Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL.
暂无分享,去创建一个
[1] A. Horwich,et al. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL , 1997, Nature.
[2] J. Weissman,et al. Release of both native and non-native proteins from a cis-only GroEL ternary complex , 1996, Nature.
[3] J. Weissman,et al. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction , 1996, Cell.
[4] J. Weissman,et al. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes , 1995, Cell.
[5] Zbyszek Otwinowski,et al. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å , 1994, Nature.
[6] Y. Kashi,et al. Residues in chaperonin GroEL required for polypeptide binding and release , 1994, Nature.
[7] Yechezkel Kashi,et al. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms , 1994, Cell.
[8] G. Lorimer,et al. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. , 1994, Science.