Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22

Optical Structural Analysis of Individual α-Synuclein Oligomers

(2018) Juan A. Varela et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Secondary nucleation in amyloid formation

(2018) Mattias Törnquist et al.   CHEMICAL COMMUNICATIONS

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide

(2018) Samuel I. A. Cohen et al.   Nature Chemistry

A new era for understanding amyloid structures and disease

(2018) Matthew G. Iadanza et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils

(2017) Katie L. Stewart et al.   JOURNAL OF MOLECULAR BIOLOGY

From Aβ Filament to Fibril: Molecular Mechanism of Surface-Activated Secondary Nucleation from All-Atom MD Simulations

(2017) Nadine Schwierz et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Multistep Conformation Selection in Amyloid Assembly

(2017) Ming-Chien Hsieh et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Pathways of Amyloid-β Aggregation Depend on Oligomer Shape

(2017) Bogdan Barz et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes

(2017) Wei Qiang et al.   NATURE

Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers

(2017) Giuliana Fusco et al.   SCIENCE

Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers

(2017) Lydia M. Young et al.   Chemical Science

Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method

(2017) Francesco A. Aprile et al.   Science Advances

The Cellular Phase of Alzheimer’s Disease

(2016) Bart De Strooper et al.   CELL

Understanding Amyloid-β Oligomerization at the Molecular Level: The Role of the Fibril Surface

(2016) Bogdan Barz et al.   CHEMISTRY-A EUROPEAN JOURNAL

Exploring the aggregation free energy landscape of the amyloid-β protein (1–40)

(2016) Weihua Zheng et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry

(2015) Lydia M. Young et al.   ANALYST

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

(2015) Risto Cukalevski et al.   Chemical Science

Structural Conversion of Aβ17–42 Peptides from Disordered Oligomers to U-Shape Protofilaments via Multiple Kinetic Pathways

(2015) Mookyung Cheon et al.   PLoS Computational Biology

Mechanism of Amyloid-β Fibril Elongation

(2014) Thomas Gurry et al.   BIOCHEMISTRY

The physical properties of supramolecular peptide assemblies: from building block association to technological applications

(2014) Lihi Adler-Abramovich et al.   CHEMICAL SOCIETY REVIEWS

The amyloid state and its association with protein misfolding diseases

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

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 Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

(2013) Jun-Xia Lu et al.   CELL

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

(2013) Mathias Jucker et al.   NATURE

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

(2013) Claire J Sarell et al.   Prion

Quantitative analysis of the time course of Aβ oligomerization and subsequent growth steps using tetramethylrhodamine-labeled Aβ

(2013) Kanchan Garai et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

Covalent Cross-Linking within Supramolecular Peptide Structures

(2012) George W. Preston et al.   ANALYTICAL CHEMISTRY

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

Antiparallel  -sheet architecture in Iowa-mutant  -amyloid fibrils

(2012) W. Qiang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulations

(2012) Mookyung Cheon et al.   PROTEIN SCIENCE

Spontaneous Formation of Twisted Aβ16-22 Fibrils in Large-Scale Molecular-Dynamics Simulations

(2011) Mookyung Cheon et al.   BIOPHYSICAL JOURNAL

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

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

Probing aromatic, hydrophobic, and steric effects on the self-assembly of an amyloid-β fragment peptide

(2010) F. Timur Senguen et al.   Molecular BioSystems

Extending the PRIME model for protein aggregation to all 20 amino acids

(2010) Mookyung Cheon et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

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

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

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease

(2009) Summer L. Bernstein et al.   Nature Chemistry

Trifluoromethyldiazirine: an effective photo-induced cross-linking probe for exploring amyloid formation

(2008) David P. Smith et al.   CHEMICAL COMMUNICATIONS

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