{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,25]],"date-time":"2026-06-25T20:48:16Z","timestamp":1782420496287,"version":"3.54.5"},"reference-count":62,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,4,1]],"date-time":"2026-04-01T00:00:00Z","timestamp":1775001600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100003693","name":"Korea Institute of Science and Technology","doi-asserted-by":"publisher","award":["2E32234"],"award-info":[{"award-number":["2E32234"]}],"id":[{"id":"10.13039\/501100003693","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003693","name":"Korea Institute of Science and Technology","doi-asserted-by":"publisher","award":["2E32233"],"award-info":[{"award-number":["2E32233"]}],"id":[{"id":"10.13039\/501100003693","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002551","name":"Seoul National University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002551","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["2022R1A2C3013138"],"award-info":[{"award-number":["2022R1A2C3013138"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2024-00403094"],"award-info":[{"award-number":["RS-2024-00403094"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2023-00227950"],"award-info":[{"award-number":["RS-2023-00227950"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2024-00407331"],"award-info":[{"award-number":["RS-2024-00407331"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["RS-2024-00338426"],"award-info":[{"award-number":["RS-2024-00338426"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"publisher","award":["2020M3E5D9079742"],"award-info":[{"award-number":["2020M3E5D9079742"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Chemical Biology"],"published-print":{"date-parts":[[2026,4]]},"DOI":"10.1016\/j.chembiol.2026.03.010","type":"journal-article","created":{"date-parts":[[2026,4,6]],"date-time":"2026-04-06T17:08:24Z","timestamp":1775495304000},"page":"474-489.e4","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Distinct autophagy impairment mechanisms of huntingtin aggregates with different polyQ lengths"],"prefix":"10.1016","volume":"33","author":[{"given":"Heejung","family":"Kim","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hae Nim","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suhyun","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seung Jae","family":"Hyeon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyunmin","family":"Jo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyung-Soo","family":"Inn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hoon","family":"Ryu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jihye","family":"Seong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2026.03.010_bib1","doi-asserted-by":"crossref","DOI":"10.1038\/nrdp.2015.5","article-title":"Huntington disease","volume":"1","author":"Bates","year":"2015","journal-title":"Nat. Rev. Dis. Primers"},{"key":"10.1016\/j.chembiol.2026.03.010_bib2","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.chembiol.2026.03.010_bib3","doi-asserted-by":"crossref","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":"10.1016\/j.chembiol.2026.03.010_bib4","doi-asserted-by":"crossref","first-page":"8808","DOI":"10.1074\/jbc.M109.075028","article-title":"Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease","volume":"285","author":"Landles","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib5","doi-asserted-by":"crossref","first-page":"20211","DOI":"10.1074\/jbc.M401267200","article-title":"Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain\/caspase fragments in the nucleus","volume":"279","author":"Gafni","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib6","doi-asserted-by":"crossref","first-page":"7862","DOI":"10.1523\/JNEUROSCI.22-18-07862.2002","article-title":"Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease","volume":"22","author":"Wellington","year":"2002","journal-title":"J. Neurosci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib7","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.chembiol.2026.03.010_bib8","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. Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib9","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1212\/WNL.0b013e318249f683","article-title":"CAG repeat expansion in Huntington disease determines age at onset in a fully dominant fashion","volume":"78","author":"Lee","year":"2012","journal-title":"Neurology"},{"key":"10.1016\/j.chembiol.2026.03.010_bib10","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.cell.2015.07.003","article-title":"Identification of Genetic Factors that Modify Clinical Onset of Huntington's Disease","volume":"162","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.03.010_bib11","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.642773","article-title":"Juvenile Huntington's Disease and Other PolyQ Diseases, Update on Neurodevelopmental Character and Comparative Bioinformatic Review of Transcriptomic and Proteomic Data","volume":"9","author":"\u015awito\u0144ska-Kurkowska","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib12","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1016\/j.cell.2024.11.038","article-title":"Long somatic DNA-repeat expansion drives neurodegeneration in Huntington's disease","volume":"188","author":"Handsaker","year":"2025","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.03.010_bib13","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1016\/j.molcel.2018.04.007","article-title":"A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation","volume":"70","author":"Peskett","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.03.010_bib14","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.chembiol.2026.03.010_bib15","doi-asserted-by":"crossref","first-page":"4263","DOI":"10.1111\/j.1742-4658.2008.06562.x","article-title":"Huntington\u2019s disease: degradation of mutant huntingtin by autophagy","volume":"275","author":"Sarkar","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.chembiol.2026.03.010_bib16","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a006734","article-title":"Integration of clearance mechanisms: the proteasome and autophagy","volume":"2","author":"Wong","year":"2010","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib17","doi-asserted-by":"crossref","DOI":"10.1038\/emm.2014.117","article-title":"Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies","volume":"47","author":"Ciechanover","year":"2015","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.chembiol.2026.03.010_bib18","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.tcb.2017.01.001","article-title":"Autophagy Receptors and Neurodegenerative Diseases","volume":"27","author":"Deng","year":"2017","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib19","doi-asserted-by":"crossref","first-page":"311","DOI":"10.3390\/cells9020311","article-title":"Targeting Aggrephagy for the Treatment of Alzheimer\u2019s Disease","volume":"9","author":"Malampati","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.chembiol.2026.03.010_bib20","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nn.2528","article-title":"Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease","volume":"13","author":"Martinez-Vicente","year":"2010","journal-title":"Nat. Neurosci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib21","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1523\/JNEUROSCI.1870-13.2014","article-title":"The regulation of autophagosome dynamics by huntingtin and HAP1 is disrupted by expression of mutant huntingtin, leading to defective cargo degradation","volume":"34","author":"Wong","year":"2014","journal-title":"J. Neurosci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib22","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.nbd.2018.08.010","article-title":"A role for autophagy in Huntington's disease","volume":"122","author":"Croce","year":"2019","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.chembiol.2026.03.010_bib23","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.neulet.2011.10.070","article-title":"Optineurin in Huntington's disease intranuclear inclusions","volume":"506","author":"Schwab","year":"2012","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.chembiol.2026.03.010_bib24","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.neuroscience.2011.11.059","article-title":"Cell type-specific localization of optineurin in the striatal neurons of mice: implications for neuronal vulnerability in Huntington's disease","volume":"202","author":"Okita","year":"2012","journal-title":"Neuroscience"},{"key":"10.1016\/j.chembiol.2026.03.010_bib25","doi-asserted-by":"crossref","DOI":"10.3390\/brainsci7060063","article-title":"Striatal Vulnerability in Huntington's Disease: Neuroprotection Versus Neurotoxicity","volume":"7","author":"Morigaki","year":"2017","journal-title":"Brain Sci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib26","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1021\/acssensors.0c00809","article-title":"Visualization of Autophagy Progression by a Red-Green-Blue Autophagy Sensor","volume":"5","author":"Kim","year":"2020","journal-title":"ACS Sens."},{"key":"10.1016\/j.chembiol.2026.03.010_bib27","article-title":"Fluorescent Protein-Based Autophagy Biosensors","volume":"14","author":"Kim","year":"2021","journal-title":"Materials"},{"key":"10.1016\/j.chembiol.2026.03.010_bib28","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1006\/mcne.1999.0773","article-title":"Nuclear Targeting of Mutant Huntingtin Increases Toxicity","volume":"14","author":"Peters","year":"1999","journal-title":"Mol. Cell. Neurosci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib29","doi-asserted-by":"crossref","first-page":"24131","DOI":"10.1074\/jbc.M702824200","article-title":"p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy","volume":"282","author":"Pankiv","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib30","doi-asserted-by":"crossref","first-page":"2692","DOI":"10.1242\/jcs.081232","article-title":"p62\/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate","volume":"124","author":"Watanabe","year":"2011","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib31","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202004062","article-title":"Liquid-liquid phase separation in autophagy","volume":"219","author":"Noda","year":"2020","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib32","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/S0002-9440(10)64369-6","article-title":"p62 Is a common component of cytoplasmic inclusions in protein aggregation diseases","volume":"160","author":"Zatloukal","year":"2002","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib33","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1038\/s41422-022-00662-6","article-title":"Myosin 1D and the branched actin network control the condensation of p62 bodies","volume":"32","author":"Feng","year":"2022","journal-title":"Cell Res."},{"key":"10.1016\/j.chembiol.2026.03.010_bib34","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1186\/s13578-023-00978-9","article-title":"Enhanced liquidity of p62 droplets mediated by Smurf1 links Nrf2 activation and autophagy","volume":"13","author":"Xia","year":"2023","journal-title":"Cell Biosci."},{"key":"10.1016\/j.chembiol.2026.03.010_bib35","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2023.112037","article-title":"The selective autophagy adaptor p62\/SQSTM1 forms phase condensates regulated by HSP27 that facilitate the clearance of damaged lysosomes via lysophagy","volume":"42","author":"Gallagher","year":"2023","journal-title":"Cell Rep."},{"key":"10.1016\/j.chembiol.2026.03.010_bib36","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/s41422-018-0017-7","article-title":"Polyubiquitin chain-induced p62 phase separation drives autophagic cargo segregation","volume":"28","author":"Sun","year":"2018","journal-title":"Cell Res."},{"key":"10.1016\/j.chembiol.2026.03.010_bib37","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1038\/s41586-020-2992-3","article-title":"Wetting regulates autophagy of phase-separated compartments and the cytosol","volume":"591","author":"Agudo-Canalejo","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.chembiol.2026.03.010_bib38","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2026.03.010_bib39","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.jsb.2005.06.006","article-title":"Mechanism of thioflavin T binding to amyloid fibrils","volume":"151","author":"Khurana","year":"2005","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib40","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1111\/j.1440-1789.2011.01199.x","article-title":"Optineurin in neurodegenerative diseases","volume":"31","author":"Osawa","year":"2011","journal-title":"Neuropathology"},{"key":"10.1016\/j.chembiol.2026.03.010_bib41","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/B978-0-12-394305-7.00005-7","article-title":"Cellular and molecular biology of optineurin","volume":"294","author":"Ying","year":"2012","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib42","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1080\/15548627.2017.1391970","article-title":"Structural insights into the ubiquitin recognition by OPTN (optineurin) and its regulation by TBK1-mediated phosphorylation","volume":"14","author":"Li","year":"2018","journal-title":"Autophagy"},{"key":"10.1016\/j.chembiol.2026.03.010_bib43","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/0092-8674(93)90585-E","article-title":"A Novel Gene Containing a Trinucleotide Repeat that Is Expanded and Unstable on Huntington\u2019s Disease Chromosomes","volume":"72","author":"Group","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.chembiol.2026.03.010_bib44","doi-asserted-by":"crossref","first-page":"3039","DOI":"10.1093\/hmg\/ddp242","article-title":"Somatic expansion of the Huntington's disease CAG repeat in the brain is associated with an earlier age of disease onset","volume":"18","author":"Swami","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.chembiol.2026.03.010_bib45","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.64674","article-title":"Propensity for somatic expansion increases over the course of life in Huntington disease","volume":"10","author":"Kacher","year":"2021","journal-title":"eLife"},{"key":"10.1016\/j.chembiol.2026.03.010_bib46","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1111\/j.1399-0004.2004.00241.x","article-title":"A new model for prediction of the age of onset and penetrance for Huntington's disease based on CAG length","volume":"65","author":"Langbehn","year":"2004","journal-title":"Clin. Genet."},{"key":"10.1016\/j.chembiol.2026.03.010_bib47","doi-asserted-by":"crossref","first-page":"754","DOI":"10.3389\/fgene.2020.00754","article-title":"Phase Transition of Huntingtin: Factors and Pathological Relevance","volume":"11","author":"Yang","year":"2020","journal-title":"Front. Genet."},{"key":"10.1016\/j.chembiol.2026.03.010_bib48","doi-asserted-by":"crossref","first-page":"1980","DOI":"10.1016\/j.molcel.2024.04.018","article-title":"Autophagy preferentially degrades non-fibrillar polyQ aggregates","volume":"84","author":"Zhao","year":"2024","journal-title":"Mol. Cell"},{"key":"10.1016\/j.chembiol.2026.03.010_bib49","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/s41556-021-00669-y","article-title":"Autophagosome biogenesis comes out of the black box","volume":"23","author":"Chang","year":"2021","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib50","doi-asserted-by":"crossref","first-page":"7338","DOI":"10.1038\/s41467-023-42829-8","article-title":"Local membrane source gathering by p62 body drives autophagosome formation","volume":"14","author":"Feng","year":"2023","journal-title":"Nat. Commun."},{"key":"10.1016\/j.chembiol.2026.03.010_bib51","doi-asserted-by":"crossref","first-page":"1092","DOI":"10.1093\/hmg\/ddu522","article-title":"Depletion of p62 reduces nuclear inclusions and paradoxically ameliorates disease phenotypes in Huntington's model mice","volume":"24","author":"Kurosawa","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.chembiol.2026.03.010_bib52","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1074\/jbc.M117.801944","article-title":"Optineurin promotes autophagosome formation by recruiting the autophagy-related Atg12-5-16L1 complex to phagophores containing the Wipi2 protein","volume":"293","author":"Bansal","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib53","doi-asserted-by":"crossref","first-page":"25108","DOI":"10.1074\/jbc.M110.187591","article-title":"Tumor necrosis factor receptor-associated factor 6 (TRAF6) associates with huntingtin protein and promotes its atypical ubiquitination to enhance aggregate formation","volume":"286","author":"Zucchelli","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib54","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2018100730","article-title":"A protein quality control pathway regulated by linear ubiquitination","volume":"38","author":"van Well","year":"2019","journal-title":"EMBO J."},{"key":"10.1016\/j.chembiol.2026.03.010_bib55","doi-asserted-by":"crossref","first-page":"R1357","DOI":"10.1016\/j.cub.2022.11.002","article-title":"Orchestration of selective autophagy by cargo receptors","volume":"32","author":"Adriaenssens","year":"2022","journal-title":"Curr. Biol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib56","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1080\/15548627.2022.2070331","article-title":"Multifaceted roles of TAX1BP1 in autophagy","volume":"19","author":"White","year":"2023","journal-title":"Autophagy"},{"key":"10.1016\/j.chembiol.2026.03.010_bib57","doi-asserted-by":"crossref","first-page":"5212","DOI":"10.1038\/s41467-021-25572-w","article-title":"Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin condensate formation and autophagy initiation","volume":"12","author":"Turco","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.chembiol.2026.03.010_bib58","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1007\/s00401-022-02462-z","article-title":"Decreased FAK activity and focal adhesion dynamics impair proper neurite formation of medium spiny neurons in Huntington's disease","volume":"144","author":"Lee","year":"2022","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib59","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1021\/acs.analchem.0c03323","article-title":"Spatiotemporal Characterization of GPCR Activity and Function during Endosomal Trafficking Pathway","volume":"93","author":"Kim","year":"2021","journal-title":"Anal. Chem."},{"key":"10.1016\/j.chembiol.2026.03.010_bib60","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1007\/s00401-017-1732-8","article-title":"Remodeling of heterochromatin structure slows neuropathological progression and prolongs survival in an animal model of Huntington's disease","volume":"134","author":"Lee","year":"2017","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.chembiol.2026.03.010_bib61","article-title":"Abeta modulates actin cytoskeleton via SHIP2-mediated phosphoinositide metabolism","volume":"9","author":"Lee","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.chembiol.2026.03.010_bib62","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1021\/ed038p559","article-title":"An Easily Prepared Wide Range Buffer Series","volume":"38","author":"Carmody","year":"1961","journal-title":"J. Chem. Educ."}],"container-title":["Cell Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626001029?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2451945626001029?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,25]],"date-time":"2026-06-25T20:10:45Z","timestamp":1782418245000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2451945626001029"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4]]},"references-count":62,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2026,4]]}},"alternative-id":["S2451945626001029"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.03.010","relation":{},"ISSN":["2451-9456"],"issn-type":[{"value":"2451-9456","type":"print"}],"subject":[],"published":{"date-parts":[[2026,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Distinct autophagy impairment mechanisms of huntingtin aggregates with different polyQ lengths","name":"articletitle","label":"Article Title"},{"value":"Cell Chemical Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2026.03.010","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}