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- [26] The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding Nature Structural Biology, 1998, 5 : 977 - 985
- [27] Hot papers - Biochemistry structural biology - The crystal structure of the bacterial chaperonin GroEL at 2.8 angstroms by K. Braig, Z. Otwinowski, R. Hegde, D.C. Boisvert, A. Joachimiak, A.L. Horwich, P.B. Sigler - Residues in chaperonin GroEL required for polypeptide binding and release by W.A. Fenton, Y. Kaishi, K. Furtak, A. Horwich - Comments SCIENTIST, 1996, 10 (05): : 14 - 14
- [28] Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis EMBO JOURNAL, 1996, 15 (22): : 6111 - 6121