{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T07:16:30Z","timestamp":1793949390335,"version":"4.8.0"},"reference-count":101,"publisher":"Springer Science and Business Media LLC","issue":"5","license":[{"start":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T00:00:00Z","timestamp":1777507200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T00:00:00Z","timestamp":1777507200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R35CA197589"],"award-info":[{"award-number":["R35CA197589"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Cell Biol"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1038\/s41556-026-01936-6","type":"journal-article","created":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T09:02:35Z","timestamp":1777539755000},"page":"930-945","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["The atypical E3 ligase HOIL-1 safeguards the ribosome during cellular stress"],"prefix":"10.1038","volume":"28","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6053-9345","authenticated-orcid":false,"given":"Todd","family":"Douglas","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pengju","family":"Nie","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4637-5655","authenticated-orcid":false,"given":"Jiasheng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3355-5788","authenticated-orcid":false,"given":"Kyrillos S.","family":"Abdallah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiping","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meghan","family":"McReynolds","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5620-5951","authenticated-orcid":false,"given":"Kazuhiro","family":"Iwai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0472-7648","authenticated-orcid":false,"given":"Junmin","family":"Peng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wendy V.","family":"Gilbert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lawrence H.","family":"Young","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8456-2005","authenticated-orcid":false,"given":"Craig M.","family":"Crews","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,4,30]]},"reference":[{"key":"1936_CR1","doi-asserted-by":"publisher","first-page":"eaat5314","DOI":"10.1126\/science.aat5314","volume":"368","author":"M Costa-Mattioli","year":"2020","unstructured":"Costa-Mattioli, M. & Walter, P. The integrated stress response: from mechanism to disease. Science 368, eaat5314 (2020).","journal-title":"Science"},{"key":"1936_CR2","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1016\/j.cell.2020.06.006","volume":"182","author":"CC Wu","year":"2020","unstructured":"Wu, C. C., Peterson, A., Zinshteyn, B., Regot, S. & Green, R. Ribosome collisions trigger general stress responses to regulate cell fate. Cell 182, 404\u2013416 (2020).","journal-title":"Cell"},{"key":"1936_CR3","doi-asserted-by":"publisher","first-page":"2036","DOI":"10.1016\/j.cmet.2022.10.011","volume":"34","author":"G Snieckute","year":"2022","unstructured":"Snieckute, G. et al. Ribosome stalling is a signal for metabolic regulation by the ribotoxic stress response. Cell Metab. 34, 2036\u20132046 (2022).","journal-title":"Cell Metab."},{"key":"1936_CR4","doi-asserted-by":"publisher","DOI":"10.1126\/science.adf3208","volume":"382","author":"G Snieckute","year":"2023","unstructured":"Snieckute, G. et al. ROS-induced ribosome impairment underlies ZAK\u03b1-mediated metabolic decline in obesity and aging. Science 382, eadf3208 (2023).","journal-title":"Science"},{"key":"1936_CR5","doi-asserted-by":"publisher","first-page":"1178","DOI":"10.1038\/ni.2457","volume":"13","author":"B Boisson","year":"2012","unstructured":"Boisson, B. et al. Immunodeficiency, autoinflammation and amylopectinosis in humans with inherited HOIL-1 and LUBAC deficiency. Nat. Immunol. 13, 1178\u20131186 (2012).","journal-title":"Nat. Immunol."},{"key":"1936_CR6","doi-asserted-by":"publisher","first-page":"914","DOI":"10.1002\/ana.23963","volume":"74","author":"J Nilsson","year":"2013","unstructured":"Nilsson, J. et al. Polyglucosan body myopathy caused by defective ubiquitin ligase RBCK1. Ann. Neurol. 74, 914\u2013919 (2013).","journal-title":"Ann. Neurol."},{"key":"1936_CR7","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/gm471","volume":"5","author":"K Wang","year":"2013","unstructured":"Wang, K. et al. Whole-genome DNA\/RNA sequencing identifies truncating mutations in RBCK1 in anovel Mendelian disease with neuromuscular and cardiac involvement. Genome Med. 5, 1\u20138 (2013).","journal-title":"Genome Med."},{"key":"1936_CR8","doi-asserted-by":"publisher","first-page":"394","DOI":"10.1007\/s00415-017-8710-x","volume":"265","author":"M Krenn","year":"2018","unstructured":"Krenn, M. et al. Mutations outside the N-terminal part of RBCK1 may cause polyglucosan body myopathy with immunological dysfunction: expanding the genotype\u2013phenotype spectrum. J. Neurol. 265, 394\u2013401 (2018).","journal-title":"J. Neurol."},{"key":"1936_CR9","doi-asserted-by":"publisher","first-page":"1002","DOI":"10.1002\/jimd.12234","volume":"43","author":"R Phadke","year":"2020","unstructured":"Phadke, R. et al. RBCK1-related disease: a rare multisystem disorder with polyglucosan storage auto-inflammation recurrent infections skeletal AND cardiac myopathy\u2014four additional patients AND a review of the current literature. J. Inherit. Metab. Dis. 43, 1002\u20131013 (2020).","journal-title":"J. Inherit. Metab. Dis."},{"key":"1936_CR10","doi-asserted-by":"publisher","first-page":"45","DOI":"10.17712\/nsj.2022.1.20210681","volume":"27","author":"T AlAnzi","year":"2022","unstructured":"AlAnzi, T., Al Harbi, F., AlGhamdi, A. & Mohamed, S. A novel variant of RBCK1 gene causes mild polyglucosan myopathy. Neurosciences 27, 45\u201349 (2022).","journal-title":"Neurosciences"},{"key":"1936_CR11","doi-asserted-by":"publisher","first-page":"1","DOI":"10.3390\/genes14010182","volume":"14","author":"C Maurer","year":"2023","unstructured":"Maurer, C. et al. Genetic insights from consanguineous cardiomyopathy families. Genes 14, 1\u201311 (2023).","journal-title":"Genes"},{"key":"1936_CR12","first-page":"101031","volume":"38","author":"M P\u00fchringer","year":"2024","unstructured":"P\u00fchringer, M., Eisenk\u00f6lbl, A. & Gr\u00f6ppel, G. Expanding the phenotype of RBCK1-associated polyglucosan body myopathy type 1. Mol. Genet. Metab. Rep. 38, 101031 (2024).","journal-title":"Mol. Genet. Metab. Rep."},{"key":"1936_CR13","doi-asserted-by":"publisher","first-page":"1472","DOI":"10.1002\/ehf2.14702","volume":"11","author":"M MozafaryBazargany","year":"2024","unstructured":"MozafaryBazargany, M. et al. A novel likely pathogenic homozygous RBCK1 variant in dilated cardiomyopathy with muscle weakness. ESC Heart Fail. 11, 1472\u20131482 (2024).","journal-title":"ESC Heart Fail."},{"key":"1936_CR14","doi-asserted-by":"publisher","DOI":"10.1002\/mgg3.2432","volume":"12","author":"Q Sun","year":"2024","unstructured":"Sun, Q., Xie, Z., Song, L. & Fu, D. A case of polyglucosan body myopathy caused by an RBCK1 gene variant and literature review. Mol. Genet. Genomic Med. 12, e2432 (2024).","journal-title":"Mol. Genet. Genomic Med."},{"key":"1936_CR15","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1038\/nature09814","volume":"471","author":"F Ikeda","year":"2011","unstructured":"Ikeda, F. et al. SHARPIN forms a linear ubiquitin ligase complex regulating NF-\u03baB activity and apoptosis. Nature 471, 637\u2013641 (2011).","journal-title":"Nature"},{"key":"1936_CR16","doi-asserted-by":"publisher","first-page":"2463","DOI":"10.1038\/emboj.2013.184","volume":"32","author":"Y Sasaki","year":"2013","unstructured":"Sasaki, Y. et al. Defective immune responses in mice lacking LUBAC-mediated linear ubiquitination in B cells. EMBO J. 32, 2463\u20132476 (2013).","journal-title":"EMBO J."},{"key":"1936_CR17","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1084\/jem.20141130","volume":"212","author":"B Boisson","year":"2015","unstructured":"Boisson, B. et al. Human HOIP and LUBAC deficiency underlies autoinflammation, immunodeficiency, amylopectinosis, and lymphangiectasia. J. Exp. Med. 212, 939\u2013951 (2015).","journal-title":"J. Exp. Med."},{"key":"1936_CR18","doi-asserted-by":"publisher","DOI":"10.1038\/srep36135","volume":"6","author":"K Okamura","year":"2016","unstructured":"Okamura, K. et al. Survival of mature T cells depends on signaling through HOIP. Sci. Rep. 6, 36135 (2016).","journal-title":"Sci. Rep."},{"key":"1936_CR19","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms13353","volume":"7","author":"CE Teh","year":"2016","unstructured":"Teh, C. E. et al. Linear ubiquitin chain assembly complex coordinates late thymic T-cell differentiation and regulatory T-cell homeostasis. Nat. Commun. 7, 13353 (2016).","journal-title":"Nat. Commun."},{"key":"1936_CR20","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2021.658048","volume":"12","author":"J Wang","year":"2021","unstructured":"Wang, J. et al. LUBAC suppresses IL-21-induced apoptosis in CD40-activated murine B cells and promotes germinal center B cell survival and the T-dependent antibody response. Front. Immunol. 12, 658048 (2021).","journal-title":"Front. Immunol."},{"key":"1936_CR21","doi-asserted-by":"publisher","first-page":"2946","DOI":"10.1038\/s41418-021-00850-8","volume":"28","author":"R Jain","year":"2021","unstructured":"Jain, R. et al. Dual roles for LUBAC signaling in thymic epithelial cell development and survival. Cell Death Differ. 28, 2946\u20132956 (2021).","journal-title":"Cell Death Differ."},{"key":"1936_CR22","doi-asserted-by":"publisher","first-page":"e171108","DOI":"10.1172\/jci.insight.171108","volume":"9","author":"Y Fuseya","year":"2024","unstructured":"Fuseya, Y. et al. Attenuation of HOIL-1L ligase activity promotes systemic autoimmune disorders by augmenting linear ubiquitin signaling. JCI Insight 9, e171108 (2024).","journal-title":"JCI Insight"},{"key":"1936_CR23","doi-asserted-by":"publisher","first-page":"764","DOI":"10.1038\/s41590-024-01817-w","volume":"25","author":"H Oda","year":"2024","unstructured":"Oda, H. et al. Biallelic human SHARPIN loss of function induces autoinflammation and immunodeficiency. Nat. Immunol. 25, 764\u2013777 (2024).","journal-title":"Nat. Immunol."},{"key":"1936_CR24","doi-asserted-by":"publisher","DOI":"10.15252\/embj.2021109700","volume":"41","author":"IR Kelsall","year":"2022","unstructured":"Kelsall, I. R. et al. HOIL-1 ubiquitin ligase activity targets unbranched glucosaccharides and is required to prevent polyglucosan accumulation. EMBO J. 41, e109700 (2022).","journal-title":"EMBO J."},{"key":"1936_CR25","doi-asserted-by":"publisher","first-page":"13293","DOI":"10.1073\/pnas.1905873116","volume":"116","author":"IR Kelsall","year":"2019","unstructured":"Kelsall, I. R., Zhang, J., Knebel, A., Arthur, J. S. C. & Cohen, P. The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells. PNAS 116, 13293\u201313298 (2019).","journal-title":"PNAS"},{"key":"1936_CR26","doi-asserted-by":"publisher","first-page":"5909","DOI":"10.1111\/febs.15896","volume":"288","author":"T Petrova","year":"2021","unstructured":"Petrova, T., Zhang, J., Nanda, S. K., Figueras-Vadillo, C. & Cohen, P. HOIL-1-catalysed, ester-linked ubiquitylation restricts IL-18 signaling in cytotoxic T cells but promotes TLR signalling in macrophages. FEBS J. 288, 5909\u20135924 (2021).","journal-title":"FEBS J."},{"key":"1936_CR27","doi-asserted-by":"publisher","first-page":"2419","DOI":"10.1042\/BCJ20220510","volume":"479","author":"EH McCrory","year":"2022","unstructured":"McCrory, E. H., Akimov, V., Cohen, P. & Blagoev, B. Identification of ester-linked ubiquitylation sites during TLR7 signalling increases the number of inter-ubiquitin linkages from 8 to 12. Biochem. J. 479, 2419\u20132431 (2022).","journal-title":"Biochem. J."},{"key":"1936_CR28","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1038\/s41586-018-0064-8","volume":"557","author":"N Peltzer","year":"2018","unstructured":"Peltzer, N. et al. LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis. Nature 557, 112\u2013117 (2018).","journal-title":"Nature"},{"key":"1936_CR29","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1038\/ncb1821","volume":"11","author":"F Tokunaga","year":"2009","unstructured":"Tokunaga, F. et al. Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation. Nat. Cell Biol. 11, 123\u2013132 (2009).","journal-title":"Nat. Cell Biol."},{"key":"1936_CR30","doi-asserted-by":"publisher","first-page":"1192","DOI":"10.1016\/j.celrep.2018.03.112","volume":"23","author":"H Fujita","year":"2018","unstructured":"Fujita, H. et al. Cooperative Domain formation by homologous motifs in HOIL-1L and SHARPIN plays a crucial role in LUBAC stabilization. Cell Rep. 23, 1192\u20131204 (2018).","journal-title":"Cell Rep."},{"key":"1936_CR31","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1038\/s41556-020-0517-9","volume":"22","author":"Y Fuseya","year":"2020","unstructured":"Fuseya, Y. et al. The HOIL-1L ligase modulates immune signalling and cell death via monoubiquitination of LUBAC. Nat. Cell Biol. 22, 663\u2013673 (2020).","journal-title":"Nat. Cell Biol."},{"key":"1936_CR32","doi-asserted-by":"publisher","first-page":"a008763","DOI":"10.1101\/cshperspect.a008763","volume":"4","author":"BJ Altman","year":"2012","unstructured":"Altman, B. J. & Rathmell, J. C. Metabolic stress in autophagy and cell death pathways. Cold Spring Harb. Perspect. Biol. 4, a008763 (2012).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"1936_CR33","doi-asserted-by":"publisher","first-page":"1131","DOI":"10.1056\/NEJM199704173361603","volume":"336","author":"G Olivetti","year":"1997","unstructured":"Olivetti, G. et al. Apoptosis in the failing human heart. New Engl. J. Med. 336, 1131\u20131141 (1997).","journal-title":"New Engl. J. Med."},{"key":"1936_CR34","doi-asserted-by":"publisher","first-page":"856","DOI":"10.1161\/01.RES.85.9.856","volume":"85","author":"S Guerra","year":"1999","unstructured":"Guerra, S. et al. Myocyte death in the failing human heart is gender dependent. Circ. Res. 85, 856\u2013866 (1999).","journal-title":"Circ. Res."},{"key":"1936_CR35","doi-asserted-by":"publisher","first-page":"1497","DOI":"10.1172\/JCI17664","volume":"111","author":"D Wencker","year":"2003","unstructured":"Wencker, D. et al. A mechanistic role for cardiac myocyte apoptosis in heart failure. J. Clin. Invest. 111, 1497\u20131504 (2003).","journal-title":"J. Clin. Invest."},{"key":"1936_CR36","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1146\/annurev.physiol.010908.163111","volume":"72","author":"RS Whelan","year":"2010","unstructured":"Whelan, R. S., Kaplinskiy, V. & Kitsis, R. N. Cell death in the pathogenesis of heart disease: mechanisms and significance. Annu. Rev. Physiol 72, 19\u201344 (2010).","journal-title":"Annu. Rev. Physiol"},{"key":"1936_CR37","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1038\/s41419-023-06183-3","volume":"14","author":"L Gao","year":"2023","unstructured":"Gao, L. et al. The mechanism of linear ubiquitination in regulating cell death and correlative diseases. Cell Death Dis. 14, 659 (2023).","journal-title":"Cell Death Dis."},{"key":"1936_CR38","doi-asserted-by":"publisher","first-page":"14240","DOI":"10.1074\/jbc.M117.798405","volume":"292","author":"P Koppula","year":"2017","unstructured":"Koppula, P., Zhang, Y., Shi, J., Li, W. & Gan, B. The glutamate\/cystine antiporter SLC7A11\/xCT enhances cancer cell dependency on glucose by exporting glutamate. J. Biol. Chem. 292, 14240\u201314249 (2017).","journal-title":"J. Biol. Chem."},{"key":"1936_CR39","doi-asserted-by":"publisher","DOI":"10.3389\/fimmu.2021.734646","volume":"12","author":"W Xu","year":"2021","unstructured":"Xu, W. et al. Comprehensive multi-omics identification of interferon-\u03b3 response characteristics reveals that RBCK1 regulates the immunosuppressive microenvironment of renal cell carcinoma. Front. Immunol. 12, 734646 (2021).","journal-title":"Front. Immunol."},{"key":"1936_CR40","doi-asserted-by":"publisher","first-page":"700","DOI":"10.1016\/j.bbrc.2018.12.164","volume":"509","author":"K Katsuya","year":"2019","unstructured":"Katsuya, K. et al. Small-molecule inhibitors of linear ubiquitin chain assembly complex (LUBAC), HOIPINs, suppress NF-\u03baB signaling. Biochem. Biophys. Res. Commun. 509, 700\u2013706 (2019).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"1936_CR41","doi-asserted-by":"publisher","first-page":"1215","DOI":"10.1016\/j.cell.2016.07.019","volume":"166","author":"RB Damgaard","year":"2016","unstructured":"Damgaard, R. B. et al. The deubiquitinase OTULIN is an essential negative regulator of inflammation and autoimmunity. Cell 166, 1215\u201312301 (2016).","journal-title":"Cell"},{"key":"1936_CR42","doi-asserted-by":"publisher","first-page":"e9324","DOI":"10.15252\/emmm.201809324","volume":"11","author":"RB Damgaard","year":"2019","unstructured":"Damgaard, R. B. et al. OTULIN deficiency in ORAS causes cell type-specific LUBAC degradation, dysregulated TNF signalling and cell death. EMBO Mol. Med. 11, e9324 (2019).","journal-title":"EMBO Mol. Med."},{"key":"1936_CR43","doi-asserted-by":"publisher","first-page":"1335","DOI":"10.1038\/cdd.2010.21","volume":"17","author":"A Caro-Maldonado","year":"2010","unstructured":"Caro-Maldonado, A. et al. Glucose deprivation induces an atypical form of apoptosis mediated by caspase-8 in Bax-, Bak-deficient cells. Cell Death Differ. 17, 1335\u20131344 (2010).","journal-title":"Cell Death Differ."},{"key":"1936_CR44","doi-asserted-by":"publisher","first-page":"e00479","DOI":"10.1128\/MCB.00479-16","volume":"37","author":"R Iurlaro","year":"2017","unstructured":"Iurlaro, R. et al. Glucose deprivation induces ATF4-mediated apoptosis through TRAIL death receptors. Mol. Cell. Biol. 37, e00479\u201316 (2017).","journal-title":"Mol. Cell. Biol."},{"key":"1936_CR45","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1161\/01.RES.85.5.403","volume":"85","author":"S Bialik","year":"1999","unstructured":"Bialik, S. et al. The mitochondrial apoptotic pathway is activated by serum and glucose deprivation in cardiac myocytes. Circ. Res. 85, 403\u2013414 (1999).","journal-title":"Circ. Res."},{"key":"1936_CR46","doi-asserted-by":"publisher","first-page":"3647","DOI":"10.1111\/febs.13369","volume":"282","author":"CL Le\u00f3n-Annicchiarico","year":"2015","unstructured":"Le\u00f3n-Annicchiarico, C. L. et al. ATF4 mediates necrosis induced by glucose deprivation and apoptosis induced by 2-deoxyglucose in the same cells. FEBS J. 282, 3647\u20133658 (2015).","journal-title":"FEBS J."},{"key":"1936_CR47","doi-asserted-by":"publisher","DOI":"10.1038\/srep22538","volume":"6","author":"B Ding","year":"2016","unstructured":"Ding, B. et al. Sestrin2 is induced by glucose starvation via the unfolded protein response and protects cells from non-canonical necroptotic cell death. Sci. Rep. 6, 22538 (2016).","journal-title":"Sci. Rep."},{"key":"1936_CR48","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-23004-3","volume":"12","author":"JY Baik","year":"2021","unstructured":"Baik, J. Y. et al. ZBP1 not RIPK1 mediates tumor necroptosis in breast cancer. Nat. Commun. 12, 2666 (2021).","journal-title":"Nat. Commun."},{"key":"1936_CR49","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/j.celrep.2017.06.037","volume":"20","author":"JC Hamann","year":"2017","unstructured":"Hamann, J. C. et al. Entosis is induced by glucose starvation. Cell Rep. 20, 201\u2013210 (2017).","journal-title":"Cell Rep."},{"key":"1936_CR50","doi-asserted-by":"publisher","first-page":"404","DOI":"10.1038\/s41556-023-01091-2","volume":"25","author":"X Liu","year":"2023","unstructured":"Liu, X. et al. Actin cytoskeleton vulnerability to disulfide stress mediates disulfidptosis. Nat. Cell Biol. 25, 404\u2013414 (2023).","journal-title":"Nat. Cell Biol."},{"key":"1936_CR51","doi-asserted-by":"publisher","first-page":"476","DOI":"10.1038\/s41556-020-0496-x","volume":"22","author":"X Liu","year":"2020","unstructured":"Liu, X. et al. Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer. Nat. Cell Biol. 22, 476\u2013486 (2020).","journal-title":"Nat. Cell Biol."},{"key":"1936_CR52","doi-asserted-by":"publisher","first-page":"731","DOI":"10.1016\/j.gendis.2020.11.010","volume":"8","author":"X Liu","year":"2021","unstructured":"Liu, X., Zhang, Y., Zhuang, L., Olszewski, K. & Gan, B. NADPH debt drives redox bankruptcy: SLC7A11\/xCT-mediated cystine uptake as a double-edged sword in cellular redox regulation. Gene. Dis 8, 731\u2013745 (2021).","journal-title":"Gene. Dis"},{"key":"1936_CR53","doi-asserted-by":"publisher","first-page":"731","DOI":"10.1038\/s41589-020-0533-x","volume":"16","author":"JM Ghergurovich","year":"2020","unstructured":"Ghergurovich, J. M. et al. A small molecule G6PD inhibitor reveals immune dependence on pentose phosphate pathway. Nat. Chem. Biol. 16, 731\u2013739 (2020).","journal-title":"Nat. Chem. Biol."},{"key":"1936_CR54","doi-asserted-by":"publisher","first-page":"1088","DOI":"10.1038\/nchembio.2454","volume":"13","author":"V Cracan","year":"2017","unstructured":"Cracan, V., Titov, D. V., Shen, H., Grabarek, Z. & Mootha, V. K. A genetically encoded tool for manipulation of NADP(+)\/NADPH in living cells. Nat. Chem. Biol. 13, 1088\u20131095 (2017).","journal-title":"Nat. Chem. Biol."},{"key":"1936_CR55","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2023.112724","volume":"42","author":"JKC Kre\u00df","year":"2023","unstructured":"Kre\u00df, J. K. C. et al. The integrated stress response effector ATF4 is an obligatory metabolic activator of NRF2. Cell Rep. 42, 112724 (2023).","journal-title":"Cell Rep."},{"key":"1936_CR56","doi-asserted-by":"publisher","first-page":"402","DOI":"10.1038\/s41586-023-06090-9","volume":"618","author":"H Foronda","year":"2023","unstructured":"Foronda, H. et al. Heteromeric clusters of ubiquitinated ER-shaping proteins drive ER-phagy. Nature 618, 402\u2013410 (2023).","journal-title":"Nature"},{"key":"1936_CR57","doi-asserted-by":"publisher","first-page":"e99847","DOI":"10.15252\/embj.201899847","volume":"38","author":"A Forrester","year":"2019","unstructured":"Forrester, A. et al. A selective ER-phagy exerts procollagen quality control via a calnexin\u2013FAM134B complex. EMBO J. 38, e99847 (2019).","journal-title":"EMBO J."},{"key":"1936_CR58","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1016\/j.molcel.2019.03.033","volume":"74","author":"H Chino","year":"2019","unstructured":"Chino, H., Hatta, T., Natsume, T. & Mizushima, N. Intrinsically disordered protein TEX264 mediates ER-phagy. Mol. Cell 74, 909\u2013921 (2019).","journal-title":"Mol. Cell"},{"key":"1936_CR59","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1016\/j.cell.2020.02.017","volume":"180","author":"JR Liang","year":"2020","unstructured":"Liang, J. R. et al. A genome-wide ER-phagy screen highlights key roles of mitochondrial metabolism and ER-resident UFMylation. Cell 180, 1160\u20131177 (2020).","journal-title":"Cell"},{"key":"1936_CR60","doi-asserted-by":"publisher","first-page":"135","DOI":"10.1038\/s41556-017-0007-x","volume":"20","author":"H An","year":"2018","unstructured":"An, H. & Harper, J. W. Systematic analysis of ribophagy in human cells reveals bystander flux during selective autophagy. Nat. Cell Biol. 20, 135\u2013143 (2018).","journal-title":"Nat. Cell Biol."},{"key":"1936_CR61","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1016\/j.molcel.2016.11.039","volume":"65","author":"S Juszkiewicz","year":"2017","unstructured":"Juszkiewicz, S. & Hegde, R. S. Initiation of quality control during poly(A) translation requires site-specific ribosome ubiquitination. Mol. Cell 65, 743\u2013750 (2017).","journal-title":"Mol. Cell"},{"key":"1936_CR62","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-00188-1","volume":"8","author":"Y Matsuo","year":"2017","unstructured":"Matsuo, Y. et al. Ubiquitination of stalled ribosome triggers ribosome-associated quality control. Nat. Commun. 8, 159 (2017).","journal-title":"Nat. Commun."},{"key":"1936_CR63","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1007\/s00294-020-01111-w","volume":"67","author":"S Meydan","year":"2021","unstructured":"Meydan, S. & Guydosh, N. R. A cellular handbook for collided ribosomes: surveillance pathways and collision types. Curr. Genet. 67, 19\u201326 (2021).","journal-title":"Curr. Genet."},{"key":"1936_CR64","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1016\/j.molcel.2020.11.033","volume":"81","author":"LL Yan","year":"2021","unstructured":"Yan, L. L. & Zaher, H. S. Ribosome quality control antagonizes the activation of the integrated stress response on colliding ribosomes. Mol. Cell 81, 614\u2013628 (2021).","journal-title":"Mol. Cell"},{"key":"1936_CR65","doi-asserted-by":"publisher","first-page":"3652","DOI":"10.1016\/j.cell.2024.05.018","volume":"187","author":"NK Sinha","year":"2024","unstructured":"Sinha, N.K. et al. The ribotoxic stress response drives UV-mediated cell death. Cell 187, 3652\u20133670 (2024).","journal-title":"Cell"},{"key":"1936_CR66","doi-asserted-by":"publisher","first-page":"e100276","DOI":"10.15252\/embj.2018100276","volume":"38","author":"K Ikeuchi","year":"2019","unstructured":"Ikeuchi, K. et al. Collided ribosomes form a unique structural interface to induce Hel2-driven quality control pathways. EMBO J. 38, e100276 (2019).","journal-title":"EMBO J."},{"key":"1936_CR67","doi-asserted-by":"publisher","first-page":"469","DOI":"10.1016\/j.molcel.2018.08.037","volume":"72","author":"S Juszkiewicz","year":"2018","unstructured":"Juszkiewicz, S. et al. ZNF598 is a quality control sensor of collided ribosomes. Mol. Cell 72, 469\u2013481 (2018).","journal-title":"Mol. Cell"},{"key":"1936_CR68","doi-asserted-by":"publisher","first-page":"e58828","DOI":"10.7554\/eLife.58828","volume":"9","author":"NK Sinha","year":"2020","unstructured":"Sinha, N. K. et al. EDF1 coordinates cellular responses to ribosome collisions. eLife 9, e58828 (2020).","journal-title":"eLife"},{"key":"1936_CR69","doi-asserted-by":"publisher","first-page":"e60038","DOI":"10.7554\/eLife.60038","volume":"9","author":"S Juszkiewicz","year":"2020","unstructured":"Juszkiewicz, S. et al. Ribosome collisions trigger cis-acting feedback inhibition of translation initiation. eLife 9, e60038 (2020).","journal-title":"eLife"},{"key":"1936_CR70","doi-asserted-by":"publisher","first-page":"950","DOI":"10.1016\/j.molcel.2020.07.007","volume":"79","author":"KL Hickey","year":"2020","unstructured":"Hickey, K. L. et al. GIGYF2 and 4EHP inhibit translation initiation of defective messenger RNAs to assist ribosome-associated quality control. Mol. Cell 79, 950\u2013962 (2020).","journal-title":"Mol. Cell"},{"key":"1936_CR71","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1038\/s41422-019-0236-6","volume":"30","author":"L Wang","year":"2020","unstructured":"Wang, L. et al. UFMylation of RPL26 links translocation-associated quality control to endoplasmic reticulum protein homeostasis. Cell Res. 30, 5\u201320 (2020).","journal-title":"Cell Res."},{"key":"1936_CR72","doi-asserted-by":"publisher","first-page":"e1500154","DOI":"10.1126\/sciadv.1500154","volume":"1","author":"L Arthur","year":"2015","unstructured":"Arthur, L. et al. Translational control by lysine-encoding A-rich sequences. Sci. Adv. 1, e1500154 (2015).","journal-title":"Sci. Adv."},{"key":"1936_CR73","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1038\/33198","volume":"392","author":"AW Craig","year":"1998","unstructured":"Craig, A. W., Haghighat, A., Yu, A. T. & Sonenberg, N. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392, 520\u2013523 (1998).","journal-title":"Nature"},{"key":"1936_CR74","doi-asserted-by":"publisher","first-page":"104","DOI":"10.1101\/gad.1262905","volume":"19","author":"A Kahvejian","year":"2005","unstructured":"Kahvejian, A., Svitkin, Y. V., Sukarieh, R., M\u2019Boutchou, M. N. & Sonenberg, N. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 19, 104\u2013113 (2005).","journal-title":"Genes Dev."},{"key":"1936_CR75","doi-asserted-by":"publisher","first-page":"1081","DOI":"10.1016\/j.molcel.2018.05.009","volume":"70","author":"H Yi","year":"2018","unstructured":"Yi, H. et al. PABP cooperates with the CCR4\u2013NOT complex to promote mRNA deadenylation and block precocious decay. Mol. Cell 70, 1081\u20131088 (2018).","journal-title":"Mol. Cell"},{"key":"1936_CR76","doi-asserted-by":"publisher","first-page":"1089","DOI":"10.1016\/j.molcel.2018.05.033","volume":"70","author":"MW Webster","year":"2018","unstructured":"Webster, M. W. et al. mRNA deadenylation is coupled to translation rates by the differential activities of Ccr4-Not nucleases. Mol. Cell 70, 1089\u20131100 (2018).","journal-title":"Mol. Cell"},{"key":"1936_CR77","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s13059-019-1814-0","volume":"20","author":"A Hildebrandt","year":"2019","unstructured":"Hildebrandt, A. et al. The RNA-binding ubiquitin ligase MKRN1 functions in ribosome-associated quality control of poly(A) translation. Genome Biol. 20, 1\u201320 (2019).","journal-title":"Genome Biol."},{"key":"1936_CR78","doi-asserted-by":"publisher","first-page":"913","DOI":"10.1016\/j.chom.2024.04.012","volume":"32","author":"M Szczesna","year":"2024","unstructured":"Szczesna, M. et al. Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity. Cell Host Microbe 32, 913\u2013924 (2024).","journal-title":"Cell Host Microbe"},{"key":"1936_CR79","doi-asserted-by":"publisher","first-page":"67","DOI":"10.1016\/j.yjmcc.2013.09.014","volume":"65","author":"ME Reichelt","year":"2013","unstructured":"Reichelt, M. E., Mellor, K. M., Curl, C. L., Stapleton, D. & Delbridge, L. M. Myocardial glycophagy \u2013 a specific glycogen handling response to metabolic stress is accentuated in the female heart. J. Mol. Cell. Cardiol. 65, 67\u201375 (2013).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"1936_CR80","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/j.yjmcc.2024.02.009","volume":"189","author":"KM Mellor","year":"2024","unstructured":"Mellor, K. M. et al. Myocardial glycophagy flux dysregulation and glycogen accumulation characterize diabetic cardiomyopathy. J. Mol. Cell. Cardiol. 189, 83\u201389 (2024).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"1936_CR81","doi-asserted-by":"publisher","first-page":"1098144","DOI":"10.3389\/fmolb.2022.1098144","volume":"9","author":"Q Wu","year":"2022","unstructured":"Wu, Q., Koliopoulos, M. G., Rittinger, K. & Stieglitz, B. Structural basis for ubiquitylation by HOIL-1. Front. Mol. Biosci. 9, 1098144 (2022).","journal-title":"Front. Mol. Biosci."},{"key":"1936_CR82","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-35871-z","volume":"14","author":"XS Wang","year":"2023","unstructured":"Wang, X. S. et al. The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family. Nat. Commun. 14, 168 (2023).","journal-title":"Nat. Commun."},{"key":"1936_CR83","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1056\/NEJMoa033349","volume":"352","author":"M Arad","year":"2005","unstructured":"Arad, M. et al. Glycogen storage diseases presenting as hypertrophic cardiomyopathy. New Engl. J. Med. 352, 362\u2013372 (2005).","journal-title":"New Engl. J. Med."},{"key":"1936_CR84","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1172\/JCI0214571","volume":"109","author":"M Arad","year":"2002","unstructured":"Arad, M. et al. Constitutively active AMP kinase mutations cause glycogen storage disease mimicking hypertrophic cardiomyopathy. J. Clin. Investig. 109, 357\u2013362 (2002).","journal-title":"J. Clin. Investig."},{"key":"1936_CR85","doi-asserted-by":"publisher","first-page":"1739","DOI":"10.1006\/jmcc.2001.1437","volume":"33","author":"LJ Bloem","year":"2001","unstructured":"Bloem, L. J. et al. Tissue distribution and functional expression of a cDNA encoding a novel mixed lineage kinase. J. Mol. Cellular Cardiol. 33, 1739\u20131750 (2001).","journal-title":"J. Mol. Cellular Cardiol."},{"key":"1936_CR86","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1006\/bbrc.2000.3236","volume":"274","author":"TC Liu","year":"2000","unstructured":"Liu, T. C. et al. Cloning and expression of ZAK, a mixed lineage kinase-like protein containing a leucine-zipper and a sterile-alpha motif. Biochem. Biophys. Res. Commun. 274, 811\u2013816 (2000).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"1936_CR87","doi-asserted-by":"publisher","first-page":"973","DOI":"10.1016\/j.bbrc.2004.09.156","volume":"324","author":"CY Huang","year":"2004","unstructured":"Huang, C. Y. et al. ZAK re-programs atrial natriuretic factor expression and induces hypertrophic growth in H9c2 cardiomyoblast cells. Biochem. Biophys. Res. Commun. 324, 973\u2013980 (2004).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"1936_CR88","doi-asserted-by":"publisher","first-page":"705","DOI":"10.1016\/j.yjmcc.2004.06.004","volume":"37","author":"M Christe","year":"2004","unstructured":"Christe, M. et al. Transgenic mice with cardiac-specific over-expression of MLK7 have increased mortality when exposed to chronic beta-adrenergic stimulation. J. Mol. Cellular Cardiol. 37, 705\u2013715 (2004).","journal-title":"J. Mol. Cellular Cardiol."},{"key":"1936_CR89","doi-asserted-by":"publisher","first-page":"2114","DOI":"10.1021\/acs.jmedchem.9b00664","volume":"63","author":"J Yang","year":"2020","unstructured":"Yang, J. et al. Design, synthesis, and structure-activity relationships of 1,2,3-triazole benzenesulfonamides as new selective leucine-zipper and sterile-\u03b1 motif kinase (ZAK) inhibitors. J. Med. Chem. 63, 2114\u20132130 (2020).","journal-title":"J. Med. Chem."},{"key":"1936_CR90","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2021.109642","volume":"36","author":"DM Garshott","year":"2021","unstructured":"Garshott, D. M. et al. iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA translation initiation. Cell Rep. 36, 109642 (2021).","journal-title":"Cell Rep."},{"key":"1936_CR91","doi-asserted-by":"publisher","first-page":"jcs251983","DOI":"10.1242\/jcs.251983","volume":"133","author":"BP Phillips","year":"2020","unstructured":"Phillips, B. P. & Miller, E. A. Ribosome-associated quality control of membrane proteins at the endoplasmic reticulum. J. Cell Sci. 133, jcs251983 (2020).","journal-title":"J. Cell Sci."},{"key":"1936_CR92","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2023.113056","volume":"42","author":"LA Gurzeler","year":"2023","unstructured":"Gurzeler, L. A. et al. Drug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control. Cell Rep. 42, 113056 (2023).","journal-title":"Cell Rep."},{"key":"1936_CR93","doi-asserted-by":"publisher","first-page":"346","DOI":"10.1016\/j.cell.2022.12.025","volume":"186","author":"K Oltion","year":"2023","unstructured":"Oltion, K. et al. An E3 ligase network engages GCN1 to promote the degradation of translation factors on stalled ribosomes. Cell 186, 346\u2013362 (2023).","journal-title":"Cell"},{"key":"1936_CR94","doi-asserted-by":"crossref","unstructured":"Rodschinka, G. et al. Comparative CRISPRi screens reveal a human stem cell dependence on mRNA translation-coupled quality control. Nat. Struct. Mol. Biol. 32, 1932\u20131946 (2025).","DOI":"10.1038\/s41594-025-01616-3"},{"key":"1936_CR95","doi-asserted-by":"publisher","first-page":"636","DOI":"10.1080\/15476286.2022.2065784","volume":"19","author":"AR Guzikowski","year":"2022","unstructured":"Guzikowski, A. R. et al. Differential translation elongation directs protein synthesis in response to acute glucose deprivation in yeast. RNA Biol. 19, 636\u2013649 (2022).","journal-title":"RNA Biol."},{"key":"1936_CR96","doi-asserted-by":"publisher","DOI":"10.1038\/srep21228","volume":"6","author":"N Li","year":"2016","unstructured":"Li, N. et al. miR-182 modulates myocardial hypertrophic response induced by angiogenesis in heart. Sci. Rep. 6, 21228 (2016).","journal-title":"Sci. Rep."},{"key":"1936_CR97","doi-asserted-by":"publisher","first-page":"151892","DOI":"10.1016\/j.aanat.2022.151892","volume":"241","author":"FS da Silva","year":"2022","unstructured":"da Silva, F. S., Aquino de Souza, N. C. S., de Moraes, M. V., Abreu, B. J. & de Oliveira, M. F. CmyoSize: an ImageJ macro for automated analysis of cardiomyocyte size in images of routine histology staining. Ann. Anat. 241, 151892 (2022).","journal-title":"Ann. Anat."},{"key":"1936_CR98","doi-asserted-by":"publisher","first-page":"e46","DOI":"10.1002\/cpz1.46","volume":"1","author":"K Labun","year":"2021","unstructured":"Labun, K., Krause, M., Torres Cleuren, Y. & Valen, E. CRISPR genome editing made easy through the CHOPCHOP website. Curr. Protoc. 1, e46 (2021).","journal-title":"Curr. Protoc."},{"key":"1936_CR99","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1016\/j.molcel.2018.02.025","volume":"70","author":"S Namkoong","year":"2018","unstructured":"Namkoong, S., Ho, A., Woo, Y. M., Kwak, H. & Lee, J. H. Systematic characterization of stress-induced RNA granulation. Mol. Cell 70, 175\u2013187 (2018).","journal-title":"Mol. Cell"},{"key":"1936_CR100","doi-asserted-by":"publisher","first-page":"442","DOI":"10.1038\/s41586-024-07250-1","volume":"628","author":"S Radko-Juettner","year":"2024","unstructured":"Radko-Juettner, S. et al. Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing SWI\/SNF. Nature 628, 442\u2013449 (2024).","journal-title":"Nature"},{"key":"1936_CR101","doi-asserted-by":"publisher","first-page":"3663","DOI":"10.1074\/mcp.O114.039586","volume":"13","author":"X Wang","year":"2014","unstructured":"Wang, X. et al. JUMP: a tag-based database search tool for peptide identification with high sensitivity and accuracy. Mol. Cell. Proteomics. 13, 3663\u20133673 (2014).","journal-title":"Mol. Cell. Proteomics."}],"container-title":["Nature Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41556-026-01936-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41556-026-01936-6","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41556-026-01936-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T00:03:23Z","timestamp":1793923403000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41556-026-01936-6"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,4,30]]},"references-count":101,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,5]]}},"alternative-id":["1936"],"URL":"https:\/\/doi.org\/10.1038\/s41556-026-01936-6","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2024.10.10.617692","asserted-by":"object"}]},"ISSN":["1465-7392","1476-4679"],"issn-type":[{"value":"1465-7392","type":"print"},{"value":"1476-4679","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,4,30]]},"assertion":[{"value":"24 October 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 March 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 April 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 November 2026","order":5,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Update","order":6,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"In the version of the article initially published, in the Source Data for Fig. 1b, the values for the \u201cFemale dBR-Pre\u201d and \u201cFemale dBR-Post\u201d columns were incorrect; the correct values have now been added. In the Source Data for Fig. 4b, RT-qPCR data not included in the article have been removed and a formatting error has been corrected. In the Source Data for Extended Data Fig. 2d, a label has been added to identify the location of the summary data \u201c% glycogen retention\u201d. In the Source Data for Extended Data Fig. 5c, a note has been added to clarify that the TBP values are the same as those in Fig. 3d because they derive from the same RT-qPCR run. The corrected Source Data file is now available online.","order":7,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Ethics"}}]}}