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

7Citations
Citations of this article
16Readers
Mendeley users who have this article in their library.

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.

Cite

CITATION STYLE

APA

Hingant, E., Fontes, P., Alvarez-Martinez, M. T., Arnaud, J. D., Liautard, J. P., & Pujo-Menjouet, L. (2014). A Micellar On-Pathway Intermediate Step Explains the Kinetics of Prion Amyloid Formation. PLoS Computational Biology, 10(8). https://doi.org/10.1371/journal.pcbi.1003735

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free