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Volumn 9, Issue 19, 2000, Pages 2811-2820

Mechanisms of chaperone suppression of polyglutamine disease: Selectivity, synergy and modulation of protein solubility in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHAPERONE; HEAT SHOCK PROTEIN 70; HUNTINGTIN; NEUROTOXIN; POLYGLUTAMINE;

EID: 0034703863     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/9.19.2811     Document Type: Article
Times cited : (279)

References (29)
  • 18
    • 0032489556 scopus 로고    scopus 로고
    • The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydjl assist Hsp70 in protein folding
    • (1998) J. Biol. Chem. , vol.273 , pp. 5970-5978
    • Lu, Z.1    Cyr, D.M.2
  • 19
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 23
    • 0032837196 scopus 로고    scopus 로고
    • Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality
    • (1999) Mol Biol. Cell. , vol.10 , pp. 2101-2117
    • Elefant, F.1    Palter, K.2
  • 24
    • 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
    • (1998) Genes Dev. , vol.12 , pp. 3788-3796
    • Morimoto, R.I.1
  • 27


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.