Implications of peptide assemblies in amyloid diseases

PC Ke, MA Sani, F Ding, A Kakinen, I Javed… - Chemical Society …, 2017 - pubs.rsc.org
Neurodegenerative disorders and type 2 diabetes are global epidemics compromising the
quality of life of millions worldwide, with profound social and economic implications. Despite …

The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease

OD King, AD Gitler, J Shorter - Brain research, 2012 - Elsevier
Prions are self-templating protein conformers that are naturally transmitted between
individuals and promote phenotypic change. In yeast, prion-encoded phenotypes can be …

Biological and chemical approaches to diseases of proteostasis deficiency

ET Powers, RI Morimoto, A Dillin… - Annual review of …, 2009 - annualreviews.org
Many diseases appear to be caused by the misregulation of protein maintenance. Such
diseases of protein homeostasis, or “proteostasis,” include loss-of-function diseases (cystic …

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 …

Amyloid assembly and disassembly

E Chuang, AM Hori, CD Hesketh… - Journal of Cell …, 2018 - journals.biologists.com
Amyloid fibrils are protein homopolymers that adopt diverse cross-β conformations. Some
amyloid fibrils are associated with the pathogenesis of devastating neurodegenerative …

Resveratrol selectively remodels soluble oligomers and fibrils of amyloid Aβ into off-pathway conformers

ARA Ladiwala, JC Lin, SS Bale… - Journal of Biological …, 2010 - ASBMB
Misfolded proteins associated with diverse aggregation disorders assemble not only into a
single toxic conformer but rather into a suite of aggregated conformers with unique …

Prion-like disorders: blurring the divide between transmissibility and infectivity

M Cushman, BS Johnson, OD King… - Journal of cell …, 2010 - journals.biologists.com
Prions are proteins that access self-templating amyloid forms, which confer phenotypic
changes that can spread from individual to individual within or between species. These …

Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans

ML Duennwald, AL Echeverria, J Shorter - PLoS biology, 2012 - journals.plos.org
How small heat shock proteins (sHsps) might empower proteostasis networks to control
beneficial prions or disassemble pathological amyloid is unknown. Here, we establish that …

Aromatic small molecules remodel toxic soluble oligomers of amyloid β through three independent pathways

ARA Ladiwala, JS Dordick, PM Tessier - Journal of Biological Chemistry, 2011 - ASBMB
In protein conformational disorders ranging from Alzheimer to Parkinson disease, proteins of
unrelated sequence misfold into a similar array of aggregated conformers ranging from …

Discovery of 2-aminothiazoles as potent antiprion compounds

S Ghaemmaghami, BCH May, AR Renslo… - Journal of …, 2010 - Am Soc Microbiol
Prion diseases are fatal, untreatable neurodegenerative diseases caused by the
accumulation of the misfolded, infectious isoform of the prion protein (PrP), termed PrPSc. In …