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Article

The structural basis of huntingtin (Htt) fibril polymorphism, revealed by cryo-EM of exon 1 Htt fibrils

2021-09-23

Abstract excerpt

The lack of detailed insight into the structure of aggregates formed by the huntingtin protein has hampered efforts to develop therapeutics and diagnostics targeting pathology formation in the brain of patients with Huntington’s disease. To address this knowledge gap, we investigated the structural properties of in vitro generated fibrils from exon1 of the huntingtin protein by electron cryo-microscopy and single-...

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Literature Corpus work
b6604389-47f4-5bf1-8210-4a73dfd191af
DOI
10.1101/2021.09.23.461534
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The structural basis of huntingtin (Htt) fibril polymorphism, revealed by cryo-EM of exon 1 Htt fibrilsDOI 10.1101/2021.09.23.461534
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