Heterogeneous Seeding of a Prion Structure by a Generic Amyloid Form of the Fungal Prion-forming Domain HET-s(218–289)

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

Degradation of Fungal Prion HET-s(218-289) Induces Formation of a Generic Amyloid Fold

(2012) William Wan et al.   BIOPHYSICAL JOURNAL

Cellular mechanisms of protein aggregate propagation

(2012) Brandon B. Holmes et al.   CURRENT OPINION IN NEUROLOGY

Stabilization of a Prion Strain of Synthetic Origin Requires Multiple Serial Passages

(2012) Natallia Makarava et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A New Mechanism for Transmissible Prion Diseases

(2012) N. Makarava et al.   JOURNAL OF NEUROSCIENCE

High natural prevalence of a fungal prion

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

A Unifying Role for Prions in Neurodegenerative Diseases

(2012) S. B. Prusiner   SCIENCE

Two structurally similar fungal prions efficiently cross-seed in vivo but form distinct polymers when coexpressed

(2011) Laura Benkemoun et al.   MOLECULAR MICROBIOLOGY

Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy

(2011) N. Mizuno et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The [Het-s] prion of Podospora anserina and its role in heterokaryon incompatibility

(2011) Sven J. Saupe   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY

Genesis of Mammalian Prions: From Non-infectious Amyloid Fibrils to a Transmissible Prion Disease

(2011) Natallia Makarava et al.   PLoS Pathogens

Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity

(2010) Christian Wasmer et al.   JOURNAL OF MOLECULAR BIOLOGY

Two Amyloid States of the Prion Protein Display Significantly Different Folding Patterns

(2010) Valeriy G. Ostapchenko et al.   JOURNAL OF MOLECULAR BIOLOGY

Atomic-Resolution Three-Dimensional Structure of HET-s(218−289) Amyloid Fibrils by Solid-State NMR Spectroscopy

(2010) Hélène Van Melckebeke et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

The Common Architecture of Cross-β Amyloid

(2009) Thomas R. Jahn et al.   JOURNAL OF MOLECULAR BIOLOGY

The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis

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

Natural and synthetic prion structure from X-ray fiber diffraction

(2009) H. Wille et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Functional Amyloids As Natural Storage of Peptide Hormones in Pituitary Secretory Granules

(2009) S. K. Maji et al.   SCIENCE

Infectious and Noninfectious Amyloids of the HET‐s(218–289) Prion Have Different NMR Spectra

(2008) Christian Wasmer et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Amyloids of Shuffled Prion Domains That Form Prions Have a Parallel In-Register β-Sheet Structure†

(2008) Frank Shewmaker et al.   BIOCHEMISTRY

Enclosed chambers for humidity control and sample containment in fiber diffraction

(2008) Michele McDonald et al.   JOURNAL OF APPLIED CRYSTALLOGRAPHY

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

(2008) C. Wasmer et al.   SCIENCE