They also say that their graphene grid method could be used to determine the structures of other small and unstable proteins—including the amyloid-beta peptide that builds up in the brain in ...

The research team, coordinated by pharma startup Cortexyme, did not claim to have discovered definitive evidence of Alzheimer ...

Researchers from Osaka University found that peristaltic pump flow mechanically breaks supersaturation to induce amyloid ...

The factor that tips you over the edge from being at risk for a disease to actually developing the disease is not always ...

Misfolded proteins (also called toxic conformations) are typically insoluble, and they tend to form long linear or fibrillar aggregates known as amyloid deposits. But how can a protein change so ...

During her talk, Rice had described how a peptide called amyloid precursor protein (APP) gets broken down in the brain into smaller pieces such as amyloid-β, the peptide that notoriously goes on to ...

Jr., "The carboxy terminus of the b amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease," Biochemistry, 32:4693-7, 1993. (Cited ...

protein, amyloid-beta. Pathological forms of amyloid-beta start appearing in a patient’s blood 15–20 years before AD symptoms occur. The scientists investigated how early the test could be effective ...

Researchers at the University of Cologne have identified a specific form of the tau protein that is responsible for mediating the toxicity of harmful protein clumps in human neurons and thus represent ...

The buildup of knot-like RNA structures in brain cells may be the key to understanding how uncontrolled protein aggregation drives Alzheimer’s disease.