로고    scopus 로고
    • Deletion of the eIF2alpha Kinase GCN2 fails to rescue the memory decline associated with Alzheimer's disease
    • Devi, L., Ohno, M., Deletion of the eIF2alpha Kinase GCN2 fails to rescue the memory decline associated with Alzheimer's disease. PLoS One, 8, 2013, e77335.
    • (2013) PLoS One , vol.8 , pp. e77335
    • Devi, L.1    Ohno, M.2
  • 30
    • 84990976938 scopus 로고    scopus 로고
    • PharmaSphere: Emerging Biotechnologies – Gene Therapy Market Analysis, vol
    • 1, ed. GlobalData
    • Dion, A., 2015. PharmaSphere: Emerging Biotechnologies – Gene Therapy Market Analysis, vol. 1, ed. GlobalData.
    • (2015)
    • Dion, A.1
  • 32
    • 34547114745 scopus 로고    scopus 로고
    • IRE1 signaling is essential for ischemia-induced vascular endothelial growth factor-A expression and contributes to angiogenesis and tumor growth in vivo
    • Drogat, B., Auguste, P., Nguyen, D.T., Bouchecareilh, M., Pineau, R., Nalbantoglu, J., Kaufman, R.J., Chevet, E., Bikfalvi, A., Moenner, M., IRE1 signaling is essential for ischemia-induced vascular endothelial growth factor-A expression and contributes to angiogenesis and tumor growth in vivo. Cancer Res. 67 (2007), 6700–6707.
    • (2007) Cancer Res. , vol.67 , pp. 6700-6707
    • Drogat, B.1    Auguste, P.2    Nguyen, D.T.3    Bouchecareilh, M.4    Pineau, R.5    Nalbantoglu, J.6    Kaufman, R.J.7    Chevet, E.8    Bikfalvi, A.9    Moenner, M.10
  • 34
    • 84895811770 scopus 로고    scopus 로고
    • Memory loss in Alzheimer's disease: are the alterations in the UPR network involved in the cognitive impairment?
    • Duran-Aniotz, C., Martinez, G., Hetz, C., Memory loss in Alzheimer's disease: are the alterations in the UPR network involved in the cognitive impairment?. Front. Aging Neurosci., 6, 2014, 8.
    • (2014) Front. Aging Neurosci. , vol.6 , pp. 8
    • Duran-Aniotz, C.1    Martinez, G.2    Hetz, C.3
  • 35
    • 79953148080 scopus 로고    scopus 로고
    • The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death
    • Egawa, N., Yamamoto, K., Inoue, H., Hikawa, R., Nishi, K., Mori, K., Takahashi, R., The endoplasmic reticulum stress sensor, ATF6alpha, protects against neurotoxin-induced dopaminergic neuronal death. J. Biol. Chem. 286 (2011), 7947–7957.
    • (2011) J. Biol. Chem. , vol.286 , pp. 7947-7957
    • Egawa, N.1    Yamamoto, K.2    Inoue, H.3    Hikawa, R.4    Nishi, K.5    Mori, K.6    Takahashi, R.7
  • 37
    • 0028534879 scopus 로고
    • Adeno-associated virus vector gene expression occurs in nondividing cells in the absence of vector DNA integration
    • Flotte, T.R., Afione, S.A., Zeitlin, P.L., Adeno-associated virus vector gene expression occurs in nondividing cells in the absence of vector DNA integration. Am. J. Respir. Cell Mol. Biol. 11 (1994), 517–521.
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.11 , pp. 517-521
    • Flotte, T.R.1    Afione, S.A.2    Zeitlin, P.L.3
  • 38
    • 38649088555 scopus 로고    scopus 로고
    • Neonatal intraperitoneal or intravenous injections of recombinant adeno-associated virus type 8 transduce dorsal root ganglia and lower motor neurons
    • Foust, K.D., Poirier, A., Pacak, C.A., Mandel, R.J., Flotte, T.R., Neonatal intraperitoneal or intravenous injections of recombinant adeno-associated virus type 8 transduce dorsal root ganglia and lower motor neurons. Hum. Gene Ther. 19 (2008), 61–70.
    • (2008) Hum. Gene Ther. , vol.19 , pp. 61-70
    • Foust, K.D.1    Poirier, A.2    Pacak, C.A.3    Mandel, R.J.4    Flotte, T.R.5
  • 40
    • 84962106972 scopus 로고    scopus 로고
    • The UPR and synaptic dysfunction in neurodegeneration
    • Freeman, O.J., Mallucci, G.R., The UPR and synaptic dysfunction in neurodegeneration. Brain Res., 2016.
    • (2016) Brain Res.
    • Freeman, O.J.1    Mallucci, G.R.2
  • 46
    • 80052982705 scopus 로고    scopus 로고
    • Optimizing promoters for recombinant adeno-associated virus-mediated gene expression in the peripheral and central nervous system using self-complementary vectors
    • Gray, S.J., Foti, S.B., Schwartz, J.W., Bachaboina, L., Taylor-Blake, B., Coleman, J., Ehlers, M.D., Zylka, M.J., McCown, T.J., Samulski, R.J., Optimizing promoters for recombinant adeno-associated virus-mediated gene expression in the peripheral and central nervous system using self-complementary vectors. Hum. Gene Ther. 22 (2011), 1143–1153.
    • (2011) Hum. Gene Ther. , vol.22 , pp. 1143-1153
    • Gray, S.J.1    Foti, S.B.2    Schwartz, J.W.3    Bachaboina, L.4    Taylor-Blake, B.5    Coleman, J.6    Ehlers, M.D.7    Zylka, M.J.8    McCown, T.J.9    Samulski, R.J.10
  • 47
    • 80955178939 scopus 로고    scopus 로고
    • ER stress in retinal degeneration: a target for rational therapy?
    • Griciuc, A., Aron, L., Ueffing, M., ER stress in retinal degeneration: a target for rational therapy?. Trends Mol. Med. 17 (2011), 442–451.
    • (2011) Trends Mol. Med. , vol.17 , pp. 442-451
    • Griciuc, A.1    Aron, L.2    Ueffing, M.3
  • 48
    • 84929237684 scopus 로고    scopus 로고
    • Review: modulating the unfolded protein response to prevent neurodegeneration and enhance memory
    • Halliday, M., Mallucci, G.R., Review: modulating the unfolded protein response to prevent neurodegeneration and enhance memory. Neuropathol. Appl. Neurobiol. 41 (2015), 414–427.
    • (2015) Neuropathol. Appl. Neurobiol. , vol.41 , pp. 414-427
    • Halliday, M.1    Mallucci, G.R.2
  • 50
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding, H.P., Zhang, Y., Bertolotti, A., Zeng, H., Ron, D., Perk is essential for translational regulation and cell survival during the unfolded protein response. Mol. Cell 5 (2000), 897–904.
    • (2000) Mol. Cell , vol.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 52
    • 84868135034 scopus 로고    scopus 로고
    • ATF6alpha promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson's disease
    • Hashida, K., Kitao, Y., Sudo, H., Awa, Y., Maeda, S., Mori, K., Takahashi, R., Iinuma, M., Hori, O., ATF6alpha promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson's disease. PLoS One, 7, 2012, e47950.
    • (2012) PLoS One , vol.7 , pp. e47950
    • Hashida, K.1    Kitao, Y.2    Sudo, H.3    Awa, Y.4    Maeda, S.5    Mori, K.6    Takahashi, R.7    Iinuma, M.8    Hori, O.9
  • 53
    • 34250766661 scopus 로고    scopus 로고
    • The proapoptotic BCL-2 family member BIM mediates motoneuron loss in a model of amyotrophic lateral sclerosis
    • Hetz, C., Thielen, P., Fisher, J., Pasinelli, P., Brown, R.H., Korsmeyer, S., Glimcher, L., The proapoptotic BCL-2 family member BIM mediates motoneuron loss in a model of amyotrophic lateral sclerosis. Cell Death Differ. 14 (2007), 1386–1389.
    • (2007) Cell Death Differ. , vol.14 , pp. 1386-1389
    • Hetz, C.1    Thielen, P.2    Fisher, J.3    Pasinelli, P.4    Brown, R.H.5    Korsmeyer, S.6    Glimcher, L.7
  • 54
    • 69749123786 scopus 로고    scopus 로고
    • Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome
    • Hetz, C., Glimcher, L.H., Fine-tuning of the unfolded protein response: assembling the IRE1alpha interactome. Mol. Cell 35 (2009), 551–561.
    • (2009) Mol. Cell , vol.35 , pp. 551-561
    • Hetz, C.1    Glimcher, L.H.2
  • 56
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: controlling cell fate decisions under ER stress and beyond
    • Hetz, C., The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13 (2012), 89–102.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 89-102
    • Hetz, C.1
  • 57
    • 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
  • 58
    • 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
  • 59
    • 84934275896 scopus 로고    scopus 로고
    • Proteostasis control by the unfolded protein response
    • Hetz, C., Chevet, E., Oakes, S.A., Proteostasis control by the unfolded protein response. Nat. Cell Biol. 17 (2015), 829–838.
    • (2015) Nat. Cell Biol. , vol.17 , pp. 829-838
    • Hetz, C.1    Chevet, E.2    Oakes, S.A.3
  • 62
    • 84861473427 scopus 로고    scopus 로고
    • Endoplasmic reticulum: the unfolded protein response is tangled in neurodegeneration
    • Hoozemans, J.J., Scheper, W., Endoplasmic reticulum: the unfolded protein response is tangled in neurodegeneration. Int. J. Biochem. Cell Biol. 44 (2012), 1295–1298.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 1295-1298
    • Hoozemans, J.J.1    Scheper, W.2
  • 64
    • 84921762084 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress as a novel neuronal mediator in Alzheimer's disease
    • Huang, H.C., Tang, D., Lu, S.Y., Jiang, Z.F., Endoplasmic reticulum stress as a novel neuronal mediator in Alzheimer's disease. Neurol. Res. 37 (2015), 366–374.
    • (2015) Neurol. Res. , vol.37 , pp. 366-374
    • Huang, H.C.1    Tang, D.2    Lu, S.Y.3    Jiang, Z.F.4
  • 65
    • 84904860146 scopus 로고    scopus 로고
    • Guanabenz delays the onset of disease symptoms, extends lifespan, improves motor performance and attenuates motor neuron loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis
    • Jiang, H.Q., Ren, M., Jiang, H.Z., Wang, J., Zhang, J., Yin, X., Wang, S.Y., Qi, Y., Wang, X.D., Feng, H.L., Guanabenz delays the onset of disease symptoms, extends lifespan, improves motor performance and attenuates motor neuron loss in the SOD1 G93A mouse model of amyotrophic lateral sclerosis. Neuroscience 277 (2014), 132–138.
    • (2014) Neuroscience , vol.277 , pp. 132-138
    • Jiang, H.Q.1    Ren, M.2    Jiang, H.Z.3    Wang, J.4    Zhang, J.5    Yin, X.6    Wang, S.Y.7    Qi, Y.8    Wang, X.D.9    Feng, H.L.10
  • 66
    • 77249127919 scopus 로고    scopus 로고
    • eIF2alpha phosphorylation-dependent translation in CA1 pyramidal cells impairs hippocampal memory consolidation without affecting general translation
    • Jiang, Z., Belforte, J.E., Lu, Y., Yabe, Y., Pickel, J., Smith, C.B., Je, H.S., Lu, B., Nakazawa, K., eIF2alpha phosphorylation-dependent translation in CA1 pyramidal cells impairs hippocampal memory consolidation without affecting general translation. J. Neurosci. 30 (2010), 2582–2594.
    • (2010) J. Neurosci. , vol.30 , pp. 2582-2594
    • Jiang, Z.1    Belforte, J.E.2    Lu, Y.3    Yabe, Y.4    Pickel, J.5    Smith, C.B.6    Je, H.S.7    Lu, B.8    Nakazawa, K.9
  • 69
    • 84949559900 scopus 로고    scopus 로고
    • Proteostasis and aging
    • Kaushik, S., Cuervo, A.M., Proteostasis and aging. Nat. Med. 21 (2015), 1406–1415.
    • (2015) Nat. Med. , vol.21 , pp. 1406-1415
    • Kaushik, S.1    Cuervo, A.M.2
  • 72
    • 84871922036 scopus 로고    scopus 로고
    • Deciphering the mechanism underlying late-onset Alzheimer disease
    • Krstic, D., Knuesel, I., Deciphering the mechanism underlying late-onset Alzheimer disease. Nat. Rev. Neurol. 9 (2013), 25–34.
    • (2013) Nat. Rev. Neurol. , vol.9 , pp. 25-34
    • Krstic, D.1    Knuesel, I.2
  • 73
    • 84922481787 scopus 로고    scopus 로고
    • Dissection of genetic factors associated with amyotrophic lateral sclerosis
    • Leblond, C.S., Kaneb, H.M., Dion, P.A., Rouleau, G.A., Dissection of genetic factors associated with amyotrophic lateral sclerosis. Exp. Neurol., 2014, 91–101.
    • (2014) Exp. Neurol. , pp. 91-101
    • Leblond, C.S.1    Kaneb, H.M.2    Dion, P.A.3    Rouleau, G.A.4
  • 74
    • 0142059951 scopus 로고    scopus 로고
    • XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response
    • Lee, A.H., Iwakoshi, N.N., Glimcher, L.H., XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol. Cell Biol. 23 (2003), 7448–7459.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7448-7459
    • Lee, A.H.1    Iwakoshi, N.N.2    Glimcher, L.H.3
  • 77
    • 84875632050 scopus 로고    scopus 로고
    • Polymorphism-116C/G of human X-box-binding protein 1 promoter is associated with risk of Alzheimer's disease
    • Liu, S.Y., Wang, W., Cai, Z.Y., Yao, L.F., Chen, Z.W., Wang, C.Y., Zhao, B., Li, K.S., Polymorphism-116C/G of human X-box-binding protein 1 promoter is associated with risk of Alzheimer's disease. CNS Neurosci. Ther. 19 (2013), 229–234.
    • (2013) CNS Neurosci. Ther. , vol.19 , pp. 229-234
    • Liu, S.Y.1    Wang, W.2    Cai, Z.Y.3    Yao, L.F.4    Chen, Z.W.5    Wang, C.Y.6    Zhao, B.7    Li, K.S.8
  • 79
    • 39849083186 scopus 로고    scopus 로고
    • BDNF: a key regulator for protein synthesis-dependent LTP and long-term memory?
    • Lu, Y., Christian, K., Lu, B., BDNF: a key regulator for protein synthesis-dependent LTP and long-term memory?. Neurobiol. Learn. Mem. 89 (2008), 312–323.
    • (2008) Neurobiol. Learn. Mem. , vol.89 , pp. 312-323
    • Lu, Y.1    Christian, K.2    Lu, B.3
  • 80
    • 84921403151 scopus 로고    scopus 로고
    • Druggable sensors of the unfolded protein response
    • Maly, D.J., Papa, F.R., Druggable sensors of the unfolded protein response. Nat. Chem. Biol. 10 (2014), 892–901.
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 892-901
    • Maly, D.J.1    Papa, F.R.2
  • 83
    • 77951290227 scopus 로고    scopus 로고
    • TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages
    • Martinon, F., Chen, X., Lee, A.H., Glimcher, L.H., TLR activation of the transcription factor XBP1 regulates innate immune responses in macrophages. Nat. Immunol. 11 (2010), 411–418.
    • (2010) Nat. Immunol. , vol.11 , pp. 411-418
    • Martinon, F.1    Chen, X.2    Lee, A.H.3    Glimcher, L.H.4
  • 84
    • 84864866226 scopus 로고    scopus 로고
    • Hormesis: protecting neurons against cellular stress in Parkinson disease
    • Matus, S., Castillo, K., Hetz, C., Hormesis: protecting neurons against cellular stress in Parkinson disease. Autophagy 8 (2012), 997–1001.
    • (2012) Autophagy , vol.8 , pp. 997-1001
    • Matus, S.1    Castillo, K.2    Hetz, C.3
  • 85
    • 84880423261 scopus 로고    scopus 로고
    • Functional contribution of the transcription factor ATF4 to the pathogenesis of amyotrophic lateral sclerosis
    • Matus, S., Lopez, E., Valenzuela, V., Nassif, M., Hetz, C., Functional contribution of the transcription factor ATF4 to the pathogenesis of amyotrophic lateral sclerosis. PLoS One, 8, 2013, e66672.
    • (2013) PLoS One , vol.8 , pp. e66672
    • Matus, S.1    Lopez, E.2    Valenzuela, V.3    Nassif, M.4    Hetz, C.5
  • 87
    • 84902204258 scopus 로고    scopus 로고
    • Common ground: stem cell approaches find shared pathways underlying ALS
    • Matus, S., Medinas, D.B., Hetz, C., Common ground: stem cell approaches find shared pathways underlying ALS. Cell Stem Cell 14 (2014), 697–699.
    • (2014) Cell Stem Cell , vol.14 , pp. 697-699
    • Matus, S.1    Medinas, D.B.2    Hetz, C.3
  • 89
    • 33847339301 scopus 로고    scopus 로고
    • NSAIDs and Alzheimer disease: epidemiological, animal model and clinical studies
    • McGeer, P.L., McGeer, E.G., NSAIDs and Alzheimer disease: epidemiological, animal model and clinical studies. Neurobiol. Aging 28 (2007), 639–647.
    • (2007) Neurobiol. Aging , vol.28 , pp. 639-647
    • McGeer, P.L.1    McGeer, E.G.2
  • 90
    • 84875259777 scopus 로고    scopus 로고
    • An ERcentric view of Parkinson's disease
    • Mercado, G., Valdes, P., Hetz, C., An ERcentric view of Parkinson's disease. Trends Mol. Med. 19 (2013), 165–175.
    • (2013) Trends Mol. Med. , vol.19 , pp. 165-175
    • Mercado, G.1    Valdes, P.2    Hetz, C.3
  • 91
    • 84926343690 scopus 로고    scopus 로고
    • ER proteostasis disturbances in Parkinson's disease: novel insights
    • Mercado, G., Castillo, V., Vidal, R., Hetz, C., ER proteostasis disturbances in Parkinson's disease: novel insights. Front. Aging Neurosci., 7, 2015, 39.
    • (2015) Front. Aging Neurosci. , vol.7 , pp. 39
    • Mercado, G.1    Castillo, V.2    Vidal, R.3    Hetz, C.4
  • 94
    • 84880759156 scopus 로고    scopus 로고
    • Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction
    • Mucke, L., Selkoe, D.J., Neurotoxicity of amyloid beta-protein: synaptic and network dysfunction. Cold Spring Harb. Perspect. Med., 2, 2012, a006338.
    • (2012) Cold Spring Harb. Perspect. Med. , vol.2 , pp. a006338
    • Mucke, L.1    Selkoe, D.J.2
  • 95
    • 84964863009 scopus 로고    scopus 로고
    • Endoplasmic Reticulum Stress Induced Synthesis of a Novel Viral Factor Mediates Efficient Replication of Genotype-1 Hepatitis E Virus
    • Nair, V.P., Anang, S., Subramani, C., Madhvi, A., Bakshi, K., Srivastava, A., Shalimar, Nayak, B., Ct, R.K., Surjit, M., Endoplasmic Reticulum Stress Induced Synthesis of a Novel Viral Factor Mediates Efficient Replication of Genotype-1 Hepatitis E Virus. Plos. Pathog., 12, 2016, e1005521.
    • (2016) Plos. Pathog. , vol.12 , pp. e1005521
    • Nair, V.P.1    Anang, S.2    Subramani, C.3    Madhvi, A.4    Bakshi, K.5    Srivastava, A.6    Shalimar7    Nayak, B.8    Ct, R.K.9    Surjit, M.10
  • 98
    • 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
  • 99
    • 84959432869 scopus 로고    scopus 로고
    • Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury
    • Onate, M., Catenaccio, A., Martinez, G., Armentano, D., Parsons, G., Kerr, B., Hetz, C., Court, F.A., Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury. Sci. Rep., 6, 2016, 21709.
    • (2016) Sci. Rep. , vol.6 , pp. 21709
    • Onate, M.1    Catenaccio, A.2    Martinez, G.3    Armentano, D.4    Parsons, G.5    Kerr, B.6    Hetz, C.7    Court, F.A.8
  • 101
    • 84929000939 scopus 로고    scopus 로고
    • Emerging mechanisms of molecular pathology in ALS
    • Peters, O.M., Ghasemi, M., Brown, R.H. Jr., Emerging mechanisms of molecular pathology in ALS. J. Clin. Investig., 125, 2015, 2548.
    • (2015) J. Clin. Investig. , vol.125 , pp. 2548
    • Peters, O.M.1    Ghasemi, M.2    Brown, R.H.3
  • 102
    • 84940564728 scopus 로고    scopus 로고
    • Viral expression cassette elements to enhance transgene target specificity and expression in gene therapy
    • Powell, S.K., Rivera-Soto, R., Gray, S.J., Viral expression cassette elements to enhance transgene target specificity and expression in gene therapy. Discov. Med. 19 (2015), 49–57.
    • (2015) Discov. Med. , vol.19 , pp. 49-57
    • Powell, S.K.1    Rivera-Soto, R.2    Gray, S.J.3
  • 103
    • 84975516571 scopus 로고    scopus 로고
    • The ER proteostasis network in ALS: explaining the differential motoneuron vulnerability
    • Rozas, P., Bargsted, L., Martinez, F., Hetz, C., Medinas, D., The ER proteostasis network in ALS: explaining the differential motoneuron vulnerability. Neurosci. Lett., 2016, 10.1016/j.neulet.2016.04.066.
    • (2016) Neurosci. Lett.
    • Rozas, P.1    Bargsted, L.2    Martinez, F.3    Hetz, C.4    Medinas, D.5
  • 105
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E., Caroni, P., A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci. 12 (2009), 627–636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 106
    • 79960167259 scopus 로고    scopus 로고
    • Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration
    • Saxena, S., Caroni, P., Selective neuronal vulnerability in neurodegenerative diseases: from stressor thresholds to degeneration. Neuron 71 (2011), 35–48.
    • (2011) Neuron , vol.71 , pp. 35-48
    • Saxena, S.1    Caroni, P.2
  • 107
    • 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. 130:3 (2015), 315–331, 10.1007/s00401-015-1462-8.
    • (2015) Acta Neuropathol. , vol.130 , Issue.3 , pp. 315-331
    • Scheper, W.1    Hoozemans, J.J.2
  • 108
    • 85006208844 scopus 로고    scopus 로고
    • Investor outlook: significance of the positive LCA2 gene therapy Phase III results
    • Schimmer, J., Breazzano, S., Investor outlook: significance of the positive LCA2 gene therapy Phase III results. Hum. Gene Ther. Clin. Dev. 26 (2015), 208–210.
    • (2015) Hum. Gene Ther. Clin. Dev. , vol.26 , pp. 208-210
    • Schimmer, J.1    Breazzano, S.2
  • 109
    • 84991014981 scopus 로고    scopus 로고
    • Gene Therapy 2016 Update and Outlook; Tracking the Progress
    • vol. 1, ed. PiperJaffray
    • Schimmer, J., Breazzano, S., Yang, J., 2016. Gene Therapy 2016 Update and Outlook; Tracking the Progress. In: Industry Note, vol. 1, ed. PiperJaffray.
    • (2016) Industry Note
    • Schimmer, J.1    Breazzano, S.2    Yang, J.3
  • 110
    • 84859717205 scopus 로고    scopus 로고
    • Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling
    • Selvaraj, S., Sun, Y., Watt, J.A., Wang, S., Lei, S., Birnbaumer, L., Singh, B.B., Neurotoxin-induced ER stress in mouse dopaminergic neurons involves downregulation of TRPC1 and inhibition of AKT/mTOR signaling. J. Clin. Investig. 122 (2012), 1354–1367.
    • (2012) J. Clin. Investig. , vol.122 , pp. 1354-1367
    • Selvaraj, S.1    Sun, Y.2    Watt, J.A.3    Wang, S.4    Lei, S.5    Birnbaumer, L.6    Singh, B.B.7
  • 114
    • 70350043611 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinsonian substantia nigra and present in the core of Lewy bodies
    • Slodzinski, H., Moran, L.B., Michael, G.J., Wang, B., Novoselov, S., Cheetham, M.E., Pearce, R.K., Graeber, M.B., Homocysteine-induced endoplasmic reticulum protein (herp) is up-regulated in parkinsonian substantia nigra and present in the core of Lewy bodies. Clin. Neuropathol. 28 (2009), 333–343.
    • (2009) Clin. Neuropathol. , vol.28 , pp. 333-343
    • Slodzinski, H.1    Moran, L.B.2    Michael, G.J.3    Wang, B.4    Novoselov, S.5    Cheetham, M.E.6    Pearce, R.K.7    Graeber, M.B.8
  • 115
    • 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
  • 117
    • 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
  • 120
    • 74349088517 scopus 로고    scopus 로고
    • Efficient transduction of non-human primate motor neurons after intramuscular delivery of recombinant AAV serotype 6
    • Towne, C., Schneider, B.L., Kieran, D., Redmond, D.E. Jr., Aebischer, P., Efficient transduction of non-human primate motor neurons after intramuscular delivery of recombinant AAV serotype 6. Gene Ther. 17 (2010), 141–146.
    • (2010) Gene Ther. , vol.17 , pp. 141-146
    • Towne, C.1    Schneider, B.L.2    Kieran, D.3    Redmond, D.E.4    Aebischer, P.5
  • 121
    • 84872778575 scopus 로고    scopus 로고
    • Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention
    • Tsaytler, P., Bertolotti, A., Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention. FEBS J. 280 (2013), 766–770.
    • (2013) FEBS J. , vol.280 , pp. 766-770
    • Tsaytler, P.1    Bertolotti, A.2
  • 125
    • 84857852395 scopus 로고    scopus 로고
    • Activation of the unfolded protein response enhances motor recovery after spinal cord injury
    • Valenzuela, V., Collyer, E., Armentano, D., Parsons, G.B., Court, F.A., Hetz, C., Activation of the unfolded protein response enhances motor recovery after spinal cord injury. Cell Death Dis., 3, 2012, e272.
    • (2012) Cell Death Dis. , vol.3 , pp. e272
    • Valenzuela, V.1    Collyer, E.2    Armentano, D.3    Parsons, G.B.4    Court, F.A.5    Hetz, C.6
  • 129
    • 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 334 (2011), 1081–1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 130
    • 84940534837 scopus 로고    scopus 로고
    • State-of-the-art human gene therapy: Part II. Gene therapy strategies and clinical applications
    • Wang, D., Gao, G., State-of-the-art human gene therapy: Part II. Gene therapy strategies and clinical applications. Discov. Med. 18 (2014), 151–161.
    • (2014) Discov. Med. , vol.18 , pp. 151-161
    • Wang, D.1    Gao, G.2
  • 131
    • 84916928035 scopus 로고    scopus 로고
    • State-of-the-art human gene therapy: Part I. Gene delivery technologies
    • Wang, D., Gao, G., State-of-the-art human gene therapy: Part I. Gene delivery technologies. Discov. Med. 18 (2014), 67–77.
    • (2014) Discov. Med. , vol.18 , pp. 67-77
    • Wang, D.1    Gao, G.2
  • 132
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • Wang, I.F., Guo, B.S., Liu, Y.C., Wu, C.C., Yang, C.H., Tsai, K.J., Shen, C.K., Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc. Natl. Acad. Sci. USA 109 (2012), 15024–15029.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15024-15029
    • Wang, I.F.1    Guo, B.S.2    Liu, Y.C.3    Wu, C.C.4    Yang, C.H.5    Tsai, K.J.6    Shen, C.K.7
  • 133
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang, L., Popko, B., Roos, R.P., The unfolded protein response in familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 20 (2011), 1008–1015.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 134
    • 84908344184 scopus 로고    scopus 로고
    • Guanabenz, which enhances the unfolded protein response, ameliorates mutant SOD1-induced amyotrophic lateral sclerosis
    • Wang, L., Popko, B., Tixier, E., Roos, R.P., Guanabenz, which enhances the unfolded protein response, ameliorates mutant SOD1-induced amyotrophic lateral sclerosis. Neurobiol. Dis. 71 (2014), 317–324.
    • (2014) Neurobiol. Dis. , vol.71 , pp. 317-324
    • Wang, L.1    Popko, B.2    Tixier, E.3    Roos, R.P.4
  • 135
    • 84875240244 scopus 로고    scopus 로고
    • Adeno-associated virus (AAV) gene therapy for neurological disease
    • Weinberg, M.S., Samulski, R.J., McCown, T.J., Adeno-associated virus (AAV) gene therapy for neurological disease. Neuropharmacology 69 (2013), 82–88.
    • (2013) Neuropharmacology , vol.69 , pp. 82-88
    • Weinberg, M.S.1    Samulski, R.J.2    McCown, T.J.3
  • 136
    • 85016650308 scopus 로고    scopus 로고
    • Systemic AAV9 gene transfer in adult GM1 gangliosidosis mice reduces lysosomal storage in CNS and extends lifespan
    • Weismann, C.M., Ferreira, J., Keeler, A.M., Su, Q., Qui, L., Shaffer, S.A., Xu, Z., Gao, G., Sena-Esteves, M., Systemic AAV9 gene transfer in adult GM1 gangliosidosis mice reduces lysosomal storage in CNS and extends lifespan. Hum. Mol. Genet. 24 (2015), 4353–4364.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 4353-4364
    • Weismann, C.M.1    Ferreira, J.2    Keeler, A.M.3    Su, Q.4    Qui, L.5    Shaffer, S.A.6    Xu, Z.7    Gao, G.8    Sena-Esteves, M.9
  • 138
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto, K., Sato, T., Matsui, T., Sato, M., Okada, T., Yoshida, H., Harada, A., Mori, K., Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev. Cell 13 (2007), 365–376.
    • (2007) Dev. Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 140
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., Mori, K., XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107 (2001), 881–891.
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 141
    • 33751247922 scopus 로고    scopus 로고
    • Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress
    • Yu, C.Y., Hsu, Y.W., Liao, C.L., Lin, Y.L., Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J. Virol. 80 (2006), 11868–11880.
    • (2006) J. Virol. , vol.80 , pp. 11868-11880
    • Yu, C.Y.1    Hsu, Y.W.2    Liao, C.L.3    Lin, Y.L.4
  • 144
    • 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., Vidal, R.L., Armentano, D., Parsons, G., Hetz, C., 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    Vidal, R.L.2    Armentano, D.3    Parsons, G.4    Hetz, C.5


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