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19 in total

1. Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.

Authors: A I Jewett; A Baumketner; J-E Shea
Journal: Proc Natl Acad Sci U S A Date: 2004-08-26 Impact factor: 11.205

2. Archaeal-like chaperonins in bacteria.

Authors: Stephen M Techtmann; Frank T Robb
Journal: Proc Natl Acad Sci U S A Date: 2010-11-05 Impact factor: 11.205

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

To fold or not to fold....

1. Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway.

2. Archaeal-like chaperonins in bacteria.

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. Do chaperonins boost protein yields by accelerating folding or preventing aggregation?

Review 7. Reconciling theories of chaperonin accelerated folding with experimental evidence.

Review 8. Hsp70--a multi-gene, multi-structure, multi-function family with potential clinical applications.

9. Engineering an enzyme to resist boiling.

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