Chaperonin complex with a newly folded protein encapsulated in the folding chamber
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature07479.pdf
Reference36 articles.
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2. Kerner, M. J. et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli . Cell 122, 209–220 (2005)
3. Rye, H. S. et al. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97, 325–338 (1999)
4. Sigler, P. B. et al. Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem. 67, 581–608 (1998)
5. Horwich, A. L., Fenton, W. A., Chapman, E. & Farr, G. W. Two families of chaperonin: Physiology and mechanism. Annu. Rev. Cell Dev. Biol. 23, 115–145 (2007)
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