An illustration of how swapping an amino acid in beta amyloid
precursor proteins results in longer and shorter strands
An illustration of how swapping an amino acid in beta amyloid
precursor proteins results in longer and shorter strands (Credit: Brian Kladko and Weihong Song / University of British Columbia)
Not exact matches
In the brains of patients with Alzheimer's disease (AD), amyloid
precursor protein is broken apart, and the
resulting fragments — β - amyloid peptides, or Aβ peptides — aggregate to form plaques.
The
result was a slightly lowered level of cancer - related
proteins, which are a
precursor for the growth of cancer cells.
Proteolytic cleavage of amyloid - β -
protein precursor (AβPP) by β - and γ - secretases
results in production of the amyloid - β peptide (Aβ) that accumulates in the brains of sufferers of Alzheimer's disease (AD).
The production of neurotoxic Aβ peptide
results from the specific proteolytic processing of the amyloid
precursor protein (APP).
Aβ
results from the normal cleavage of amyloid
precursor protein (APP), but its accumulation and aggregation into plaques represents the quintessential feature of AD.27 Aβ is found in orders of magnitude greater in AD brains than in healthy brains.28 This fact is noteworthy because lower concentrations of Aβ tend to stay soluble; higher concentrations form plaques more readily.29