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Volumn 11, Issue 5, 2002, Pages 1192-1198

Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli

Author keywords

ClpB; Differential scanning calorimetry; Folding domain; Molecular chaperone; Protein stability; Protein protein interactions

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; LUCIFERASE; PROTEIN CLPB; UNCLASSIFIED DRUG;

EID: 0036225109     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.4860102     Document Type: Article
Times cited : (30)

References (26)
  • 3
    • 0034462084 scopus 로고    scopus 로고
    • The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942
    • (2000) J. Bacteriol. , vol.182 , pp. 7092-7096
    • Clarke, A.K.1    Eriksson, M.J.2
  • 5
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 25
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.