Assembly and deposition of physiologically generated, amyloidogenic
proteins occur in various human diseases, referred to as
amyloidoses, through misfolding that is either partial unfolding or
partial folding of the proteins. A growing body of evidence
suggests that misfolding of a given protein is driven by point
mutations or by the presence of environmental factors favourable
for amyloidogenesis. In this book, the authors present topical
research in the study of the composition, function and pathology of
amyloids, including the effect of yeast red pigment on amyloid
fibrils in vivo and in vitro; amyloid precursor protein and its
relation to Alzheimer's disease; amyloid precursor protein
expression after traumatic brain injury; protein aggregation as a
modulatory factor in EPMI and the atomic-resolution structures of
prion AGAAAAGA amyloid fibrils.
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