We may have been overestimating the role of a pathological class of misfolded protein in neurodegenerative disease.
Called prions, these molecules are responsible for conditions such as bovine spongiform encephalopathy or 'mad cow disease', chronic wasting disease in deer, and Creutzfeldt-Jakob disease in humans.
A new study in mice has found that some of the hallmarks of prion disease in brain tissue – such as the appearance of sponge-like holes, scarring, and accumulation of amyloid plaques – can develop even in the complete absence of prions in their infectious configuration.
Related: Misfolded Proteins Could Make Dementia Transmissible, Scientists Suggest
Instead, the study found that non-infectious prion precursors in the presence of chronic inflammation driven by a bac

ScienceAlert en Español
The Post and Courier
People Top Story
VICE
San Bernardino Sun
New York Post Health
Verywell Health
St. Louis Public Radio
The Daily Mining Gazette