An Efficient Kinetic Model for Assemblies of Amyloid Fibrils and Its Application to Polyglutamine Aggregation

Scaling limit of a discrete prion dynamics model

(2013) Marie Doumic et al.   Communications in Mathematical Sciences

Dynamics of polymerization shed light on the mechanisms that lead to multiple amyloid structures of the prion protein

(2011) Maria-Teresa Alvarez-Martinez et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent

(2011) Karunakar Kar et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

On the Calibration of a Size-Structured Population Model from Experimental Data

(2010) Marie Doumic et al.   ACTA BIOTHEORETICA

Model Discrimination and Mechanistic Interpretation of Kinetic Data in Protein Aggregation Studies

(2009) Joseph P. Bernacki et al.   BIOPHYSICAL JOURNAL

Numerical solution of an inverse problem in size-structured population dynamics

(2009) Marie Doumic et al.   INVERSE PROBLEMS

Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis

(2009) W.-F. Xue et al.   PROTEIN ENGINEERING DESIGN & SELECTION

An Analytical Solution to the Kinetics of Breakable Filament Assembly

(2009) T. P. J. Knowles et al.   SCIENCE

Size distribution dependence of prion aggregates infectivity

(2008) Vincent Calvez et al.   MATHEMATICAL BIOSCIENCES

Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly

(2008) Wei-Feng Xue et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core

(2008) C. Wasmer et al.   SCIENCE