The misfolded proteins responsible for a fatal neurological illness in deer have a twist. The first detailed structure of an infectious prion that causes chronic wasting disease, or CWD, reveals ...

Neurodegenerative diseases are characterized by the deposition of clumped proteins in the brain and progressive neuronal cell death. Although the causal link between protein aggregates and ...

Close-up on three ropes and marine knots isolated on white background. Each is photographed separately. Prion diseases are rare but deadly neurodegenerative brain diseases that result from misfolding ...

In a new study, researchers from Case Western Reserve University School of Medicine have identified the structure of protein fibrils linked to a hereditary form of human prion disease. This insight, ...

A study from Bochum describes a mammal-specific domain of the prion protein and offers new approaches for research into neurodegenerative diseases. At first, they cause memory deficits and ...

Prion diseases are rare and occur due to proteins in the brain that “misfold.” Another name for prion disease is transmissible spongiform encephalopathies (TSEs). There are many types of prion ...

PROVIDENCE, R.I. -- Two Brown Medical School biologists have figured out the fate of healthy protein when it comes in contact with the infectious prion form in yeast: The protein converts to the prion ...

Protein aggregation is typical of various neurodegenerative diseases such as Alzheimer's, Parkinson's and prion diseases such as Creutzfeld-Jakob disease. A research team has now used new in vitro and ...

Yeast prions are increasingly recognised as pivotal agents in non-Mendelian inheritance, whereby protein conformations rather than nucleic acids dictate heritable traits. In Saccharomyces cerevisiae ...

When Julie Moreno arrived at Texas A&M University as a first-generation student in 2000, she wanted to work in veterinary medicine. But the opportunity to work in a research laboratory during her time ...

Scientists at Northwestern University and University of California, Santa Barbara have created the first synthetic fragment of tau protein that acts like a prion. The “mini prion” folds and stacks ...