Inhibition of proteasome and Shaggy/Glycogen synthase kinase-3β kinase prevents clearance of phosphorylated tau inDrosophila
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience
Reference36 articles.
1. Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
2. Rapamycin alleviates toxicity of different aggregate-prone proteins
3. Targeted increase in shaggy activity levels blocks wingless signaling
4. Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons
5. Proteasome-mediated degradation of tau proteins occurs independently of the chymotrypsin-like activity by a nonprocessive pathway
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2. S6K/p70S6K1 protects against tau-mediated neurodegeneration by decreasing the level of tau phosphorylated at Ser262 in a Drosophila model of tauopathy;Neurobiology of Aging;2018-11
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5. Rescue from tau-induced neuronal dysfunction produces insoluble tau oligomers;Scientific Reports;2015-11-26
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