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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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| Autori principali: | , , , , , , , , , , , |
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| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
2009
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| Soggetti: | |
| Accesso online: | 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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