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Literature DB >> 14506295

Caging helps proteins fold.

D Thirumalai¹, Dmitri K Klimov, George H Lorimer.

Abstract

Mesh：

Year: 2003 PMID： 14506295 PMCID： PMC208732 DOI： 10.1073/pnas.2035072100

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

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19 in total

Review 1. Implications of macromolecular crowding for protein assembly.

Authors: A P Minton
Journal: Curr Opin Struct Biol Date: 2000-02 Impact factor: 6.809

Review 2. Macromolecular crowding: an important but neglected aspect of the intracellular environment.

Authors: R J Ellis
Journal: Curr Opin Struct Biol Date: 2001-02 Impact factor: 6.809

3. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.

Authors: M R Betancourt; D Thirumalai
Journal: J Mol Biol Date: 1999-04-02 Impact factor: 5.469

Review 4. Fast kinetics and mechanisms in protein folding.

Authors: W A Eaton; V Muñoz; S J Hagen; G S Jas; L J Lapidus; E R Henry; J Hofrichter
Journal: Annu Rev Biophys Biomol Struct Date: 2000

Review 5. Understanding protein folding via free-energy surfaces from theory and experiment.

Authors: A R Dinner; A Sali; L J Smith; C M Dobson; M Karplus
Journal: Trends Biochem Sci Date: 2000-07 Impact factor: 13.807

6. Stabilization of proteins in confined spaces.

Authors: H X Zhou; K A Dill
Journal: Biochemistry Date: 2001-09-25 Impact factor: 3.162

7. Global minimization of an off-lattice potential energy function using a chaperone-based refolding method.

Authors: D Gorse
Journal: Biopolymers Date: 2001-11 Impact factor: 2.505

Review 8. Protein folding theory: from lattice to all-atom models.

Authors: L Mirny; E Shakhnovich
Journal: Annu Rev Biophys Biomol Struct Date: 2001

Review 9. Chaperonin-mediated protein folding.

Authors: D Thirumalai; G H Lorimer
Journal: Annu Rev Biophys Biomol Struct Date: 2001

Review 10. Review: allostery in chaperonins.

Authors: A Horovitz; Y Fridmann; G Kafri; O Yifrach
Journal: J Struct Biol Date: 2001-08 Impact factor: 2.867

28 in total

1. Unfolding of Green Fluorescent Protein mut2 in wet nanoporous silica gels.

Authors: Barbara Campanini; Sara Bologna; Fabio Cannone; Giuseppe Chirico; Andrea Mozzarelli; Stefano Bettati
Journal: Protein Sci Date: 2005-03-31 Impact factor: 6.725

Review 2. 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

3. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.

Authors: Eli Chapman; George W Farr; Renata Usaite; Krystyna Furtak; Wayne A Fenton; Tapan K Chaudhuri; Elise R Hondorp; Rowena G Matthews; Sharon G Wolf; John R Yates; Marc Pypaert; Arthur L Horwich
Journal: Proc Natl Acad Sci U S A Date: 2006-10-16 Impact factor: 11.205

Caging helps proteins fold.

Review 1. Implications of macromolecular crowding for protein assembly.

Review 2. Macromolecular crowding: an important but neglected aspect of the intracellular environment.

3. Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity.

Review 4. Fast kinetics and mechanisms in protein folding.

Review 5. Understanding protein folding via free-energy surfaces from theory and experiment.

6. Stabilization of proteins in confined spaces.

7. Global minimization of an off-lattice potential energy function using a chaperone-based refolding method.

Review 8. Protein folding theory: from lattice to all-atom models.

Review 9. Chaperonin-mediated protein folding.

Review 10. Review: allostery in chaperonins.

1. Unfolding of Green Fluorescent Protein mut2 in wet nanoporous silica gels.

Review 2. GroEL-mediated protein folding: making the impossible, possible.

3. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.

4. Translocation boost protein-folding efficiency of double-barreled chaperonins.

5. GroEL stimulates protein folding through forced unfolding.

6. Thermodynamics and kinetics of protein folding under confinement.

7. Confinement effects on the kinetics and thermodynamics of protein dimerization.

8. Monte Carlo simulations of proteins in cages: influence of confinement on the stability of intermediate states.

9. Protein folding under confinement: a role for solvent.

10. Assisted peptide folding by surface pattern recognition.