Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted

Huntingtin exon-1 (HTTex1) consists of a N-terminal N17 domain, the disease causing polyQ domain and a C-terminal proline-rich domain (PRD). Here, the authors combine electron paramagnetic resonance (EPR), solid-state NMR with other biophysical method to characterise the structural differences of va...

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Autores principales: J. Mario Isas, Nitin K. Pandey, Hui Xu, Kazuki Teranishi, Alan K. Okada, Ellisa K. Fultz, Anoop Rawat, Anise Applebaum, Franziska Meier, Jeannie Chen, Ralf Langen, Ansgar B. Siemer
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a
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