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- W2499006706 abstract "Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates the turnover of some proteins (termed clients) by linking them to the degradation pathways. This activity is critical to normal protein homeostasis, yet it appears to fail in diseases associated with abnormal protein accumulation. It is not clear why Hsp70 promotes client degradation under some conditions, while sparing that protein under others. Here, we used a combination of chemical biology and genetic strategies to systematically perturb the affinity of Hsp70 for the model client, tau. This approach revealed that tight complexes between Hsp70 and tau were associated with enhanced turnover while transient interactions favored tau retention. These results suggest that client affinity is one important parameter governing Hsp70-mediated quality control." @default.
- W2499006706 created "2016-08-23" @default.
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- W2499006706 date "2016-08-01" @default.
- W2499006706 modified "2023-10-17" @default.
- W2499006706 title "Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy" @default.
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- W2499006706 doi "https://doi.org/10.1016/j.chembiol.2016.04.014" @default.
- W2499006706 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4992411" @default.
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