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Biol."},{"key":"10.1016\/j.jmb.2021.167222_b0345","doi-asserted-by":"crossref","first-page":"3942","DOI":"10.1021\/acs.biochem.5b00281","article-title":"Solid-state nuclear magnetic resonance on the static and dynamic domains of huntingtin exon-1 fibrils","volume":"54","author":"Isas","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2021.167222_b0350","doi-asserted-by":"crossref","first-page":"21647","DOI":"10.1074\/jbc.M109.016923","article-title":"Monoclonal antibodies recognize distinct conformational epitopes formed by polyglutamine in a mutant huntingtin fragment","volume":"284","author":"Legleiter","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167222_b0355","doi-asserted-by":"crossref","first-page":"14777","DOI":"10.1074\/jbc.M109.093708","article-title":"Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in Vitro and in Vivo","volume":"285","author":"Legleiter","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167222_b0360","doi-asserted-by":"crossref","first-page":"2560","DOI":"10.1074\/jbc.M114.603332","article-title":"Molecular interaction between the chaperone Hsc70 and the N-terminal flank of huntingtin exon 1 modulates aggregation","volume":"290","author":"Monsellier","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2021.167222_b0365","doi-asserted-by":"crossref","first-page":"7841","DOI":"10.1073\/pnas.140202897","article-title":"Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils","volume":"97","author":"Muchowski","year":"2000","journal-title":"Proc. Natl. Acad. 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Sci."},{"key":"10.1016\/j.jmb.2021.167222_b0455","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1080\/19336934.2015.1118591","article-title":"Non-cell autonomous cell death caused by transmission of Huntingtin aggregates in Drosophila","volume":"9","author":"Babcock","year":"2015","journal-title":"Fly"},{"key":"10.1016\/j.jmb.2021.167222_b0460","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/nature21362","article-title":"C. elegans neurons jettison protein aggregates and mitochondria under neurotoxic stress","volume":"542","author":"Melentijevic","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2021.167222_b0465","doi-asserted-by":"crossref","first-page":"647","DOI":"10.3389\/fnins.2017.00647","article-title":"The evidence for the spread and seeding capacities of the mutant huntingtin protein in in vitro systems and their therapeutic implications","volume":"11","author":"Masnata","year":"2017","journal-title":"Front. 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