PMID: 9162143Jan 1, 1995Paper

Revisiting the Anfinsen cage

Folding & Design
R J Ellis

Abstract

In the past five years, ideas about protein folding inside cells have changed as a results of experiments with the chaperonin family of molecular chaperones. The folding of at least some proteins is no longer regarded as a spontaneous energy-independent process, but as involving transient interactions with chaperonin ATPases that serve to increase the efficiency of correct folding within the highly crowded intracellular environment. This review discusses in an historical context one model for how the chaperonins function. This model suggests that proteins fold inside cells in the same way as they do in pure dilute solution, but that they do so inside macromolecular Anfinsen cages that serve as sequestration devices to prevent and reverse unproductive interactions.

References

Jul 4, 1991·Nature·T E Creighton
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Nov 4, 1991·FEBS Letters·T E Gray, A R Fersht
Aug 1, 1989·Trends in Biochemical Sciences·R J Ellis, S M Hemmingsen
Jul 20, 1973·Science·C B Anfinsen
Nov 7, 1995·Biochemistry·L S ItzhakiA R Fersht
Oct 13, 1995·The Journal of Biological Chemistry·G TianN J Cowan
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Jul 1, 1994·Current Biology : CB·R J Ellis
May 1, 1993·Current Biology : CB·H R SaibilR J Ellis
Jul 17, 2010·Genes & Development·Ulrich RassStephen C West

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Citations

Jan 1, 1997·Folding & Design·J E CoyleS E Radford
Jan 7, 1997·Proceedings of the National Academy of Sciences of the United States of America·G M Clore, A M Gronenborn
May 27, 1997·Proceedings of the National Academy of Sciences of the United States of America·C Frieden, A C Clark

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