{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T15:46:51Z","timestamp":1792252011410,"version":"4.4.0"},"reference-count":134,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,7]],"date-time":"2020-12-07T00:00:00Z","timestamp":1607299200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM043601"],"award-info":[{"award-number":["R01 GM043601"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Harvard Brain Science","award":["Seed grant"],"award-info":[{"award-number":["Seed grant"]}]},{"DOI":"10.13039\/100013013","name":"Target ALS","doi-asserted-by":"publisher","award":["grant"],"award-info":[{"award-number":["grant"]}],"id":[{"id":"10.13039\/100013013","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Harvard Medical School Hearst Fund","award":["Postdoctoral Award"],"award-info":[{"award-number":["Postdoctoral Award"]}]},{"DOI":"10.13039\/100000884","name":"Cancer Research Institute","doi-asserted-by":"publisher","award":["Irvington Postdoctoral Fellowship"],"award-info":[{"award-number":["Irvington Postdoctoral Fellowship"]}],"id":[{"id":"10.13039\/100000884","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM132129"],"award-info":[{"award-number":["R01 GM132129"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"HHS | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01 GM97645"],"award-info":[{"award-number":["R01 GM97645"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100011776","name":"MND Scotland","doi-asserted-by":"publisher","award":["grant"],"award-info":[{"award-number":["grant"]}],"id":[{"id":"10.13039\/100011776","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":[[2021,1]]},"DOI":"10.1074\/jbc.ra120.015960","type":"journal-article","created":{"date-parts":[[2020,12,4]],"date-time":"2020-12-04T20:46:13Z","timestamp":1607114773000},"page":"100153","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":51,"special_numbering":"C","title":["Global proteomics of Ubqln2-based murine models of ALS"],"prefix":"10.1016","volume":"296","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-4144-7605","authenticated-orcid":false,"given":"Alexandra M.","family":"Whiteley","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4914-1619","authenticated-orcid":false,"given":"Miguel A.","family":"Prado","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefanie A.H.","family":"de Poot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4291-413X","authenticated-orcid":false,"given":"Joao A.","family":"Paulo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marissa","family":"Ashton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sara","family":"Dominguez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5039-5010","authenticated-orcid":false,"given":"Martin","family":"Weber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai","family":"Ngu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John","family":"Szpyt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark P.","family":"Jedrychowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amy","family":"Easton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7626-0034","authenticated-orcid":false,"given":"Steven P.","family":"Gygi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0700-6993","authenticated-orcid":false,"given":"Thimo","family":"Kurz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1740-5309","authenticated-orcid":false,"given":"Mervyn J.","family":"Monteiro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2125-6286","authenticated-orcid":false,"given":"Eric J.","family":"Brown","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel","family":"Finley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.015960_bib1","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1007\/s00401-013-1125-6","article-title":"Protein aggregation in amyotrophic lateral sclerosis","volume":"125","author":"Blokhuis","year":"2013","journal-title":"Acta Neuropathol."},{"key":"10.1074\/jbc.RA120.015960_bib2","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10 Suppl","author":"Ross","year":"2004","journal-title":"Nat. Med."},{"key":"10.1074\/jbc.RA120.015960_bib3","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1046\/j.0305-1846.2003.00518.x","article-title":"Protein aggregation in motor neurone disorders","volume":"29","author":"Wood","year":"2003","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1074\/jbc.RA120.015960_bib4","doi-asserted-by":"crossref","first-page":"1668","DOI":"10.1126\/science.1154584","article-title":"TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"319","author":"Sreedharan","year":"2008","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.015960_bib5","doi-asserted-by":"crossref","first-page":"1440","DOI":"10.1001\/archneurol.2011.250","article-title":"SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis","volume":"68","author":"Fecto","year":"2011","journal-title":"Arch. Neurol."},{"key":"10.1074\/jbc.RA120.015960_bib6","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1038\/nature08971","article-title":"Mutations of optineurin in amyotrophic lateral sclerosis","volume":"465","author":"Maruyama","year":"2010","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.015960_bib7","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1016\/S0140-6736(10)61156-7","article-title":"Amyotrophic lateral sclerosis","volume":"377","author":"Kiernan","year":"2011","journal-title":"Lancet"},{"key":"10.1074\/jbc.RA120.015960_bib8","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/j.jmb.2019.01.021","article-title":"Structure of hRpn10 bound to UBQLN2 UBL illustrates basis for complementarity between shuttle factors and substrates at the proteasome","volume":"431","author":"Chen","year":"2019","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib9","doi-asserted-by":"crossref","first-page":"3868","DOI":"10.1091\/mbc.e02-11-0766","article-title":"The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome","volume":"14","author":"Kleijnen","year":"2003","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib10","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S1097-2765(00)00040-X","article-title":"The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome","volume":"6","author":"Kleijnen","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib11","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.jmb.2007.12.029","article-title":"Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains","volume":"377","author":"Zhang","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib12","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1083\/jcb.133.6.1331","article-title":"Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center","volume":"133","author":"Biggins","year":"1996","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib13","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1038\/ncb0805-742","article-title":"Delivery of ubiquitinated substrates to protein-unfolding machines","volume":"7","author":"Elsasser","year":"2005","journal-title":"Nat. Cell Biol"},{"key":"10.1074\/jbc.RA120.015960_bib14","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1186\/1741-7007-7-75","article-title":"A\u00a0genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2","volume":"7","author":"Liu","year":"2009","journal-title":"BMC Biol."},{"key":"10.1074\/jbc.RA120.015960_bib15","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1038\/sj.embor.7400164","article-title":"A\u00a0genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation","volume":"5","author":"Medicherla","year":"2004","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib16","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1038\/ncb845","article-title":"Proteasome subunit Rpn1 binds ubiquitin-like protein domains","volume":"4","author":"Elsasser","year":"2002","journal-title":"Nat. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib17","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1146\/annurev.biochem.78.081507.101607","article-title":"Recognition and processing of ubiquitin-protein conjugates by the proteasome","volume":"78","author":"Finley","year":"2009","journal-title":"Annu. Rev. Biochem."},{"key":"10.1074\/jbc.RA120.015960_bib18","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1021\/bi011892y","article-title":"Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a","volume":"41","author":"Walters","year":"2002","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.015960_bib19","doi-asserted-by":"crossref","DOI":"10.1126\/science.aad9421","article-title":"Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome","volume":"351","author":"Shi","year":"2016","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.015960_bib20","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.1016\/j.str.2016.05.018","article-title":"Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 reveal distinct binding mechanisms between substrate receptors and shuttle factors of the proteasome","volume":"24","author":"Chen","year":"2016","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.015960_bib21","doi-asserted-by":"crossref","first-page":"11691","DOI":"10.1074\/jbc.M200245200","article-title":"Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23","volume":"277","author":"Rao","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015960_bib22","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/S0006-291X(02)00340-6","article-title":"Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis","volume":"293","author":"Saeki","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1074\/jbc.RA120.015960_bib23","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1038\/ncb1001-939","article-title":"Proteins containing the UBA domain are able to bind to multi-ubiquitin chains","volume":"3","author":"Wilkinson","year":"2001","journal-title":"Nat. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib24","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1073\/pnas.012585199","article-title":"Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome","volume":"99","author":"Funakoshi","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib25","doi-asserted-by":"crossref","first-page":"1568","DOI":"10.1016\/j.bbagen.2019.06.002","article-title":"The specificity of ubiquitin binding to ubiquilin-1 is regulated by sequences besides its UBA domain","volume":"1863","author":"Harman","year":"2019","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1074\/jbc.RA120.015960_bib26","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1038\/embor.2009.192","article-title":"Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities","volume":"10","author":"Hjerpe","year":"2009","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib27","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.febslet.2004.04.031","article-title":"Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains","volume":"566","author":"Ko","year":"2004","journal-title":"FEBS Lett."},{"key":"10.1074\/jbc.RA120.015960_bib28","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1038\/nsmb.1637","article-title":"Avid interactions underlie the Lys63-linked polyubiquitin binding specificities observed for UBA domains","volume":"16","author":"Sims","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib29","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1016\/j.molcel.2018.02.004","article-title":"Ubiquitin modulates liquid-liquid phase separation of UBQLN2 via disruption of multivalent interactions","volume":"69","author":"Dao","year":"2018","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib30","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.molcel.2016.05.020","article-title":"Ubiquilins chaperone and triage mitochondrial membrane proteins for degradation","volume":"63","author":"Itakura","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib31","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/j.molcel.2017.04.024","article-title":"In\u00a0vivo ubiquitin linkage-type analysis reveals that the Cdc48-Rad23\/Dsk2 Axis contributes to K48-linked chain specificity of the proteasome","volume":"66","author":"Tsuchiya","year":"2017","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib32","doi-asserted-by":"crossref","first-page":"842","DOI":"10.15252\/embr.201541402","article-title":"UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation","volume":"17","author":"Suzuki","year":"2016","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib33","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.cell.2016.07.001","article-title":"UBQLN2 mediates autophagy-independent protein aggregate clearance by the proteasome","volume":"166","author":"Hjerpe","year":"2016","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.015960_bib34","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.26435","article-title":"Ubiquilin1 promotes antigen-receptor mediated proliferation by eliminating mislocalized mitochondrial proteins","volume":"6","author":"Whiteley","year":"2017","journal-title":"Elife"},{"key":"10.1074\/jbc.RA120.015960_bib35","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1186\/1471-2148-14-63","article-title":"The ubiquilin gene family: evolutionary patterns and functional insights","volume":"14","author":"Marin","year":"2014","journal-title":"BMC Evol. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib36","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1038\/embor.2013.22","article-title":"Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery","volume":"14","author":"Lee","year":"2013","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib37","doi-asserted-by":"crossref","first-page":"573","DOI":"10.4161\/auto.5.4.8312","article-title":"Ubiquilins accelerate autophagosome maturation and promote cell survival during nutrient starvation","volume":"5","author":"N'Diaye","year":"2009","journal-title":"Autophagy"},{"key":"10.1074\/jbc.RA120.015960_bib38","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1038\/embor.2008.238","article-title":"PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation","volume":"10","author":"N'Diaye","year":"2009","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib39","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1093\/hmg\/ddq231","article-title":"Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy","volume":"19","author":"Rothenberg","year":"2010","journal-title":"Hum. Mol. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib40","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/s41556-019-0281-x","article-title":"Ubiquilins regulate autophagic flux through mTOR signalling and lysosomal acidification","volume":"21","author":"Senturk","year":"2019","journal-title":"Nat. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib41","doi-asserted-by":"crossref","first-page":"15230","DOI":"10.1073\/pnas.1917371117","article-title":"ALS\/FTD mutations in UBQLN2 impede autophagy by reducing autophagosome acidification through loss of function","volume":"117","author":"Wu","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib42","doi-asserted-by":"crossref","first-page":"2565","DOI":"10.1093\/hmg\/ddv020","article-title":"ALS-linked mutations in ubiquilin-2 or hnRNPA1 reduce interaction between ubiquilin-2 and hnRNPA1","volume":"24","author":"Gilpin","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib43","article-title":"Defective proteasome delivery of polyubiquitinated proteins by ubiquilin-2 proteins containing ALS mutations","volume":"10","author":"Chang","year":"2015","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.015960_bib44","doi-asserted-by":"crossref","first-page":"E11485","DOI":"10.1073\/pnas.1811997115","article-title":"Ubiquilin 2 modulates ALS\/FTD-linked FUS-RNA complex dynamics and stress granule formation","volume":"115","author":"Alexander","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib45","doi-asserted-by":"crossref","first-page":"E10495","DOI":"10.1073\/pnas.1810522115","article-title":"Mutant UBQLN2 promotes toxicity by modulating intrinsic self-assembly","volume":"115","author":"Sharkey","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib46","doi-asserted-by":"crossref","first-page":"105016","DOI":"10.1016\/j.nbd.2020.105016","article-title":"Modeling UBQLN2-mediated neurodegenerative disease in mice: shared and divergent properties of wild type and mutant UBQLN2 in phase separation, subcellular localization, altered proteostasis pathways, and selective cytotoxicity","volume":"143","author":"Sharkey","year":"2020","journal-title":"Neurobiol. Dis."},{"key":"10.1074\/jbc.RA120.015960_bib47","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/nature10353","article-title":"Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset ALS and ALS\/dementia","volume":"477","author":"Deng","year":"2011","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.015960_bib48","doi-asserted-by":"crossref","first-page":"2596","DOI":"10.1093\/hmg\/ddaa152","article-title":"Ubiquilin-2 differentially regulates polyglutamine disease proteins","volume":"29","author":"Gerson","year":"2020","journal-title":"Hum. Mol. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib49","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/s00401-014-1367-y","article-title":"Pathogenic Ubqln2 gains toxic properties to induce neuron death","volume":"129","author":"Wu","year":"2015","journal-title":"Acta Neuropathol."},{"key":"10.1074\/jbc.RA120.015960_bib50","doi-asserted-by":"crossref","first-page":"239.e11","DOI":"10.1016\/j.neurobiolaging.2017.06.018","article-title":"Novel UBQLN2 mutations linked to amyotrophic lateral sclerosis and atypical hereditary spastic paraplegia phenotype through defective HSP70-mediated proteolysis","volume":"58","author":"Teyssou","year":"2017","journal-title":"Neurobiol. Aging"},{"key":"10.1074\/jbc.RA120.015960_bib51","doi-asserted-by":"crossref","first-page":"2527.e3","DOI":"10.1016\/j.neurobiolaging.2012.05.008","article-title":"UBQLN2\/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis","volume":"33","author":"Williams","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"10.1074\/jbc.RA120.015960_bib52","doi-asserted-by":"crossref","first-page":"2230.e1","DOI":"10.1016\/j.neurobiolaging.2012.03.015","article-title":"UBQLN2 mutations are rare in French and French-Canadian amyotrophic lateral sclerosis","volume":"33","author":"Daoud","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"10.1074\/jbc.RA120.015960_bib53","doi-asserted-by":"crossref","first-page":"2949.e13","DOI":"10.1016\/j.neurobiolaging.2012.07.002","article-title":"Screening in ALS and FTD patients reveals 3 novel UBQLN2 mutations outside the PXX domain and a pure FTD phenotype","volume":"33","author":"Synofzik","year":"2012","journal-title":"Neurobiol. Aging"},{"key":"10.1074\/jbc.RA120.015960_bib54","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.brainres.2013.06.006","article-title":"Unbiased screen reveals ubiquilin-1 and -2 highly associated with huntingtin inclusions","volume":"1524","author":"Rutherford","year":"2013","journal-title":"Brain Res."},{"key":"10.1074\/jbc.RA120.015960_bib55","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1093\/hmg\/ddl017","article-title":"Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin","volume":"15","author":"Wang","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib56","doi-asserted-by":"crossref","first-page":"13416","DOI":"10.1073\/pnas.1206786109","article-title":"Ubiquilin-1 regulates amyloid precursor protein maturation and degradation by stimulating K63-linked polyubiquitination of lysine 688","volume":"109","author":"El Ayadi","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib57","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1083\/jcb.151.4.847","article-title":"Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation","volume":"151","author":"Mah","year":"2000","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib58","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1042\/BJ20060441","article-title":"Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins","volume":"399","author":"Ford","year":"2006","journal-title":"Biochem. J."},{"key":"10.1074\/jbc.RA120.015960_bib59","doi-asserted-by":"crossref","first-page":"E7580","DOI":"10.1073\/pnas.1608432113","article-title":"Motor neuron disease, TDP-43 pathology, and memory deficits in mice expressing ALS-FTD-linked UBQLN2 mutations","volume":"113","author":"Le","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib60","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/j.celrep.2015.06.064","article-title":"Neurolastin, a dynamin family GTPase, regulates excitatory synapses and spine density","volume":"12","author":"Lomash","year":"2015","journal-title":"Cell Rep."},{"issue":"Pt 20","key":"10.1074\/jbc.RA120.015960_bib61","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1242\/jcs.088799","article-title":"TRIM32 promotes neural differentiation through retinoic acid receptor-mediated transcription","volume":"124","author":"Sato","year":"2011","journal-title":"J.\u00a0Cell Sci"},{"key":"10.1074\/jbc.RA120.015960_bib62","doi-asserted-by":"crossref","first-page":"6287","DOI":"10.1073\/pnas.0600158103","article-title":"Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin ligase, as a Bardet-Biedl syndrome gene (BBS11)","volume":"103","author":"Chiang","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib63","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.jmb.2005.09.068","article-title":"Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin","volume":"354","author":"Kudryashova","year":"2005","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib64","doi-asserted-by":"crossref","first-page":"2344","DOI":"10.1093\/hmg\/ddp167","article-title":"TRIM32\u00a0is an E3 ubiquitin ligase for dysbindin","volume":"18","author":"Locke","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib65","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1083\/jcb.201110067","article-title":"Ubiquitylation by Trim32 causes coupled loss of desmin, Z-bands, and thin filaments in muscle atrophy","volume":"198","author":"Cohen","year":"2012","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib66","doi-asserted-by":"crossref","first-page":"28646","DOI":"10.1074\/jbc.M112.362608","article-title":"TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA\/STING protein for K63-linked ubiquitination","volume":"287","author":"Zhang","year":"2012","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015960_bib67","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1186\/s12929-018-0479-4","article-title":"Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology","volume":"25","author":"Lee","year":"2018","journal-title":"J.\u00a0Biomed. Sci."},{"key":"10.1074\/jbc.RA120.015960_bib68","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.15252\/embj.201487943","article-title":"Msp1\/ATAD1 maintains mitochondrial function by facilitating the degradation of mislocalized tail-anchored proteins","volume":"33","author":"Chen","year":"2014","journal-title":"EMBO J."},{"key":"10.1074\/jbc.RA120.015960_bib69","doi-asserted-by":"crossref","first-page":"8019","DOI":"10.1073\/pnas.1405755111","article-title":"The conserved AAA-ATPase Msp1 confers organelle specificity to tail-anchored proteins","volume":"111","author":"Okreglak","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib70","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1159\/000084963","article-title":"A\u00a0family of neofunctionalized Ty3\/gypsy retrotransposon genes in mammalian genomes","volume":"110","author":"Brandt","year":"2005","journal-title":"Cytogenet. Genome Res."},{"key":"10.1074\/jbc.RA120.015960_bib71","doi-asserted-by":"crossref","first-page":"8482","DOI":"10.1074\/jbc.M409197200","article-title":"Human retroviral gag - and gag-pol -like proteins interact with the transforming growth factor-\u03b2 receptor activin receptor-like kinase 1","volume":"280","author":"Lux","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.015960_bib72","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0008686","article-title":"Genetic and molecular analyses of PEG10 reveal new aspects of genomic organization, transcription and translation","volume":"5","author":"Lux","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.RA120.015960_bib73","doi-asserted-by":"crossref","first-page":"37359","DOI":"10.1074\/jbc.M705676200","article-title":"Mammalian gene PEG10 expresses two reading frames by high efficiency -1 frameshifting in embryonic-associated tissues","volume":"282","author":"Clark","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015960_bib74","doi-asserted-by":"crossref","first-page":"4079","DOI":"10.1093\/nar\/29.19.4079","article-title":"Identification and characterisation of a developmentally regulated mammalian gene that utilises -1 programmed ribosomal frameshifting","volume":"29","author":"Shigemoto","year":"2001","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.RA120.015960_bib75","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0214110","article-title":"The Gag protein PEG10 binds to RNA and regulates\u00a0trophoblast stem cell lineage specification","volume":"14","author":"Abed","year":"2019","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.015960_bib76","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1016\/j.celrep.2015.07.012","article-title":"The placental gene PEG10 promotes progression of neuroendocrine prostate cancer","volume":"12","author":"Akamatsu","year":"2015","journal-title":"Cell Rep."},{"key":"10.1074\/jbc.RA120.015960_bib77","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/ng1699","article-title":"Deletion of Peg10, an imprinted gene acquired from a retrotransposon, causes early embryonic lethality","volume":"38","author":"Ono","year":"2006","journal-title":"Nat. Genet."},{"key":"10.1074\/jbc.RA120.015960_bib78","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.cell.2017.12.022","article-title":"Retrovirus-like gag protein Arc1 binds RNA and traffics across synaptic boutons","volume":"172","author":"Ashley","year":"2018","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.015960_bib79","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.cell.2017.12.024","article-title":"The neuronal gene arc encodes a repurposed retrotransposon gag protein that mediates intercellular RNA transfer","volume":"172","author":"Pastuzyn","year":"2018","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.015960_bib80","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/j.neuron.2013.05.029","article-title":"Rapid single-step induction of functional neurons from human pluripotent stem cells","volume":"78","author":"Zhang","year":"2013","journal-title":"Neuron"},{"key":"10.1074\/jbc.RA120.015960_bib81","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.1091\/mbc.e07-08-0775","article-title":"The ubiquitin-like protein PLIC-2 is a negative regulator of G protein-coupled receptor endocytosis","volume":"19","author":"N'Diaye","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib82","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nrm.2017.132","article-title":"Mechanisms of clathrin-mediated endocytosis","volume":"19","author":"Kaksonen","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib83","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1146\/annurev-biochem-060310-170328","article-title":"The ubiquitin code","volume":"81","author":"Komander","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"10.1074\/jbc.RA120.015960_bib84","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1083\/jcb.200810114","article-title":"K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway","volume":"185","author":"Lauwers","year":"2009","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib85","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.1128\/MCB.00048-14","article-title":"Cell fate decisions regulated by K63 ubiquitination of tumor necrosis factor receptor 1","volume":"34","author":"Fritsch","year":"2014","journal-title":"Mol. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib86","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nmeth.3179","article-title":"Directed evolution of APEX2\u00a0for\u00a0electron microscopy and proximity labeling","volume":"12","author":"Lam","year":"2015","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.RA120.015960_bib87","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1002\/jcb.29830","article-title":"Ubiquilin proteins regulate EGFR levels and activity in lung adenocarcinoma cells","volume":"122","author":"Kurlawala","year":"2020","journal-title":"J.\u00a0Cell Biochem."},{"key":"10.1074\/jbc.RA120.015960_bib88","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s00401-016-1575-8","article-title":"Comparative interactomics analysis of different ALS-associated proteins identifies converging molecular pathways","volume":"132","author":"Blokhuis","year":"2016","journal-title":"Acta Neuropathol."},{"key":"10.1074\/jbc.RA120.015960_bib89","doi-asserted-by":"crossref","first-page":"D607","DOI":"10.1093\/nar\/gky1131","article-title":"STRING v11: protein-protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets","volume":"47","author":"Szklarczyk","year":"2019","journal-title":"Nucleic Acids Res."},{"key":"10.1074\/jbc.RA120.015960_bib90","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1038\/nrm1762","article-title":"The Cbl interactome and its functions","volume":"6","author":"Schmidt","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1074\/jbc.RA120.015960_bib91","doi-asserted-by":"crossref","first-page":"2140","DOI":"10.1038\/emboj.2013.149","article-title":"Threshold-controlled ubiquitination of the EGFR directs receptor fate","volume":"32","author":"Sigismund","year":"2013","journal-title":"EMBO J."},{"key":"10.1074\/jbc.RA120.015960_bib92","doi-asserted-by":"crossref","first-page":"a017459","DOI":"10.1101\/cshperspect.a017459","article-title":"Endocytosis of receptor tyrosine kinases","volume":"5","author":"Goh","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib93","doi-asserted-by":"crossref","DOI":"10.1101\/cshperspect.a016808","article-title":"Ubiquitin-dependent sorting in endocytosis","volume":"6","author":"Piper","year":"2014","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1074\/jbc.RA120.015960_bib94","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1038\/s41580-019-0177-4","article-title":"The many functions of ESCRTs","volume":"21","author":"Vietri","year":"2020","journal-title":"Nat. Rev. Mol. Cell Biol"},{"issue":"11 Pt B","key":"10.1074\/jbc.RA120.015960_bib95","doi-asserted-by":"crossref","first-page":"2138","DOI":"10.1016\/j.bbamcr.2017.07.017","article-title":"Role of ubiquitination and proteolysis in the regulation of pro- and anti-apoptotic TNF-R1 signaling","volume":"1864","author":"Fritsch","year":"2017","journal-title":"Biochim. Biophys. Acta Mol. Cell Res"},{"key":"10.1074\/jbc.RA120.015960_bib96","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/j.molcel.2013.07.014","article-title":"TRAF4 promotes TGF-beta receptor signaling and drives breast cancer metastasis","volume":"51","author":"Zhang","year":"2013","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib97","doi-asserted-by":"crossref","first-page":"e30917","DOI":"10.1371\/journal.pone.0030917","article-title":"In\u00a0vivo evidence that TRAF4 is required for central nervous system myelin homeostasis","volume":"7","author":"Blaise","year":"2012","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.015960_bib98","doi-asserted-by":"crossref","first-page":"ra8","DOI":"10.1126\/scisignal.aad0848","article-title":"ESCRT proteins restrict constitutive NF-kappaB signaling by trafficking cytokine receptors","volume":"9","author":"Maminska","year":"2016","journal-title":"Sci. Signal"},{"key":"10.1074\/jbc.RA120.015960_bib99","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.3389\/fimmu.2018.01849","article-title":"Tumor necrosis factor receptor-associated factor regulation of nuclear factor kappaB and mitogen-activated protein kinase pathways","volume":"9","author":"Shi","year":"2018","journal-title":"Front. Immunol."},{"key":"10.1074\/jbc.RA120.015960_bib100","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1093\/jmcb\/mju005","article-title":"TRIM4 modulates type I interferon induction and cellular antiviral response by targeting RIG-I for K63-linked ubiquitination","volume":"6","author":"Yan","year":"2014","journal-title":"J.\u00a0Mol. Cell Biol"},{"key":"10.1074\/jbc.RA120.015960_bib101","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.chom.2018.10.007","article-title":"Trivalent RING assembly on retroviral capsids activates TRIM5 ubiquitination and innate immune signaling","volume":"24","author":"Fletcher","year":"2018","journal-title":"Cell Host Microbe"},{"key":"10.1074\/jbc.RA120.015960_bib102","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.virol.2015.02.033","article-title":"Ubiquitination in the antiviral immune response","volume":"479-480","author":"Davis","year":"2015","journal-title":"Virology"},{"key":"10.1074\/jbc.RA120.015960_bib103","doi-asserted-by":"crossref","first-page":"2957","DOI":"10.4049\/jimmunol.1800656","article-title":"The otubain YOD1 suppresses aggregation and activation of the signaling adaptor MAVS through Lys63-linked deubiquitination","volume":"202","author":"Liu","year":"2019","journal-title":"J.\u00a0Immunol."},{"key":"10.1074\/jbc.RA120.015960_bib104","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death","volume":"171","author":"Bjorkoy","year":"2005","journal-title":"J.\u00a0Cell Biol"},{"key":"10.1074\/jbc.RA120.015960_bib105","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/j.molcel.2009.01.020","article-title":"A\u00a0role for NBR1 in autophagosomal degradation of ubiquitinated substrates","volume":"33","author":"Kirkin","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.015960_bib106","doi-asserted-by":"crossref","first-page":"5404","DOI":"10.1074\/jbc.TM117.000117","article-title":"Ubiquitin signaling and autophagy","volume":"293","author":"Grumati","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1074\/jbc.RA120.015960_bib107","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/embor.2012.3","article-title":"DeSUMOylating isopeptidase: a second class of SUMO protease","volume":"13","author":"Shin","year":"2012","journal-title":"EMBO Rep."},{"key":"10.1074\/jbc.RA120.015960_bib108","doi-asserted-by":"crossref","first-page":"E4199","DOI":"10.1073\/pnas.1711017115","article-title":"Nuclear export of ubiquitinated proteins via the UBIN-POST system","volume":"115","author":"Hirayama","year":"2018","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1074\/jbc.RA120.015960_bib109","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/nature22366","article-title":"Architecture of the human interactome defines protein communities and disease networks","volume":"545","author":"Huttlin","year":"2017","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.015960_bib110","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1021\/acs.jproteome.7b00572","article-title":"BioPlex display: an interactive suite for large-scale AP-MS protein-protein interaction data","volume":"17","author":"Schweppe","year":"2018","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1074\/jbc.RA120.015960_bib111","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/j.cels.2016.08.009","article-title":"Highly multiplexed quantitative mass spectrometry analysis of ubiquitylomes","volume":"3","author":"Rose","year":"2016","journal-title":"Cell Syst."},{"key":"10.1074\/jbc.RA120.015960_bib112","doi-asserted-by":"crossref","first-page":"79","DOI":"10.3233\/JAD-2004-6109","article-title":"Overexpression of ubiquilin decreases ubiquitination and degradation of presenilin proteins","volume":"6","author":"Massey","year":"2004","journal-title":"J.\u00a0Alzheimers Dis."},{"key":"10.1074\/jbc.RA120.015960_bib113","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nbt1191","article-title":"Engineering of a monomeric green-to-red photoactivatable fluorescent protein induced by blue light","volume":"24","author":"Gurskaya","year":"2006","journal-title":"Nat. Biotechnol."},{"key":"10.1074\/jbc.RA120.015960_bib114","doi-asserted-by":"crossref","first-page":"3859","DOI":"10.1007\/s00018-019-03394-w","article-title":"Amyotrophic lateral sclerosis-linked UBQLN2 mutants inhibit endoplasmic reticulum to Golgi transport, leading to Golgi fragmentation and ER stress","volume":"77","author":"Halloran","year":"2020","journal-title":"Cell Mol. Life Sci."},{"key":"10.1074\/jbc.RA120.015960_bib115","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1016\/j.febslet.2004.12.030","article-title":"LDOC1, a novel MZF-1-interacting protein, induces apoptosis","volume":"579","author":"Inoue","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1074\/jbc.RA120.015960_bib116","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1002\/ijc.11122","article-title":"Leucine-zipper protein, LDOC1, inhibits NF-kappaB activation and sensitizes pancreatic cancer cells to apoptosis","volume":"105","author":"Nagasaki","year":"2003","journal-title":"Int. J. Cancer"},{"key":"10.1074\/jbc.RA120.015960_bib117","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1111\/j.1365-2362.2006.01722.x","article-title":"Brain site-specific gene expression analysis in Alzheimer's disease patients","volume":"36","author":"Yokota","year":"2006","journal-title":"Eur. J. Clin. Invest"},{"key":"10.1074\/jbc.RA120.015960_bib118","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1038\/labinvest.2016.63","article-title":"The ubiquitin ligase tripartite-motif-protein 32 is induced in Duchenne muscular dystrophy","volume":"96","author":"Assereto","year":"2016","journal-title":"Lab. Invest"},{"key":"10.1074\/jbc.RA120.015960_bib119","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1007\/s11064-016-2142-3","article-title":"Upregulated expression of TRIM32 is involved in Schwann cell differentiation, migration and neurite outgrowth after sciatic nerve crush","volume":"42","author":"Liu","year":"2017","journal-title":"Neurochem. Res."},{"key":"10.1074\/jbc.RA120.015960_bib120","doi-asserted-by":"crossref","first-page":"185","DOI":"10.3389\/fnins.2018.00185","article-title":"Serotonergic dysfunction in amyotrophic lateral sclerosis and Parkinson's disease: similar mechanisms, dissimilar outcomes","volume":"12","author":"Vermeiren","year":"2018","journal-title":"Front. Neurosci."},{"key":"10.1074\/jbc.RA120.015960_bib121","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1038\/nmeth.1593","article-title":"Chemically defined conditions for human iPSC derivation and culture","volume":"8","author":"Chen","year":"2011","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.RA120.015960_bib122","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/nbt.3081","article-title":"Cationic lipid-mediated delivery of proteins enables efficient protein-based genome editing in\u00a0vitro and in\u00a0vivo","volume":"33","author":"Zuris","year":"2015","journal-title":"Nat. Biotechnol."},{"key":"10.1074\/jbc.RA120.015960_bib123","article-title":"A\u00a0simple composite phenotype scoring system for evaluating mouse models of cerebellar ataxia","volume":"39","author":"Guyenet","year":"2010","journal-title":"J.\u00a0Vis. Exp."},{"key":"10.1074\/jbc.RA120.015960_bib124","doi-asserted-by":"crossref","DOI":"10.1523\/ENEURO.0047-15.2015","article-title":"Cognitive deficits, changes in synaptic function, and brain pathology in a mouse model of normal aging(1,2,3)","volume":"2","author":"Weber","year":"2015","journal-title":"eNeuro"},{"key":"10.1074\/jbc.RA120.015960_bib125","doi-asserted-by":"crossref","first-page":"e18152","DOI":"10.1371\/journal.pone.0018152","article-title":"The effects of breeding protocol in C57BL\/6J mice on adult offspring behaviour","volume":"6","author":"Foldi","year":"2011","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.015960_bib126","doi-asserted-by":"crossref","first-page":"7150","DOI":"10.1021\/ac502040v","article-title":"MultiNotch MS3 enables accurate, sensitive, and multiplexed detection of differential expression across cancer cell line proteomes","volume":"86","author":"McAlister","year":"2014","journal-title":"Anal. Chem."},{"key":"10.1074\/jbc.RA120.015960_bib127","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/j.cell.2010.12.001","article-title":"A\u00a0tissue-specific atlas of mouse protein phosphorylation and expression","volume":"143","author":"Huttlin","year":"2010","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.015960_bib128","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1021\/acs.jproteome.8b00217","article-title":"Streamlined tandem mass tag (SL-TMT) protocol: an efficient strategy for quantitative (phospho)proteome profiling using tandem mass tag-synchronous precursor selection-MS3","volume":"17","author":"Navarrete-Perea","year":"2018","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1074\/jbc.RA120.015960_bib129","doi-asserted-by":"crossref","first-page":"1620","DOI":"10.1007\/s13361-016-1434-9","article-title":"A\u00a0triple knockout (TKO) proteomics standard for diagnosing ion interference in isobaric labeling experiments","volume":"27","author":"Paulo","year":"2016","journal-title":"J.\u00a0Am. Soc. Mass Spectrom."},{"key":"10.1074\/jbc.RA120.015960_bib130","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1089\/omi.2011.0118","article-title":"clusterProfiler: an R package for comparing biological themes among gene clusters","volume":"16","author":"Yu","year":"2012","journal-title":"OMICS"},{"key":"10.1074\/jbc.RA120.015960_bib131","doi-asserted-by":"crossref","first-page":"e62342","DOI":"10.1371\/journal.pone.0062342","article-title":"EGFR inhibitor erlotinib delays disease progression but does not extend survival in the SOD1 mouse model of ALS","volume":"8","author":"Le Pichon","year":"2013","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA120.015960_bib132","doi-asserted-by":"crossref","first-page":"6425","DOI":"10.1523\/JNEUROSCI.4963-13.2014","article-title":"A\u00a0death receptor 6-amyloid precursor protein pathway regulates synapse density in the mature CNS but does not contribute to Alzheimer's disease-related pathophysiology in murine models","volume":"34","author":"Kallop","year":"2014","journal-title":"J.\u00a0Neurosci."},{"key":"10.1074\/jbc.RA120.015960_bib133","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/j.cell.2017.03.028","article-title":"Multidimensional tracking of GPCR signaling via peroxidase-catalyzed proximity labeling","volume":"169","author":"Paek","year":"2017","journal-title":"Cell"},{"key":"10.1074\/jbc.RA120.015960_bib134","doi-asserted-by":"crossref","first-page":"D442","DOI":"10.1093\/nar\/gky1106","article-title":"The PRIDE database and related tools and resources in 2019: improving support for quantification data","volume":"47","author":"Perez-Riverol","year":"2019","journal-title":"Nucleic Acids Res."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820001465?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820001465?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.015960","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,16]],"date-time":"2021-10-16T22:16:13Z","timestamp":1634422573000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820001465"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1]]},"references-count":134,"alternative-id":["S0021925820001465"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.015960","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2020.02.22.956524","asserted-by":"object"}]},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2021,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Global proteomics of Ubqln2-based murine models of ALS","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.015960","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"100153"}}