Characterization of Oligomers of Heterogeneous Size as Precursors of Amyloid Fibril Nucleation of an SH3 Domain: An Experimental Kinetics Study

Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides

(2011) Andreas Vitalis et al.   BIOPHYSICAL CHEMISTRY

Salt-Induced Modulation of the Pathway of Amyloid Fibril Formation by the Mouse Prion Protein

(2010) Shweta Jain et al.   BIOCHEMISTRY

Environmental Conditions Affect the Kinetics of Nucleation of Amyloid Fibrils and Determine Their Morphology

(2010) Bertrand Morel et al.   BIOPHYSICAL JOURNAL

A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state

(2009) Lorena Varela et al.   FEBS LETTERS

Lumry−Eyring Nucleated-Polymerization Model of Protein Aggregation Kinetics. 2. Competing Growth via Condensation and Chain Polymerization

(2009) Yi Li et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Protein aggregation kinetics, mechanism, and curve-fitting: A review of the literature

(2008) Aimee M. Morris et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Direct characterization of amyloidogenic oligomers by single-molecule fluorescence

(2008) A. Orte et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA