{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T20:13:14Z","timestamp":1790021594550,"version":"4.0.1"},"reference-count":89,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2018,5,1]],"date-time":"2018-05-01T00:00:00Z","timestamp":1525132800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,5,1]],"date-time":"2018-05-01T00:00:00Z","timestamp":1525132800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,4,4]],"date-time":"2018-04-04T00:00:00Z","timestamp":1522800000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006260","name":"Technion-Israel Institute of Technology","doi-asserted-by":"publisher","award":["3200003"],"award-info":[{"award-number":["3200003"]}],"id":[{"id":"10.13039\/501100006260","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013616","name":"American Society for Biochemistry and Molecular Biology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013616","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000032","name":"Institute of Infection and Immunity","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000032","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001779","name":"Monash University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001779","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2018,5]]},"DOI":"10.1016\/j.jmb.2018.03.031","type":"journal-article","created":{"date-parts":[[2018,4,5]],"date-time":"2018-04-05T20:12:10Z","timestamp":1522959130000},"page":"1442-1458","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":73,"title":["Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length"],"prefix":"10.1016","volume":"430","author":[{"given":"Estella A.","family":"Newcombe","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiersten M.","family":"Ruff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashish","family":"Sethi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Angelique R.","family":"Ormsby","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasmin M.","family":"Ramdzan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Archa","family":"Fox","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony W.","family":"Purcell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul R.","family":"Gooley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rohit V.","family":"Pappu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danny M.","family":"Hatters","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2018.03.031_bb0005","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0140-6736(07)60111-1","article-title":"Huntington's disease","volume":"369","author":"Walker","year":"2007","journal-title":"Lancet (Lond. Engl.)"},{"key":"10.1016\/j.jmb.2018.03.031_bb0010","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1126\/science.277.5334.1990","article-title":"Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain","volume":"277","author":"DiFiglia","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.jmb.2018.03.031_bb0015","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0092-8674(00)80513-9","article-title":"Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation","volume":"90","author":"Davies","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2018.03.031_bb0020","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1093\/hmg\/ddg075","article-title":"Transgenic rat model of Huntington's disease","volume":"12","author":"von Horsten","year":"2003","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2018.03.031_bb0025","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1038\/nature06975","article-title":"Towards a transgenic model of Huntington\/'s disease in a non-human primate","volume":"453","author":"Yang","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2018.03.031_bb0030","doi-asserted-by":"crossref","first-page":"2753","DOI":"10.1038\/ncomms3753","article-title":"Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress","volume":"4","author":"Leitman","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jmb.2018.03.031_bb0035","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"Arrasate","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2018.03.031_bb0040","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.chembiol.2010.03.011","article-title":"Conformation sensors that distinguish monomeric proteins from oligomers in live cells","volume":"17","author":"Ramdzan","year":"2010","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0045","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1038\/nchembio.694","article-title":"Identifying polyglutamine protein species in situ that best predict neurodegeneration","volume":"7","author":"Miller","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0050","doi-asserted-by":"crossref","first-page":"8188","DOI":"10.1074\/jbc.M110.192013","article-title":"A compact beta model of huntingtin toxicity","volume":"286","author":"Zhang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0055","doi-asserted-by":"crossref","first-page":"16017","DOI":"10.1074\/jbc.M111.252577","article-title":"Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein","volume":"287","author":"Nucifora","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0060","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.jmb.2012.01.034","article-title":"Disease-associated polyglutamine stretches in monomeric huntingtin adopt a compact structure","volume":"421","author":"Peters-Libeu","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0065","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.celrep.2017.04.029","article-title":"Huntingtin inclusions trigger cellular quiescence, deactivate apoptosis, and lead to delayed necrosis","volume":"19","author":"Ramdzan","year":"2017","journal-title":"Cell Rep."},{"key":"10.1016\/j.jmb.2018.03.031_bb0070","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.jmb.2012.01.030","article-title":"Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence","volume":"421","author":"Wetzel","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0075","doi-asserted-by":"crossref","first-page":"31739","DOI":"10.1074\/jbc.M112.353839","article-title":"Structural features and domain organization of huntingtin fibrils","volume":"287","author":"Bugg","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0080","doi-asserted-by":"crossref","first-page":"17451","DOI":"10.1074\/jbc.M115.655373","article-title":"Structural mechanisms of mutant huntingtin aggregation suppression by the synthetic chaperonin-like CCT5 complex explained by cryoelectron tomography","volume":"290","author":"Darrow","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0085","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.2018.03.031_bb0090","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1021\/jacs.6b10893","article-title":"Structure and dynamics of the huntingtin exon-1 n-terminus: a solution NMR perspective","volume":"139","author":"Baias","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0095","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/S0014-5793(02)02335-9","article-title":"Solution structure of polyglutamine tracts in GST\u2013polyglutamine fusion proteins","volume":"513","author":"Masino","year":"2002","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jmb.2018.03.031_bb0100","doi-asserted-by":"crossref","first-page":"1205","DOI":"10.1016\/j.str.2009.08.002","article-title":"Secondary structure of Huntingtin amino-terminal region","volume":"17","author":"Kim","year":"2009","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2018.03.031_bb0105","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/nature25502","article-title":"The cryo-electron microscopy structure of huntingtin","volume":"555","author":"Guo","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2018.03.031_bb0110","doi-asserted-by":"crossref","first-page":"14456","DOI":"10.1021\/jacs.7b06659","article-title":"Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths","volume":"139","author":"Warner","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0115","doi-asserted-by":"crossref","first-page":"4215","DOI":"10.1093\/hmg\/ddt273","article-title":"Linear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10","volume":"22","author":"Klein","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2018.03.031_bb0120","doi-asserted-by":"crossref","first-page":"2507","DOI":"10.1016\/j.jmb.2015.05.023","article-title":"Anti-polyQ antibodies recognize a short polyQ stretch in both normal and mutant huntingtin exon 1","volume":"427","author":"Owens","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0125","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2018.03.031_bb0130","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1017\/S0033583500005217","article-title":"Hydrogen exchange and structural dynamics of proteins and nucleic acids","author":"Englander","year":"1983","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.jmb.2018.03.031_bb0135","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.jmb.2008.09.026","article-title":"Atomistic simulations of the effects of polyglutamine chain length and solvent quality on conformational equilibria and spontaneous homodimerization","volume":"384","author":"Vitalis","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0140","doi-asserted-by":"crossref","DOI":"10.1063\/1.4812791","article-title":"A quantitative measure for protein conformational heterogeneity","volume":"139","author":"Lyle","year":"2013","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.jmb.2018.03.031_bb0145","doi-asserted-by":"crossref","first-page":"16764","DOI":"10.1073\/pnas.0608175103","article-title":"Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions","volume":"103","author":"Crick","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0150","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.sbi.2015.03.008","article-title":"Relating sequence encoded information to form and function of intrinsically disordered proteins","volume":"32","author":"Das","year":"2015","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0155","doi-asserted-by":"crossref","first-page":"20075","DOI":"10.1073\/pnas.1320626110","article-title":"Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation","volume":"110","author":"Crick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0160","doi-asserted-by":"crossref","first-page":"12605","DOI":"10.1073\/pnas.0900678106","article-title":"Single homopolypeptide chains collapse into mechanically rigid conformations","volume":"106","author":"Dougan","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0165","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.jmb.2009.08.034","article-title":"Examining polyglutamine peptide length: a connection between collapsed conformations and increased aggregation","volume":"393","author":"Walters","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0170","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1002\/prot.20761","article-title":"Characterizing the conformational ensemble of monomeric polyglutamine","volume":"63","author":"Wang","year":"2006","journal-title":"Proteins Struct. Funct. Bioinforma."},{"key":"10.1016\/j.jmb.2018.03.031_bb0175","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.bpj.2009.05.003","article-title":"Thermodynamics of beta-sheet formation in polyglutamine","volume":"97","author":"Vitalis","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2018.03.031_bb0180","doi-asserted-by":"crossref","first-page":"8820","DOI":"10.1021\/jacs.7b00838","article-title":"Emerging \u03b2-sheet rich conformations in supercompact huntingtin exon-1 mutant structures","volume":"139","author":"Kang","year":"2017","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0185","doi-asserted-by":"crossref","first-page":"2984","DOI":"10.1021\/ja512062h","article-title":"Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation","volume":"137","author":"Holehouse","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0190","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1146\/annurev.biophys.27.1.357","article-title":"The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins","volume":"27","author":"Gardner","year":"1998","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.jmb.2018.03.031_bb0195","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/BF00175245","article-title":"The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data","volume":"4","author":"Wishart","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2018.03.031_bb0200","doi-asserted-by":"crossref","first-page":"6201","DOI":"10.1021\/bi960157x","article-title":"The three-dimensional solution structure of the SH2 domain from p55blk kinase","volume":"35","author":"Metzler","year":"1996","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.jmb.2018.03.031_bb0205","doi-asserted-by":"crossref","first-page":"13818","DOI":"10.1021\/bi00213a010","article-title":"Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern","volume":"32","author":"Metzler","year":"1993","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.jmb.2018.03.031_bb0210","doi-asserted-by":"crossref","first-page":"11597","DOI":"10.1021\/jp206373g","article-title":"Secondary structures of native and pathogenic huntingtin N-terminal fragments","volume":"115","author":"Dlugosz","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jmb.2018.03.031_bb0215","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1093\/hmg\/ddm217","article-title":"Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity","volume":"16","author":"Atwal","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2018.03.031_bb0220","doi-asserted-by":"crossref","first-page":"45996","DOI":"10.1074\/jbc.M106777200","article-title":"Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein","author":"Bussell","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0225","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/j.jmb.2007.07.008","article-title":"Residual structure, backbone dynamics, and interactions within the synuclein family","volume":"372","author":"Sung","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0230","doi-asserted-by":"crossref","first-page":"25090","DOI":"10.1074\/jbc.M115.658583","article-title":"Phosphorylation-induced conformational ensemble switching in an intrinsically disordered cancer\/testis antigen","volume":"290","author":"He","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0235","doi-asserted-by":"crossref","first-page":"15323","DOI":"10.1021\/jacs.6b10272","article-title":"Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation","volume":"138","author":"Martin","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0240","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1002\/jcc.21005","article-title":"ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions","volume":"30","author":"Vitalis","year":"2009","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0255","doi-asserted-by":"crossref","first-page":"3734","DOI":"10.1074\/jbc.RA117.000357","article-title":"Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers","volume":"293","author":"Posey","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0260","doi-asserted-by":"crossref","first-page":"21807","DOI":"10.1074\/jbc.M109.084434","article-title":"Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool","volume":"285","author":"Olshina","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0265","doi-asserted-by":"crossref","first-page":"D447","DOI":"10.1093\/nar\/gku1003","article-title":"STRING v10: protein\u2013protein interaction networks, integrated over the tree of life","volume":"43","author":"Szklarczyk","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jmb.2018.03.031_bb0270","doi-asserted-by":"crossref","first-page":"2222","DOI":"10.1002\/jcp.24395","article-title":"FUS\/TLS assembles into stress granules and is a prosurvival factor during hyperosmolar stress","volume":"228","author":"Sama","year":"2013","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0275","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1083\/jcb.201302044","article-title":"Stress granules as crucibles of ALS pathogenesis","volume":"201","author":"Li","year":"2013","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0280","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/j.cell.2012.04.017","article-title":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels","volume":"149","author":"Kato","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2018.03.031_bb0285","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0136362","article-title":"Proteins with intrinsically disordered domains are preferentially recruited to polyglutamine aggregates","volume":"10","author":"Wear","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2018.03.031_bb0290","doi-asserted-by":"crossref","first-page":"14610","DOI":"10.1073\/pnas.1301342110","article-title":"Polyglutamine domain flexibility mediates the proximity between flanking sequences in huntingtin","volume":"110","author":"Caron","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0295","doi-asserted-by":"crossref","first-page":"11884","DOI":"10.1073\/pnas.182276099","article-title":"Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation","volume":"99","author":"Chen","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0300","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.bpc.2011.04.006","article-title":"Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides","volume":"159","author":"Vitalis","year":"2011","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0305","doi-asserted-by":"crossref","first-page":"15197","DOI":"10.1021\/jacs.6b08665","article-title":"The aggregation free energy landscapes of polyglutamine repeats","volume":"138","author":"Chen","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.jmb.2018.03.031_bb0310","doi-asserted-by":"crossref","first-page":"4406","DOI":"10.1073\/pnas.1702237114","article-title":"Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease","volume":"114","author":"Chen","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0315","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1038\/nsmb1215","article-title":"A toxic monomeric conformer of the polyglutamine protein","volume":"14","author":"Nagai","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0320","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.2018.03.031_bb0325","doi-asserted-by":"crossref","first-page":"10887","DOI":"10.1073\/pnas.0409283102","article-title":"Formation of morphologically similar globular aggregates from diverse aggregation-prone proteins in mammalian cells","volume":"102","author":"Mukai","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0330","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1093\/hmg\/ddp467","article-title":"Identical oligomeric and fibrillar structures captured from the brains of R6\/2 and knock-in mouse models of Huntington's disease","volume":"19","author":"Sathasivam","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jmb.2018.03.031_bb0340","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1006\/jmbi.2001.4850","article-title":"Polyglutamine aggregation behavior in vitro supports a recruitment mechanism of cytotoxicity","volume":"311","author":"Chen","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0345","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/j.jmb.2007.05.028","article-title":"Pathogenic and non-pathogenic polyglutamine tracts have similar structural properties: towards a length-dependent toxicity gradient","volume":"371","author":"Klein","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0350","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1016\/j.neuron.2012.05.009","article-title":"Sustained therapeutic reversal of Huntington's disease by transient repression of huntingtin synthesis","volume":"74","author":"Kordasiewicz","year":"2012","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2018.03.031_bb0355","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2018.03.031_bb0360","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev-biochem-060614-034325","article-title":"Biochemical properties and biological functions of FET proteins","volume":"84","author":"Schwartz","year":"2015","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jmb.2018.03.031_bb0365","doi-asserted-by":"crossref","first-page":"5239","DOI":"10.1073\/pnas.77.9.5239","article-title":"Ligand-linked phase changes in a biological system: applications to sickle cell hemoglobin","volume":"77","author":"Wyman","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jmb.2018.03.031_bb0370","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/nsmb.1992","article-title":"Critical nucleus size for disease-related polyglutamine aggregation is repeat-length dependent","volume":"18","author":"Kar","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0375","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/j.pep.2005.01.016","article-title":"Protein production by auto-induction in high density shaking cultures","volume":"41","author":"Studier","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.jmb.2018.03.031_bb0380","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1023\/A:1008222131470","article-title":"An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli","volume":"11","author":"Cai","year":"1998","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2018.03.031_bb0385","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1007\/978-1-59745-196-3_19","article-title":"Expression and purification of soluble His6-tagged TEV protease","volume":"498","author":"Tropea","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0390","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.ijms.2010.07.030","article-title":"MSTools\u2014Web based application for visualization and presentation of HXMS data","volume":"302","author":"Kavan","year":"2011","journal-title":"Int. J. Mass Spectrom."},{"key":"10.1016\/j.jmb.2018.03.031_bb0395","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2018.03.031_bb0400","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","article-title":"NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy","volume":"31","author":"Lee","year":"2015","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2018.03.031_bb0405","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1000307","article-title":"Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy","volume":"5","author":"Bahrami","year":"2009","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0410","doi-asserted-by":"crossref","first-page":"2085","DOI":"10.1093\/bioinformatics\/btp345","article-title":"PINE-SPARKY: graphical interface for evaluating automated probabilistic peak assignments in protein NMR spectroscopy","volume":"25","author":"Lee","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jmb.2018.03.031_bb0415","doi-asserted-by":"crossref","first-page":"5984","DOI":"10.1021\/bi00185a040","article-title":"Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation","volume":"33","author":"Farrow","year":"1994","journal-title":"Biochemistry (Mosc)"},{"key":"10.1016\/j.jmb.2018.03.031_bb0420","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms11344","article-title":"The complex binding mode of the peptide hormone H2 relaxin to its receptor RXFP1","volume":"7","author":"Sethi","year":"2016","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jmb.2018.03.031_bb0425","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s10858-007-9213-3","article-title":"Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor","volume":"40","author":"d'Auvergne","year":"2008","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.jmb.2018.03.031_bb0430","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.jmb.2011.12.043","article-title":"N-terminal segments modulate the alpha-helical propensities of the intrinsically disordered basic regions of bZIP proteins","volume":"416","author":"Das","year":"2012","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0435","doi-asserted-by":"crossref","first-page":"6862","DOI":"10.1021\/jp212637r","article-title":"Improved atomistic Monte Carlo simulations demonstrate that poly-L-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks","volume":"116","author":"Radhakrishnan","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jmb.2018.03.031_bb0440","doi-asserted-by":"crossref","first-page":"4468","DOI":"10.4049\/jimmunol.1502062","article-title":"Characterization of the antigen processing machinery and endogenous peptide presentation of a bat MHC class i molecule","volume":"196","author":"Wynne","year":"2016","journal-title":"J. Immunol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0445","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1038\/nbt.1511","article-title":"MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification","volume":"26","author":"Cox","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.jmb.2018.03.031_bb0450","doi-asserted-by":"crossref","first-page":"2513","DOI":"10.1074\/mcp.M113.031591","article-title":"Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ","volume":"13","author":"Cox","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.jmb.2018.03.031_bb0455","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nmeth1019","article-title":"Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry","volume":"4","author":"Elias","year":"2007","journal-title":"Nat. Methods"},{"key":"10.1016\/j.jmb.2018.03.031_bb0460","doi-asserted-by":"crossref","first-page":"D1063","DOI":"10.1093\/nar\/gks1262","article-title":"The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013","volume":"41","author":"Vizca\u00edno","year":"2013","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283618301827?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283618301827?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T22:02:41Z","timestamp":1762207361000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283618301827"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,5]]},"references-count":89,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2018,5]]}},"alternative-id":["S0022283618301827"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2018.03.031","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/179663","asserted-by":"object"}]},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2018,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2018.03.031","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 The Author(s). Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}]}}