In April 2025, three people in Oregon developed Creutzfeldt-Jakob disease (CJD), a rare, fatal neurological condition that is ...

In vitro structural studies have shown that misfolding and aggregation involve a large structural rearrangement of the protein, forming cross-β amyloid-like fibrils, which seems to be the common ...

Contribution from the Dipartimento di Chimica, Università di Firenze, Via della Lastruccia 3, I-50019 Sesto Fiorentino, Italy, European Laboratory for Nonlinear Spectroscopy (LENS), Via Nello Carrara ...

The patient was unknowingly infected with an abnormal protein that causes a rare, fatal neurological disease with no ...

A 58-year-old woman died of a rare prion disease, iatrogenic Creutzfeldt-Jakob disease, nearly five decades after receiving ...

“The detection of this isolated case of atypical BSE shows that the UK’s surveillance programme is working well. There is no risk to the public, as the animal’s carcass will have been destroyed and no ...

The Vallabh/Minikel lab at the Broad Institute has selected Argonaut Manufacturing Services, Inc., "Argonaut," as the drug product manufacturer for a therapeutic compound for a potential clinical ...

is caused by the misfolding of the prion protein (PrP) and leads to rapid cognitive decline and death. Approximately 500 new cases are diagnosed each year in the United States. The investigational ...

*To whom correspondence should be addressed: Department of Biochemistry, Vail Building, Room 302, Dartmouth Medical School, Hanover, NH 03755. Phone: (603) 650-1192. Fax: (603) 650-1193. E-mail: ...

An enzyme as key to protein quality Date: May 9, 2025 Source: University of Würzburg Summary: In neurodegenerative diseases such as Alzheimer's or Parkinson's, proteins accumulate in the body's ...

Get Instant Summarized Text (Gist) Increasing levels of the secreted Klotho protein (s-KL) in mice extends lifespan by 15–20% and improves muscle, bone, and cognitive health during aging ...

Prion diseases are characterised by the accumulation of misfolded prion proteins and provide a highly tractable platform to determine if TREM2 has disease-modifying effects. Conclusion: We conclude ...