{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T00:17:11Z","timestamp":1789777031964,"version":"4.0.1"},"reference-count":69,"publisher":"Elsevier BV","issue":"14","license":[{"start":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T00:00:00Z","timestamp":1782864000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,7,1]],"date-time":"2026-07-01T00:00:00Z","timestamp":1782864000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,6,6]],"date-time":"2026-06-06T00:00:00Z","timestamp":1780704000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000289","name":"Cancer Research UK","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000289","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000691","name":"Academy of Medical Sciences","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000288","name":"The Royal Society","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000288","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000781","name":"European Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000781","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004282","name":"Evelyn Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004282","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000265","name":"UK Research and Innovation Medical Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020098","name":"Innovative Medicines Initiative","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100020098","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Cell"],"published-print":{"date-parts":[[2026,7]]},"DOI":"10.1016\/j.molcel.2026.06.014","type":"journal-article","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T14:38:28Z","timestamp":1781879908000},"page":"2828-2842.e12","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["LRRC58 defines an E3 ubiquitin ligase complex sensitive to cysteine abundance"],"prefix":"10.1016","volume":"86","author":[{"given":"Dylan E.","family":"Ramage","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lianne H.E.","family":"Wieske","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charlotte","family":"Crowe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens B.","family":"Christensen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Theo A.","family":"von Wilmowski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zoe","family":"Bannister","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Drew W.","family":"Grant","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark A.","family":"Nakasone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin","family":"Haubrich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Dorward","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iva A.","family":"Tchasovnikarova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael P.","family":"Weekes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicholas J.","family":"Matheson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N. Sumru","family":"Bayin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessio","family":"Ciulli","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7275-597X","authenticated-orcid":false,"given":"Richard T.","family":"Timms","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.molcel.2026.06.014_bib1","doi-asserted-by":"crossref","first-page":"397","DOI":"10.15252\/embj.201696010","article-title":"Nutrient sensing and TOR signaling in yeast and mammals","volume":"36","author":"Gonz\u00e1lez","year":"2017","journal-title":"EMBO J."},{"key":"10.1016\/j.molcel.2026.06.014_bib2","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/nature14190","article-title":"Nutrient-sensing mechanisms and pathways","volume":"517","author":"Efeyan","year":"2015","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib3","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S1097-2765(00)00028-9","article-title":"Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain","volume":"6","author":"Dong","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib4","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1042\/BST20190331","article-title":"Towards a model of GCN2 activation","volume":"47","author":"Masson","year":"2019","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.molcel.2026.06.014_bib5","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1016\/j.cell.2017.02.004","article-title":"mTOR Signaling in Growth, Metabolism, and Disease","volume":"168","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib6","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1126\/science.aab2674","article-title":"Sestrin2 is a leucine sensor for the mTORC1 pathway","volume":"351","author":"Wolfson","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.molcel.2026.06.014_bib7","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1126\/science.aad2087","article-title":"Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway","volume":"351","author":"Saxton","year":"2016","journal-title":"Science"},{"key":"10.1016\/j.molcel.2026.06.014_bib8","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.cell.2016.02.035","article-title":"The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway","volume":"165","author":"Chantranupong","year":"2016","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib9","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1038\/nature19079","article-title":"Mechanism of arginine sensing by CASTOR1 upstream of mTORC1","volume":"536","author":"Saxton","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib10","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1126\/science.aao3265","article-title":"SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway","volume":"358","author":"Gu","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.molcel.2026.06.014_bib11","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abn3868","article-title":"Molecular mechanism of S-adenosylmethionine sensing by SAMTOR in mTORC1 signaling","volume":"8","author":"Tang","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.molcel.2026.06.014_bib12","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1038\/s41580-023-00641-8","article-title":"The molecular basis of nutrient sensing and signalling by mTORC1 in metabolism regulation and disease","volume":"24","author":"Goul","year":"2023","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib13","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/s41586-024-08248-5","article-title":"Human HDAC6 senses valine abundancy to regulate DNA damage","volume":"637","author":"Jin","year":"2025","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib14","doi-asserted-by":"crossref","first-page":"2581","DOI":"10.1016\/j.molcel.2025.05.035","article-title":"BAG2 releases SAMD4B upon sensing of arginine deficiency to promote tumor cell survival","volume":"85","author":"Chen","year":"2025","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib15","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"THE UBIQUITIN SYSTEM","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.molcel.2026.06.014_bib16","doi-asserted-by":"crossref","first-page":"868","DOI":"10.1038\/s41580-025-00870-z","article-title":"Degrons: defining the rules of protein degradation","volume":"26","author":"Zhang","year":"2025","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib17","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/nrm.2017.83","article-title":"Ubiquitylation at the crossroads of development and disease","volume":"19","author":"Rape","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib18","doi-asserted-by":"crossref","DOI":"10.1002\/bies.202300139","article-title":"As a matter of fat: Emerging roles of lipid-sensitive E3 ubiquitin ligases","volume":"45","author":"Gawden-Bone","year":"2023","journal-title":"BioEssays"},{"key":"10.1016\/j.molcel.2026.06.014_bib19","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.40009","article-title":"The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and hrd1","volume":"7","author":"Menzies","year":"2018","journal-title":"eLife"},{"key":"10.1016\/j.molcel.2026.06.014_bib20","article-title":"The E3 ubiquitin ligase MARCHF6 as a metabolic integrator in cholesterol synthesis and beyond","volume":"1866","author":"Scott","year":"2021","journal-title":"Biochim. Biophys. Acta Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.molcel.2026.06.014_bib21","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1126\/science.1160489","article-title":"Global protein stability profiling in mammalian cells","volume":"322","author":"Yen","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.molcel.2026.06.014_bib22","doi-asserted-by":"crossref","first-page":"1622","DOI":"10.1016\/j.cell.2018.04.028","article-title":"The Eukaryotic Proteome Is Shaped by E3 Ubiquitin Ligases Targeting C-Terminal Degrons","volume":"173","author":"Koren","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib23","doi-asserted-by":"crossref","first-page":"2494S","DOI":"10.1093\/jn\/nxaa094","article-title":"Metabolism of sulfur-containing amino acids: How the body copes with excess methionine, cysteine, and sulfide","volume":"150","author":"Stipanuk","year":"2020","journal-title":"J. Nutr."},{"key":"10.1016\/j.molcel.2026.06.014_bib24","article-title":"A proposed role for CDO1 in CNS development: Three children with rare missense variants and a neurological phenotype","volume":"6","author":"Rowe","year":"2025","journal-title":"HGG Adv."},{"key":"10.1016\/j.molcel.2026.06.014_bib25","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1038\/s41556-023-01229-2","article-title":"Defining E3 ligase\u2013substrate relationships through multiplex CRISPR screening","volume":"25","author":"Timms","year":"2023","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib26","doi-asserted-by":"crossref","first-page":"4633","DOI":"10.1021\/cr300163e","article-title":"Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery","volume":"113","author":"Paulsen","year":"2013","journal-title":"Chem. Rev."},{"key":"10.1016\/j.molcel.2026.06.014_bib27","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.freeradbiomed.2014.11.013","article-title":"The Basics of Thiols and Cysteines in Redox Biology and Chemistry","volume":"80","author":"Poole","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.molcel.2026.06.014_bib28","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1038\/s41416-020-01156-1","article-title":"Cysteine metabolic circuitries: druggable targets in cancer","volume":"124","author":"Bonif\u00e1cio","year":"2021","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.molcel.2026.06.014_bib29","doi-asserted-by":"crossref","first-page":"E439","DOI":"10.1152\/ajpendo.00336.2003","article-title":"The ubiquitin-proteasome system is responsible for cysteine-responsive regulation of cysteine dioxygenase concentration in liver","volume":"286","author":"Stipanuk","year":"2004","journal-title":"Am. J. Physiol., Endocrinol. Metab."},{"key":"10.1016\/j.molcel.2026.06.014_bib30","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1158\/0008-5472.CAN-22-3000","article-title":"Comprehensive Metabolic Tracing Reveals the Origin and Catabolism of Cysteine in Mammalian Tissues and Tumors","volume":"83","author":"Yoon","year":"2023","journal-title":"Cancer Res."},{"key":"10.1016\/j.molcel.2026.06.014_bib31","doi-asserted-by":"crossref","first-page":"1633","DOI":"10.1038\/sj.leu.2402238","article-title":"Sulfasalazine, a potent suppressor of lymphoma growth by inhibition of the x(c)- cystine transporter: a new action for an old drug","volume":"15","author":"Gout","year":"2001","journal-title":"Leukemia"},{"key":"10.1016\/j.molcel.2026.06.014_bib32","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1038\/s41422-022-00642-w","article-title":"The structure of erastin-bound xCT-4F2hc complex reveals molecular mechanisms underlying erastin-induced ferroptosis","volume":"32","author":"Yan","year":"2022","journal-title":"Cell Res."},{"key":"10.1016\/j.molcel.2026.06.014_bib33","doi-asserted-by":"crossref","first-page":"8023","DOI":"10.1074\/jbc.M900301200","article-title":"An ATP-competitive Mammalian Target of Rapamycin Inhibitor Reveals Rapamycin-resistant Functions of mTORC1","volume":"284","author":"Thoreen","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib34","doi-asserted-by":"crossref","first-page":"12188","DOI":"10.1074\/jbc.M800044200","article-title":"Synthesis of Amino Acid Cofactor in Cysteine Dioxygenase Is Regulated by Substrate and Represents a Novel Post-translational Regulation of Activity","volume":"283","author":"Dominy","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib35","doi-asserted-by":"crossref","first-page":"3369","DOI":"10.1093\/jn\/132.11.3369","article-title":"Enzymes and metabolites of cysteine metabolism in nonhepatic tissues of rats show little response to changes in dietary protein or sulfur amino acid levels","volume":"132","author":"Stipanuk","year":"2002","journal-title":"J. Nutr."},{"key":"10.1016\/j.molcel.2026.06.014_bib37","doi-asserted-by":"crossref","first-page":"8005","DOI":"10.1074\/jbc.M706987200","article-title":"Characterization of Cullin-box sequences that direct recruitment of Cul2-Rbx1 and Cul5-Rbx2 modules to Elongin BC-based ubiquitin ligases","volume":"283","author":"Mahrour","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib38","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/nature22366","article-title":"Architecture of the human interactome defines protein communities and disease networks","volume":"545","author":"Huttlin","year":"2017","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib39","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib36","doi-asserted-by":"crossref","DOI":"10.1186\/s13059-014-0554-4","article-title":"MAGeCK enables robust identification of essential genes from genome-scale CRISPR\/Cas9 knockout screens","volume":"15","author":"Li","year":"2014","journal-title":"Genome Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib40","doi-asserted-by":"crossref","first-page":"3377","DOI":"10.1016\/j.molcel.2023.08.022","article-title":"Elucidation of E3 ubiquitin ligase specificity through proteome-wide internal degron mapping","volume":"83","author":"Zhang","year":"2023","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib41","doi-asserted-by":"crossref","first-page":"3391","DOI":"10.1074\/jbc.M609337200","article-title":"An Insight into the Mechanism of Human Cysteine Dioxygenase: KEY ROLES OF THE THIOETHER-BONDED TYROSINE-CYSTEINE COFACTOR","volume":"282","author":"Ye","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib42","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1111\/febs.15842","article-title":"Understanding the role of cysteine in ferroptosis: progress & paradoxes","volume":"289","author":"Poltorack","year":"2022","journal-title":"FEBS Journal"},{"key":"10.1016\/j.molcel.2026.06.014_bib43","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.1016\/j.cell.2012.03.042","article-title":"Ferroptosis: An iron-dependent form of nonapoptotic cell death","volume":"149","author":"Dixon","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib44","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/S0891-5849(02)00848-1","article-title":"C11-BODIPY(581\/591), an oxidation-sensitive fluorescent lipid peroxidation probe: (micro)spectroscopic characterization and validation of methodology","volume":"33","author":"Drummen","year":"2002","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.molcel.2026.06.014_bib45","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0378-1119(01)00691-6","article-title":"Murine cysteine dioxygenase gene: structural organization, tissue-specific expression and promoter identification","volume":"277","author":"Hirschberger","year":"2001","journal-title":"Gene"},{"key":"10.1016\/j.molcel.2026.06.014_bib46","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1038\/cdd.2011.16","article-title":"Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms","volume":"18","author":"de Bie","year":"2011","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.molcel.2026.06.014_bib47","doi-asserted-by":"crossref","first-page":"2436","DOI":"10.1074\/jbc.RA118.005069","article-title":"Cholesterol increases protein levels of the E3 ligase March6 and thereby stimulates protein degradation","volume":"294","author":"Sharpe","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib48","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-026-72524-3","article-title":"Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1","volume":"17","author":"Andree","year":"2026","journal-title":"Nat. Commun."},{"key":"10.1016\/j.molcel.2026.06.014_bib49","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.tips.2018.02.007","article-title":"Cysteine metabolism in neuronal redox homeostasis","volume":"39","author":"Paul","year":"2018","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.molcel.2026.06.014_bib50","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1038\/s41589-025-01936-x","article-title":"A small-molecule VHL molecular glue degrader for cysteine dioxygenase 1","volume":"21","author":"Tutter","year":"2025","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.molcel.2026.06.014_bib51","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1038\/s41586-025-09535-5","article-title":"Covariation MS uncovers a protein that controls cysteine catabolism","volume":"647","author":"Xiao","year":"2025","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2026.06.014_bib52","doi-asserted-by":"crossref","DOI":"10.3390\/cancers11050678","article-title":"The Non-Essential Amino Acid Cysteine Becomes Essential for Tumor Proliferation and Survival","volume":"11","author":"Combs","year":"2019","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.molcel.2026.06.014_bib53","doi-asserted-by":"crossref","first-page":"dev204811","DOI":"10.1242\/dev.204811","article-title":"A conserved differentiation programme facilitates inhibitory neuron production in the developing mouse and human cerebellum","volume":"152","author":"Christensen","year":"2025","journal-title":"Development"},{"key":"10.1016\/j.molcel.2026.06.014_bib54","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1016\/j.celrep.2016.09.079","article-title":"A CRISPR Dropout Screen Identifies Genetic Vulnerabilities and Therapeutic Targets in Acute Myeloid Leukemia","volume":"17","author":"Tzelepis","year":"2016","journal-title":"Cell Rep."},{"key":"10.1016\/j.molcel.2026.06.014_bib55","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.115263","article-title":"Spatial proteomics identifies a CRTC-dependent viral signaling pathway that stimulates production of interleukin-11","volume":"44","author":"Ravenhill","year":"2025","journal-title":"Cell Rep."},{"key":"10.1016\/j.molcel.2026.06.014_bib56","doi-asserted-by":"crossref","first-page":"E2564","DOI":"10.1073\/pnas.1604935113","article-title":"BiGBac enables rapid gene assembly for the expression of large multisubunit protein complexes","volume":"113","author":"Weissmann","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.molcel.2026.06.014_bib57","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1038\/nmeth.3047","article-title":"Improved vectors and genome-wide libraries for CRISPR screening","volume":"11","author":"Sanjana","year":"2014","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2026.06.014_bib58","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1038\/nmeth983","article-title":"Protein complex expression by using multigene baculoviral vectors","volume":"3","author":"Fitzgerald","year":"2006","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2026.06.014_bib59","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.str.2017.04.009","article-title":"Crystal Structure of the Cul2-Rbx1-EloBC-VHL Ubiquitin Ligase Complex","volume":"25","author":"Cardote","year":"2017","journal-title":"Structure"},{"key":"10.1016\/j.molcel.2026.06.014_bib60","doi-asserted-by":"crossref","first-page":"8014","DOI":"10.1021\/ja051306e","article-title":"Very Fast Two-Dimensional NMR Spectroscopy for Real-Time Investigation of Dynamic Events in Proteins on the Time Scale of Seconds","volume":"127","author":"Schanda","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.molcel.2026.06.014_bib61","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/0022-2364(90)90150-8","article-title":"Improved linear prediction for truncated signals of known phase","volume":"90","author":"Zhu","year":"1990","journal-title":"J. Magn. Reson. (1969)"},{"key":"10.1016\/j.molcel.2026.06.014_bib62","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1038\/s41587-019-0032-3","article-title":"CRISPResso2 provides accurate and rapid genome editing sequence analysis","volume":"37","author":"Clement","year":"2019","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.molcel.2026.06.014_bib63","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adg2235","article-title":"A histone deacetylase 3 and mitochondrial complex I axis regulates toxic formaldehyde production","volume":"9","author":"Wit","year":"2023","journal-title":"Sci. Adv."},{"key":"10.1016\/j.molcel.2026.06.014_bib64","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.27713","article-title":"Environmental cystine drives glutamine anaplerosis and sensitizes cancer cells to glutaminase inhibition","volume":"6","author":"Muir","year":"2017","journal-title":"eLife"},{"key":"10.1016\/j.molcel.2026.06.014_bib65","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.molcel.2014.05.008","article-title":"Tracing Compartmentalized NADPH Metabolism in the Cytosol and Mitochondria of Mammalian Cells","volume":"55","author":"Lewis","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.molcel.2026.06.014_bib66","doi-asserted-by":"crossref","first-page":"20621","DOI":"10.1074\/jbc.M706494200","article-title":"Quantifying Reductive Carboxylation Flux of Glutamine to Lipid in a Brown Adipocyte Cell Line","volume":"283","author":"Yoo","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib67","doi-asserted-by":"crossref","first-page":"7554","DOI":"10.1021\/ac0708893","article-title":"Accurate assessment of amino acid mass isotopomer distributions for metabolic flux analysis","volume":"79","author":"Antoniewicz","year":"2007","journal-title":"Anal. Chem."},{"key":"10.1016\/j.molcel.2026.06.014_bib68","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1002\/(SICI)1096-9888(199603)31:3<255::AID-JMS290>3.0.CO;2-3","article-title":"Correction of 13C Mass Isotopomer Distributions for Natural Stable Isotope Abundance","volume":"31","author":"Fernandez","year":"1996","journal-title":"J. Mass Spectrom."},{"key":"10.1016\/j.molcel.2026.06.014_bib69","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.ymben.2006.09.001","article-title":"Elementary Metabolite Units (EMU): a novel framework for modeling isotopic distributions","volume":"9","author":"Antoniewicz","year":"2006","journal-title":"Metab. Eng."}],"container-title":["Molecular Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276526003850?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276526003850?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T15:10:36Z","timestamp":1784214636000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1097276526003850"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,7]]},"references-count":69,"journal-issue":{"issue":"14","published-print":{"date-parts":[[2026,7]]}},"alternative-id":["S1097276526003850"],"URL":"https:\/\/doi.org\/10.1016\/j.molcel.2026.06.014","relation":{},"ISSN":["1097-2765"],"issn-type":[{"value":"1097-2765","type":"print"}],"subject":[],"published":{"date-parts":[[2026,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"LRRC58 defines an E3 ubiquitin ligase complex sensitive to cysteine abundance","name":"articletitle","label":"Article Title"},{"value":"Molecular Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.molcel.2026.06.014","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Author(s). Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}