Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway

Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

(2016) Julien Roche et al.   BIOCHEMISTRY

Solvent Removal Induces a Reversible β-to-α Switch in Oligomeric Aβ Peptide

(2016) Senthil T. Kumar et al.   JOURNAL OF MOLECULAR BIOLOGY

C-Terminal Threonine Reduces Aβ 43 Amyloidogenicity Compared with Aβ 42

(2016) Saketh Chemuru et al.   JOURNAL OF MOLECULAR BIOLOGY

Huntingtin exon 1 fibrils feature an interdigitated β-hairpin–based polyglutamine core

(2016) Cody L. Hoop et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Folding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer

(2016) Bankanidhi Sahoo et al.   PLoS One

Huntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues

(2015) James R. Arndt et al.   BIOCHEMISTRY

Assembly of Aβ Proceeds via Monomeric Nuclei

(2015) Frank A. Ferrone   JOURNAL OF MOLECULAR BIOLOGY

Successive Stages of Amyloid-β Self-Assembly Characterized by Solid-State Nuclear Magnetic Resonance with Dynamic Nuclear Polarization

(2015) Alexey Potapov et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Targeting protein aggregation for the treatment of degenerative diseases

(2015) Yvonne S. Eisele et al.   NATURE REVIEWS DRUG DISCOVERY

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

Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy

(2015) András Micsonai et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

Aggregation Behavior of Chemically Synthesized, Full-Length Huntingtin Exon1

(2014) Bankanidhi Sahoo et al.   BIOCHEMISTRY

Role of the Coiled-Coil Structural Motif in Polyglutamine Aggregation

(2014) Bashkim Kokona et al.   BIOCHEMISTRY

Polyglutamine Amyloid Core Boundaries and Flanking Domain Dynamics in Huntingtin Fragment Fibrils Determined by Solid-State Nuclear Magnetic Resonance

(2014) Cody L. Hoop et al.   BIOCHEMISTRY

Dynamical Phase Transitions Reveal Amyloid-like States on Protein Folding Landscapes

(2014) Jeffrey K. Weber et al.   BIOPHYSICAL JOURNAL

Biophysical Underpinnings of the Repeat Length Dependence of Polyglutamine Amyloid Formation

(2014) Elizabeth Landrum et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular Interaction between the Chaperone Hsc70 and the N-terminal Flank of Huntingtin Exon 1 Modulates Aggregation

(2014) Elodie Monsellier et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A serendipitous survey of prediction algorithms for amyloidogenicity

(2013) Bartholomew P. Roland et al.   BIOPOLYMERS

Kinetically Competing Huntingtin Aggregation Pathways Control Amyloid Polymorphism and Properties

(2012) Murali Jayaraman et al.   BIOCHEMISTRY

Aβ Toxicity in Alzheimer's Disease

(2012) Virve Cavallucci et al.   MOLECULAR NEUROBIOLOGY

Bacterial Inclusion Bodies of Alzheimer's Disease β-Amyloid Peptides Can Be Employed To Study Native-Like Aggregation Intermediate States

(2011) Muralidhar Dasari et al.   CHEMBIOCHEM

Inhibiting the Nucleation of Amyloid Structure in a Huntingtin Fragment by Targeting α-Helix-Rich Oligomeric Intermediates

(2011) Rakesh Mishra et al.   JOURNAL OF MOLECULAR BIOLOGY

Slow Amyloid Nucleation via α-Helix-Rich Oligomeric Intermediates in Short Polyglutamine-Containing Huntingtin Fragments

(2011) Murali Jayaraman et al.   JOURNAL OF MOLECULAR BIOLOGY

Amyloid-β forms fibrils by nucleated conformational conversion of oligomers

(2011) Jiyong Lee et al.   Nature Chemical Biology

Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent

(2011) Karunakar Kar et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Natural tri- to hexapeptides self-assemble in water to amyloid  -type fiber aggregates by unexpected  -helical intermediate structures

(2011) C. A. E. Hauser et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Biophysical Characterization of Aβ42 C-Terminal Fragments: Inhibitors of Aβ42 Neurotoxicity

(2010) Huiyuan Li et al.   BIOCHEMISTRY

Aβ(1–40) Forms Five Distinct Amyloid Structures whose β-Sheet Contents and Fibril Stabilities Are Correlated

(2010) Ravindra Kodali et al.   JOURNAL OF MOLECULAR BIOLOGY

Distinct Structures of Scrapie Prion Protein (PrPSc)-seededVersusSpontaneous Recombinant Prion Protein Fibrils Revealed by Hydrogen/Deuterium Exchange

(2009) Vytautas Smirnovas et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Modulation of Polyglutamine Conformations and Dimer Formation by the N-Terminus of Huntingtin

(2009) Tim E. Williamson et al.   JOURNAL OF MOLECULAR BIOLOGY

Conversion of Aβ42 into a Folded Soluble Native-like Protein using a Semi-random Library of Amphipathic Helices

(2009) Pharhad Eli Arslan et al.   JOURNAL OF MOLECULAR BIOLOGY

Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism

(2009) Ashwani K Thakur et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides

(2009) A. Abedini et al.   PROTEIN ENGINEERING DESIGN & SELECTION

An Analytical Solution to the Kinetics of Breakable Filament Assembly

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

C-terminal peptides coassemble into A 42 oligomers and protect neurons against A 42-induced neurotoxicity

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

On the nucleation of amyloid β-protein monomer folding

(2005) Noel D. Lazo et al.   PROTEIN SCIENCE