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Volumn 113, Issue 35, 2016, Pages E5212-E5221

Holdase activity of secreted Hsp70 masks amyloid-β42 neurotoxicity in Drosophila

Author keywords

Amyloid ; Drosophila; Engineered chaperones; Hsp70; Neuroprotections

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMYLOID BETA PROTEIN[1-42]; CHAPERONE; HEAT SHOCK PROTEIN 70; HOLDASE; PROTEIN AGGREGATE; SIGNAL PEPTIDE; UNCLASSIFIED DRUG; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT; PROTEIN BINDING;

EID: 84984674677     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1608045113     Document Type: Article
Times cited : (52)

References (60)
  • 1
    • 77953892400 scopus 로고    scopus 로고
    • Molecular mechanisms of neurodegeneration in Alzheimer's disease
    • Crews L, Masliah E (2010) Molecular mechanisms of neurodegeneration in Alzheimer's disease. Hum Mol Genet 19(R1):R12-R20.
    • (2010) Hum Mol Genet , vol.19 , Issue.1 R , pp. R12-R20
    • Crews, L.1    Masliah, E.2
  • 3
    • 67651180986 scopus 로고    scopus 로고
    • The amyloid hypothesis for Alzheimer's disease: A critical reappraisal
    • Hardy J (2009) The amyloid hypothesis for Alzheimer's disease: A critical reappraisal. J Neurochem 110(4):1129-1134.
    • (2009) J Neurochem , vol.110 , Issue.4 , pp. 1129-1134
    • Hardy, J.1
  • 4
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B (2012) The toxic Aβ oligomer and Alzheimer's disease: An emperor in need of clothes. Nat Neurosci 15(3):349-357.
    • (2012) Nat Neurosci , vol.15 , Issue.3 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8(2):101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 6
    • 38549169530 scopus 로고    scopus 로고
    • The two faces of protein misfolding: Gainand loss-of-function in neurodegenerative diseases
    • Winklhofer KF, Tatzelt J, Haass C (2008) The two faces of protein misfolding: Gainand loss-of-function in neurodegenerative diseases. EMBO J 27(2):336-349.
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 336-349
    • Winklhofer, K.F.1    Tatzelt, J.2    Haass, C.3
  • 7
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings CJ, et al. (1998) Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat Genet 19(2): 148-154.
    • (1998) Nat Genet , vol.19 , Issue.2 , pp. 148-154
    • Cummings, C.J.1
  • 8
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien DL, et al. (1999) Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum Mol Genet 8(5):731-741.
    • (1999) Hum Mol Genet , vol.8 , Issue.5 , pp. 731-741
    • Stenoien, D.L.1
  • 9
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman SK, Raymond GJ, Caughey B, Lindquist S (1997) Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc Natl Acad Sci USA 94(25):13938-13943.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.25 , pp. 13938-13943
    • DebBurman, S.K.1    Raymond, G.J.2    Caughey, B.3    Lindquist, S.4
  • 10
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in drosophila by the molecular chaperone HSP70
    • Warrick JM, et al. (1999) Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70. Nat Genet 23(4):425-428.
    • (1999) Nat Genet , vol.23 , Issue.4 , pp. 425-428
    • Warrick, J.M.1
  • 11
    • 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 (2002) Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295(5556):865-868.
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 12
    • 0037444446 scopus 로고    scopus 로고
    • Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein
    • Adachi H, et al. (2003) Heat shock protein 70 chaperone overexpression ameliorates phenotypes of the spinal and bulbar muscular atrophy transgenic mouse model by reducing nuclear-localized mutant androgen receptor protein. J Neurosci 23(6):2203-2211.
    • (2003) J Neurosci , vol.23 , Issue.6 , pp. 2203-2211
    • Adachi, H.1
  • 13
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • Cummings CJ, et al. (2001) Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice. Hum Mol Genet 10(14): 1511-1518.
    • (2001) Hum Mol Genet , vol.10 , Issue.14 , pp. 1511-1518
    • Cummings, C.J.1
  • 14
    • 11144356089 scopus 로고    scopus 로고
    • CHIP and hsp70 regulate tau ubiquitination, degradation and aggregation
    • Petrucelli L, et al. (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum Mol Genet 13(7):703-714.
    • (2004) Hum Mol Genet , vol.13 , Issue.7 , pp. 703-714
    • Petrucelli, L.1
  • 15
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL (2005) Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6(1):11-22.
    • (2005) Nat Rev Neurosci , vol.6 , Issue.1 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 16
    • 82455210670 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
    • Neef DW, Jaeger AM, Thiele DJ (2011) Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases. Nat Rev Drug Discov 10(12):930-944.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.12 , pp. 930-944
    • Neef, D.W.1    Jaeger, A.M.2    Thiele, D.J.3
  • 17
    • 68649113747 scopus 로고    scopus 로고
    • The role of molecular chaperones in human misfolding diseases
    • Broadley SA, Hartl FU (2009) The role of molecular chaperones in human misfolding diseases. FEBS Lett 583(16):2647-2653.
    • (2009) FEBS Lett , vol.583 , Issue.16 , pp. 2647-2653
    • Broadley, S.A.1    Hartl, F.U.2
  • 18
    • 33845918172 scopus 로고    scopus 로고
    • Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro
    • Evans CG, Wisén S, Gestwicki JE (2006) Heat shock proteins 70 and 90 inhibit early stages of amyloid beta-(1-42) aggregation in vitro. J Biol Chem 281(44):33182-33191.
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33182-33191
    • Evans, C.G.1    Wisén, S.2    Gestwicki, J.E.3
  • 19
    • 84864515731 scopus 로고    scopus 로고
    • Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers
    • Mannini B, et al. (2012) Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc Natl Acad Sci USA 109(31):12479-12484.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.31 , pp. 12479-12484
    • Mannini, B.1
  • 20
    • 1242274389 scopus 로고    scopus 로고
    • Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons
    • Magrané J, Smith RC, Walsh K, Querfurth HW (2004) Heat shock protein 70 participates in the neuroprotective response to intracellularly expressed beta-amyloid in neurons. J Neurosci 24(7):1700-1706.
    • (2004) J Neurosci , vol.24 , Issue.7 , pp. 1700-1706
    • Magrané, J.1    Smith, R.C.2    Walsh, K.3    Querfurth, H.W.4
  • 21
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A (2006) Opposing activities protect against age-onset proteotoxicity. Science 313(5793):1604-1610.
    • (2006) Science , vol.313 , Issue.5793 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 22
    • 79955415881 scopus 로고    scopus 로고
    • Suppression of Alzheimer's disease-related phenotypes by expression of heat shock protein 70 in mice
    • Hoshino T, et al. (2011) Suppression of Alzheimer's disease-related phenotypes by expression of heat shock protein 70 in mice. J Neurosci 31(14):5225-5234.
    • (2011) J Neurosci , vol.31 , Issue.14 , pp. 5225-5234
    • Hoshino, T.1
  • 23
    • 84857135997 scopus 로고    scopus 로고
    • Drosophila models of proteinopathies: The little fly that could
    • Rincon-Limas DE, Jensen K, Fernandez-Funez P (2012) Drosophila models of proteinopathies: The little fly that could. Curr Pharm Des 18(8):1108-1122.
    • (2012) Curr Pharm Des , vol.18 , Issue.8 , pp. 1108-1122
    • Rincon-Limas, D.E.1    Jensen, K.2    Fernandez-Funez, P.3
  • 24
    • 84947037627 scopus 로고    scopus 로고
    • Modeling the complex pathology of Alzheimer's disease in drosophila
    • Fernandez-Funez P, de Mena L, Rincon-Limas DE (2015) Modeling the complex pathology of Alzheimer's disease in Drosophila. Exp Neurol 274(Pt A):58-71.
    • (2015) Exp Neurol , vol.274 , pp. 58-71
    • Fernandez-Funez, P.1    De Mena, L.2    Rincon-Limas, D.E.3
  • 25
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4.0: Discriminating signal peptides from transmembrane regions. Nat Methods 8(10):785-786.
    • (2011) Nat Methods , vol.8 , Issue.10 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    Von Heijne, G.3    Nielsen, H.4
  • 26
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand AH, Perrimon N (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118(2):401-415.
    • (1993) Development , vol.118 , Issue.2 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 27
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in drosophila
    • Warrick JM, et al. (1998) Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 93(6):939-949.
    • (1998) Cell , vol.93 , Issue.6 , pp. 939-949
    • Warrick, J.M.1
  • 28
    • 79956036398 scopus 로고    scopus 로고
    • The ER stress factor XBP1s prevents amyloid-beta neurotoxicity
    • Casas-Tinto S, et al. (2011) The ER stress factor XBP1s prevents amyloid-beta neurotoxicity. Hum Mol Genet 20(11):2144-2160.
    • (2011) Hum Mol Genet , vol.20 , Issue.11 , pp. 2144-2160
    • Casas-Tinto, S.1
  • 29
    • 2142645114 scopus 로고    scopus 로고
    • Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic drosophila
    • Greeve I, et al. (2004) Age-dependent neurodegeneration and Alzheimer-amyloid plaque formation in transgenic Drosophila. J Neurosci 24(16):3899-3906.
    • (2004) J Neurosci , vol.24 , Issue.16 , pp. 3899-3906
    • Greeve, I.1
  • 30
    • 80052858465 scopus 로고    scopus 로고
    • Activation of JNK signaling mediates amyloid-β-dependent cell death
    • Tare M, et al. (2011) Activation of JNK signaling mediates amyloid-β-dependent cell death. PLoS One 6(9):e24361.
    • (2011) PLoS One , vol.6 , Issue.9
    • Tare, M.1
  • 31
    • 17044394194 scopus 로고    scopus 로고
    • Olfactory memory formation in drosophila: From molecular to systems neuroscience
    • Davis RL (2005) Olfactory memory formation in Drosophila: From molecular to systems neuroscience. Annu Rev Neurosci 28:275-302.
    • (2005) Annu Rev Neurosci , vol.28 , pp. 275-302
    • Davis, R.L.1
  • 32
    • 43749097858 scopus 로고    scopus 로고
    • Neuronal assemblies of the drosophila mushroom body
    • Tanaka NK, Tanimoto H, Ito K (2008) Neuronal assemblies of the Drosophila mushroom body. J Comp Neurol 508(5):711-755.
    • (2008) J Comp Neurol , vol.508 , Issue.5 , pp. 711-755
    • Tanaka, N.K.1    Tanimoto, H.2    Ito, K.3
  • 33
    • 79961000597 scopus 로고    scopus 로고
    • Characterization of oligomer formation of amyloid-beta peptide using a split-luciferase complementation assay
    • Hashimoto T, Adams KW, Fan Z, McLean PJ, Hyman BT (2011) Characterization of oligomer formation of amyloid-beta peptide using a split-luciferase complementation assay. J Biol Chem 286(31):27081-27091.
    • (2011) J Biol Chem , vol.286 , Issue.31 , pp. 27081-27091
    • Hashimoto, T.1    Adams, K.W.2    Fan, Z.3    McLean, P.J.4    Hyman, B.T.5
  • 34
    • 0032837196 scopus 로고    scopus 로고
    • Tissue-specific expression of dominant negative mutant drosophila HSC70 causes developmental defects and lethality
    • Elefant F, Palter KB (1999) Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality. Mol Biol Cell 10(7): 2101-2117.
    • (1999) Mol Biol Cell , vol.10 , Issue.7 , pp. 2101-2117
    • Elefant, F.1    Palter, K.B.2
  • 35
    • 84899069290 scopus 로고    scopus 로고
    • Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove
    • Rohrer KM, Haug M, Schwörer D, Kalbacher H, Holzer U (2014) Mutations in the substrate binding site of human heat-shock protein 70 indicate specific interaction with HLA-DR outside the peptide binding groove. Immunology 142(2):237-247.
    • (2014) Immunology , vol.142 , Issue.2 , pp. 237-247
    • Rohrer, K.M.1    Haug, M.2    Schwörer, D.3    Kalbacher, H.4    Holzer, U.5
  • 36
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman BC, Morimoto RI (1996) The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J 15(12):2969-2979.
    • (1996) EMBO J , vol.15 , Issue.12 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 38
    • 84893642253 scopus 로고    scopus 로고
    • Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases
    • Guo JL, Lee VM (2014) Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases. Nat Med 20(2):130-138.
    • (2014) Nat Med , vol.20 , Issue.2 , pp. 130-138
    • Guo, J.L.1    Lee, V.M.2
  • 39
    • 0035254227 scopus 로고    scopus 로고
    • Hsp72 functions as a natural inhibitory protein of c-jun N-terminal kinase
    • Park HS, Lee JS, Huh SH, Seo JS, Choi EJ (2001) Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase. EMBO J 20(3):446-456.
    • (2001) EMBO J , vol.20 , Issue.3 , pp. 446-456
    • Park, H.S.1    Lee, J.S.2    Huh, S.H.3    Seo, J.S.4    Choi, E.J.5
  • 40
    • 38149065825 scopus 로고    scopus 로고
    • Exogenous hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress
    • Robinson MB, Taylor AR, Gifondorwa DJ, Tytell M, Milligan CE (2008) Exogenous Hsc70, but not thermal preconditioning, confers protection to motoneurons subjected to oxidative stress. Dev Neurobiol 68(1):1-17.
    • (2008) Dev Neurobiol , vol.68 , Issue.1 , pp. 1-17
    • Robinson, M.B.1    Taylor, A.R.2    Gifondorwa, D.J.3    Tytell, M.4    Milligan, C.E.5
  • 41
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • Bader N, Grune T (2006) Protein oxidation and proteolysis. Biol Chem 387(10-11): 1351-1355.
    • (2006) Biol Chem , vol.387 , Issue.10-11 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 42
    • 84869498101 scopus 로고    scopus 로고
    • Chaperones in autophagy
    • Kaushik S, Cuervo AM (2012) Chaperones in autophagy. Pharmacol Res 66(6):484-493.
    • (2012) Pharmacol Res , vol.66 , Issue.6 , pp. 484-493
    • Kaushik, S.1    Cuervo, A.M.2
  • 43
    • 84863986350 scopus 로고    scopus 로고
    • Roles of extracellular chaperones in amyloidosis
    • Wyatt AR, Yerbury JJ, Dabbs RA, Wilson MR (2012) Roles of extracellular chaperones in amyloidosis. J Mol Biol 421(4-5):499-516.
    • (2012) J Mol Biol , vol.421 , Issue.4-5 , pp. 499-516
    • Wyatt, A.R.1    Yerbury, J.J.2    Dabbs, R.A.3    Wilson, M.R.4
  • 44
    • 84877353475 scopus 로고    scopus 로고
    • Extracellular chaperones prevent Aβ42-induced toxicity in rat brains
    • Cascella R, et al. (2013) Extracellular chaperones prevent Aβ42-induced toxicity in rat brains. Biochim Biophys Acta 1832(8):1217-1226.
    • (2013) Biochim Biophys Acta , vol.1832 , Issue.8 , pp. 1217-1226
    • Cascella, R.1
  • 45
    • 0036678856 scopus 로고    scopus 로고
    • Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease
    • DeMattos RB, et al. (2002) Clusterin promotes amyloid plaque formation and is critical for neuritic toxicity in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 99(16):10843-10848.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.16 , pp. 10843-10848
    • DeMattos, R.B.1
  • 46
    • 4143138471 scopus 로고    scopus 로고
    • In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology
    • Holtzman DM (2004) In vivo effects of ApoE and clusterin on amyloid-beta metabolism and neuropathology. J Mol Neurosci 23(3):247-254.
    • (2004) J Mol Neurosci , vol.23 , Issue.3 , pp. 247-254
    • Holtzman, D.M.1
  • 47
    • 84949233665 scopus 로고    scopus 로고
    • Anti-Aβ single-chain variable fragment antibodies exert synergistic neuroprotective activities in drosophila models of Alzheimer's disease
    • Fernandez-Funez P, et al. (2015) Anti-Aβ single-chain variable fragment antibodies exert synergistic neuroprotective activities in Drosophila models of Alzheimer's disease. Hum Mol Genet 24(21):6093-6105.
    • (2015) Hum Mol Genet , vol.24 , Issue.21 , pp. 6093-6105
    • Fernandez-Funez, P.1
  • 48
    • 0034597833 scopus 로고    scopus 로고
    • Identification of genes that modify ataxin-1-induced neurodegeneration
    • Fernandez-Funez P, et al. (2000) Identification of genes that modify ataxin-1-induced neurodegeneration. Nature 408(6808):101-106.
    • (2000) Nature , vol.408 , Issue.6808 , pp. 101-106
    • Fernandez-Funez, P.1
  • 49
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431(7010):805-810.
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 50
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor JP, et al. (2003) Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum Mol Genet 12(7):749-757.
    • (2003) Hum Mol Genet , vol.12 , Issue.7 , pp. 749-757
    • Taylor, J.P.1
  • 51
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11(11):777-788.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 52
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin P, Melki R, Kopito R (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 11(4):301-307.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 53
    • 84883688262 scopus 로고    scopus 로고
    • Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
    • Jucker M, Walker LC (2013) Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501(7465):45-51.
    • (2013) Nature , vol.501 , Issue.7465 , pp. 45-51
    • Jucker, M.1    Walker, L.C.2
  • 54
    • 0343092052 scopus 로고    scopus 로고
    • The level of DLDB/CHIP controls the activity of the LIM homeodomain protein apterous: Evidence for a functional tetramer complex in vivo
    • Rincón-Limas DE, Lu CH, Canal I, Botas J (2000) The level of DLDB/CHIP controls the activity of the LIM homeodomain protein apterous: Evidence for a functional tetramer complex in vivo. EMBO J 19(11):2602-2614.
    • (2000) EMBO J , vol.19 , Issue.11 , pp. 2602-2614
    • Rincón-Limas, D.E.1    Lu, C.H.2    Canal, I.3    Botas, J.4
  • 55
    • 67651047286 scopus 로고    scopus 로고
    • In vivo generation of neurotoxic prion protein: Role for hsp70 in accumulation of misfolded isoforms
    • Fernandez-Funez P, et al. (2009) In vivo generation of neurotoxic prion protein: Role for hsp70 in accumulation of misfolded isoforms. PLoS Genet 5(6):e1000507.
    • (2009) PLoS Genet , vol.5 , Issue.6
    • Fernandez-Funez, P.1
  • 56
    • 0019945644 scopus 로고
    • Genetic transformation of drosophila with transposable element vectors
    • Rubin GM, Spradling AC (1982) Genetic transformation of Drosophila with transposable element vectors. Science 218(4570):348-353.
    • (1982) Science , vol.218 , Issue.4570 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 57
    • 2542582998 scopus 로고    scopus 로고
    • Apical accumulation of the drosophila PDGF/VEGF receptor ligands provides a mechanism for triggering localized actin polymerization
    • Rosin D, Schejter E, Volk T, Shilo BZ (2004) Apical accumulation of the Drosophila PDGF/VEGF receptor ligands provides a mechanism for triggering localized actin polymerization. Development 131(9):1939-1948.
    • (2004) Development , vol.131 , Issue.9 , pp. 1939-1948
    • Rosin, D.1    Schejter, E.2    Volk, T.3    Shilo, B.Z.4
  • 58
    • 33846219134 scopus 로고    scopus 로고
    • Unfolded protein response in a drosophila model for retinal degeneration
    • Ryoo HD, Domingos PM, Kang MJ, Steller H (2007) Unfolded protein response in a Drosophila model for retinal degeneration. EMBO J 26(1):242-252.
    • (2007) EMBO J , vol.26 , Issue.1 , pp. 242-252
    • Ryoo, H.D.1    Domingos, P.M.2    Kang, M.J.3    Steller, H.4
  • 59
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabayashi T, et al. (2001) Age-dependent changes in brain, CSF, and plasma amyloid (beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J Neurosci 21(2):372-381.
    • (2001) J Neurosci , vol.21 , Issue.2 , pp. 372-381
    • Kawarabayashi, T.1
  • 60
    • 44949217679 scopus 로고    scopus 로고
    • BRI2 (ITM2b) inhibits abeta deposition in vivo
    • Kim J, et al. (2008) BRI2 (ITM2b) inhibits Abeta deposition in vivo. J Neurosci 28(23): 6030-6036.
    • (2008) J Neurosci , vol.28 , Issue.23 , pp. 6030-6036
    • Kim, J.1


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