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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Auteurs principaux: | , , , , , , , , , , , |
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Format: | article |
Langue: | EN |
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Nature Portfolio
2021
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Accès en ligne: | https://doaj.org/article/a3ad6629dcdc4912b80f4ba73af97d8a |
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