Literature DB >> 15036202

Principles of protein folding, misfolding and aggregation.

Christopher M Dobson1.   

Abstract

This review summarises our current understanding of the underlying and universal mechanism by which newly synthesised proteins achieve their biologically functional states. Protein molecules, however, all have a finite tendency either to misfold, or to fail to maintain their correctly folded states, under some circumstances. This article describes some of the consequences of such behaviour, particularly in the context of the aggregation events that are frequently associated with aberrant folding. It focuses in particular on the emerging links between protein aggregation and the increasingly prevalent forms of debilitating disease with which it is now known to be associated.

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Year:  2004        PMID: 15036202     DOI: 10.1016/j.semcdb.2003.12.008

Source DB:  PubMed          Journal:  Semin Cell Dev Biol        ISSN: 1084-9521            Impact factor:   7.727


  216 in total

1.  A missense LAMB2 mutation causes congenital nephrotic syndrome by impairing laminin secretion.

Authors:  Ying Maggie Chen; Yamato Kikkawa; Jeffrey H Miner
Journal:  J Am Soc Nephrol       Date:  2011-04-21       Impact factor: 10.121

2.  Protein folding is mechanistically robust.

Authors:  Jeffrey K Weber; Vijay S Pande
Journal:  Biophys J       Date:  2012-02-21       Impact factor: 4.033

3.  Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.

Authors:  Richard J Nowak; Gregory D Cuny; Sungwoon Choi; Peter T Lansbury; Soumya S Ray
Journal:  J Med Chem       Date:  2010-04-08       Impact factor: 7.446

4.  A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response.

Authors:  Jonathon N Winnay; Jeremie Boucher; Marcelo A Mori; Kohjiro Ueki; C Ronald Kahn
Journal:  Nat Med       Date:  2010-03-28       Impact factor: 53.440

5.  Tracking the heterogeneous distribution of amyloid spherulites and their population balance with free fibrils.

Authors:  V Foderà; A M Donald
Journal:  Eur Phys J E Soft Matter       Date:  2010-11-04       Impact factor: 1.890

6.  Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle.

Authors:  Jose H Pereira; Corie Y Ralston; Nicholai R Douglas; Daniel Meyer; Kelly M Knee; Daniel R Goulet; Jonathan A King; Judith Frydman; Paul D Adams
Journal:  J Biol Chem       Date:  2010-06-23       Impact factor: 5.157

Review 7.  Aggregate reactivation mediated by the Hsp100 chaperones.

Authors:  Michal Zolkiewski; Ting Zhang; Maria Nagy
Journal:  Arch Biochem Biophys       Date:  2012-01-28       Impact factor: 4.013

Review 8.  Nanoimaging for prion related diseases.

Authors:  Alexey V Krasnoslobodtsev; Alexander M Portillo; Tanja Deckert-Gaudig; Volker Deckert; Yuri L Lyubchenko
Journal:  Prion       Date:  2010-10-23       Impact factor: 3.931

9.  Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme.

Authors:  Oxana V Polyakova; Olivier Roitel; Regina A Asryants; Alexei A Poliakov; Guy Branlant; Vladimir I Muronetz
Journal:  Protein Sci       Date:  2005-03-01       Impact factor: 6.725

10.  Effect of Grafting on Aggregation of Intrinsically Disordered Proteins.

Authors:  Dino Osmanovic; Yitzhak Rabin
Journal:  Biophys J       Date:  2018-01-31       Impact factor: 4.033

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