Molecular Chaperones: Opening and closing the Anfinsen cage

Current Biology

Volumn 4, Issue 7, 1994, Pages 633-635

  John Ellis, R ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; T4 GENE 31 PROTEIN; VIRUS PROTEIN;

BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; MACROMOLECULE; PHYSIOLOGY; PROTEIN CONFORMATION; PROTEIN FOLDING; REVIEW;

ADENOSINE TRIPHOSPHATE; CHAPERONIN 10; CHAPERONIN 60; CHAPERONINS; MACROMOLECULAR SYSTEMS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; VIRAL PROTEINS;

EID: 0028465426     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00140-8     Document Type: Article

References (21)

1. ATP induces large quaternary rearrangements in a cage-like chaperonin structure
2. Principles that govern the folding of polypeptide chains
3. Roles of molecular chaperones in protein folding
4. Molecular chaperones in protein folding: the art of avoiding sticky situations
5. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
6. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL
7. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
8. Proper and improper folding of proteins in the cellular environment
9. Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
10. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle; implications for the mechanism of assisted protein folding
11. Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin
12. Protein synthesis in chloroplasts: IX Assembly of newly synthesised large subunits of ribulose bisphosphate carboxylase in isolated intact pea chloroplasts
13. A newly synthesized protein interacts with GroES on the surface of chaperonin GroEL
14. Co-operativity in ATP hydrolysis by GroEL is increased by GroES
15. Chaperonin-mediated protein folding at the surface of groEl through a ‘molten globule’ intermediate
16. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding
17. One member of a GroESL-like chaperonin multigene family in Bradyrhizobium japonicum is co-regulated with symbiotic nitrogen fixation genes
18. Molecular chaperones: the plant connection
19. Purification and Properties of Ribulosebisphosphate Carboxylase Large Subunit Binding Protein
20. Identification, characterisation and DNA sequence of a functional ‘double’ GroES-like chaperonin from chloroplasts of higher plants
21. How chaperonins monitor their protein charges