Dynamics of polymerization shed light on the mechanisms that lead to multiple amyloid structures of the prion protein-Reference-Cited by-同舟云学术

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

Published:2011-10 Issue:10 Volume:1814 Page:1305-1317
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Alvarez-Martinez Maria-Teresa,Fontes Pascaline,Zomosa-Signoret Viviana,Arnaud Jacques-Damien,Hingant Erwan,Pujo-Menjouet Laurent,Liautard Jean-Pierre

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference69 articles.

1. Prions;Prusiner;Proc. Natl. Acad. Sci. U. S. A,1998

2. A kinetic model for amyloid formation in the prion diseases: importance of seeding;Come;Proc. Natl. Acad. Sci. U. S. A,1993

3. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?;Jarrett;Cell,1993

4. Analysis of protein aggregation kinetics;Ferrone;Methods Enzymol.,1999

5. Principles of protein–protein recognition;Chothia;Nature,1975

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4. Generalizing a mathematical model of prion aggregation allows strain coexistence and co-stability by including a novel misfolded species;Journal of Mathematical Biology;2018-08-16

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