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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.

SUBMITTER: Hingant E

PROVIDER: S-EPMC4125056 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation.

Hingant Erwan E Fontes Pascaline P Alvarez-Martinez Maria Teresa MT Arnaud Jacques-Damien JD Liautard Jean-Pierre JP Pujo-Menjouet Laurent L

PLoS computational biology 20140807 8

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 ...[more]

PMID: 25101755

Similar Datasets

Hingant2014 - Micellar On-Pathway Intermediate in Prion Amyloid Formation

Project description:Hingant2014 - Micellar On-Pathway Intermediate in Prion Amyloid Formation Hingant2014 - Micellar On-Pathway Intermediate in Prion Amyloid Formation Encoded non-curated model. Issues: - Missing kinetic parameters This model is described in the article: A micellar on-pathway intermediate step explains the kinetics of prion amyloid formation. Hingant E, Fontes P, Alvarez-Martinez MT, Arnaud JD, Liautard JP, Pujo-Menjouet L. PLoS Comput. Biol. 2014 Aug; 10(8): e1003735 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. This model is hosted on BioModels Database and identified by: MODEL1409230001. To cite BioModels Database, please use: BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

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