{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T17:52:06Z","timestamp":1789581126516,"version":"build-2803163510"},"reference-count":86,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T00:00:00Z","timestamp":1638316800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,10,28]],"date-time":"2021-10-28T00:00:00Z","timestamp":1635379200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 GM060293"],"award-info":[{"award-number":["R01 GM060293"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35 GM118090"],"award-info":[{"award-number":["R35 GM118090"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T32 GM071339"],"award-info":[{"award-number":["T32 GM071339"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2021,12]]},"DOI":"10.1016\/j.jbc.2021.101363","type":"journal-article","created":{"date-parts":[[2021,10,31]],"date-time":"2021-10-31T18:21:12Z","timestamp":1635704472000},"page":"101363","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":32,"title":["N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate"],"prefix":"10.1016","volume":"297","author":[{"given":"Leah","family":"Gottlieb","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lin","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Shorter","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronen","family":"Marmorstein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2021.101363_bib1","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/B978-0-444-52014-2.00003-3","article-title":"Molecular biology of Huntington's disease","volume":"100","author":"McFarland","year":"2011","journal-title":"Handb. Clin. Neurol."},{"key":"10.1016\/j.jbc.2021.101363_bib2","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1016\/j.jmb.2013.01.016","article-title":"beta-hairpin-mediated nucleation of polyglutamine amyloid formation","volume":"425","author":"Kar","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib3","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.jbc.2021.101363_bib4","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3389\/fnins.2017.00145","article-title":"Chaperones in polyglutamine aggregation: Beyond the Q-stretch","volume":"11","author":"Kuiper","year":"2017","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.jbc.2021.101363_bib5","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","article-title":"A\u00a0novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington\u2019s disease chromosomes","volume":"72","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib6","first-page":"16","article-title":"Phenotypic characterization of individuals with 30\u201340 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36\u201339 repeats","volume":"59","author":"Rubinsztein","year":"1996","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib7","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1002\/mds.21195","article-title":"Autopsy-proven Huntington's disease with 29 trinucleotide repeats","volume":"22","author":"Kenney","year":"2007","journal-title":"Mov. Disord."},{"key":"10.1016\/j.jbc.2021.101363_bib8","first-page":"852","article-title":"Huntington disease without CAG expansion: Phenocopies or errors in assignment?","volume":"54","author":"Andrew","year":"1994","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib9","doi-asserted-by":"crossref","DOI":"10.1136\/bmjno-2019-000027","article-title":"Case report and literature review of Huntington disease with intermediate CAG expansion","volume":"2","author":"Jevtic","year":"2020","journal-title":"BMJ Neurol. Open"},{"key":"10.1016\/j.jbc.2021.101363_bib10","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.jns.2016.02.030","article-title":"Late onset Huntington's disease with 29 CAG repeat expansion","volume":"363","author":"Garcia-Ruiz","year":"2016","journal-title":"J.\u00a0Neurol. Sci."},{"key":"10.1016\/j.jbc.2021.101363_bib11","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.jns.2019.05.010","article-title":"Clinical phenotype in carriers of intermediate alleles in the huntingtin gene","volume":"402","author":"Savitt","year":"2019","journal-title":"J.\u00a0Neurol. Sci."},{"key":"10.1016\/j.jbc.2021.101363_bib12","doi-asserted-by":"crossref","first-page":"1794","DOI":"10.1002\/mds.21820","article-title":"Re: Autopsy-proven Huntington's disease with 29 trinucleotide repeats","volume":"23","author":"Semaka","year":"2008","journal-title":"Mov. Disord."},{"key":"10.1016\/j.jbc.2021.101363_bib13","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.jns.2016.07.021","article-title":"Reply: Late onset Huntington's disease with 29 CAG repeat expansion","volume":"368","author":"Oosterloo","year":"2016","journal-title":"J.\u00a0Neurol. Sci."},{"key":"10.1016\/j.jbc.2021.101363_bib14","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/j.neuron.2020.11.005","article-title":"Pathogenic huntingtin repeat expansions in patients with frontotemporal dementia and amyotrophic lateral sclerosis","volume":"109","author":"Dewan","year":"2020","journal-title":"Neuron"},{"key":"10.1016\/j.jbc.2021.101363_bib15","doi-asserted-by":"crossref","first-page":"12784","DOI":"10.1073\/pnas.221451398","article-title":"Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis","volume":"98","author":"Kim","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101363_bib16","doi-asserted-by":"crossref","first-page":"2582","DOI":"10.1038\/s41467-020-16318-1","article-title":"Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form","volume":"11","author":"Yang","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101363_bib17","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1006\/exnr.1998.7005","article-title":"Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein","volume":"156","author":"Sieradzan","year":"1999","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.jbc.2021.101363_bib18","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.cell.2017.08.009","article-title":"In situ architecture and cellular interactions of PolyQ inclusions","volume":"171","author":"Bauerlein","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib19","doi-asserted-by":"crossref","first-page":"1097","DOI":"10.1083\/jcb.141.5.1097","article-title":"The influence of huntingtin protein size on nuclear localization and cellular toxicity","volume":"141","author":"Hackam","year":"1998","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib20","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.1093\/hmg\/11.23.2905","article-title":"Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells","volume":"11","author":"Yang","year":"2002","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib21","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/S0092-8674(00)81369-0","article-title":"Exon 1 of the HD gene with an expanded CAG repeat is sufficient to cause a progressive neurological phenotype in transgenic mice","volume":"87","author":"Mangiarini","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib22","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1021\/acs.biochem.9b00689","article-title":"Nucleation inhibition of huntingtin protein (htt) by polyproline PPII helices: A potential interaction with the N-terminal alpha-helical region of Htt","volume":"59","author":"Arndt","year":"2020","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101363_bib23","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.str.2020.04.008","article-title":"Flanking regions determine the structure of the poly-glutamine in huntingtin through mechanisms common among glutamine-rich human proteins","volume":"28","author":"Urbanek","year":"2020","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2021.101363_bib24","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1093\/hmg\/ddl440","article-title":"The first 17 amino acids of huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis","volume":"16","author":"Rockabrand","year":"2007","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib25","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.jbc.2021.101363_bib26","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1515\/bmc-2015-0001","article-title":"The emerging role of the first 17 amino acids of huntingtin in Huntington's disease","volume":"6","author":"Arndt","year":"2015","journal-title":"Biomol. Concepts"},{"key":"10.1016\/j.jbc.2021.101363_bib27","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1038\/nsmb.1570","article-title":"Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism","volume":"16","author":"Thakur","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib28","doi-asserted-by":"crossref","first-page":"4558","DOI":"10.1021\/ja110715f","article-title":"The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils","volume":"133","author":"Sivanandam","year":"2011","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2021.101363_bib29","doi-asserted-by":"crossref","first-page":"11045","DOI":"10.1073\/pnas.0604547103","article-title":"Flanking sequences profoundly alter polyglutamine toxicity in yeast","volume":"103","author":"Duennwald","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101363_bib30","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.jmb.2011.12.010","article-title":"Slow amyloid nucleation via alpha-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments","volume":"415","author":"Jayaraman","year":"2012","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib31","doi-asserted-by":"crossref","first-page":"2597","DOI":"10.1074\/jbc.M117.813667","article-title":"The 17-residue-long N terminus in huntingtin controls stepwise aggregation in solution and on membranes via different mechanisms","volume":"293","author":"Pandey","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib32","doi-asserted-by":"crossref","first-page":"4722","DOI":"10.1016\/j.jmb.2020.06.021","article-title":"Protofilament structure and supramolecular polymorphism of aggregated mutant huntingtin exon 1","volume":"432","author":"Boatz","year":"2020","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib33","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1016\/j.molcel.2019.03.012","article-title":"Dual role of ribosome-binding domain of NAC as a potent suppressor of protein aggregation and aging-related proteinopathies","volume":"74","author":"Shen","year":"2019","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib34","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.18065","article-title":"Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract","volume":"5","author":"Shen","year":"2016","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2021.101363_bib35","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1038\/nsmb.1700","article-title":"The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation","volume":"16","author":"Tam","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib36","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib37","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1093\/hmg\/7.9.1463","article-title":"Huntingtin interacts with a family of WW domain proteins","volume":"7","author":"Faber","year":"1998","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib38","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.bpj.2016.06.018","article-title":"Acetylation within the first 17 residues of huntingtin exon 1 alters aggregation and lipid binding","volume":"111","author":"Chaibva","year":"2016","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2021.101363_bib39","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.cell.2009.03.018","article-title":"Acetylation targets mutant huntingtin to autophagosomes for degradation","volume":"137","author":"Jeong","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib40","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1038\/nn1702","article-title":"Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function","volume":"9","author":"Yanai","year":"2006","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.jbc.2021.101363_bib41","doi-asserted-by":"crossref","first-page":"18540","DOI":"10.1074\/jbc.RA118.004621","article-title":"N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting","volume":"293","author":"DeGuire","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib42","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1126\/science.1092194","article-title":"SUMO modification of Huntingtin and Huntington's disease pathology","volume":"304","author":"Steffan","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.jbc.2021.101363_bib43","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1038\/s41598-018-19538-0","article-title":"Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies","volume":"8","author":"Juenemann","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2021.101363_bib44","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1093\/hmg\/ddu544","article-title":"Aged monkey brains reveal the role of ubiquitin-conjugating enzyme UBE2N in the synaptosomal accumulation of mutant huntingtin","volume":"24","author":"Yin","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib45","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fnmol.2015.00001","article-title":"Detection of ubiquitinated huntingtin species in intracellular aggregates","volume":"8","author":"Juenemann","year":"2015","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.jbc.2021.101363_bib46","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0041450","article-title":"Temporal separation of aggregation and ubiquitination during early inclusion formation in transgenic mice carrying the Huntington's disease mutation","volume":"7","author":"Gong","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib47","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/837015","article-title":"The ubiquitin-proteasome system in Huntington's disease: Are proteasomes impaired, initiators of disease, or coming to the rescue?","author":"Schipper-Krom","year":"2012","journal-title":"Biochem. Res. Int."},{"key":"10.1016\/j.jbc.2021.101363_bib48","doi-asserted-by":"crossref","first-page":"8157","DOI":"10.1073\/pnas.0901931106","article-title":"Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans","volume":"106","author":"Arnesen","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2021.101363_bib49","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1002169","article-title":"NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation","volume":"7","author":"Van Damme","year":"2011","journal-title":"PLoS Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib50","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.tibs.2020.08.005","article-title":"Protein N-terminal acetylation: Structural basis, mechanism, versatility, and regulation","volume":"46","author":"Deng","year":"2021","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jbc.2021.101363_bib51","doi-asserted-by":"crossref","first-page":"1898","DOI":"10.1128\/MCB.01199-09","article-title":"The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregation","volume":"30","author":"Arnesen","year":"2010","journal-title":"Mol. Cell Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib52","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1021\/acs.biochem.6b00936","article-title":"Proteins containing expanded polyglutamine tracts and neurodegenerative disease","volume":"56","author":"Adegbuyiro","year":"2017","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101363_bib53","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0155747","article-title":"Folding landscape of mutant huntingtin Exon1: Diffusible multimers, oligomers and fibrils, and no detectable monomer","volume":"11","author":"Sahoo","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib54","doi-asserted-by":"crossref","first-page":"11635","DOI":"10.1074\/jbc.M412042200","article-title":"Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes","volume":"280","author":"Jana","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib55","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1007\/s12035-014-8932-1","article-title":"Polyglutamine aggregation in Huntington disease: Does structure determine toxicity?","volume":"52","author":"Hoffner","year":"2015","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.jbc.2021.101363_bib56","article-title":"Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin","volume":"10","author":"Huang","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib57","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1002\/pro.2088","article-title":"N-terminal acetylation of alpha-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer","volume":"21","author":"Kang","year":"2012","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2021.101363_bib58","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0103727","article-title":"N-alpha-acetylation of alpha-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation","volume":"9","author":"Bartels","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib88","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1016\/j.jmb.2018.03.017","article-title":"Self-assembly of mutant Huntingtin exon-1 fragments into large complex fibrillar structures involves nucleated branching","volume":"430","author":"Wagner","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib62","doi-asserted-by":"crossref","first-page":"95","DOI":"10.3389\/fmolb.2019.00095","article-title":"The role of post-translational modifications on the energy landscape of huntingtin N-terminus","volume":"6","author":"Yalinca","year":"2019","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2021.101363_bib63","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1021\/bi301325q","article-title":"Membrane interactions of the amphipathic amino terminus of huntingtin","volume":"52","author":"Michalek","year":"2013","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101363_bib64","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.nbd.2018.08.019","article-title":"Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease","volume":"120","author":"Drombosky","year":"2018","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.jbc.2021.101363_bib65","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.bpj.2013.06.030","article-title":"Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach","volume":"105","author":"Michalek","year":"2013","journal-title":"Biophys. J."},{"key":"10.1016\/j.jbc.2021.101363_bib60","doi-asserted-by":"crossref","DOI":"10.1116\/1.4984009","article-title":"Assembly of Huntingtin headpiece into alpha-helical bundles","volume":"12","author":"Ozgur","year":"2017","journal-title":"Biointerphases"},{"key":"10.1016\/j.jbc.2021.101363_bib66","doi-asserted-by":"crossref","first-page":"3652","DOI":"10.1074\/jbc.M113.512459","article-title":"N-terminal acetylation stabilizes N-terminal helicity in lipid- and micelle-bound alpha-synuclein and increases its affinity for physiological membranes","volume":"289","author":"Dikiy","year":"2014","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib78","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1016\/j.dib.2018.09.026","article-title":"Mass spectrometry data confirming tetrameric alpha-synuclein N-terminal acetylation","volume":"20","author":"Fernandez","year":"2018","journal-title":"Data Brief"},{"key":"10.1016\/j.jbc.2021.101363_bib68","article-title":"Transcription regulation of HYPK by heat shock factor 1","volume":"9","author":"Das","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib69","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0051415","article-title":"Identification of HYPK-interacting proteins reveals involvement of HYPK in regulating cell growth, cell cycle, unfolded protein response and cell death","volume":"7","author":"Choudhury","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2021.101363_bib70","doi-asserted-by":"crossref","first-page":"12556","DOI":"10.1038\/s41598-017-12897-0","article-title":"HSF1-dependent and -independent regulation of the mammalian in\u00a0vivo heat shock response and its impairment in Huntington's disease mouse models","volume":"7","author":"Neueder","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2021.101363_bib71","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.jprot.2015.11.007","article-title":"Differential proteomic and genomic profiling of mouse striatal cell model of Huntington's disease and control; probable implications to the disease biology","volume":"132","author":"Choudhury","year":"2016","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.jbc.2021.101363_bib72","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1016\/j.bbagen.2013.12.006","article-title":"Heat shock transcription factor HSF1 regulates the expression of the Huntingtin-interacting protein HYPK","volume":"1840","author":"Sakurai","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2021.101363_bib73","doi-asserted-by":"crossref","first-page":"14405","DOI":"10.1038\/ncomms14405","article-title":"Abnormal degradation of the neuronal stress-protective transcription factor HSF1 in Huntington's disease","volume":"8","author":"Gomez-Pastor","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101363_bib67","doi-asserted-by":"crossref","first-page":"4383","DOI":"10.1038\/ncomms5383","article-title":"Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding","volume":"5","author":"Holmes","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2021.101363_bib74","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1091\/mbc.e08-04-0436","article-title":"The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype","volume":"20","author":"Pezza","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.jbc.2021.101363_bib75","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1021\/acschemneuro.8b00498","article-title":"Role of Parkinson's disease-linked mutations and N-terminal acetylation on the oligomerization of alpha-synuclein induced by 3,4-dihydroxyphenylacetaldehyde","volume":"10","author":"Lima","year":"2019","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.jbc.2021.101363_bib76","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature10324","article-title":"alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation","volume":"477","author":"Bartels","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2021.101363_bib77","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1016\/j.febslet.2013.02.049","article-title":"Exploring the accessible conformations of N-terminal acetylated alpha-synuclein","volume":"587","author":"Moriarty","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2021.101363_bib79","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3000318","article-title":"Identification of N-linked glycans as specific mediators of neuronal uptake of acetylated alpha-synuclein","volume":"17","author":"Birol","year":"2019","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jbc.2021.101363_bib80","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1093\/hmg\/ddm301","article-title":"HYPK, a Huntingtin interacting protein, reduces aggregates and apoptosis induced by N-terminal Huntingtin with 40 glutamines in Neuro2a cells and exhibits chaperone-like activity","volume":"17","author":"Raychaudhuri","year":"2008","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.jbc.2021.101363_bib81","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1007\/s12038-014-9442-z","article-title":"Conserved C-terminal nascent peptide binding domain of HYPK facilitates its chaperone-like activity","volume":"39","author":"Raychaudhuri","year":"2014","journal-title":"J.\u00a0Biosci."},{"key":"10.1016\/j.jbc.2021.101363_bib82","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.bbrc.2014.11.035","article-title":"Chaperone protein HYPK interacts with the first 17 amino acid region of Huntingtin and modulates mutant HTT-mediated aggregation and cytotoxicity","volume":"456","author":"Choudhury","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2021.101363_bib83","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1021\/acs.biochem.7b00776","article-title":"Disordered nanostructure in huntingtin interacting protein K acts as a stabilizing switch to prevent protein aggregation","volume":"57","author":"Ghosh","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2021.101363_bib84","doi-asserted-by":"crossref","first-page":"328","DOI":"10.2144\/00282rr03","article-title":"Approaches to detecting false positives in yeast two-hybrid systems","volume":"28","author":"Serebriiskii","year":"2000","journal-title":"BioTechniques"},{"key":"10.1016\/j.jbc.2021.101363_bib85","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1093\/nar\/27.4.919","article-title":"Yeast forward and reverse 'n'-hybrid systems","volume":"27","author":"Vidal","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2021.101363_bib86","doi-asserted-by":"crossref","first-page":"37002","DOI":"10.1074\/jbc.M111.282863","article-title":"Structure of a ternary Naa50p (NAT5\/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation","volume":"286","author":"Liszczak","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2021.101363_bib87","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1016\/j.str.2018.04.003","article-title":"Structure of human NatA and its regulation by the huntingtin interacting protein HYPK","volume":"26","author":"Gottlieb","year":"2018","journal-title":"Structure"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821011698?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925821011698?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:08:11Z","timestamp":1758240491000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925821011698"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12]]},"references-count":86,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2021,12]]}},"alternative-id":["S0021925821011698"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101363","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2021,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2021.101363","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"101363"}}