Amyloid fibrils in those with frontotemporal lobar degeneration (FTLD) contain a little-known protein called TMEM106B. Researchers speculate TMEM106B could be found to be the cause of FTLD.
Drugs that stabilize amyloid fibril "frustration" block further aggregation and could provide a new method to prevent the progression of Alzheimer's.
A new high-resolution 3D model reveals strong similarities in fibril structures associated with Alzheimer's and type 2 diabetes.
Far-infrared free-electron lasers may be a new way in which we fight the effects of Alzheimer's disease. Researchers report the technology can break down protein aggregates associated with the disease deep within the brain.
Researchers have captured some of the sharpest images of Alzheimer's associated amyloid fibrils to date. The 3D structure of the fibrils displays some previously unknown structural details that researchers believe could help answer some important questions about the development of Alzheimer's disease.
Researchers report they have discovered the mechanism that leads to the rapid build up of amyloid plaques in Alzheimer's disease.
A metallic molecule allows for real time motoring of amyloid beta plaques.
Researchers made a subtle alteration to the amyloid beta protein. The change affect its aggregation behavior and stabilizes an intermediate form with enhanced toxicity.
Researchers have identified the point at which proteins in the brain turn toxic during the decent into Parkinson's disease.
A new study reports a molecular chaperone can inhibit a key stage in the development of Alzheimer's disease.
A new study has pinpointed a catalytic trigger for the onset of Alzheimer's disease. The findings could play a central role in the diagnostics and new drug development for neurodegenerative diseases.