NR AMBJ
AU Vitek,M.P.
TI Radical changes in beta-amyloid form and function
QU Molecular and Chemical Neuropathology 1996 May-Aug; 28(1-3): 49-55
PT journal article; review; review, tutorial
AB A growing body of evidence supports the nucleation hypothesis of fibrillar amyloid formation. In this article, it is hypothesized that the fibrils formed with human A beta, rodent A beta, and a mixture of the two peptides may form nearly identical physical structures with clearly different biological activities. Data is reported supporting the concept that a specific "strain" of nucleation seed could impart a new structure on a growing amyloid fibril, thereby changing its biological activity. The data that the biological activities of specific prion strains have a basis in strain-specific structure have been supported experimentally.
ZR 10
MH Alzheimer Disease/metabolism; Amino Acid Sequence; Amyloid beta-Protein/*chemistry/*physiology/toxicity; Animal; Comparative Study; Glycosylation End Products, Advanced/metabolism; Human; Molecular Sequence Data; Prions/chemistry; Protein Structure, Secondary; Rodentia; Sequence Homology, Amino Acid
AD Duke University Medical Center, Durham, NC 27710, USA
SP englisch
PO USA