{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T09:57:33Z","timestamp":1781863053368,"version":"3.54.5"},"reference-count":161,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T00:00:00Z","timestamp":1781740800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>The canonical transsulfuration (TSS) pathway enzymes cystathionine \u03b2-synthase (CBS) and cystathionine \u03b3-lyase (CTH) are traditionally recognized for their roles in the sequential conversion of homocysteine to cysteine and in endogenous hydrogen sulfide (H2S) production. Increasing evidence, however, suggests that these enzymes may also exhibit non-canonical (\u201cmoonlighting\u201d) functions that extend beyond metabolic regulation. In this review, we evaluate the hypothesis that CTH may participate in translational regulation, particularly in the control of hypoxia-inducible factor-1\u03b1 (HIF-1\u03b1) expression in clear cell ovarian carcinoma (CCOC). We first highlight limitations of the prevailing H2S- and cysteine-centric view of the TSS pathway, which may not fully explain emerging context-dependent functions of CTH in cancer biology. Current evidence suggests that CTH enhances HIF-1\u03b1 protein expression through mechanisms independent of transcription, protein stability, or H2S production, implicating a potential role in translational regulation, although direct mechanistic evidence remains limited. To critically evaluate this emerging hypothesis, we categorize evidence according to its level of experimental support, ranging from direct experimental evidence to indirect mechanistic observations and computational predictions. Within this framework, we examine three non-mutually exclusive models: (1) regulation through PI3K\/AKT\/mTOR-dependent translational signaling; (2) modulation of translational control through interaction with translation-associated proteins and RNA-binding proteins (RBPs) involved in HIF1A mRNA regulation; and (3) the more speculative possibility of direct interaction between CTH and HIF1A mRNA. Collectively, these observations support a model in which CTH contributes to selective translational regulation beyond its canonical metabolic functions, potentially linking sulfur metabolism to stress-adaptive gene expression in cancer.<\/jats:p>","DOI":"10.3390\/cells15121106","type":"journal-article","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T09:18:43Z","timestamp":1781860723000},"page":"1106","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Beyond Hydrogen Sulfide and Cysteine Metabolism: Reframing Cystathionine \u03b3-Lyase as a Potential Translational Regulator of Hypoxia-Inducible Factor-1\u03b1 in Clear Cell Ovarian Carcinoma"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3202-6171","authenticated-orcid":false,"given":"Amal M.","family":"EL-Naggar","sequence":"first","affiliation":[{"name":"Department of Pathology, Faculty of Medicine, Menoufia University, Shibin EL-Kom 32511, Egypt"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1007\/s00018-023-04781-0","article-title":"Moonlighting enzymes: When cellular context defines specificity","volume":"80","author":"Gupta","year":"2023","journal-title":"Cell Mol. Life Sci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1039\/B900658N","article-title":"Moonlighting proteins\u2014An update","volume":"5","author":"Jeffery","year":"2009","journal-title":"Mol. Biosyst."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"7412","DOI":"10.1038\/ncomms8412","article-title":"Extreme multifunctional proteins identified from a human protein interaction network","volume":"6","author":"Chapple","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.cell.2007.10.009","article-title":"Ribosomal protein S3: A KH domain subunit in NF-kappaB complexes that mediates selective gene regulation","volume":"131","author":"Wan","year":"2007","journal-title":"Cell"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.tem.2015.09.012","article-title":"Metabolic Enzymes Enjoying New Partnerships as RNA-Binding Proteins","volume":"26","author":"Castello","year":"2015","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1016\/j.tcb.2022.02.009","article-title":"Transsulfuration, minor player or crucial for cysteine homeostasis in cancer","volume":"32","author":"Zhang","year":"2022","journal-title":"Trends Cell Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1002\/path.6433","article-title":"Cystathionine gamma-lyase-mediated hypoxia inducible factor 1-alpha expression drives clear cell ovarian cancer progression","volume":"266","author":"Li","year":"2025","journal-title":"J. Pathol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1152\/physrev.00028.2021","article-title":"Physiological roles of hydrogen sulfide in mammalian cells, tissues, and organs","volume":"103","author":"Cirino","year":"2023","journal-title":"Physiol. Rev."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"e661","DOI":"10.1002\/mco2.661","article-title":"Role of hydrogen sulfide in health and disease","volume":"5","author":"Jin","year":"2024","journal-title":"MedComm"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1111\/bph.14446","article-title":"Regulators of the transsulfuration pathway","volume":"176","author":"Sbodio","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"22457","DOI":"10.1074\/jbc.M109.010868","article-title":"Relative contributions of cystathionine beta-synthase and gamma-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions","volume":"284","author":"Singh","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Andres, C.M.C., Perez de la Lastra, J.M., Andres Juan, C., Plou, F.J., and Perez-Lebena, E. (2023). Chemistry of Hydrogen Sulfide-Pathological and Physiological Functions in Mammalian Cells. Cells, 12.","DOI":"10.3390\/cells12232684"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.cmet.2019.09.009","article-title":"Transsulfuration Activity Can Support Cell Growth upon Extracellular Cysteine Limitation","volume":"30","author":"Zhu","year":"2019","journal-title":"Cell Metab."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"3205125","DOI":"10.1155\/2018\/3205125","article-title":"Cystathionine beta-Synthase in Physiology and Cancer","volume":"2018","author":"Zhu","year":"2018","journal-title":"Biomed. Res. Int."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.2741\/4286","article-title":"Regulation of cystathionine gamma-lyase\/H(2)S system and its pathological implication","volume":"19","author":"Zhao","year":"2014","journal-title":"Front. Biosci. (Landmark Ed.)"},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Rao, S.P., Dobariya, P., Bellamkonda, H., and More, S.S. (2023). Role of 3-Mercaptopyruvate Sulfurtransferase (3-MST) in Physiology and Disease. Antioxidants, 12.","DOI":"10.3390\/antiox12030603"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"13433","DOI":"10.1074\/jbc.M600246200","article-title":"Dynamics of carbon monoxide binding to cystathionine beta-synthase","volume":"281","author":"Puranik","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.abb.2004.04.027","article-title":"Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: Evidence that lysine 119 is a general base","volume":"427","author":"Evande","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1111\/febs.15360","article-title":"CRY1-CBS binding regulates circadian clock function and metabolism","volume":"288","author":"Growe","year":"2021","journal-title":"FEBS J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"102469","DOI":"10.1016\/j.redox.2022.102469","article-title":"MPST deficiency promotes intestinal epithelial cell apoptosis and aggravates inflammatory bowel disease via AKT","volume":"56","author":"Zhang","year":"2022","journal-title":"Redox Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1089\/ars.2014.5917","article-title":"Modes of physiologic H2S signaling in the brain and peripheral tissues","volume":"22","author":"Paul","year":"2015","journal-title":"Antioxid. Redox Signal"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"e2528478122","DOI":"10.1073\/pnas.2528478122","article-title":"Cystathionine gamma-lyase is a major regulator of cognitive function through neurotrophin signaling and neurogenesis","volume":"122","author":"Chakraborty","year":"2025","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s10528-013-9624-7","article-title":"Regulation of cystathionine gamma-lyase in mammalian cells by hypoxia","volume":"52","author":"Wang","year":"2014","journal-title":"Biochem. Genet."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.1074\/jbc.M115.685578","article-title":"Transcriptional Regulation of Cystathionine-gamma-Lyase in Endothelial Cells by NADPH Oxidase 4-Dependent Signaling","volume":"291","author":"Mistry","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1056\/NEJM196302142680701","article-title":"Cystathioninuria","volume":"268","author":"Frimpter","year":"1963","journal-title":"N. Engl. J. Med."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1203\/00006450-197802000-00012","article-title":"Cystathionase deficiency: Evidence for genetic heterogeneity in primary cystathioninuria","volume":"12","author":"Pascal","year":"1978","journal-title":"Pediatr. Res."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1126\/science.1198108","article-title":"Vitamin B6-responsive and -unresponsive cystathioninuria: Two variant molecular forms","volume":"190","author":"Pascal","year":"1975","journal-title":"Science"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1056\/NEJM196803142781104","article-title":"Cystathioninuria in two healthy siblings","volume":"278","author":"Perry","year":"1968","journal-title":"N. Engl. J. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/S0002-9378(99)70525-9","article-title":"Maternal gamma-cystathionase deficiency: Absence of both teratogenic effects and pregnancy complications","volume":"181","author":"Vargas","year":"1999","journal-title":"Am. J. Obstet. Gynecol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1016\/j.ymgme.2009.04.001","article-title":"Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies","volume":"97","author":"Kraus","year":"2009","journal-title":"Mol. Genet. Metab."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Agrawal, N., and Banerjee, R. (2008). Human polycomb 2 protein is a SUMO E3 ligase and alleviates substrate-induced inhibition of cystathionine beta-synthase sumoylation. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0004032"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"H2S signals through protein S-sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1126\/science.1162667","article-title":"H2S as a physiologic vasorelaxant: Hypertension in mice with deletion of cystathionine gamma-lyase","volume":"322","author":"Yang","year":"2008","journal-title":"Science"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"26358","DOI":"10.1074\/jbc.M110.147439","article-title":"Cystathionine gamma-Lyase-deficient mice require dietary cysteine to protect against acute lethal myopathy and oxidative injury","volume":"285","author":"Ishii","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1111\/cas.14862","article-title":"Cystathionine-gamma-lyase overexpression in T cells enhances antitumor effect independently of cysteine autonomy","volume":"112","author":"Lancien","year":"2021","journal-title":"Cancer Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"107507","DOI":"10.1016\/j.phrs.2024.107507","article-title":"Formation of CSE-YAP complex drives FOXD3-mediated transition of neurotoxic astrocytes in Parkinson\u2019s disease","volume":"210","author":"Zhu","year":"2024","journal-title":"Pharmacol. Res."},{"key":"ref_37","first-page":"473","article-title":"Cystathionine-gamma-lyase promotes the metastasis of breast cancer via the VEGF signaling pathway","volume":"55","author":"Wang","year":"2019","journal-title":"Int. J. Oncol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"e45986","DOI":"10.15252\/embr.201845986","article-title":"Dysregulation of cystathionine gamma-lyase promotes prostate cancer progression and metastasis","volume":"20","author":"Wang","year":"2019","journal-title":"EMBO Rep."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"102773","DOI":"10.1016\/j.redox.2023.102773","article-title":"Cystathionine gamma-lyase (CTH) inhibition attenuates glioblastoma formation","volume":"64","author":"Peleli","year":"2023","journal-title":"Redox Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"5238","DOI":"10.1038\/s41388-022-02512-6","article-title":"Cystathionine gamma-lyase mediates cell proliferation, migration, and invasion of nasopharyngeal carcinoma","volume":"41","author":"Zhang","year":"2022","journal-title":"Oncogene"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2884","DOI":"10.1158\/2159-8290.CD-20-1690","article-title":"Proteomic Screens for Suppressors of Anoikis Identify IL1RAP as a Promising Surface Target in Ewing Sarcoma","volume":"11","author":"Zhang","year":"2021","journal-title":"Cancer Discov."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/s42003-019-0431-5","article-title":"Non-enzymatic hydrogen sulfide production from cysteine in blood is catalyzed by iron and vitamin B6","volume":"2","author":"Yang","year":"2019","journal-title":"Commun. Biol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Katsouda, A., Markou, M., Zampas, P., Varela, A., Davos, C.H., Vellecco, V., Cirino, G., Bucci, M., and Papapetropoulos, A. (2023). CTH\/MPST double ablation results in enhanced vasorelaxation and reduced blood pressure via upregulation of the eNOS\/sGC pathway. Front. Pharmacol., 14.","DOI":"10.3389\/fphar.2023.1090654"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2307\/4577000","article-title":"Hydrogen Sulphide Literature","volume":"39","author":"Mitchell","year":"1924","journal-title":"Public Health Rep. (1896\u20131970)"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1016\/S0196-0644(86)80383-3","article-title":"Hydrogen sulfide poisoning from toxic inhalations of roofing asphalt fumes","volume":"15","author":"Hoidal","year":"1986","journal-title":"Ann. Emerg. Med."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1139\/o82-076","article-title":"Sulphide as an inhibitor and electron donor for the cytochrome c oxidase system","volume":"60","author":"Nicholls","year":"1982","journal-title":"Can. J. Biochem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1016\/0041-008X(90)90321-K","article-title":"Effects of hydrogen sulfide exposure on lung mitochondrial respiratory chain enzymes in rats","volume":"103","author":"Khan","year":"1990","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"18769","DOI":"10.1073\/pnas.1911895116","article-title":"Overproduction of H2S, generated by CBS, inhibits mitochondrial Complex IV and suppresses oxidative phosphorylation in Down syndrome","volume":"116","author":"Panagaki","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1158\/1541-7786.MCR-05-0126","article-title":"Evidence that hydrogen sulfide is a genotoxic agent","volume":"4","author":"Wagner","year":"2006","journal-title":"Mol. Cancer Res."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1093\/toxsci\/kfs125","article-title":"Hydrogen sulfide induced disruption of Na+ homeostasis in the cortex","volume":"128","author":"Chao","year":"2012","journal-title":"Toxicol. Sci."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.bcp.2017.09.010","article-title":"A timeline of hydrogen sulfide (H2S) research: From environmental toxin to biological mediator","volume":"149","author":"Szabo","year":"2018","journal-title":"Biochem. Pharmacol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"101772","DOI":"10.1016\/j.redox.2020.101772","article-title":"Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics","volume":"38","author":"Paul","year":"2021","journal-title":"Redox Biol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1111\/bph.12369","article-title":"Regulation of mitochondrial bioenergetic function by hydrogen sulfide. Part I. Biochemical and physiological mechanisms","volume":"171","author":"Szabo","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_54","doi-asserted-by":"crossref","unstructured":"Borisov, V.B., and Forte, E. (2021). Impact of Hydrogen Sulfide on Mitochondrial and Bacterial Bioenergetics. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222312688"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"R1479","DOI":"10.1152\/ajpregu.90566.2008","article-title":"Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values","volume":"295","author":"Furne","year":"2008","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.niox.2013.07.002","article-title":"Hydrogen sulfide chemical biology: Pathophysiological roles and detection","volume":"35","author":"Kolluru","year":"2013","journal-title":"Nitric Oxide"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"6290931","DOI":"10.1155\/2018\/6290931","article-title":"Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology","volume":"2018","author":"Giuffre","year":"2018","journal-title":"Oxid. Med. Cell Longev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"113775","DOI":"10.1016\/j.bcp.2019.113775","article-title":"Hydrogen sulfide modulates epithelial-mesenchymal transition and angiogenesis in non-small cell lung cancer via HIF-1alpha activation","volume":"172","author":"Wang","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"ref_59","first-page":"3247","article-title":"Exogenous H2S promotes cancer progression by activating JAK2\/STAT3 signaling pathway in esophageal EC109 cells","volume":"11","author":"Lei","year":"2018","journal-title":"Int. J. Clin. Exp. Pathol."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Moon, J.Y., Kye, B.H., Ko, S.H., and Yoo, R.N. (2023). Sulfur Metabolism of the Gut Microbiome and Colorectal Cancer: The Threat to the Younger Generation. Nutrients, 15.","DOI":"10.3390\/nu15081966"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"e70029","DOI":"10.1111\/fcp.70029","article-title":"Hydrogen Sulfide Treatment Enhanced Paclitaxel\u2019s Anticancer Effect on the ID8 Murine Epithelial Ovarian Cancer Cell Line","volume":"39","year":"2025","journal-title":"Fundam. Clin. Pharmacol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"4322","DOI":"10.1111\/bph.12773","article-title":"Utilizing hydrogen sulfide as a novel anti-cancer agent by targeting cancer glycolysis and pH imbalance","volume":"171","author":"Lee","year":"2014","journal-title":"Br. J. Pharmacol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/978-3-319-18144-8_12","article-title":"Hydrogen Sulfide and Cancer","volume":"230","author":"Hellmich","year":"2015","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Lee, Z.W., Zhou, J., Chen, C.S., Zhao, Y., Tan, C.H., Li, L., Moore, P.K., and Deng, L.W. (2011). The slow-releasing hydrogen sulfide donor, GYY4137, exhibits novel anti-cancer effects in vitro and in vivo. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0021077"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"101220","DOI":"10.1016\/j.redox.2019.101220","article-title":"Sodium sulfide selectively induces oxidative stress, DNA damage, and mitochondrial dysfunction and radiosensitizes glioblastoma (GBM) cells","volume":"26","author":"Xiao","year":"2019","journal-title":"Redox Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1515\/hsz-2015-0148","article-title":"Exogenous hydrogen sulfide exhibits anti-cancer effects though p38 MAPK signaling pathway in C6 glioma cells","volume":"396","author":"Zhao","year":"2015","journal-title":"Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"3182","DOI":"10.1073\/pnas.1321871111","article-title":"Hydrogen sulfide cytoprotective signaling is endothelial nitric oxide synthase-nitric oxide dependent","volume":"111","author":"King","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1161\/HYPERTENSIONAHA.117.10562","article-title":"Cystathionine gamma-Lyase-Produced Hydrogen Sulfide Controls Endothelial NO Bioavailability and Blood Pressure","volume":"71","author":"Szijarto","year":"2018","journal-title":"Hypertension"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"102517","DOI":"10.1016\/j.redox.2022.102517","article-title":"Human ultrarare genetic disorders of sulfur metabolism demonstrate redundancies in H2S homeostasis","volume":"58","author":"Kozich","year":"2022","journal-title":"Redox Biol."},{"key":"ref_70","doi-asserted-by":"crossref","unstructured":"Zainol Abidin, Q.H., Ida, T., Morita, M., Matsunaga, T., Nishimura, A., Jung, M., Hassan, N., Takata, T., Ishii, I., and Kruger, W. (2023). Synthesis of Sulfides and Persulfides Is Not Impeded by Disruption of Three Canonical Enzymes in Sulfur Metabolism. Antioxidants, 12.","DOI":"10.3390\/antiox12040868"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"10573","DOI":"10.1021\/ja505371z","article-title":"Understanding hydrogen sulfide storage: Probing conditions for sulfide release from hydrodisulfides","volume":"136","author":"Bailey","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"7606","DOI":"10.1073\/pnas.1321232111","article-title":"Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling","volume":"111","author":"Ida","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Trummer, M., Galardon, E., Fischer, A., Toegel, S., Mayer, B., Steiner, G., and Kloesch, B. (2021). Characterization of the Inducible and Slow-Releasing Hydrogen Sulfide and Persulfide Donor P*: Insights into Hydrogen Sulfide Signaling. Antioxidants, 10.","DOI":"10.3390\/antiox10071049"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"18689","DOI":"10.1021\/jacs.4c05874","article-title":"Transpersulfidation or H2S Release? Understanding the Landscape of Persulfide Chemical Biology","volume":"146","author":"Fosnacht","year":"2024","journal-title":"J. Am. Chem. Soc."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"104066","DOI":"10.1016\/j.redox.2026.104066","article-title":"Endothelial cystathionine-gamma-lyase (CTH) regulates body weight and insulin resistance in mice fed a high-fat diet","volume":"91","author":"Yagi","year":"2026","journal-title":"Redox Biol."},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Geng, B., Cai, B., Liao, F., Zheng, Y., Zeng, Q., Fan, X., Gong, Y., Yang, J., Cui, Q.H., and Tang, C. (2013). Increase or decrease hydrogen sulfide exert opposite lipolysis, but reduce global insulin resistance in high fatty diet induced obese mice. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0073892"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1161\/CIRCULATIONAHA.118.034757","article-title":"Cystathionine gamma Lyase Sulfhydrates the RNA Binding Protein Human Antigen R to Preserve Endothelial Cell Function and Delay Atherogenesis","volume":"139","author":"Bibli","year":"2019","journal-title":"Circulation"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"bqaa176","DOI":"10.1210\/endocr\/bqaa176","article-title":"Enhanced Stromal Cell CBS-H2S Production Promotes Estrogen-Stimulated Human Endometrial Angiogenesis","volume":"161","author":"Qi","year":"2020","journal-title":"Endocrinology"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1636S","DOI":"10.1093\/jn\/136.6.1636S","article-title":"The sulfur-containing amino acids: An overview","volume":"136","author":"Brosnan","year":"2006","journal-title":"J. Nutr."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1038\/s43018-022-00355-4","article-title":"MYCN mediates cysteine addiction and sensitizes neuroblastoma to ferroptosis","volume":"3","author":"Alborzinia","year":"2022","journal-title":"Nat. Cancer"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/s42255-020-0253-2","article-title":"Polyamine pathway activity promotes cysteine essentiality in cancer cells","volume":"2","author":"Zhang","year":"2020","journal-title":"Nat. Metab."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.cmet.2020.12.007","article-title":"Non-canonical Glutamate-Cysteine Ligase Activity Protects against Ferroptosis","volume":"33","author":"Kang","year":"2021","journal-title":"Cell Metab."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1182\/bloodadvances.2023010786","article-title":"The nonessential amino acid cysteine is required to prevent ferroptosis in acute myeloid leukemia","volume":"8","author":"Cunningham","year":"2024","journal-title":"Blood Adv."},{"key":"ref_84","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":"ref_85","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1089\/ars.2019.7850","article-title":"Cysteine Deprivation Targets Ovarian Clear Cell Carcinoma Via Oxidative Stress and Iron-Sulfur Cluster Biogenesis Deficit","volume":"33","author":"Novera","year":"2020","journal-title":"Antioxid. Redox Signal"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"31189","DOI":"10.1073\/pnas.2017152117","article-title":"Oncogenic activation of PI3K-AKT-mTOR signaling suppresses ferroptosis via SREBP-mediated lipogenesis","volume":"117","author":"Yi","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"420","DOI":"10.1016\/j.chembiol.2018.11.016","article-title":"Exogenous Monounsaturated Fatty Acids Promote a Ferroptosis-Resistant Cell State","volume":"26","author":"Magtanong","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.1111\/j.1476-5381.2012.02113.x","article-title":"Hydrogen sulfide inhibits the translational expression of hypoxia-inducible factor-1alpha","volume":"167","author":"Wu","year":"2012","journal-title":"Br. J. Pharmacol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.biochi.2015.03.009","article-title":"Hydrogen sulphide induces HIF-1alpha and Nrf2 in THP-1 macrophages","volume":"112","author":"Lohninger","year":"2015","journal-title":"Biochimie"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"eaaz8534","DOI":"10.1126\/sciadv.aaz8534","article-title":"Cystathione beta-synthase regulates HIF-1alpha stability through persulfidation of PHD2","volume":"6","author":"Dey","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1021\/acs.biochem.6b01172","article-title":"Structural Snapshots of an Engineered Cystathionine-gamma-lyase Reveal the Critical Role of Electrostatic Interactions in the Active Site","volume":"56","author":"Yan","year":"2017","journal-title":"Biochemistry"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1089\/ars.2011.4349","article-title":"Role of cystathionine gamma-lyase\/hydrogen sulfide pathway in cardiovascular disease: A novel therapeutic strategy?","volume":"17","author":"Pan","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.cmet.2025.10.003","article-title":"Cystine import and oxidative catabolism fuel vascular growth and repair via nutrient-responsive histone acetylation","volume":"38","author":"Drekolia","year":"2026","journal-title":"Cell Metab."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2943","DOI":"10.1073\/pnas.1115634109","article-title":"Hydrogen sulfide (H2S) metabolism in mitochondria and its regulatory role in energy production","volume":"109","author":"Fu","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"H927","DOI":"10.1152\/ajpheart.00718.2012","article-title":"Hydrogen sulfide in the mouse ductus arteriosus: A naturally occurring relaxant with potential EDHF function","volume":"304","author":"Baragatti","year":"2013","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"H1568","DOI":"10.1152\/ajpheart.00555.2010","article-title":"Extracellular transsulfuration generates hydrogen sulfide from homocysteine and protects endothelium from redox stress","volume":"299","author":"Bearden","year":"2010","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1681\/ASN.2008040406","article-title":"Large-scale proteomics and phosphoproteomics of urinary exosomes","volume":"20","author":"Gonzales","year":"2009","journal-title":"J. Am. Soc. Nephrol."},{"key":"ref_98","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":"ref_99","doi-asserted-by":"crossref","first-page":"1.30.1","DOI":"10.1002\/cpbi.5","article-title":"The GeneCards Suite: From Gene Data Mining to Disease Genome Sequence Analyses","volume":"54","author":"Stelzer","year":"2016","journal-title":"Curr. Protoc. Bioinform."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"3076","DOI":"10.1074\/jbc.M805459200","article-title":"Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H2S","volume":"284","author":"Sun","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/nrm.2017.130","article-title":"A brave new world of RNA-binding proteins","volume":"19","author":"Hentze","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"190096","DOI":"10.1098\/rsob.190096","article-title":"RNA-protein interactions: Disorder, moonlighting and junk contribute to eukaryotic complexity","volume":"9","author":"Balcerak","year":"2019","journal-title":"Open Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"e1714","DOI":"10.1002\/wrna.1714","article-title":"Deep structural insights into RNA-binding disordered protein regions","volume":"13","author":"Zeke","year":"2022","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1016\/j.tibs.2015.08.012","article-title":"Emerging Roles of Disordered Sequences in RNA-Binding Proteins","volume":"40","author":"Calabretta","year":"2015","journal-title":"Trends Biochem. Sci."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"200328","DOI":"10.1098\/rsob.200328","article-title":"The role of disorder in RNA binding affinity and specificity","volume":"10","author":"Ottoz","year":"2020","journal-title":"Open Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1042\/BST20200664","article-title":"The expanding world of metabolic enzymes moonlighting as RNA binding proteins","volume":"49","author":"Curtis","year":"2021","journal-title":"Biochem. Soc. Trans."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1186\/s12964-016-0132-3","article-title":"The new (dis)order in RNA regulation","volume":"14","author":"Jarvelin","year":"2016","journal-title":"Cell Commun. Signal"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"D508","DOI":"10.1093\/nar\/gks1226","article-title":"D2P2: Database of disordered protein predictions","volume":"41","author":"Oates","year":"2013","journal-title":"Nucleic Acids Res."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"9364","DOI":"10.1038\/s41598-024-57625-7","article-title":"Catalytic specificity and crystal structure of cystathionine gamma-lyase from Pseudomonas aeruginosa","volume":"14","author":"Pedretti","year":"2024","journal-title":"Sci. Rep."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1161\/CIRCRESAHA.123.323084","article-title":"Disrupted Binding of Cystathionine gamma-Lyase to p53 Promotes Endothelial Senescence","volume":"133","author":"Hu","year":"2023","journal-title":"Circ. Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"D535","DOI":"10.1093\/nar\/gkj109","article-title":"BioGRID: A general repository for interaction datasets","volume":"34","author":"Stark","year":"2006","journal-title":"Nucleic Acids Res."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1002\/pro.3978","article-title":"The BioGRID database: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions","volume":"30","author":"Oughtred","year":"2021","journal-title":"Protein Sci."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"D452","DOI":"10.1093\/nar\/gkh052","article-title":"IntAct: An open source molecular interaction database","volume":"32","author":"Hermjakob","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"D358","DOI":"10.1093\/nar\/gkt1115","article-title":"The MIntAct project\u2014IntAct as a common curation platform for 11 molecular interaction databases","volume":"42","author":"Orchard","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"D744","DOI":"10.1093\/nar\/gkq897","article-title":"HitPredict: A database of quality assessed protein-protein interactions in nine species","volume":"39","author":"Patil","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1212","DOI":"10.1016\/j.cell.2014.10.050","article-title":"A proteome-scale map of the human interactome network","volume":"159","author":"Rolland","year":"2014","journal-title":"Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.cell.2015.06.043","article-title":"The BioPlex Network: A Systematic Exploration of the Human Interactome","volume":"162","author":"Huttlin","year":"2015","journal-title":"Cell"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/s41586-020-2188-x","article-title":"A reference map of the human binary protein interactome","volume":"580","author":"Luck","year":"2020","journal-title":"Nature"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"3022","DOI":"10.1016\/j.cell.2021.04.011","article-title":"Dual proteome-scale networks reveal cell-specific remodeling of the human interactome","volume":"184","author":"Huttlin","year":"2021","journal-title":"Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"4043","DOI":"10.1038\/s41467-022-31809-z","article-title":"Scalable multiplex co-fractionation\/mass spectrometry platform for accelerated protein interactome discovery","volume":"13","author":"Havugimana","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"4906","DOI":"10.1038\/s41467-022-32689-z","article-title":"Spatiotemporal-resolved protein networks profiling with photoactivation dependent proximity labeling","volume":"13","author":"Zhai","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_122","doi-asserted-by":"crossref","unstructured":"Minor, M.M., Hollinger, F.B., McNees, A.L., Jung, S.Y., Jain, A., Hyser, J.M., Bissig, K.D., and Slagle, B.L. (2020). Hepatitis B Virus HBx Protein Mediates the Degradation of Host Restriction Factors through the Cullin 4 DDB1 E3 Ubiquitin Ligase Complex. Cells, 9.","DOI":"10.3390\/cells9040834"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"32046","DOI":"10.1074\/jbc.M403044200","article-title":"Comprehensive proteomic analysis of interphase and mitotic 14-3-3-binding proteins","volume":"279","author":"Meek","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"8963","DOI":"10.1038\/s41598-021-88355-9","article-title":"A novel cystathionine gamma-lyase inhibitor, I194496, inhibits the growth and metastasis of human TNBC via downregulating multiple signaling pathways","volume":"11","author":"Liu","year":"2021","journal-title":"Sci. Rep."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nmeth.1283","article-title":"Cost-effective strategies for completing the interactome","volume":"6","author":"Schwartz","year":"2009","journal-title":"Nat. Methods"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"2506","DOI":"10.1016\/j.devcel.2024.06.002","article-title":"Next-generation Drosophila protein interactome map and its functional implications","volume":"59","author":"Bhat","year":"2024","journal-title":"Dev. Cell"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.bbagrm.2018.10.006","article-title":"m6A-mediated translation regulation","volume":"1862","author":"Meyer","year":"2019","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1388","DOI":"10.1016\/j.cell.2015.05.014","article-title":"N6-methyladenosine Modulates Messenger RNA Translation Efficiency","volume":"161","author":"Wang","year":"2015","journal-title":"Cell"},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Zha, T., Yao, J., Wang, H., Cao, Q., Zhang, J., Chen, Z., and Wang, J. (2026). RNA binding protein YWHAZ mediates translation of specific mRNA and regulates cell Proliferation and apoptosis in diabetic foot ulcer. Front. Med. (Pathol. Sect.), 13.","DOI":"10.3389\/fmed.2026.1751279"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1038\/s41388-024-02959-9","article-title":"TMEM65 promotes gastric tumorigenesis by targeting YWHAZ to activate PI3K-Akt-mTOR pathway and is a therapeutic target","volume":"43","author":"Shi","year":"2024","journal-title":"Oncogene"},{"key":"ref_131","doi-asserted-by":"crossref","unstructured":"Zanon, A., Rakovic, A., Blankenburg, H., Doncheva, N.T., Schwienbacher, C., Serafin, A., Alexa, A., Weichenberger, C.X., Albrecht, M., and Klein, C. (2013). Profiling of Parkin-binding partners using tandem affinity purification. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0078648"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1158\/1541-7786.MCR-21-0729","article-title":"PARK2 regulates eIF4B-driven lymphomagenesis","volume":"20","author":"Kapadia","year":"2022","journal-title":"Mol. Cancer Res."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.gene.2010.09.003","article-title":"Diminution of eIF4E activity suppresses parkin mutant phenotypes","volume":"470","author":"Ottone","year":"2011","journal-title":"Gene"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1007\/s13577-020-00362-6","article-title":"SDC1 promotes cisplatin resistance in hepatic carcinoma cells via PI3K-AKT pathway","volume":"33","author":"Yu","year":"2020","journal-title":"Hum. Cell"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"117783","DOI":"10.1016\/j.bcp.2026.117783","article-title":"CUL4A promotes glycolytic metabolism of fibroblast-like synoviocytes by targeting FGF2 in rheumatoid arthritis","volume":"247","author":"Sun","year":"2026","journal-title":"Biochem. Pharmacol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1128\/MCB.00973-07","article-title":"RNA-binding proteins HuR and PTB promote the translation of hypoxia-inducible factor 1alpha","volume":"28","author":"Galban","year":"2008","journal-title":"Mol. Cell Biol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1002\/path.4516","article-title":"Multifocal endometriotic lesions associated with cancer are clonal and carry a high mutation burden","volume":"236","author":"Anglesio","year":"2015","journal-title":"J. Pathol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2538","DOI":"10.1158\/1078-0432.CCR-10-3314","article-title":"IL6-STAT3-HIF signaling and therapeutic response to the angiogenesis inhibitor sunitinib in ovarian clear cell cancer","volume":"17","author":"Anglesio","year":"2011","journal-title":"Clin. Cancer Res."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3962","DOI":"10.1158\/1078-0432.CCR-18-3691","article-title":"Survival Following Chemotherapy in Ovarian Clear Cell Carcinoma Is Not Associated with Pathological Misclassification of Tumor Histotype","volume":"25","author":"Takenaka","year":"2019","journal-title":"Clin. Cancer Res."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1038\/modpathol.2013.216","article-title":"Loss of ARID1A expression and its relationship with PI3K-Akt pathway alterations and ZNF217 amplification in ovarian clear cell carcinoma","volume":"27","author":"Huang","year":"2014","journal-title":"Mod. Pathol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1038\/modpathol.2011.161","article-title":"Loss of ARID1A expression is related to shorter progression-free survival and chemoresistance in ovarian clear cell carcinoma","volume":"25","author":"Katagiri","year":"2012","journal-title":"Mod. Pathol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"6118","DOI":"10.1038\/ncomms7118","article-title":"Coexistent ARID1A-PIK3CA mutations promote ovarian clear-cell tumorigenesis through pro-tumorigenic inflammatory cytokine signalling","volume":"6","author":"Chandler","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Amano, T., Murakami, A., Murakami, T., and Chano, T. (2021). Antioxidants and Therapeutic Targets in Ovarian Clear Cell Carcinoma. Antioxidants, 10.","DOI":"10.3390\/antiox10020187"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"34949","DOI":"10.1038\/srep34949","article-title":"Quantitative Profiling of Single Formalin Fixed Tumour Sections: Proteomics for translational research","volume":"6","author":"Hughes","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1002\/path.4934","article-title":"Clear cell and endometrioid carcinomas: Are their differences attributable to distinct cells of origin?","volume":"243","author":"Cochrane","year":"2017","journal-title":"J. Pathol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"7678","DOI":"10.1158\/0008-5472.CAN-04-2933","article-title":"Mutation of the PIK3CA gene in ovarian and breast cancer","volume":"64","author":"Campbell","year":"2004","journal-title":"Cancer Res."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.2353\/ajpath.2009.081000","article-title":"Frequent activating mutations of PIK3CA in ovarian clear cell carcinoma","volume":"174","author":"Kuo","year":"2009","journal-title":"Am. J. Pathol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.apsb.2015.05.007","article-title":"HIF-1alpha pathway: Role, regulation and intervention for cancer therapy","volume":"5","author":"Masoud","year":"2015","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s00280-024-04748-3","article-title":"Targeting on the PI3K\/mTOR: A potential treatment strategy for clear cell ovarian carcinoma","volume":"95","author":"Zheng","year":"2025","journal-title":"Cancer Chemother. Pharmacol."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"e2317846121","DOI":"10.1073\/pnas.2317846121","article-title":"Stress response regulation of mRNA translation: Implications for antioxidant enzyme expression in cancer","volume":"121","author":"Kim","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Muppirala, U.K., Honavar, V.G., and Dobbs, D. (2011). Predicting RNA-protein interactions using only sequence information. BMC Bioinform., 12.","DOI":"10.1186\/1471-2105-12-489"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"182","DOI":"10.4172\/jcsb.1000115","article-title":"Computational tools for investigating RNA-protein interaction partners","volume":"6","author":"Muppirala","year":"2013","journal-title":"J. Comput Sci. Syst. Biol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"D277","DOI":"10.1093\/nar\/gkq1108","article-title":"PRIDB: A Protein-RNA interface database","volume":"39","author":"Lewis","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"922","DOI":"10.1111\/bph.12171","article-title":"Selectivity of commonly used pharmacological inhibitors for cystathionine beta synthase (CBS) and cystathionine gamma lyase (CSE)","volume":"169","author":"Asimakopoulou","year":"2013","journal-title":"Br. J. Pharmacol."},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Wei, L., El-Naggar, A.M., Li, Y., Ding, Y., Li, E., Lam, T., Wang, Y., Turgu, B., and Huntsman, D.G. (2026). Co-targeting cystathionine gamma-lyase and mTOR: A promising therapeutic strategy in clear cell ovarian cancer. BMC Cancer.","DOI":"10.1186\/s12885-026-16092-1"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"e11","DOI":"10.1017\/S0033583516000056","article-title":"The molecular choreography of protein synthesis: Translational control, regulation, and pathways","volume":"49","author":"Chen","year":"2016","journal-title":"Q. Rev. Biophys."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Ikeuchi, K., Izawa, T., and Inada, T. (2018). Recent Progress on the Molecular Mechanism of Quality Controls Induced by Ribosome Stalling. Front. Genet., 9.","DOI":"10.3389\/fgene.2018.00743"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1093\/nar\/gkz763","article-title":"Ribosome pausing, a dangerous necessity for co-translational events","volume":"48","author":"Collart","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"a032813","DOI":"10.1101\/cshperspect.a032813","article-title":"Stress Granules and Processing Bodies in Translational Control","volume":"11","author":"Ivanov","year":"2019","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/s41419-025-07800-z","article-title":"Stress granules and cell death: Crosstalk and potential therapeutic strategies in infectious diseases","volume":"16","author":"Huang","year":"2025","journal-title":"Cell Death Dis."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1007\/s00204-025-04026-y","article-title":"Intracellular hydrogen sulfide induces stress granule formation and translational repression through eIF2alpha phosphorylation","volume":"99","author":"Kanno","year":"2025","journal-title":"Arch. Toxicol."}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/12\/1106\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T09:35:12Z","timestamp":1781861712000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/15\/12\/1106"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,18]]},"references-count":161,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2026,6]]}},"alternative-id":["cells15121106"],"URL":"https:\/\/doi.org\/10.3390\/cells15121106","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,18]]}}}