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Volumn 9, Issue 13, 2000, Pages 2009-2018

Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: Their role in suppression of aggregation and cellular toxicity

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL PROTEIN; CHAPERONE; ECDYSONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HUNTINGTIN; POLYGLUTAMINE; UBIQUITIN;

EID: 0034641589     PISSN: 09646906     EISSN: None     Source Type: Journal    
DOI: 10.1093/hmg/9.13.2009     Document Type: Article
Times cited : (380)

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    • (1997) , pp. 89-95
    • Cyr, D.M.1
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    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
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    • The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.