Polymorphic Triple β-Sheet Structures Contribute to Amide Hydrogen/Deuterium (H/D) Exchange Protection in the Alzheimer Amyloid β42 Peptide

Mutations Alter the Geometry and Mechanical Properties of Alzheimer’s Aβ(1−40) Amyloid Fibrils

(2010) Raffaella Paparcone et al.   BIOCHEMISTRY

Association Thermodynamics and Conformational Stability of β-Sheet Amyloid β(17-42) Oligomers: Effects of E22Q (Dutch) Mutation and Charge Neutralization

(2010) Nikolay Blinov et al.   BIOPHYSICAL JOURNAL

Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape

(2010) Yifat Miller et al.   CHEMICAL REVIEWS

Molecular Structure of Amyloid Fibrils Formed by Residues 127 to 147 of the Human Prion Protein

(2010) Ni-Shian Lin et al.   CHEMISTRY-A EUROPEAN JOURNAL

Polymorphic C-terminal β-Sheet Interactions Determine the Formation of Fibril or Amyloid β-derived Diffusible Ligand-like Globulomer for the Alzheimer Aβ42 Dodecamer

(2010) Buyong Ma 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

Kinetic Intermediates of β2-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis

(2010) Tsuyoshi Konuma 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

Hollow core of Alzheimer's A 42 amyloid observed by cryoEM is relevant at physiological pH

(2010) Y. Miller et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds

(2010) Yang Shen et al.   PROTEIN SCIENCE

Structural Characterization of a Soluble Amyloid β-Peptide Oligomer

(2009) Liping Yu et al.   BIOCHEMISTRY

Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid Fibrils

(2009) Robert Tycko et al.   BIOCHEMISTRY

Determination of the Oligomer Size of Amyloidogenic Protein β-Amyloid(1–40) by Single-Molecule Spectroscopy

(2009) Hao Ding et al.   BIOPHYSICAL JOURNAL

Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid β but Do Not Seed Fibril Formation

(2009) Jessica W. Wu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Molecular mechanisms for protein-encoded inheritance

(2009) Jed J W Wiltzius et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Interprotofilament interactions between Alzheimer's A 1-42 peptides in amyloid fibrils revealed by cryoEM

(2009) R. Zhang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Comparison of Alzheimer A (1-40) and A (1-42) amyloid fibrils reveals similar protofilament structures

(2009) M. Schmidt et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Seeded growth of  -amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure

(2009) A. K. Paravastu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Amyloid fibril dynamics revealed by combined hydrogen/deuterium exchange and nuclear magnetic resonance

(2008) Anders Olofsson et al.   ANALYTICAL BIOCHEMISTRY

Cognitive-Performance Recovery of Alzheimer's Disease Model Mice by Modulation of Early Soluble Amyloidal Assemblies

(2008) Anat Frydman-Marom et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Aβ-globulomers are formed independently of the fibril pathway

(2008) Gerald P. Gellermann et al.   NEUROBIOLOGY OF DISEASE

Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation

(2008) Wolfgang Hoyer et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant

(2002) Francesca Massi et al.   PROTEIN SCIENCE