The hydrophobic effect characterises the thermodynamic signature of amyloid fibril growth

Thermodynamic Stability of Polar and Nonpolar Amyloid Fibrils

(2019) Farbod Mahmoudinobar et al.   Journal of Chemical Theory and Computation

The growth of amyloid fibrils: rates and mechanisms

(2019) Alexander K. Buell   BIOCHEMICAL JOURNAL

The characteristics of molten globule states and folding pathways strongly depend on the sequence of a protein

(2018) M.J.J. Dijkstra et al.   MOLECULAR PHYSICS

The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

(2018) Matthew G. Iadanza et al.   Nature Communications

AmyPro: a database of proteins with validated amyloidogenic regions

(2017) Mihaly Varadi et al.   NUCLEIC ACIDS RESEARCH

Interaction with prefibrillar species and amyloid-like fibrils changes the stiffness of lipid bilayers

(2017) Bruno C. Borro et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

Role of Water in the Selection of Stable Proteins at Ambient and Extreme Thermodynamic Conditions

(2017) Valentino Bianco et al.   Physical Review X

Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation

(2016) Arshdeep Sidhu et al.   ACS Chemical Neuroscience

Coarse-grained and All-atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

(2016) Mara Chiricotto et al.   ISRAEL JOURNAL OF CHEMISTRY

Insights into the variability of nucleated amyloid polymerization by a minimalistic model of stochastic protein assembly

(2016) Sarah Eugène et al.   JOURNAL OF CHEMICAL PHYSICS

Primary Fibril Nucleation of Aggregation Prone Tau Fragments PHF6 and PHF6*

(2016) Florent X. Smit et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Dynamics of Hydration Water around Native and Misfolded α-Lactalbumin

(2016) Z. F. Brotzakis et al.   JOURNAL OF PHYSICAL CHEMISTRY B

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

Physical determinants of the self-replication of protein fibrils

(2016) Anđela Šarić et al.   Nature Physics

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold Denaturation

(2016) Erik van Dijk et al.   PHYSICAL REVIEW LETTERS

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

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Computational Studies of Protein Aggregation: Methods and Applications

(2015) Alex Morriss-Andrews et al.   Annual Review of Physical Chemistry

Water Mediated Interactions and the Protein Folding Phase Diagram in the Temperature–Pressure Plane

(2015) Brian J. Sirovetz et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Competition between surface adsorption and folding of fibril-forming polypeptides

(2015) Ran Ni et al.   PHYSICAL REVIEW E

The Hydrophobic Temperature Dependence of Amino Acids Directly Calculated from Protein Structures

(2015) Erik van Dijk et al.   PLoS Computational Biology

Cold Denaturation of α-Synuclein Amyloid Fibrils

(2014) Tatsuya Ikenoue et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Surface Effects on Aggregation Kinetics of Amyloidogenic Peptides

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

A Simple Lattice Model That Captures Protein Folding, Aggregation and Amyloid Formation

(2014) Sanne Abeln et al.   PLoS One

β2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH

(2014) Sophia C. Goodchild et al.   PLoS One

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

Interplay between Folding and Assembly of Fibril-Forming Polypeptides

(2013) Ran Ni et al.   PHYSICAL REVIEW LETTERS

High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin

(2013) N. Vajpai et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Amino acid behavior in aqueous amide solutions: Temperature dependence of the l-phenylalanine–N,N-dimethylformamide interaction

(2013) Andrey V. Kustov   THERMOCHIMICA ACTA

Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth

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

Perturbation of the Stability of Amyloid Fibrils through Alteration of Electrostatic Interactions

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

Accounting for Protein-Solvent Contacts Facilitates Design of Nonaggregating Lattice Proteins

(2011) Sanne Abeln et al.   BIOPHYSICAL JOURNAL

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

(2011) Andrew J. Baldwin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The role of protonation in protein fibrillation

(2010) Martin D. Jeppesen et al.   FEBS LETTERS

Glucagon Fibril Polymorphism Reflects Differences in Protofilament Backbone Structure

(2010) Christian Beyschau Andersen et al.   JOURNAL OF MOLECULAR BIOLOGY

The Thermodynamic Stability of Amyloid Fibrils Studied by Differential Scanning Calorimetry

(2010) Bertrand Morel et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Surface Attachment of Protein Fibrils via Covalent Modification Strategies

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

The hydrophobic effect and its role in cold denaturation

(2009) Cristiano L. Dias et al.   CRYOBIOLOGY