N-terminal Prion Protein Peptides (PrP(120–144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways

Neurodegenerative Diseases: Expanding the Prion Concept

(2015) Lary C. Walker et al.   Annual Review of Neuroscience

Effects of Hydrophobic Macromolecular Crowders on Amyloid β (16–22) Aggregation

(2015) David C. Latshaw et al.   BIOPHYSICAL JOURNAL

Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases

(2015) Prajwal Ciryam et al.   TRENDS IN PHARMACOLOGICAL SCIENCES

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

Parallel In-register Intermolecular β-Sheet Architectures for Prion-seeded Prion Protein (PrP) Amyloids

(2014) Bradley R. Groveman et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Effects of Macromolecular Crowding on Amyloid Beta (16–22) Aggregation Using Coarse-Grained Simulations

(2014) David C. Latshaw et al.   JOURNAL OF PHYSICAL CHEMISTRY B

How do amino acid substitutions affect the amyloidogenic properties and seeding efficiency of prion peptides

(2013) Chi-Chen Chuang et al.   AMINO ACIDS

Nucleation Process of a Fibril Precursor in the C-Terminal Segment of Amyloid-β

(2013) Fahimeh Baftizadeh et al.   PHYSICAL REVIEW LETTERS

Amyloid Core Formed of Full-Length Recombinant Mouse Prion Protein Involves Sequence 127–143 but Not Sequence 107–126

(2013) Biswanath Chatterjee et al.   PLoS One

Conserved amyloid core structure of stop mutants of the human prion protein

(2013) Markus Zweckstetter   Prion

Burial of the Polymorphic Residue 129 in Amyloid Fibrils of Prion Stop Mutants

(2012) Lukasz Skora et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Protein Aggregation: Kinetics versus Thermodynamics

(2012) Piero Ricchiuto et al.   JOURNAL OF PHYSICAL CHEMISTRY B

In Situ Molecular-Level Insights into the Interfacial Structure Changes of Membrane-Associated Prion Protein Fragment [118–135] Investigated by Sum Frequency Generation Vibrational Spectroscopy

(2012) Hongchun Li et al.   LANGMUIR

Determination of amyloid core structure using chemical shifts

(2012) Lukasz Skora et al.   PROTEIN SCIENCE

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

(2012) Mookyung Cheon et al.   PROTEIN SCIENCE

Atomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion Disease

(2011) Marcin I. Apostol et al.   BIOCHEMISTRY

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

(2011) Mookyung Cheon et al.   BIOPHYSICAL JOURNAL

Structural Polymorphism in Amyloids

(2011) Eric M. Jones et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Fibrillization Propensity for Short Designed Hexapeptides Predicted by Computer Simulation

(2011) Victoria A. Wagoner et al.   JOURNAL OF MOLECULAR BIOLOGY

A Multistage Pathway for Human Prion Protein Aggregation in Vitro: From Multimeric Seeds to β-Oligomers and Nonfibrillar Structures

(2011) Kang R. Cho et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy

(2011) Jonathan J. Helmus et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

(2011) Vytautas Smirnovas et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

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

Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease

(2010) Marcin I. Apostol et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Energy Matrix of Structurally Important Side-Chain/Side-Chain Interactions in Proteins

(2010) Karel Berka et al.   Journal of Chemical Theory and Computation

Conformational Flexibility of Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State Nuclear Magnetic Resonance Spectroscopy

(2010) Jonathan J. Helmus et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

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

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

Conformational Plasticity of the Gerstmann–Sträussler–Scheinker Disease Peptide as Indicated by Its Multiple Aggregation Pathways

(2008) Antonino Natalello et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils

(2008) J. J. Helmus et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Amyloid Fibrils of the HET-s(218-289) Prion Form a   Solenoid with a Triangular Hydrophobic Core

(2008) C. Wasmer et al.   SCIENCE