{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T20:12:54Z","timestamp":1790021574193,"version":"4.0.1"},"reference-count":84,"publisher":"American Chemical Society (ACS)","issue":"41","license":[{"start":{"date-parts":[[2017,11,7]],"date-time":"2017-11-07T00:00:00Z","timestamp":1510012800000},"content-version":"vor","delay-in-days":46,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000065","name":"National Institute of Neurological Disorders and Stroke","doi-asserted-by":"publisher","award":["R01NS056114"],"award-info":[{"award-number":["R01NS056114"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100005725","name":"CHDI Foundation","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100005725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010665","name":"H2020 Marie Sklodowska-Curie Actions","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Ecole Polytechnique F?d?rale de Lausanne","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2017,10,18]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Huntington?s disease is caused by expansion of a polyglutamine (polyQ) domain within exon 1 of the huntingtin gene (Httex1). The prevailing hypothesis is that the monomeric Httex1 protein undergoes sharp conformational changes as the polyQ length exceeds a threshold of 36?37 residues. Here, we test this hypothesis by combining novel semi-synthesis strategies with state-of-the-art single-molecule Fo?rster resonance energy transfer measurements on biologically relevant, monomeric Httex1 proteins of five different polyQ lengths. Our results, integrated with atomistic simulations, negate the hypothesis of a sharp, polyQ length-dependent change in the structure of monomeric Httex1. Instead, they support a continuous global compaction with increasing polyQ length that derives from increased prominence of the globular polyQ domain. Importantly, we show that monomeric Httex1 adopts tadpole-like architectures for polyQ lengths below and above the pathological threshold. Our results suggest that higher order homotypic and\/or heterotypic interactions within distinct sub-populations of neurons, which are inevitable at finite cellular concentrations, are likely to be the main source of sharp polyQ length dependencies of HD.<\/jats:p>","DOI":"10.1021\/jacs.7b06659","type":"journal-article","created":{"date-parts":[[2017,9,22]],"date-time":"2017-09-22T13:54:57Z","timestamp":1506088497000},"page":"14456-14469","source":"Crossref","is-referenced-by-count":104,"title":["Monomeric\nHuntingtin Exon 1 Has Similar Overall Structural\nFeatures for Wild-Type and Pathological Polyglutamine Lengths"],"prefix":"10.1021","volume":"139","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5562-5620","authenticated-orcid":true,"suffix":"IV","given":"John B.","family":"Warner","sequence":"first","affiliation":[{"name":"Ecole Polytechnique Fe?de?rale de Lausanne (EPFL) , , ,","place":["Lausanne, Switzerland, CH-1015"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3240-1856","authenticated-orcid":true,"given":"Kiersten M.","family":"Ruff","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Piau Siong","family":"Tan","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory (EMBL) , , ,","place":["Heidelberg, Germany, 69117"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward A.","family":"Lemke","sequence":"additional","affiliation":[{"name":"European Molecular Biology Laboratory (EMBL) , , ,","place":["Heidelberg, Germany, 69117"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2568-1378","authenticated-orcid":true,"given":"Rohit V.","family":"Pappu","sequence":"additional","affiliation":[{"name":"Washington University in St. Louis , , , ,","place":["St. Louis, Missouri, United States, 63130"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7682-8320","authenticated-orcid":true,"given":"Hilal A.","family":"Lashuel","sequence":"additional","affiliation":[{"name":"Ecole Polytechnique Fe?de?rale de Lausanne (EPFL) , , ,","place":["Lausanne, Switzerland, CH-1015"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2017,9,22]]},"reference":[{"issue":"6","key":"2026082619472853600_cit1","doi-asserted-by":"publisher","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","volume":"72","author":"MacDonald","year":"1993","journal-title":"Cell"},{"issue":"4","key":"2026082619472853600_cit2","doi-asserted-by":"publisher","first-page":"398","DOI":"10.1038\/ng0893-398","volume":"4","author":"Andrew","year":"1993","journal-title":"Nat. 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