Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis-Reference-Cited by-同舟云学术

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Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis

Published:2005-02-06 Issue:3 Volume:12 Page:233-237
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Rivenzon-Segal Dalia,Wolf Sharon G,Shimon Liat,Willison Keith R,Horovitz Amnon

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb901.pdf

Reference36 articles.

1. Llorca, O. et al. 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin. Nat. Struct. Biol. 6, 639–642 (1999).

2. Ranson, N.A. et al. ATP-bound states of GroEL captured by cryo-electron microscopy. Cell 107, 869–879 (2001).

3. Horovitz, A., Fridmann, Y., Kafri, G. & Yifrach, O. Review: Allostery in chaperonins. J. Struct. Biol. 135, 104–114 (2001).

4. Saibil, H.R., Horwich, A.L. & Fenton, W.A. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Adv. Protein Chem. 59, 45–72 (2002).

5. Bukau, B. & Horwich, A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92, 351–366 (1998).

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