Amyloid - β 42 (Aβ42) has a strong ability to oligomerize to form diffusible oligomers as well as larger polymers
called fibrils that form insoluble amyloid plaques, a major hallmark of AD.
And that sequence can form long chains called oligomers as well as fibers
called fibrils.
Many peptides and proteins have an innate ability to assemble into long, slender fibers
called fibrils and other shapes.
More than 40 illnesses known as amyloid diseases — Alzheimer's, Parkinson's and rheumatoid arthritis are a few — are linked to the buildup of proteins after they have transformed from their normally folded, biologically active forms to abnormally folded, grouped deposits
called fibrils or plaques.
Not exact matches
Co-lead researcher, Australian National University Professor John Carver, said that two unrelated proteins aggregate in UHT milk over a period of months to form clusters
called amyloid
fibrils, which cause the milk to transform from a liquid into a gel.
When myocilin goes wrong, or «misfolds,» it makes
fibrils that damage tissue
called the trabecular meshwork that normally allows the fluid inside the eye to drain and relieve interior pressure.
The structures,
called amyloid
fibrils, are also implicated in neurodegenerative conditions such as Alzheimer's and Parkinson's, and in prion diseases like Creutzfeldt - Jacob and mad cow disease.
Researchers believed that the
fibrils should come from a rigid structure
called a β - sheet.
For example, clumps of proteins
called amyloid
fibrils are thought to be the cause of Alzheimer's disease as well as several other devastating illnesses.
In recent years, scientists made the surprising discovery that seminal fluid harbors fragments of proteins that clump together, forming structures
called amyloid
fibrils.