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Volumn 23, Issue 4, 1999, Pages 425-428

Suppression of polyglutamine-mediated neurodegeneration in Drosophila by the molecular chaperone HSP70

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLUTAMINE; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; POLYAMINOACID;

EID: 0032727617     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/70532     Document Type: Article
Times cited : (743)

References (30)
  • 1
    • 0033071176 scopus 로고    scopus 로고
    • Protein fate in neurodegenerative proteinopathies: Polyglutamine diseases join the (mis)fold
    • Paulson, H. Protein fate in neurodegenerative proteinopathies: polyglutamine diseases join the (mis)fold. Am. J. Hum. Genet. 64, 339-345 (1999).
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 339-345
    • Paulson, H.1
  • 2
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz, M. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24, 58-63 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.1
  • 3
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • Davies, S.W. et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90, 537-548 (1997).
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1
  • 4
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990-1993 (1997).
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1
  • 5
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • Paulson, H.L. et al. Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19, 333-344 (1997).
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1
  • 6
    • 0033030565 scopus 로고    scopus 로고
    • Evidence for proteasome involvement in polyglutamine disease: Localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro
    • Chai, Y., Koppenmhafer, S., Shoesmith, S., Perez, M. & Paulson, H. Evidence for proteasome involvement in polyglutamine disease: localization to nuclear inclusions in SCA3/MJD and suppression of polyglutamine aggregation in vitro. Hum. Mol. Genet. 8, 673-682 (1998).
    • (1998) Hum. Mol. Genet. , vol.8 , pp. 673-682
    • Chai, Y.1    Koppenmhafer, S.2    Shoesmith, S.3    Perez, M.4    Paulson, H.5
  • 7
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C.J. et al. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nature Genet. 19, 148-154 (1998).
    • (1998) Nature Genet. , vol.19 , 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, D. et al. 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, 731-741 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 731-741
    • Stenoien, D.1
  • 9
    • 85088173192 scopus 로고    scopus 로고
    • Analysis of the role of heat shock protein (Hsp) chaperones in polyglutamine disease
    • in press
    • Chai, Y., Koppenhafer, S., Bonini, N. & Paulson, H. Analysis of the role of heat shock protein (Hsp) chaperones in polyglutamine disease. J. Neurosci. (in press).
    • J. Neurosci.
    • Chai, Y.1    Koppenhafer, S.2    Bonini, N.3    Paulson, H.4
  • 10
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick, J.M. et al. Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila Cell 93, 939-949 (1998).
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1
  • 11
    • 0029134871 scopus 로고
    • Spinocerebellar ataxia type 1 and Machado-Joseph disease: Incidence of CAG expansions among adult-onset ataxia patients from 311 families with dominant, recessive, or sporadic ataxia
    • Ranum, L. et al. Spinocerebellar ataxia type 1 and Machado-Joseph disease: incidence of CAG expansions among adult-onset ataxia patients from 311 families with dominant, recessive, or sporadic ataxia. Am. J. Hum. Genet. 57, 603-603 (1995).
    • (1995) Am. J. Hum. Genet. , vol.57 , pp. 603-603
    • Ranum, L.1
  • 12
    • 0028988941 scopus 로고
    • Trinucleotide expansion within the MJDI gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients
    • Schols, L. et al. Trinucleotide expansion within the MJDI gene presents clinically as spinocerebellar ataxia and occurs most frequently in German SCA patients. Hum. Mol. Genet. 4, 1001-1005 (1995).
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1001-1005
    • Schols, L.1
  • 13
    • 9244225693 scopus 로고    scopus 로고
    • Spinocerebellar ataxia 3 and Machado-Joseph disease: Clinical, molecular and neuropathologic features
    • Durr, A. et al. Spinocerebellar ataxia 3 and Machado-Joseph disease: clinical, molecular and neuropathologic features. Ann. Neurol. 39, 490-491 (1996).
    • (1996) Ann. Neurol. , vol.39 , pp. 490-491
    • Durr, A.1
  • 14
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • Ikeda, H. et al. Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nature Genet. 13, 196-202 (1996).
    • (1996) Nature Genet. , vol.13 , pp. 196-202
    • Ikeda, H.1
  • 15
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. & Perrimon, N. Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development 118, 401-415 (1993).
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 16
    • 0003739085 scopus 로고
    • (eds Bate, M. & Martinez-Arias, A.) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wolff, T. & Ready, D.F. in The Development of Drosophila melanogaster (eds Bate, M. & Martinez-Arias, A.) 1277-1325 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1993).
    • (1993) The Development of Drosophila Melanogaster , pp. 1277-1325
    • Wolff, T.1    Ready, D.F.2
  • 17
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. Molecular chaperones in cellular protein folding. Nature 381, 571-580 (1996).
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.1
  • 18
    • 0000097632 scopus 로고
    • Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70
    • Hunt, C. & Morimoto, R. Conserved features of eukaryotic hsp70 genes revealed by comparison with the nucleotide sequence of human hsp70. Proc. Natl Acad. Sci. USA 82, 6455-6459 (1985).
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 6455-6459
    • Hunt, C.1    Morimoto, R.2
  • 19
    • 0028147879 scopus 로고
    • Ectopic and increased expression of fasciclin II alters motoneuron growth cone guidance
    • Lin, D.M. & Goodman, C.S. Ectopic and increased expression of fasciclin II alters motoneuron growth cone guidance. Neuron 13, 507-523 (1994).
    • (1994) Neuron , vol.13 , pp. 507-523
    • Lin, D.M.1    Goodman, C.S.2
  • 20
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-mediated disease in SCA1 transgenic mice
    • Klement, I. et al. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-mediated disease in SCA1 transgenic mice. Cell 95, 41-53 (1998).
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.1
  • 21
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. & Greenberg, M. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66 (1998).
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.4
  • 22
    • 0032837196 scopus 로고    scopus 로고
    • Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality
    • Elefant, F. & Palter, K. Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality. Mol. Biol. Cell 10, 2101-2117 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2101-2117
    • Elefant, F.1    Palter, K.2
  • 23
    • 0031443433 scopus 로고    scopus 로고
    • Chaperone-supervised conversion of prion protein to its protease-resistant form
    • DebBurman, S., Raymond, G., Caughey, B. & Lindquist, S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl Acad. Sci. USA 94, 13938-13943 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13938-13943
    • DebBurman, S.1    Raymond, G.2    Caughey, B.3    Lindquist, S.4
  • 24
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover, J. & Lindquist, S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82 (1998).
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.1    Lindquist, S.2
  • 25
    • 0032168160 scopus 로고    scopus 로고
    • Polyglutamine-expanded human Huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons
    • Jackson, G. et al. Polyglutamine-expanded human Huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons. Neuron 21, 633-642 (1998).
    • (1998) Neuron , vol.21 , pp. 633-642
    • Jackson, G.1
  • 26
    • 0344431341 scopus 로고    scopus 로고
    • Structural neurobiology: Are seeds at the root of neuronal degeneration?
    • Landsbury, P. Jr Structural neurobiology: are seeds at the root of neuronal degeneration? Neuron 19, 1151-1154 (1997).
    • (1997) Neuron , vol.19 , pp. 1151-1154
    • Landsbury P., Jr.1
  • 27
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner, S. Prion diseases and the BSE crisis. Science 278, 245-251 (1997).
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.1
  • 28
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • Selkoe, D. Alzheimer's disease: genotypes, phenotypes, and treatments. Science 275, 630-631 (1997).
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.1
  • 29
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos, M. et al. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276, 2045-2047 (1997).
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.1
  • 30
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin, G.M. & Spradling, A.C. Genetic transformation of Drosophila with transposable element vectors. Science 218, 348-353 (1982).
    • (1982) Science , vol.218 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.