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Volumn 12, Issue 2, 2016, Pages 225-244

Interplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders

Author keywords

Alzheimer disease; Amyotrophic lateral sclerosis and HIV associated neurocognitive disorders; Autophagy; ER stress; Neurodegenerative disorders; Parkinson disease; Prion diseases

Indexed keywords

ALZHEIMER DISEASE; AMYOTROPHIC LATERAL SCLEROSIS; AUTOPHAGY; CELL ORGANELLE; DEGENERATIVE DISEASE; ENDOPLASMIC RETICULUM STRESS; HIV ASSOCIATED DEMENTIA; HUMAN; NONHUMAN; PARKINSON DISEASE; PATHOGENESIS; PRION DISEASE; PROTEIN AGGREGATION; PROTEIN FOLDING; REVIEW; SIGNAL TRANSDUCTION; TAUOPATHY; UNFOLDED PROTEIN RESPONSE; ANIMAL; BIOLOGICAL MODEL; PATHOLOGY;

EID: 84964501883     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.1080/15548627.2015.1121360     Document Type: Review
Times cited : (212)

References (195)
  • 1
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • PMID:20965419
    • Buchberger A, Bukau B, Sommer T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 2010; 40:238-52; PMID:20965419; http://dx.doi.org/10.1016/j.molcel.2010.10.001
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 2
    • 45549091524 scopus 로고    scopus 로고
    • The stress rheostat: An interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration
    • PMID:18473817
    • Matus S, Lisbona F, Torres M, Leon C, Thielen P, Hetz C. The stress rheostat: an interplay between the unfolded protein response (UPR) and autophagy in neurodegeneration. Curr Mol Med 2008; 8:157-72; PMID:18473817; http://dx.doi.org/10.2174/156652408784221324
    • (2008) Curr Mol Med , vol.8 , pp. 157-172
    • Matus, S.1    Lisbona, F.2    Torres, M.3    Leon, C.4    Thielen, P.5    Hetz, C.6
  • 3
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • PMID:22078875
    • Mizushima N, Komatsu M. Autophagy: renovation of cells and tissues. Cell 2011; 147:728-41; PMID:22078875; http://dx.doi.org/10.1016/j.cell.2011.10.026
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 4
    • 84863229959 scopus 로고    scopus 로고
    • Neuronal autophagy and neurodegenerative diseases
    • PMID:22257884
    • Son JH, Shim JH, Kim KH, Ha JY, Han JY. Neuronal autophagy and neurodegenerative diseases. Exp Mol Med 2012; 44:89-98; PMID:22257884; http://dx.doi.org/10.3858/emm.2012.44.2.031
    • (2012) Exp Mol Med , vol.44 , pp. 89-98
    • Son, J.H.1    Shim, J.H.2    Kim, K.H.3    Ha, J.Y.4    Han, J.Y.5
  • 5
    • 56649102055 scopus 로고    scopus 로고
    • HIV-1 Tat activates neuronal ryanodine receptors with rapid induction of the unfolded protein response and mitochondrial hyperpolarization
    • PMID:19009018
    • Norman JP, Perry SW, Reynolds HM, Kiebala M, De Mesy Bentley KL, Trejo M, Volsky DJ, Maggirwar SB, Dewhurst S, Masliah E, et al. HIV-1 Tat activates neuronal ryanodine receptors with rapid induction of the unfolded protein response and mitochondrial hyperpolarization. PloS One 2008; 3:e3731; PMID:19009018; http://dx.doi.org/10.1371/journal.pone.0003731
    • (2008) Plos One , vol.3
    • Norman, J.P.1    Perry, S.W.2    Reynolds, H.M.3    Kiebala, M.4    De Mesy Bentley, K.L.5    Trejo, M.6    Volsky, D.J.7    Maggirwar, S.B.8    Dewhurst, S.9    Masliah, E.10
  • 6
    • 43649100018 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis
    • PMID:18440237
    • Atkin JD, Farg MA, Walker AK, McLean C, Tomas D, Horne MK. Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis 2008; 30:400-7; PMID:18440237; http://dx.doi.org/10.1016/j. nbd.2008.02.009
    • (2008) Neurobiol Dis , vol.30 , pp. 400-407
    • Atkin, J.D.1    Farg, M.A.2    Walker, A.K.3    McLean, C.4    Tomas, D.5    Horne, M.K.6
  • 7
    • 0032847276 scopus 로고    scopus 로고
    • Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat
    • PMID:10501179
    • Haughey NJ, Holden CP, Nath A, Geiger JD. Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat. J Neurochem 1999; 73:1363-74; PMID:10501179; http://dx.doi. org/10.1046/j.1471-4159.1999.0731363.x
    • (1999) J Neurochem , vol.73 , pp. 1363-1374
    • Haughey, N.J.1    Holden, C.P.2    Nath, A.3    Geiger, J.D.4
  • 8
    • 0034979346 scopus 로고    scopus 로고
    • Subcellular mechanisms of presenilin-mediated enhancement of calcium signaling
    • PMID:11442355
    • Leissring MA, LaFerla FM, Callamaras N, Parker I. Subcellular mechanisms of presenilin-mediated enhancement of calcium signaling. Neurobiol Dis 2001; 8:469-78; PMID:11442355; http://dx.doi. org/10.1006/nbdi.2001.0382
    • (2001) Neurobiol Dis , vol.8 , pp. 469-478
    • Leissring, M.A.1    Laferla, F.M.2    Callamaras, N.3    Parker, I.4
  • 9
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y, Hendershot LM. ER chaperone functions during normal and stress conditions. J Chem Neuroanatomy 2004; 28:51-65; http://dx. doi.org/10.1016/j.jchemneu.2003.08.007
    • (2004) J Chem Neuroanatomy , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 10
    • 0033613952 scopus 로고    scopus 로고
    • The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase
    • PMID:9915866
    • Lucero HA, Kaminer B. The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase. J Biol Chem 1999; 274:3243-51; PMID:9915866; http://dx.doi.org/10.1074/jbc.274.5.3243
    • (1999) J Biol Chem , vol.274 , pp. 3243-3251
    • Lucero, H.A.1    Kaminer, B.2
  • 11
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • PMID:12438434
    • Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110:1389-98; PMID:12438434; http://dx.doi.org/10.1172/JCI0216886
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 12
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • PMID:15952902
    • Schroder M, Kaufman RJ. The mammalian unfolded protein response. Ann Rev Biochem 2005; 74:739-89; PMID:15952902; http://dx.doi.org/10.1146/annurev.biochem.73.011303.074134
    • (2005) Ann Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 13
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • PMID:9930704
    • Harding HP, Zhang Y, Ron D. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature 1999; 397:271-4; PMID:9930704; http://dx.doi.org/10.1038/16729
    • (1999) Nature , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 14
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • PMID:15479734
    • Lu PD, Harding HP, Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J Cell Biol 2004; 167:27-33; PMID:15479734; http://dx.doi. org/10.1083/jcb.200408003
    • (2004) J Cell Biol , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 15
    • 77950525966 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and atherosclerosis
    • PMID:20376052
    • Hotamisligil GS. Endoplasmic reticulum stress and atherosclerosis. Nat Med 2010; 16:396-9; PMID:20376052; http://dx.doi.org/10.1038/nm0410-396
    • (2010) Nat Med , vol.16 , pp. 396-399
    • Hotamisligil, G.S.1
  • 16
    • 0032979420 scopus 로고    scopus 로고
    • Disturbances of the functioning of endoplasmic reticulum: A key mechanism underlying neuronal cell injury?
    • Paschen W, Doutheil J. Disturbances of the functioning of endoplasmic reticulum: a key mechanism underlying neuronal cell injury? J Cerebral Blood Flow Metab 1999; 19:1-18; http://dx.doi.org/10.1097/00004647-199901000-00001
    • (1999) J Cerebral Blood Flow Metab , vol.19 , pp. 1-18
    • Paschen, W.1    Doutheil, J.2
  • 17
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • PMID:11780124
    • Calfon M, Zeng H, Urano F, Till JH, Hubbard SR, Harding HP, et al. IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA. Nature 2002; 415:92-6; PMID:11780124; http://dx.doi.org/10.1038/415092a
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6
  • 18
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • PMID:17565364
    • Ron D, Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007; 8:519-29; PMID:17565364; http://dx.doi.org/10.1038/nrm2199
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 19
    • 69749123786 scopus 로고    scopus 로고
    • Glimcher LH. Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome
    • PMID:19748352
    • Hetz C, Glimcher LH. Fine-tuning of the unfolded protein response: Assembling the IRE1alpha interactome. Mol Cell 2009; 35:551-61; PMID:19748352; http://dx.doi.org/10.1016/j.molcel.2009.08.021
    • (2009) Mol Cell , vol.35 , pp. 551-561
    • Hetz, C.1
  • 20
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • PMID:10564271
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999; 10:3787-99; PMID:10564271; http://dx. doi.org/10.1091/mbc.10.11.3787
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 21
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi
    • PMID:11821395
    • Chen X, Shen J, Prywes R. The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 2002; 277:13045-52; PMID:11821395; http://dx.doi.org/10.1074/jbc.M110636200
    • (2002) J Biol Chem , vol.277 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 22
    • 79953870477 scopus 로고    scopus 로고
    • Luminal domain of ATF6 alone is sufficient for sensing endoplasmic reticulum stress and subsequent transport to the Golgi apparatus
    • PMID:21150130
    • Sato Y, Nadanaka S, Okada T, Okawa K, Mori K. Luminal domain of ATF6 alone is sufficient for sensing endoplasmic reticulum stress and subsequent transport to the Golgi apparatus. Cell Structure Function 2011; 36:35-47; PMID:21150130; http://dx.doi.org/10.1247/csf.10010
    • (2011) Cell Structure Function , vol.36 , pp. 35-47
    • Sato, Y.1    Nadanaka, S.2    Okada, T.3    Okawa, K.4    Mori, K.5
  • 23
    • 34548189283 scopus 로고    scopus 로고
    • ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress
    • PMID:17765679
    • Wu J, Rutkowski DT, Dubois M, Swathirajan J, Saunders T, Wang J, Song B, Yau GD, Kaufman RJ. ATF6alpha optimizes long-term endoplasmic reticulum function to protect cells from chronic stress. Dev Cell 2007; 13:351-64; PMID:17765679; http://dx.doi.org/10.1016/j.devcel.2007.07.005
    • (2007) Dev Cell , vol.13 , pp. 351-364
    • Wu, J.1    Rutkowski, D.T.2    Dubois, M.3    Swathirajan, J.4    Saunders, T.5    Wang, J.6    Song, B.7    Yau, G.D.8    Kaufman, R.J.9
  • 24
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • PMID:20581817
    • Wong E, Cuervo AM. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci 2010; 13:805-11; PMID:20581817; http://dx. doi.org/10.1038/nn.2575
    • (2010) Nat Neurosci , vol.13 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 25
    • 84897143522 scopus 로고    scopus 로고
    • To be or not to be? How selective autophagy and cell death govern cell fate
    • PMID:24679527
    • Green DR, Levine B. To be or not to be? How selective autophagy and cell death govern cell fate. Cell 2014; 157:65-75; PMID:24679527; http://dx.doi.org/10.1016/j.cell.2014.02.049
    • (2014) Cell , vol.157 , pp. 65-75
    • Green, D.R.1    Levine, B.2
  • 27
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • PMID:11007884
    • Kegel KB, Kim M, Sapp E, McIntyre C, Castano JG, Aronin N, DiFiglia M. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci 2000; 20:7268-78; PMID:11007884
    • (2000) J Neurosci , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3    McIntyre, C.4    Castano, J.G.5    Aronin, N.6    Difiglia, M.7
  • 29
    • 4344656905 scopus 로고    scopus 로고
    • Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: A brain biopsy study
    • PMID:15325593
    • Sikorska B, Liberski PP, Giraud P, Kopp N, Brown P. Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: a brain biopsy study. Int J Biochem Cell Biol 2004; 36:2563-73; PMID:15325593; http://dx.doi.org/10.1016/j.biocel.2004.04.014
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2563-2573
    • Sikorska, B.1    Liberski, P.P.2    Giraud, P.3    Kopp, N.4    Brown, P.5
  • 30
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • PMID:17909521
    • Xie Z, Klionsky DJ. Autophagosome formation: core machinery and adaptations. Nature cell biology 2007; 9:1102-9; PMID:17909521; http://dx.doi.org/10.1038/ncb1007-1102
    • (2007) Nature Cell Biology , vol.9 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 31
    • 78349308821 scopus 로고    scopus 로고
    • Negative regulation of autophagy
    • PMID:20865012
    • Liang C. Negative regulation of autophagy. Cell Death Differ 2010; 17:1807-15; PMID:20865012; http://dx.doi.org/10.1038/cdd.2010.115
    • (2010) Cell Death Differ , vol.17 , pp. 1807-1815
    • Liang, C.1
  • 32
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • PMID:20965422
    • Kroemer G, Marino G, Levine B. Autophagy and the integrated stress response. Mol Cell 2010; 40:280-93; PMID:20965422; http://dx.doi. org/10.1016/j.molcel.2010.09.023
    • (2010) Mol Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 33
    • 77951221542 scopus 로고    scopus 로고
    • The role of the Atg1/ULK1 complex in autophagy regulation
    • PMID:20056399
    • Mizushima N. The role of the Atg1/ULK1 complex in autophagy regulation. Curr Opin Cell Biol 2010; 22:132-9; PMID:20056399; http://dx.doi.org/10.1016/j.ceb.2009.12.004
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 132-139
    • Mizushima, N.1
  • 35
    • 33846514235 scopus 로고    scopus 로고
    • Hierarchy of Atg proteins in pre-autophagosomal structure organization
    • PMID:17295840
    • Suzuki K, Kubota Y, Sekito T, Ohsumi Y. Hierarchy of Atg proteins in pre-autophagosomal structure organization. Genes Cells 2007; 12:209-18; PMID:17295840; http://dx.doi.org/10.1111/j.1365-2443.2007.01050.x
    • (2007) Genes Cells , vol.12 , pp. 209-218
    • Suzuki, K.1    Kubota, Y.2    Sekito, T.3    Ohsumi, Y.4
  • 36
    • 68149139456 scopus 로고    scopus 로고
    • The autophagy effector Beclin 1: A novel BH3-only protein
    • PMID:19641499
    • Sinha S, Levine B. The autophagy effector Beclin 1: a novel BH3-only protein. Oncogene 2008; 27 Suppl 1:S137-48; PMID:19641499; http://dx.doi.org/10.1038/onc.2009.51
    • (2008) Oncogene , vol.27 , pp. S137-S148
    • Sinha, S.1    Levine, B.2
  • 38
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • PMID:23921753
    • Nixon RA. The role of autophagy in neurodegenerative disease. Nat Med 2013; 19:983-97; PMID:23921753; http://dx.doi.org/10.1038/nm.3232
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 39
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • PMID:20034776
    • Yang Z, Klionsky DJ. Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 2010; 22:124-31; PMID:20034776; http://dx.doi.org/10.1016/j.ceb.2009.11.014
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 40
    • 84934440388 scopus 로고    scopus 로고
    • LC3 and Autophagy
    • Tanida I, Ueno T, Kominami E. LC3 and Autophagy. Meth Mol Biol 2008; 445:77-88; http://dx.doi.org/10.1007/978-1-59745-157-4_4
    • (2008) Meth Mol Biol , vol.445 , pp. 77-88
    • Tanida, I.1    Ueno, T.2    Kominami, E.3
  • 41
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • PMID:19653858
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009; 43:67-93; PMID:19653858; http://dx.doi.org/10.1146/annurev-genet-102808-114910
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 42
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • PMID:19696797
    • Grant BD, Donaldson JG. Pathways and mechanisms of endocytic recycling. Nat Rev Mol Cell Biol 2009; 10:597-608; PMID:19696797; http://dx.doi.org/10.1038/nrm2755
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 43
    • 33845903831 scopus 로고    scopus 로고
    • Characterization of the Rab8-specific membrane traffic route linked to protrusion formation
    • PMID:17105768
    • Hattula K, Furuhjelm J, Tikkanen J, Tanhuanpaa K, Laakkonen P, Peranen J. Characterization of the Rab8-specific membrane traffic route linked to protrusion formation. J Cell Sci 2006; 119:4866-77; PMID:17105768; http://dx.doi.org/10.1242/jcs.03275
    • (2006) J Cell Sci , vol.119 , pp. 4866-4877
    • Hattula, K.1    Furuhjelm, J.2    Tikkanen, J.3    Tanhuanpaa, K.4    Laakkonen, P.5    Peranen, J.6
  • 44
    • 84905377699 scopus 로고    scopus 로고
    • Hook1, microtubules, and Rab22: Mediators of selective sorting of clathrin-independent endocytic cargo proteins on endosomes
    • PMID:24284901
    • Maldonado-Baez L, Donaldson JG. Hook1, microtubules, and Rab22: mediators of selective sorting of clathrin-independent endocytic cargo proteins on endosomes. Bioarchitecture 2013; 3:141-6; PMID:24284901; http://dx.doi.org/10.4161/bioa.26638
    • (2013) Bioarchitecture , vol.3 , pp. 141-146
    • Maldonado-Baez, L.1    Donaldson, J.G.2
  • 45
    • 84939550403 scopus 로고    scopus 로고
    • GRAF1 forms a complex with MICAL-L1 and EHD1 to cooperate in tubular recycling endosome vesiculation
    • PMID:25364729
    • Cai B, Xie S, Caplan S, Naslavsky N. GRAF1 forms a complex with MICAL-L1 and EHD1 to cooperate in tubular recycling endosome vesiculation. Front Cell Dev Biol 2014; 2:22; PMID:25364729; http://dx.doi.org/10.3389/fcell.2014.00022
    • (2014) Front Cell Dev Biol , vol.2 , pp. 22
    • Cai, B.1    Xie, S.2    Caplan, S.3    Naslavsky, N.4
  • 46
    • 84899447630 scopus 로고    scopus 로고
    • Rapid degradation of the complement regulator, CD59, by a novel inhibitor
    • PMID:24616098
    • Cai B, Xie S, Liu F, Simone LC, Caplan S, Qin X, Naslavsky N. Rapid degradation of the complement regulator, CD59, by a novel inhibitor. J Biol Chem 2014; 289:12109-25; PMID:24616098; http://dx.doi. org/10.1074/jbc.M113.547083
    • (2014) J Biol Chem , vol.289 , pp. 12109-12125
    • Cai, B.1    Xie, S.2    Liu, F.3    Simone, L.C.4    Caplan, S.5    Qin, X.6    Naslavsky, N.7
  • 47
    • 84911420322 scopus 로고    scopus 로고
    • Diacylglycerol Kinase a Regulates Tubular Recycling Endosome Biogenesis and Major Histocompatibility Complex Class I Recycling
    • PMID:25248744
    • Xie S, Naslavsky N, Caplan S. Diacylglycerol Kinase a Regulates Tubular Recycling Endosome Biogenesis and Major Histocompatibility Complex Class I Recycling. J Biol Chem 2014; 289:31914-26; PMID:25248744; http://dx.doi.org/10.1074/jbc.M114.594291
    • (2014) J Biol Chem , vol.289 , pp. 31914-31926
    • Xie, S.1    Naslavsky, N.2    Caplan, S.3
  • 48
    • 84862611041 scopus 로고    scopus 로고
    • TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes
    • PMID:22613832
    • Longatti A, Lamb CA, Razi M, Yoshimura S, Barr FA, Tooze SA. TBC1D14 regulates autophagosome formation via Rab11-and ULK1-positive recycling endosomes. J Cell Biol 2012; 197:659-75; PMID:22613832; http://dx.doi.org/10.1083/jcb.201111079
    • (2012) J Cell Biol , vol.197 , pp. 659-675
    • Longatti, A.1    Lamb, C.A.2    Razi, M.3    Yoshimura, S.4    Barr, F.A.5    Tooze, S.A.6
  • 51
    • 33846211417 scopus 로고    scopus 로고
    • ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation
    • PMID:16794605
    • Kouroku Y, Fujita E, Tanida I, Ueno T, Isoai A, Kumagai H, Ogawa S, Kaufman RJ, Kominami E, Momoi T. ER stress (PERK/eIF2alpha phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ 2007; 14:230-9; PMID:16794605; http://dx.doi.org/10.1038/sj. cdd.4401984
    • (2007) Cell Death Differ , vol.14 , pp. 230-239
    • Kouroku, Y.1    Fujita, E.2    Tanida, I.3    Ueno, T.4    Isoai, A.5    Kumagai, H.6    Ogawa, S.7    Kaufman, R.J.8    Kominami, E.9    Momoi, T.10
  • 56
    • 84879607395 scopus 로고    scopus 로고
    • Stress-induced selfcannibalism: On the regulation of autophagy by endoplasmic reticulum stress
    • PMID:23052213
    • Deegan S, Saveljeva S, Gorman AM, Samali A. Stress-induced selfcannibalism: on the regulation of autophagy by endoplasmic reticulum stress. Cell Mol Life Sci 2013; 70:2425-41; PMID:23052213; http://dx.doi.org/10.1007/s00018-012-1173-4
    • (2013) Cell Mol Life Sci , vol.70 , pp. 2425-2441
    • Deegan, S.1    Saveljeva, S.2    Gorman, A.M.3    Samali, A.4
  • 57
    • 44949237240 scopus 로고    scopus 로고
    • JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy
    • PMID:18570871
    • Wei Y, Pattingre S, Sinha S, Bassik M, Levine B. JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy. Mol Cell 2008; 30:678-88; PMID:18570871; http://dx.doi.org/10.1016/j.molcel.2008.06.001
    • (2008) Mol Cell , vol.30 , pp. 678-688
    • Wei, Y.1    Pattingre, S.2    Sinha, S.3    Bassik, M.4    Levine, B.5
  • 58
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • PMID:10650002
    • Urano F, Wang X, Bertolotti A, Zhang Y, Chung P, Harding HP, Ron D. Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 2000; 287:664-6; PMID:10650002; http://dx.doi.org/10.1126/science.287.5453.664
    • (2000) Science , vol.287 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 59
    • 84878772042 scopus 로고    scopus 로고
    • Oxidized lipids activate autophagy in a JNKdependent manner by stimulating the endoplasmic reticulum stress response
    • PMID:24024137
    • Haberzettl P, Hill BG. Oxidized lipids activate autophagy in a JNKdependent manner by stimulating the endoplasmic reticulum stress response. Redox Biol 2013; 1:56-64; PMID:24024137; http://dx.doi. org/10.1016/j.redox.2012.10.003
    • (2013) Redox Biol , vol.1 , pp. 56-64
    • Haberzettl, P.1    Hill, B.G.2
  • 60
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy
    • PMID:22337954
    • Vidal RL, Figueroa A, Court FA, Thielen P, Molina C, Wirth C, Caballero B, Kiffin R, Segura-Aguilar J, Cuervo AM, et al. Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy. Hum Mol Genet 2012; 21:2245-62; PMID:22337954; http://dx.doi.org/10.1093/hmg/dds040
    • (2012) Hum Mol Genet , vol.21 , pp. 2245-2262
    • Vidal, R.L.1    Figueroa, A.2    Court, F.A.3    Thielen, P.4    Molina, C.5    Wirth, C.6    Caballero, B.7    Kiffin, R.8    Segura-Aguilar, J.9    Cuervo, A.M.10
  • 61
    • 84876416042 scopus 로고    scopus 로고
    • XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells
    • PMID:23277279
    • Zhao Y, Li X, Cai MY, Ma K, Yang J, Zhou J, Fu W, Wei FZ, Wang L, Xie D, et al. XBP-1u suppresses autophagy by promoting the degradation of FoxO1 in cancer cells. Cell Res 2013; 23:491-507; PMID:23277279; http://dx.doi.org/10.1038/cr.2013.2
    • (2013) Cell Res , vol.23 , pp. 491-507
    • Zhao, Y.1    Li, X.2    Cai, M.Y.3    Ma, K.4    Yang, J.5    Zhou, J.6    Fu, W.7    Wei, F.Z.8    Wang, L.9    Xie, D.10
  • 63
    • 84907856144 scopus 로고    scopus 로고
    • Regulation of the death-associated protein kinase 1 expression and autophagy via ATF6 requires apoptosis signal-regulating kinase 1
    • PMID:25135476
    • Gade P, Manjegowda SB, Nallar SC, Maachani UB, Cross AS, Kalvakolanu DV. Regulation of the death-associated protein kinase 1 expression and autophagy via ATF6 requires apoptosis signal-regulating kinase 1. Mol Cell Biol 2014; 34:4033-48; PMID:25135476; http://dx.doi.org/10.1128/MCB.00397-14
    • (2014) Mol Cell Biol , vol.34 , pp. 4033-4048
    • Gade, P.1    Manjegowda, S.B.2    Nallar, S.C.3    Maachani, U.B.4    Cross, A.S.5    Kalvakolanu, D.V.6
  • 64
    • 84869447873 scopus 로고    scopus 로고
    • IFNG and autophagy: A critical role for the ER-stress mediator ATF6 in controlling bacterial infections
    • PMID:22874566
    • Kalvakolanu DV, Gade P. IFNG and autophagy: a critical role for the ER-stress mediator ATF6 in controlling bacterial infections. Autophagy 2012; 8:1673-4; PMID:22874566; http://dx.doi.org/10.4161/auto.21403
    • (2012) Autophagy , vol.8 , pp. 1673-1674
    • Kalvakolanu, D.V.1    Gade, P.2
  • 65
    • 61849102389 scopus 로고    scopus 로고
    • DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy
    • PMID:19180116
    • Zalckvar E, Berissi H, Mizrachy L, Idelchuk Y, Koren I, Eisenstein M, Sabanay H, Pinkas-Kramarski R, Kimchi A. DAP-kinase-mediated phosphorylation on the BH3 domain of beclin 1 promotes dissociation of beclin 1 from Bcl-XL and induction of autophagy. EMBO Rep 2009; 10:285-92; PMID:19180116; http://dx.doi.org/10.1038/embor.2008.246
    • (2009) EMBO Rep , vol.10 , pp. 285-292
    • Zalckvar, E.1    Berissi, H.2    Mizrachy, L.3    Idelchuk, Y.4    Koren, I.5    Eisenstein, M.6    Sabanay, H.7    Pinkas-Kramarski, R.8    Kimchi, A.9
  • 66
    • 0032413192 scopus 로고    scopus 로고
    • Alzheimer disease: Genetic studies and transgenic models
    • PMID:9928488
    • Price DL, Tanzi RE, Borchelt DR, Sisodia SS. Alzheimer disease: genetic studies and transgenic models. Ann Rev Genet 1998; 32:461-93; PMID:9928488; http://dx.doi.org/10.1146/annurev.genet.32.1.461
    • (1998) Ann Rev Genet , vol.32 , pp. 461-493
    • Price, D.L.1    Tanzi, R.E.2    Borchelt, D.R.3    Sisodia, S.S.4
  • 67
    • 0027314026 scopus 로고
    • Pathology and biology of the Lewy body
    • PMID: 7684074
    • Pollanen MS, Dickson DW, Bergeron C. Pathology and biology of the Lewy body. J Neuropathol Exp Neurol 1993; 52:183-91; PMID: 7684074; http://dx.doi.org/10.1097/00005072-199305000-00001
    • (1993) J Neuropathol Exp Neurol , vol.52 , pp. 183-191
    • Pollanen, M.S.1    Dickson, D.W.2    Bergeron, C.3
  • 68
    • 0347695007 scopus 로고    scopus 로고
    • Reduction of calcium release from the endoplasmic reticulum could only provide partial neuroprotection against b-amyloid peptide toxicity
    • PMID:14713297
    • Suen KC, Lin KF, Elyaman W, So KF, Chang RC, Hugon J. Reduction of calcium release from the endoplasmic reticulum could only provide partial neuroprotection against b-amyloid peptide toxicity. J Neurochem 2003; 87:1413-26; PMID:14713297; http://dx.doi.org/10.1111/j.1471-4159.2003.02259.x
    • (2003) J Neurochem , vol.87 , pp. 1413-1426
    • Suen, K.C.1    Lin, K.F.2    Elyaman, W.3    So, K.F.4    Chang, R.C.5    Hugon, J.6
  • 69
    • 84878934982 scopus 로고    scopus 로고
    • Ca(2C)-dependent endoplasmic reticulum stress correlates with astrogliosis in oligomeric amyloid b-treated astrocytes and in a model of Alzheimer disease
    • PMID:23409977
    • Alberdi E, Wyssenbach A, Alberdi M, Sanchez-Gomez MV, Cavaliere F, Rodriguez JJ, Verkhratsky A, Matute C. Ca(2C)-dependent endoplasmic reticulum stress correlates with astrogliosis in oligomeric amyloid b-treated astrocytes and in a model of Alzheimer disease. Aging Cell 2013; 12:292-302; PMID:23409977; http://dx.doi. org/10.1111/acel.12054
    • (2013) Aging Cell , vol.12 , pp. 292-302
    • Alberdi, E.1    Wyssenbach, A.2    Alberdi, M.3    Sanchez-Gomez, M.V.4    Cavaliere, F.5    Rodriguez, J.J.6    Verkhratsky, A.7    Matute, C.8
  • 70
    • 84867031150 scopus 로고    scopus 로고
    • Mitochondrial dysfunction associated with increased oxidative stress and a-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue
    • PMID:23039195
    • Imaizumi Y, Okada Y, Akamatsu W, Koike M, Kuzumaki N, Hayakawa H, Nihira T, Kobayashi T, Ohyama M, Sato S, et al. Mitochondrial dysfunction associated with increased oxidative stress and a-synuclein accumulation in PARK2 iPSC-derived neurons and postmortem brain tissue. Mol Brain 2012; 5:35; PMID:23039195; http://dx.doi.org/10.1186/1756-6606-5-35
    • (2012) Mol Brain , vol.5 , pp. 35
    • Imaizumi, Y.1    Okada, Y.2    Akamatsu, W.3    Koike, M.4    Kuzumaki, N.5    Hayakawa, H.6    Nihira, T.7    Kobayashi, T.8    Ohyama, M.9    Sato, S.10
  • 71
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro
    • PMID:10208537
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E. Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro. Neuroreport 1999; 10:717-21; PMID:10208537; http://dx.doi.org/10.1097/00001756-199903170-00011
    • (1999) Neuroreport , vol.10 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6    Masliah, E.7
  • 73
    • 79955921784 scopus 로고    scopus 로고
    • Neuroinflammation and a-synuclein dysfunction potentiate each other, driving chronic progression of neurodegeneration in a mouse model of Parkinson disease
    • PMID:21245015
    • Gao HM, Zhang F, Zhou H, Kam W, Wilson B, Hong JS. Neuroinflammation and a-synuclein dysfunction potentiate each other, driving chronic progression of neurodegeneration in a mouse model of Parkinson disease. Environ Health Perspect 2011; 119:807-14; PMID:21245015; http://dx.doi.org/10.1289/ehp.1003013
    • (2011) Environ Health Perspect , vol.119 , pp. 807-814
    • Gao, H.M.1    Zhang, F.2    Zhou, H.3    Kam, W.4    Wilson, B.5    Hong, J.S.6
  • 76
    • 84866657775 scopus 로고    scopus 로고
    • A link between LRRK2, autophagy and NAADP-mediated endolysosomal calcium signalling
    • PMID:22988879
    • Gomez-Suaga P, Churchill GC, Patel S, Hilfiker S. A link between LRRK2, autophagy and NAADP-mediated endolysosomal calcium signalling. Biochem Soc Trans 2012; 40:1140-6; PMID:22988879; http://dx.doi.org/10.1042/BST20120138
    • (2012) Biochem Soc Trans , vol.40 , pp. 1140-1146
    • Gomez-Suaga, P.1    Churchill, G.C.2    Patel, S.3    Hilfiker, S.4
  • 77
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer disease: Genes, proteins, and therapy
    • PMID:11274343
    • Selkoe DJ. Alzheimer disease: genes, proteins, and therapy. Physiol Rev 2001; 81:741-66; PMID:11274343
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 78
    • 84895768762 scopus 로고    scopus 로고
    • Familial Alzheimer mutations within APPTM increase Abeta42 production by enhancing accessibility of epsilon-cleavage site
    • PMID:24390130
    • Chen W, Gamache E, Rosenman DJ, Xie J, Lopez MM, Li YM, Wang C. Familial Alzheimer mutations within APPTM increase Abeta42 production by enhancing accessibility of epsilon-cleavage site. Nat Commun 2014; 5:3037; PMID:24390130
    • (2014) Nat Commun , vol.5 , pp. 3037
    • Chen, W.1    Gamache, E.2    Rosenman, D.J.3    Xie, J.4    Lopez, M.M.5    Li, Y.M.6    Wang, C.7
  • 79
    • 84943349735 scopus 로고    scopus 로고
    • Protein misfolding and dysregulated protein homeostasis in autoinflammatory diseases and beyond
    • PMID:25994946
    • Agyemang AF, Harrison SR, Siegel RM, McDermott MF. Protein misfolding and dysregulated protein homeostasis in autoinflammatory diseases and beyond. Semin Immunopathol 2015; 37(4):335-47; PMID:25994946; http://dx.doi.org/10.1007/s00281-015-0496-2
    • (2015) Semin Immunopathol , vol.37 , Issue.4 , pp. 335-347
    • Agyemang, A.F.1    Harrison, S.R.2    Siegel, R.M.3    McDermott, M.F.4
  • 80
    • 84858000638 scopus 로고    scopus 로고
    • The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies
    • PMID:22102449
    • Nijholt DA, van Haastert ES, Rozemuller AJ, Scheper W, Hoozemans JJ. The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies. J Pathol 2012; 226:693-702; PMID:22102449; http://dx.doi.org/10.1002/path.3969
    • (2012) J Pathol , vol.226 , pp. 693-702
    • Nijholt, D.A.1    Van Haastert, E.S.2    Rozemuller, A.J.3    Scheper, W.4    Hoozemans, J.J.5
  • 81
    • 84875254177 scopus 로고    scopus 로고
    • B amyloid peptide plaques fail to alter evoked neuronal calcium signals in APP/PS1 Alzheimer disease mice
    • PMID:23337342
    • Briggs CA, Schneider C, Richardson JC, Stutzmann GE. b amyloid peptide plaques fail to alter evoked neuronal calcium signals in APP/PS1 Alzheimer disease mice. Neurobiol Aging 2013; 34:1632-43; PMID:23337342; http://dx.doi.org/10.1016/j. neurobiolaging.2012.12.013
    • (2013) Neurobiol Aging , vol.34 , pp. 1632-1643
    • Briggs, C.A.1    Schneider, C.2    Richardson, J.C.3    Stutzmann, G.E.4
  • 82
    • 84883746997 scopus 로고    scopus 로고
    • Presenilin-ryanodine receptor connection
    • PMID:23995445
    • D’Adamio L, Castillo PE. Presenilin-ryanodine receptor connection. Proc Natl Acad Sci U S A 2013; 110:14825-6; PMID:23995445; http://dx.doi.org/10.1073/pnas.1313996110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 14825-14826
    • D’Adamio, L.1    Castillo, P.E.2
  • 83
    • 0033015485 scopus 로고    scopus 로고
    • The endoplasmic reticulum stressresponsive protein GRP78 protects neurons against excitotoxicity and apoptosis: Suppression of oxidative stress and stabilization of calcium homeostasis
    • PMID:10072306
    • Yu Z, Luo H, Fu W, Mattson MP. The endoplasmic reticulum stressresponsive protein GRP78 protects neurons against excitotoxicity and apoptosis: suppression of oxidative stress and stabilization of calcium homeostasis. Exp Neurol 1999; 155:302-14; PMID:10072306; http://dx.doi.org/10.1006/exnr.1998.7002
    • (1999) Exp Neurol , vol.155 , pp. 302-314
    • Yu, Z.1    Luo, H.2    Fu, W.3    Mattson, M.P.4
  • 88
  • 90
    • 78650716872 scopus 로고    scopus 로고
    • Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer disease ameliorates amyloid pathologies and memory deficits
    • PMID:21186265
    • Yang DS, Stavrides P, Mohan PS, Kaushik S, Kumar A, Ohno M, Schmidt SD, Wesson D, Bandyopadhyay U, Jiang Y, et al. Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer disease ameliorates amyloid pathologies and memory deficits. Brain 2011; 134:258-77; PMID:21186265; http://dx.doi.org/10.1093/brain/awq341
    • (2011) Brain , vol.134 , pp. 258-277
    • Yang, D.S.1    Stavrides, P.2    Mohan, P.S.3    Kaushik, S.4    Kumar, A.5    Ohno, M.6    Schmidt, S.D.7    Wesson, D.8    Bandyopadhyay, U.9    Jiang, Y.10
  • 91
    • 84896338549 scopus 로고    scopus 로고
    • Temsirolimus promotes autophagic clearance of amyloid-b and provides protective effects in cellular and animal models of Alzheimer disease
    • PMID:24602800
    • Jiang T, Yu JT, Zhu XC, Tan MS, Wang HF, Cao L, Zhang QQ, Shi JQ, Gao L, Qin H, et al. Temsirolimus promotes autophagic clearance of amyloid-b and provides protective effects in cellular and animal models of Alzheimer disease. Pharmacol Res 2014; 81:54-63; PMID:24602800; http://dx.doi.org/10.1016/j.phrs.2014.02.008
    • (2014) Pharmacol Res , vol.81 , pp. 54-63
    • Jiang, T.1    Yu, J.T.2    Zhu, X.C.3    Tan, M.S.4    Wang, H.F.5    Cao, L.6    Zhang, Q.Q.7    Shi, J.Q.8    Gao, L.9    Qin, H.10
  • 93
    • 84878333056 scopus 로고    scopus 로고
    • Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation
    • PMID:23719816
    • Abisambra JF, Jinwal UK, Blair LJ, O’Leary JC, 3rd, Li Q, Brady S, Wang L, Guidi CE, Zhang B, Nordhues BA, et al. Tau accumulation activates the unfolded protein response by impairing endoplasmic reticulum-associated degradation. J Neurosci 2013; 33:9498-507; PMID:23719816; http://dx.doi.org/10.1523/JNEUROSCI.5397-12.2013
    • (2013) J Neurosci , vol.33 , pp. 9498-9507
    • Abisambra, J.F.1    Jinwal, U.K.2    Blair, L.J.3    O’Leary, J.C.4    Li, Q.5    Brady, S.6    Wang, L.7    Guidi, C.E.8    Zhang, B.9    Nordhues, B.A.10
  • 94
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • PMID:12065827
    • Taylor JP, Hardy J, Fischbeck KH. Toxic proteins in neurodegenerative disease. Science 2002; 296:1991-5; PMID:12065827; http://dx. doi.org/10.1126/science.1067122
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 95
    • 84901950037 scopus 로고    scopus 로고
    • Brain injury in the context of tauopathies
    • Abisambra JF, Scheff S. Brain injury in the context of tauopathies. J Alzheimer Dis 2014; 40:495-518
    • (2014) J Alzheimer Dis , vol.40 , pp. 495-518
    • Abisambra, J.F.1    Scheff, S.2
  • 97
    • 84860219621 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is an early event in Alzheimer and Parkinson disease
    • PMID:22302012
    • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Scheper W. Activation of the unfolded protein response is an early event in Alzheimer and Parkinson disease. Neurodegener Dis 2012; 10:212-5; PMID:22302012; http://dx.doi.org/10.1159/000334536
    • (2012) Neurodegener Dis , vol.10 , pp. 212-215
    • Hoozemans, J.J.1    Van Haastert, E.S.2    Nijholt, D.A.3    Rozemuller, A.J.4    Scheper, W.5
  • 98
    • 65349093893 scopus 로고    scopus 로고
    • The unfolded protein response is activated in pretangle neurons in Alzheimer disease hippocampus
    • PMID:19264902
    • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Eikelenboom P, Scheper W. The unfolded protein response is activated in pretangle neurons in Alzheimer disease hippocampus. Am J Pathol 2009; 174:1241-51; PMID:19264902; http://dx.doi.org/10.2353/ajpath.2009.080814
    • (2009) Am J Pathol , vol.174 , pp. 1241-1251
    • Hoozemans, J.J.1    Van Haastert, E.S.2    Nijholt, D.A.3    Rozemuller, A.J.4    Eikelenboom, P.5    Scheper, W.6
  • 100
    • 84875855976 scopus 로고    scopus 로고
    • Unfolded protein response activates glycogen synthase kinase-3 via selective lysosomal degradation
    • PMID:23415837
    • Nijholt DA, Nolle A, van Haastert ES, Edelijn H, Toonen RF, Hoozemans JJ, Scheper W. Unfolded protein response activates glycogen synthase kinase-3 via selective lysosomal degradation. Neurobiol Aging 2013; 34:1759-71; PMID:23415837; http://dx.doi.org/10.1016/j.neurobiolaging.2013.01.008
    • (2013) Neurobiol Aging , vol.34 , pp. 1759-1771
    • Nijholt, D.A.1    Nolle, A.2    Van Haastert, E.S.3    Edelijn, H.4    Toonen, R.F.5    Hoozemans, J.J.6    Scheper, W.7
  • 103
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • PMID:21776078
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011; 475:324-32; PMID:21776078; http://dx.doi.org/10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 104
    • 37149014221 scopus 로고    scopus 로고
    • Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity
    • PMID:18075673
    • Wilson MR, Yerbury JJ, Poon S. Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity. Mol Biosyst 2008; 4:42-52; PMID:18075673; http://dx.doi.org/10.1039/B712728F
    • (2008) Mol Biosyst , vol.4 , pp. 42-52
    • Wilson, M.R.1    Yerbury, J.J.2    Poon, S.3
  • 105
    • 84855320950 scopus 로고    scopus 로고
    • Clusterin in Alzheimer disease
    • PMID:22397031
    • Wu ZC, Yu JT, Li Y, Tan L. Clusterin in Alzheimer disease. Adv Clin Chem 2012; 56:155-73; PMID:22397031; http://dx.doi.org/10.1016/B978-0-12-394317-0.00011-X
    • (2012) Adv Clin Chem , vol.56 , pp. 155-173
    • Wu, Z.C.1    Yu, J.T.2    Li, Y.3    Tan, L.4
  • 106
    • 33847345982 scopus 로고    scopus 로고
    • Transthyretin and Alzheimer disease: Where in the brain?
    • PMID:16698124
    • Sousa JC, Cardoso I, Marques F, Saraiva MJ, Palha JA. Transthyretin and Alzheimer disease: where in the brain? Neurobiol Aging 2007; 28:713-8; PMID:16698124; http://dx.doi.org/10.1016/j. neurobiolaging.2006.03.015
    • (2007) Neurobiol Aging , vol.28 , pp. 713-718
    • Sousa, J.C.1    Cardoso, I.2    Marques, F.3    Saraiva, M.J.4    Palha, J.A.5
  • 107
    • 33645147707 scopus 로고    scopus 로고
    • Prion disease genetics
    • PMID:16391566
    • Mead S. Prion disease genetics. Eur J Hum Genet 2006; 14:273-81; PMID:16391566; http://dx.doi.org/10.1038/sj.ejhg.5201544
    • (2006) Eur J Hum Genet , vol.14 , pp. 273-281
    • Mead, S.1
  • 108
    • 77249108916 scopus 로고    scopus 로고
    • PrPSc accumulation in neuronal plasma membranes links Notch-1 activation to dendritic degeneration in prion diseases
    • Dearmond SJ, Bajsarowicz K. PrPSc accumulation in neuronal plasma membranes links Notch-1 activation to dendritic degeneration in prion diseases. Mol Neurodegeneration 2010; 5:6; http://dx. doi.org/10.1186/1750-1326-5-6
    • (2010) Mol Neurodegeneration , vol.5 , pp. 6
    • Dearmond, S.J.1    Bajsarowicz, K.2
  • 109
    • 34250351315 scopus 로고    scopus 로고
    • Perturbation of endoplasmic reticulum homeostasis facilitates prion replication
    • PMID:17329244
    • Hetz C, Castilla J, Soto C. Perturbation of endoplasmic reticulum homeostasis facilitates prion replication. J Biol Chem 2007; 282:12725-33; PMID:17329244
    • (2007) J Biol Chem , vol.282 , pp. 12725-12733
    • Hetz, C.1    Castilla, J.2    Soto, C.3
  • 110
    • 33646175291 scopus 로고    scopus 로고
    • Stressing out the ER: A role of the unfolded protein response in prion-related disorders
    • PMID:16472111
    • Hetz CA, Soto C. Stressing out the ER: a role of the unfolded protein response in prion-related disorders. Curr Mol Med 2006; 6:37-43; PMID:16472111; http://dx.doi.org/10.2174/156652406775574578
    • (2006) Curr Mol Med , vol.6 , pp. 37-43
    • Hetz, C.A.1    Soto, C.2
  • 111
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer b-amyloid fibrils
    • PMID:15653506
    • Petkova AT, Leapman RD, Guo Z, Yau WM, Mattson MP, Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer b-amyloid fibrils. Science 2005; 307:262-5; PMID:15653506; http://dx.doi.org/10.1126/science.1105850
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 113
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • PMID:19282288
    • Frost B, Jacks RL, Diamond MI. Propagation of tau misfolding from the outside to the inside of a cell. J Biol Chem 2009; 284:12845-52; PMID:19282288; http://dx.doi.org/10.1074/jbc.M808759200
    • (2009) J Biol Chem , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 114
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • PMID:14532116
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003; 22:5435-45; PMID:14532116; http://dx.doi.org/10.1093/emboj/cdg537
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 115
    • 38049162500 scopus 로고    scopus 로고
    • Involvement of mitochondria in endoplasmic reticulum stressinduced apoptotic cell death pathway triggered by the prion peptide PrP(106-126)
    • PMID:17995926
    • Ferreiro E, Costa R, Marques S, Cardoso SM, Oliveira CR, Pereira CM. Involvement of mitochondria in endoplasmic reticulum stressinduced apoptotic cell death pathway triggered by the prion peptide PrP(106-126). J Neurochem 2008; 104:766-76; PMID:17995926
    • (2008) J Neurochem , vol.104 , pp. 766-776
    • Ferreiro, E.1    Costa, R.2    Marques, S.3    Cardoso, S.M.4    Oliveira, C.R.5    Pereira, C.M.6
  • 116
    • 84862001706 scopus 로고    scopus 로고
    • Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity
    • PMID:22685557
    • Wang SB, Shi Q, Xu Y, Xie WL, Zhang J, Tian C, Guo Y, Wang K, Zhang BY, Chen C, et al. Protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and PrP mutant-induced cytotoxicity. PloS One 2012; 7: e38221; PMID:22685557; http://dx.doi.org/10.1371/journal. pone.0038221
    • (2012) Plos One , vol.7
    • Wang, S.B.1    Shi, Q.2    Xu, Y.3    Xie, W.L.4    Zhang, J.5    Tian, C.6    Guo, Y.7    Wang, K.8    Zhang, B.Y.9    Chen, C.10
  • 118
    • 78649937640 scopus 로고    scopus 로고
    • Transcriptional analysis implicates endoplasmic reticulum stress in bovine spongiform encephalopathy
    • PMID:21151970
    • Tang Y, Xiang W, Terry L, Kretzschmar HA, Windl O. Transcriptional analysis implicates endoplasmic reticulum stress in bovine spongiform encephalopathy. PloS one 2010; 5:e14207; PMID:21151970; http://dx.doi.org/10.1371/journal.pone.0014207
    • (2010) Plos One , vol.5
    • Tang, Y.1    Xiang, W.2    Terry, L.3    Kretzschmar, H.A.4    Windl, O.5
  • 119
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-b peptides neurotoxicity
    • PMID:16844381
    • Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CM. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-b peptides neurotoxicity. Neurobiol Dis 2006; 23:669-78; PMID:16844381; http://dx.doi.org/10.1016/j. nbd.2006.05.011
    • (2006) Neurobiol Dis , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.5
  • 120
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • PMID:16908519
    • Orsi A, Fioriti L, Chiesa R, Sitia R. Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein. J Biol Chem 2006; 281:30431-8; PMID:16908519; http://dx.doi.org/10.1074/jbc.M605320200
    • (2006) J Biol Chem , vol.281 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 121
    • 78650843400 scopus 로고    scopus 로고
    • Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress
    • PMID:21209925
    • Torres M, Castillo K, Armisen R, Stutzin A, Soto C, Hetz C. Prion protein misfolding affects calcium homeostasis and sensitizes cells to endoplasmic reticulum stress. PloS One 2010; 5:e15658; PMID:21209925; http://dx.doi.org/10.1371/journal.pone.0015658
    • (2010) Plos One , vol.5
    • Torres, M.1    Castillo, K.2    Armisen, R.3    Stutzin, A.4    Soto, C.5    Hetz, C.6
  • 122
    • 38649108109 scopus 로고    scopus 로고
    • Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis
    • PMID:18178615
    • Hetz C, Lee AH, Gonzalez-Romero D, Thielen P, Castilla J, Soto C, Glimcher LH. Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. Proc Natl Acad Sci U S A 2008; 105:757-62; PMID:18178615; http://dx.doi.org/10.1073/pnas.0711094105
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 757-762
    • Hetz, C.1    Lee, A.H.2    Gonzalez-Romero, D.3    Thielen, P.4    Castilla, J.5    Soto, C.6    Glimcher, L.H.7
  • 125
    • 79551568451 scopus 로고    scopus 로고
    • Reticulon 3 attenuates the clearance of cytosolic prion aggregates via inhibiting autophagy
    • PMID:21119307
    • Chen R, Jin R, Wu L, Ye X, Yang Y, Luo K, Wang W, Wu D, Ye X, Huang L, et al. Reticulon 3 attenuates the clearance of cytosolic prion aggregates via inhibiting autophagy. Autophagy 2011; 7:205-16; PMID:21119307; http://dx.doi.org/10.4161/auto.7.2.14197
    • (2011) Autophagy , vol.7 , pp. 205-216
    • Chen, R.1    Jin, R.2    Wu, L.3    Ye, X.4    Yang, Y.5    Luo, K.6    Wang, W.7    Wu, D.8    Ye, X.9    Huang, L.10
  • 127
    • 84868139191 scopus 로고    scopus 로고
    • Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity
    • PMID:22575359
    • Jeong JK, Moon MH, Lee YJ, Seol JW, Park SY. Autophagy induced by the class III histone deacetylase Sirt1 prevents prion peptide neurotoxicity. Neurobiol Aging 2013; 34:146-56; PMID:22575359; http://dx.doi.org/10.1016/j.neurobiolaging.2012.04.002
    • (2013) Neurobiol Aging , vol.34 , pp. 146-156
    • Jeong, J.K.1    Moon, M.H.2    Lee, Y.J.3    Seol, J.W.4    Park, S.Y.5
  • 128
    • 61849102412 scopus 로고    scopus 로고
    • Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy
    • PMID:19183256
    • Heiseke A, Aguib Y, Riemer C, Baier M, Schatzl HM. Lithium induces clearance of protease resistant prion protein in prion-infected cells by induction of autophagy. J Neurochem 2009; 109:25-34; PMID:19183256; http://dx.doi.org/10.1111/j.1471-4159.2009.05906.x
    • (2009) J Neurochem , vol.109 , pp. 25-34
    • Heiseke, A.1    Aguib, Y.2    Riemer, C.3    Baier, M.4    Schatzl, H.M.5
  • 129
    • 65249103439 scopus 로고    scopus 로고
    • Autophagy induction by trehalose counteracts cellular prion infection
    • PMID:19182537
    • Aguib Y, Heiseke A, Gilch S, Riemer C, Baier M, Schatzl HM, Ertmer A. Autophagy induction by trehalose counteracts cellular prion infection. Autophagy 2009; 5:361-9; PMID:19182537; http://dx.doi. org/10.4161/auto.5.3.7662
    • (2009) Autophagy , vol.5 , pp. 361-369
    • Aguib, Y.1    Heiseke, A.2    Gilch, S.3    Riemer, C.4    Baier, M.5    Schatzl, H.M.6    Ertmer, A.7
  • 130
    • 84865749298 scopus 로고    scopus 로고
    • Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Straussler-Scheinker disease
    • PMID:22956830
    • Cortes CJ, Qin K, Cook J, Solanki A, Mastrianni JA. Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Straussler-Scheinker disease. J Neurosci 2012; 32:12396-405; PMID:22956830; http://dx.doi.org/10.1523/JNEUROSCI.6189-11.2012
    • (2012) J Neurosci , vol.32 , pp. 12396-12405
    • Cortes, C.J.1    Qin, K.2    Cook, J.3    Solanki, A.4    Mastrianni, J.A.5
  • 132
    • 0032497504 scopus 로고    scopus 로고
    • Parkinson disease. First of two parts
    • Lang AE, Lozano AM. Parkinson disease. First of two parts. N Eng J Med 1998; 339:1044-53; http://dx.doi.org/10.1056/NEJM199810083391506
    • (1998) N Eng J Med , vol.339 , pp. 1044-1053
    • Lang, A.E.1    Lozano, A.M.2
  • 133
    • 0032531924 scopus 로고    scopus 로고
    • Parkinson disease. Second of two parts
    • Lang AE, Lozano AM. Parkinson disease. Second of two parts. N Eng J med 1998; 339:1130-43; http://dx.doi.org/10.1056/NEJM199810153391607
    • (1998) N Eng J Med , vol.339 , pp. 1130-1143
    • Lang, A.E.1    Lozano, A.M.2
  • 134
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson disease
    • PMID:12486162
    • Ryu EJ, Harding HP, Angelastro JM, Vitolo OV, Ron D, Greene LA. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson disease. J Neurosci 2002; 22:10690-8; PMID:12486162
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 137
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of a-synucleinopathy in vivo
    • Colla E, Coune P, Liu Y, Pletnikova O, Troncoso JC, Iwatsubo T, Schneider BL, Lee MK. Endoplasmic reticulum stress is important for the manifestations of a-synucleinopathy in vivo. J Neurosc 2012; 32:3306-20; http://dx.doi.org/10.1523/JNEUROSCI.5367-11.2012
    • (2012) J Neurosc , vol.32 , pp. 3306-3320
    • Colla, E.1    Coune, P.2    Liu, Y.3    Pletnikova, O.4    Troncoso, J.C.5    Iwatsubo, T.6    Schneider, B.L.7    Lee, M.K.8
  • 138
    • 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
    • PMID:16135078
    • Silva RM, Ries V, Oo TF, Yarygina O, Jackson-Lewis V, Ryu EJ, Lu PD, Marciniak SJ, Ron D, Przedborski S, 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 2005; 95:974-86; PMID:16135078; http://dx.doi.org/10.1111/j.1471-4159.2005.03428.x
    • (2005) J Neurochem , vol.95 , pp. 974-986
    • Silva, R.M.1    Ries, V.2    Oo, T.F.3    Yarygina, O.4    Jackson-Lewis, V.5    Ryu, E.J.6    Lu, P.D.7    Marciniak, S.J.8    Ron, D.9    Przedborski, S.10
  • 139
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy
    • PMID:15333840
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant a-synuclein by chaperone-mediated autophagy. Science 2004; 305:1292-5; PMID:15333840; http://dx.doi. org/10.1126/science.1101738
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 140
    • 33644778845 scopus 로고    scopus 로고
    • Parkin enhances mitochondrial biogenesis in proliferating cells
    • PMID:16449237
    • Kuroda Y, Mitsui T, Kunishige M, Shono M, Akaike M, Azuma H, Matsumoto T. Parkin enhances mitochondrial biogenesis in proliferating cells. Hum Mol Genet 2006; 15:883-95; PMID:16449237; http://dx.doi.org/10.1093/hmg/ddl006
    • (2006) Hum Mol Genet , vol.15 , pp. 883-895
    • Kuroda, Y.1    Mitsui, T.2    Kunishige, M.3    Shono, M.4    Akaike, M.5    Azuma, H.6    Matsumoto, T.7
  • 141
    • 84871005673 scopus 로고    scopus 로고
    • The pathways of mitophagy for quality control and clearance of mitochondria
    • PMID:22743996
    • Ashrafi G, Schwarz TL. The pathways of mitophagy for quality control and clearance of mitochondria. Cell Death Differ 2013; 20:31-42; PMID:22743996; http://dx.doi.org/10.1038/cdd.2012.81
    • (2013) Cell Death Differ , vol.20 , pp. 31-42
    • Ashrafi, G.1    Schwarz, T.L.2
  • 142
    • 77958450202 scopus 로고    scopus 로고
    • Inhibition of mitochondrial fusion by a-synuclein is rescued by PINK1, Parkin and DJ-1
    • PMID:20842103
    • Kamp F, Exner N, Lutz AK, Wender N, Hegermann J, Brunner B, Nuscher B, Bartels T, Giese A, Beyer K, et al. Inhibition of mitochondrial fusion by a-synuclein is rescued by PINK1, Parkin and DJ-1. EMBO J 2010; 29:3571-89; PMID:20842103; http://dx.doi.org/10.1038/emboj.2010.223
    • (2010) EMBO J , vol.29 , pp. 3571-3589
    • Kamp, F.1    Exner, N.2    Lutz, A.K.3    Wender, N.4    Hegermann, J.5    Brunner, B.6    Nuscher, B.7    Bartels, T.8    Giese, A.9    Beyer, K.10
  • 143
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • PMID:10973942
    • Imai Y, Soda M, Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 2000; 275:35661-4; PMID:10973942; http://dx. doi.org/10.1074/jbc.C000447200
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 144
    • 84907892583 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induced by tunicamycin and thapsigargin protects against transient ischemic brain injury: Involvement of PARK2-dependent mitophagy
    • PMID:25126734
    • Zhang X, Yuan Y, Jiang L, Zhang J, Gao J, Shen Z, Zheng Y, Deng T, Yan H, Li W, et al. Endoplasmic reticulum stress induced by tunicamycin and thapsigargin protects against transient ischemic brain injury: Involvement of PARK2-dependent mitophagy. Autophagy 2014; 10:1801-13; PMID:25126734; http://dx.doi.org/10.4161/auto.32136
    • (2014) Autophagy , vol.10 , pp. 1801-1813
    • Zhang, X.1    Yuan, Y.2    Jiang, L.3    Zhang, J.4    Gao, J.5    Shen, Z.6    Zheng, Y.7    Deng, T.8    Yan, H.9    Li, W.10
  • 145
    • 84891300736 scopus 로고    scopus 로고
    • Ubiquitination increases parkin activity to promote autophagic a-synuclein clearance
    • PMID:24386307
    • Lonskaya I, Desforges NM, Hebron ML, Moussa CE. Ubiquitination increases parkin activity to promote autophagic a-synuclein clearance. PloS One 2013; 8:e83914; PMID:24386307; http://dx.doi.org/10.1371/journal.pone.0083914
    • (2013) Plos One , vol.8
    • Lonskaya, I.1    Desforges, N.M.2    Hebron, M.L.3    Moussa, C.E.4
  • 146
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • PMID:16924260
    • Pasinelli P, Brown RH. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 2006; 7:710-23; PMID:16924260; http://dx.doi.org/10.1038/nrn1971
    • (2006) Nat Rev Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 148
    • 23844538993 scopus 로고    scopus 로고
    • The pathobiology of amyotrophic lateral sclerosis: A proteinopathy?
    • PMID:16106213
    • Strong MJ, Kesavapany S, Pant HC. The pathobiology of amyotrophic lateral sclerosis: a proteinopathy? J Neuropathol Exp Neurol 2005; 64:649-64; PMID:16106213; http://dx.doi.org/10.1097/01. jnen.0000173889.71434.ea
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 649-664
    • Strong, M.J.1    Kesavapany, S.2    Pant, H.C.3
  • 149
    • 65449130022 scopus 로고    scopus 로고
    • TARDBP (TDP-43) sequence analysis in patients with familial and sporadic ALS: Identification of two novel mutations
    • PMID:19236453
    • Del Bo R, Ghezzi S, Corti S, Pandolfo M, Ranieri M, Santoro D, Ghione I, Prelle A, Orsetti V, Mancuso M, et al. TARDBP (TDP-43) sequence analysis in patients with familial and sporadic ALS: identification of two novel mutations. Eur J Neurol 2009; 16:727-32; PMID:19236453; http://dx.doi.org/10.1111/j.1468-1331.2008.02424.x
    • (2009) Eur J Neurol , vol.16 , pp. 727-732
    • Del Bo, R.1    Ghezzi, S.2    Corti, S.3    Pandolfo, M.4    Ranieri, M.5    Santoro, D.6    Ghione, I.7    Prelle, A.8    Orsetti, V.9    Mancuso, M.10
  • 150
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • PMID:18372902
    • Kabashi E, Valdmanis PN, Dion P, Spiegelman D, McConkey BJ, Vande Velde C, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 2008; 40:572-4; PMID:18372902; http://dx.doi.org/10.1038/ng.132
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Spiegelman, D.4    McConkey, B.J.5    Vande Velde, C.6
  • 152
    • 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
    • PMID:16847061
    • Atkin JD, Farg MA, Turner BJ, Tomas D, Lysaght JA, Nunan J, Rembach A, Nagley P, Beart PM, Cheema SS, 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 2006; 281:30152-65; PMID:16847061; http://dx.doi.org/10.1074/jbc.M603393200
    • (2006) J Biol Chem , vol.281 , pp. 30152-30165
    • Atkin, J.D.1    Farg, M.A.2    Turner, B.J.3    Tomas, D.4    Lysaght, J.A.5    Nunan, J.6    Rembach, A.7    Nagley, P.8    Beart, P.M.9    Cheema, S.S.10
  • 153
    • 27644485845 scopus 로고    scopus 로고
    • ATF3 expression precedes death of spinal motoneurons in amyotrophic lateral sclerosis-SOD1 transgenic mice and correlates with c-Jun phosphorylation, CHOP expression, somato-dendritic ubiquitination and Golgi fragmentation
    • PMID:16262628
    • Vlug AS, Teuling E, Haasdijk ED, French P, Hoogenraad CC, Jaarsma D. ATF3 expression precedes death of spinal motoneurons in amyotrophic lateral sclerosis-SOD1 transgenic mice and correlates with c-Jun phosphorylation, CHOP expression, somato-dendritic ubiquitination and Golgi fragmentation. Eur J Neurosci 2005; 22:1881-94; PMID:16262628; http://dx.doi.org/10.1111/j.1460-9568.2005.04389.x
    • (2005) Eur J Neurosci , vol.22 , pp. 1881-1894
    • Vlug, A.S.1    Teuling, E.2    Haasdijk, E.D.3    French, P.4    Hoogenraad, C.C.5    Jaarsma, D.6
  • 154
    • 38049097948 scopus 로고    scopus 로고
    • Deletion of the BH3-only protein puma protects motoneurons from ER stressinduced apoptosis and delays motoneuron loss in ALS mice
    • PMID:18077368
    • Kieran D, Woods I, Villunger A, Strasser A, Prehn JH. Deletion of the BH3-only protein puma protects motoneurons from ER stressinduced apoptosis and delays motoneuron loss in ALS mice. Proc Natl Acad Sci U S A 2007; 104:20606-11; PMID:18077368; http://dx. doi.org/10.1073/pnas.0707906105
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20606-20611
    • Kieran, D.1    Woods, I.2    Villunger, A.3    Strasser, A.4    Prehn, J.H.5
  • 156
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • PMID:19762508
    • Hetz C, Thielen P, Matus S, Nassif M, Court F, Kiffin R, Martinez G, Cuervo AM, Brown RH, Glimcher LH. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev 2009; 23:2294-306; PMID:19762508; http://dx.doi.org/10.1101/gad.1830709
    • (2009) Genes Dev , vol.23 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5    Kiffin, R.6    Martinez, G.7    Cuervo, A.M.8    Brown, R.H.9    Glimcher, L.H.10
  • 157
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • PMID:18957508
    • Ayala YM, Zago P, D’Ambrogio A, Xu YF, Petrucelli L, Buratti E, Baralle FE. Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci 2008; 121:3778-85; PMID:18957508; http://dx.doi.org/10.1242/jcs.038950
    • (2008) J Cell Sci , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1    Zago, P.2    D’Ambrogio, A.3    Xu, Y.F.4    Petrucelli, L.5    Buratti, E.6    Baralle, F.E.7
  • 158
    • 84857772495 scopus 로고    scopus 로고
    • TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes
    • PMID:22323604
    • Kawahara Y, Mieda-Sato A. TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes. Proc Natl Acad Sci U S A 2012; 109:3347-52; PMID:22323604; http://dx.doi.org/10.1073/pnas.1112427109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 3347-3352
    • Kawahara, Y.1    Mieda-Sato, A.2
  • 159
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • PMID:20071528
    • Barmada SJ, Skibinski G, Korb E, Rao EJ, Wu JY, Finkbeiner S. Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J Neurosci 2010; 30:639-49; PMID:20071528; http://dx.doi.org/10.1523/JNEUROSCI.4988-09.2010
    • (2010) J Neurosci , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 160
    • 84896710448 scopus 로고    scopus 로고
    • ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation
    • PMID:24312274
    • Walker AK, Soo KY, Sundaramoorthy V, Parakh S, Ma Y, Farg MA, Wallace RH, Crouch PJ, Turner BJ, Horne MK, et al. ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PloS One 2013; 8:e81170; PMID:24312274; http://dx.doi.org/10.1371/journal.pone.0081170
    • (2013) Plos One , vol.8
    • Walker, A.K.1    Soo, K.Y.2    Sundaramoorthy, V.3    Parakh, S.4    Ma, Y.5    Farg, M.A.6    Wallace, R.H.7    Crouch, P.J.8    Turner, B.J.9    Horne, M.K.10
  • 161
    • 84866748196 scopus 로고    scopus 로고
    • Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase
    • PMID:22459602
    • Farg MA, Soo KY, Walker AK, Pham H, Orian J, Horne MK, Warraich ST, Williams KL, Blair IP, Atkin JD. Mutant FUS induces endoplasmic reticulum stress in amyotrophic lateral sclerosis and interacts with protein disulfide-isomerase. Neurobiol Aging 2012; 33:2855-68; PMID:22459602; http://dx.doi.org/10.1016/j. neurobiolaging.2012.02.009
    • (2012) Neurobiol Aging , vol.33 , pp. 2855-2868
    • Farg, M.A.1    Soo, K.Y.2    Walker, A.K.3    Pham, H.4    Orian, J.5    Horne, M.K.6    Warraich, S.T.7    Williams, K.L.8    Blair, I.P.9    Atkin, J.D.10
  • 162
    • 84929708271 scopus 로고    scopus 로고
    • Autophagy receptor defects and ALS-FTLD
    • PMID:25683489
    • Majcher V, Goode A, James V, Layfield R. Autophagy receptor defects and ALS-FTLD. Mol Cell Neurosci 2015; 66:43-52; PMID:25683489; http://dx.doi.org/10.1016/j.mcn.2015.01.002
    • (2015) Mol Cell Neurosci , vol.66 , pp. 43-52
    • Majcher, V.1    Goode, A.2    James, V.3    Layfield, R.4
  • 163
    • 84455169931 scopus 로고    scopus 로고
    • Regulation of autophagy by neuropathological protein TDP-43
    • PMID:22052911
    • Bose JK, Huang CC, Shen CK. Regulation of autophagy by neuropathological protein TDP-43. J Biol Chem 2011; 286:44441-8; PMID:22052911; http://dx.doi.org/10.1074/jbc.M111.237115
    • (2011) J Biol Chem , vol.286 , pp. 44441-44448
    • Bose, J.K.1    Huang, C.C.2    Shen, C.K.3
  • 164
    • 77955784599 scopus 로고    scopus 로고
    • ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
    • PMID:20624952
    • Ling SC, Albuquerque CP, Han JS, Lagier-Tourenne C, Tokunaga S, Zhou H, Cleveland DW. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc Natl Acad Sci U S A 2010; 107:13318-23; PMID:20624952; http://dx.doi.org/10.1073/pnas.1008227107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 13318-13323
    • Ling, S.C.1    Albuquerque, C.P.2    Han, J.S.3    Lagier-Tourenne, C.4    Tokunaga, S.5    Zhou, H.6    Cleveland, D.W.7
  • 166
    • 84911386329 scopus 로고    scopus 로고
    • Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons
    • PMID:25216585
    • Ryu HH, Jun MH, Min KJ, Jang DJ, Lee YS, Kim HK, Lee JA. Autophagy regulates amyotrophic lateral sclerosis-linked fused in sarcoma-positive stress granules in neurons. Neurobiol Aging 2014; 35:2822-31; PMID:25216585; http://dx.doi.org/10.1016/j. neurobiolaging.2014.07.026
    • (2014) Neurobiol Aging , vol.35 , pp. 2822-2831
    • Ryu, H.H.1    Jun, M.H.2    Min, K.J.3    Jang, D.J.4    Lee, Y.S.5    Kim, H.K.6    Lee, J.A.7
  • 167
    • 84880037292 scopus 로고    scopus 로고
    • Optineurin and amyotrophic lateral sclerosis
    • PMID:23279185
    • Maruyama H, Kawakami H. Optineurin and amyotrophic lateral sclerosis. Geriatr Gerontol Int 2013; 13:528-32; PMID:23279185; http://dx.doi.org/10.1111/ggi.12022
    • (2013) Geriatr Gerontol Int , vol.13 , pp. 528-532
    • Maruyama, H.1    Kawakami, H.2
  • 168
    • 84867103427 scopus 로고    scopus 로고
    • Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome
    • PMID:23023224
    • Tumbarello DA, Waxse BJ, Arden SD, Bright NA, Kendrick-Jones J, Buss F. Autophagy receptors link myosin VI to autophagosomes to mediate Tom1-dependent autophagosome maturation and fusion with the lysosome. Nat Cell Biol 2012; 14:1024-35; PMID:23023224; http://dx.doi.org/10.1038/ncb2589
    • (2012) Nat Cell Biol , vol.14 , pp. 1024-1035
    • Tumbarello, D.A.1    Waxse, B.J.2    Arden, S.D.3    Bright, N.A.4    Kendrick-Jones, J.5    Buss, F.6
  • 169
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • PMID:25294927
    • Wong YC, Holzbaur EL. Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc Natl Acad Sci U S A 2014; 111:E4439-48; PMID:25294927; http://dx.doi.org/10.1073/pnas.1405752111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. E4439-E4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 170
    • 84873654068 scopus 로고    scopus 로고
    • Age-dependent molecular alterations in the autophagy pathway in HIVE patients and in a gp120 tg mouse model: Reversal with beclin-1 gene transfer
    • PMID:23341224
    • Fields J, Dumaop W, Rockenstein E, Mante M, Spencer B, Grant I, Ellis R, Letendre S, Patrick C, Adame A, et al. Age-dependent molecular alterations in the autophagy pathway in HIVE patients and in a gp120 tg mouse model: reversal with beclin-1 gene transfer. J Neurovirol 2013; 19: 89-101; PMID:23341224; http://dx.doi.org/10.1007/s13365-012-0145-7
    • (2013) J Neurovirol , vol.19 , pp. 89-101
    • Fields, J.1    Dumaop, W.2    Rockenstein, E.3    Mante, M.4    Spencer, B.5    Grant, I.6    Ellis, R.7    Letendre, S.8    Patrick, C.9    Adame, A.10
  • 171
    • 84958121533 scopus 로고    scopus 로고
    • Role of Sigma Receptor in Cocaine-Mediated Induction of Glial Fibrillary Acidic Protein: Implications for HAND
    • Epub ahead of printPMID:25631712
    • Yang L, Yao H, Chen X, Cai Y, Callen S, Buch S. Role of Sigma Receptor in Cocaine-Mediated Induction of Glial Fibrillary Acidic Protein: Implications for HAND. Mol Neurobiol 2015; [Epub ahead of print]; PMID:25631712; http://dx.doi.org/10.1007/s12035-015-9094-5
    • (2015) Mol Neurobiol
    • Yang, L.1    Yao, H.2    Chen, X.3    Cai, Y.4    Callen, S.5    Buch, S.6
  • 172
    • 84953354467 scopus 로고    scopus 로고
    • HIV Tat-Mediated Induction of Human Brain Microvascular Endothelial Cell Apoptosis Involves Endoplasmic Reticulum Stress and Mitochondrial Dysfunction
    • Ma R, Yang L, Niu F, Buch S. HIV Tat-Mediated Induction of Human Brain Microvascular Endothelial Cell Apoptosis Involves Endoplasmic Reticulum Stress and Mitochondrial Dysfunction. Mol Neurobiol 2014; 2016; 53:132-42; http://dx.doi.org/10.1007/s12035-014-8991-3
    • (2016) Mol Neurobiol 2014 , vol.53 , pp. 132-142
    • Ma, R.1    Yang, L.2    Niu, F.3    Buch, S.4
  • 173
    • 84863229175 scopus 로고    scopus 로고
    • Activation status of integrated stress response pathways in neurones and astrocytes of HIV-associated neurocognitive disorders (HAND) cortex
    • PMID:21883374
    • Akay C, Lindl KA, Shyam N, Nabet B, Goenaga-Vazquez Y, Ruzbarsky J, Wang Y, Kolson DL, Jordan-Sciutto KL. Activation status of integrated stress response pathways in neurones and astrocytes of HIV-associated neurocognitive disorders (HAND) cortex. Neuropathol Appl Neurobiol 2012; 38:175-200; PMID:21883374; http://dx. doi.org/10.1111/j.1365-2990.2011.01215.x
    • (2012) Neuropathol Appl Neurobiol , vol.38 , pp. 175-200
    • Akay, C.1    Lindl, K.A.2    Shyam, N.3    Nabet, B.4    Goenaga-Vazquez, Y.5    Ruzbarsky, J.6    Wang, Y.7    Kolson, D.L.8    Jordan-Sciutto, K.L.9
  • 174
    • 33745101399 scopus 로고    scopus 로고
    • The immunophilin ligand GPI1046 protects neurons from the lethal effects of the HIV-1 proteins gp120 and Tat by modulating endoplasmic reticulum calcium load
    • PMID:16805804
    • Caporello E, Nath A, Slevin J, Galey D, Hamilton G, Williams L, Steiner JP, Haughey NJ. The immunophilin ligand GPI1046 protects neurons from the lethal effects of the HIV-1 proteins gp120 and Tat by modulating endoplasmic reticulum calcium load. J Neurochem 2006; 98:146-55; PMID:16805804; http://dx.doi.org/10.1111/j.1471-4159.2006.03863.x
    • (2006) J Neurochem , vol.98 , pp. 146-155
    • Caporello, E.1    Nath, A.2    Slevin, J.3    Galey, D.4    Hamilton, G.5    Williams, L.6    Steiner, J.P.7    Haughey, N.J.8
  • 175
    • 84943809647 scopus 로고    scopus 로고
    • Cocaine mediated microglial activation involves the ER stress-Autophagy axis
    • PMID:26043790
    • Guo ML, Liao K, Periyasamy P, Yang L, Cai Y, Callen SE, Buch S. Cocaine mediated microglial activation involves the ER stress-Autophagy axis. Autophagy 2015; 11(7):995-1009; PMID:26043790; http://dx.doi.org/10.1080/15548627.2015.1052205
    • (2015) Autophagy , vol.11 , Issue.7 , pp. 995-1009
    • Guo, M.L.1    Liao, K.2    Periyasamy, P.3    Yang, L.4    Cai, Y.5    Callen, S.E.6    Buch, S.7
  • 176
    • 53549096775 scopus 로고    scopus 로고
    • Decreased neuronal autophagy in HIV dementia: A mechanism of indirect neurotoxicity
    • PMID:18772620
    • Alirezaei M, Kiosses WB, Fox HS. Decreased neuronal autophagy in HIV dementia: a mechanism of indirect neurotoxicity. Autophagy 2008; 4:963-6; PMID:18772620; http://dx.doi.org/10.4161/auto.6805
    • (2008) Autophagy , vol.4 , pp. 963-966
    • Alirezaei, M.1    Kiosses, W.B.2    Fox, H.S.3
  • 177
    • 51449119611 scopus 로고    scopus 로고
    • Disruption of neuronal autophagy by infected microglia results in neurodegeneration
    • Alirezaei M, Kiosses WB, Flynn CT, Brady NR, Fox HS. Disruption of neuronal autophagy by infected microglia results in neurodegeneration. Plos One 2008; 3:e2906; http://dx.doi.org/10.1371/journal.pone.0002906
    • (2008) Plos One , vol.3
    • Alirezaei, M.1    Kiosses, W.B.2    Flynn, C.T.3    Brady, N.R.4    Fox, H.S.5
  • 178
    • 79956204926 scopus 로고    scopus 로고
    • Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis
    • PMID:21592995
    • Zhou D, Masliah E, Spector SA. Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis. J Infect Dis 2011; 203:1647-57; PMID:21592995; http://dx.doi.org/10.1093/infdis/jir163
    • (2011) J Infect Dis , vol.203 , pp. 1647-1657
    • Zhou, D.1    Masliah, E.2    Spector, S.A.3
  • 179
    • 67649585835 scopus 로고    scopus 로고
    • Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages
    • PMID:19635843
    • Kyei GB, Dinkins C, Davis AS, Roberts E, Singh SB, Dong C, Wu L, Kominami E, Ueno T, Yamamoto A, et al. Autophagy pathway intersects with HIV-1 biosynthesis and regulates viral yields in macrophages. J Cell Biol 2009; 186:255-68; PMID:19635843; http://dx.doi. org/10.1083/jcb.200903070
    • (2009) J Cell Biol , vol.186 , pp. 255-268
    • Kyei, G.B.1    Dinkins, C.2    Davis, A.S.3    Roberts, E.4    Singh, S.B.5    Dong, C.6    Wu, L.7    Kominami, E.8    Ueno, T.9    Yamamoto, A.10
  • 180
    • 78650310661 scopus 로고    scopus 로고
    • HIV-1 trans-activator protein dysregulates IFN-gamma signaling and contributes to the suppression of autophagy induction
    • PMID:21099673
    • Li JC, Au KY, Fang JW, Yim HC, Chow KH, Ho PL, Lau AS. HIV-1 trans-activator protein dysregulates IFN-gamma signaling and contributes to the suppression of autophagy induction. Aids 2011; 25:15-25; PMID:21099673; http://dx.doi.org/10.1097/QAD.0b013e328340fd61
    • (2011) Aids , vol.25 , pp. 15-25
    • Li, J.C.1    Au, K.Y.2    Fang, J.W.3    Yim, H.C.4    Chow, K.H.5    Ho, P.L.6    Lau, A.S.7
  • 181
    • 77955375856 scopus 로고    scopus 로고
    • HIV-1 Inhibits Autophagy in Bystander Macrophage/Monocytic Cells through Src-Akt and STAT3
    • Van Grol J, Subauste C, Andrade RM, Fujinaga K, Nelson J, Subauste CS. HIV-1 Inhibits Autophagy in Bystander Macrophage/Monocytic Cells through Src-Akt and STAT3. PloS One 2010; 5:14
    • (2010) Plos One , vol.5 , pp. 14
    • Van Grol, J.1    Subauste, C.2    Rade, R.M.3    Fujinaga, K.4    Nelson, J.5    Subauste, C.S.6
  • 182
    • 84867592757 scopus 로고    scopus 로고
    • Role of endolysosomes in HIV-1 Tat-induced neurotoxicity
    • PMID:22591512
    • Hui L, Chen XS, Haughey NJ, Geiger JD. Role of endolysosomes in HIV-1 Tat-induced neurotoxicity. Asn Neuro 2012; 4:243-52; PMID:22591512; http://dx.doi.org/10.1042/AN20120017
    • (2012) Asn Neuro , vol.4 , pp. 243-252
    • Hui, L.1    Chen, X.S.2    Haughey, N.J.3    Geiger, J.D.4
  • 183
    • 84922390366 scopus 로고    scopus 로고
    • HIV-1 Tat Alters Neuronal Autophagy by Modulating Autophagosome Fusion to the Lysosome: Implications for HIV-Associated Neurocognitive Disorders
    • PMID:25653352
    • Fields J, Dumaop W, Elueteri S, Campos S, Serger E, Trejo M, Kosberg K, Adame A, Spencer B, Rockenstein E, et al. HIV-1 Tat Alters Neuronal Autophagy by Modulating Autophagosome Fusion to the Lysosome: Implications for HIV-Associated Neurocognitive Disorders. J Neurosci 2015; 35:1921-38; PMID:25653352; http://dx.doi. org/10.1523/JNEUROSCI.3207-14.2015
    • (2015) J Neurosci , vol.35 , pp. 1921-1938
    • Fields, J.1    Dumaop, W.2    Elueteri, S.3    Campos, S.4    Serger, E.5    Trejo, M.6    Kosberg, K.7    Adame, A.8    Spencer, B.9    Rockenstein, E.10
  • 184
    • 77950853379 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis
    • PMID:20448480
    • Sasaki S. Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2010; 69:346-55; PMID:20448480; http://dx.doi.org/10.1097/NEN.0b013e3181d44992
    • (2010) J Neuropathol Exp Neurol , vol.69 , pp. 346-355
    • Sasaki, S.1
  • 185
    • 84876991539 scopus 로고    scopus 로고
    • Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments
    • PMID:23583182
    • Shoulders MD, Ryno LM, Genereux JC, Moresco JJ, Tu PG, Wu C, Yates JR, 3rd, Su AI, Kelly JW, Wiseman RL. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Reports 2013; 3:1279-92; PMID:23583182; http://dx.doi.org/10.1016/j.celrep.2013.03.024
    • (2013) Cell Reports , vol.3 , pp. 1279-1292
    • Shoulders, M.D.1    Ryno, L.M.2    Genereux, J.C.3    Moresco, J.J.4    Tu, P.G.5    Wu, C.6    Yates, J.R.7    Su, A.I.8    Kelly, J.W.9    Wiseman, R.L.10
  • 188
    • 66449134941 scopus 로고    scopus 로고
    • VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death
    • PMID:19237541
    • Gitcho MA, Strider J, Carter D, Taylor-Reinwald L, Forman MS, Goate AM, Cairns NJ. VCP mutations causing frontotemporal lobar degeneration disrupt localization of TDP-43 and induce cell death. J Biol Chem 2009; 284:12384-98; PMID:19237541; http://dx.doi.org/10.1074/jbc.M900992200
    • (2009) J Biol Chem , vol.284 , pp. 12384-12398
    • Gitcho, M.A.1    Strider, J.2    Carter, D.3    Taylor-Reinwald, L.4    Forman, M.S.5    Goate, A.M.6    Cairns, N.J.7
  • 189
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia
    • PMID:21857683
    • Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, Yang Y, Fecto F, Shi Y, Zhai H, et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS/dementia. Nature 2011; 477:211-5; PMID:21857683; http://dx.doi.org/10.1038/nature10353
    • (2011) Nature , vol.477 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5    Siddique, N.6    Yang, Y.7    Fecto, F.8    Shi, Y.9    Zhai, H.10
  • 190
    • 79954594082 scopus 로고    scopus 로고
    • Optineurin inclusions occur in a minority of TDP-43 positive ALS and FTLD-TDP cases and are rarely observed in other neurodegenerative disorders
    • PMID:21360076
    • Hortobagyi T, Troakes C, Nishimura AL, Vance C, van Swieten JC, Seelaar H, King A, Al-Sarraj S, Rogelj B, Shaw CE. Optineurin inclusions occur in a minority of TDP-43 positive ALS and FTLD-TDP cases and are rarely observed in other neurodegenerative disorders. Acta Neuropathologica 2011; 121:519-27; PMID:21360076; http://dx. doi.org/10.1007/s00401-011-0813-3
    • (2011) Acta Neuropathologica , vol.121 , pp. 519-527
    • Hortobagyi, T.1    Troakes, C.2    Nishimura, A.L.3    Vance, C.4    Van Swieten, J.C.5    Seelaar, H.6    King, A.7    Al-Sarraj, S.8    Rogelj, B.9    Shaw, C.E.10
  • 191
    • 80855138704 scopus 로고    scopus 로고
    • Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau)
    • PMID:21720721
    • Dickson DW, Kouri N, Murray ME, Josephs KA. Neuropathology of frontotemporal lobar degeneration-tau (FTLD-tau). J Mol Neurosci 2011; 45:384-9; PMID:21720721; http://dx.doi.org/10.1007/s12031-011-9589-0
    • (2011) J Mol Neurosci , vol.45 , pp. 384-389
    • Dickson, D.W.1    Kouri, N.2    Murray, M.E.3    Josephs, K.A.4
  • 192
    • 0035900779 scopus 로고    scopus 로고
    • Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer disease-linked presenilin-1 mutations
    • PMID:11551913
    • Katayama T, Imaizumi K, Honda A, Yoneda T, Kudo T, Takeda M, Mori K, Rozmahel R, Fraser P, George-Hyslop PS, et al. Disturbed activation of endoplasmic reticulum stress transducers by familial Alzheimer disease-linked presenilin-1 mutations. J Biol Chem 2001; 276:43446-54; PMID:11551913; http://dx.doi.org/10.1074/jbc.M104096200
    • (2001) J Biol Chem , vol.276 , pp. 43446-43454
    • Katayama, T.1    Imaizumi, K.2    Honda, A.3    Yoneda, T.4    Kudo, T.5    Takeda, M.6    Mori, K.7    Rozmahel, R.8    Fraser, P.9    George-Hyslop, P.S.10
  • 193
    • 0036447671 scopus 로고    scopus 로고
    • The unfolded protein response is involved in the pathology of Alzheimer disease
    • PMID:12480772
    • Kudo T, Katayama T, Imaizumi K, Yasuda Y, Yatera M, Okochi M, Tohyama M, Takeda M. The unfolded protein response is involved in the pathology of Alzheimer disease. Ann N Y Acad Sci 2002; 977:349-55; PMID:12480772; http://dx.doi.org/10.1111/j.1749-6632.2002.tb04837.x
    • (2002) Ann N Y Acad Sci , vol.977 , pp. 349-355
    • Kudo, T.1    Katayama, T.2    Imaizumi, K.3    Yasuda, Y.4    Yatera, M.5    Okochi, M.6    Tohyama, M.7    Takeda, M.8
  • 194
    • 84867592757 scopus 로고    scopus 로고
    • Role of endolysosomes in HIV-1 Tat-induced neurotoxicity
    • PMID:22591512
    • Hui L, Chen X, Haughey NJ, Geiger JD. Role of endolysosomes in HIV-1 Tat-induced neurotoxicity. ASN neuro 2012; 4:243-52; PMID:22591512; http://dx.doi.org/10.1042/AN20120017
    • (2012) ASN Neuro , vol.4 , pp. 243-252
    • Hui, L.1    Chen, X.2    Haughey, N.J.3    Geiger, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.