The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neuro...
The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Converging evidence points to the N-terminal domain comprising the first 17 amino acids of the Huntingtin protein (Nt17) as a key regulator of its aggregation, cellular properties and toxicity. In this study, we further investigated the interplay between Nt17 and the polyQ domain repeat length in regulating the aggregation and inclusion formation o...
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The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1
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TN_cdi_proquest_journals_2505435954
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2505435954
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E-ISSN
2692-8205
DOI
10.1101/2021.02.15.431207
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https://www.proquest.com/docview/2505435954?pq-origsite=primo&accountid=13902
