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Literature DB >> 29472450

Race to the native state.

Robert B Best¹.

Abstract

Mesh：

Year: 2018 PMID： 29472450 PMCID： PMC5877981 DOI： 10.1073/pnas.1722622115

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

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21 in total

1. Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model.

Authors: D J Bicout; A Szabo
Journal: Protein Sci Date: 2000-03 Impact factor: 6.725

2. Structure of a serpin-protease complex shows inhibition by deformation.

Authors: J A Huntington; R J Read; R W Carrell
Journal: Nature Date: 2000-10-19 Impact factor: 49.962

3. Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase.

Authors: Paul Maragakis; Martin Karplus
Journal: J Mol Biol Date: 2005-09-30 Impact factor: 5.469

Review 4. Molecular gymnastics: serpin structure, folding and misfolding.

Authors: James C Whisstock; Stephen P Bottomley
Journal: Curr Opin Struct Biol Date: 2006-10-31 Impact factor: 6.809

Review 5. From Levinthal to pathways to funnels.

Authors: K A Dill; H S Chan
Journal: Nat Struct Biol Date: 1997-01

6. Serpin latency transition at atomic resolution.

Authors: Giorgia Cazzolli; Fang Wang; Silvio a Beccara; Anne Gershenson; Pietro Faccioli; Patrick L Wintrode
Journal: Proc Natl Acad Sci U S A Date: 2014-10-13 Impact factor: 11.205

Review 7. Proteins that switch folds.

Authors: Philip N Bryan; John Orban
Journal: Curr Opin Struct Biol Date: 2010-06-28 Impact factor: 6.809

Race to the native state.

1. Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model.

2. Structure of a serpin-protease complex shows inhibition by deformation.

3. Large amplitude conformational change in proteins explored with a plastic network model: adenylate kinase.

Review 4. Molecular gymnastics: serpin structure, folding and misfolding.

Review 5. From Levinthal to pathways to funnels.

6. Serpin latency transition at atomic resolution.

Review 7. Proteins that switch folds.

Review 8. Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.

9. Simple model of protein folding kinetics.

10. Structures of active and latent PAI-1: a possible stabilizing role for chloride ions.

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