Issue 1, 2013
From the journal:

Molecular BioSystems

Understanding protein aggregation from the view of monomer dynamics

Lisa J. Lapidus*a  

* Corresponding authors

a Department of Physics and Astronomy and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, USA
E-mail: lapidus@msu.edu

Abstract

Much work in recent years has been devoted to understanding the complex process of protein aggregation. This review looks at the earliest stages of aggregation, long before the formation of fibrils that are the hallmark of many aggregation-based diseases, and proposes that the first steps are controlled by the reconfiguration dynamics of the monomer. When reconfiguration is much faster or much slower than bimolecular diffusion, then aggregation is slow, but when they are similar, aggregation is fast. The experimental evidence for this model is reviewed and the prospects for small molecule aggregation inhibitors to prevent disease are discussed.

Graphical abstract: Understanding protein aggregation from the view of monomer dynamics

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Article information

DOI
https://doi.org/10.1039/C2MB25334H
Article type
Review Article
Submitted
15 Aug 2012
Accepted
08 Oct 2012
First published
09 Oct 2012

Mol. BioSyst., 2013,9, 29-35

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Understanding protein aggregation from the view of monomer dynamics

L. J. Lapidus, Mol. BioSyst., 2013, 9, 29 DOI: 10.1039/C2MB25334H

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