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Volumn 45, Issue 11, 2010, Pages 1333-1338

Neurodegenerative conformational disease and heat shock proteins

Author keywords

synuclein; amyloid; Heat shock protein; Neurodegenerative conformational disease; Protein misfolding

Indexed keywords

HEAT SHOCK PROTEIN; OLIGOMER; PROTEASOME; UBIQUITIN;

EID: 78651259312     PISSN: 05134870     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (2)

References (28)
  • 1
    • 69449108391 scopus 로고    scopus 로고
    • Identification of independent APP locus duplication in Japanese patients with early-onset Alzheimer disease
    • J
    • Kasuga K, Shimohata T, Nishimura A, et al. Identification of independent APP locus duplication in Japanese patients with early-onset Alzheimer disease [J]. Neurol Neurosurg Psychiatry, 2009, 80: 1050-1052.
    • (2009) Neurol Neurosurg Psychiatry , vol.80 , pp. 1050-1052
    • Kasuga, K.1    Shimohata, T.2    Nishimura, A.3
  • 2
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of a-synuclein aggregation
    • J
    • Vladimir N. Uversky. Neuropathology, biochemistry, and biophysics of a-synuclein aggregation [J]. J Neurochem, 2007, 103: 17-37.
    • (2007) J Neurochem , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 3
    • 70350036064 scopus 로고    scopus 로고
    • Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease
    • J
    • Yumoto S, Kakimi S, Ohsaki A, et al. Demonstration of aluminum in amyloid fibers in the cores of senile plaques in the brains of patients with Alzheimer's disease [J]. J Inorg Biochem, 2009, 103: 1579-1584.
    • (2009) J Inorg Biochem , vol.103 , pp. 1579-1584
    • Yumoto, S.1    Kakimi, S.2    Ohsaki, A.3
  • 6
    • 23244449092 scopus 로고    scopus 로고
    • Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p
    • J
    • Chan JC, Oyler NA, Yau WM, et al. Parallel β-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p [J]. Biochemistry, 2005, 44: 10669-10680.
    • (2005) Biochemistry , vol.44 , pp. 10669-10680
    • Chan, J.C.1    Oyler, N.A.2    Yau, W.M.3
  • 7
    • 71949086967 scopus 로고    scopus 로고
    • Molecular pathogenesis of protein misfolding diseases: Pathological molecular environments versus quality control systems against misfolded proteins
    • J
    • Naiki H, Nagai, Y. Molecular pathogenesis of protein misfolding diseases: pathological molecular environments versus quality control systems against misfolded proteins [J]. J Biochem, 2009, 146: 751-756.
    • (2009) J Biochem , vol.146 , pp. 751-756
    • Naiki, H.1    Nagai, Y.2
  • 8
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity
    • J
    • Simakova O, Arispe NJ. The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity [J]. J Neurosci, 2007, 27: 13719-13729.
    • (2007) J Neurosci , vol.27 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 9
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • DOI 10.1038/nature02621
    • Mattson MP. Pathways towards and away from Alzheimer's disease [J]. Nature, 2004, 430: 631-639. (Pubitemid 39061671)
    • (2004) Nature , vol.430 , Issue.7000 , pp. 631-639
    • Mattson, M.P.1
  • 10
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre B, et al. Neurodegenerative disease: amyloid pores from pathogenic mutations [J]. Nature, 2002, 418: 291. (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 11
    • 34248159338 scopus 로고    scopus 로고
    • Protein stress and stress proteins: Implications in aging and disease
    • DOI 10.1007/s12038-007-0050-z
    • Soti C, Csermely P. Protein stress and stress proteins: implications in aging and disease [J]. J Biosci, 2007, 32: 511-515. (Pubitemid 46708701)
    • (2007) Journal of Biosciences , vol.32 , Issue.3 , pp. 511-515
    • Soti, C.1    Csermely, P.2
  • 12
    • 58149388879 scopus 로고    scopus 로고
    • Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: A mechanistic link between Abeta and tau pathology
    • J
    • Oddo S, Caccamo A, Tseng B, et al. Blocking Abeta42 accumulation delays the onset and progression of tau pathology via the C terminus of heat shock protein70-interacting protein: a mechanistic link between Abeta and tau pathology [J]. J Neurosci, 2008, 28: 12163-12175.
    • (2008) J Neurosci , vol.28 , pp. 12163-12175
    • Oddo, S.1    Caccamo, A.2    Tseng, B.3
  • 13
    • 33745874108 scopus 로고    scopus 로고
    • Small heat shock proteins differentially affect Abeta aggregation and toxicity
    • DOI 10.1016/j.bbrc.2006.06.128, PII S0006291X06014513
    • Lee S, Carson K, Rice-Ficht A, et al. Small heat shock proteins differentially affect Abeta aggregation and toxicity [J]. Biochem Biophys Res Commun, 2006, 347: 527-533. (Pubitemid 44041445)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.2 , pp. 527-533
    • Lee, S.1    Carson, K.2    Rice-Ficht, A.3    Good, T.4
  • 14
    • 33745959291 scopus 로고    scopus 로고
    • Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
    • J
    • Dickey CA, Yue M, Lin WL, et al. Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species [J]. J Neurosci, 2006, 26: 6985-6996.
    • (2006) J Neurosci , vol.26 , pp. 6985-6996
    • Dickey, C.A.1    Yue, M.2    Lin, W.L.3
  • 15
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular beta-amyloid-induced inhibition of complex IV and limit apoptosis
    • DOI 10.1074/jbc.M602533200
    • Veereshwarayya V, Kumar P, Rosen KM, et al. Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular beta-amyloid-induced inhibition of complex IV and limit apoptosis [J]. J Biol Chem, 2006, 281: 29468-29478. (Pubitemid 44536955)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 16
    • 38149110518 scopus 로고    scopus 로고
    • Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein
    • J
    • Fonte V, Kipp DR, Yerg J, et al. Suppression of in vivo beta-amyloid peptide toxicity by overexpression of the HSP-16.2 small chaperone protein [J]. J Biol Chem, 2008, 283: 784-791.
    • (2008) J Biol Chem , vol.283 , pp. 784-791
    • Fonte, V.1    Kipp, D.R.2    Yerg, J.3
  • 17
    • 42449091462 scopus 로고    scopus 로고
    • Small heat shock proteins Hsp27 or alphaB-crystallin and the protein components of neurofibrillary tangles: Tau and neurofilaments
    • DOI 10.1002/jnr.21589
    • Bjorkdahl C, Sjogren MJ, Zhou X, et al. Small heat shock proteins Hsp27 or alphaB-crystallin and the protein components of neurofibrillary tangles: tau and neurofilaments [J]. J Neurosci Res, 2008, 86: 1343-1352. (Pubitemid 351571908)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.6 , pp. 1343-1352
    • Bjorkdahl, C.1    Sjogren, M.J.2    Zhou, X.3    Concha, H.4    Avila, J.5    Winblad, B.6    Pei, J.-J.7
  • 18
    • 70449461063 scopus 로고    scopus 로고
    • The small heat shock protein Hsp27 protects cortical neurons against the toxic effects of beta-amyloid peptide
    • J
    • King M, Nafar F, Clarke J, et al. The small heat shock protein Hsp27 protects cortical neurons against the toxic effects of beta-amyloid peptide [J]. J Neurosci Res, 2009, 87: 3161-3175.
    • (2009) J Neurosci Res , vol.87 , pp. 3161-3175
    • King, M.1    Nafar, F.2    Clarke, J.3
  • 19
    • 33646555755 scopus 로고    scopus 로고
    • +in SK-N-SH cells
    • DOI 10.1016/j.febslet.2006.04.057, PII S001457930600500X
    • Fan GH, Zhou HY, Yang H, et al. Heat shock proteins reduce alpha-synuclein aggregation induced by MPP+ in SK-N-SH cells [J]. FEBS Lett, 2006, 580: 3091-3098. (Pubitemid 43729666)
    • (2006) FEBS Letters , vol.580 , Issue.13 , pp. 3091-3098
    • Fan, G.-H.1    Zhou, H.-Y.2    Yang, H.3    Chen, S.-D.4
  • 20
    • 28844451001 scopus 로고    scopus 로고
    • Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
    • DOI 10.1074/jbc.M505524200
    • Shen HY, He JC, Wang Y, et al. Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice [J]. J Biol Chem, 2005, 280: 39962-39969. (Pubitemid 41779131)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39962-39969
    • Shen, H.-Y.1    He, J.-C.2    Wang, Y.3    Huang, Q.-Y.4    Chen, J.-F.5
  • 21
    • 13244267202 scopus 로고    scopus 로고
    • Mechanisms of suppression of {alpha}-synuclein neurotoxicity by geldanamycin in Drosophila
    • J
    • Auluck PK, Meulener MC, Bonini NM. Mechanisms of suppression of {alpha}-synuclein neurotoxicity by geldanamycin in Drosophila [J]. 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
  • 22
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • J
    • Flower TR, Chesnokova LS, Froelich CA, et al. Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease [J]. J Mol Biol, 2005, 351: 1081-1100.
    • (2005) J Mol Biol , vol.351 , pp. 1081-1100
    • Flower, T.R.1    Chesnokova, L.S.2    Froelich, C.A.3
  • 23
    • 11844274735 scopus 로고    scopus 로고
    • Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells
    • DOI 10.1016/j.bbrc.2004.12.066, PII S0006291X04028670
    • Gorman AM, Szegezdi E, Quigney DJ, et al. Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells [J]. Biochem Biophys Res Commun, 2005, 327: 801-810. (Pubitemid 40092820)
    • (2005) Biochemical and Biophysical Research Communications , vol.327 , Issue.3 , pp. 801-810
    • Gorman, A.M.1    Szegezdi, E.2    Quigney, D.J.3    Samali, A.4
  • 24
    • 10944241135 scopus 로고    scopus 로고
    • Hsp70 gene transfer by adeno-associated virusi inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease
    • DOI 10.1016/j.ymthe.2004.09.007, PII S1525001604014480
    • Dong Z, Wolfer DP, Lipp HP, et al. Hsp70 gene transfer by adeno-associated virus inhibits MPTP-induced nigrostriatal degeneration in the mouse model of Parkinson disease [J]. Mol Ther, 2005, 11: 80-88. (Pubitemid 40012001)
    • (2005) Molecular Therapy , vol.11 , Issue.1 , pp. 80-88
    • Dong, Z.1    Wolfer, D.P.2    Lipp, H.-P.3    Bueler, H.4
  • 25
    • 33750873994 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates
    • J
    • Huang C, Cheng H, Hao S, et al. Heat shock protein 70 inhibits alpha-synuclein fibril formation via interactions with diverse intermediates [J]. J Mol Biol, 2006, 364: 323-336.
    • (2006) J Mol Biol , vol.364 , pp. 323-336
    • Huang, C.1    Cheng, H.2    Hao, S.3
  • 26
    • 56749117866 scopus 로고    scopus 로고
    • Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly
    • J
    • Luk KC, Mills IP, Trojanowski JQ, et al. Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly [J]. Biochemistry, 2008, 47: 12614-12625.
    • (2008) Biochemistry , vol.47 , pp. 12614-12625
    • Luk, K.C.1    Mills, I.P.2    Trojanowski, J.Q.3
  • 27
    • 51349150684 scopus 로고    scopus 로고
    • Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
    • J
    • Lo Bianco C, Shorter J, Regulier E, et al. Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease [J]. J Clin Invest, 2008, 118: 3087-3097.
    • (2008) J Clin Invest , vol.118 , pp. 3087-3097
    • Lo Bianco, C.1    Shorter, J.2    Regulier, E.3
  • 28
    • 33751216491 scopus 로고    scopus 로고
    • Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation
    • J
    • Outeiro TF, Klucken J, Strathearn KE, et al. Small heat shock proteins protect against alpha-synuclein-induced toxicity and aggregation [J]. Biochem Biophys Res Commun, 2006, 351: 631-638.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 631-638
    • Outeiro, T.F.1    Klucken, J.2    Strathearn, K.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.