Imaging Aβ(1–42) fibril elongation reveals strongly polarised growth and growth incompetent states

Dynamics of Seeded Aβ40-Fibril Growth from Atomistic Molecular Dynamics Simulations: Kinetic Trapping and Reduced Water Mobility in the Locking Step

(2016) Nadine Schwierz et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Molecular mechanisms of protein aggregation from global fitting of kinetic models

(2016) Georg Meisl et al.   Nature Protocols

Nanoscopic insights into seeding mechanisms and toxicity of α-synuclein species in neurons

(2016) Dorothea Pinotsi et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

High-speed atomic force microscopy reveals structural dynamics of amyloid β1–42aggregates

(2016) Takahiro Watanabe-Nakayama et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

(2016) Marielle Aulikki Wälti et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

A minimal conformational switching-dependent model for amyloid self-assembly

(2016) Srivastav Ranganathan et al.   Scientific Reports

Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes

(2015) Ellen Hubin et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Single Fibril Growth Kinetics of α-Synuclein

(2015) Michael M. Wördehoff et al.   JOURNAL OF MOLECULAR BIOLOGY

N-Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42

(2015) Olga Szczepankiewicz et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

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

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

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

Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation

(2015) Axel Abelein et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

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

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

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

Fibril Elongation by Aβ17–42: Kinetic Network Analysis of Hybrid-Resolution Molecular Dynamics Simulations

(2014) Wei Han 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

Solution conditions determine the relative importance of nucleation and growth processes in  -synuclein aggregation

(2014) A. K. Buell 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

Kinetic theory of amyloid fibril templating

(2013) Jeremy D. Schmit   JOURNAL OF CHEMICAL PHYSICS

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

(2013) Jae Sun Jeong et al.   JOURNAL OF MOLECULAR BIOLOGY

Polymorph-Specific Kinetics and Thermodynamics of β-Amyloid Fibril Growth

(2013) Wei Qiang et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Direct Observation of Heterogeneous Amyloid Fibril Growth Kinetics via Two-Color Super-Resolution Microscopy

(2013) Dorothea Pinotsi et al.   NANO LETTERS

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

Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth

(2012) Alexander K. Buell et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Role of Elongation and Secondary Pathways in S6 Amyloid Fibril Growth

(2012) Nikolai Lorenzen et al.   BIOPHYSICAL JOURNAL

From Macroscopic Measurements to Microscopic Mechanisms of Protein Aggregation

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

Inhibition of Amyloid Formation

(2012) Torleif Härd et al.   JOURNAL OF MOLECULAR BIOLOGY

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

(2012) Iryna Benilova et al.   NATURE NEUROSCIENCE

Purified and synthetic Alzheimer's amyloid beta (A ) prions

(2012) J. Stohr et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Template-Assisted Lateral Growth of Amyloid-β42 Fibrils Studied by Differential Labeling with Gold Nanoparticles

(2011) Muriel Arimon et al.   BIOCONJUGATE CHEMISTRY

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

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

The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate

(2011) C. Cabaleiro-Lago et al.   LANGMUIR

Nanomechanics of functional and pathological amyloid materials

(2011) Tuomas P. J. Knowles et al.   Nature Nanotechnology

Neurotoxicity of Alzheimer's disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio

(2010) Inna Kuperstein et al.   EMBO JOURNAL

Surface Attachment of Protein Fibrils via Covalent Modification Strategies

(2010) Alexander K. Buell et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Protein Aggregation in Crowded Environments

(2010) Duncan A. White et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Stop-and-go kinetics in amyloid fibrillation

(2010) Jesper Ferkinghoff-Borg et al.   PHYSICAL REVIEW E

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

(2009) Erik Hellstrand et al.   ACS Chemical Neuroscience

Branching in Amyloid Fibril Growth

(2009) Christian Beyschau Andersen et al.   BIOPHYSICAL JOURNAL

Thermodynamic Perspective on the Dock−Lock Growth Mechanism of Amyloid Fibrils

(2009) Edward P. O’Brien et al.   JOURNAL OF PHYSICAL CHEMISTRY B