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Volumn 8, Issue 5, 2002, Pages 232-236

The role of chaperones in polyglutamine disease

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; POLYGLUTAMINE;

EID: 0036247596     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4914(02)02310-9     Document Type: Review
Times cited : (35)

References (51)
  • 2
    • 0035393427 scopus 로고    scopus 로고
    • SCA17, a novel autosomal dominant cerebellar ataxia caused by an expanded polyglutamine in TATA-binding protein
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1441-1448
    • Nakamura, K.1
  • 3
    • 0033230850 scopus 로고    scopus 로고
    • Expanding our understanding of polyglutamine diseases through mouse models
    • (1999) Neuron , vol.24 , pp. 499-502
    • Lin, X.1
  • 5
    • 0035421417 scopus 로고    scopus 로고
    • SCA7 mouse models show selective stabilization of mutant ataxin-7 and similar cellular responses in different neuronal cell types
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1679-1692
    • Yvert, G.1
  • 6
    • 0035575858 scopus 로고    scopus 로고
    • Changes in cortical and striatal neurons predict behavioral and electrophysiological abnormalities in a transgenic murine model of Huntington's disease
    • (2001) J. Neurosci. , vol.21 , pp. 9112-9123
    • Laforet, G.A.1
  • 8
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1
  • 9
    • 17344367977 scopus 로고    scopus 로고
    • Behavioural abnormalities and selective neuronal loss in HD transgenic mice expressing mutated full-length HD cDNA
    • (1998) Nat. Genet. , vol.20 , pp. 198-202
    • Reddy, P.H.1
  • 10
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1
  • 12
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.1
  • 13
    • 0033499931 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease
    • (1999) J. Neurosci. , vol.19 , pp. 10338-10347
    • Chai, Y.1
  • 14
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1
  • 15
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1
  • 17
    • 0034646426 scopus 로고    scopus 로고
    • Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2898-2903
    • Wyttenbach, A.1
  • 19
    • 0035964965 scopus 로고    scopus 로고
    • Nuclear aggregation of huntingtin is not prevented by deletion of chaperone Hspl04
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 158-166
    • Cao, F.1
  • 20
    • 0032727617 scopus 로고    scopus 로고
    • Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70
    • (1999) Nat. Genet. , vol.23 , pp. 425-428
    • Warrick, J.M.1
  • 22
    • 0034597833 scopus 로고    scopus 로고
    • Identification of genes that modify ataxin-1-induced neurodegeneration
    • (2000) Nature , vol.408 , pp. 101-106
    • Fernandez-Funez, P.1
  • 23
    • 0035394668 scopus 로고    scopus 로고
    • Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1511-1518
    • Cummings, C.J.1
  • 26
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1
  • 27
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • (2001) Nat. Cell Biol. , vol.3 , pp. 93-96
    • Connell, P.1
  • 28
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase. Identification of Hsc70 as a target for ubiquitylation
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1
  • 30
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1
  • 34
    • 0033636785 scopus 로고    scopus 로고
    • The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome
    • (2000) Mol. Cell , vol.6 , pp. 409-419
    • Kleijnen, M.F.1
  • 35
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Luders, J.1
  • 36
    • 0034703397 scopus 로고    scopus 로고
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2305-2312
    • Davidson, J.D.1
  • 39
    • 0034703863 scopus 로고    scopus 로고
    • Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2811-2820
    • Chan, H.Y.1
  • 40
    • 0001388128 scopus 로고    scopus 로고
    • Expression of polyglutamine-expanded Huntingtin activates the SEK1-JNK pathway and induces apoptosis in a hippocampal neuronal cell line
    • (1998) J. Biol. Chem. , vol.273 , pp. 28873-28877
    • Liu, Y.F.1
  • 41
    • 6744248868 scopus 로고    scopus 로고
    • Triggering of neuronal cell death by accumulation of activated SEK1 on nuclear polyglutamine aggregations in PML bodies
    • (1999) Genes Cells , vol.4 , pp. 743-756
    • Yasuda, S.1
  • 42
    • 0034607702 scopus 로고    scopus 로고
    • Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway
    • (2000) Science , vol.288 , pp. 870-874
    • Tournier, C.1
  • 43
    • 0034532599 scopus 로고    scopus 로고
    • Suppression of stress kinase JNK is involved in HSP72-mediated protection of myogenic cells from transient energy deprivation. HSP72 alleviates the stress-induced inhibition of JNK dephosphorylation
    • (2000) J. Biol. Chem. , vol.275 , pp. 38088-38094
    • Gabai, V.L.1
  • 44
    • 0032932192 scopus 로고    scopus 로고
    • Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: A novel pathway controlled by HSP72
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2547-2555
    • Meriin, A.B.1
  • 46
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • (2000) Nat. Cell Biol. , vol.2 , pp. 469-475
    • Beere, H.M.1
  • 47
    • 0035930598 scopus 로고    scopus 로고
    • Chaperone suppression of cellular toxicity of huntingtin is independent of polyglutamine aggregation
    • (2001) J. Biol. Chem. , vol.276 , pp. 48417-48424
    • Zhou, H.1
  • 48
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein nusfolding in SCA1
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1
  • 49
    • 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
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 731-741
    • Stenoien, D.L.1
  • 50
    • 0034708793 scopus 로고    scopus 로고
    • Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract
    • (2000) J. Biol. Chem. , vol.275 , pp. 8772-8778
    • Kobayashi, Y.1
  • 51
    • 0034641589 scopus 로고    scopus 로고
    • Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2009-2018
    • Jana, N.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.