{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T01:12:47Z","timestamp":1788311567990,"version":"build-2803163510"},"reference-count":74,"publisher":"American Chemical Society (ACS)","issue":"24","license":[{"start":{"date-parts":[[2015,6,12]],"date-time":"2015-06-12T00:00:00Z","timestamp":1434067200000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AG019322"],"award-info":[{"award-number":["AG019322"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,6,24]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Repeat length disease thresholds vary among the 10 expanded polyglutamine (polyQ) repeat diseases, from about 20 to about 50 glutamine residues. The unique amino acid sequences flanking the polyQ segment are thought to contribute to these repeat length thresholds. The specific portions of the flanking sequences that modulate polyQ properties are not always clear, however. This ambiguity may be important in Huntington\u2019s disease (HD), for example, where in vitro studies of aggregation mechanisms have led to distinctly different mechanistic models. Most in vitro studies of the aggregation of the huntingtin (HTT) exon1 fragment implicated in the HD mechanism have been conducted on inexact molecules that are imprecise either on the N-terminus (recombinantly produced peptides) or on the C-terminus (chemically synthesized peptides). In this paper, we investigate the aggregation properties of chemically synthesized HTT exon1 peptides that are full-length and complete, containing both normal and expanded polyQ repeat lengths, and compare the results directly to previously investigated molecules containing truncated C-termini. The results on the full-length peptides are consistent with a two-step aggregation mechanism originally developed based on studies of the C-terminally truncated analogues. Thus, we observe relatively rapid formation of spherical oligomers containing from 100 to 600 HTT exon1 molecules and intermediate formation of short protofibril-like structures containing from 500 to 2600 molecules. In contrast to this relatively rapid assembly, mature HTT exon1 amyloid requires about one month to dissociate in vitro, which is similar to the time required for neuronal HTT exon1 aggregates to disappear in vivo after HTT production is discontinued.<\/jats:p>","DOI":"10.1021\/bi500300c","type":"journal-article","created":{"date-parts":[[2014,6,12]],"date-time":"2014-06-12T10:48:25Z","timestamp":1402570105000},"page":"3897-3907","source":"Crossref","is-referenced-by-count":44,"title":["Aggregation Behavior of Chemically Synthesized, Full-Length\nHuntingtin Exon1"],"prefix":"10.1021","volume":"53","author":[{"given":"Bankanidhi","family":"Sahoo","sequence":"first","affiliation":[{"name":"University of Pittsburgh School of Medicine and , , , ,","place":["Pittsburgh, Pennsylvania, United States, 15260"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Singer","sequence":"additional","affiliation":[{"name":"Leipzig University , , ,","place":["Leipzig, Germany, 04103"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ravindra","family":"Kodali","sequence":"additional","affiliation":[{"name":"University of Pittsburgh School of Medicine and , , , ,","place":["Pittsburgh, Pennsylvania, United States, 15260"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thole","family":"Zuchner","sequence":"additional","affiliation":[{"name":"Leipzig University , , ,","place":["Leipzig, Germany, 04103"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald","family":"Wetzel","sequence":"additional","affiliation":[{"name":"University of Pittsburgh School of Medicine and , , , ,","place":["Pittsburgh, Pennsylvania, United States, 15260"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,6,12]]},"reference":[{"key":"2026090120152550200_cit1","volume-title":"Huntington\u2019s Disease","author":"Bates","year":"2002","edition":"3"},{"key":"2026090120152550200_cit2","volume-title":"Huntington\u2019s Disease","author":"Bates","year":"2014","edition":"4"},{"key":"2026090120152550200_cit3","first-page":"429","article-title":"The polyglutamine diseases","volume-title":"Huntington\u2019s\nDisease","author":"Bates","year":"2002"},{"key":"2026090120152550200_cit4","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.neuron.2011.03.021","article-title":"An antisense CAG\nrepeat transcript\nat JPH3 locus mediates expanded polyglutamine protein toxicity in\nHuntington\u2019s disease-like 2 mice","volume":"70","author":"Wilburn","year":"2011","journal-title":"Neuron"},{"key":"2026090120152550200_cit5","doi-asserted-by":"crossref","first-page":"8808","DOI":"10.1074\/jbc.M109.075028","article-title":"Proteolysis of mutant\nhuntingtin produces an exon 1\nfragment that accumulates as an aggregated protein in neuronal nuclei\nin Huntington disease","volume":"285","author":"Landles","year":"2010","journal-title":"J. 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J."},{"key":"2026090120152550200_cit37","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0015245","article-title":"Formation and Toxicity of Soluble Polyglutamine Oligomers\nin Living Cells","volume":"5","author":"Lajoie","year":"2010","journal-title":"PLoS One"},{"key":"2026090120152550200_cit38","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0044457","article-title":"Fragments\nof HdhQ150 mutant huntingtin form a soluble oligomer pool that declines\nwith aggregate deposition upon aging","volume":"7","author":"Marcellin","year":"2012","journal-title":"PLoS One"},{"key":"2026090120152550200_cit39","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1073\/pnas.96.8.4604","article-title":"Self-assembly\nof polyglutamine-containing huntingtin fragments into amyloid-like\nfibrils: implications for Huntington\u2019s disease pathology","volume":"96","author":"Scherzinger","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. 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