Literature DB >> 26445435

A Kinetic Model for Cell Damage Caused by Oligomer Formation.

Liu Hong1, Ya-Jing Huang2, Wen-An Yong2.   

Abstract

It is well known that the formation of amyloid fiber may cause invertible damage to cells, although the underlying mechanism has not been fully understood. In this article, a microscopic model considering the detailed processes of amyloid formation and cell damage is constructed based on four simple assumptions, one of which is that cell damage is raised by oligomers rather than mature fibrils. By taking the maximum entropy principle, this microscopic model in the form of infinite mass-action equations together with two reaction-convection partial differential equations (PDEs) has been greatly coarse-grained into a macroscopic system consisting of only five ordinary differential equations (ODEs). With this simple model, the effects of primary nucleation, elongation, fragmentation, and protein and seeds concentration on amyloid formation and cell damage have been extensively explored and compared with experiments. We hope that our results will provide new insights into the quantitative linkage between amyloid formation and cell damage.
Copyright © 2015 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Year:  2015        PMID: 26445435      PMCID: PMC4601094          DOI: 10.1016/j.bpj.2015.08.007

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  38 in total

1.  Modeling fibril fragmentation in real-time.

Authors:  Pengzhen Tan; Liu Hong
Journal:  J Chem Phys       Date:  2013-08-28       Impact factor: 3.488

2.  Simple moment-closure model for the self-assembly of breakable amyloid filaments.

Authors:  Liu Hong; Wen-An Yong
Journal:  Biophys J       Date:  2013-02-05       Impact factor: 4.033

3.  A kinetic study of amyloid formation: fibril growth and length distributions.

Authors:  John S Schreck; Jian-Min Yuan
Journal:  J Phys Chem B       Date:  2013-05-20       Impact factor: 2.991

Review 4.  Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity.

Authors:  Marcus Fändrich
Journal:  J Mol Biol       Date:  2012-01-12       Impact factor: 5.469

5.  Turn nucleation perturbs amyloid β self-assembly and cytotoxicity.

Authors:  Todd M Doran; Elizabeth A Anderson; Sarah E Latchney; Lisa A Opanashuk; Bradley L Nilsson
Journal:  J Mol Biol       Date:  2012-02-07       Impact factor: 5.469

6.  The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.

Authors:  Nikolai Lorenzen; Søren Bang Nielsen; Alexander K Buell; Jørn Døvling Kaspersen; Paolo Arosio; Brian Stougaard Vad; Wojciech Paslawski; Gunna Christiansen; Zuzana Valnickova-Hansen; Maria Andreasen; Jan J Enghild; Jan Skov Pedersen; Christopher M Dobson; Tuomas P J Knowles; Daniel Erik Otzen
Journal:  J Am Chem Soc       Date:  2014-02-28       Impact factor: 15.419

Review 7.  From macroscopic measurements to microscopic mechanisms of protein aggregation.

Authors:  Samuel I A Cohen; Michele Vendruscolo; Christopher M Dobson; Tuomas P J Knowles
Journal:  J Mol Biol       Date:  2012-03-08       Impact factor: 5.469

Review 8.  Membrane and surface interactions of Alzheimer's Aβ peptide--insights into the mechanism of cytotoxicity.

Authors:  Thomas L Williams; Louise C Serpell
Journal:  FEBS J       Date:  2011-07-26       Impact factor: 5.542

9.  Single-channel Ca(2+) imaging implicates Aβ1-42 amyloid pores in Alzheimer's disease pathology.

Authors:  Angelo Demuro; Martin Smith; Ian Parker
Journal:  J Cell Biol       Date:  2011-10-24       Impact factor: 10.539

10.  Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.

Authors:  Samuel I A Cohen; Sara Linse; Leila M Luheshi; Erik Hellstrand; Duncan A White; Luke Rajah; Daniel E Otzen; Michele Vendruscolo; Christopher M Dobson; Tuomas P J Knowles
Journal:  Proc Natl Acad Sci U S A       Date:  2013-05-23       Impact factor: 11.205

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