The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation

(2014) Kenjiro Ono et al.   BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

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

Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation

(2014) Anna Assarsson et al.   LANGMUIR

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

(2014) Georg Meisl et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Molecular Structures of Amyloid and Prion Fibrils: Consensus versus Controversy

(2013) Robert Tycko et al.   ACCOUNTS OF CHEMICAL RESEARCH

Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils

(2013) Lei Gu et al.   JOURNAL OF NEUROCHEMISTRY

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

Assessing the causes and consequences of co-polymerization in amyloid formation

(2013) Claire J Sarell et al.   Prion

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

Role of Aromatic Side Chains in Amyloid β-Protein Aggregation

(2012) Risto Cukalevski et al.   ACS Chemical Neuroscience

Alzheimer's disease and Down's syndrome: Treating two paths to dementia

(2012) Marc E. Weksler et al.   AUTOIMMUNITY REVIEWS

The Amyloid State of Proteins in Human Diseases

(2012) David Eisenberg et al.   CELL

From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

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

Cross-seeding effects of amyloid β-protein and α-synuclein

(2012) Kenjiro Ono et al.   JOURNAL OF NEUROCHEMISTRY

Dissociation between the Processivity and Total Activity of γ-Secretase: Implications for the Mechanism of Alzheimer's Disease-Causing Presenilin Mutations

(2011) Omar Quintero-Monzon et al.   BIOCHEMISTRY

Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40Ratios in Alzheimer Disease

(2011) Kris Pauwels et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular Basis for Transmission Barrier and Interference between Closely Related Prion Proteins in Yeast

(2011) Evgenia G. Afanasieva et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A New Structural Model of Aβ40Fibrils

(2011) Ivano Bertini et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Monte Carlo simulations of protein amyloid formation reveal origin of sigmoidal aggregation kinetics

(2011) Björn Linse et al.   Molecular BioSystems

Interaction between Amyloid Beta Peptide and an Aggregation Blocker Peptide Mimicking Islet Amyloid Polypeptide

(2011) Nasrollah Rezaei-Ghaleh et al.   PLoS One

Molecular basis for amyloid-  polymorphism

(2011) J.-P. Colletier et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

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

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

(2010) Matthew Biancalana et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Aβ42 Neurotoxicity Is Mediated by Ongoing Nucleated Polymerization Process Rather than by Discrete Aβ42 Species

(2010) Asad Jan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Role of Protein Sequence and Amino Acid Composition in Amyloid Formation: Scrambling and Backward Reading of IAPP Amyloid Fibrils

(2010) Raimon Sabaté et al.   JOURNAL OF MOLECULAR BIOLOGY

Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils

(2010) Mahiuddin Ahmed et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process

(2010) Bart De Strooper   PHYSIOLOGICAL REVIEWS

Identifying the amylome, proteins capable of forming amyloid-like fibrils

(2010) Lukasz Goldschmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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 chemistry of Alzheimer’s disease

(2009) Arvi Rauk   CHEMICAL SOCIETY REVIEWS

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

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

The Recombinant Amyloid-β Peptide Aβ1–42 Aggregates Faster and Is More Neurotoxic than Synthetic Aβ1–42

(2009) Verena H. Finder et al.   JOURNAL OF MOLECULAR BIOLOGY

The Ratio of Monomeric to Aggregated Forms of Aβ40 and Aβ42 Is an Important Determinant of Amyloid-β Aggregation, Fibrillogenesis, and Toxicity

(2008) Asad Jan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Amyloid-  Peptide (A ) Neurotoxicity Is Modulated by the Rate of Peptide Aggregation: A  Dimers and Trimers Correlate with Neurotoxicity

(2008) L. W. Hung et al.   JOURNAL OF NEUROSCIENCE

Molecular structural basis for polymorphism in Alzheimer's  -amyloid fibrils

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