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- W2765989831 abstract "Significance The findings in this manuscript report on the identification of a posttranslational modification in the huntingtin protein (phosphorylation on residue T3 in the N17 region of the protein), which can revert the conformational effects of the Huntington’s disease (HD) mutation itself on the huntingtin protein and inhibit its aggregation properties in vitro. Using the first ultrasensitive immunoassay for a posttranslational modification of huntingtin protein, we demonstrate that pT3 levels are decreased in mutant huntingtin in preclinical models as well as in clinically relevant samples from HD patients. These findings are of high significance to Huntington’s disease biology, provide insights into mechanisms of Huntington’s disease pathogenesis, and open new opportunities for the development of therapeutics and diagnostics for Huntington’s disease." @default.
- W2765989831 created "2017-11-10" @default.
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- W2765989831 date "2017-11-21" @default.
- W2765989831 modified "2023-10-09" @default.
- W2765989831 title "Phosphorylation of huntingtin at residue T3 is decreased in Huntington’s disease and modulates mutant huntingtin protein conformation" @default.
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