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Volumn 2, Issue 1, 2014, Pages

Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies

Author keywords

Alpha synuclein; Apoptosis; Autophagy; Heat shock protein; Hsp70; Hsp90; Molecular chaperone; Neurodegeneration; Parkinson's disease; Proteasome

Indexed keywords


EID: 85005900833     PISSN: None     EISSN: 20515960     Source Type: Journal    
DOI: 10.1186/2051-5960-1-79     Document Type: Review
Times cited : (71)

References (197)
  • 1
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau LM, Breteler MM: Epidemiology of Parkinson's disease. Lancet Neurol 2006, 5: 525-535. 10.1016/S1474-4422(06)70471-9
    • (2006) Lancet Neurol , vol.5 , pp. 525-535
    • de Lau, L.M.1    Breteler, M.M.2
  • 2
    • 66949152096 scopus 로고    scopus 로고
    • Parkinson's disease
    • Lees AJ, Hardy J, Revesz T: Parkinson's disease. Lancet 2009, 373: 2055-2066. 10.1016/S0140-6736(09)60492-X
    • (2009) Lancet , vol.373 , pp. 2055-2066
    • Lees, A.J.1    Hardy, J.2    Revesz, T.3
  • 3
    • 84872729641 scopus 로고    scopus 로고
    • Parkinson's disease and parkinsonism: neuropathology
    • Dickson DW: Parkinson's disease and parkinsonism: neuropathology. Cold Spring Harb Perspect Med 2012, 2: a009258.
    • (2012) Cold Spring Harb Perspect Med , vol.2
    • Dickson, D.W.1
  • 5
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: from structure and toxicity to therapeutic target
    • Lashuel HA, Overk CR, Oueslati A, Masliah E: The many faces of alpha-synuclein: from structure and toxicity to therapeutic target. Nat Rev Neurosci 2013, 14: 38-48.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 6
    • 79960842310 scopus 로고    scopus 로고
    • Neuropathology underlying clinical variability in patients with synucleinopathies
    • Halliday GM, Holton JL, Revesz T, Dickson DW: Neuropathology underlying clinical variability in patients with synucleinopathies. Acta Neuropathol 2011, 122: 187-204. 10.1007/s00401-011-0852-9
    • (2011) Acta Neuropathol , vol.122 , pp. 187-204
    • Halliday, G.M.1    Holton, J.L.2    Revesz, T.3    Dickson, D.W.4
  • 8
    • 84883174947 scopus 로고    scopus 로고
    • Parkinson's disease dementia: convergence of alpha-synuclein, tau and amyloid-beta pathologies
    • Irwin DJ, Lee VM, Trojanowski JQ: Parkinson's disease dementia: convergence of alpha-synuclein, tau and amyloid-beta pathologies. Nat Rev Neurosci 2013, 14: 626-636. 10.1038/nrn3549
    • (2013) Nat Rev Neurosci , vol.14 , pp. 626-636
    • Irwin, D.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 13
    • 4644236043 scopus 로고    scopus 로고
    • Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease
    • Ibanez P, Bonnet AM, Debarges B, Lohmann E, Tison F, Pollak P, Agid Y, Durr A, Brice A: Causal relation between alpha-synuclein gene duplication and familial Parkinson's disease. Lancet 2004, 364: 1169-1171. 10.1016/S0140-6736(04)17104-3
    • (2004) Lancet , vol.364 , pp. 1169-1171
    • Ibanez, P.1    Bonnet, A.M.2    Debarges, B.3    Lohmann, E.4    Tison, F.5    Pollak, P.6    Agid, Y.7    Durr, A.8    Brice, A.9
  • 16
    • 84865861347 scopus 로고    scopus 로고
    • Molecular chaperones and co-chaperones in Parkinson disease
    • Dimant H, Ebrahimi-Fakhari D, McLean PJ: Molecular chaperones and co-chaperones in Parkinson disease. Neuroscientist 2012, 18: 589-601. 10.1177/1073858412441372
    • (2012) Neuroscientist , vol.18 , pp. 589-601
    • Dimant, H.1    Ebrahimi-Fakhari, D.2    McLean, P.J.3
  • 17
    • 84858263923 scopus 로고    scopus 로고
    • Molecular Chaperones in Parkinson's Disease - Present and Future
    • Ebrahimi-Fakhari D, Wahlster L, McLean PJ: Molecular Chaperones in Parkinson's Disease - Present and Future. J Parkinsons Dis 2011, 1: 299-320.
    • (2011) J Parkinsons Dis , vol.1 , pp. 299-320
    • Ebrahimi-Fakhari, D.1    Wahlster, L.2    McLean, P.J.3
  • 18
    • 84865860748 scopus 로고    scopus 로고
    • Protein degradation pathways in Parkinson's disease: curse or blessing
    • Ebrahimi-Fakhari D, Wahlster L, McLean PJ: Protein degradation pathways in Parkinson's disease: curse or blessing. Acta Neuropathol 2012, 124: 153-172. 10.1007/s00401-012-1004-6
    • (2012) Acta Neuropathol , vol.124 , pp. 153-172
    • Ebrahimi-Fakhari, D.1    Wahlster, L.2    McLean, P.J.3
  • 19
    • 84875415994 scopus 로고    scopus 로고
    • Lang AE: alpha-Synuclein oligomers and clinical implications for Parkinson disease
    • Kalia LV, Kalia SK, McLean PJ, Lozano AM: Lang AE: alpha-Synuclein oligomers and clinical implications for Parkinson disease. Ann Neurol 2013, 73: 155-169. 10.1002/ana.23746
    • (2013) Ann Neurol , vol.73 , pp. 155-169
    • Kalia, L.V.1    Kalia, S.K.2    McLean, P.J.3    Lozano, A.M.4
  • 20
    • 84857254436 scopus 로고    scopus 로고
    • Alpha-synuclein's degradation in vivo: opening a new (cranial) window on the roles of degradation pathways in Parkinson disease
    • Ebrahimi-Fakhari D, McLean PJ, Unni VK: Alpha-synuclein's degradation in vivo: opening a new (cranial) window on the roles of degradation pathways in Parkinson disease. Autophagy 2012, 8: 281-283. 10.4161/auto.8.2.18938
    • (2012) Autophagy , vol.8 , pp. 281-283
    • Ebrahimi-Fakhari, D.1    McLean, P.J.2    Unni, V.K.3
  • 22
    • 78649239916 scopus 로고    scopus 로고
    • Molecular chaperones as rational drug targets for Parkinson's disease therapeutics
    • Kalia SK, Kalia LV, McLean PJ: Molecular chaperones as rational drug targets for Parkinson's disease therapeutics. CNS Neurol Disord Drug Targets 2010, 9: 741-753. 10.2174/187152710793237386
    • (2010) CNS Neurol Disord Drug Targets , vol.9 , pp. 741-753
    • Kalia, S.K.1    Kalia, L.V.2    McLean, P.J.3
  • 23
    • 84882254367 scopus 로고    scopus 로고
    • The role of autophagy in neurodegenerative disease
    • Nixon RA: The role of autophagy in neurodegenerative disease. Nat Med 2013, 19: 983-997. 10.1038/nm.3232
    • (2013) Nat Med , vol.19 , pp. 983-997
    • Nixon, R.A.1
  • 24
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration
    • Chandra S, Gallardo G, Fernandez-Chacon R, Schluter OM, Sudhof TC: Alpha-synuclein cooperates with CSPalpha in preventing neurodegeneration. Cell 2005, 123: 383-396. 10.1016/j.cell.2005.09.028
    • (2005) Cell , vol.123 , pp. 383-396
    • Chandra, S.1    Gallardo, G.2    Fernandez-Chacon, R.3    Schluter, O.M.4    Sudhof, T.C.5
  • 25
    • 77957347060 scopus 로고    scopus 로고
    • Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro
    • Burre J, Sharma M, Tsetsenis T, Buchman V, Etherton MR, Sudhof TC: Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 2010, 329: 1663-1667. 10.1126/science.1195227
    • (2010) Science , vol.329 , pp. 1663-1667
    • Burre, J.1    Sharma, M.2    Tsetsenis, T.3    Buchman, V.4    Etherton, M.R.5    Sudhof, T.C.6
  • 26
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson WS, Jonas A, Clayton DF, George JM: Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 1998, 273: 9443-9449. 10.1074/jbc.273.16.9443
    • (1998) J Biol Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 27
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr: NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 1996, 35: 13709-13715. 10.1021/bi961799n
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, P.T.5
  • 28
    • 80052398365 scopus 로고    scopus 로고
    • alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, DJ S: alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011, 477: 107-110. 10.1038/nature10324
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2
  • 30
    • 84874769548 scopus 로고    scopus 로고
    • In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells
    • Dettmer U, Newman AJ, Luth ES, Bartels T, Selkoe D: In vivo cross-linking reveals principally oligomeric forms of alpha-synuclein and beta-synuclein in neurons and non-neural cells. J Biol Chem 2013, 288: 6371-6385. 10.1074/jbc.M112.403311
    • (2013) J Biol Chem , vol.288 , pp. 6371-6385
    • Dettmer, U.1    Newman, A.J.2    Luth, E.S.3    Bartels, T.4    Selkoe, D.5
  • 32
    • 84859577559 scopus 로고    scopus 로고
    • alpha-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
    • Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, et al.: alpha-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer. J Biol Chem 2012, 287: 15345-15364. 10.1074/jbc.M111.318949
    • (2012) J Biol Chem , vol.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6    Tsika, E.7    Coune, P.8    Prudent, M.9    Lion, N.10
  • 33
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
    • Conway KA, Lee SJ, Rochet JC, Ding TT, Williamson RE, Lansbury PT Jr: Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy. Proc Natl Acad Sci U S A 2000, 97: 571-576. 10.1073/pnas.97.2.571
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 34
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M, Hsu LJ, Xia Y, Takeda A, Sisk A, Sundsmo M, Masliah E: Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. Neuroreport 1999, 10: 717-721. 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
  • 36
  • 37
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • Li W, West N, Colla E, Pletnikova O, Troncoso JC, Marsh L, Dawson TM, Jakala P, Hartmann T, Price DL, Lee MK: Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc Natl Acad Sci U S A 2005, 102: 2162-2167. 10.1073/pnas.0406976102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6    Dawson, T.M.7    Jakala, P.8    Hartmann, T.9    Price, D.L.10    Lee, M.K.11
  • 39
    • 0035834655 scopus 로고    scopus 로고
    • Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins
    • Perrin RJ, Woods WS, Clayton DF, George JM: Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J Biol Chem 2001, 276: 41958-41962. 10.1074/jbc.M105022200
    • (2001) J Biol Chem , vol.276 , pp. 41958-41962
    • Perrin, R.J.1    Woods, W.S.2    Clayton, D.F.3    George, J.M.4
  • 40
    • 0037456578 scopus 로고    scopus 로고
    • The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease
    • Sharon R, Bar-Joseph I, Frosch MP, Walsh DM, Hamilton JA, Selkoe DJ: The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson's disease. Neuron 2003, 37: 583-595. 10.1016/S0896-6273(03)00024-2
    • (2003) Neuron , vol.37 , pp. 583-595
    • Sharon, R.1    Bar-Joseph, I.2    Frosch, M.P.3    Walsh, D.M.4    Hamilton, J.A.5    Selkoe, D.J.6
  • 41
    • 53949108957 scopus 로고    scopus 로고
    • N-terminal region of alpha-synuclein is essential for the fatty acid-induced oligomerization of the molecules
    • Karube H, Sakamoto M, Arawaka S, Hara S, Sato H, Ren CH, Goto S, Koyama S, Wada M, Kawanami T, et al.: N-terminal region of alpha-synuclein is essential for the fatty acid-induced oligomerization of the molecules. FEBS Lett 2008, 582: 3693-3700. 10.1016/j.febslet.2008.10.001
    • (2008) FEBS Lett , vol.582 , pp. 3693-3700
    • Karube, H.1    Sakamoto, M.2    Arawaka, S.3    Hara, S.4    Sato, H.5    Ren, C.H.6    Goto, S.7    Koyama, S.8    Wada, M.9    Kawanami, T.10
  • 42
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou KE, Kragh CL, Mann DM, Salem SA, Al-Shami R, Allsop D, Hassan AH, Jensen PH, El-Agnaf OM: Detection of elevated levels of soluble alpha-synuclein oligomers in post-mortem brain extracts from patients with dementia with Lewy bodies. Brain 2009, 132: 1093-1101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3    Salem, S.A.4    Al-Shami, R.5    Allsop, D.6    Hassan, A.H.7    Jensen, P.H.8    El-Agnaf, O.M.9
  • 46
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer KM, Ruf WP, Putcha P, Joyner D, Hashimoto T, Glabe C, Hyman BT, McLean PJ: Heat-shock protein 70 modulates toxic extracellular alpha-synuclein oligomers and rescues trans-synaptic toxicity. Faseb J 2011, 25: 326-336. 10.1096/fj.10-164624
    • (2011) Faseb J , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6    Hyman, B.T.7    McLean, P.J.8
  • 50
    • 84860501370 scopus 로고    scopus 로고
    • Beyond alpha-synuclein transfer: pathology propagation in Parkinson's disease
    • Hansen C, Li JY: Beyond alpha-synuclein transfer: pathology propagation in Parkinson's disease. Trends Mol Med 2012, 18: 248-255. 10.1016/j.molmed.2012.03.002
    • (2012) Trends Mol Med , vol.18 , pp. 248-255
    • Hansen, C.1    Li, J.Y.2
  • 52
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M: Molecular chaperones in protein folding and proteostasis. Nature 2011, 475: 324-332. 10.1038/nature10317
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 53
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B: Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 2010, 11: 777-788. 10.1038/nrm2993
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 55
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • Finka A, Goloubinoff P: Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress Chaperones 2013, 18: 591-605. 10.1007/s12192-013-0413-3
    • (2013) Cell Stress Chaperones , vol.18 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 56
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl FU, Hayer-Hartl M: Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 2009, 16: 574-581. 10.1038/nsmb.1591
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 57
    • 80054026084 scopus 로고    scopus 로고
    • Distinct Roles In Vivo for the Ubiquitin-Proteasome System and the Autophagy Lysosomal Pathway in the Degradation of (alpha}-Synuclein
    • Ebrahimi-Fakhari D, Cantuti-Castelvetri I, Fan Z, Rockenstein E, Masliah E, Hyman BT, McLean PJ, Unni VK: Distinct Roles In Vivo for the Ubiquitin-Proteasome System and the Autophagy-Lysosomal Pathway in the Degradation of (alpha}-Synuclein. J Neurosci 2011, 31: 14508-14520. 10.1523/JNEUROSCI.1560-11.2011
    • (2011) J Neurosci , vol.31 , pp. 14508-14520
    • Ebrahimi-Fakhari, D.1    Cantuti-Castelvetri, I.2    Fan, Z.3    Rockenstein, E.4    Masliah, E.5    Hyman, B.T.6    McLean, P.J.7    Unni, V.K.8
  • 58
    • 79951681576 scopus 로고    scopus 로고
    • Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells
    • Finka A, Mattoo RU, Goloubinoff P: Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 2011, 16: 15-31. 10.1007/s12192-010-0216-8
    • (2011) Cell Stress Chaperones , vol.16 , pp. 15-31
    • Finka, A.1    Mattoo, R.U.2    Goloubinoff, P.3
  • 59
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter K, Haslbeck M, Buchner J: The heat shock response: life on the verge of death. Mol Cell 2010, 40: 253-266. 10.1016/j.molcel.2010.10.006
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 61
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R: Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 1998, 94: 471-480. 10.1016/S0092-8674(00)81588-3
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 62
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser DD, Theodorakis NG, Morimoto RI: Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells. Mol Cell Biol 1988, 8: 4736-4744.
    • (1988) Mol Cell Biol , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 63
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • Morimoto RI: Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes Dev 1998, 12: 3788-3796. 10.1101/gad.12.24.3788
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 64
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y, Mosser DD, Morimoto RI: Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev 1998, 12: 654-666. 10.1101/gad.12.5.654
    • (1998) Genes Dev , vol.12 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 65
    • 84864318195 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: a unique way to enter the lysosome world
    • Kaushik S, Cuervo AM: Chaperone-mediated autophagy: a unique way to enter the lysosome world. Trends Cell Biol 2012, 22: 407-417. 10.1016/j.tcb.2012.05.006
    • (2012) Trends Cell Biol , vol.22 , pp. 407-417
    • Kaushik, S.1    Cuervo, A.M.2
  • 66
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF: Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990, 15: 305-309. 10.1016/0968-0004(90)90019-8
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 67
    • 0024975155 scopus 로고
    • A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins
    • Chiang HL, Terlecky SR, Plant CP, Dice JF: A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 1989, 246: 382-385. 10.1126/science.2799391
    • (1989) Science , vol.246 , pp. 382-385
    • Chiang, H.L.1    Terlecky, S.R.2    Plant, C.P.3    Dice, J.F.4
  • 68
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes FA, Dice JF: A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001, 114: 2491-2499.
    • (2001) J Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 69
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo AM, Dice JF: A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996, 273: 501-503. 10.1126/science.273.5274.501
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 70
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes FA, Terlecky SR, Dice JF: An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 1997, 137: 825-834. 10.1083/jcb.137.4.825
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 71
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM: The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008, 28: 5747-5763. 10.1128/MCB.02070-07
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 72
    • 0031041902 scopus 로고    scopus 로고
    • A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
    • Cuervo AM, Dice JF, Knecht E: A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins. J Biol Chem 1997, 272: 5606-5615. 10.1074/jbc.272.9.5606
    • (1997) J Biol Chem , vol.272 , pp. 5606-5615
    • Cuervo, A.M.1    Dice, J.F.2    Knecht, E.3
  • 73
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • Cuervo AM, Dice JF: Age-related decline in chaperone-mediated autophagy. J Biol Chem 2000, 275: 31505-31513.
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 75
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, Mancini MA, Antalffy B, DeFranco DB, Orr HT, Zoghbi HY: Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 1998, 19: 148-154. 10.1038/502
    • (1998) Nat Genet , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 76
    • 0034629073 scopus 로고    scopus 로고
    • Genetic suppression of polyglutamine toxicity in Drosophila
    • Kazemi-Esfarjani P, Benzer S: Genetic suppression of polyglutamine toxicity in Drosophila. Science 2000, 287: 1837-1840. 10.1126/science.287.5459.1837
    • (2000) Science , vol.287 , pp. 1837-1840
    • Kazemi-Esfarjani, P.1    Benzer, S.2
  • 77
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • Chai Y, Koppenhafer SL, Bonini NM, Paulson HL: Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 1999, 19: 10338-10347.
    • (1999) J Neurosci , vol.19 , pp. 10338-10347
    • Chai, Y.1    Koppenhafer, S.L.2    Bonini, N.M.3    Paulson, H.L.4
  • 78
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • Warrick JM, Chan HY, Gray-Board GL, Chai Y, Paulson HL, Bonini NM: Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 1999, 23: 425-428. 10.1038/70532
    • (1999) Nat Genet , vol.23 , pp. 425-428
    • Warrick, J.M.1    Chan, H.Y.2    Gray-Board, G.L.3    Chai, Y.4    Paulson, H.L.5    Bonini, N.M.6
  • 79
    • 0036846119 scopus 로고    scopus 로고
    • TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation
    • McLean PJ, Kawamata H, Shariff S, Hewett J, Sharma N, Ueda K, Breakefield XO, Hyman BT: TorsinA and heat shock proteins act as molecular chaperones: suppression of alpha-synuclein aggregation. J Neurochem 2002, 83: 846-854. 10.1046/j.1471-4159.2002.01190.x
    • (2002) J Neurochem , vol.83 , pp. 846-854
    • McLean, P.J.1    Kawamata, H.2    Shariff, S.3    Hewett, J.4    Sharma, N.5    Ueda, K.6    Breakefield, X.O.7    Hyman, B.T.8
  • 81
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck PK, Chan HY, Trojanowski JQ, Lee VM, Bonini NM: Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 2002, 295: 865-868. 10.1126/science.1067389
    • (2002) Science , vol.295 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 84
    • 0037237358 scopus 로고    scopus 로고
    • The mouse MPTP model: gene expression changes in dopaminergic neurons
    • Kuhn K, Wellen J, Link N, Maskri L, Lubbert H, Stichel CC: The mouse MPTP model: gene expression changes in dopaminergic neurons. Eur J Neurosci 2003, 17: 1-12. 10.1046/j.1460-9568.2003.02408.x
    • (2003) Eur J Neurosci , vol.17 , pp. 1-12
    • Kuhn, K.1    Wellen, J.2    Link, N.3    Maskri, L.4    Lubbert, H.5    Stichel, C.C.6
  • 86
    • 84855929223 scopus 로고    scopus 로고
    • SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones
    • Donmez G, Arun A, Chung CY, McLean PJ, Lindquist S, Guarente L: SIRT1 protects against alpha-synuclein aggregation by activating molecular chaperones. J Neurosci 2012, 32: 124-132. 10.1523/JNEUROSCI.3442-11.2012
    • (2012) J Neurosci , vol.32 , pp. 124-132
    • Donmez, G.1    Arun, A.2    Chung, C.Y.3    McLean, P.J.4    Lindquist, S.5    Guarente, L.6
  • 87
    • 33646555755 scopus 로고    scopus 로고
    • Heat shock proteins reduce alpha-synuclein aggregation induced by MPP+in SK-N-SH cells
    • Fan GH, Zhou HY, Yang H, Chen SD: Heat shock proteins reduce alpha-synuclein aggregation induced by MPP+in SK-N-SH cells. FEBS Lett 2006, 580: 3091-3098. 10.1016/j.febslet.2006.04.057
    • (2006) FEBS Lett , vol.580 , pp. 3091-3098
    • Fan, G.H.1    Zhou, H.Y.2    Yang, H.3    Chen, S.D.4
  • 89
    • 1642356755 scopus 로고    scopus 로고
    • Payne Smith MD, Latchman DS: HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells
    • Zourlidou A: Payne Smith MD, Latchman DS: HSP27 but not HSP70 has a potent protective effect against alpha-synuclein-induced cell death in mammalian neuronal cells. J Neurochem 2004, 88: 1439-1448. 10.1046/j.1471-4159.2003.02273.x
    • (2004) J Neurochem , vol.88 , pp. 1439-1448
    • Zourlidou, A.1
  • 90
    • 7444256611 scopus 로고    scopus 로고
    • A single amino acid substitution differentiates Hsp70-dependent effects on alpha-synuclein degradation and toxicity
    • Klucken J, Shin Y, Hyman BT, McLean PJ: A single amino acid substitution differentiates Hsp70-dependent effects on alpha-synuclein degradation and toxicity. Biochem Biophys Res Commun 2004, 325: 367-373. 10.1016/j.bbrc.2004.10.037
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 367-373
    • Klucken, J.1    Shin, Y.2    Hyman, B.T.3    McLean, P.J.4
  • 91
    • 2942620074 scopus 로고    scopus 로고
    • Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity
    • Klucken J, Shin Y, Masliah E, Hyman BT, McLean PJ: Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity. J Biol Chem 2004, 279: 25497-25502. 10.1074/jbc.M400255200
    • (2004) J Biol Chem , vol.279 , pp. 25497-25502
    • Klucken, J.1    Shin, Y.2    Masliah, E.3    Hyman, B.T.4    McLean, P.J.5
  • 92
    • 77956297983 scopus 로고    scopus 로고
    • The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy
    • Shimshek DR, Mueller M, Wiessner C, Schweizer T, van der Putten PH: The HSP70 molecular chaperone is not beneficial in a mouse model of alpha-synucleinopathy. PLoS One 2010, 5: e10014. 10.1371/journal.pone.0010014
    • (2010) PLoS One , vol.5
    • Shimshek, D.R.1    Mueller, M.2    Wiessner, C.3    Schweizer, T.4    van der Putten, P.H.5
  • 93
    • 17644392138 scopus 로고    scopus 로고
    • Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans
    • Cao S, Gelwix CC, Caldwell KA, Caldwell GA: Torsin-mediated protection from cellular stress in the dopaminergic neurons of Caenorhabditis elegans. J Neurosci 2005, 25: 3801-3812. 10.1523/JNEUROSCI.5157-04.2005
    • (2005) J Neurosci , vol.25 , pp. 3801-3812
    • Cao, S.1    Gelwix, C.C.2    Caldwell, K.A.3    Caldwell, G.A.4
  • 94
    • 84869756871 scopus 로고    scopus 로고
    • Evaluation of TorsinA as a target for Parkinson disease therapy in mouse models
    • Li X, Lee J, Parsons D, Janaurajs K, Standaert DG: Evaluation of TorsinA as a target for Parkinson disease therapy in mouse models. PLoS One 2012, 7: e50063. 10.1371/journal.pone.0050063
    • (2012) PLoS One , vol.7
    • Li, X.1    Lee, J.2    Parsons, D.3    Janaurajs, K.4    Standaert, D.G.5
  • 95
    • 56749117866 scopus 로고    scopus 로고
    • Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly
    • Luk KC, Mills IP, Trojanowski JQ, Lee VM: Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly. Biochemistry 2008, 47: 12614-12625. 10.1021/bi801475r
    • (2008) Biochemistry , vol.47 , pp. 12614-12625
    • Luk, K.C.1    Mills, I.P.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 96
    • 33750873994 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates
    • Huang C, Cheng H, Hao S, Zhou H, Zhang X, Gao J, Sun QH, Hu H, Wang CC: Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates. J Mol Biol 2006, 364: 323-336. 10.1016/j.jmb.2006.08.062
    • (2006) J Mol Biol , vol.364 , pp. 323-336
    • Huang, C.1    Cheng, H.2    Hao, S.3    Zhou, H.4    Zhang, X.5    Gao, J.6    Sun, Q.H.7    Hu, H.8    Wang, C.C.9
  • 97
    • 84866556269 scopus 로고    scopus 로고
    • Identification of Protein Interfaces between alpha-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p
    • Redeker V, Pemberton S, Bienvenut W, Bousset L, Melki R: Identification of Protein Interfaces between alpha-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p. J Biol Chem 2012, 287: 32630-32639. 10.1074/jbc.M112.387530
    • (2012) J Biol Chem , vol.287 , pp. 32630-32639
    • Redeker, V.1    Pemberton, S.2    Bienvenut, W.3    Bousset, L.4    Melki, R.5
  • 98
    • 33750117120 scopus 로고    scopus 로고
    • Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging
    • Klucken J, Outeiro TF, Nguyen P, McLean PJ, Hyman BT: Detection of novel intracellular alpha-synuclein oligomeric species by fluorescence lifetime imaging. FASEB J 2006, 20: 2050-2057. 10.1096/fj.05-5422com
    • (2006) FASEB J , vol.20 , pp. 2050-2057
    • Klucken, J.1    Outeiro, T.F.2    Nguyen, P.3    McLean, P.J.4    Hyman, B.T.5
  • 100
    • 84863683967 scopus 로고    scopus 로고
    • Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
    • Duennwald ML, Echeverria A, Shorter J: Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 2012, 10: e1001346. 10.1371/journal.pbio.1001346
    • (2012) PLoS Biol , vol.10
    • Duennwald, M.L.1    Echeverria, A.2    Shorter, J.3
  • 101
    • 71449111785 scopus 로고    scopus 로고
    • The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein
    • Falsone SF, Kungl AJ, Rek A, Cappai R, Zangger K: The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein. J Biol Chem 2009, 284: 31190-31199. 10.1074/jbc.M109.057240
    • (2009) J Biol Chem , vol.284 , pp. 31190-31199
    • Falsone, S.F.1    Kungl, A.J.2    Rek, A.3    Cappai, R.4    Zangger, K.5
  • 102
    • 84886728386 scopus 로고    scopus 로고
    • Hsp90 Inhibits alpha-Synuclein Aggregation by Interacting with Soluble Oligomers
    • Daturpalli S, Waudby CA, Meehan S, Jackson SE: Hsp90 Inhibits alpha-Synuclein Aggregation by Interacting with Soluble Oligomers. J Mol Biol 2013, 22: 4614-4628.
    • (2013) J Mol Biol , vol.22 , pp. 4614-4628
    • Daturpalli, S.1    Waudby, C.A.2    Meehan, S.3    Jackson, S.E.4
  • 103
    • 79960046164 scopus 로고    scopus 로고
    • Cellular stress response pathways and ageing: intricate molecular relationships
    • Kourtis N, Tavernarakis N: Cellular stress response pathways and ageing: intricate molecular relationships. Embo J 2011, 30: 2520-2531. 10.1038/emboj.2011.162
    • (2011) Embo J , vol.30 , pp. 2520-2531
    • Kourtis, N.1    Tavernarakis, N.2
  • 104
    • 0026539546 scopus 로고
    • Accumulation of alpha B-crystallin in central nervous system glia and neurons in pathologic conditions
    • Iwaki T, Wisniewski T, Iwaki A, Corbin E, Tomokane N, Tateishi J, Goldman JE: Accumulation of alpha B-crystallin in central nervous system glia and neurons in pathologic conditions. Am J Pathol 1992, 140: 345-356.
    • (1992) Am J Pathol , vol.140 , pp. 345-356
    • Iwaki, T.1    Wisniewski, T.2    Iwaki, A.3    Corbin, E.4    Tomokane, N.5    Tateishi, J.6    Goldman, J.E.7
  • 111
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions
    • Chu Y, Dodiya H, Aebischer P, Olanow CW, Kordower JH: Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol Dis 2009, 35: 385-398. 10.1016/j.nbd.2009.05.023
    • (2009) Neurobiol Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 116
    • 78649640867 scopus 로고    scopus 로고
    • Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones
    • Hinault MP, Cuendet AF, Mattoo RU, Mensi M, Dietler G, Lashuel HA, Goloubinoff P: Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. J Biol Chem 2010, 285: 38173-38182. 10.1074/jbc.M110.127753
    • (2010) J Biol Chem , vol.285 , pp. 38173-38182
    • Hinault, M.P.1    Cuendet, A.F.2    Mattoo, R.U.3    Mensi, M.4    Dietler, G.5    Lashuel, H.A.6    Goloubinoff, P.7
  • 117
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D: Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305: 1292-1295. 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
  • 118
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L: Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 2008, 283: 23542-23556. 10.1074/jbc.M801992200
    • (2008) J Biol Chem , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 119
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L: Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS One 2009, 4: e5515. 10.1371/journal.pone.0005515
    • (2009) PLoS One , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 121
    • 58149215720 scopus 로고    scopus 로고
    • Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy
    • Yang Q, She H, Gearing M, Colla E, Lee M, Shacka JJ, Mao Z: Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 2009, 323: 124-127. 10.1126/science.1166088
    • (2009) Science , vol.323 , pp. 124-127
    • Yang, Q.1    She, H.2    Gearing, M.3    Colla, E.4    Lee, M.5    Shacka, J.J.6    Mao, Z.7
  • 122
    • 0031763264 scopus 로고    scopus 로고
    • The synuclein family
    • Lavedan C: The synuclein family. Genome Res 1998, 8: 871-880.
    • (1998) Genome Res , vol.8 , pp. 871-880
    • Lavedan, C.1
  • 124
    • 84875876495 scopus 로고    scopus 로고
    • Influence of microRNA deregulation on chaperone-mediated autophagy and alpha-synuclein pathology in Parkinson's disease
    • Alvarez-Erviti L, Seow Y, Schapira AH, Rodriguez-Oroz MC, Obeso JA, Cooper JM: Influence of microRNA deregulation on chaperone-mediated autophagy and alpha-synuclein pathology in Parkinson's disease. Cell Death Dis 2013, 4: e545. 10.1038/cddis.2013.73
    • (2013) Cell Death Dis , vol.4
    • Alvarez-Erviti, L.1    Seow, Y.2    Schapira, A.H.3    Rodriguez-Oroz, M.C.4    Obeso, J.A.5    Cooper, J.M.6
  • 125
    • 84860833596 scopus 로고    scopus 로고
    • Regional deficiencies in chaperone-mediated autophagy underlie alpha-synuclein aggregation and neurodegeneration
    • Malkus KA, Ischiropoulos H: Regional deficiencies in chaperone-mediated autophagy underlie alpha-synuclein aggregation and neurodegeneration. Neurobiol Dis 2012, 46: 732-744. 10.1016/j.nbd.2012.03.017
    • (2012) Neurobiol Dis , vol.46 , pp. 732-744
    • Malkus, K.A.1    Ischiropoulos, H.2
  • 128
    • 67649460932 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in neuronal injury
    • Galluzzi L, Blomgren K, Kroemer G: Mitochondrial membrane permeabilization in neuronal injury. Nat Rev Neurosci 2009, 10: 481-494. 10.1038/nrn2665
    • (2009) Nat Rev Neurosci , vol.10 , pp. 481-494
    • Galluzzi, L.1    Blomgren, K.2    Kroemer, G.3
  • 129
  • 130
    • 77955965172 scopus 로고    scopus 로고
    • Cellular stress responses: cell survival and cell death
    • Fulda S, Gorman AM, Hori O, Samali A: Cellular stress responses: cell survival and cell death. Int J Cell Biol 2010, 2010: 214074.
    • (2010) Int J Cell Biol , vol.2010 , pp. 214074
    • Fulda, S.1    Gorman, A.M.2    Hori, O.3    Samali, A.4
  • 131
    • 79951587313 scopus 로고    scopus 로고
    • Heat shock proteins: multiple neuroprotective functions and implications for neurologic disease
    • Benarroch EE: Heat shock proteins: multiple neuroprotective functions and implications for neurologic disease. Neurology 2011, 76: 660-667. 10.1212/WNL.0b013e31820c3119
    • (2011) Neurology , vol.76 , pp. 660-667
    • Benarroch, E.E.1
  • 132
    • 33244474580 scopus 로고    scopus 로고
    • Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation
    • Stankiewicz AR, Lachapelle G, Foo CP, Radicioni SM, Mosser DD: Hsp70 inhibits heat-induced apoptosis upstream of mitochondria by preventing Bax translocation. J Biol Chem 2005, 280: 38729-38739. 10.1074/jbc.M509497200
    • (2005) J Biol Chem , vol.280 , pp. 38729-38739
    • Stankiewicz, A.R.1    Lachapelle, G.2    Foo, C.P.3    Radicioni, S.M.4    Mosser, D.D.5
  • 133
    • 1842843854 scopus 로고    scopus 로고
    • Mori M: hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria
    • Gotoh T, Terada K, Oyadomari S: Mori M: hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 2004, 11: 390-402. 10.1038/sj.cdd.4401369
    • (2004) Cell Death Differ , vol.11 , pp. 390-402
    • Gotoh, T.1    Terada, K.2    Oyadomari, S.3
  • 136
    • 84867581392 scopus 로고    scopus 로고
    • Over-expression of HSP70 attenuates caspase-dependent and caspase-independent pathways and inhibits neuronal apoptosis
    • Sabirzhanov B, Stoica BA, Hanscom M, Piao CS, Faden AI: Over-expression of HSP70 attenuates caspase-dependent and caspase-independent pathways and inhibits neuronal apoptosis. J Neurochem 2012, 123: 542-554. 10.1111/j.1471-4159.2012.07927.x
    • (2012) J Neurochem , vol.123 , pp. 542-554
    • Sabirzhanov, B.1    Stoica, B.A.2    Hanscom, M.3    Piao, C.S.4    Faden, A.I.5
  • 143
    • 70149124059 scopus 로고    scopus 로고
    • Induction of heat shock protein 70 reduces the alteration of striatal electrical activity caused by mitochondrial impairment
    • Tantucci M, Mariucci G, Taha E, Spaccatini C, Tozzi A, Luchetti E, Calabresi P, Ambrosini MV: Induction of heat shock protein 70 reduces the alteration of striatal electrical activity caused by mitochondrial impairment. Neuroscience 2009, 163: 735-740. 10.1016/j.neuroscience.2009.06.070
    • (2009) Neuroscience , vol.163 , pp. 735-740
    • Tantucci, M.1    Mariucci, G.2    Taha, E.3    Spaccatini, C.4    Tozzi, A.5    Luchetti, E.6    Calabresi, P.7    Ambrosini, M.V.8
  • 144
    • 0345283071 scopus 로고    scopus 로고
    • Heat shock protects PC12 cells against MPP+toxicity
    • Quigney DJ, Gorman AM, Samali A: Heat shock protects PC12 cells against MPP+toxicity. Brain Res 2003, 993: 133-139. 10.1016/j.brainres.2003.09.004
    • (2003) Brain Res , vol.993 , pp. 133-139
    • Quigney, D.J.1    Gorman, A.M.2    Samali, A.3
  • 145
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
    • Bush KT, Goldberg AL, Nigam SK: Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem 1997, 272: 9086-9092. 10.1074/jbc.272.14.9086
    • (1997) J Biol Chem , vol.272 , pp. 9086-9092
    • Bush, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 146
    • 10944241135 scopus 로고    scopus 로고
    • Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease
    • Dong Z, Wolfer DP, Lipp HP, Bueler H: Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease. Mol Ther 2005, 11: 80-88.
    • (2005) Mol Ther , vol.11 , pp. 80-88
    • Dong, Z.1    Wolfer, D.P.2    Lipp, H.P.3    Bueler, H.4
  • 147
    • 42249103388 scopus 로고    scopus 로고
    • Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease
    • Nagel F, Falkenburger BH, Tonges L, Kowsky S, Poppelmeyer C, Schulz JB, Bahr M, Dietz GP: Tat-Hsp70 protects dopaminergic neurons in midbrain cultures and in the substantia nigra in models of Parkinson's disease. J Neurochem 2008, 105: 853-864. 10.1111/j.1471-4159.2007.05204.x
    • (2008) J Neurochem , vol.105 , pp. 853-864
    • Nagel, F.1    Falkenburger, B.H.2    Tonges, L.3    Kowsky, S.4    Poppelmeyer, C.5    Schulz, J.B.6    Bahr, M.7    Dietz, G.P.8
  • 148
    • 11844274735 scopus 로고    scopus 로고
    • Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells
    • Gorman AM, Szegezdi E, Quigney DJ, Samali A: Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells. Biochem Biophys Res Commun 2005, 327: 801-810. 10.1016/j.bbrc.2004.12.066
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 801-810
    • Gorman, A.M.1    Szegezdi, E.2    Quigney, D.J.3    Samali, A.4
  • 149
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P, Ron D: The unfolded protein response: from stress pathway to homeostatic regulation. Science 2011, 334: 1081-1086. 10.1126/science.1209038
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 150
    • 84863740827 scopus 로고    scopus 로고
    • The impact of the unfolded protein response on human disease
    • Wang S, Kaufman RJ: The impact of the unfolded protein response on human disease. J Cell Biol 2012, 197: 857-867. 10.1083/jcb.201110131
    • (2012) J Cell Biol , vol.197 , pp. 857-867
    • Wang, S.1    Kaufman, R.J.2
  • 151
    • 84870159094 scopus 로고    scopus 로고
    • Structural basis of the unfolded protein response
    • Korennykh A, Walter P: Structural basis of the unfolded protein response. Annu Rev Cell Dev Biol 2012, 28: 251-277. 10.1146/annurev-cellbio-101011-155826
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 251-277
    • Korennykh, A.1    Walter, P.2
  • 152
    • 84859799949 scopus 로고    scopus 로고
    • Stress management at the ER: regulators of ER stress-induced apoptosis
    • Gorman AM, Healy SJ, Jager R, Samali A: Stress management at the ER: regulators of ER stress-induced apoptosis. Pharmacol Ther 2012, 134: 306-316. 10.1016/j.pharmthera.2012.02.003
    • (2012) Pharmacol Ther , vol.134 , pp. 306-316
    • Gorman, A.M.1    Healy, S.J.2    Jager, R.3    Samali, A.4
  • 154
    • 84860219621 scopus 로고    scopus 로고
    • Activation of the unfolded protein response is an early event in Alzheimer's and Parkinson's disease
    • Hoozemans JJ, van Haastert ES, Nijholt DA, Rozemuller AJ, Scheper W: Activation of the unfolded protein response is an early event in Alzheimer's and Parkinson's disease. Neurodegener Dis 2012, 10: 212-215. 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
  • 155
    • 77956700757 scopus 로고    scopus 로고
    • Involvement of endoplasmic reticulum stress defined by activated unfolded protein response in multiple system atrophy
    • Makioka K, Yamazaki T, Fujita Y, Takatama M, Nakazato Y, Okamoto K: Involvement of endoplasmic reticulum stress defined by activated unfolded protein response in multiple system atrophy. J Neurol Sci 2010, 297: 60-65. 10.1016/j.jns.2010.06.019
    • (2010) J Neurol Sci , vol.297 , pp. 60-65
    • Makioka, K.1    Yamazaki, T.2    Fujita, Y.3    Takatama, M.4    Nakazato, Y.5    Okamoto, K.6
  • 156
    • 29644434199 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity
    • Smith WW, Jiang H, Pei Z, Tanaka Y, Morita H, Sawa A, Dawson VL, Dawson TM, Ross CA: Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity. Hum Mol Genet 2005, 14: 3801-3811. 10.1093/hmg/ddi396
    • (2005) Hum Mol Genet , vol.14 , pp. 3801-3811
    • Smith, W.W.1    Jiang, H.2    Pei, Z.3    Tanaka, Y.4    Morita, H.5    Sawa, A.6    Dawson, V.L.7    Dawson, T.M.8    Ross, C.A.9
  • 158
    • 53149133169 scopus 로고    scopus 로고
    • Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediated cell death
    • Sugeno N, Takeda A, Hasegawa T, Kobayashi M, Kikuchi A, Mori F, Wakabayashi K, Itoyama Y: Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediated cell death. J Biol Chem 2008, 283: 23179-23188. 10.1074/jbc.M802223200
    • (2008) J Biol Chem , vol.283 , pp. 23179-23188
    • Sugeno, N.1    Takeda, A.2    Hasegawa, T.3    Kobayashi, M.4    Kikuchi, A.5    Mori, F.6    Wakabayashi, K.7    Itoyama, Y.8
  • 160
    • 84863230467 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is important for the manifestations of alpha-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 alpha-synucleinopathy in vivo. J Neurosci 2012, 32: 3306-3320. 10.1523/JNEUROSCI.5367-11.2012
    • (2012) J Neurosci , 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
  • 162
    • 84863229691 scopus 로고    scopus 로고
    • Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo
    • Colla E, Jensen PH, Pletnikova O, Troncoso JC, Glabe C, Lee MK: Accumulation of toxic alpha-synuclein oligomer within endoplasmic reticulum occurs in alpha-synucleinopathy in vivo. J Neurosci 2012, 32: 3301-3305. 10.1523/JNEUROSCI.5368-11.2012
    • (2012) J 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
  • 164
    • 84880673845 scopus 로고    scopus 로고
    • Pharmacological approaches to restore mitochondrial function
    • Andreux PA, Houtkooper RH, Auwerx J: Pharmacological approaches to restore mitochondrial function. Nat Rev Drug Discov 2013, 12: 465-483. 10.1038/nrd4023
    • (2013) Nat Rev Drug Discov , vol.12 , pp. 465-483
    • Andreux, P.A.1    Houtkooper, R.H.2    Auwerx, J.3
  • 166
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: tipping the balance in protein folding diseases
    • Voisine C, Pedersen JS, Morimoto RI: Chaperone networks: tipping the balance in protein folding diseases. Neurobiol Dis 2010, 40: 12-20. 10.1016/j.nbd.2010.05.007
    • (2010) Neurobiol Dis , vol.40 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 167
    • 0036852712 scopus 로고    scopus 로고
    • Pharmacological prevention of Parkinson disease in Drosophila
    • Auluck PK, Bonini NM: Pharmacological prevention of Parkinson disease in Drosophila. Nat Med 2002, 8: 1185-1186. 10.1038/nm1102-1185
    • (2002) Nat Med , vol.8 , pp. 1185-1186
    • Auluck, P.K.1    Bonini, N.M.2
  • 168
    • 4344569643 scopus 로고    scopus 로고
    • Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro
    • McLean PJ, Klucken J, Shin Y, Hyman BT: Geldanamycin induces Hsp70 and prevents alpha-synuclein aggregation and toxicity in vitro. Biochem Biophys Res Commun 2004, 321: 665-669. 10.1016/j.bbrc.2004.07.021
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 665-669
    • McLean, P.J.1    Klucken, J.2    Shin, Y.3    Hyman, B.T.4
  • 169
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of Suppression of (alpha}-Synuclein Neurotoxicity by Geldanamycin in Drosophila
    • Auluck PK, Meulener MC, Bonini NM: Mechanisms of Suppression of (alpha}-Synuclein Neurotoxicity by Geldanamycin in Drosophila. J Biol Chem 2005, 280: 2873-2878.
    • (2005) J Biol Chem , vol.280 , pp. 2873-2878
    • Auluck, P.K.1    Meulener, M.C.2    Bonini, N.M.3
  • 170
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • Flower TR, Chesnokova LS, Froelich CA, Dixon C, Witt SN: Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J Mol Biol 2005, 351: 1081-1100. 10.1016/j.jmb.2005.06.060
    • (2005) J Mol Biol , vol.351 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3    Dixon, C.4    Witt, S.N.5
  • 171
    • 59649097036 scopus 로고    scopus 로고
    • Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein
    • Liu J, Zhang JP, Shi M, Quinn T, Bradner J, Beyer R, Chen S, Zhang J: Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein. J Neurosci 2009, 29: 1480-1485. 10.1523/JNEUROSCI.6202-08.2009
    • (2009) J Neurosci , vol.29 , pp. 1480-1485
    • Liu, J.1    Zhang, J.P.2    Shi, M.3    Quinn, T.4    Bradner, J.5    Beyer, R.6    Chen, S.7    Zhang, J.8
  • 172
    • 77951976610 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou E, Stefanis L, Vekrellis K: Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome. Neurobiol Aging 2010, 31: 953-968. 10.1016/j.neurobiolaging.2008.07.008
    • (2010) Neurobiol Aging , vol.31 , pp. 953-968
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 173
    • 77649305375 scopus 로고    scopus 로고
    • 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy
    • Riedel M, Goldbaum O, Schwarz L, Schmitt S, Richter-Landsberg C: 17-AAG induces cytoplasmic alpha-synuclein aggregate clearance by induction of autophagy. PLoS One 2010, 5: e8753. 10.1371/journal.pone.0008753
    • (2010) PLoS One , vol.5
    • Riedel, M.1    Goldbaum, O.2    Schwarz, L.3    Schmitt, S.4    Richter-Landsberg, C.5
  • 175
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC: Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 2007, 282: 5641-5652.
    • (2007) J Biol Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 176
    • 84861899099 scopus 로고    scopus 로고
    • Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils
    • Yu WB, Jiang T, Lan DM, Lu JH, Yue ZY, Wang J, Zhou P: Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils. Arch Biochem Biophys 2012, 523: 144-150. 10.1016/j.abb.2012.04.021
    • (2012) Arch Biochem Biophys , vol.523 , pp. 144-150
    • Yu, W.B.1    Jiang, T.2    Lan, D.M.3    Lu, J.H.4    Yue, Z.Y.5    Wang, J.6    Zhou, P.7
  • 177
    • 84879052027 scopus 로고    scopus 로고
    • A blood-brain barrier (BBB) disrupter is also a potent alpha-synuclein (alpha-syn) aggregation inhibitor: a novel dual mechanism of mannitol for the treatment of Parkinson disease (PD)
    • Shaltiel-Karyo R, Frenkel-Pinter M, Rockenstein E, Patrick C, Levy-Sakin M, Schiller A, Egoz-Matia N, Masliah E, Segal D, Gazit E: A blood-brain barrier (BBB) disrupter is also a potent alpha-synuclein (alpha-syn) aggregation inhibitor: a novel dual mechanism of mannitol for the treatment of Parkinson disease (PD). J Biol Chem 2013, 288: 17579-17588. 10.1074/jbc.M112.434787
    • (2013) J Biol Chem , vol.288 , pp. 17579-17588
    • Shaltiel-Karyo, R.1    Frenkel-Pinter, M.2    Rockenstein, E.3    Patrick, C.4    Levy-Sakin, M.5    Schiller, A.6    Egoz-Matia, N.7    Masliah, E.8    Segal, D.9    Gazit, E.10
  • 178
    • 84877839143 scopus 로고
    • Inhibition of formation of alpha-synuclein inclusions by mannosylglycerate in a yeast model of Parkinson's disease
    • Faria C, Jorge CD, Borges N, Tenreiro S, Outeiro TF, Santos H: Inhibition of formation of alpha-synuclein inclusions by mannosylglycerate in a yeast model of Parkinson's disease. Biochim Biophys Acta 1830, 2013: 4065-4072.
    • (1830) Biochim Biophys Acta , vol.2013 , pp. 4065-4072
    • Faria, C.1    Jorge, C.D.2    Borges, N.3    Tenreiro, S.4    Outeiro, T.F.5    Santos, H.6
  • 180
    • 77952551024 scopus 로고    scopus 로고
    • Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy
    • Porter JR, Fritz CC, Depew KM: Discovery and development of Hsp90 inhibitors: a promising pathway for cancer therapy. Curr Opin Chem Biol 2010, 14: 412-420. 10.1016/j.cbpa.2010.03.019
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 412-420
    • Porter, J.R.1    Fritz, C.C.2    Depew, K.M.3
  • 181
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • Shen HY, He JC, Wang Y, Huang QY, Chen JF: Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice. J Biol Chem 2005, 280: 39962-39969. 10.1074/jbc.M505524200
    • (2005) J Biol Chem , vol.280 , pp. 39962-39969
    • Shen, H.Y.1    He, J.C.2    Wang, Y.3    Huang, Q.Y.4    Chen, J.F.5
  • 182
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM: The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998, 42: 273-279. 10.1007/s002800050817
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 184
    • 23844529468 scopus 로고    scopus 로고
    • Celastrol protects against MPTP- and 3-nitropropionic acid-induced neurotoxicity
    • Cleren C, Calingasan NY, Chen J, Beal MF: Celastrol protects against MPTP- and 3-nitropropionic acid-induced neurotoxicity. J Neurochem 2005, 94: 995-1004. 10.1111/j.1471-4159.2005.03253.x
    • (2005) J Neurochem , vol.94 , pp. 995-1004
    • Cleren, C.1    Calingasan, N.Y.2    Chen, J.3    Beal, M.F.4
  • 185
    • 79952104480 scopus 로고    scopus 로고
    • The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells
    • Casarejos MJ, Solano RM, Gomez A, Perucho J, de Yebenes JG, Mena MA: The accumulation of neurotoxic proteins, induced by proteasome inhibition, is reverted by trehalose, an enhancer of autophagy, in human neuroblastoma cells. Neurochem Int 2011, 58: 512-520. 10.1016/j.neuint.2011.01.008
    • (2011) Neurochem Int , vol.58 , pp. 512-520
    • Casarejos, M.J.1    Solano, R.M.2    Gomez, A.3    Perucho, J.4    de Yebenes, J.G.5    Mena, M.A.6
  • 186
    • 34249814605 scopus 로고    scopus 로고
    • Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone
    • Inden M, Kitamura Y, Takeuchi H, Yanagida T, Takata K, Kobayashi Y, Taniguchi T, Yoshimoto K, Kaneko M, Okuma Y, et al.: Neurodegeneration of mouse nigrostriatal dopaminergic system induced by repeated oral administration of rotenone is prevented by 4-phenylbutyrate, a chemical chaperone. J Neurochem 2007, 101: 1491-1504. 10.1111/j.1471-4159.2006.04440.x
    • (2007) J Neurochem , vol.101 , pp. 1491-1504
    • Inden, M.1    Kitamura, Y.2    Takeuchi, H.3    Yanagida, T.4    Takata, K.5    Kobayashi, Y.6    Taniguchi, T.7    Yoshimoto, K.8    Kaneko, M.9    Okuma, Y.10
  • 187
    • 84874901074 scopus 로고    scopus 로고
    • Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: implications for therapy
    • Malik B, Nirmalananthan N, Gray AL, La Spada AR, Hanna MG, Greensmith L: Co-induction of the heat shock response ameliorates disease progression in a mouse model of human spinal and bulbar muscular atrophy: implications for therapy. Brain 2013, 136: 926-943. 10.1093/brain/aws343
    • (2013) Brain , vol.136 , pp. 926-943
    • Malik, B.1    Nirmalananthan, N.2    Gray, A.L.3    La Spada, A.R.4    Hanna, M.G.5    Greensmith, L.6
  • 189
    • 72249101104 scopus 로고    scopus 로고
    • Arimoclomol: a potential therapy under development for ALS
    • Lanka V, Wieland S, Barber J, Cudkowicz M: Arimoclomol: a potential therapy under development for ALS. Expert Opin Investig Drugs 2009, 18: 1907-1918. 10.1517/13543780903357486
    • (2009) Expert Opin Investig Drugs , vol.18 , pp. 1907-1918
    • Lanka, V.1    Wieland, S.2    Barber, J.3    Cudkowicz, M.4
  • 190
    • 70349574602 scopus 로고    scopus 로고
    • Neuroprotective effects of compounds with antioxidant and anti-inflammatory properties in a Drosophila model of Parkinson's disease
    • Faust K, Gehrke S, Yang Y, Yang L, Beal MF, Lu B: Neuroprotective effects of compounds with antioxidant and anti-inflammatory properties in a Drosophila model of Parkinson's disease. BMC Neurosci 2009, 10: 109. 10.1186/1471-2202-10-109
    • (2009) BMC Neurosci , vol.10 , pp. 109
    • Faust, K.1    Gehrke, S.2    Yang, Y.3    Yang, L.4    Beal, M.F.5    Lu, B.6
  • 191
    • 75749136948 scopus 로고    scopus 로고
    • Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease
    • Neef DW, Turski ML, Thiele DJ: Modulation of heat shock transcription factor 1 as a therapeutic target for small molecule intervention in neurodegenerative disease. PLoS Biol 2010, 8: e1000291. 10.1371/journal.pbio.1000291
    • (2010) PLoS Biol , vol.8
    • Neef, D.W.1    Turski, M.L.2    Thiele, D.J.3
  • 192
    • 84874832163 scopus 로고    scopus 로고
    • Protein homeostasis as a therapeutic target for diseases of protein conformation
    • Calamini B, Morimoto RI: Protein homeostasis as a therapeutic target for diseases of protein conformation. Curr Top Med Chem 2012, 12: 2623-2640.
    • (2012) Curr Top Med Chem , vol.12 , pp. 2623-2640
    • Calamini, B.1    Morimoto, R.I.2
  • 196
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer V, Lavenir I, Ozcelik S, Tolnay M, Winkler DT, Goedert M: Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain 2012, 135: 2169-2177. 10.1093/brain/aws143
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 197
    • 84862285881 scopus 로고    scopus 로고
    • Autophagic degradation of tau in primary neurons and its enhancement by trehalose
    • Kruger U, Wang Y, Kumar S, Mandelkow EM: Autophagic degradation of tau in primary neurons and its enhancement by trehalose. Neurobiol Aging 2012, 33: 2291-2305. 10.1016/j.neurobiolaging.2011.11.009
    • (2012) Neurobiol Aging , vol.33 , pp. 2291-2305
    • Kruger, U.1    Wang, Y.2    Kumar, S.3    Mandelkow, E.M.4


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