Prions | Nature

Letter | 29 August 2018

Structures of filaments from Pick’s disease reveal a novel tau protein fold

The structures of tau filaments from patients with the neurodegenerative disorder Pick’s disease show that the filament fold is different from that of the tau filaments found in Alzheimer’s disease.

Benjamin Falcon
, Wenjuan Zhang
& Michel Goedert

Letter | 31 July 2013

The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein

Biochemical and structural investigation of a model for prion-induced neurodegeneration—antibody binding to PrP^C—reveals the role of the PrP flexible tail and reactive oxygen species in mediating toxicity.

Tiziana Sonati
, Regina R. Reimann
& Adriano Aguzzi

Letter | 02 May 2012

Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β

It is shown that the formation of amyloid-β oligomers, one of the histopathological signatures of Alzheimer’s disease, can be triggered by small quantities of a specifically truncated and post-translationally modified version of amyloid-β.

Justin M. Nussbaum
, Stephan Schilling
& George S. Bloom

News Feature | 15 February 2012

Prions and chaperones: Outside the fold

Susan Lindquist has challenged conventional thinking on how misfolded proteins drive disease and may power evolution. But she still finds that criticism stings.

Bijal P. Trivedi

Article | 15 February 2012

Prions are a common mechanism for phenotypic inheritance in wild yeasts

Previously thought to be rare laboratory artefacts or diseases of yeast, prions are actually found in one third of 700 wild strains; the prions give their hosts beneficial traits that can be transmitted epigenetically to the next generation, and then fixed in the genome.

Randal Halfmann
, Daniel F. Jarosz
& Susan Lindquist

Research Highlights | 17 August 2011

Prion-like immune trigger

Outlook | 13 July 2011

Amyloid: Little proteins, big clues

After a quarter of a century, the amyloid hypothesis for Alzheimer's disease is reconnecting to its roots in prion research.

Jim Schnabel

News & Views | 23 February 2011

Infectivity versus toxicity

Prions are infectious proteins that can cause deadly diseases in mammals. Detailed measurements of infectivity suggest that there may be distinct infectious and toxic versions of this protein. See Letter p.540