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        Immuno-based Detection Assays to Quantify Distinct Mutant Huntingtin Conformations in Biological Samples

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        521
        A pathological hallmark of many protein-misfolding diseases is the formation of insoluble aggregates. Quantitative methods are needed to better resolve and define the formation, aggregation, and temporal dynamics of soluble misfolded proteins in native settings. In this book chapter we describe simple and sensitive detection methods to characterize high ordered aggregates (AGERA) and subsets of distinct soluble aggregates (SEC-FRET) of mutant huntingtin protein in biological samples.
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