{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T07:15:26Z","timestamp":1793862926328,"version":"4.6.1"},"reference-count":60,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2019,5,27]],"date-time":"2019-05-27T00:00:00Z","timestamp":1558915200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2019,5,27]],"date-time":"2019-05-27T00:00:00Z","timestamp":1558915200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Chem Biol"],"published-print":{"date-parts":[[2019,7]]},"DOI":"10.1038\/s41589-019-0291-9","type":"journal-article","created":{"date-parts":[[2019,5,27]],"date-time":"2019-05-27T12:03:31Z","timestamp":1558958611000},"page":"681-689","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":631,"title":["Mitochondrial metabolism promotes adaptation to proteotoxic stress"],"prefix":"10.1038","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7577-2342","authenticated-orcid":false,"given":"Peter","family":"Tsvetkov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9364-1621","authenticated-orcid":false,"given":"Alexandre","family":"Detappe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kai","family":"Cai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1371-2288","authenticated-orcid":false,"given":"Heather R.","family":"Keys","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zarina","family":"Brune","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weiwen","family":"Ying","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prathapan","family":"Thiru","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mairead","family":"Reidy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillaume","family":"Kugener","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jordan","family":"Rossen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mustafa","family":"Kocak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nora","family":"Kory","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3797-1877","authenticated-orcid":false,"given":"Aviad","family":"Tsherniak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7528-9668","authenticated-orcid":false,"given":"Sandro","family":"Santagata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luke","family":"Whitesell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene M.","family":"Ghobrial","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John L.","family":"Markley","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan","family":"Lindquist","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0113-2403","authenticated-orcid":false,"given":"Todd R.","family":"Golub","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2019,5,27]]},"reference":[{"key":"291_CR1","doi-asserted-by":"publisher","first-page":"835","DOI":"10.1016\/j.cell.2009.05.006","volume":"137","author":"J Luo","year":"2009","unstructured":"Luo, J. et al. A genome-wide RNAi screen identifies multiple synthetic lethal interactions with the ras oncogene. Cell 137, 835\u2013848 (2009).","journal-title":"Cell"},{"key":"291_CR2","doi-asserted-by":"publisher","first-page":"182","DOI":"10.1016\/j.ccr.2013.07.008","volume":"24","author":"F Petrocca","year":"2013","unstructured":"Petrocca, F. et al. A genome-wide siRNA screen identifies proteasome addiction as a vulnerability of basal-like triple-negative breast cancer cells. Cancer Cell 24, 182\u2013196 (2013).","journal-title":"Cancer Cell"},{"key":"291_CR3","first-page":"2615","volume":"59","author":"J Adams","year":"1999","unstructured":"Adams, J. et al. Proteasome inhibitors: a novel class of potent and effective antitumor agents. Cancer Res. 59, 2615\u20132622 (1999).","journal-title":"Cancer Res."},{"key":"291_CR4","doi-asserted-by":"publisher","DOI":"10.1186\/s12915-014-0094-0","volume":"12","author":"RJ Deshaies","year":"2014","unstructured":"Deshaies, R. J. Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy. BMC Biol. 12, 94 (2014).","journal-title":"BMC Biol."},{"key":"291_CR5","doi-asserted-by":"publisher","first-page":"1451","DOI":"10.1158\/1535-7163.MCT-10-0106","volume":"9","author":"SL Holbeck","year":"2010","unstructured":"Holbeck, S. L., Collins, J. M. & Doroshow, J. H. Analysis of food and drug administration-approved anticancer agents in the NCI60 panel of human tumor cell lines. Mol. Cancer Ther. 9, 1451\u20131460 (2010).","journal-title":"Mol. Cancer Ther."},{"key":"291_CR6","doi-asserted-by":"publisher","first-page":"1649","DOI":"10.1158\/1078-0432.CCR-07-2218","volume":"14","author":"RZ Orlowski","year":"2008","unstructured":"Orlowski, R. Z. & Kuhn, D. J. Proteasome inhibitors in cancer therapy: lessons from the first decade. Clin. Cancer Res. 14, 1649\u20131657 (2008).","journal-title":"Clin. Cancer Res."},{"key":"291_CR7","doi-asserted-by":"publisher","first-page":"1356","DOI":"10.1158\/1541-7786.MCR-08-0108","volume":"6","author":"S Markovina","year":"2008","unstructured":"Markovina, S. et al. Bortezomib-resistant nuclear factor-kappaB activity in multiple myeloma cells. Mol. Cancer Res. 6, 1356\u20131364 (2008).","journal-title":"Mol. Cancer Res."},{"key":"291_CR8","doi-asserted-by":"publisher","first-page":"29854","DOI":"10.1074\/jbc.M115.664953","volume":"290","author":"B Li","year":"2015","unstructured":"Li, B. et al. The nuclear factor (erythroid-derived 2)-like 2 and proteasome maturation protein axis mediate bortezomib resistance in multiple myeloma. J. Biol. Chem. 290, 29854\u201329868 (2015).","journal-title":"J. Biol. Chem."},{"key":"291_CR9","doi-asserted-by":"publisher","first-page":"639","DOI":"10.1016\/j.ccell.2016.03.026","volume":"29","author":"XD Zhang","year":"2016","unstructured":"Zhang, X. D. et al. Tight junction protein 1 modulates proteasome capacity and proteasome inhibitor sensitivity in multiple myeloma via EGFR\/JAK1\/STAT3 signaling. Cancer Cell 29, 639\u2013652 (2016).","journal-title":"Cancer Cell"},{"key":"291_CR10","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.chembiol.2012.01.003","volume":"19","author":"AF Kisselev","year":"2012","unstructured":"Kisselev, A. F., van der Linden, W. A. & Overkleeft, H. S. Proteasome inhibitors: an expanding army attacking a unique target. Chem. Biol. 19, 99\u2013115 (2012).","journal-title":"Chem. Biol."},{"key":"291_CR11","doi-asserted-by":"publisher","first-page":"382","DOI":"10.1073\/pnas.1619067114","volume":"114","author":"P Tsvetkov","year":"2017","unstructured":"Tsvetkov, P. et al. Suppression of 19S proteasome subunits marks emergence of an altered cell state in diverse cancers. Proc. Natl Acad. Sci. USA 114, 382\u2013387 (2017).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"291_CR12","doi-asserted-by":"publisher","unstructured":"Tsvetkov, P. et al. Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome. eLife 4, \n                    https:\/\/doi.org\/10.7554\/eLife.08467\n                    \n                   (2015).","DOI":"10.7554\/eLife.08467"},{"key":"291_CR13","doi-asserted-by":"publisher","first-page":"2862","DOI":"10.1158\/1535-7163.MCT-17-0130","volume":"16","author":"CX Shi","year":"2017","unstructured":"Shi, C. X. et al. CRISPR genome-wide screening identifies dependence on the proteasome subunit PSMC6 for bortezomib sensitivity in multiple myeloma. Mol. Cancer. Ther. 16, 2862\u20132870 (2017).","journal-title":"Mol. Cancer. Ther."},{"key":"291_CR14","doi-asserted-by":"publisher","first-page":"e08153","DOI":"10.7554\/eLife.08153","volume":"4","author":"D Acosta-Alvear","year":"2015","unstructured":"Acosta-Alvear, D. et al. Paradoxical resistance of multiple myeloma to proteasome inhibitors by decreased levels of 19S proteasomal subunits. eLife 4, e08153 (2015).","journal-title":"eLife"},{"key":"291_CR15","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1038\/nbt.1606","volume":"28","author":"VM Gohil","year":"2010","unstructured":"Gohil, V. M. et al. Nutrient-sensitized screening for drugs that shift energy metabolism from mitochondrial respiration to glycolysis. Nat. Biotechnol. 28, 249\u2013255 (2010).","journal-title":"Nat. Biotechnol."},{"key":"291_CR16","doi-asserted-by":"publisher","first-page":"419","DOI":"10.1038\/nbt.3460","volume":"34","author":"C Yu","year":"2016","unstructured":"Yu, C. et al. High-throughput identification of genotype-specific cancer vulnerabilities in mixtures of barcoded tumor cell lines. Nat. Biotechnol. 34, 419\u2013423 (2016).","journal-title":"Nat. Biotechnol"},{"key":"291_CR17","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1007\/s00280-009-1232-1","volume":"66","author":"S Ackler","year":"2010","unstructured":"Ackler, S. et al. The Bcl-2 inhibitor ABT-263 enhances the response of multiple chemotherapeutic regimens in hematologic tumors in vivo. Cancer Chemo. Pharmacol. 66, 869\u2013880 (2010).","journal-title":"Cancer Chemo. Pharmacol."},{"key":"291_CR18","doi-asserted-by":"publisher","first-page":"5452","DOI":"10.1200\/JCO.2008.17.1579","volume":"27","author":"S O\u2019Day","year":"2009","unstructured":"O\u2019Day, S. et al. Phase II, randomized, controlled, double-blinded trial of weekly elesclomol plus paclitaxel versus paclitaxel alone for stage IV metastatic melanoma. J. Clin. Oncol. 27, 5452\u20135458 (2009).","journal-title":"J. Clin. Oncol"},{"key":"291_CR19","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/j.jinorgbio.2014.04.004","volume":"137","author":"BB Hasinoff","year":"2014","unstructured":"Hasinoff, B. B., Yadav, A. A., Patel, D. & Wu, X. The cytotoxicity of the anticancer drug elesclomol is due to oxidative stress indirectly mediated through its complex with Cu(II). J. Inorg. Biochem. 137, 22\u201330 (2014).","journal-title":"J. Inorg. Biochem"},{"key":"291_CR20","doi-asserted-by":"publisher","first-page":"2142","DOI":"10.1016\/j.freeradbiomed.2012.03.017","volume":"52","author":"M Nagai","year":"2012","unstructured":"Nagai, M. et al. The oncology drug elesclomol selectively transports copper to the mitochondria to induce oxidative stress in cancer cells. Free Radic. Biol. Med. 52, 2142\u20132150 (2012).","journal-title":"Free Radic. Biol. Med"},{"key":"291_CR21","doi-asserted-by":"publisher","first-page":"8161","DOI":"10.1073\/pnas.1806296115","volume":"115","author":"S Soma","year":"2018","unstructured":"Soma, S. et al. Elesclomol restores mitochondrial function in genetic models of copper deficiency. Proc. Natl Acad. Sci. USA 115, 8161\u20138166 (2018).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"291_CR22","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jinorgbio.2013.04.013","volume":"126","author":"AA Yadav","year":"2013","unstructured":"Yadav, A. A., Patel, D., Wu, X. & Hasinoff, B. B. Molecular mechanisms of the biological activity of the anticancer drug elesclomol and its complexes with Cu(II), Ni(II) and Pt(II). J. Inorg. Biochem. 126, 1\u20136 (2013).","journal-title":"J. Inorg. Biochem."},{"key":"291_CR23","doi-asserted-by":"publisher","first-page":"e40690","DOI":"10.1371\/journal.pone.0040690","volume":"7","author":"M Barbi de Moura","year":"2012","unstructured":"Barbi de Moura, M. et al. Mitochondrial respiration\u2013an important therapeutic target in melanoma. PLoS ONE 7, e40690 (2012).","journal-title":"PLoS ONE"},{"key":"291_CR24","doi-asserted-by":"publisher","first-page":"e29798","DOI":"10.1371\/journal.pone.0029798","volume":"7","author":"RK Blackman","year":"2012","unstructured":"Blackman, R. K. et al. Mitochondrial electron transport is the cellular target of the oncology drug elesclomol. PLoS ONE 7, e29798 (2012).","journal-title":"PLoS ONE"},{"key":"291_CR25","doi-asserted-by":"publisher","first-page":"2319","DOI":"10.1158\/1535-7163.MCT-08-0298","volume":"7","author":"JR Kirshner","year":"2008","unstructured":"Kirshner, J. R. et al. Elesclomol induces cancer cell apoptosis through oxidative stress. Mol Cancer Ther. 7, 2319\u20132327 (2008).","journal-title":"Mol Cancer Ther"},{"key":"291_CR26","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1021\/acs.biochem.6b00447","volume":"56","author":"K Cai","year":"2017","unstructured":"Cai, K., Tonelli, M., Frederick, R. O. & Markley, J. L. Human mitochondrial ferredoxin 1 (FDX1) and ferredoxin 2 (FDX2) both bind cysteine desulfurase and donate electrons for iron\u2013sulfur cluster biosynthesis. Biochemistry 56, 487\u2013499 (2017).","journal-title":"Biochemistry"},{"key":"291_CR27","doi-asserted-by":"publisher","first-page":"11775","DOI":"10.1073\/pnas.1004250107","volume":"107","author":"AD Sheftel","year":"2010","unstructured":"Sheftel, A. D. et al. Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe\/S cluster biosynthesis. Proc. Natl Acad. Sci. USA 107, 11775\u201311780 (2010).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"291_CR28","doi-asserted-by":"publisher","first-page":"484","DOI":"10.1016\/j.bbamcr.2011.11.002","volume":"1823","author":"Y Shi","year":"2012","unstructured":"Shi, Y., Ghosh, M., Kovtunovych, G., Crooks, D. R. & Rouault, T. A. Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis. Biochim Biophys. Acta 1823, 484\u2013492 (2012).","journal-title":"Biochim Biophys. Acta"},{"key":"291_CR29","doi-asserted-by":"publisher","first-page":"875","DOI":"10.1016\/j.cmet.2016.08.017","volume":"24","author":"JD Arroyo","year":"2016","unstructured":"Arroyo, J. D. et al. A genome-wide CRISPR death screen identifies genes essential for oxidative phosphorylation. Cell Metab. 24, 875\u2013885 (2016).","journal-title":"Cell Metab"},{"key":"291_CR30","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1016\/j.cell.2013.12.010","volume":"156","author":"WS Yang","year":"2014","unstructured":"Yang, W. S. et al. Regulation of ferroptotic cancer cell death by GPX4. Cell 156, 317\u2013331 (2014).","journal-title":"Cell"},{"key":"291_CR31","doi-asserted-by":"publisher","first-page":"585","DOI":"10.1016\/j.chembiol.2018.02.010","volume":"25","author":"K Shimada","year":"2018","unstructured":"Shimada, K. et al. Copper-binding small molecule induces oxidative stress and cell-cycle arrest in glioblastoma-patient-derived cells. Cell Chem. Biol. 25, 585\u2013594 e587 (2018).","journal-title":"Cell Chem. Biol."},{"key":"291_CR32","doi-asserted-by":"publisher","first-page":"6235","DOI":"10.1021\/ja109413c","volume":"133","author":"S Tardito","year":"2011","unstructured":"Tardito, S. et al. Copper binding agents acting as copper ionophores lead to caspase inhibition and paraptotic cell death in human cancer cells. J. Am. Chem. Soc. 133, 6235\u20136242 (2011).","journal-title":"J. Am. Chem. Soc."},{"key":"291_CR33","doi-asserted-by":"publisher","first-page":"6914","DOI":"10.1021\/jm049568z","volume":"47","author":"D Cen","year":"2004","unstructured":"Cen, D., Brayton, D., Shahandeh, B., Meyskens, F. L. Jr. & Farmer, P. J. Disulfiram facilitates intracellular Cu uptake and induces apoptosis in human melanoma cells. J. Med. Chem. 47, 6914\u20136920 (2004).","journal-title":"J. Med. Chem."},{"key":"291_CR34","doi-asserted-by":"publisher","first-page":"1234","DOI":"10.1038\/nm.4399","volume":"23","author":"EM Kuntz","year":"2017","unstructured":"Kuntz, E. M. et al. Targeting mitochondrial oxidative phosphorylation eradicates therapy-resistant chronic myeloid leukemia stem cells. Nat. Med. 23, 1234\u20131240 (2017).","journal-title":"Nat. Med."},{"key":"291_CR35","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/j.cmet.2017.09.009","volume":"26","author":"KM Lee","year":"2017","unstructured":"Lee, K. M. et al. MYC and MCL1 cooperatively promote chemotherapy-resistant breast cancer stem cells via regulation of mitochondrial oxidative phosphorylation. Cell Metab. 26, 633\u2013647 e637 (2017).","journal-title":"Cell Metab"},{"key":"291_CR36","doi-asserted-by":"publisher","first-page":"1542","DOI":"10.1038\/cdd.2016.39","volume":"23","author":"DS Matassa","year":"2016","unstructured":"Matassa, D. S. et al. Oxidative metabolism drives inflammation-induced platinum resistance in human ovarian cancer. Cell Death Differ. 23, 1542\u20131554 (2016).","journal-title":"Cell Death Differ"},{"key":"291_CR37","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/j.ccr.2012.11.020","volume":"23","author":"F Vazquez","year":"2013","unstructured":"Vazquez, F. et al. PGC1alpha expression defines a subset of human melanoma tumors with increased mitochondrial capacity and resistance to oxidative stress. Cancer Cell 23, 287\u2013301 (2013).","journal-title":"Cancer Cell"},{"key":"291_CR38","doi-asserted-by":"publisher","first-page":"2870","DOI":"10.1158\/1078-0432.CCR-14-2290","volume":"21","author":"TT Vellinga","year":"2015","unstructured":"Vellinga, T. T. et al. SIRT1\/PGC1alpha-dependent increase in oxidative phosphorylation supports chemotherapy resistance of colon cancer. Clin. Cancer Res. 21, 2870\u20132879 (2015).","journal-title":"Clin. Cancer Res."},{"key":"291_CR39","doi-asserted-by":"publisher","first-page":"2198","DOI":"10.1038\/leu.2016.102","volume":"30","author":"GP Soriano","year":"2016","unstructured":"Soriano, G. P. et al. Proteasome inhibitor-adapted myeloma cells are largely independent from proteasome activity and show complex proteomic changes, in particular in redox and energy metabolism. Leukemia 30, 2198\u20132207 (2016).","journal-title":"Leukemia"},{"key":"291_CR40","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1186\/s40170-017-0169-9","volume":"5","author":"EA Zaal","year":"2017","unstructured":"Zaal, E. A. et al. Bortezomib resistance in multiple myeloma is associated with increased serine synthesis. Cancer Metab. 5, 7 (2017).","journal-title":"Cancer Metab"},{"key":"291_CR41","doi-asserted-by":"publisher","first-page":"142","DOI":"10.1016\/j.molcel.2016.11.007","volume":"65","author":"I Frumkin","year":"2017","unstructured":"Frumkin, I. et al. Gene architectures that minimize cost of gene expression. Mol. Cell 65, 142\u2013153 (2017).","journal-title":"Mol. Cell"},{"key":"291_CR42","doi-asserted-by":"publisher","first-page":"29215","DOI":"10.1074\/jbc.M113.482570","volume":"288","author":"A Peth","year":"2013","unstructured":"Peth, A., Nathan, J. A. & Goldberg, A. L. The ATP costs and time required to degrade ubiquitinated proteins by the 26 S proteasome. J. Biol. Chem. 288, 29215\u201329222 (2013).","journal-title":"J. Biol. Chem."},{"key":"291_CR43","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1016\/j.mam.2016.05.001","volume":"50","author":"R Raynes","year":"2016","unstructured":"Raynes, R., Pomatto, L. C. & Davies, K. J. Degradation of oxidized proteins by the proteasome: distinguishing between the 20S, 26S, and immunoproteasome proteolytic pathways. Mol. Aspects. Med. 50, 41\u201355 (2016).","journal-title":"Mol. Aspects. Med."},{"key":"291_CR44","doi-asserted-by":"publisher","first-page":"1960","DOI":"10.1126\/science.1121925","volume":"310","author":"RM Vabulas","year":"2005","unstructured":"Vabulas, R. M. & Hartl, F. U. Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 310, 1960\u20131963 (2005).","journal-title":"Science"},{"key":"291_CR45","doi-asserted-by":"publisher","first-page":"242","DOI":"10.1016\/j.molcel.2012.08.003","volume":"48","author":"A Suraweera","year":"2012","unstructured":"Suraweera, A., Munch, C., Hanssum, A. & Bertolotti, A. Failure of amino acid homeostasis causes cell death following proteasome inhibition. Mol. Cell 48, 242\u2013253 (2012).","journal-title":"Mol. Cell"},{"key":"291_CR46","first-page":"ra88","volume":"3","author":"X Wang","year":"2010","unstructured":"Wang, X., Yen, J., Kaiser, P. & Huang, L. Regulation of the 26S proteasome complex during oxidative stress. Sci. Signal 3, ra88 (2010).","journal-title":"Sci. Signal"},{"key":"291_CR47","doi-asserted-by":"publisher","first-page":"614","DOI":"10.1016\/j.cell.2013.03.040","volume":"153","author":"PF Cho-Park","year":"2013","unstructured":"Cho-Park, P. F. & Steller, H. Proteasome regulation by ADP-ribosylation. Cell 153, 614\u2013627 (2013).","journal-title":"Cell"},{"key":"291_CR48","doi-asserted-by":"publisher","first-page":"11272","DOI":"10.1074\/jbc.M113.537175","volume":"289","author":"P Tsvetkov","year":"2014","unstructured":"Tsvetkov, P. et al. NADH binds and stabilizes the 26S proteasomes independent of ATP. J. Biol. Chem. 289, 11272\u201311281 (2014).","journal-title":"J. Biol. Chem."},{"key":"291_CR49","doi-asserted-by":"publisher","first-page":"184","DOI":"10.1038\/nature18943","volume":"536","author":"A Rousseau","year":"2016","unstructured":"Rousseau, A. & Bertolotti, A. An evolutionarily conserved pathway controls proteasome homeostasis. Nature 536, 184\u2013189 (2016).","journal-title":"Nature"},{"key":"291_CR50","doi-asserted-by":"publisher","first-page":"15790","DOI":"10.1073\/pnas.1521919112","volume":"112","author":"J Zhao","year":"2015","unstructured":"Zhao, J., Zhai, B., Gygi, S. P. & Goldberg, A. L. mTOR inhibition activates overall protein degradation by the ubiquitin proteasome system as well as by autophagy. Proc. Natl Acad. Sci. USA 112, 15790\u201315797 (2015).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"291_CR51","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1093\/bioinformatics\/bts635","volume":"29","author":"A Dobin","year":"2013","unstructured":"Dobin, A. et al. STAR: ultrafast universal RNA-Seq aligner. Bioinformatics 29, 15\u201321 (2013).","journal-title":"Bioinformatics"},{"key":"291_CR52","doi-asserted-by":"publisher","first-page":"15545","DOI":"10.1073\/pnas.0506580102","volume":"102","author":"A Subramanian","year":"2005","unstructured":"Subramanian, A. et al. Gene set enrichment analysis: a knowledge-based approach for interpreting genome-wide expression profiles. Proc. Natl Acad. Sci. USA 102, 15545\u201315550 (2005).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"291_CR53","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1038\/nmeth.2956","volume":"11","author":"Y Zhu","year":"2014","unstructured":"Zhu, Y., Qiu, P. & Ji, Y. TCGA-assembler: open-source software for retrieving and processing TCGA data. Nat. Methods 11, 599\u2013600 (2014).","journal-title":"Nat. Methods"},{"key":"291_CR54","doi-asserted-by":"publisher","first-page":"2498","DOI":"10.1101\/gr.1239303","volume":"13","author":"P Shannon","year":"2003","unstructured":"Shannon, P. et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498\u20132504 (2003).","journal-title":"Genome Res"},{"key":"291_CR55","doi-asserted-by":"publisher","first-page":"e0146021","DOI":"10.1371\/journal.pone.0146021","volume":"10","author":"C Ritz","year":"2015","unstructured":"Ritz, C., Baty, F., Streibig, J. C. & Gerhard, D. Dose-Response analysis using R. PLoS ONE 10, e0146021 (2015).","journal-title":"PLoS ONE"},{"key":"291_CR56","doi-asserted-by":"publisher","first-page":"2333","DOI":"10.12688\/f1000research.9611.1","volume":"5","author":"Z Safikhani","year":"2016","unstructured":"Safikhani, Z. et al. Revisiting inconsistency in large pharmacogenomic studies. F1000Res. 5, 2333 (2016).","journal-title":"F1000Res."},{"key":"291_CR57","doi-asserted-by":"publisher","first-page":"2851","DOI":"10.1021\/jm401279n","volume":"57","author":"EM Wijeratne","year":"2014","unstructured":"Wijeratne, E. M. et al. Structure-activity relationships for withanolides as inducers of the cellular heat-shock response. J. Med. Chem. 57, 2851\u20132863 (2014).","journal-title":"J. Med. Chem."},{"key":"291_CR58","doi-asserted-by":"publisher","first-page":"pdb.prot090811","DOI":"10.1101\/pdb.prot090811","volume":"2016","author":"T Wang","year":"2016","unstructured":"Wang, T., Lander, E. S. & Sabatini, D. M. Viral Packaging and cell culture for CRISPR-based screens. Cold Spring Harb. Protoc. 2016, pdb.prot090811 (2016).","journal-title":"Cold Spring Harb. Protoc."},{"key":"291_CR59","doi-asserted-by":"publisher","first-page":"1491","DOI":"10.1021\/acs.biochem.7b01234","volume":"57","author":"K Cai","year":"2018","unstructured":"Cai, K., Frederick, R. O., Tonelli, M. & Markley, J. L. ISCU(M108I) and ISCU(D39V) differ from wild-type ISCU in Their failure to form cysteine desulfurase complexes containing both frataxin and ferredoxin. Biochemistry 57, 1491\u20131500 (2018).","journal-title":"Biochemistry"},{"key":"291_CR60","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.jinorgbio.2018.03.007","volume":"183","author":"K Cai","year":"2018","unstructured":"Cai, K., Frederick, R. O., Tonelli, M. & Markley, J. L. Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe\u2013S cluster assembly. J. Inorg. Biochem. 183, 107\u2013116 (2018).","journal-title":"J. Inorg. Biochem."}],"updated-by":[{"DOI":"10.1038\/s41589-019-0315-5","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2019,6,4]],"date-time":"2019-06-04T00:00:00Z","timestamp":1559606400000}}],"container-title":["Nature Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/s41589-019-0291-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/s41589-019-0291-9","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/s41589-019-0291-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,20]],"date-time":"2023-05-20T18:27:27Z","timestamp":1684607247000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41589-019-0291-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5,27]]},"references-count":60,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2019,7]]}},"alternative-id":["291"],"URL":"https:\/\/doi.org\/10.1038\/s41589-019-0291-9","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/288365","asserted-by":"object"}]},"ISSN":["1552-4450","1552-4469"],"issn-type":[{"value":"1552-4450","type":"print"},{"value":"1552-4469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,5,27]]},"assertion":[{"value":"20 November 2018","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"16 April 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 May 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"T.R.G. is a consultant in GlaxoSmithKline, Sherlock Biosciences and Foundation medicine; co-founder of Sherlock Biosciences and Foundation medicine. S.S. has consulted for RareCyte Inc. A.T. is a consultant for Tango Therapeutics. W.Y. is employed by Ranok Therapeutics Co. Ltd. and is also the sole proprietor of OnTarget Pharmaceutical Consulting LLC.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}