Molecular chaperones: Inside and outside the Anfinsen cage

Current Biology

Volumn 11, Issue 24, 2001, Pages

  Ellis, R John ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0035846548     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00620-0     Document Type: Review

References (23)

1. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
2. Unfolding protein folding
3. Revisiting the Anfinsen cage
4. Heat shock proteins and protein folding
5. Physical principles in the construction of regular viruses
6. Principles that govern the folding of protein chains
7. Dual function of protein confinement in chaperonin-assisted protein folding
8. GroEL/GroES-mediated folding of a protein too large to be encapsulated
9. Folding of newly translated proteins in vivo: The role of molecular chaperones
10. Principles of protein folding in the cellular environment
11. The effect of macromolecular crowding on chaperonin-mediated protein folding
12. Macromolecular crowding: Obvious but underappreciated
13. Folding in vivo of bacterial cytoplasmic proteins
14. From Levinthal to pathways to funnels
15. Chaperonin-mediated protein folding
16. Molecular chaperones: Pathways and networks
17. Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
18. Towards a mechanism for GroEl-GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
19. Chaperonin function: Folding by forced unfolding
20. Folding of malate dehydrogenase inside the GroEL-GroES cavity
21. Macromolecular crowding perturbs protein refolding kinetics: Implications for protein folding inside the cell
22. Confinement as a determinant of macromolecular structure and reactivity
23. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirements for hsp60 and hsp10