Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques

(2015) Thomas C. T. Michaels et al.   INTERNATIONAL JOURNAL OF MODERN PHYSICS B

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

(2015) Samuel I A Cohen et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

On the lag phase in amyloid fibril formation

(2015) Paolo Arosio et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

(2015) Samuel I A Cohen et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation

(2014) Cecilia Månsson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

(2014) Robert Vácha et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The amyloid state and its association with protein misfolding diseases

(2014) Tuomas P. J. Knowles et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Chemical kinetics for drug discovery to combat protein aggregation diseases

(2014) Paolo Arosio et al.   TRENDS IN PHARMACOLOGICAL SCIENCES

DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios

(2013) Cecilia Månsson et al.   CELL STRESS & CHAPERONES

Quantification of the Concentration of Aβ42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay

(2013) Paolo Arosio et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2

(2013) L.-Q. Xu et al.   PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES

Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

(2013) S. I. A. Cohen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Amyloid State of Proteins in Human Diseases

(2012) David Eisenberg et al.   CELL

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

(2012) I. W. Hamley   CHEMICAL REVIEWS

From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

(2012) Samuel I.A. Cohen et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers

(2012) B. Mannini et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Hydrophobicity and Conformational Change as Mechanistic Determinants for Nonspecific Modulators of Amyloid β Self-Assembly

(2011) Axel Abelein et al.   BIOCHEMISTRY

Binding of the Molecular Chaperone αB-Crystallin to Aβ Amyloid Fibrils Inhibits Fibril Elongation

(2011) Sarah L. Shammas et al.   BIOPHYSICAL JOURNAL

Nucleated polymerization with secondary pathways. II. Determination of self-consistent solutions to growth processes described by non-linear master equations

(2011) Samuel I. A. Cohen et al.   JOURNAL OF CHEMICAL PHYSICS

Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments

(2011) Samuel I. A. Cohen et al.   JOURNAL OF CHEMICAL PHYSICS

Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation

(2011) Stuart A. Sievers et al.   NATURE

Molecular chaperones in protein folding and proteostasis

(2011) F. Ulrich Hartl et al.   NATURE

Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation

(2010) Celia Cabaleiro-Lago et al.   ACS Chemical Neuroscience

Strategies for the Inhibition of Protein Aggregation in Human Diseases

(2010) Manuela Bartolini et al.   CHEMBIOCHEM

Studying the effects of chaperones on amyloid fibril formation

(2010) Hong Zhang et al.   METHODS

Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process

(2009) Erik Hellstrand et al.   ACS Chemical Neuroscience

The extracellular domain of Bri2 (ITM2B) binds the ABri peptide (1–23) and amyloid β-peptide (Aβ1–40): Implications for Bri2 effects on processing of amyloid precursor protein and Aβ aggregation

(2009) Siwei Peng et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide

(2009) Dominic M. Walsh et al.   FEBS Journal

An Analytical Solution to the Kinetics of Breakable Filament Assembly

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

Insights into the mechanism of prion propagation

(2008) Sarah Perrett et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation

(2008) Vito Foderà et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles

(2008) Celia Cabaleiro-Lago et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers

(2008) Dagmar E Ehrnhoefer et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE