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- W1993776979 abstract "Abstract Tau isoforms migrating at 46–68 and 97–115 kDa were prominent within heat‐stableTriton‐soluble material, and were present in lesser concentration within Triton‐insolublecytoskeletons, derived from undifferentiated SH‐SY‐5Y human neuroblastoma cells. Conversely,a 26–30 kDa tau isoform was enriched in the cytoskeleton and detected at relatively minor levelswithin cytosolic fractions. Pulse labeling with 35 S‐methionine indicated that this 26–30kDa small tau did not represent a breakdown product of larger isoforms. Since the nucleus isretained within the Triton‐insoluble cytoskeleton, additional cultures were fractionated ontosucrose to obtain purified nuclei. The vast majority of small tau was recovered within purifiednuclei. Small tau was reactive with tau antibodies directed towards N‐terminal, C‐terminal andcentral epitopes, further confirming that this small isoform was not derived from proteolyticcleavage of larger tau isoforms. Small tau demonstrated alkaline phosphatase‐sensitive reactivitywith multiple phospho‐dependent tau antibodies. Small tau was depleted within 3 days of retinoicacid‐induced differentiation, suggesting that the putative function of this isoform may be obsoletefollowing terminal differentiation of neurons." @default.
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- W1993776979 date "1998-02-01" @default.
- W1993776979 modified "2023-09-27" @default.
- W1993776979 title "A 26–30 kDa developmentally‐regulated tauisoform localized within nuclei of mitotic humanneuroblastoma cells" @default.
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- W1993776979 doi "https://doi.org/10.1016/s0736-5748(97)00044-0" @default.
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