Mechanism of folding chamber closure in a group II chaperonin-Reference-Cited by-同舟云学术

Mechanism of folding chamber closure in a group II chaperonin

Published:2010-01 Issue:7279 Volume:463 Page:379-383
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Zhang Junjie,Baker Matthew L.,Schröder Gunnar F.,Douglas Nicholai R.,Reissmann Stefanie,Jakana Joanita,Dougherty Matthew,Fu Caroline J.,Levitt Michael,Ludtke Steven J.,Frydman Judith,Chiu Wah

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature08701.pdf

Reference39 articles.

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2. Frydman, J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu. Rev. Biochem. 70, 603–647 (2001)

3. Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852–1858 (2002)

4. Ditzel, L. et al. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93, 125–138 (1998)

5. Reissmann, S., Parnot, C., Booth, C. R., Chiu, W. & Frydman, J. Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nature Struct. Mol. Biol. 14, 432–440 (2007)

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