A new Yale study has found a promising target for treating the brain fog that can follow COVID-19 and offers new insight into ...

Amyloid Beta Protein Gets Bum Rap Date: November 10, 2009 Source: Saint Louis University Summary: While too much amyloid beta protein in the brain is linked to the development of Alzheimer's ...

Novel Role Of Protein In Generating Amyloid-beta Peptide. ScienceDaily . Retrieved June 4, 2025 from www.sciencedaily.com / releases / 2009 / 04 / 090427193240.htm ...

Amyloid beta peptide (Aβ) is produced through the proteolytic processing of a transmembrane protein, amyloid precursor protein (APP), by β- and γ-secretases. Aβ accumulation in the brain is ...

After using mouse models of AD, researchers discovered that amyloid beta produced by oligodendrocytes was associated with the formation of plaques. The team found that by blocking the production of ...

Amyloid beta is a normal peptide byproduct of brain function, but in CAA and Alzheimer's, ... Amyloid beta induced production of oxygen free radicals, which damages arteries, ...

Study suggests stalled amyloid protein production drives Alzheimer’s disease ... (APP), which – once processed into amyloid beta (Aβ) protein ...

At the heart of more than 50 different neurodegenerative diseases is the molecule amyloid beta. This peptide (a chain of amino acids) has a tendency to clump together, forming structures known as ...

A new study sheds light on the differences between increased amyloid beta protein in aging, healthy brains and the brains of those with Alzheimer’s. Researchers at the University of Southern ...

Accumulating evidence suggests that dysregulated levels of amyloid β-protein precursor (APP) and its catabolites contribute to the impaired synaptic plasticity and seizure incidence observed in ...

Amyloid beta (Aβ) accumulation in the brain is proposed to be an early toxic event in the pathogenesis of Alzheimer’s disease (AD). However, the processes linked to the production of Aβ are ...

This revealed that part of the amyloid beta protein it was binding to was actually folded back onto itself in a hairpin-like shape, a structure that had never been seen before.