Polyglutamine disruption of the huntingtin exon1 N-terminus triggers a complex aggregation mechanism

Simple polyglutamine (polyQ) peptides aggregate in vitro via a nucleated growth pathway directly yielding amyloid-like aggregates. We show here that the 17 amino acid flanking sequence (htt(NT)) N-terminal to the polyQ in the toxic huntingtin exon1 fragment imparts onto this peptide a complex altern...

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Main Authors: Thakur, Ashwani K., Jayaraman, Murali, Mishra, Rakesh, Thakur, Monika, Chellgren, Veronique M., Byeon, In-Ja, Anjum, Dalaver H., Kodali, Ravindra, Creamer, Trevor P., Conway, James F., M.Gronenborn, Angela, Wetzel, Ronald
Format: Artigo
Language:Inglês
Published: 2009
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Article
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC2706102/
https://ncbi.nlm.nih.gov/pubmed/19270701
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.1570
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