{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:18:31Z","timestamp":1790641111956,"version":"4.1.0"},"reference-count":75,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2019,7,6]],"date-time":"2019-07-06T00:00:00Z","timestamp":1562371200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2019,7,6]],"date-time":"2019-07-06T00:00:00Z","timestamp":1562371200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100000406","name":"Motor Neurone Disease Association","doi-asserted-by":"publisher","award":["Rattray\/Apr15\/837-791"],"award-info":[{"award-number":["Rattray\/Apr15\/837-791"]}],"id":[{"id":"10.13039\/501100000406","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Neurochem Res"],"published-print":{"date-parts":[[2020,6]]},"DOI":"10.1007\/s11064-019-02832-2","type":"journal-article","created":{"date-parts":[[2019,7,6]],"date-time":"2019-07-06T09:02:23Z","timestamp":1562403743000},"page":"1354-1364","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Endoplasmic Reticulum Stress Signalling Induces Casein Kinase 1-Dependent Formation of Cytosolic TDP-43 Inclusions in Motor Neuron-Like Cells"],"prefix":"10.1007","volume":"45","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6045-1063","authenticated-orcid":false,"given":"David A.","family":"Hicks","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura L.","family":"Cross","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ritchie","family":"Williamson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcus","family":"Rattray","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,7,6]]},"reference":[{"key":"2832_CR1","doi-asserted-by":"publisher","first-page":"942","DOI":"10.1016\/S0140-6736(10)61156-7","volume":"377","author":"MC Kiernan","year":"2011","unstructured":"Kiernan MC, Vucic S, Cheah BC, Turner MR, Eisen A, Hardiman O, Burrell JR, Zoing MC (2011) Amyotrophic lateral sclerosis. Lancet 377:942\u2013955","journal-title":"Lancet"},{"key":"2832_CR2","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1186\/1750-1326-8-28","volume":"8","author":"S Chen","year":"2013","unstructured":"Chen S, Sayana P, Zhang X, Le W (2013) Genetics of amyotrophic lateral sclerosis: an update. Mol Neurodegener 8:28","journal-title":"Mol Neurodegener"},{"key":"2832_CR3","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1038\/362059a0","volume":"362","author":"DR Rosen","year":"1993","unstructured":"Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, Hentati A, Donaldson D, Goto J et al (1993) Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59\u201362","journal-title":"Nature"},{"key":"2832_CR4","doi-asserted-by":"publisher","first-page":"1668","DOI":"10.1126\/science.1154584","volume":"319","author":"J Sreedharan","year":"2008","unstructured":"Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, Rogelj B, Ackerley S, Durnall JC et al (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319:1668\u20131672","journal-title":"Science"},{"key":"2832_CR5","doi-asserted-by":"publisher","first-page":"1205","DOI":"10.1126\/science.1166066","volume":"323","author":"TJ Kwiatkowski Jr","year":"2009","unstructured":"Kwiatkowski TJ Jr, Bosco DA, Leclerc AL, Tamrazian E, Vanderburg CR, Russ C, Davis A, Gilchrist J et al (2009) Mutations in the FUS\/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323:1205\u20131208","journal-title":"Science"},{"key":"2832_CR6","doi-asserted-by":"publisher","first-page":"1208","DOI":"10.1126\/science.1165942","volume":"323","author":"C Vance","year":"2009","unstructured":"Vance C, Rogelj B, Hortobagyi T, De Vos KJ, Nishimura AL, Sreedharan J, Hu X, Smith B et al (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323:1208\u20131211","journal-title":"Science"},{"key":"2832_CR7","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.neuron.2011.09.011","volume":"72","author":"M DeJesus-Hernandez","year":"2011","unstructured":"DeJesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M, Rutherford NJ, Nicholson AM, Finch NA et al (2011) Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72:245\u2013256","journal-title":"Neuron"},{"key":"2832_CR8","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/j.neuron.2011.09.010","volume":"72","author":"AE Renton","year":"2011","unstructured":"Renton AE, Majounie E, Waite A, Simon-Sanchez J, Rollinson S, Gibbs JR, Schymick JC, Laaksovirta H et al (2011) A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72:257\u2013268","journal-title":"Neuron"},{"key":"2832_CR9","doi-asserted-by":"publisher","first-page":"130","DOI":"10.1126\/science.1134108","volume":"314","author":"M Neumann","year":"2006","unstructured":"Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, Bruce J, Schuck T et al (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314:130\u2013133","journal-title":"Science"},{"key":"2832_CR10","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1007\/s00401-007-0206-9","volume":"113","author":"CF Tan","year":"2007","unstructured":"Tan CF, Eguchi H, Tagawa A, Onodera O, Iwasaki T, Tsujino A, Nishizawa M, Kakita A et al (2007) TDP-43 immunoreactivity in neuronal inclusions in familial amyotrophic lateral sclerosis with or without SOD1 gene mutation. Acta Neuropathol 113:535\u2013542","journal-title":"Acta Neuropathol"},{"key":"2832_CR11","doi-asserted-by":"publisher","first-page":"4309","DOI":"10.1073\/pnas.1317317111","volume":"111","author":"JA Austin","year":"2014","unstructured":"Austin JA, Wright GS, Watanabe S, Grossmann JG, Antonyuk SV, Yamanaka K, Hasnain SS (2014) Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life. Proc Natl Acad Sci USA 111:4309\u20134314","journal-title":"Proc Natl Acad Sci USA"},{"key":"2832_CR12","doi-asserted-by":"publisher","first-page":"R77","DOI":"10.1093\/hmg\/ddt349","volume":"22","author":"J Janssens","year":"2013","unstructured":"Janssens J, Van Broeckhoven C (2013) Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders. Hum Mol Genet 22:R77\u2013R87","journal-title":"Hum Mol Genet"},{"key":"2832_CR13","doi-asserted-by":"publisher","first-page":"228","DOI":"10.1038\/s41593-017-0047-3","volume":"21","author":"CC Chou","year":"2018","unstructured":"Chou CC, Zhang Y, Umoh ME, Vaughan SW, Lorenzini I, Liu F, Sayegh M, Donlin-Asp PG et al (2018) TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS\/FTD. Nat Neurosci 21:228\u2013239","journal-title":"Nat Neurosci"},{"key":"2832_CR14","doi-asserted-by":"publisher","first-page":"44","DOI":"10.1177\/1087057113501553","volume":"19","author":"JD Boyd","year":"2014","unstructured":"Boyd JD, Lee-Armandt JP, Feiler MS, Zaarur N, Liu M, Kraemer B, Concannon JB, Ebata A et al (2014) A high-content screen identifies novel compounds that inhibit stress-induced TDP-43 cellular aggregation and associated cytotoxicity. J Biomol Screen 19:44\u201356","journal-title":"J Biomol Screen"},{"key":"2832_CR15","doi-asserted-by":"publisher","first-page":"e42117","DOI":"10.1371\/journal.pone.0042117","volume":"7","author":"A Vaccaro","year":"2012","unstructured":"Vaccaro A, Patten SA, Ciura S, Maios C, Therrien M, Drapeau P, Kabashi E, Parker JA (2012) Methylene blue protects against TDP-43 and FUS neuronal toxicity in C. elegans and D. rerio. PLoS ONE 7:e42117","journal-title":"PLoS ONE"},{"key":"2832_CR16","doi-asserted-by":"publisher","first-page":"2419","DOI":"10.1016\/j.febslet.2009.06.042","volume":"583","author":"M Yamashita","year":"2009","unstructured":"Yamashita M, Nonaka T, Arai T, Kametani F, Buchman VL, Ninkina N, Bachurin SO, Akiyama H et al (2009) Methylene blue and dimebon inhibit aggregation of TDP-43 in cellular models. FEBS Lett 583:2419\u20132424","journal-title":"FEBS Lett"},{"key":"2832_CR17","doi-asserted-by":"publisher","first-page":"19437","DOI":"10.1074\/jbc.M116.737726","volume":"291","author":"R Cascella","year":"2016","unstructured":"Cascella R, Capitini C, Fani G, Dobson CM, Cecchi C, Chiti F (2016) Quantification of the relative contributions of loss-of-function and gain-of-function mechanisms in TAR DNA-binding protein 43 (TDP-43) proteinopathies. J Biol Chem 291:19437\u201319448","journal-title":"J Biol Chem"},{"key":"2832_CR18","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1038\/nrn3121","volume":"13","author":"EB Lee","year":"2012","unstructured":"Lee EB, Lee VM, Trojanowski JQ (2012) Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci 13:38\u201350","journal-title":"Nat Rev Neurosci"},{"key":"2832_CR19","first-page":"4473","volume":"25","author":"S Orru","year":"2016","unstructured":"Orru S, Coni P, Floris A, Littera R, Carcassi C, Sogos V, Brancia C (2016) Reduced stress granule formation and cell death in fibroblasts with the A382T mutation of TARDBP gene: evidence for loss of TDP-43 nuclear function. Hum Mol Genet 25:4473\u20134483","journal-title":"Hum Mol Genet"},{"key":"2832_CR20","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1111\/jnc.14327","volume":"146","author":"J Gao","year":"2018","unstructured":"Gao J, Wang L, Huntley ML, Perry G, Wang X (2018) Pathomechanisms of TDP-43 in neurodegeneration. J Neurochem 146:7\u201320","journal-title":"J Neurochem"},{"key":"2832_CR21","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1007\/s00401-018-1870-7","volume":"136","author":"F Krach","year":"2018","unstructured":"Krach F, Batra R, Wheeler EC, Vu AQ, Wang R, Hutt K, Rabin SJ, Baughn MW et al (2018) Transcriptome-pathology correlation identifies interplay between TDP-43 and the expression of its kinase CK1E in sporadic ALS. Acta Neuropathol 136:405\u2013423","journal-title":"Acta Neuropathol"},{"key":"2832_CR22","doi-asserted-by":"publisher","first-page":"1025","DOI":"10.1093\/hmg\/ddt498","volume":"23","author":"DK Choksi","year":"2014","unstructured":"Choksi DK, Roy B, Chatterjee S, Yusuff T, Bakhoum MF, Sengupta U, Ambegaokar S, Kayed R et al (2014) TDP-43 phosphorylation by casein kinase Iepsilon promotes oligomerization and enhances toxicity in vivo. Hum Mol Genet 23:1025\u20131035","journal-title":"Hum Mol Genet"},{"key":"2832_CR23","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1074\/jbc.M117.814111","volume":"293","author":"CW Goh","year":"2018","unstructured":"Goh CW, Lee IC, Sundaram JR, George SE, Yusoff P, Brush MH, Sze NSK, Shenolikar S (2018) Chronic oxidative stress promotes GADD34-mediated phosphorylation of the TAR DNA-binding protein TDP-43, a modification linked to neurodegeneration. J Biol Chem 293:163\u2013176","journal-title":"J Biol Chem"},{"key":"2832_CR24","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1016\/j.bbrc.2009.03.038","volume":"382","author":"F Kametani","year":"2009","unstructured":"Kametani F, Nonaka T, Suzuki T, Arai T, Dohmae N, Akiyama H, Hasegawa M (2009) Identification of casein kinase-1 phosphorylation sites on TDP-43. Biochem Biophys Res Commun 382:405\u2013409","journal-title":"Biochem Biophys Res Commun"},{"key":"2832_CR25","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1002\/ana.21425","volume":"64","author":"M Hasegawa","year":"2008","unstructured":"Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, Beach TG, Buratti E et al (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64:60\u201370","journal-title":"Ann Neurol"},{"key":"2832_CR26","doi-asserted-by":"publisher","first-page":"5473","DOI":"10.1074\/jbc.M115.695379","volume":"291","author":"T Nonaka","year":"2016","unstructured":"Nonaka T, Suzuki G, Tanaka Y, Kametani F, Hirai S, Okado H, Miyashita T, Saitoe M et al (2016) Phosphorylation of TAR DNA-binding protein of 43\u00a0kDa (TDP-43) by truncated casein kinase 1delta triggers mislocalization and accumulation of TDP-43. J Biol Chem 291:5473\u20135483","journal-title":"J Biol Chem"},{"key":"2832_CR27","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1186\/s13024-016-0102-7","volume":"11","author":"C Alquezar","year":"2016","unstructured":"Alquezar C, Salado IG, de la Encarnacion A, Perez DI, Moreno F, Gil C, de Munain AL, Martinez A et al (2016) Targeting TDP-43 phosphorylation by Casein Kinase-1delta inhibitors: a novel strategy for the treatment of frontotemporal dementia. Mol Neurodegener 11:36","journal-title":"Mol Neurodegener"},{"key":"2832_CR28","doi-asserted-by":"publisher","first-page":"151","DOI":"10.1016\/j.ejps.2015.07.011","volume":"78","author":"FR Makhuri","year":"2015","unstructured":"Makhuri FR, Ghasemi JB (2015) Computer-aided scaffold hopping to identify a novel series of casein kinase 1 delta (CK1d) inhibitors for amyotrophic lateral sclerosis. Eur J Pharm Sci 78:151\u2013162","journal-title":"Eur J Pharm Sci"},{"key":"2832_CR29","doi-asserted-by":"publisher","first-page":"2755","DOI":"10.1021\/jm500065f","volume":"57","author":"IG Salado","year":"2014","unstructured":"Salado IG, Redondo M, Bello ML, Perez C, Liachko NF, Kraemer BC, Miguel L, Lecourtois M et al (2014) Protein kinase CK-1 inhibitors as new potential drugs for amyotrophic lateral sclerosis. J Med Chem 57:2755\u20132772","journal-title":"J Med Chem"},{"key":"2832_CR30","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1186\/s12859-016-1379-9","volume":"17","author":"K Joshi","year":"2016","unstructured":"Joshi K, Goyal S, Grover S, Jamal S, Singh A, Dhar P, Grover A (2016) Novel group-based QSAR and combinatorial design of CK-1delta inhibitors as neuroprotective agents. BMC Bioinform 17:515","journal-title":"BMC Bioinform"},{"key":"2832_CR31","doi-asserted-by":"publisher","first-page":"e13250","DOI":"10.1371\/journal.pone.0013250","volume":"5","author":"L Liu-Yesucevitz","year":"2010","unstructured":"Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderweyde T, Citro A, Mehta T, Zaarur N, McKee A et al (2010) Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS ONE 5:e13250","journal-title":"PLoS ONE"},{"key":"2832_CR32","doi-asserted-by":"publisher","first-page":"56","DOI":"10.1186\/1750-1326-7-56","volume":"7","author":"B Wolozin","year":"2012","unstructured":"Wolozin B (2012) Regulated protein aggregation: stress granules and neurodegeneration. Mol Neurodegener 7:56","journal-title":"Mol Neurodegener"},{"key":"2832_CR33","doi-asserted-by":"publisher","first-page":"823","DOI":"10.1083\/jcb.200212128","volume":"160","author":"H Tourriere","year":"2003","unstructured":"Tourriere H, Chebli K, Zekri L, Courselaud B, Blanchard JM, Bertrand E, Tazi J (2003) The RasGAP-associated endoribonuclease G3BP assembles stress granules. J Cell Biol 160:823\u2013831","journal-title":"J Cell Biol"},{"key":"2832_CR34","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1186\/s13024-019-0310-z","volume":"14","author":"J Chew","year":"2019","unstructured":"Chew J, Cook C, Gendron TF, Jansen-West K, Del Rosso G, Daughrity LM, Castanedes-Casey M, Kurti A et al (2019) Aberrant deposition of stress granule-resident proteins linked to C9orf72-associated TDP-43 proteinopathy. Mol Neurodegener 14:9","journal-title":"Mol Neurodegener"},{"key":"2832_CR35","doi-asserted-by":"publisher","first-page":"3696","DOI":"10.1074\/jbc.RA118.006351","volume":"294","author":"Y Chen","year":"2019","unstructured":"Chen Y, Cohen TJ (2019) Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation. J Biol Chem 294:3696\u20133706","journal-title":"J Biol Chem"},{"key":"2832_CR36","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1007\/978-3-319-29073-7_11","volume":"907","author":"AC Fan","year":"2016","unstructured":"Fan AC, Leung AK (2016) RNA granules and diseases: a case study of stress granules in ALS and FTLD. Adv Exp Med Biol 907:263\u2013296","journal-title":"Adv Exp Med Biol"},{"key":"2832_CR37","doi-asserted-by":"publisher","first-page":"173","DOI":"10.1007\/978-3-319-89689-2_7","volume":"20","author":"N Fernandes","year":"2018","unstructured":"Fernandes N, Eshleman N, Buchan JR (2018) Stress granules and ALS: a case of causation or correlation? Adv Neurobiol 20:173\u2013212","journal-title":"Adv Neurobiol"},{"key":"2832_CR38","doi-asserted-by":"publisher","first-page":"e39578","DOI":"10.7554\/eLife.39578","volume":"8","author":"P Zhang","year":"2019","unstructured":"Zhang P, Fan B, Yang P, Temirov J, Messing J, Kim HJ, Taylor JP (2019) Chronic optogenetic induction of stress granules is cytotoxic and reveals the evolution of ALS-FTD pathology. Elife 8:e39578","journal-title":"Elife"},{"key":"2832_CR39","doi-asserted-by":"publisher","first-page":"7551","DOI":"10.1038\/s41598-018-25767-0","volume":"8","author":"Y Khalfallah","year":"2018","unstructured":"Khalfallah Y, Kuta R, Grasmuck C, Prat A, Durham HD, Vande Velde C (2018) TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types. Sci Rep 8:7551","journal-title":"Sci Rep"},{"key":"2832_CR40","doi-asserted-by":"publisher","first-page":"400","DOI":"10.1016\/j.nbd.2008.02.009","volume":"30","author":"JD Atkin","year":"2008","unstructured":"Atkin JD, Farg MA, Walker AK, McLean C, Tomas D, Horne MK (2008) Endoplasmic reticulum stress and induction of the unfolded protein response in human sporadic amyotrophic lateral sclerosis. Neurobiol Dis 30:400\u2013407","journal-title":"Neurobiol Dis"},{"key":"2832_CR41","doi-asserted-by":"publisher","first-page":"37","DOI":"10.1080\/14728222.2016.1254197","volume":"21","author":"E Perri","year":"2017","unstructured":"Perri E, Parakh S, Atkin J (2017) Protein disulphide isomerases: emerging roles of PDI and ERp57 in the nervous system and as therapeutic targets for ALS. Expert Opin Ther Targets 21:37\u201349","journal-title":"Expert Opin Ther Targets"},{"key":"2832_CR42","doi-asserted-by":"publisher","first-page":"470","DOI":"10.1016\/j.nbd.2009.08.013","volume":"36","author":"Y Ito","year":"2009","unstructured":"Ito Y, Yamada M, Tanaka H, Aida K, Tsuruma K, Shimazawa M, Hozumi I, Inuzuka T et al (2009) Involvement of CHOP, an ER-stress apoptotic mediator, in both human sporadic ALS and ALS model mice. Neurobiol Dis 36:470\u2013476","journal-title":"Neurobiol Dis"},{"key":"2832_CR43","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1097\/NEN.0b013e3181d44992","volume":"69","author":"S Sasaki","year":"2010","unstructured":"Sasaki S (2010) Endoplasmic reticulum stress in motor neurons of the spinal cord in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 69:346\u2013355","journal-title":"J Neuropathol Exp Neurol"},{"key":"2832_CR44","doi-asserted-by":"publisher","first-page":"3111","DOI":"10.1093\/brain\/awm190","volume":"130","author":"EV Ilieva","year":"2007","unstructured":"Ilieva EV, Ayala V, Jove M, Dalfo E, Cacabelos D, Povedano M, Bellmunt MJ, Ferrer I et al (2007) Oxidative and endoplasmic reticulum stress interplay in sporadic amyotrophic lateral sclerosis. Brain 130:3111\u20133123","journal-title":"Brain"},{"key":"2832_CR45","doi-asserted-by":"publisher","first-page":"444","DOI":"10.3109\/17482968.2011.594055","volume":"12","author":"Y Honjo","year":"2011","unstructured":"Honjo Y, Kaneko S, Ito H, Horibe T, Nagashima M, Nakamura M, Fujita K, Takahashi R et al (2011) Protein disulfide isomerase-immunopositive inclusions in patients with amyotrophic lateral sclerosis. Amyotroph Lateral Scler 12:444\u2013450","journal-title":"Amyotroph Lateral Scler"},{"key":"2832_CR46","doi-asserted-by":"publisher","first-page":"e25545","DOI":"10.1371\/journal.pone.0025545","volume":"6","author":"G Nardo","year":"2011","unstructured":"Nardo G, Pozzi S, Pignataro M, Lauranzano E, Spano G, Garbelli S, Mantovani S, Marinou K et al (2011) Amyotrophic lateral sclerosis multiprotein biomarkers in peripheral blood mononuclear cells. PLoS ONE 6:e25545","journal-title":"PLoS ONE"},{"key":"2832_CR47","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/j.freeradbiomed.2013.01.001","volume":"58","author":"CT Kwok","year":"2013","unstructured":"Kwok CT, Morris AG, Frampton J, Smith B, Shaw CE, de Belleroche J (2013) Association studies indicate that protein disulfide isomerase is a risk factor in amyotrophic lateral sclerosis. Free Radic Biol Med 58:81\u201386","journal-title":"Free Radic Biol Med"},{"key":"2832_CR48","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1007\/s00401-018-1934-8","volume":"137","author":"M Gautam","year":"2019","unstructured":"Gautam M, Jara JH, Kocak N, Rylaarsdam LE, Kim KD, Bigio EH, Hande Ozdinler P (2019) Mitochondria, ER, and nuclear membrane defects reveal early mechanisms for upper motor neuron vulnerability with respect to TDP-43 pathology. Acta Neuropathol 137:47\u201369","journal-title":"Acta Neuropathol"},{"key":"2832_CR49","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1038\/nn.2297","volume":"12","author":"S Saxena","year":"2009","unstructured":"Saxena S, Cabuy E, Caroni P (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat Neurosci 12:627\u2013636","journal-title":"Nat Neurosci"},{"key":"2832_CR50","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/0006-291X(74)90925-5","volume":"58","author":"SC Kuo","year":"1974","unstructured":"Kuo SC, Lampen JO (1974) Tunicamycin\u2013an inhibitor of yeast glycoprotein synthesis. Biochem Biophys Res Commun 58:287\u2013295","journal-title":"Biochem Biophys Res Commun"},{"key":"2832_CR51","doi-asserted-by":"publisher","first-page":"209","DOI":"10.1002\/aja.1001940306","volume":"194","author":"NR Cashman","year":"1992","unstructured":"Cashman NR, Durham HD, Blusztajn JK, Oda K, Tabira T, Shaw IT, Dahrouge S, Antel JP (1992) Neuroblastoma x spinal cord (NSC) hybrid cell lines resemble developing motor neurons. Dev Dyn 194:209\u2013221","journal-title":"Dev Dyn"},{"key":"2832_CR52","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.1016\/j.neuint.2013.03.008","volume":"62","author":"O Maier","year":"2013","unstructured":"Maier O, Bohm J, Dahm M, Bruck S, Beyer C, Johann S (2013) Differentiated NSC-34 motoneuron-like cells as experimental model for cholinergic neurodegeneration. Neurochem Int 62:1029\u20131038","journal-title":"Neurochem Int"},{"key":"2832_CR53","doi-asserted-by":"publisher","first-page":"1895","DOI":"10.1046\/j.1471-4159.2000.0741895.x","volume":"74","author":"CJ Eggett","year":"2000","unstructured":"Eggett CJ, Crosier S, Manning P, Cookson MR, Menzies FM, McNeil CJ, Shaw PJ (2000) Development and characterisation of a glutamate-sensitive motor neurone cell line. J Neurochem 74:1895\u20131902","journal-title":"J Neurochem"},{"key":"2832_CR54","doi-asserted-by":"publisher","first-page":"1241","DOI":"10.1038\/emboj.2011.471","volume":"31","author":"TJ Cohen","year":"2012","unstructured":"Cohen TJ, Hwang AW, Unger T, Trojanowski JQ, Lee VM (2012) Redox signalling directly regulates TDP-43 via cysteine oxidation and disulphide cross-linking. EMBO J 31:1241\u20131252","journal-title":"EMBO J"},{"key":"2832_CR55","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","volume":"150","author":"PK Smith","year":"1985","unstructured":"Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM et al (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150:76\u201385","journal-title":"Anal Biochem"},{"key":"2832_CR56","first-page":"552","volume":"29","author":"MJ Blanca","year":"2017","unstructured":"Blanca MJ, Alarcon R, Arnau J, Bono R, Bendayan R (2017) Non-normal data: is ANOVA still a valid option? Psicothema 29:552\u2013557","journal-title":"Psicothema"},{"key":"2832_CR57","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1186\/s40478-017-0480-2","volume":"5","author":"RH Tan","year":"2017","unstructured":"Tan RH, Yang Y, Kim WS, Dobson-Stone C, Kwok JB, Kiernan MC, Halliday GM (2017) Distinct TDP-43 inclusion morphologies in frontotemporal lobar degeneration with and without amyotrophic lateral sclerosis. Acta Neuropathol Commun 5:76","journal-title":"Acta Neuropathol Commun"},{"key":"2832_CR58","doi-asserted-by":"publisher","first-page":"1140","DOI":"10.7150\/ijbs.12657","volume":"11","author":"X Wang","year":"2015","unstructured":"Wang X, Zhou S, Ding X, Ma M, Zhang J, Zhou Y, Wu E, Teng J (2015) Activation of ER stress and autophagy induced by TDP-43 A315T as pathogenic mechanism and the corresponding histological changes in skin as potential biomarker for ALS with the mutation. Int J Biol Sci 11:1140\u20131149","journal-title":"Int J Biol Sci"},{"key":"2832_CR59","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1038\/sj.embor.7400048","volume":"5","author":"G Rena","year":"2004","unstructured":"Rena G, Bain J, Elliott M, Cohen P (2004) D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a. EMBO Rep 5:60\u201365","journal-title":"EMBO Rep"},{"key":"2832_CR60","doi-asserted-by":"publisher","first-page":"F933","DOI":"10.1152\/ajprenal.00197.2014","volume":"309","author":"K Solocinski","year":"2015","unstructured":"Solocinski K, Richards J, All S, Cheng KY, Khundmiri SJ, Gumz ML (2015) Transcriptional regulation of NHE3 and SGLT1 by the circadian clock protein Per1 in proximal tubule cells. Am J Physiol Renal Physiol 309:F933\u2013F942","journal-title":"Am J Physiol Renal Physiol"},{"key":"2832_CR61","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.jns.2012.02.027","volume":"317","author":"C Leggett","year":"2012","unstructured":"Leggett C, McGehee DS, Mastrianni J, Yang W, Bai T, Brorson JR (2012) Tunicamycin produces TDP-43 cytoplasmic inclusions in cultured brain organotypic slices. J Neurol Sci 317:66\u201373","journal-title":"J Neurol Sci"},{"key":"2832_CR62","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1007\/s00401-011-0850-y","volume":"122","author":"V Ayala","year":"2011","unstructured":"Ayala V, Granado-Serrano AB, Cacabelos D, Naudi A, Ilieva EV, Boada J, Caraballo-Miralles V, Llado J et al (2011) Cell stress induces TDP-43 pathological changes associated with ERK1\/2 dysfunction: implications in ALS. Acta Neuropathol 122:259\u2013270","journal-title":"Acta Neuropathol"},{"key":"2832_CR63","doi-asserted-by":"publisher","first-page":"e81170","DOI":"10.1371\/journal.pone.0081170","volume":"8","author":"AK Walker","year":"2013","unstructured":"Walker AK, Soo KY, Sundaramoorthy V, Parakh S, Ma Y, Farg MA, Wallace RH, Crouch PJ et al (2013) ALS-associated TDP-43 induces endoplasmic reticulum stress, which drives cytoplasmic TDP-43 accumulation and stress granule formation. PLoS ONE 8:e81170","journal-title":"PLoS ONE"},{"key":"2832_CR64","doi-asserted-by":"publisher","first-page":"963","DOI":"10.1042\/bst0300963","volume":"30","author":"N Kedersha","year":"2002","unstructured":"Kedersha N, Anderson P (2002) Stress granules: sites of mRNA triage that regulate mRNA stability and translatability. Biochem Soc Trans 30:963\u2013969","journal-title":"Biochem Soc Trans"},{"key":"2832_CR65","doi-asserted-by":"publisher","first-page":"1400","DOI":"10.1093\/hmg\/ddr021","volume":"20","author":"KK McDonald","year":"2011","unstructured":"McDonald KK, Aulas A, Destroismaisons L, Pickles S, Beleac E, Camu W, Rouleau GA, Vande Velde C (2011) TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. Hum Mol Genet 20:1400\u20131410","journal-title":"Hum Mol Genet"},{"key":"2832_CR66","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1111\/j.1471-4159.2009.06383.x","volume":"111","author":"C Colombrita","year":"2009","unstructured":"Colombrita C, Zennaro E, Fallini C, Weber M, Sommacal A, Buratti E, Silani V, Ratti A (2009) TDP-43 is recruited to stress granules in conditions of oxidative insult. J Neurochem 111:1051\u20131061","journal-title":"J Neurochem"},{"key":"2832_CR67","doi-asserted-by":"publisher","first-page":"1098","DOI":"10.1128\/MCB.01279-10","volume":"31","author":"CM Dewey","year":"2011","unstructured":"Dewey CM, Cenik B, Sephton CF, Dries DR, Mayer P 3rd, Good SK, Johnson BA, Herz J et al (2011) TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol Cell Biol 31:1098\u20131108","journal-title":"Mol Cell Biol"},{"issue":"987\u20131000","key":"2832_CR68","first-page":"e7","volume":"24","author":"EM Hock","year":"2018","unstructured":"Hock EM, Maniecka Z, Hruska-Plochan M, Reber S, Laferriere F, Sahadevan MKS, Ederle H, Gittings L et al (2018) Hypertonic stress causes cytoplasmic translocation of neuronal, but not astrocytic, FUS due to impaired transportin function. Cell Rep 24(987\u20131000):e7","journal-title":"Cell Rep"},{"key":"2832_CR69","doi-asserted-by":"publisher","first-page":"e67433","DOI":"10.1371\/journal.pone.0067433","volume":"8","author":"D Moujalled","year":"2013","unstructured":"Moujalled D, James JL, Parker SJ, Lidgerwood GE, Duncan C, Meyerowitz J, Nonaka T, Hasegawa M et al (2013) Kinase inhibitor screening identifies cyclin-dependent kinases and glycogen synthase kinase 3 as potential modulators of TDP-43 cytosolic accumulation during cell stress. PLoS ONE 8:e67433","journal-title":"PLoS ONE"},{"key":"2832_CR70","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1186\/1750-1326-6-57","volume":"6","author":"J Meyerowitz","year":"2011","unstructured":"Meyerowitz J, Parker SJ, Vella LJ, Ng D, Price KA, Liddell JR, Caragounis A, Li QX et al (2011) C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress. Mol Neurodegener 6:57","journal-title":"Mol Neurodegener"},{"key":"2832_CR71","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.neuron.2016.05.021","volume":"91","author":"S Lee","year":"2016","unstructured":"Lee S, Shang Y, Redmond SA, Urisman A, Tang AA, Li KH, Burlingame AL, Pak RA et al (2016) Activation of HIPK2 promotes ER stress-mediated neurodegeneration in amyotrophic lateral sclerosis. Neuron 91:41\u201355","journal-title":"Neuron"},{"key":"2832_CR72","doi-asserted-by":"publisher","first-page":"862","DOI":"10.1016\/j.nbd.2011.12.002","volume":"45","author":"Y Iguchi","year":"2012","unstructured":"Iguchi Y, Katsuno M, Takagi S, Ishigaki S, Niwa J, Hasegawa M, Tanaka F, Sobue G (2012) Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies. Neurobiol Dis 45:862\u2013870","journal-title":"Neurobiol Dis"},{"key":"2832_CR73","doi-asserted-by":"publisher","first-page":"e0196528","DOI":"10.1371\/journal.pone.0196528","volume":"13","author":"P Baskaran","year":"2018","unstructured":"Baskaran P, Shaw C, Guthrie S (2018) TDP-43 causes neurotoxicity and cytoskeletal dysfunction in primary cortical neurons. PLoS ONE 13:e0196528","journal-title":"PLoS ONE"},{"key":"2832_CR74","doi-asserted-by":"publisher","first-page":"2063","DOI":"10.1002\/stem.2388","volume":"34","author":"R Dafinca","year":"2016","unstructured":"Dafinca R, Scaber J, Ababneh N, Lalic T, Weir G, Christian H, Vowles J, Douglas AG et al (2016) C9orf72 hexanucleotide expansions are associated with altered endoplasmic reticulum calcium homeostasis and stress granule formation in induced pluripotent stem cell-derived neurons from patients with amyotrophic lateral sclerosis and frontotemporal dementia. Stem Cells 34:2063\u20132078","journal-title":"Stem Cells"},{"key":"2832_CR75","doi-asserted-by":"publisher","DOI":"10.1007\/s12035-018-1249-8","author":"D Posa","year":"2018","unstructured":"Posa D, Martinez-Gonzalez L, Bartolome F, Nagaraj S, Porras G, Martinez A, Martin-Requero A (2018) Recapitulation of pathological TDP-43 features in immortalized lymphocytes from sporadic ALS patients. Mol Neurobiol. \n                  https:\/\/doi.org\/10.1007\/s12035-018-1249-8","journal-title":"Mol Neurobiol"}],"container-title":["Neurochemical Research"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-019-02832-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s11064-019-02832-2\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s11064-019-02832-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,7,4]],"date-time":"2020-07-04T23:13:29Z","timestamp":1593904409000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s11064-019-02832-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,7,6]]},"references-count":75,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2020,6]]}},"alternative-id":["2832"],"URL":"https:\/\/doi.org\/10.1007\/s11064-019-02832-2","relation":{},"ISSN":["0364-3190","1573-6903"],"issn-type":[{"value":"0364-3190","type":"print"},{"value":"1573-6903","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,7,6]]},"assertion":[{"value":"18 April 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 June 2019","order":2,"name":"revised","label":"Revised","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 June 2019","order":3,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 July 2019","order":4,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with Ethical Standards"}},{"value":"The authors declare no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}