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- W2066595280 abstract "UBIQUITIN (Ub)-immunocytochemistry on Alzheimer's disease (AD) brain sections shows diverse Ub-associated deposits in the neuropil and senile plaques, elevated levels of Ub reactivity in hippocampal neurons and glia, and co-localization of Ub and β-amyloid precursor protein (βPP) epitope reactivity in dystrophic axons. These observations may suggest a role for Ub and stress-related mechanisms in AD pathogenesis. Here we show for the first time that Ub interacts avidly but non-covalently with βPP and such complexes, apparently formed in vivo, can be isolated from AD brain extracts by Ub-gel matrix affinity chromatography. Polyclonal antibodies specific to Ub and to different regions of βPP were employed to characterize these proteins. The implication of Ub-βPP complex formation is discussed in the context of βPP processing." @default.
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- W2066595280 date "1997-08-01" @default.
- W2066595280 modified "2023-09-24" @default.
- W2066595280 title "Ubiquitin (Ub) interacts non-covalently with Alzheimer amyloid precursor protein (βPP)" @default.
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- W2066595280 doi "https://doi.org/10.1097/00001756-199708180-00026" @default.
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