{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T08:20:23Z","timestamp":1793866823478,"version":"4.6.1"},"reference-count":71,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2025,1,7]],"date-time":"2025-01-07T00:00:00Z","timestamp":1736208000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Mol. Biosci."],"abstract":"<jats:p>Huntington\u2019s disease (HD) is primarily caused by the aberrant aggregation of the N-terminal exon 1 fragment of mutant huntingtin protein (mHttex1) with expanded polyglutamine (polyQ) repeats in neurons. The first 17 amino acids of the N-terminus of Httex1 (N17 domain) immediately preceding the polyQ repeat domain are evolutionarily conserved across vertebrates and play multifaceted roles in the pathogenesis of HD. Due to its amphipathic helical properties, the N17 domain, both alone and when membrane-associated, promotes mHttEx1 aggregation. Diverse post-translational modifications (PTMs) in the N17 domain alter the aggregation state, thus modulating the cellular toxicity of mHttex1. Furthermore, the N17 domain serves as a nuclear export signal (NES) and mediates the cytoplasmic localization of mHttex1. This review summarizes the four main roles of the N17 domain in regulating HD pathology and discusses potential therapeutic approaches targeting this N17 domain to mitigate HD progression.<\/jats:p>","DOI":"10.3389\/fmolb.2024.1527313","type":"journal-article","created":{"date-parts":[[2025,1,7]],"date-time":"2025-01-07T01:51:22Z","timestamp":1736214682000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":8,"title":["The N17 domain of huntingtin as a multifaceted player in Huntington\u2019s disease"],"prefix":"10.3389","volume":"11","author":[{"given":"Hyunju","family":"Cho","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2025,1,7]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"29427","DOI":"10.1074\/jbc.M109.013193","article-title":"Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity","volume":"284","author":"Aiken","year":"2009","journal-title":"J. Biol. Chem."},{"key":"B2","doi-asserted-by":"publisher","first-page":"453","DOI":"10.1038\/nchembio.582","article-title":"Kinase inhibitors modulate huntingtin cell localization and toxicity","volume":"7","author":"Atwal","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"B3","doi-asserted-by":"publisher","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":"B4","doi-asserted-by":"publisher","first-page":"15005","DOI":"10.1038\/nrdp.2015.5","article-title":"Huntington disease","volume":"1","author":"Bates","year":"2015","journal-title":"Nat. Rev. Dis. Prim."},{"key":"B5","doi-asserted-by":"publisher","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":"B\u00e4uerlein","year":"2017","journal-title":"Cell."},{"key":"B6","doi-asserted-by":"publisher","first-page":"3067","DOI":"10.1021\/acs.jpcb.1c10254","article-title":"Physicochemical properties altered by the tail group of lipid membranes influence huntingtin aggregation and lipid binding","volume":"126","author":"Beasley","year":"2022","journal-title":"J. Phys. Chem. B"},{"key":"B7","doi-asserted-by":"publisher","first-page":"183497","DOI":"10.1016\/j.bbamem.2020.183497","article-title":"Lipid headgroups alter huntingtin aggregation on membranes","volume":"1863","author":"Beasley","year":"2021","journal-title":"Biochim. Biophys. Acta Biomembr."},{"key":"B8","doi-asserted-by":"publisher","first-page":"E7081-E7090","DOI":"10.1073\/pnas.1801772115","article-title":"N6-Furfuryladenine is protective in Huntington\u2019s disease models by signaling huntingtin phosphorylation","volume":"115","author":"Bowie","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B9","doi-asserted-by":"publisher","first-page":"3763","DOI":"10.1093\/hmg\/ddx260","article-title":"Protein phosphatase 1 regulates huntingtin exon 1 aggregation and toxicity","volume":"26","author":"Branco-Santos","year":"2017","journal-title":"Hum. Mol. Genet."},{"key":"B10","doi-asserted-by":"publisher","first-page":"E10809-E10818","DOI":"10.1073\/pnas.1705372114","article-title":"Phosphorylation of huntingtin at residue T3 is decreased in Huntington\u2019s disease and modulates mutant huntingtin protein conformation","volume":"114","author":"Cariulo","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B11","doi-asserted-by":"publisher","first-page":"e202302006","DOI":"10.26508\/lsa.202302006","article-title":"IKBKB reduces huntingtin aggregation by phosphorylating serine 13 via a non-canonical IKK pathway","volume":"6","author":"Cariulo","year":"2023","journal-title":"Life Sci. Alliance"},{"key":"B12","doi-asserted-by":"publisher","first-page":"2355","DOI":"10.1021\/bi401619q","article-title":"Curvature enhances binding and aggregation of huntingtin at lipid membranes","volume":"53","author":"Chaibva","year":"2014","journal-title":"Biochemistry"},{"key":"B13","doi-asserted-by":"publisher","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":"B14","doi-asserted-by":"publisher","first-page":"5202","DOI":"10.1002\/anie.201611750","article-title":"Mutant Exon1 huntingtin aggregation is regulated by T3 phosphorylation-induced structural changes and crosstalk between T3 phosphorylation and acetylation at K6","volume":"56","author":"Chiki","year":"2017","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"B15","doi-asserted-by":"publisher","first-page":"M111.009829","DOI":"10.1074\/mcp.M111.009829","article-title":"Mass spectrometric identification of novel lysine acetylation sites in huntingtin","volume":"10","author":"Cong","year":"2011","journal-title":"Mol. and Cell. Proteomics"},{"key":"B16","doi-asserted-by":"publisher","first-page":"198","DOI":"10.1038\/ng1503","article-title":"Polyglutamine expansion of huntingtin impairs its nuclear export","volume":"37","author":"Cornett","year":"2005","journal-title":"Nat. Genet."},{"key":"B17","doi-asserted-by":"publisher","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":"B18","doi-asserted-by":"publisher","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":"B19","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1038\/s41594-023-00920-0","article-title":"The structure of pathogenic huntingtin exon 1 defines the bases of its aggregation propensity","volume":"30","author":"Elena-Real","year":"2023","journal-title":"Nat. Struct. Mol. Biol."},{"key":"B20","doi-asserted-by":"publisher","first-page":"1471","DOI":"10.1126\/science.1124514","article-title":"Progressive disruption of cellular protein folding in models of polyglutamine diseases","volume":"311","author":"Gidalevitz","year":"2006","journal-title":"Science"},{"key":"B21","doi-asserted-by":"publisher","first-page":"726","DOI":"10.1016\/j.neuron.2015.01.008","article-title":"N17 Modifies mutant Huntingtin nuclear pathogenesis and severity of disease in HD BAC transgenic mice","volume":"85","author":"Gu","year":"2015","journal-title":"Neuron"},{"key":"B22","doi-asserted-by":"publisher","first-page":"828","DOI":"10.1016\/j.neuron.2009.11.020","article-title":"Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice","volume":"64","author":"Gu","year":"2009","journal-title":"Neuron"},{"key":"B23","doi-asserted-by":"publisher","first-page":"109","DOI":"10.1038\/35039051","article-title":"Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease","volume":"1","author":"Gusella","year":"2000","journal-title":"Nat. Rev. Neurosci."},{"key":"B24","doi-asserted-by":"publisher","first-page":"e104671","DOI":"10.15252\/embj.2020104671","article-title":"TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington\u2019s disease models","volume":"39","author":"Hegde","year":"2020","journal-title":"EMBO J."},{"key":"B25","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1038\/s41586-022-05575-3","article-title":"An atlas of substrate specificities for the human serine\/threonine kinome","volume":"613","author":"Johnson","year":"2023","journal-title":"Nature"},{"key":"B26","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"B27","doi-asserted-by":"publisher","first-page":"7268","DOI":"10.1523\/JNEUROSCI.20-19-07268.2000","article-title":"Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy","volume":"20","author":"Kegel","year":"2000","journal-title":"J. Neurosci."},{"key":"B28","doi-asserted-by":"publisher","first-page":"951","DOI":"10.1016\/j.molcel.2016.07.022","article-title":"Soluble oligomers of PolyQ-expanded huntingtin target a multiplicity of key cellular factors","volume":"63","author":"Kim","year":"2016","journal-title":"Mol. Cell."},{"key":"B29","doi-asserted-by":"publisher","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\u2019s 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":"B30","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.tcb.2005.01.005","article-title":"Leucine-rich nuclear-export signals: born to be weak","volume":"15","author":"Kutay","year":"2005","journal-title":"Trends Cell. Biol."},{"key":"B31","doi-asserted-by":"publisher","first-page":"4764","DOI":"10.1073\/pnas.071058398","article-title":"Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington\u2019s disease","volume":"98","author":"Lecerf","year":"2001","journal-title":"Proc. Natl. Acad. Sci."},{"key":"B32","doi-asserted-by":"publisher","first-page":"1602","DOI":"10.1093\/hmg\/ddu574","article-title":"Disruption of the nuclear membrane by perinuclear inclusions of mutant huntingtin causes cell-cycle re-entry and striatal cell death in mouse and cell models of Huntington\u2019s disease","volume":"24","author":"Liu","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"B33","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1016\/s1097-2765(02)00602-0","article-title":"Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions","volume":"10","author":"Lunkes","year":"2002","journal-title":"Mol. Cell."},{"key":"B34","doi-asserted-by":"publisher","first-page":"1383","DOI":"10.1093\/hmg\/dds554","article-title":"The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal","volume":"22","author":"Maiuri","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"B35","doi-asserted-by":"publisher","first-page":"2085","DOI":"10.1074\/jbc.REV118.002810","article-title":"Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones","volume":"294","author":"Mayer","year":"2019","journal-title":"J. Biol. Chem."},{"key":"B36","doi-asserted-by":"publisher","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":"","journal-title":"Biophys. J."},{"key":"B37","doi-asserted-by":"publisher","first-page":"847","DOI":"10.1021\/bi301325q","article-title":"Membrane interactions of the amphipathic amino terminus of huntingtin","volume":"52","author":"Michalek","year":"","journal-title":"Biochemistry"},{"key":"B38","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jmb.2012.09.011","article-title":"Serine phosphorylation suppresses huntingtin amyloid accumulation by altering protein aggregation properties","volume":"424","author":"Mishra","year":"2012","journal-title":"J. Mol. Biol."},{"key":"B39","doi-asserted-by":"publisher","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":"B40","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1038\/s41598-017-01510-z","article-title":"The pathogenic exon 1 HTT protein is produced by incomplete splicing in Huntington\u2019s disease patients","volume":"7","author":"Neueder","year":"2017","journal-title":"Sci. Rep."},{"key":"B41","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1016\/j.celrep.2013.06.034","article-title":"SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation","volume":"4","author":"O\u2019Rourke","year":"2013","journal-title":"Cell. Rep."},{"key":"B42","doi-asserted-by":"publisher","first-page":"2783","DOI":"10.1523\/JNEUROSCI.0106-08.2008","article-title":"N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking","volume":"28","author":"Orr","year":"2008","journal-title":"J. Neurosci."},{"key":"B43","doi-asserted-by":"publisher","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. Biol. Chem."},{"key":"B44","doi-asserted-by":"publisher","first-page":"731","DOI":"10.1038\/nn884","article-title":"Early mitochondrial calcium defects in Huntington\u2019s disease are a direct effect of polyglutamines","volume":"5","author":"Panov","year":"2002","journal-title":"Nat. Neurosci."},{"key":"B45","doi-asserted-by":"publisher","first-page":"e2107187119","DOI":"10.1073\/pnas.2107187119","article-title":"Deletion of SUMO1 attenuates behavioral and anatomical deficits by regulating autophagic activities in Huntington disease","volume":"119","author":"Ram\u00edrez-Jarqu\u00edn","year":"2022","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"B46","doi-asserted-by":"publisher","first-page":"6579","DOI":"10.1038\/s41467-021-26684-z","article-title":"Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties","volume":"12","author":"Riguet","year":"2021","journal-title":"Nat. Commun."},{"key":"B47","doi-asserted-by":"publisher","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":"B48","doi-asserted-by":"publisher","first-page":"2366","DOI":"10.1073\/pnas.1221891110","article-title":"Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease","volume":"110","author":"Sathasivam","year":"2013","journal-title":"Proc. Natl. Acad. Sci."},{"key":"B49","doi-asserted-by":"publisher","first-page":"910","DOI":"10.1016\/j.neuron.2016.02.003","article-title":"The biology of huntingtin","volume":"89","author":"Saudou","year":"2016","journal-title":"Neuron"},{"key":"B50","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1016\/s0092-8674(00)80514-0","article-title":"Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo","volume":"90","author":"Scherzinger","year":"1997","journal-title":"Cell."},{"key":"B51","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1021\/acschemneuro.9b00509","article-title":"SUMOylation prevents huntingtin fibrillization and localization onto lipid membranes","volume":"11","author":"Sedighi","year":"2020","journal-title":"ACS Chem. Neurosci."},{"key":"B52","doi-asserted-by":"publisher","first-page":"e00710","DOI":"10.7554\/eLife.00710","article-title":"TRiC\u2019s tricks inhibit huntingtin aggregation","volume":"2","author":"Shahmoradian","year":"2013","journal-title":"eLife"},{"key":"B53","doi-asserted-by":"publisher","first-page":"e18065","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":"B54","doi-asserted-by":"publisher","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. Am. Chem. Soc."},{"key":"B55","doi-asserted-by":"publisher","first-page":"3654","DOI":"10.1093\/hmg\/ddw212","article-title":"An enhanced Q175 knock-in mouse model of Huntington disease with higher mutant huntingtin levels and accelerated disease phenotypes","volume":"25","author":"Southwell","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"B56","doi-asserted-by":"publisher","first-page":"100","DOI":"10.1126\/science.1092194","article-title":"SUMO modification of Huntingtin and Huntington\u2019s disease pathology","volume":"304","author":"Steffan","year":"2004","journal-title":"Science"},{"key":"B57","doi-asserted-by":"publisher","first-page":"1327","DOI":"10.1126\/science.1172871","article-title":"Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity","volume":"324","author":"Subramaniam","year":"2009","journal-title":"Science"},{"key":"B58","doi-asserted-by":"publisher","first-page":"870","DOI":"10.1111\/j.1471-4159.2005.03620.x","article-title":"Interaction of huntingtin fragments with brain membranes--clues to early dysfunction in Huntington\u2019s disease","volume":"96","author":"Suopanki","year":"2006","journal-title":"J. Neurochem."},{"key":"B59","doi-asserted-by":"publisher","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":"B60","doi-asserted-by":"publisher","first-page":"1570","DOI":"10.1016\/j.str.2019.08.003","article-title":"Structure of membrane-bound huntingtin exon 1 reveals membrane interaction and aggregation mechanisms","volume":"27","author":"Tao","year":"2019","journal-title":"Structure"},{"key":"B61","doi-asserted-by":"publisher","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":"B62","doi-asserted-by":"publisher","first-page":"1083","DOI":"10.1083\/jcb.200909067","article-title":"IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome","volume":"187","author":"Thompson","year":"2009","journal-title":"J. Cell. Biol."},{"key":"B63","doi-asserted-by":"publisher","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":"B64","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/nrm2330","article-title":"Membrane lipids: where they are and how they behave","volume":"9","author":"van Meer","year":"2008","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"B65","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1186\/s13024-015-0063-2","article-title":"The N17 domain mitigates nuclear toxicity in a novel zebrafish Huntington\u2019s disease model","volume":"10","author":"Veldman","year":"2015","journal-title":"Mol. Neurodegener."},{"key":"B66","doi-asserted-by":"publisher","first-page":"167222","DOI":"10.1016\/j.jmb.2021.167222","article-title":"The Nt17 domain and its helical conformation regulate the aggregation, cellular properties and neurotoxicity of mutant huntingtin exon 1","volume":"433","author":"Vieweg","year":"2021","journal-title":"J. Mol. Biol."},{"key":"B67","doi-asserted-by":"publisher","first-page":"1393","DOI":"10.1091\/mbc.12.5.1393","article-title":"Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation","volume":"12","author":"Waelter","year":"2001","journal-title":"Mol. Biol. Cell."},{"key":"B68","doi-asserted-by":"publisher","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":"B69","doi-asserted-by":"publisher","first-page":"1174","DOI":"10.1038\/s41586-024-07407-y","article-title":"The intrinsic substrate specificity of the human tyrosine kinome","volume":"629","author":"Yaron-Barir","year":"2024","journal-title":"Nature"},{"key":"B70","doi-asserted-by":"publisher","first-page":"2193","DOI":"10.1523\/JNEUROSCI.23-06-02193.2003","article-title":"Mutant huntingtin causes context-dependent neurodegeneration in mice with Huntington\u2019s disease","volume":"23","author":"Yu","year":"2003","journal-title":"J. Neurosci."},{"key":"B71","doi-asserted-by":"publisher","first-page":"6063","DOI":"10.1074\/jbc.M112.413575","article-title":"An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1","volume":"288","author":"Zheng","year":"2013","journal-title":"J. Biol. Chem."}],"container-title":["Frontiers in Molecular Biosciences"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2024.1527313\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,1,7]],"date-time":"2025-01-07T01:51:24Z","timestamp":1736214684000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fmolb.2024.1527313\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1,7]]},"references-count":71,"alternative-id":["10.3389\/fmolb.2024.1527313"],"URL":"https:\/\/doi.org\/10.3389\/fmolb.2024.1527313","relation":{},"ISSN":["2296-889X"],"issn-type":[{"value":"2296-889X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,1,7]]},"article-number":"1527313"}}