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- W2012781495 abstract "We have investigated ubiquitinated paired helical filaments, which produce a proteinaceous smear in SDS-polyacrylamide gel electrophoresis and immunoblotting. The smear consisted largely of the carboxy-terminal portion of tau and ubiquitin. The ubiquitin-targeted protein was identified as tau in paired helical filaments, and the conjugation sites were localized to the microtubule-binding region. Most ubiquitin in paired helical filaments occurred as a monoubiquitinated form, and only a small proportion of ubiquitin formed multiubiquitin chains. There was a ubiquitin-negative smear, in which tau was much less processed in the amino-terminal portion. This strongly suggests that the amino-terminal processing of tau in paired helical filaments precedes its ubiquitination." @default.
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- W2012781495 date "1993-06-01" @default.
- W2012781495 modified "2023-10-17" @default.
- W2012781495 title "Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments" @default.
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- W2012781495 doi "https://doi.org/10.1016/0896-6273(93)90063-w" @default.
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