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Literature DB >> 7953542

Molecular chaperones. Opening and closing the Anfinsen cage.

Abstract

Dynamic interactions between chaperonins allow newly synthesized polypeptides to begin correct folding inside a transiently closed cage. Specialized chaperonins may be used to deal with recalcitrant proteins.

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Year: 1994 PMID： 7953542 DOI： 10.1016/s0960-9822(00)00140-8

Source DB: PubMed Journal: Curr Biol ISSN： 0960-9822 Impact factor: 10.834

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Cited

18 in total

1. Expansion and compression of a protein folding intermediate by GroEL.

Authors: Zong Lin; Hays S Rye
Journal: Mol Cell Date: 2004-10-08 Impact factor: 17.970

2. Chaperone-assisted protein folding: the path to discovery from a personal perspective.

Authors: F Ulrich Hartl
Journal: Nat Med Date: 2011-10-11 Impact factor: 53.440

Review 3. GroEL-mediated protein folding: making the impossible, possible.

Authors: Zong Lin; Hays S Rye
Journal: Crit Rev Biochem Mol Biol Date: 2006 Jul-Aug Impact factor: 8.250

Review 4. Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

Authors: Vijay M Krishnamurthy; George K Kaufman; Adam R Urbach; Irina Gitlin; Katherine L Gudiksen; Douglas B Weibel; George M Whitesides
Journal: Chem Rev Date: 2008-03 Impact factor: 60.622

10. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.

Authors: M K Hayer-Hartl; F Weber; F U Hartl
Journal: EMBO J Date: 1996-11-15 Impact factor: 11.598

Molecular chaperones. Opening and closing the Anfinsen cage.

1. Expansion and compression of a protein folding intermediate by GroEL.

2. Chaperone-assisted protein folding: the path to discovery from a personal perspective.

Review 3. GroEL-mediated protein folding: making the impossible, possible.

Review 4. Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

5. GroEL stimulates protein folding through forced unfolding.

6. In silico chaperonin-like cycle helps folding of proteins for structure prediction.

Review 7. Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.

8. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.

9. SurA assists the folding of Escherichia coli outer membrane proteins.

10. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis.