Literature DB >> 17530168

On the structural definition of amyloid fibrils and other polypeptide aggregates.

M Fändrich1.   

Abstract

Amyloid fibrils occur inside the human body, associated with ageing or a group of diseases that includes, amongst others, Alzheimer's disease, atherosclerosis and type II diabetes. Many natural polypeptide chains are able to form amyloid fibrils in vivo or in vitro, and this ability has been suggested to represent an inherent consequence of the chemical structure of the polypeptide chain. Recent literature has provided a wealth of information about the structure of aggregates, precipitates, amyloid fibrils and other types of fibrillar polypeptide assemblies. However, the biophysical meaning associated with these terms can differ considerably depending on the context of their usage. This overview presents a structural comparison of amyloid fibrils and other types of polypeptide assemblies and defines amyloid fibrils, based on structural considerations, as fibrillar polypeptide aggregates with a cross-beta conformation.

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Year:  2007        PMID: 17530168     DOI: 10.1007/s00018-007-7110-2

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  64 in total

Review 1.  Polyglutamine misfolding in yeast: toxic and protective aggregation.

Authors:  Martin L Duennwald
Journal:  Prion       Date:  2011-10-01       Impact factor: 3.931

2.  An amyloid organelle, solid-state NMR evidence for cross-β assembly of gas vesicles.

Authors:  Marvin J Bayro; Eugenio Daviso; Marina Belenky; Robert G Griffin; Judith Herzfeld
Journal:  J Biol Chem       Date:  2011-12-06       Impact factor: 5.157

Review 3.  Nonhuman primate models of Alzheimer-like cerebral proteopathy.

Authors:  Eric Heuer; Rebecca F Rosen; Amarallys Cintron; Lary C Walker
Journal:  Curr Pharm Des       Date:  2012       Impact factor: 3.116

4.  Formation of dynamic soluble surfactant-induced amyloid β peptide aggregation intermediates.

Authors:  Axel Abelein; Jørn Døvling Kaspersen; Søren Bang Nielsen; Grethe Vestergaard Jensen; Gunna Christiansen; Jan Skov Pedersen; Jens Danielsson; Daniel E Otzen; Astrid Gräslund
Journal:  J Biol Chem       Date:  2013-06-17       Impact factor: 5.157

Review 5.  Misfolded proteins in Alzheimer's disease and type II diabetes.

Authors:  Alaina S DeToma; Samer Salamekh; Ayyalusamy Ramamoorthy; Mi Hee Lim
Journal:  Chem Soc Rev       Date:  2011-08-04       Impact factor: 54.564

6.  The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.

Authors:  Matthias J Feige; Sandra Groscurth; Moritz Marcinowski; Zu Thur Yew; Vincent Truffault; Emanuele Paci; Horst Kessler; Johannes Buchner
Journal:  Proc Natl Acad Sci U S A       Date:  2008-09-03       Impact factor: 11.205

Review 7.  Amyloid beta-protein assembly and Alzheimer disease.

Authors:  Robin Roychaudhuri; Mingfeng Yang; Minako M Hoshi; David B Teplow
Journal:  J Biol Chem       Date:  2008-10-09       Impact factor: 5.157

8.  Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures.

Authors:  Matthias Schmidt; Carsten Sachse; Walter Richter; Chen Xu; Marcus Fändrich; Nikolaus Grigorieff
Journal:  Proc Natl Acad Sci U S A       Date:  2009-10-20       Impact factor: 11.205

9.  Computational modeling of the relationship between amyloid and disease.

Authors:  Damien Hall; Herman Edskes
Journal:  Biophys Rev       Date:  2012-09

Review 10.  Lessons learned from protein aggregation: toward technological and biomedical applications.

Authors:  César L Avila; Silvina Chaves; Sergio B Socias; Esteban Vera-Pingitore; Florencia González-Lizárraga; Cecilia Vera; Diego Ploper; Rosana Chehín
Journal:  Biophys Rev       Date:  2017-09-13
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