Skip to Main content Skip to Navigation
Journal articles

A Micellar On-Pathway Intermediate Step Explains the Kinetics of Prion Amyloid Formation

Abstract : In a previous work by Alvarez-Martinez et al. (2011), the authors pointed out some fallacies in the mainstream interpretation of the prion amyloid formation. It appeared necessary to propose an original hypothesis able to reconcile the in vitro data with the predictions of a mathematical model describing the problem. Here, a model is developed accordingly with the hypothesis that an intermediate on-pathway leads to the conformation of the prion protein into an amyloid competent isoform thanks to a structure, called micelles, formed from hydrodynamic interaction. The authors also compare data to the prediction of their model and propose a new hypothesis for the formation of infectious prion amyloids.
Document type :
Journal articles
Complete list of metadata

Cited literature [27 references]  Display  Hide  Download
Contributor : Laurent Pujo-Menjouet <>
Submitted on : Friday, March 13, 2020 - 10:54:17 AM
Last modification on : Friday, March 12, 2021 - 2:10:02 PM
Long-term archiving on: : Sunday, June 14, 2020 - 1:41:13 PM


MT_AM-2014 PLOS Computational ...
Publisher files allowed on an open archive


Distributed under a Creative Commons Attribution 4.0 International License



Erwan Hingant, Pascaline Fontes, Maria-Teresa Alvarez-Martinez, Jacques-Damien Arnaud, Jean-Pierre Liautard, et al.. A Micellar On-Pathway Intermediate Step Explains the Kinetics of Prion Amyloid Formation. PLoS Computational Biology, Public Library of Science, 2014, 10 (8), pp.e1003735. ⟨10.1371/journal.pcbi.1003735⟩. ⟨hal-01104265⟩



Record views


Files downloads