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- W2000251927 endingPage "12807" @default.
- W2000251927 startingPage "12798" @default.
- W2000251927 abstract "In Alzheimer's disease, tau is hyperphosphorylated, which is thought to detach it from microtubules (MTs), induce MT destabilization, and promote aggregation. Using a previously described in vivo model, we investigated whether hyperphosphorylation impacts tau function in wild-type and transgenic mice. We found that after anesthesia-induced hypothermia, MT-free tau was hyperphosphorylated, which impaired its ability to bind MTs and promote MT assembly. MT-bound tau was more resistant to hyperphosphorylation compared with free tau and tau did not dissociate from MTs in wild-type mice. However, 3-repeat tau detached from MT in the transgenic mice. Surprisingly, dissociation of tau from MTs did not lead to overt depolymerization of tubulin, and there was no collapse, or disturbance of axonal MT networks. These results indicate that, in vivo , a subpopulation of tau bound to MTs does not easily dissociate under conditions that extensively phosphorylate tau. Tau remaining on the MTs under these conditions is sufficient to maintain MT network integrity." @default.
- W2000251927 created "2016-06-24" @default.
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- W2000251927 date "2008-11-26" @default.
- W2000251927 modified "2023-10-05" @default.
- W2000251927 title "Anesthesia-Induced Hyperphosphorylation Detaches 3-Repeat Tau from Microtubules without Affecting Their Stability<i>In Vivo</i>" @default.
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- W2000251927 doi "https://doi.org/10.1523/jneurosci.4101-08.2008" @default.
- W2000251927 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2610528" @default.
- W2000251927 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19036972" @default.
- W2000251927 hasPublicationYear "2008" @default.