{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:26:10Z","timestamp":1791851170313,"version":"4.3.4"},"reference-count":69,"publisher":"Oxford University Press (OUP)","issue":"10","license":[{"start":{"date-parts":[[2023,1,5]],"date-time":"2023-01-05T00:00:00Z","timestamp":1672876800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["EXC 2030-390661388"],"award-info":[{"award-number":["EXC 2030-390661388"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,5,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Stress granules are membrane-less ribonucleoprotein organelles that assemble upon exposure to stress conditions, but rapidly disassemble upon removal of stress. However, chronic stress can lead to persistent stress granules, a feature of distinct age-related neurodegenerative disorders. Among them, Huntington\u2019s disease (HD), which is caused by mutant expansion of the polyglutamine (polyQ) repeats of huntingtin protein (HTT), leading to its aggregation. To identify modulators of mutant HTT aggregation, we define its interactome in striatal neurons differentiated from patient-derived induced pluripotent stem cells (HD-iPSCs). We find that HTT interacts with G3BP1, a characteristic component of stress granules. Knockdown of G3BP1 increases mutant HTT protein levels and abolishes the ability of iPSCs as well as their differentiated neural counterparts to suppress mutant HTT aggregation. Moreover, loss of G3BP1 hastens polyQ-expanded aggregation and toxicity in the neurons of HD C. elegans models. Likewise, the assembly of G3BP1 into stress granules upon distinct stress conditions also reduces its interaction with HTT in human cells, promoting mutant HTT aggregation. Notably, enhancing the levels of G3BP1 is sufficient to induce proteasomal degradation of mutant HTT and prevent its aggregation, whereas the formation of stress granules blocks these ameliorative effects. In contrast, a mutant G3BP1 variant that cannot accumulate into granules retains its capacity to prevent mutant HTT aggregation even when the cells assemble stress granules. Thus, our findings indicate a direct role of G3BP1 and stress granule assembly in mutant HTT aggregation that may have implications for HD.<\/jats:p>","DOI":"10.1093\/hmg\/ddac304","type":"journal-article","created":{"date-parts":[[2022,12,15]],"date-time":"2022-12-15T19:14:50Z","timestamp":1671131690000},"page":"1607-1621","source":"Crossref","is-referenced-by-count":37,"title":["G3BP1-dependent mechanism suppressing protein aggregation in Huntington\u2019s models and its demise upon stress granule assembly"],"prefix":"10.1093","volume":"32","author":[{"given":"Ricardo","family":"Guti\u00e9rrez-Garcia","sequence":"first","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seda","family":"Koyuncu","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franziska","family":"Hommen","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayg\u0131n","family":"Bilican","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hyun Ju","family":"Lee","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Azra","family":"Fatima","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0801-0743","authenticated-orcid":false,"given":"David","family":"Vilchez","sequence":"additional","affiliation":[{"name":"Cologne Excellence Cluster for Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne , Cologne , Germany"},{"name":"Center for Molecular Medicine Cologne (CMMC), University of Cologne , Cologne , Germany"},{"name":"Faculty of Medicine, University Hospital Cologne , Cologne , Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2023,1,5]]},"reference":[{"key":"2023071912022015900_ref1","doi-asserted-by":"crossref","first-page":"a007476","DOI":"10.1101\/cshperspect.a007476","article-title":"Huntington's disease","volume":"3","author":"Finkbeiner","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2023071912022015900_ref2","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1002\/mds.25075","article-title":"The incidence and prevalence of Huntington's disease: a systematic review and meta-analysis","volume":"27","author":"Pringsheim","year":"2012","journal-title":"Mov. Disord."},{"key":"2023071912022015900_ref3","doi-asserted-by":"crossref","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":"2023071912022015900_ref4","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.3390\/ijms18071568","article-title":"Proteostasis of huntingtin in health and disease","volume":"18","author":"Koyuncu","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"2023071912022015900_ref5","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1093\/hmg\/10.14.1511","article-title":"Over-expression of inducible HSP70 chaperone suppresses neuropathology and improves motor function in SCA1 mice","volume":"10","author":"Cummings","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"2023071912022015900_ref6","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1126\/science.287.5459.1837","article-title":"Genetic suppression of polyglutamine toxicity in drosophila","volume":"287","author":"Kazemi-Esfarjani","year":"2000","journal-title":"Science"},{"key":"2023071912022015900_ref7","doi-asserted-by":"crossref","first-page":"1163","DOI":"10.1038\/ncb1478","article-title":"Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state","volume":"8","author":"Kitamura","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"2023071912022015900_ref8","doi-asserted-by":"crossref","first-page":"6403","DOI":"10.1073\/pnas.0307697101","article-title":"Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation","volume":"101","author":"Nollen","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2023071912022015900_ref9","doi-asserted-by":"crossref","first-page":"13649","DOI":"10.1038\/ncomms13649","article-title":"Somatic increase of CCT8 mimics proteostasis of human pluripotent stem cells and extends C. elegans lifespan","volume":"7","author":"Noormohammadi","year":"2016","journal-title":"Nat. Commun."},{"key":"2023071912022015900_ref10","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1038\/ncb1477","article-title":"The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions","volume":"8","author":"Tam","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"2023071912022015900_ref11","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.molcel.2020.02.022","article-title":"DNAJB6, a key factor in neuronal sensitivity to Amyloidogenesis","volume":"78","author":"Thiruvalluvan","year":"2020","journal-title":"Mol. Cell"},{"key":"2023071912022015900_ref12","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/70532","article-title":"Suppression of polyglutamine-mediated neurodegeneration in drosophila by the molecular chaperone HSP70","volume":"23","author":"Warrick","year":"1999","journal-title":"Nat. Genet."},{"key":"2023071912022015900_ref13","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. Biol. Chem."},{"key":"2023071912022015900_ref14","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1038\/s41467-018-05320-3","article-title":"The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington's disease patients","volume":"9","author":"Koyuncu","year":"2018","journal-title":"Nat. Commun."},{"key":"2023071912022015900_ref15","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1111\/jnc.12647","article-title":"Sulforaphane enhances proteasomal and autophagic activities in mice and is a potential therapeutic reagent for Huntington's disease","volume":"129","author":"Liu","year":"2014","journal-title":"J. Neurochem."},{"key":"2023071912022015900_ref16","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1128\/MCB.01227-08","article-title":"Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process","volume":"29","author":"Tonoki","year":"2009","journal-title":"Mol. Cell. Biol."},{"key":"2023071912022015900_ref17","doi-asserted-by":"crossref","first-page":"22044","DOI":"10.1074\/jbc.M212235200","article-title":"Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function","volume":"278","author":"Tsai","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023071912022015900_ref18","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1038\/nature11315","article-title":"RPN-6 determines C. elegans longevity under proteotoxic stress conditions","volume":"489","author":"Vilchez","year":"2012","journal-title":"Nature"},{"key":"2023071912022015900_ref19","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1016\/j.yexcr.2006.10.031","article-title":"Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin","volume":"313","author":"Yang","year":"2007","journal-title":"Exp. Cell Res."},{"key":"2023071912022015900_ref20","doi-asserted-by":"crossref","first-page":"1642","DOI":"10.1016\/S0140-6736(03)13304-1","article-title":"Huntingtin aggregation and toxicity in Huntington's disease","volume":"361","author":"Bates","year":"2003","journal-title":"Lancet"},{"key":"2023071912022015900_ref21","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/S0072-9752(07)01256-0","article-title":"Neuropathology of Huntington's disease","volume":"89","author":"Vonsattel","year":"2008","journal-title":"Handb. Clin. Neurol."},{"key":"2023071912022015900_ref22","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.stem.2012.04.027","article-title":"Induced pluripotent stem cells from patients with Huntington's disease show CAG-repeat-expansion-associated phenotypes","volume":"11","author":"Consortium, H.D.i","year":"2012","journal-title":"Cell Stem Cell"},{"key":"2023071912022015900_ref23","doi-asserted-by":"crossref","first-page":"2054","DOI":"10.1002\/stem.1135","article-title":"Neuronal properties, in vivo effects, and pathology of a Huntington's disease patient-derived induced pluripotent stem cells","volume":"30","author":"Jeon","year":"2012","journal-title":"Stem Cells"},{"key":"2023071912022015900_ref24","doi-asserted-by":"crossref","first-page":"769","DOI":"10.4103\/1673-5374.249223","article-title":"Induced pluripotent stem cells from Huntington's disease patients: a promising approach to define and correct disease-related alterations","volume":"14","author":"Fatima","year":"2019","journal-title":"Neural Regen. Res."},{"key":"2023071912022015900_ref25","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1016\/j.ceb.2020.08.005","article-title":"The intrinsic proteostasis network of stem cells","volume":"67","author":"Llamas","year":"2020","journal-title":"Curr. Opin. Cell Biol."},{"key":"2023071912022015900_ref26","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1111\/jnc.15280","article-title":"The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease","volume":"157","author":"Sidibe","year":"2021","journal-title":"J. Neurochem."},{"key":"2023071912022015900_ref27","doi-asserted-by":"crossref","first-page":"a032813","DOI":"10.1101\/cshperspect.a032813","article-title":"Stress granules and processing bodies in translational control","volume":"11","author":"Ivanov","year":"2019","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"2023071912022015900_ref28","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.cell.2015.12.038","article-title":"ATPase-modulated stress granules contain a diverse proteome and substructure","volume":"164","author":"Jain","year":"2016","journal-title":"Cell"},{"key":"2023071912022015900_ref29","doi-asserted-by":"crossref","first-page":"e18413","DOI":"10.7554\/eLife.18413","article-title":"Distinct stages in stress granule assembly and disassembly","volume":"5","author":"Wheeler","year":"2016","journal-title":"Elife"},{"key":"2023071912022015900_ref30","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1038\/s41583-019-0222-5","article-title":"Stress granules and neurodegeneration","volume":"20","author":"Wolozin","year":"2019","journal-title":"Nat. Rev. Neurosci."},{"key":"2023071912022015900_ref31","doi-asserted-by":"crossref","first-page":"e140723","DOI":"10.1172\/JCI140723","article-title":"Huntington's disease mice and human brain tissue exhibit increased G3BP1 granules and TDP43 mislocalization","volume":"131","author":"Sanchez","year":"2021","journal-title":"J. Clin. Invest."},{"key":"2023071912022015900_ref32","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.stem.2012.01.021","article-title":"Human embryonic stem cell-derived GABA neurons correct locomotion deficits in quinolinic acid-lesioned mice","volume":"10","author":"Ma","year":"2012","journal-title":"Cell Stem Cell"},{"key":"2023071912022015900_ref33","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/j.cell.2008.07.041","article-title":"Disease-specific induced pluripotent stem cells","volume":"134","author":"Park","year":"2008","journal-title":"Cell"},{"key":"2023071912022015900_ref34","first-page":"4117","article-title":"Mechanism suppressing H3K9 trimethylation in pluripotent stem cells and its demise by polyQ-expanded huntingtin mutations","volume":"27","author":"Irmak","year":"2018","journal-title":"Hum. Mol. Genet."},{"key":"2023071912022015900_ref35","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1038\/s42003-020-0984-3","article-title":"The ubiquitin-conjugating enzyme UBE2K determines neurogenic potential through histone H3 in human embryonic stem cells","volume":"3","author":"Fatima","year":"2020","journal-title":"Commun. Biol."},{"key":"2023071912022015900_ref36","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1002\/cne.23405","article-title":"Splicing factor TRA2B is required for neural progenitor survival","volume":"522","author":"Roberts","year":"2014","journal-title":"J. Comp. Neurol."},{"key":"2023071912022015900_ref37","doi-asserted-by":"crossref","first-page":"3188","DOI":"10.1074\/jbc.M008099200","article-title":"Isolation of a 40-kDa huntingtin-associated protein","volume":"276","author":"Peters","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2023071912022015900_ref38","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/gtc.12023","article-title":"Both G3BP1 and G3BP2 contribute to stress granule formation","volume":"18","author":"Matsuki","year":"2013","journal-title":"Genes Cells"},{"key":"2023071912022015900_ref39","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1038\/378403a0","article-title":"Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias","volume":"378","author":"Trottier","year":"1995","journal-title":"Nature"},{"key":"2023071912022015900_ref40","doi-asserted-by":"crossref","first-page":"7597","DOI":"10.1523\/JNEUROSCI.0990-06.2006","article-title":"Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model","volume":"26","author":"Brignull","year":"2006","journal-title":"J. Neurosci."},{"key":"2023071912022015900_ref41","doi-asserted-by":"crossref","first-page":"eabg3012","DOI":"10.1126\/sciadv.abg3012","article-title":"Systemic regulation of mitochondria by germline proteostasis prevents protein aggregation in the soma of C. elegans","volume":"7","author":"Calculli","year":"2021","journal-title":"Sci. Adv."},{"key":"2023071912022015900_ref42","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/j.neuron.2019.07.004","article-title":"Inhibition of axon regeneration by liquid-like TIAR-2 granules","volume":"104","author":"Andrusiak","year":"2019","journal-title":"Neuron"},{"key":"2023071912022015900_ref43","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1038\/nmeth.1463","article-title":"Enhanced neuronal RNAi in C. elegans using SID-1","volume":"7","author":"Calixto","year":"2010","journal-title":"Nat. Methods"},{"key":"2023071912022015900_ref44","doi-asserted-by":"crossref","first-page":"5648","DOI":"10.1038\/s41467-019-13540-4","article-title":"The autophagy receptor p62\/SQST-1 promotes proteostasis and longevity in C. elegans by inducing autophagy","volume":"10","author":"Kumsta","year":"2019","journal-title":"Nat. Commun."},{"key":"2023071912022015900_ref45","doi-asserted-by":"crossref","first-page":"10417","DOI":"10.1073\/pnas.152161099","article-title":"The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans","volume":"99","author":"Morley","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2023071912022015900_ref46","doi-asserted-by":"crossref","first-page":"1962","DOI":"10.1016\/j.bbrc.2018.07.142","article-title":"Quantitative phosphoproteomics reveals GTBP-1 regulating C. elegans lifespan at different environmental temperatures","volume":"503","author":"Huang","year":"2018","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2023071912022015900_ref47","doi-asserted-by":"crossref","first-page":"16208","DOI":"10.1523\/JNEUROSCI.2911-10.2010","article-title":"Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy","volume":"30","author":"Liachko","year":"2010","journal-title":"J. Neurosci."},{"key":"2023071912022015900_ref48","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/hmg\/ddr417","article-title":"ALS mutations in FUS cause neuronal dysfunction and death in Caenorhabditis elegans by a dominant gain-of-function mechanism","volume":"21","author":"Murakami","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"2023071912022015900_ref49","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/j.bbadis.2014.08.010","article-title":"Sporadic and hereditary amyotrophic lateral sclerosis (ALS)","volume":"1852","author":"Ajroud-Driss","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"2023071912022015900_ref50","first-page":"755","article-title":"ALS mutant FUS proteins are recruited into stress granules in induced pluripotent stem cell-derived motoneurons","volume":"8","author":"Lenzi","year":"2015","journal-title":"Dis. Model. Mech."},{"key":"2023071912022015900_ref51","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/j.cell.2017.12.032","article-title":"Context-dependent and disease-specific diversity in protein interactions within stress granules","volume":"172","author":"Markmiller","year":"2018","journal-title":"Cell"},{"key":"2023071912022015900_ref52","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.molcel.2020.01.021","article-title":"Structure-mediated RNA decay by UPF1 and G3BP1","volume":"78","author":"Fischer","year":"2020","journal-title":"Mol. Cell"},{"key":"2023071912022015900_ref53","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/j.molmed.2016.05.005","article-title":"Hypo- and hyper-assembly diseases of RNA-protein complexes","volume":"22","author":"Shukla","year":"2016","journal-title":"Trends Mol. Med."},{"key":"2023071912022015900_ref54","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1016\/j.celrep.2016.04.045","article-title":"Interaction of tau with the RNA-binding protein TIA1 regulates tau pathophysiology and toxicity","volume":"15","author":"Vanderweyde","year":"2016","journal-title":"Cell Rep."},{"key":"2023071912022015900_ref55","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1038\/nature09320","article-title":"Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS","volume":"466","author":"Elden","year":"2010","journal-title":"Nature"},{"key":"2023071912022015900_ref56","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1038\/nature11922","article-title":"Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS","volume":"495","author":"Kim","year":"2013","journal-title":"Nature"},{"key":"2023071912022015900_ref57","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":"2023071912022015900_ref58","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1016\/j.cell.2013.07.038","article-title":"Altered ribostasis: RNA-protein granules in degenerative disorders","volume":"154","author":"Ramaswami","year":"2013","journal-title":"Cell"},{"key":"2023071912022015900_ref59","doi-asserted-by":"crossref","first-page":"e25200","DOI":"10.4161\/rdis.25200","article-title":"Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2\/B1 introduce potent steric zippers that drive excess RNP granule assembly","volume":"1","author":"Shorter","year":"2013","journal-title":"Rare Dis."},{"key":"2023071912022015900_ref60","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1126\/science.1165942","article-title":"Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6","volume":"323","author":"Vance","year":"2009","journal-title":"Science"},{"key":"2023071912022015900_ref61","doi-asserted-by":"crossref","first-page":"2931","DOI":"10.15252\/embj.201797568","article-title":"Dysregulated molecular pathways in amyotrophic lateral sclerosis-frontotemporal dementia spectrum disorder","volume":"36","author":"Gao","year":"2017","journal-title":"EMBO J."},{"key":"2023071912022015900_ref62","doi-asserted-by":"crossref","DOI":"10.3389\/fcell.2021.621779","article-title":"The integral role of RNA in stress granule formation and function","volume":"9","author":"Campos-Melo","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"2023071912022015900_ref63","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/nbt.1529","article-title":"Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling","volume":"27","author":"Chambers","year":"2009","journal-title":"Nat. Biotechnol."},{"key":"2023071912022015900_ref64","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1756-6606-3-17","article-title":"pARIS-htt: an optimised expression platform to study huntingtin reveals functional domains required for vesicular trafficking","volume":"3","author":"Pardo","year":"2010","journal-title":"Mol. Brain"},{"key":"2023071912022015900_ref65","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1093\/genetics\/77.1.71","article-title":"The genetics of Caenorhabditis elegans","volume":"77","author":"Brenner","year":"1974","journal-title":"Genetics"},{"key":"2023071912022015900_ref66","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1534\/genetics.114.170423","article-title":"Scalable and versatile genome editing using linear DNAs with microhomology to Cas9 sites in Caenorhabditis elegans","volume":"198","author":"Paix","year":"2014","journal-title":"Genetics"},{"key":"2023071912022015900_ref67","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/s41586-021-03781-z","article-title":"Rewiring of the ubiquitinated proteome determines ageing in C. elegans","volume":"596","author":"Koyuncu","year":"2021","journal-title":"Nature"},{"key":"2023071912022015900_ref68","doi-asserted-by":"crossref","first-page":"e66431","DOI":"10.1371\/journal.pone.0066431","article-title":"Genomic analysis of stress response against arsenic in Caenorhabditis elegans","volume":"8","author":"Sahu","year":"2013","journal-title":"PLoS One"},{"key":"2023071912022015900_ref69","doi-asserted-by":"crossref","first-page":"e23525","DOI":"10.1371\/journal.pone.0023525","article-title":"OASIS: online application for the survival analysis of lifespan assays performed in aging research","volume":"6","author":"Yang","year":"2011","journal-title":"PLoS One"}],"container-title":["Human Molecular Genetics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/hmg\/advance-article-pdf\/doi\/10.1093\/hmg\/ddac304\/48756489\/ddac304.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/hmg\/article-pdf\/32\/10\/1607\/50910990\/ddac304.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/hmg\/article-pdf\/32\/10\/1607\/50910990\/ddac304.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T08:10:59Z","timestamp":1689754259000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/hmg\/article\/32\/10\/1607\/6972256"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1,5]]},"references-count":69,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2023,1,5]]},"published-print":{"date-parts":[[2023,5,5]]}},"URL":"https:\/\/doi.org\/10.1093\/hmg\/ddac304","relation":{},"ISSN":["0964-6906","1460-2083"],"issn-type":[{"value":"0964-6906","type":"print"},{"value":"1460-2083","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2023,5,15]]},"published":{"date-parts":[[2023,1,5]]}}}