A new study suggests that two of Alzheimer’s disease’s most debated players may be more closely connected than they first ...

Structure of hnRNPDL-2 amyloid fibres obtained by cryoEM at 2.5 A resolution. The upper part shows the organisation of the protein with two nucleic acid binding domains in pink and a low-complexity ...

A new biophysical study why apoE and other apolipoproteins co-deposit with amyloids and provides a structural basis for understanding how apolipoproteins modulate amyloid growth and proliferation in ...

Researchers show amyloid beta and tau compete for microtubule binding, disrupting cellular transport. This interference may trigger Alzheimer’s, shifting focus from protein buildup to intracellular ...

This is a preview. Log in through your library . Abstract Amyloid-β (Aβ) fibrils exhibit self-propagating, molecular-level polymorphisms that may contribute to variations in clinical and pathological ...

The tiny protein known as transthyretin can cause big problems in the body when it misfolds after secretion. While healthy transthyretin moves hormones through blood and spinal fluid, misfolded ...

Amyloid-beta (A-beta) aggregates are tangles of proteins most notably associated with neurodegenerative diseases like Alzheimer's. Despite its constant stint in the limelight, however, researchers ...

Researchers have developed a potential new peptide-based drug delivery system by repurposing fibrils that contribute to Alzheimer’s disease pathogenesis. Researchers at the University of North ...

Amyloid fibrils appear in many neurodegenerative diseases, and scientists are eager to understand how they form and spread. But amyloids—clumped aggregations of misfolded proteins—can be difficult to ...

A team from the University of Barcelona has designed and validated in animal models an innovative compound with a pioneering ...