Literature DB >> 21255721

How one bad protein spoils the barrel: structural details of β2-microglobulin amyloidogenicity.

Lila M Gierasch1.   

Abstract

In this issue, Eichner et al. (2011) describe at atomic resolution the structure of an amyloidogenic state of β(2)-microglobulin and how it may corrupt a soluble counterpart in the pathological scenario that ensues when good proteins go to the "dark side'" and form infectious toxic amyloid. Copyright Â
© 2011 Elsevier Inc. All rights reserved.

Entities:  

Year:  2011        PMID： 21255721      PMCID： PMC3049456          DOI： 10.1016/j.molcel.2011.01.003

Source DB:  PubMed          Journal:  Mol Cell        ISSN： 1097-2765            Impact factor:   17.970


  11 in total

Review 1.  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

2.  Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond.

Authors:  Atsushi Kameda; Masaru Hoshino; Takashi Higurashi; Satoshi Takahashi; Hironobu Naiki; Yuji Goto
Journal:  J Mol Biol       Date:  2005-04-29       Impact factor: 5.469

3.  Intermolecular alignment in β2-microglobulin amyloid fibrils.

Authors:  Galia T Debelouchina; Geoffrey W Platt; Marvin J Bayro; Sheena E Radford; Robert G Griffin
Journal:  J Am Chem Soc       Date:  2010-11-15       Impact factor: 15.419

4.  A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch.

Authors:  Timo Eichner; Sheena E Radford
Journal:  J Mol Biol       Date:  2009-03-13       Impact factor: 5.469

5.  Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils.

Authors:  V Bellotti; M Stoppini; P Mangione; M Sunde; C Robinson; L Asti; D Brancaccio; G Ferri
Journal:  Eur J Biochem       Date:  1998-11-15

6.  Metal binding sheds light on mechanisms of amyloid assembly.

Authors:  Matthew F Calabrese; Andrew D Miranker
Journal:  Prion       Date:  2009-01-28       Impact factor: 3.931

7.  An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.

Authors:  Matthias J Feige; Sandra Groscurth; Moritz Marcinowski; Yuichiro Shimizu; Horst Kessler; Linda M Hendershot; Johannes Buchner
Journal:  Mol Cell       Date:  2009-06-12       Impact factor: 17.970

8.  Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.

Authors:  G Esposito; R Michelutti; G Verdone; P Viglino; H Hernández; C V Robinson; A Amoresano; F Dal Piaz; M Monti; P Pucci; P Mangione; M Stoppini; G Merlini; G Ferri; V Bellotti
Journal:  Protein Sci       Date:  2000-05       Impact factor: 6.725

9.  Amyloid formation under physiological conditions proceeds via a native-like folding intermediate.

Authors:  Thomas R Jahn; Martin J Parker; Steve W Homans; Sheena E Radford
Journal:  Nat Struct Mol Biol       Date:  2006-02-19       Impact factor: 15.369

10.  Conformational conversion during amyloid formation at atomic resolution.

Authors:  Timo Eichner; Arnout P Kalverda; Gary S Thompson; Steve W Homans; Sheena E Radford
Journal:  Mol Cell       Date:  2011-01-21       Impact factor: 17.970
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