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Volumn 363, Issue 2, 2002, Pages 329-334

The reassembling process of the nonameric Mycobacterium tuberculosis small heat-shock protein hsp16.3 occurs via a stepwise mechanism

Author keywords

Electrophoresis; Oligomeric protein; Reassembling; Urea denaturing; Urea gradient PAGE

Indexed keywords

BACTERIA; DIALYSIS; OLIGOMERS; PROTEINS; UREA;

EID: 0037090621     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3630329     Document Type: Article
Times cited : (10)

References (22)
  • 7
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    • Inactive GroEL monomers can be isolated and reassembled to functional tetradecamers that contain few bound peptides
    • (1995) J. Biol. Chem. , vol.270 , pp. 22962-22967
    • Ybarra, J.1    Horowitz, P.M.2
  • 16
    • 0033776418 scopus 로고    scopus 로고
    • Probing the roles of the only universally conserved leucine residue (Leu122) in the oligomerization and chaperone-like activity of Mycobacterium tuberculosis small heat shock protein Hsp16.3
    • (2000) J. Protein Chem. , vol.4 , pp. 319-326
    • Dai, H.1    Mao, Q.2    Yang, H.3    Huang, S.4    Chang, Z.5
  • 17
    • 0033525723 scopus 로고    scopus 로고
    • Site-directed spin labeling study of subunit interactions in the alpha-crystallin domain of small heat-shock proteins. Comparison of the oligomer symmetry in alphaA-crystallin, HSP 27, and HSP 16.3
    • (1999) J. Biol. Chem. , vol.274 , pp. 6305-6314
    • Berengian, A.R.1    Parfenova, M.2    McHaourab, H.S.3
  • 21
    • 0029124685 scopus 로고
    • Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin
    • (1995) FEBS Lett. , vol.369 , pp. 321-325
    • Das, K.P.1    Surewicz, W.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.