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Volumn 6, Issue 7, 1999, Pages 683-690

GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; LYSOZYME; TRYPTOPHAN;

EID: 0032984605     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/10735     Document Type: Article
Times cited : (64)

References (14)
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  • 2
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  • 3
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    • The crystal structure of the bacterial chaperonin GroEL at 2.8 A
    • Braig, K. et al. The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371, 578-586 (1994).
    • (1994) Nature , vol.371 , pp. 578-586
    • Braig, K.1
  • 4
  • 5
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    • Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody
    • Ishii, N., Taguchi, H., Sasabe, H. & Yoshida, M. Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody. J. Mol. Biol. 236, 691-696 (1994).
    • (1994) J. Mol. Biol. , vol.236 , pp. 691-696
    • Ishii, N.1    Taguchi, H.2    Sasabe, H.3    Yoshida, M.4
  • 6
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan, P., Henderson, S.J. & Joachimiak, A. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure 4, 79-88 (1996).
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 9
    • 0025988476 scopus 로고
    • Binding of a chaperonin to the folding intermediates of lactate dehydrogenase
    • Badcoe, I.G., et al. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase. Biochemistry 30, 9195-9200 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9195-9200
    • Badcoe, I.G.1
  • 10
    • 0028792612 scopus 로고
    • Nature and consequences of GroEL-protein interactions
    • Itzhaki, L.S., Otzen, D.E. & Fersht, A.R. Nature and consequences of GroEL-protein interactions. Biochemistry 34, 14581-14587 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14581-14587
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 11
    • 0029975103 scopus 로고    scopus 로고
    • Dynamics of the GroEL protein complex: Effects of nucleotides and folding mutants
    • Sparrer, H., Lilie, H. & Buchner, J. Dynamics of the GroEL protein complex: Effects of nucleotides and folding mutants. J. Mol. Biol. 258, 74-87 (1996).
    • (1996) J. Mol. Biol. , vol.258 , pp. 74-87
    • Sparrer, H.1    Lilie, H.2    Buchner, J.3
  • 12
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    • Effect of GroEL on the re-folding kinetics of alpha-lactalbumin
    • Katsumata, K., Okazaki, A. & Kuwajima, K. Effect of GroEL on the re-folding kinetics of alpha-lactalbumin. J. Mol. Biol. 258, 827-838 (1996).
    • (1996) J. Mol. Biol. , vol.258 , pp. 827-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 13
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    • Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL
    • Gray, I.E., Eder, J., Bycroft, M., Day, A.G. & Fersht, A.R. Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL EMBO J. 12, 4145-4150 (1993).
    • (1993) EMBO J. , vol.12 , pp. 4145-4150
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  • 14
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.