{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,5]],"date-time":"2026-11-05T23:58:38Z","timestamp":1793923118448,"version":"4.8.0"},"reference-count":72,"publisher":"Springer Science and Business Media LLC","issue":"10","license":[{"start":{"date-parts":[[2024,3,20]],"date-time":"2024-03-20T00:00:00Z","timestamp":1710892800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,3,20]],"date-time":"2024-03-20T00:00:00Z","timestamp":1710892800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R35GM130183"],"award-info":[{"award-number":["R35GM130183"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R01CA248160"],"award-info":[{"award-number":["R01CA248160"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R01CA148828"],"award-info":[{"award-number":["R01CA148828"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"U.S. Department of Health & Human Services | National Institutes of Health","doi-asserted-by":"publisher","award":["R01CA245546"],"award-info":[{"award-number":["R01CA245546"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Chem Biol"],"published-print":{"date-parts":[[2024,10]]},"DOI":"10.1038\/s41589-024-01583-8","type":"journal-article","created":{"date-parts":[[2024,3,20]],"date-time":"2024-03-20T07:02:35Z","timestamp":1710918155000},"page":"1294-1304","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Sulfide oxidation promotes hypoxic angiogenesis and neovascularization"],"prefix":"10.1038","volume":"20","author":[{"given":"Roshan","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Vitvitsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Apichaya","family":"Sethaudom","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashi","family":"Singhal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sumeet","family":"Solanki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sydney","family":"Alibeckoff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6199-0744","authenticated-orcid":false,"given":"Harrison L.","family":"Hiraki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hannah N.","family":"Bell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Andren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brendon M.","family":"Baker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Costas A.","family":"Lyssiotis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2487-4816","authenticated-orcid":false,"given":"Yatrik M.","family":"Shah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8332-3275","authenticated-orcid":false,"given":"Ruma","family":"Banerjee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,3,20]]},"reference":[{"key":"1583_CR1","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1038\/nm0603-653","volume":"9","author":"P Carmeliet","year":"2003","unstructured":"Carmeliet, P. Angiogenesis in health and disease. Nat. Med. 9, 653\u2013660 (2003).","journal-title":"Nat. Med."},{"key":"1583_CR2","doi-asserted-by":"publisher","first-page":"932","DOI":"10.1038\/nature04478","volume":"438","author":"P Carmeliet","year":"2005","unstructured":"Carmeliet, P. Angiogenesis in life, disease and medicine. Nature 438, 932\u2013936 (2005).","journal-title":"Nature"},{"key":"1583_CR3","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1146\/annurev.med.57.121304.131306","volume":"57","author":"J Folkman","year":"2006","unstructured":"Folkman, J. Angiogenesis. Annu. Rev. Med. 57, 1\u201318 (2006).","journal-title":"Annu. Rev. Med."},{"key":"1583_CR4","doi-asserted-by":"publisher","first-page":"2335","DOI":"10.1056\/NEJMoa032691","volume":"350","author":"H Hurwitz","year":"2004","unstructured":"Hurwitz, H. et al. Bevacizumab plus irinotecan, fluorouracil, and leucovorin for metastatic colorectal cancer. N. Engl. J. Med. 350, 2335\u20132342 (2004).","journal-title":"N. Engl. J. Med."},{"key":"1583_CR5","doi-asserted-by":"publisher","first-page":"981","DOI":"10.1016\/j.tranon.2019.04.022","volume":"12","author":"D Ribatti","year":"2019","unstructured":"Ribatti, D., Annese, T., Ruggieri, S., Tamma, R. & Crivellato, E. Limitations of anti-angiogenic treatment of tumors. Transl. Oncol. 12, 981\u2013986 (2019).","journal-title":"Transl. Oncol."},{"key":"1583_CR6","doi-asserted-by":"publisher","first-page":"853","DOI":"10.1111\/j.1476-5381.2010.01191.x","volume":"164","author":"C Szabo","year":"2011","unstructured":"Szabo, C. & Papapetropoulos, A. Hydrogen sulphide and angiogenesis: mechanisms and applications. Br. J. Pharmacol. 164, 853\u2013865 (2011).","journal-title":"Br. J. Pharmacol."},{"key":"1583_CR7","doi-asserted-by":"publisher","first-page":"1924","DOI":"10.1016\/j.jvs.2018.08.172","volume":"69","author":"AM Rushing","year":"2019","unstructured":"Rushing, A. M. et al. Effects of a novel hydrogen sulfide prodrug in a porcine model of acute limb ischemia. J. Vasc. Surg. 69, 1924\u20131935 (2019).","journal-title":"J. Vasc. Surg."},{"key":"1583_CR8","doi-asserted-by":"publisher","first-page":"9161","DOI":"10.1073\/pnas.1202916109","volume":"109","author":"C Coletta","year":"2012","unstructured":"Coletta, C. et al. Hydrogen sulfide and nitric oxide are mutually dependent in the regulation of angiogenesis and endothelium-dependent vasorelaxation. Proc. Natl Acad. Sci. USA 109, 9161\u20139166 (2012).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1583_CR9","doi-asserted-by":"publisher","first-page":"21972","DOI":"10.1073\/pnas.0908047106","volume":"106","author":"A Papapetropoulos","year":"2009","unstructured":"Papapetropoulos, A. et al. Hydrogen sulfide is an endogenous stimulator of angiogenesis. Proc. Natl Acad. Sci. USA 106, 21972\u201321977 (2009).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1583_CR10","doi-asserted-by":"publisher","first-page":"117","DOI":"10.1016\/j.cell.2018.03.001","volume":"173","author":"A Longchamp","year":"2018","unstructured":"Longchamp, A. et al. Amino acid restriction triggers angiogenesis via GCN2\/ATF4 regulation of VEGF and H2S production. Cell 173, 117\u2013129 (2018).","journal-title":"Cell"},{"key":"1583_CR11","doi-asserted-by":"publisher","first-page":"4011","DOI":"10.1242\/jeb.02480","volume":"209","author":"KR Olson","year":"2006","unstructured":"Olson, K. R. et al. Hydrogen sulfide as an oxygen sensor\/transducer in vertebrate hypoxic vasoconstriction and hypoxic vasodilation. J. Exp. Biol. 209, 4011\u20134023 (2006).","journal-title":"J. Exp. Biol."},{"key":"1583_CR12","doi-asserted-by":"publisher","first-page":"1293","DOI":"10.1073\/pnas.1119658109","volume":"109","author":"T Morikawa","year":"2012","unstructured":"Morikawa, T. et al. Hypoxic regulation of the cerebral microcirculation is mediated by a carbon monoxide-sensitive hydrogen sulfide pathway. Proc. Natl Acad. Sci. USA 109, 1293\u20131298 (2012).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1583_CR13","doi-asserted-by":"publisher","first-page":"1518","DOI":"10.1016\/j.bbapap.2011.02.004","volume":"1814","author":"S Singh","year":"2011","unstructured":"Singh, S. & Banerjee, R. PLP-dependent H2S biogenesis. Biochim. Biophys. Acta 1814, 1518\u20131527 (2011).","journal-title":"Biochim. Biophys. Acta"},{"key":"1583_CR14","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1089\/ars.2005.7.547","volume":"7","author":"C-G Zou","year":"2005","unstructured":"Zou, C.-G. & Banerjee, R. Homocysteine and redox signaling. Antioxid. Redox Signal. 7, 547\u2013559 (2005).","journal-title":"Antioxid. Redox Signal."},{"key":"1583_CR15","doi-asserted-by":"publisher","first-page":"R39","DOI":"10.1152\/ajpregu.00036.2004","volume":"287","author":"V Vitvitsky","year":"2004","unstructured":"Vitvitsky, V. et al. Perturbations in homocysteine-linked redox homeostasis in a murine model for hyperhomocysteinemia. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287, R39\u2013R46 (2004).","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"1583_CR16","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1080\/10409238.2021.1893641","volume":"56","author":"R Kumar","year":"2021","unstructured":"Kumar, R. & Banerjee, R. Regulation of the redox metabolome and thiol proteome by hydrogen sulfide. Crit. Rev. Biochem. Mol. Biol. 56, 221\u2013235 (2021).","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"1583_CR17","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1089\/ars.2022.0067","volume":"38","author":"D Hanna","year":"2023","unstructured":"Hanna, D., Kumar, R. & Banerjee, R. A metabolic paradigm for hydrogen sulfide signaling via electron transport chain plasticity. Antioxid. Redox Signal. 38, 57\u201367 (2023).","journal-title":"Antioxid. Redox Signal."},{"key":"1583_CR18","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1016\/j.cbpa.2017.02.021","volume":"37","author":"R Banerjee","year":"2017","unstructured":"Banerjee, R. Catalytic promiscuity and heme-dependent redox regulation of H2S synthesis. Curr. Opin. Chem. Biol. 37, 115\u2013121 (2017).","journal-title":"Curr. Opin. Chem. Biol."},{"key":"1583_CR19","doi-asserted-by":"publisher","first-page":"102517","DOI":"10.1016\/j.redox.2022.102517","volume":"58","author":"V Kozich","year":"2022","unstructured":"Kozich, V. et al. Human ultrarare genetic disorders of sulfur metabolism demonstrate redundancies in H2S homeostasis. Redox Biol. 58, 102517 (2022).","journal-title":"Redox Biol."},{"key":"1583_CR20","doi-asserted-by":"publisher","first-page":"11601","DOI":"10.1074\/jbc.M808026200","volume":"284","author":"T Chiku","year":"2009","unstructured":"Chiku, T. et al. H2S biogenesis by human cystathionine \u03b3-lyase leads to the novel sulfur metabolites lanthionine and homolanthionine and is responsive to the grade of hyperhomocysteinemia. J. Biol. Chem. 284, 11601\u201311612 (2009).","journal-title":"J. Biol. Chem."},{"key":"1583_CR21","doi-asserted-by":"publisher","first-page":"12809","DOI":"10.1021\/ja904468w","volume":"131","author":"CL Weeks","year":"2009","unstructured":"Weeks, C. L., Singh, S., Madzelan, P., Banerjee, R. & Spiro, T. G. Heme regulation of human cystathionine \u03b2-synthase activity: insights from fluorescence and Raman spectroscopy. J. Am. Chem. Soc. 131, 12809\u201312816 (2009).","journal-title":"J. Am. Chem. Soc."},{"key":"1583_CR22","doi-asserted-by":"publisher","first-page":"631","DOI":"10.1039\/B604182P","volume":"24","author":"S Singh","year":"2007","unstructured":"Singh, S., Madzelan, P. & Banerjee, R. Properties of an unusual heme cofactor in PLP-dependent cystathionine \u03b2-synthase. Nat. Prod. Rep. 24, 631\u2013639 (2007).","journal-title":"Nat. Prod. Rep."},{"key":"1583_CR23","doi-asserted-by":"publisher","first-page":"16418","DOI":"10.1074\/jbc.C116.742213","volume":"291","author":"O Kabil","year":"2016","unstructured":"Kabil, O., Yadav, V. & Banerjee, R. Heme-dependent metabolite switching regulates H2S synthesis in response to ER stress. J. Biol. Chem. 291, 16418\u201316423 (2016).","journal-title":"J. Biol. Chem."},{"key":"1583_CR24","doi-asserted-by":"publisher","first-page":"R1479","DOI":"10.1152\/ajpregu.90566.2008","volume":"295","author":"J Furne","year":"2008","unstructured":"Furne, J., Saeed, A. & Levitt, M. D. Whole tissue hydrogen sulfide concentrations are orders of magnitude lower than presently accepted values. Am. J. Physiol. Regul. Integr. Comp. Physiol. 295, R1479\u2013R1485 (2008).","journal-title":"Am. J. Physiol. Regul. Integr. Comp. Physiol."},{"key":"1583_CR25","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1089\/ars.2011.4310","volume":"17","author":"V Vitvitsky","year":"2012","unstructured":"Vitvitsky, V., Kabil, O. & Banerjee, R. High turnover rates for hydrogen sulfide allow for rapid regulation of its tissue concentrations. Antioxid. Redox Signal. 17, 22\u201331 (2012).","journal-title":"Antioxid. Redox Signal."},{"key":"1583_CR26","doi-asserted-by":"publisher","first-page":"12077","DOI":"10.1074\/jbc.RA119.009442","volume":"294","author":"M Libiad","year":"2019","unstructured":"Libiad, M. et al. Hydrogen sulfide perturbs mitochondrial bioenergetics and triggers metabolic reprogramming in colon cells. J. Biol. Chem. 294, 12077\u201312090 (2019).","journal-title":"J. Biol. Chem."},{"key":"1583_CR27","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1016\/j.tibs.2022.03.011","volume":"47","author":"R Banerjee","year":"2022","unstructured":"Banerjee, R. & Kumar, R. Gas regulation of complex II reversal via electron shunting to fumarate in the mammalian ETC. Trends Biochem. Sci. 47, 689\u2013698 (2022).","journal-title":"Trends Biochem. Sci."},{"key":"1583_CR28","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2021.100736","volume":"296","author":"V Vitvitsky","year":"2021","unstructured":"Vitvitsky, V. et al. The mitochondrial NADH pool is involved in hydrogen sulfide signaling and stimulation of aerobic glycolysis. J. Biol. Chem. 296, 100736 (2021).","journal-title":"J. Biol. Chem."},{"key":"1583_CR29","doi-asserted-by":"publisher","first-page":"115191","DOI":"10.1016\/j.ab.2023.115191","volume":"673","author":"DA Hanna","year":"2023","unstructured":"Hanna, D. A., Vitvitsky, V. & Banerjee, R. A growth chamber for chronic exposure of mammalian cells to H2S. Anal. Biochem. 673, 115191 (2023).","journal-title":"Anal. Biochem."},{"key":"1583_CR30","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2021.100950","volume":"297","author":"S Carballal","year":"2021","unstructured":"Carballal, S. et al. Hydrogen sulfide stimulates lipid biogenesis from glutamine that is dependent on the mitochondrial NAD(P)H pool. J. Biol. Chem. 297, 100950 (2021).","journal-title":"J. Biol. Chem."},{"key":"1583_CR31","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1016\/j.cell.2013.06.037","volume":"154","author":"K De Bock","year":"2013","unstructured":"De Bock, K. et al. Role of PFKFB3-driven glycolysis in vessel sprouting. Cell 154, 651\u2013663 (2013).","journal-title":"Cell"},{"key":"1583_CR32","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1038\/s42255-018-0011-x","volume":"1","author":"LP Diebold","year":"2019","unstructured":"Diebold, L. P. et al. Mitochondrial complex III is necessary for endothelial cell proliferation during angiogenesis. Nat. Metab. 1, 158\u2013171 (2019).","journal-title":"Nat. Metab."},{"key":"1583_CR33","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2021.101435","volume":"298","author":"R Kumar","year":"2022","unstructured":"Kumar, R. et al. A redox cycle with complex II prioritizes sulfide quinone oxidoreductase-dependent H2S oxidation. J. Biol. Chem. 298, 101435 (2022).","journal-title":"J. Biol. Chem."},{"key":"1583_CR34","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1126\/science.abi7495","volume":"374","author":"JB Spinelli","year":"2021","unstructured":"Spinelli, J. B. et al. Fumarate is a terminal electron acceptor in the mammalian electron transport chain. Science 374, 1227\u20131237 (2021).","journal-title":"Science"},{"key":"1583_CR35","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-021-23363-x","volume":"12","author":"E Marutani","year":"2021","unstructured":"Marutani, E. et al. Sulfide catabolism ameliorates hypoxic brain injury. Nat. Commun. 12, 3108 (2021).","journal-title":"Nat. Commun."},{"key":"1583_CR36","doi-asserted-by":"crossref","unstructured":"Jackson, M. R. et al. Discovery of a first-in-class inhibitor of sulfide:quinone oxidoreductase that protects against adverse cardiac remodeling and heart failure. Cardiovasc. Res. 118, 1771\u20131784 (2022).","DOI":"10.1093\/cvr\/cvab206"},{"key":"1583_CR37","doi-asserted-by":"publisher","first-page":"1358","DOI":"10.1152\/japplphysiol.00449.2004","volume":"97","author":"KD Mansfield","year":"2004","unstructured":"Mansfield, K. D., Simon, M. C. & Keith, B. Hypoxic reduction in cellular glutathione levels requires mitochondrial reactive oxygen species. J. Appl. Physiol. 97, 1358\u20131366 (2004).","journal-title":"J. Appl. Physiol."},{"key":"1583_CR38","doi-asserted-by":"publisher","DOI":"10.1172\/JCI143691","volume":"131","author":"R Singhal","year":"2021","unstructured":"Singhal, R. et al. HIF-2\u03b1 activation potentiates oxidative cell death in colorectal cancers by increasing cellular iron. J. Clin. Invest. 131, e143691 (2021).","journal-title":"J. Clin. Invest."},{"key":"1583_CR39","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1002\/jcp.10118","volume":"192","author":"KN Maclean","year":"2002","unstructured":"Maclean, K. N. et al. Cystathionine \u03b2-synthase is coordinately regulated with proliferation through a redox-sensitive mechanism in cultured human cells and Saccharomyces cerevisiae. J. Cell. Physiol. 192, 81\u201392 (2002).","journal-title":"J. Cell. Physiol."},{"key":"1583_CR40","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1161\/01.RES.0000031799.12850.1E","volume":"91","author":"Y Shi","year":"2002","unstructured":"Shi, Y. et al. Chronic hypoxia increases endothelial nitric oxide synthase generation of nitric oxide by increasing heat shock protein 90 association and serine phosphorylation. Circ. Res. 91, 300\u2013306 (2002).","journal-title":"Circ. Res."},{"key":"1583_CR41","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1183\/09031936.95.08040515","volume":"8","author":"V Hampl","year":"1995","unstructured":"Hampl, V., Cornfield, D. N., Cowan, N. J. & Archer, S. L. Hypoxia potentiates nitric oxide synthesis and transiently increases cytosolic calcium levels in pulmonary artery endothelial cells. Eur. Respir. J. 8, 515\u2013522 (1995).","journal-title":"Eur. Respir. J."},{"key":"1583_CR42","doi-asserted-by":"publisher","first-page":"359","DOI":"10.1002\/(SICI)1097-4652(200003)182:3<359::AID-JCP6>3.0.CO;2-3","volume":"182","author":"JM Justice","year":"2000","unstructured":"Justice, J. M., Tanner, M. A. & Myers, P. R. Endothelial cell regulation of nitric oxide production during hypoxia in coronary microvessels and epicardial arteries. J. Cell. Physiol. 182, 359\u2013365 (2000).","journal-title":"J. Cell. Physiol."},{"key":"1583_CR43","doi-asserted-by":"publisher","first-page":"1189","DOI":"10.1161\/01.HYP.0000222892.37375.4d","volume":"47","author":"J Min","year":"2006","unstructured":"Min, J. et al. Hypoxia-induced endothelial NO synthase gene transcriptional activation is mediated through the tax-responsive element in endothelial cells. Hypertension 47, 1189\u20131196 (2006).","journal-title":"Hypertension"},{"key":"1583_CR44","doi-asserted-by":"publisher","first-page":"7606","DOI":"10.1073\/pnas.1321232111","volume":"111","author":"T Ida","year":"2014","unstructured":"Ida, T. et al. Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling. Proc. Natl Acad. Sci. USA 111, 7606\u20137611 (2014).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1583_CR45","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1021\/jacs.5b10494","volume":"138","author":"PK Yadav","year":"2016","unstructured":"Yadav, P. K. et al. Biosynthesis and reactivity of cysteine persulfides in signaling. J. Am. Chem. Soc. 138, 289\u2013299 (2016).","journal-title":"J. Am. Chem. Soc."},{"key":"1583_CR46","doi-asserted-by":"publisher","first-page":"3414","DOI":"10.1039\/C5SC04818D","volume":"7","author":"R Wedmann","year":"2016","unstructured":"Wedmann, R. et al. Improved tag\u2013switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. Chem. Sci. 7, 3414\u20133426 (2016).","journal-title":"Chem. Sci."},{"key":"1583_CR47","doi-asserted-by":"publisher","first-page":"1153","DOI":"10.1039\/C9LC01170F","volume":"20","author":"WY Wang","year":"2020","unstructured":"Wang, W. Y., Lin, D., Jarman, E. H., Polacheck, W. J. & Baker, B. M. Functional angiogenesis requires microenvironmental cues balancing endothelial cell migration and proliferation. Lab Chip 20, 1153\u20131166 (2020).","journal-title":"Lab Chip"},{"key":"1583_CR48","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1126\/science.aad4017","volume":"352","author":"DV Titov","year":"2016","unstructured":"Titov, D. V. et al. Complementation of mitochondrial electron transport chain by manipulation of the NAD+\/NADH ratio. Science 352, 231\u2013235 (2016).","journal-title":"Science"},{"key":"1583_CR49","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1038\/s42255-021-00512-6","volume":"4","author":"OA Cherepanova","year":"2022","unstructured":"Cherepanova, O. A. & Byzova, T. V. Pentose phosphate pathway drives vascular maturation. Nat. Metab. 4, 15\u201316 (2022).","journal-title":"Nat. Metab."},{"key":"1583_CR50","doi-asserted-by":"publisher","first-page":"946","DOI":"10.1093\/carcin\/bgp083","volume":"30","author":"P Vizan","year":"2009","unstructured":"Vizan, P. et al. Characterization of the metabolic changes underlying growth factor angiogenic activation: identification of new potential therapeutic targets. Carcinogenesis 30, 946\u2013952 (2009).","journal-title":"Carcinogenesis"},{"key":"1583_CR51","doi-asserted-by":"publisher","first-page":"677","DOI":"10.1038\/nm0603-677","volume":"9","author":"CW Pugh","year":"2003","unstructured":"Pugh, C. W. & Ratcliffe, P. J. Regulation of angiogenesis by hypoxia: role of the HIF system. Nat. Med. 9, 677\u2013684 (2003).","journal-title":"Nat. Med."},{"key":"1583_CR52","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1016\/j.cmet.2019.08.011","volume":"30","author":"X Li","year":"2019","unstructured":"Li, X., Sun, X. & Carmeliet, P. Hallmarks of endothelial cell metabolism in health and disease. Cell Metab. 30, 414\u2013433 (2019).","journal-title":"Cell Metab."},{"key":"1583_CR53","doi-asserted-by":"publisher","first-page":"44561","DOI":"10.1074\/jbc.M112.407411","volume":"287","author":"O Kabil","year":"2012","unstructured":"Kabil, O. & Banerjee, R. Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism. J. Biol. Chem. 287, 44561\u201344567 (2012).","journal-title":"J. Biol. Chem."},{"key":"1583_CR54","doi-asserted-by":"publisher","first-page":"30901","DOI":"10.1074\/jbc.M114.602664","volume":"289","author":"M Libiad","year":"2014","unstructured":"Libiad, M., Yadav, P. K., Vitvitsky, V., Martinov, M. & Banerjee, R. Organization of the human mitochondrial hydrogen sulfide oxidation pathway. J. Biol. Chem. 289, 30901\u201330910 (2014).","journal-title":"J. Biol. Chem."},{"key":"1583_CR55","doi-asserted-by":"publisher","first-page":"464S","DOI":"10.1042\/bst024464s","volume":"24","author":"S Massari","year":"1996","unstructured":"Massari, S., Bosel, A. & Wrigglesworth, J. M. The variation of Km for oxygen of cytochrome oxidase with turnover under de-energized and energized conditions. Biochem. Soc. Trans. 24, 464S (1996).","journal-title":"Biochem. Soc. Trans."},{"key":"1583_CR56","doi-asserted-by":"publisher","first-page":"858","DOI":"10.1038\/s42255-019-0105-0","volume":"1","author":"T Ast","year":"2019","unstructured":"Ast, T. & Mootha, V. K. Oxygen and mammalian cell culture: are we repeating the experiment of Dr. Ox? Nat. Metab. 1, 858\u2013860 (2019).","journal-title":"Nat. Metab."},{"key":"1583_CR57","doi-asserted-by":"publisher","first-page":"299","DOI":"10.1016\/0005-2728(77)90216-X","volume":"460","author":"LC Petersen","year":"1977","unstructured":"Petersen, L. C. The effect of inhibitors on the oxygen kinetics of cytochrome c oxidase. Biochim. Biophys. Acta 460, 299\u2013307 (1977).","journal-title":"Biochim. Biophys. Acta"},{"key":"1583_CR58","doi-asserted-by":"publisher","first-page":"304","DOI":"10.1016\/j.cmet.2015.06.023","volume":"22","author":"AM Intlekofer","year":"2015","unstructured":"Intlekofer, A. M. et al. Hypoxia induces production of l-2-hydroxyglutarate. Cell Metab. 22, 304\u2013311 (2015).","journal-title":"Cell Metab."},{"key":"1583_CR59","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1016\/j.cmet.2015.06.021","volume":"22","author":"WM Oldham","year":"2015","unstructured":"Oldham, W. M., Clish, C. B., Yang, Y. & Loscalzo, J. Hypoxia-mediated increases in l-2-hydroxyglutarate coordinate the metabolic response to reductive stress. Cell Metab. 22, 291\u2013303 (2015).","journal-title":"Cell Metab."},{"key":"1583_CR60","doi-asserted-by":"publisher","first-page":"1756","DOI":"10.3390\/cancers13081756","volume":"13","author":"RS Berger","year":"2021","unstructured":"Berger, R. S. et al. Lactonization of the oncometabolite d-2-hydroxyglutarate produces a novel endogenous metabolite. Cancers 13, 1756 (2021).","journal-title":"Cancers"},{"key":"1583_CR61","doi-asserted-by":"publisher","unstructured":"Pan, X. et al. A genetically encoded tool to increase cellular NADH\/NAD+ ratio in living cells. Nat. Chem. Biol. https:\/\/doi.org\/10.1038\/s41589-023-01460-w (2023).","DOI":"10.1038\/s41589-023-01460-w"},{"key":"1583_CR62","doi-asserted-by":"publisher","first-page":"1526","DOI":"10.1038\/s42255-023-00854-3","volume":"5","author":"M Ji","year":"2023","unstructured":"Ji, M. et al. Methionine restriction-induced sulfur deficiency impairs antitumour immunity partially through gut microbiota. Nat. Metab. 5, 1526\u20131543 (2023).","journal-title":"Nat. Metab."},{"key":"1583_CR63","doi-asserted-by":"publisher","first-page":"132","DOI":"10.1016\/j.cell.2014.11.048","volume":"160","author":"C Hine","year":"2015","unstructured":"Hine, C. et al. Endogenous hydrogen sulfide production is essential for dietary restriction benefits. Cell 160, 132\u2013144 (2015).","journal-title":"Cell"},{"key":"1583_CR64","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.aaz5752","volume":"6","author":"J Jia","year":"2020","unstructured":"Jia, J. et al. SQR mediates therapeutic effects of H2S by targeting mitochondrial electron transport to induce mitochondrial uncoupling. Sci. Adv. 6, eaaz5752 (2020).","journal-title":"Sci. Adv."},{"key":"1583_CR65","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1038\/nature09002","volume":"465","author":"Y Wang","year":"2010","unstructured":"Wang, Y. et al. Ephrin-B2 controls VEGF-induced angiogenesis and lymphangiogenesis. Nature 465, 483\u2013486 (2010).","journal-title":"Nature"},{"key":"1583_CR66","doi-asserted-by":"publisher","first-page":"13005","DOI":"10.1021\/bi001088w","volume":"39","author":"E Mosharov","year":"2000","unstructured":"Mosharov, E., Cranford, M. R. & Banerjee, R. The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 39, 13005\u201313011 (2000).","journal-title":"Biochemistry"},{"key":"1583_CR67","doi-asserted-by":"publisher","first-page":"35785","DOI":"10.1074\/jbc.M602799200","volume":"281","author":"V Vitvitsky","year":"2006","unstructured":"Vitvitsky, V., Thomas, M., Ghorpade, A., Gendelman, H. E. & Banerjee, R. A functional transsulfuration pathway in the brain links to glutathione homeostasis. J. Biol. Chem. 281, 35785\u201335793 (2006).","journal-title":"J. Biol. Chem."},{"key":"1583_CR68","doi-asserted-by":"publisher","DOI":"10.1038\/s41598-020-67289-8","volume":"10","author":"G Carpentier","year":"2020","unstructured":"Carpentier, G. et al. Angiogenesis analyzer for ImageJ\u2014a comparative morphometric analysis of \u2018endothelial tube formation assay\u2019 and \u2018fibrin bead assay\u2019. Sci. Rep. 10, 11568 (2020).","journal-title":"Sci. Rep."},{"key":"1583_CR69","doi-asserted-by":"publisher","first-page":"10 20 1","DOI":"10.1002\/cpcb.9","volume":"72","author":"AD Doyle","year":"2016","unstructured":"Doyle, A. D. Generation of 3D collagen gels with controlled diverse architectures. Curr. Protoc. Cell Biol. 72, 10 20 1\u201310 20 16 (2016).","journal-title":"Curr. Protoc. Cell Biol."},{"key":"1583_CR70","doi-asserted-by":"publisher","first-page":"376","DOI":"10.1053\/j.gastro.2022.11.014","volume":"164","author":"S Solanki","year":"2023","unstructured":"Solanki, S. et al. Dysregulated amino acid sensing drives colorectal cancer growth and metabolic reprogramming leading to chemoresistance. Gastroenterology 164, 376\u2013391 (2023).","journal-title":"Gastroenterology"},{"key":"1583_CR71","doi-asserted-by":"publisher","first-page":"e73245","DOI":"10.7554\/eLife.73245","volume":"11","author":"SA Kerk","year":"2022","unstructured":"Kerk, S. A. et al. Metabolic requirement for GOT2 in pancreatic cancer depends on environmental context. eLife 11, e73245 (2022).","journal-title":"eLife"},{"key":"1583_CR72","doi-asserted-by":"crossref","unstructured":"Brenes, R. A. et al. Toward a mouse model of hind limb ischemia to test therapeutic angiogenesis. J. Vasc. Surg. 56, 1669\u20131679 (2012).","DOI":"10.1016\/j.jvs.2012.04.067"}],"container-title":["Nature Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41589-024-01583-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41589-024-01583-8","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41589-024-01583-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,9,26]],"date-time":"2024-09-26T13:03:17Z","timestamp":1727355797000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41589-024-01583-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3,20]]},"references-count":72,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2024,10]]}},"alternative-id":["1583"],"URL":"https:\/\/doi.org\/10.1038\/s41589-024-01583-8","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2023.03.14.532677","asserted-by":"object"}]},"ISSN":["1552-4450","1552-4469"],"issn-type":[{"value":"1552-4450","type":"print"},{"value":"1552-4469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,3,20]]},"assertion":[{"value":"13 March 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 February 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 March 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"C.A.L. has received consulting fees from Astellas Pharmaceuticals, Odyssey Therapeutics and T-Knife Therapeutics and is an inventor on patents pertaining to Kras-regulated metabolic pathways, redox control pathways in pancreatic cancer and targeting the GOT1 pathway as a therapeutic approach (US Patent number 2015126580-A1, 5 July 2015; US Patent number 20190136238, 9 May 2019; International Patent number WO2013177426-A2, 23 April 2015). The remaining authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}