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Tandem Repeats in Genes, Proteins, and DiseaseImmuno-based Detection Assays to Quantify Distinct Mutant Huntingtin Conformations in Biological Samples

Tandem Repeats in Genes, Proteins, and Disease: Immuno-based Detection Assays to Quantify... [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.] http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

Tandem Repeats in Genes, Proteins, and DiseaseImmuno-based Detection Assays to Quantify Distinct Mutant Huntingtin Conformations in Biological Samples

Part of the Methods in Molecular Biology Book Series (volume 1017)
Editors: Hatters, Danny M.; Hannan, Anthony J.

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References (10)

Publisher
Humana Press
Copyright
© Springer Science+Business Media New York 2013
ISBN
978-1-62703-437-1
Pages
163 –171
DOI
10.1007/978-1-62703-438-8_12
Publisher site
See Chapter on Publisher Site

Abstract

[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.]

Published: Apr 20, 2013

Keywords: Endogenous mutant huntingtin; Oligomers; Soluble fragments; Insoluble aggregates; Agarose gel electrophoresis; Size-exclusion chromatography

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