Prions in yeast

SW Liebman, YO Chernoff - Genetics, 2012 - academic.oup.com
The concept of a prion as an infectious self-propagating protein isoform was initially
proposed to explain certain mammalian diseases. It is now clear that yeast also has …

Solid-state NMR studies of amyloid fibril structure

R Tycko - Annual review of physical chemistry, 2011 - annualreviews.org
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and
other diseases and from their role as an alternative structural state for many peptides and …

Molecular structures of amyloid and prion fibrils: consensus versus controversy

R Tycko, RB Wickner - Accounts of chemical research, 2013 - ACS Publications
Many peptides and proteins self-assemble into amyloidfibrils. Examples include mammalian
and fungal prion proteins, polypeptides associated with human amyloid diseases, and …

Atomic-resolution three-dimensional structure of HET-s (218− 289) amyloid fibrils by solid-state NMR spectroscopy

H Van Melckebeke, C Wasmer, A Lange… - Journal of the …, 2010 - ACS Publications
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state
NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal …

Yeast prions: structure, biology, and prion-handling systems

RB Wickner, FP Shewmaker, DA Bateman… - Microbiology and …, 2015 - Am Soc Microbiol
SUMMARY A prion is an infectious protein horizontally transmitting a disease or trait without
a required nucleic acid. Yeast and fungal prions are nonchromosomal genes composed of …

Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity

J Gath, L Bousset, B Habenstein, R Melki… - PLoS …, 2014 - journals.plos.org
We structurally compare, using solid-state NMR, two different polymorphs of α-synuclein
which, as established recently, display contrasting biochemical properties, toxicity, and …

The mechanism of toxicity in HET-S/HET-s prion incompatibility

C Seuring, J Greenwald, C Wasmer, R Wepf… - PLoS …, 2012 - journals.plos.org
The HET-s protein from the filamentous fungus Podospora anserina is a prion involved in a
cell death reaction termed heterokaryon incompatibility. This reaction is observed at the …

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

SJ Saupe - Seminars in cell & developmental biology, 2011 - Elsevier
[Het-s] is a prion from the filamentous fungus Podospora anserina and corresponds to a self-
perpetuating amyloid aggregate of the HET-s protein. This prion protein is involved in a …

A Sedimented Sample of a 59 kDa Dodecameric Helicase Yields High‐Resolution Solid‐State NMR Spectra

C Gardiennet, AK Schütz, A Hunkeler… - Angewandte Chemie …, 2012 - Wiley Online Library
Solid-state NMR spectroscopy has developed into a useful method for protein structure
determination. In contrast to diffraction methods, NMR spectroscopy does not rely on long …

Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy

JJ Helmus, K Surewicz, WK Surewicz… - Journal of the …, 2010 - ACS Publications
Amyloid aggregates of a C-truncated Y145Stop mutant of human prion protein, huPrP23−
144, associated with a heritable amyloid angiopathy, have previously been shown to contain …