Ferroptosis is Involved in the Pharmacological Effect of Ginsenoside

Kiefer, D.; Pantuso, T. Panax ginseng. Am. Fam. Physician, 2003, 68(8), 1539-1542.
[PMID: 14596440]

Arring, N.M.; Millstine, D.; Marks, L.A.; Nail, L.M. Ginseng as a treatment for fatigue: A systematic review. J. Altern. Complement. Med., 2018, 24(7), 624-633.
[http://dx.doi.org/10.1089/acm.2017.0361] [PMID: 29624410]

Dixon, S.J.; Lemberg, K.M.; Lamprecht, M.R.; Skouta, R.; Zaitsev, E.M.; Gleason, C.E.; Patel, D.N.; Bauer, A.J.; Cantley, A.M.; Yang, W.S.; Morrison, B., III; Stockwell, B.R. Ferroptosis: An iron-dependent form of nonapoptotic cell death. Cell, 2012, 149(5), 1060-1072.
[http://dx.doi.org/10.1016/j.cell.2012.03.042] [PMID: 22632970]

Chen, X.; Li, J.; Kang, R.; Klionsky, D.J. Ferroptosis: Machinery and regulation. Autophagy, 2021, 17(9), 2054-2081.

Sever, B.; Altıntop, M.D.; Demir, Y.; Akalın Çiftçi, G.; Beydemir, Ş.; Özdemir, A. Design, synthesis, in vitro and in silico investigation of aldose reductase inhibitory effects of new thiazole-based compounds. Bioorg. Chem., 2020, 102, 104110.
[http://dx.doi.org/10.1016/j.bioorg.2020.104110] [PMID: 32739480]

Demir, Y.; Ceylan, H.; Türkeş, C.; Beydemir, Ş. Molecular docking and inhibition studies of vulpinic, carnosic and usnic acids on polyol pathway enzymes. J. Biomol. Struct. Dyn., 2022, 40(22), 12008-12021.
[http://dx.doi.org/10.1080/07391102.2021.1967195] [PMID: 34424822]

Stockwell, B.R.; Friedmann Angeli, J.P.; Bayir, H.; Bush, A.I.; Conrad, M.; Dixon, S.J.; Fulda, S.; Gascón, S.; Hatzios, S.K.; Kagan, V.E.; Noel, K.; Jiang, X.; Linkermann, A.; Murphy, M.E.; Overholtzer, M.; Oyagi, A.; Pagnussat, G.C.; Park, J.; Ran, Q.; Rosenfeld, C.S.; Salnikow, K.; Tang, D.; Torti, F.M.; Torti, S.V.; Toyokuni, S.; Woerpel, K.A.; Zhang, D.D. Ferroptosis: A regulated cell death nexus linking metabolism, redox biology, and disease. Cell, 2017, 171(2), 273-285.
[http://dx.doi.org/10.1016/j.cell.2017.09.021] [PMID: 28985560]

Mao, H.; Zhao, Y.; Li, H.; Lei, L. Ferroptosis as an emerging target in inflammatory diseases. Prog. Biophys. Mol. Biol., 2020, 155, 20-28.
[http://dx.doi.org/10.1016/j.pbiomolbio.2020.04.001] [PMID: 32311424]

Chen, X.; Kang, R.; Kroemer, G.; Tang, D. Broadening horizons: The role of ferroptosis in cancer. Nat. Rev. Clin. Oncol., 2021, 18(5), 280-296.
[http://dx.doi.org/10.1038/s41571-020-00462-0] [PMID: 33514910]

Li, Y.; Feng, D.; Wang, Z.; Zhao, Y.; Sun, R.; Tian, D.; Liu, D.; Zhang, F.; Ning, S.; Yao, J.; Tian, X. Ischemia-induced ACSL4 activation contributes to ferroptosis-mediated tissue injury in intestinal ischemia/reperfusion. Cell Death Differ., 2019, 26(11), 2284-2299.
[http://dx.doi.org/10.1038/s41418-019-0299-4] [PMID: 30737476]

Do Van, B.; Gouel, F.; Jonneaux, A.; Timmerman, K.; Gelé, P.; Pétrault, M.; Bastide, M.; Laloux, C.; Moreau, C.; Bordet, R.; Devos, D.; Devedjian, J.C. Ferroptosis, a newly characterized form of cell death in Parkinson’s disease that is regulated by PKC. Neurobiol. Dis., 2016, 94, 169-178.
[http://dx.doi.org/10.1016/j.nbd.2016.05.011] [PMID: 27189756]

Abdalkader, M.; Lampinen, R.; Kanninen, K.M.; Malm, T.M.; Liddell, J.R. Targeting Nrf2 to suppress ferroptosis and mitochondrial dysfunction in neurodegeneration. Front. Neurosci., 2018, 12, 466.
[http://dx.doi.org/10.3389/fnins.2018.00466] [PMID: 30042655]

Anderson, L.J.; Westwood, M.A.; Holden, S.; Davis, B.; Prescott, E.; Wonke, B.; Porter, J.B.; Malcolm Walker, J.; Pennell, D.J. Myocardial iron clearance during reversal of siderotic cardiomyopathy with intravenous desferrioxamine: A prospective study using T2* cardiovascular magnetic resonance. Br. J. Haematol., 2004, 127(3), 348-355.
[http://dx.doi.org/10.1111/j.1365-2141.2004.05202.x] [PMID: 15491298]

Dexrazoxane, D.; Database, L. Dexrazoxane, Drugs and Lactation Database; (LactMed®);: Bethesda, (MD), 2006.

Yamaguchi, Y.; Kasukabe, T.; Kumakura, S. Piperlongumine rapidly induces the death of human pancreatic cancer cells mainly through the induction of ferroptosis. Int. J. Oncol., 2018, 52(3), 1011-1022.
[http://dx.doi.org/10.3892/ijo.2018.4259] [PMID: 29393418]

Ayton, S.; Faux, N.G.; Bush, A.I.; Weiner, M.W.; Aisen, P.; Petersen, R.; Jack, C.R.; Jagust, W.; Trojanowki, J.Q.; Toga, A.W.; Beckett, L.; Green, R.C.; Saykin, A.J.; Morris, J.; Shaw, L.M.; Khachaturian, Z.; Sorensen, G.; Kuller, L.; Raichle, M.; Paul, S.; Davies, P.; Fillit, H.; Hefti, F.; Holtzman, D.; Marcel Mesulam, M.; Potter, W.; Snyder, P.; Schwartz, A.; Montine, T.; Thomas, R.G.; Donohue, M.; Walter, S.; Gessert, D.; Sather, T.; Jiminez, G.; Harvey, D.; Bernstein, M.; Fox, N.; Thompson, P.; Schuff, N.; Borowski, B.; Gunter, J.; Senjem, M.; Vemuri, P.; Jones, D.; Kantarci, K.; Ward, C.; Koeppe, R.A.; Foster, N.; Reiman, E.M.; Chen, K.; Mathis, C.; Landau, S.; Cairns, N.J.; Householder, E.; Taylor-Reinwald, L.; Lee, V.; Korecka, M.; Figurski, M.; Crawford, K.; Neu, S.; Foroud, T.M.; Potkin, S.; Shen, L.; Faber, K.; Kim, S.; Nho, K.; Thal, L.; Buckholtz, N.; Albert, M.; Frank, R.; Hsiao, J.; Kaye, J.; Quinn, J.; Lind, B.; Carter, R.; Dolen, S.; Schneider, L.S.; Pawluczyk, S.; Beccera, M.; Teodoro, L.; Spann, B.M.; Brewer, J.; Vanderswag, H.; Fleisher, A.; Heidebrink, J.L.; Lord, J.L.; Mason, S.S.; Albers, C.S.; Knopman, D.; Johnson, K.; Doody, R.S.; Villanueva-Meyer, J.; Chowdhury, M.; Rountree, S.; Dang, M.; Stern, Y.; Honig, L.S.; Bell, K.L.; Ances, B.; Carroll, M.; Leon, S.; Mintun, M.A.; Schneider, S.; Oliver, A.; Marson, D.; Griffith, R.; Clark, D.; Geldmacher, D.; Brockington, J.; Roberson, E.; Grossman, H.; Mitsis, E.; deToledo-Morrell, L.; Shah, R.C.; Duara, R.; Varon, D.; Greig, M.T.; Roberts, P.; Albert, M.; Onyike, C.; D’Agostino, D., II; Kielb, S.; Galvin, J.E.; Cerbone, B.; Michel, C.A.; Rusinek, H.; de Leon, M.J.; Glodzik, L.; De Santi, S.; Murali Doraiswamy, P.; Petrella, J.R.; Wong, T.Z.; Arnold, S.E.; Karlawish, J.H.; Wolk, D.; Smith, C.D.; Jicha, G.; Hardy, P.; Sinha, P.; Oates, E.; Conrad, G.; Lopez, O.L.; Oakley, M.A.; Simpson, D.M.; Porsteinsson, A.P.; Goldstein, B.S.; Martin, K.; Makino, K.M.; Saleem Ismail, M.; Brand, C.; Mulnard, R.A.; Thai, G.; Mc-Adams-Ortiz, C.; Womack, K.; Mathews, D.; Quiceno, M.; Diaz-Arrastia, R.; King, R.; Weiner, M.; Martin-Cook, K.; DeVous, M.; Levey, A.I.; Lah, J.J.; Cellar, J.S.; Burns, J.M.; Anderson, H.S.; Swerdlow, R.H.; Apostolova, L.; Tingus, K.; Woo, E.; Silverman, D.H.S.; Lu, P.H.; Bartzokis, G.; Graff-Radford, N.R.; Parfitt, F.; Kendall, T.; Johnson, H.; Farlow, M.R.; Hake, A.M.; Matthews, B.R.; Herring, S.; Hunt, C.; van Dyck, C.H.; Carson, R.E.; MacAvoy, M.G.; Chertkow, H.; Bergman, H.; Hosein, C.; Black, S.; Stefanovic, B.; Caldwell, C.; Robin Hsiung, G-Y.; Feldman, H.; Mudge, B.; Assaly, M.; Kertesz, A.; Rogers, J.; Bernick, C.; Munic, D.; Kerwin, D.; Mesulam, M-M.; Lipowski, K.; Wu, C-K.; Johnson, N.; Sadowsky, C.; Martinez, W.; Villena, T.; Scott Turner, R.; Johnson, K.; Reynolds, B.; Sperling, R.A.; Johnson, K.A.; Marshall, G.; Frey, M.; Lane, B.; Rosen, A.; Tinklenberg, J.; Sabbagh, M.N.; Belden, C.M.; Jacobson, S.A.; Sirrel, S.A.; Kowall, N.; Killiany, R.; Budson, A.E.; Norbash, A.; Johnson, P.L.; Allard, J.; Lerner, A.; Ogrocki, P.; Hudson, L.; Fletcher, E.; Carmichael, O.; Olichney, J.; DeCarli, C.; Kittur, S.; Borrie, M.; Lee, T-Y.; Bartha, R.; Johnson, S.; Asthana, S.; Carlsson, C.M.; Potkin, S.G.; Preda, A.; Nguyen, D.; Tariot, P.; Reeder, S.; Bates, V.; Capote, H.; Rainka, M.; Scharre, D.W.; Kataki, M.; Adeli, A.; Zimmerman, E.A.; Celmins, D.; Brown, A.D.; Pearlson, G.D.; Blank, K.; Anderson, K.; Santulli, R.B.; Kitzmiller, T.J.; Schwartz, E.S.; Sink, K.M.; Williamson, J.D.; Garg, P.; Watkins, F.; Ott, B.R.; Querfurth, H.; Tremont, G.; Salloway, S.; Malloy, P.; Correia, S.; Rosen, H.J.; Miller, B.L.; Mintzer, J.; Spicer, K.; Bachman, D.; Finger, E.; Pasternak, S.; Rachinsky, I.; Drost, D.; Pomara, N.; Hernando, R.; Sarrael, A.; Schultz, S.K.; Boles Ponto, L.L.; Shim, H.; Elizabeth Smith, K.; Relkin, N.; Chaing, G.; Raudin, L.; Smith, A.; Fargher, K.; Ashok Raj, B.; Neylan, T.; Grafman, J.; Davis, M.; Morrison, R.; Hayes, J.; Finley, S.; Friedl, K.; Fleischman, D.; Arfanakis, K.; James, O.; Massoglia, D.; Jay Fruehling, J.; Harding, S.; Peskind, E.R.; Petrie, E.C.; Li, G.; Yesavage, J.A.; Taylor, J.L.; Furst, A.J. Ferritin levels in the cerebrospinal fluid predict Alzheimer’s disease outcomes and are regulated by APOE. Nat. Commun., 2015, 6(1), 6760.
[http://dx.doi.org/10.1038/ncomms7760] [PMID: 25988319]

Bilgic, B.; Pfefferbaum, A.; Rohlfing, T.; Sullivan, E.V.; Adalsteinsson, E. MRI estimates of brain iron concentration in normal aging using quantitative susceptibility mapping. Neuroimage, 2012, 59(3), 2625-2635.
[http://dx.doi.org/10.1016/j.neuroimage.2011.08.077] [PMID: 21925274]

Devos, D.; Moreau, C.; Devedjian, J.C.; Kluza, J.; Petrault, M.; Laloux, C.; Jonneaux, A.; Ryckewaert, G.; Garçon, G.; Rouaix, N.; Duhamel, A.; Jissendi, P.; Dujardin, K.; Auger, F.; Ravasi, L.; Hopes, L.; Grolez, G.; Firdaus, W.; Sablonnière, B.; Strubi-Vuillaume, I.; Zahr, N.; Destée, A.; Corvol, J.C.; Pöltl, D.; Leist, M.; Rose, C.; Defebvre, L.; Marchetti, P.; Cabantchik, Z.I.; Bordet, R. Targeting chelatable iron as a therapeutic modality in Parkinson’s disease. Antioxid. Redox Signal., 2014, 21(2), 195-210.
[http://dx.doi.org/10.1089/ars.2013.5593] [PMID: 24251381]

Zille, M.; Karuppagounder, S.S.; Chen, Y.; Gough, P.J.; Bertin, J.; Finger, J.; Milner, T.A.; Jonas, E.A.; Ratan, R.R. Neuronal death after hemorrhagic stroke in vitro and in vivo shares features of ferroptosis and necroptosis. Stroke, 2017, 48(4), 1033-1043.
[http://dx.doi.org/10.1161/STROKEAHA.116.015609] [PMID: 28250197]

Hambright, W.S.; Fonseca, R.S.; Chen, L.; Na, R.; Ran, Q. Ablation of ferroptosis regulator glutathione peroxidase 4 in forebrain neurons promotes cognitive impairment and neurodegeneration. Redox Biol., 2017, 12, 8-17.
[http://dx.doi.org/10.1016/j.redox.2017.01.021] [PMID: 28212525]

Coles, L.D.; Tuite, P.J.; Öz, G.; Mishra, U.R.; Kartha, R.V.; Sullivan, K.M.; Cloyd, J.C.; Terpstra, M. Repeated‐dose oral NAcetylcysteine in Parkinson’s Disease: Pharmacokinetics and effect on brain glutathione and oxidative stress. J. Clin. Pharmacol., 2018, 58(2), 158-167.
[http://dx.doi.org/10.1002/jcph.1008] [PMID: 28940353]

Monti, D.A.; Zabrecky, G.; Kremens, D.; Liang, T.W.; Wintering, N.A.; Cai, J.; Wei, X.; Bazzan, A.J.; Zhong, L.; Bowen, B.; Intenzo, C.M.; Iacovitti, L.; Newberg, A.B. N-acetyl cysteine may support dopamine neurons in Parkinson’s Disease: Preliminary clinical and cell line data. PLoS One, 2016, 11(6), e0157602.
[http://dx.doi.org/10.1371/journal.pone.0157602] [PMID: 27309537]

Dolma, S.; Lessnick, S.L.; Hahn, W.C.; Stockwell, B.R. Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells. Cancer Cell, 2003, 3(3), 285-296.
[http://dx.doi.org/10.1016/S1535-6108(03)00050-3] [PMID: 12676586]

Yu, Y.; Xie, Y.; Cao, L.; Yang, L.; Yang, M.; Lotze, M.T.; Zeh, H.J.; Kang, R.; Tang, D. The ferroptosis inducer erastin enhances sensitivity of acute myeloid leukemia cells to chemotherapeutic agents. Mol. Cell. Oncol., 2015, 2(4), e1054549.
[http://dx.doi.org/10.1080/23723556.2015.1054549] [PMID: 27308510]

Gao, M.; Monian, P.; Quadri, N.; Ramasamy, R.; Jiang, X. Glutaminolysis and transferrin regulate ferroptosis. Mol. Cell, 2015, 59(2), 298-308.
[http://dx.doi.org/10.1016/j.molcel.2015.06.011] [PMID: 26166707]

Ma, S.; Henson, E.S.; Chen, Y.; Gibson, S.B. Ferroptosis is induced following siramesine and lapatinib treatment of breast cancer cells. Cell Death Dis., 2016, 7(7), e2307.
[http://dx.doi.org/10.1038/cddis.2016.208] [PMID: 27441659]

Yang, W.S.; Stockwell, B.R. Synthetic lethal screening identifies compounds activating iron-dependent, nonapoptotic cell death in oncogenic-RAS-harboring cancer cells. Chem. Biol., 2008, 15(3), 234-245.
[http://dx.doi.org/10.1016/j.chembiol.2008.02.010] [PMID: 18355723]

Liu, Q.; Barker, S.; Knutson, M.D. Iron and manganese transport in mammalian systems. Biochim. Biophys. Acta Mol. Cell Res., 2021, 1868(1), 118890.
[http://dx.doi.org/10.1016/j.bbamcr.2020.118890] [PMID: 33091506]

Sangkhae, V.; Nemeth, E. Placental iron transport: The mechanism and regulatory circuits. Free Radic. Biol. Med., 2019, 133, 254-261.
[http://dx.doi.org/10.1016/j.freeradbiomed.2018.07.001] [PMID: 29981833]

Song, X.; Zhu, S.; Chen, P.; Hou, W.; Wen, Q.; Liu, J.; Xie, Y.; Liu, J.; Klionsky, D.J.; Kroemer, G.; Lotze, M.T.; Zeh, H.J.; Kang, R.; Tang, D. AMPK-Mediated BECN1 Phosphorylation promotes ferroptosis by directly blocking system Xc– activity. Curr. Biol., 2018, 28(15), 2388-2399.e5.
[http://dx.doi.org/10.1016/j.cub.2018.05.094] [PMID: 30057310]

Imoto, S.; Kono, M.; Suzuki, T.; Shibuya, Y.; Sawamura, T.; Mizokoshi, Y.; Sawada, H.; Ohbuchi, A.; Saigo, K. Haemin-induced cell death in human monocytic cells is consistent with ferroptosis. Transf. Aphere. Sci., 2018, 57(4), 524-531.

Li, X.; Chen, J.; Yuan, S.; Zhuang, X.; Qiao, T. Activation of the P62-Keap1-NRF2 pathway protects against ferroptosis in radiationinduced lung injury. Oxid. Med. Cell. Longev., 2022, 2022, 1-16.
[http://dx.doi.org/10.1155/2022/8973509] [PMID: 35847598]

Sun, X.; Ou, Z.; Chen, R.; Niu, X.; Chen, D.; Kang, R.; Tang, D. Activation of the p62‐Keap1‐NRF2 pathway protects against ferroptosis in hepatocellular carcinoma cells. Hepatology, 2016, 63(1), 173-184.
[http://dx.doi.org/10.1002/hep.28251] [PMID: 26403645]

Alvarez, S.W.; Sviderskiy, V.O.; Terzi, E.M.; Papagiannakopoulos, T.; Moreira, A.L.; Adams, S.; Sabatini, D.M.; Birsoy, K.; Possemato, R. NFS1 undergoes positive selection in lung tumours and protects cells from ferroptosis. Nature, 2017, 551(7682), 639-643.
[http://dx.doi.org/10.1038/nature24637] [PMID: 29168506]

Wang, Y.Q.; Chang, S.Y.; Wu, Q.; Gou, Y.J.; Jia, L.; Cui, Y.M.; Yu, P.; Shi, Z.H.; Wu, W.S.; Gao, G.; Chang, Y.Z. The protective role of mitochondrial ferritin on erastin-induced ferroptosis. Front. Aging Neurosci., 2016, 8, 308.
[http://dx.doi.org/10.3389/fnagi.2016.00308] [PMID: 28066232]

Mumbauer, S.; Pascual, J.; Kolotuev, I.; Hamaratoglu, F. Ferritin heavy chain protects the developing wing from reactive oxygen species and ferroptosis. PLoS Genet., 2019, 15(9), e1008396.
[http://dx.doi.org/10.1371/journal.pgen.1008396] [PMID: 31568497]

Ma, S.; Dielschneider, R.F.; Henson, E.S.; Xiao, W.; Choquette, T.R.; Blankstein, A.R.; Chen, Y.; Gibson, S.B. Ferroptosis and autophagy induced cell death occur independently after siramesine and lapatinib treatment in breast cancer cells. PLoS One, 2017, 12(8), e0182921.
[http://dx.doi.org/10.1371/journal.pone.0182921] [PMID: 28827805]

Li, L.; Hao, Y.; Zhao, Y.; Wang, H.; Zhao, X.; Jiang, Y.; Gao, F. Ferroptosis is associated with oxygen-glucose deprivation/reoxygenation-induced Sertoli cell death. Int. J. Mol. Med., 2018, 41(5), 3051-3062.
[http://dx.doi.org/10.3892/ijmm.2018.3469] [PMID: 29436589]

Shang, Y.; Luo, M.; Yao, F.; Wang, S.; Yuan, Z.; Yang, Y. Ceruloplasmin suppresses ferroptosis by regulating iron homeostasis in hepatocellular carcinoma cells. Cell. Signal., 2020, 72, 109633.
[http://dx.doi.org/10.1016/j.cellsig.2020.109633] [PMID: 32283255]

Yi, J.; Zhu, J.; Wu, J.; Thompson, C.B.; Jiang, X. Oncogenic activation of PI3K-AKT-mTOR signaling suppresses ferroptosis via SREBP-mediated lipogenesis. Proc. Natl. Acad. Sci. USA, 2020, 117(49), 31189-31197.
[http://dx.doi.org/10.1073/pnas.2017152117] [PMID: 33229547]

Tesfay, L.; Paul, B.T.; Konstorum, A.; Deng, Z.; Cox, A.O.; Lee, J.; Furdui, C.M.; Hegde, P.; Torti, F.M.; Torti, S.V. Stearoyl-CoA desaturase 1 protects ovarian cancer cells from ferroptotic cell death. Cancer Res., 2019, 79(20), 5355-5366.
[http://dx.doi.org/10.1158/0008-5472.CAN-19-0369] [PMID: 31270077]

Lee, H.; Zandkarimi, F.; Zhang, Y.; Meena, J.K.; Kim, J.; Zhuang, L.; Tyagi, S.; Ma, L.; Westbrook, T.F.; Steinberg, G.R.; Nakada, D.; Stockwell, B.R.; Gan, B. Energy-stress-mediated AMPK activation inhibits ferroptosis. Nat. Cell Biol., 2020, 22(2), 225-234.
[http://dx.doi.org/10.1038/s41556-020-0461-8] [PMID: 32029897]

Lee, J.Y.; Nam, M.; Son, H.Y.; Hyun, K.; Jang, S.Y.; Kim, J.W.; Kim, M.W.; Jung, Y.; Jang, E.; Yoon, S.J.; Kim, J.; Kim, J.; Seo, J.; Min, J.K.; Oh, K.J.; Han, B.S.; Kim, W.K.; Bae, K.H.; Song, J.; Kim, J.; Huh, Y.M.; Hwang, G.S.; Lee, E.W.; Lee, S.C. Polyunsaturated fatty acid biosynthesis pathway determines ferroptosis sensitivity in gastric cancer. Proc. Natl. Acad. Sci. USA, 2020, 117(51), 32433-32442.
[http://dx.doi.org/10.1073/pnas.2006828117] [PMID: 33288688]

Muri, J.; Thut, H.; Bornkamm, G.W.; Kopf, M. B1 and marginal zone B Cells but not follicular B2 cells require Gpx4 to prevent lipid peroxidation and ferroptosis. Cell Rep., 2019, 29(9), 2731-2744.e4.
[http://dx.doi.org/10.1016/j.celrep.2019.10.070] [PMID: 31775041]

Ma, X.; Xiao, L.; Liu, L.; Ye, L.; Su, P.; Bi, E.; Wang, Q.; Yang, M.; Qian, J.; Yi, Q. CD36-mediated ferroptosis dampens intratumoral CD8+ T cell effector function and impairs their antitumor ability. Cell Metab., 2021, 33(5), 1001-1012.e5.
[http://dx.doi.org/10.1016/j.cmet.2021.02.015] [PMID: 33691090]

Wang, W.; Green, M.; Choi, J.E.; Gijón, M.; Kennedy, P.D.; Johnson, J.K.; Liao, P.; Lang, X.; Kryczek, I.; Sell, A.; Xia, H.; Zhou, J.; Li, G.; Li, J.; Li, W.; Wei, S.; Vatan, L.; Zhang, H.; Szeliga, W.; Gu, W.; Liu, R.; Lawrence, T.S.; Lamb, C.; Tanno, Y.; Cieslik, M.; Stone, E.; Georgiou, G.; Chan, T.A.; Chinnaiyan, A.; Zou, W. CD8+T cells regulate tumour ferroptosis during cancer immunotherapy. Nature, 2019, 569(7755), 270-274.
[http://dx.doi.org/10.1038/s41586-019-1170-y] [PMID: 31043744]

Kagan, V.E.; Mao, G.; Qu, F.; Angeli, J.P.F.; Doll, S.; Croix, C.S.; Dar, H.H.; Liu, B.; Tyurin, V.A.; Ritov, V.B.; Kapralov, A.A.; Amoscato, A.A.; Jiang, J.; Anthonymuthu, T.; Mohammadyani, D.; Yang, Q.; Proneth, B.; Klein-Seetharaman, J.; Watkins, S.; Bahar, I.; Greenberger, J.; Mallampalli, R.K.; Stockwell, B.R.; Tyurina, Y.Y.; Conrad, M.; Bayır, H. Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis. Nat. Chem. Biol., 2017, 13(1), 81-90.
[http://dx.doi.org/10.1038/nchembio.2238] [PMID: 27842066]

Nassar, Z.D.; Mah, C.Y.; Dehairs, J.; Burvenich, I.J.G.; Irani, S.; Centenera, M.M.; Helm, M.; Shrestha, R.K.; Moldovan, M.; Don, A.S.; Holst, J.; Scott, A.M.; Horvath, L.G.; Lynn, D.J.; Selth, L.A.; Hoy, A.J.; Swinnen, J.V.; Butler, L.M. Human DECR1 is an androgen-repressed survival factor that regulates PUFA oxidation to protect prostate tumor cells from ferroptosis. eLife, 2020, 9, e54166.
[http://dx.doi.org/10.7554/eLife.54166] [PMID: 32686647]

Blomme, A.; Ford, C.A.; Mui, E.; Patel, R.; Ntala, C.; Jamieson, L.E.; Planque, M.; McGregor, G.H.; Peixoto, P.; Hervouet, E.; Nixon, C.; Salji, M.; Gaughan, L.; Markert, E.; Repiscak, P.; Sumpton, D.; Blanco, G.R.; Lilla, S.; Kamphorst, J.J.; Graham, D.; Faulds, K.; MacKay, G.M.; Fendt, S.M.; Zanivan, S.; Leung, H.Y. 2,4-dienoyl-CoA reductase regulates lipid homeostasis in treatment-resistant prostate cancer. Nat. Commun., 2020, 11(1), 2508.
[http://dx.doi.org/10.1038/s41467-020-16126-7] [PMID: 32427840]

Chen, P.H.; Wu, J.; Ding, C.K.C.; Lin, C.C.; Pan, S.; Bossa, N.; Xu, Y.; Yang, W.H.; Mathey-Prevot, B.; Chi, J.T. Kinome screen of ferroptosis reveals a novel role of ATM in regulating iron metabolism. Cell Death Differ., 2020, 27(3), 1008-1022.
[http://dx.doi.org/10.1038/s41418-019-0393-7] [PMID: 31320750]

Bao, W.D.; Pang, P.; Zhou, X.T.; Hu, F.; Xiong, W.; Chen, K.; Wang, J.; Wang, F.; Xie, D.; Hu, Y.Z.; Han, Z.T.; Zhang, H.H.; Wang, W.X.; Nelson, P.T.; Chen, J.G.; Lu, Y.; Man, H.Y.; Liu, D.; Zhu, L.Q. Loss of ferroportin induces memory impairment by promoting ferroptosis in Alzheimer’s disease. Cell Death Differ., 2021, 28(5), 1548-1562.
[http://dx.doi.org/10.1038/s41418-020-00685-9] [PMID: 33398092]

Wenzel, S.E.; Tyurina, Y.Y.; Zhao, J.; St Croix, C.M.; Dar, H.H.; Mao, G.; Tyurin, V.A.; Anthonymuthu, T.S.; Kapralov, A.A.; Amoscato, A.A.; Mikulska-Ruminska, K.; Shrivastava, I.H.; Kenny, E.M.; Yang, Q.; Rosenbaum, J.C.; Sparvero, L.J.; Emlet, D.R.; Wen, X.; Minami, Y.; Qu, F.; Watkins, S.C.; Holman, T.R.; VanDemark, A.P.; Kellum, J.A.; Bahar, I.; Bayır, H.; Kagan, V.E. PEBP1 wardens ferroptosis by enabling lipoxygenase generation of lipid death signals. Cell, 2017, 171(3), 628-641.e26.
[http://dx.doi.org/10.1016/j.cell.2017.09.044] [PMID: 29053969]

Yang, W.S.; Kim, K.J.; Gaschler, M.M.; Patel, M.; Shchepinov, M.S.; Stockwell, B.R. Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis. Proc. Natl. Acad. Sci. USA, 2016, 113(34), E4966-E4975.
[http://dx.doi.org/10.1073/pnas.1603244113] [PMID: 27506793]

Ghandi, M.; Huang, F.W.; Jané-Valbuena, J.; Kryukov, G.V.; Lo, C.C.; McDonald, E.R., III; Barretina, J.; Gelfand, E.T.; Bielski, C.M.; Li, H.; Hu, K.; Andreev-Drakhlin, A.Y.; Kim, J.; Hess, J.M.; Haas, B.J.; Aguet, F.; Weir, B.A.; Rothberg, M.V.; Paolella, B.R.; Lawrence, M.S.; Akbani, R.; Lu, Y.; Tiv, H.L.; Gokhale, P.C.; de Weck, A.; Mansour, A.A.; Oh, C.; Shih, J.; Hadi, K.; Rosen, Y.; Bistline, J.; Venkatesan, K.; Reddy, A.; Sonkin, D.; Liu, M.; Lehar, J.; Korn, J.M.; Porter, D.A.; Jones, M.D.; Golji, J.; Caponigro, G.; Taylor, J.E.; Dunning, C.M.; Creech, A.L.; Warren, A.C.; McFarland, J.M.; Zamanighomi, M.; Kauffmann, A.; Stransky, N.; Imielinski, M.; Maruvka, Y.E.; Cherniack, A.D.; Tsherniak, A.; Vazquez, F.; Jaffe, J.D.; Lane, A.A.; Weinstock, D.M.; Johannessen, C.M.; Morrissey, M.P.; Stegmeier, F.; Schlegel, R.; Hahn, W.C.; Getz, G.; Mills, G.B.; Boehm, J.S.; Golub, T.R.; Garraway, L.A.; Sellers, W.R. Next-generation characterization of the cancer cell line encyclopedia. Nature, 2019, 569(7757), 503-508.
[http://dx.doi.org/10.1038/s41586-019-1186-3] [PMID: 31068700]

Zou, Y.; Li, H.; Graham, E.T.; Deik, A.A.; Eaton, J.K.; Wang, W.; Sandoval-Gomez, G.; Clish, C.B.; Doench, J.G.; Schreiber, S.L. Cytochrome P450 oxidoreductase contributes to phospholipid peroxidation in ferroptosis. Nat. Chem. Biol., 2020, 16(3), 302-309.
[http://dx.doi.org/10.1038/s41589-020-0472-6] [PMID: 32080622]

Friedmann Angeli, J.P.; Schneider, M.; Proneth, B.; Tyurina, Y.Y.; Tyurin, V.A.; Hammond, V.J.; Herbach, N.; Aichler, M.; Walch, A.; Eggenhofer, E.; Basavarajappa, D.; Rådmark, O.; Kobayashi, S.; Seibt, T.; Beck, H.; Neff, F.; Esposito, I.; Wanke, R.; Förster, H.; Yefremova, O.; Heinrichmeyer, M.; Bornkamm, G.W.; Geissler, E.K.; Thomas, S.B.; Stockwell, B.R.; O’Donnell, V.B.; Kagan, V.E.; Schick, J.A.; Conrad, M. Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice. Nat. Cell Biol., 2014, 16(12), 1180-1191.
[http://dx.doi.org/10.1038/ncb3064] [PMID: 25402683]

Angeli, J.P.F.; Shah, R.; Pratt, D.A.; Conrad, M. Ferroptosis inhibition: Mechanisms and opportunities. Trends Pharmacol. Sci., 2017, 38(5), 489-498.
[http://dx.doi.org/10.1016/j.tips.2017.02.005] [PMID: 28363764]

Yang, W.S.; SriRamaratnam, R.; Welsch, M.E.; Shimada, K.; Skouta, R.; Viswanathan, V.S.; Cheah, J.H.; Clemons, P.A.; Shamji, A.F.; Clish, C.B.; Brown, L.M.; Girotti, A.W.; Cornish, V.W.; Schreiber, S.L.; Stockwell, B.R. Regulation of ferroptotic cancer cell death by GPX4. Cell, 2014, 156(1-2), 317-331.
[http://dx.doi.org/10.1016/j.cell.2013.12.010] [PMID: 24439385]

Badgley, M.A.; Kremer, D.M.; Maurer, H.C.; DelGiorno, K.E.; Lee, H.J.; Purohit, V.; Sagalovskiy, I.R.; Ma, A.; Kapilian, J.; Firl, C.E.M.; Decker, A.R.; Sastra, S.A.; Palermo, C.F.; Andrade, L.R.; Sajjakulnukit, P.; Zhang, L.; Tolstyka, Z.P.; Hirschhorn, T.; Lamb, C.; Liu, T.; Gu, W.; Seeley, E.S.; Stone, E.; Georgiou, G.; Manor, U.; Iuga, A.; Wahl, G.M.; Stockwell, B.R.; Lyssiotis, C.A.; Olive, K.P. Cysteine depletion induces pancreatic tumor ferroptosis in mice. Science, 2020, 368(6486), 85-89.
[http://dx.doi.org/10.1126/science.aaw9872] [PMID: 32241947]

Wang, L.; Cai, H.; Hu, Y.; Liu, F.; Huang, S.; Zhou, Y.; Yu, J.; Xu, J.; Wu, F. A pharmacological probe identifies cystathionine β-synthase as a new negative regulator for ferroptosis. Cell Death Dis., 2018, 9(10), 1005.
[http://dx.doi.org/10.1038/s41419-018-1063-2] [PMID: 30258181]

Martinez, A.M.; Mirkovic, J.; Stanisz, Z.A.; Patwari, F.S.; Yang, W.S. NSC‐34 motor neuron‐like cells are sensitized to ferroptosis upon differentiation. FEBS Open Bio, 2019, 9(4), 582-593.
[http://dx.doi.org/10.1002/2211-5463.12577] [PMID: 30984534]

Jeschke, J.; O’Hagan, H.M.; Zhang, W.; Vatapalli, R.; Calmon, M.F.; Danilova, L.; Nelkenbrecher, C.; Van Neste, L.; Bijsmans, I.T.G.W.; Van Engeland, M.; Gabrielson, E.; Schuebel, K.E.; Winterpacht, A.; Baylin, S.B.; Herman, J.G.; Ahuja, N. Frequent inactivation of cysteine dioxygenase type 1 contributes to survival of breast cancer cells and resistance to anthracyclines. Clin. Cancer Res., 2013, 19(12), 3201-3211.
[http://dx.doi.org/10.1158/1078-0432.CCR-12-3751] [PMID: 23630167]

Hao, S.; Yu, J.; He, W.; Huang, Q.; Zhao, Y.; Liang, B.; Zhang, S.; Wen, Z.; Dong, S.; Rao, J.; Liao, W.; Shi, M. Cysteine dioxygenase 1 mediates erastin-induced ferroptosis in human gastric cancer cells. Neoplasia, 2017, 19(12), 1022-1032.
[http://dx.doi.org/10.1016/j.neo.2017.10.005] [PMID: 29144989]

Wang, K.; Zhang, Z.; Tsai, H.; Liu, Y.; Gao, J.; Wang, M.; Song, L.; Cao, X.; Xu, Z.; Chen, H.; Gong, A.; Wang, D.; Cheng, F.; Zhu, H. Branched-chain amino acid aminotransferase 2 regulates ferroptotic cell death in cancer cells. Cell Death Differ., 2021, 28(4), 1222-1236.
[http://dx.doi.org/10.1038/s41418-020-00644-4] [PMID: 33097833]

Zeitler, L.; Fiore, A.; Meyer, C.; Russier, M.; Zanella, G.; Suppmann, S.; Gargaro, M.; Sidhu, S.S.; Seshagiri, S.; Ohnmacht, C.; Köcher, T.; Fallarino, F.; Linkermann, A.; Murray, P.J. Anti-ferroptotic mechanism of IL4i1-mediated amino acid metabolism. eLife, 2021, 10, e64806.
[http://dx.doi.org/10.7554/eLife.64806] [PMID: 33646117]

Xie, Y.; Zhu, S.; Song, X.; Sun, X.; Fan, Y.; Liu, J.; Zhong, M.; Yuan, H.; Zhang, L.; Billiar, T.R.; Lotze, M.T.; Zeh, H.J., III; Kang, R.; Kroemer, G.; Tang, D. The tumor suppressor p53 limits ferroptosis by blocking DPP4 activity. Cell Rep., 2017, 20(7), 1692-1704.
[http://dx.doi.org/10.1016/j.celrep.2017.07.055] [PMID: 28813679]

Shimada, K.; Skouta, R.; Kaplan, A.; Yang, W.S.; Hayano, M.; Dixon, S.J.; Brown, L.M.; Valenzuela, C.A.; Wolpaw, A.J.; Stockwell, B.R. Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis. Nat. Chem. Biol., 2016, 12(7), 497-503.
[http://dx.doi.org/10.1038/nchembio.2079] [PMID: 27159577]

Viswanathan, V.S.; Ryan, M.J.; Dhruv, H.D.; Gill, S.; Eichhoff, O.M.; Seashore-Ludlow, B.; Kaffenberger, S.D.; Eaton, J.K.; Shimada, K.; Aguirre, A.J.; Viswanathan, S.R.; Chattopadhyay, S.; Tamayo, P.; Yang, W.S.; Rees, M.G.; Chen, S.; Boskovic, Z.V.; Javaid, S.; Huang, C.; Wu, X.; Tseng, Y.Y.; Roider, E.M.; Gao, D.; Cleary, J.M.; Wolpin, B.M.; Mesirov, J.P.; Haber, D.A.; Engelman, J.A.; Boehm, J.S.; Kotz, J.D.; Hon, C.S.; Chen, Y.; Hahn, W.C.; Levesque, M.P.; Doench, J.G.; Berens, M.E.; Shamji, A.F.; Clemons, P.A.; Stockwell, B.R.; Schreiber, S.L. Dependency of a therapy-resistant state of cancer cells on a lipid peroxidase pathway. Nature, 2017, 547(7664), 453-457.
[http://dx.doi.org/10.1038/nature23007] [PMID: 28678785]

Shimada, K.; Hayano, M.; Pagano, N.C.; Stockwell, B.R. Cell-line selectivity improves the predictive power of pharmacogenomic analyses and helps identify NADPH as biomarker for ferroptosis sensitivity. Cell Chem. Biol., 2016, 23(2), 225-235.
[http://dx.doi.org/10.1016/j.chembiol.2015.11.016] [PMID: 26853626]

Ding, C.K.C.; Rose, J.; Sun, T.; Wu, J.; Chen, P.H.; Lin, C.C.; Yang, W.H.; Chen, K.Y.; Lee, H.; Xu, E.; Tian, S.; Akinwuntan, J.; Zhao, J.; Guan, Z.; Zhou, P.; Chi, J.T. MESH1 is a cytosolic NADPH phosphatase that regulates ferroptosis. Nat. Metab., 2020, 2(3), 270-277.
[http://dx.doi.org/10.1038/s42255-020-0181-1] [PMID: 32462112]

Cardoso, B.R.; Hare, D.J.; Bush, A.I.; Roberts, B.R. Glutathione peroxidase 4: A new player in neurodegeneration? Mol. Psychiatry, 2017, 22(3), 328-335.
[http://dx.doi.org/10.1038/mp.2016.196] [PMID: 27777421]

Christensen, L.P. Ginsenosides chemistry, biosynthesis, analysis, and potential health effects. Adv. Food Nutr. Res., 2009, 55, 1-99.
[PMID: 18772102]

Christensen, L.P.; Jensen, M.; Kidmose, U. Simultaneous determination of ginsenosides and polyacetylenes in American ginseng root (Panax quinquefolium L.) by high-performance liquid chromatography. J. Agric. Food Chem., 2006, 54(24), 8995-9003.
[http://dx.doi.org/10.1021/jf062068p] [PMID: 17117783]

Tawab, M.A.; Bahr, U.; Karas, M.; Wurglics, M.; Schubert-Zsilavecz, M. Degradation of ginsenosides in humans after oral administration. Drug Metab. Dispos., 2003, 31(8), 1065-1071.
[http://dx.doi.org/10.1124/dmd.31.8.1065] [PMID: 12867496]

Shibata, S. Chemistry and cancer preventing activities of ginseng saponins and some related triterpenoid compounds. J. Korean Med. Sci., 2001, 16(Suppl), S28-S37.

Bae, E.A.; Han, M.J.; Kim, E.J.; Kim, D.H. Transformation of ginseng saponins to ginsenoside rh2 by acids and human intestinal bacteria and biological activities of their transformants. Arch. Pharm. Res., 2004, 27(1), 61-67.
[http://dx.doi.org/10.1007/BF02980048] [PMID: 14969341]

Amin, A.; Lotfy, M.; Mahmoud-Ghoneim, D.; Adeghate, E.; Al-Akhras, M.A.; Al-Saadi, M.; Al-Rahmoun, S.; Hameed, R. Pancreas-protective effects of chlorella in STZ-induced diabetic animal model: Insights into the mechanism. J. Diabetes Mellitus, 2011, 1(3), 36-45.
[http://dx.doi.org/10.4236/jdm.2011.13006]

Abdalla, A.; Murali, C.; Amin, A. Safranal inhibits angiogenesis via targeting HIF-1α/VEGF machinery: In vitro and ex vivo insights. Front. Oncol., 2022, 11, 789172.
[http://dx.doi.org/10.3389/fonc.2021.789172] [PMID: 35211395]

Dai, C.; Li, H.; Wang, Y.; Tang, S.; Velkov, T.; Shen, J. Inhibition of oxidative stress and ALOX12 and NF-κB pathways contribute to the protective effect of baicalein on carbon tetrachloride-induced acute liver injury. Antioxidants, 2021, 10(6), 976.
[http://dx.doi.org/10.3390/antiox10060976] [PMID: 34207230]

Li, Y.; Yu, P.; Fu, W.; Wang, S.; Zhao, W.; Ma, Y.; Wu, Y.; Cui, H.; Yu, X.; Fu, L.; Xu, H.; Sui, D. Ginsenoside Rd inhibited ferroptosis to alleviate CCl 4-induced acute liver injury in mice via cGAS/STING pathway. Am. J. Chin. Med., 2023, 51(1), 91-105.
[http://dx.doi.org/10.1142/S0192415X23500064] [PMID: 36437551]

Shan, Y.; Li, J.; Zhu, A.; Kong, W.; Ying, R.; Zhu, W. Ginsenoside Rg3 ameliorates acute pancreatitis by activating the NRF2/HO-1-mediated ferroptosis pathway. Int. J. Mol. Med., 2022, 50(1), 89.
[http://dx.doi.org/10.3892/ijmm.2022.5144] [PMID: 35582998]

Zhao, X.; Wu, J.; Guo, D.; Hu, S.; Chen, X.; Hong, L.; Wang, J.; Ma, J.; Jiang, Y.; Niu, T.; Miao, F.; Li, W.; Wang, B.; Chen, X.; Song, Y. Dynamic ginsenoside-sheltered nanocatalysts for safe ferroptosis-apoptosis combined therapy. Acta Biomater., 2022, 151, 549-560.
[http://dx.doi.org/10.1016/j.actbio.2022.08.026] [PMID: 36007778]

Ye, J.; Lyu, T.J.; Li, L.Y.; Liu, Y.; Zhang, H.; Wang, X.; Xi, X.; Liu, Z.J.; Gao, J.Q. Ginsenoside Re attenuates myocardial ischemia/reperfusion induced ferroptosis via miR-144-3p/SLC7A11. Phytomedicine, 2023, 113, 154681.
[http://dx.doi.org/10.1016/j.phymed.2023.154681] [PMID: 36893674]

Lee, G.H.; Lee, W.J.; Hur, J.; Kim, E.; Lee, H.G.; Seo, H.G. Ginsenoside Re mitigates 6-Hydroxydopamine-induced oxidative stress through upregulation of GPX4. Molecules, 2020, 25(1), 188.
[http://dx.doi.org/10.3390/molecules25010188] [PMID: 31906464]

Guo, J.; Wang, R.; Min, F. Ginsenoside Rg1 ameliorates sepsis-induced acute kidney injury by inhibiting ferroptosis in renal tubular epithelial cells. J. Leukoc. Biol., 2022, 112(5), 1065-1077.
[http://dx.doi.org/10.1002/JLB.1A0422-211R] [PMID: 35774015]

Wu, Y.; Pi, D.; Zhou, S.; Yi, Z.; Dong, Y.; Wang, W.; Ye, H.; Chen, Y.; Zuo, Q.; Ouyang, M. Ginsenoside Rh3 induces pyroptosis and ferroptosis through the Stat3/p53/NRF2 axis in colorectal cancer cells. Acta Biochim. Biophys. Sin., 2023, 55(4), 587-600.
[http://dx.doi.org/10.3724/abbs.2023068] [PMID: 37092860]

Wu, Y.; Pi, D.; Chen, Y.; Zuo, Q.; Zhou, S.; Ouyang, M. Ginsenoside Rh4 inhibits colorectal cancer cell proliferation by inducing ferroptosis via autophagy activation. Evid.-based Complem. Altern. Med.: eCAM, 2022, 2022(2022), 6177553.

Bi, S.; Ma, X.; Wang, Y.; Chi, X.; Zhang, Y.; Xu, W.; Hu, S. Protective effect of ginsenoside Rg1 on oxidative damage induced by hydrogen peroxide in chicken splenic lymphocytes. Oxid. Med. Cell. Longev., 2019, 2019, 1-13.
[http://dx.doi.org/10.1155/2019/8465030] [PMID: 31178974]

Wang, Y.; Liu, Q.; Xu, Y.; Zhang, Y.; Lv, Y.; Tan, Y.; Jiang, N.; Cao, G.; Ma, X.; Wang, J.; Cao, Z.; Yu, B.; Kou, J. Ginsenoside Rg1 protects against oxidative stress-induced neuronal apoptosis through myosin IIA-actin related cytoskeletal reorganization. Int. J. Biol. Sci., 2016, 12(11), 1341-1356.
[http://dx.doi.org/10.7150/ijbs.15992] [PMID: 27877086]

Dong, X.; Zheng, L.; Lu, S.; Yang, Y. Neuroprotective effects of pretreatment of ginsenoside R b1 on severe cerebral ischemiainduced injuries in aged mice: Involvement of anti‐oxidant signaling. Geriatr. Gerontol. Int., 2017, 17(2), 338-345.
[http://dx.doi.org/10.1111/ggi.12699] [PMID: 26712031]

Liu, X.; Gu, X.; Yu, M.; Zi, Y.; Yu, H.; Wang, Y.; Xie, Y.; Xiang, L. Effects of ginsenoside Rb1 on oxidative stress injury in rat spinal cords by regulating the eNOS/Nrf2/HO-1 signaling pathway. Exp. Ther. Med., 2018, 16(2), 1079-1086.
[http://dx.doi.org/10.3892/etm.2018.6286] [PMID: 30116359]

Kim, D.H.; Kim, D.W.; Jung, B.H.; Lee, J.H.; Lee, H.; Hwang, G.S.; Kang, K.S.; Lee, J.W. Ginsenoside Rb2 suppresses the glutamate-mediated oxidative stress and neuronal cell death in HT22 cells. J. Ginseng Res., 2019, 43(2), 326-334.
[http://dx.doi.org/10.1016/j.jgr.2018.12.002] [PMID: 30976171]