Unraveling the Potential Role of Glutathione in Multiple Forms of Cell Death in Cancer Therapy
Open accessAbstract
Glutathione is the principal intracellular antioxidant buffer against oxidative stress and mainly exists in the forms of reduced glutathione (GSH) and oxidized glutathione (GSSG). The processes of glutathione synthesis, transport, utilization, and metabolism are tightly controlled to maintain intracellular glutathione homeostasis and redox balance. As for cancer cells, they exhibit a greater ROS level than normal cells in order to meet the enhanced metabolism and vicious proliferation; meanwhile, they also have to develop an increased antioxidant defense system to cope with the higher oxidant state. Growing numbers of studies have implicated that altering the glutathione antioxidant system is associated with multiple forms of programmed cell death in cancer cells. In this review, we firstly focus on glutathione homeostasis from the perspectives of glutathione synthesis, distribution, transportation, and metabolism. Then, we discuss the function of glutathione in the antioxidant process. Afterwards, we also summarize the recent advance in the understanding of the mechanism by which glutathione plays a key role in multiple forms of programmed cell death, including apoptosis, necroptosis, ferroptosis, and autophagy. Finally, we highlight the glutathione-targeting therapeutic approaches toward cancers. A comprehensive review on the glutathione homeostasis and the role of glutathione depletion in programmed cell death provide insight into the redox-based research concerning cancer therapeutics.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Both GSH levels and the GSH/GSSG ratio are tightly controlled through regulation of synthesis, metabolism, transport, and degradation.
“Being the main intracellular antioxidant buffer, both the levels of GSH and GSH/GSSH ratio are tightly controlled through a fine regulation of their synthesis, metabolism, transport, and degradation [176,177].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [177]
Glutathione exists in two forms, reduced glutathione (GSH) and oxidized glutathione (GSSG), which are interconverted by GPx and glutathione reductase.
“Glutathione can exist in two forms: reduced glutathione (GSH) and oxidized glutathione (GSSG), which are converted into each other by the enzymatic activity of GPx (that links two GSH in one GSSG through the formation of a disulphide bond) and glutathione reductase (that catalyses the reduction of one GSSG into two GSH to the expenses of NADPH) [177].”
From The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence (2022) · cites this paper as [177]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
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., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691 · see citing works
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works
Apoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
Regulation of Ferroptotic Cancer Cell Death by GPX4
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., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713 · see citing works
Meister, A., & Anderson, M. E. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.003431 · Cited by 5,694 · see citing works
Glutathione Metabolism and Its Implications for Health
Wu, G., Lupton, J. R., Turner, N. D., Fang, Y.-Z., & Yang, S. (2004) · The Journal of Nutrition · doi:10.1093/jn/134.3.489 · Cited by 3,842 · see citing works
Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice
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., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3064 · Cited by 3,732 · see citing works
Modulation of oxidative stress as an anticancer strategy
Gorrini, C., Harris, I. S., & Mak, T. W. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4002 · Cited by 3,579 · see citing works
Reactive oxygen species, cellular redox systems, and apoptosis
Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works
Ferroptosis: Death by Lipid Peroxidation
Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088 · see citing works
Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis
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., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2238 · Cited by 3,029 · see citing works
Molecular mechanisms of necroptosis: an ordered cellular explosion
Vandenabeele, P., Galluzzi, L., Vanden Berghe, T., & Kroemer, G. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2970 · Cited by 2,382 · see citing works
Autophagy promotes ferroptosis by degradation of ferritin
Hou, W., Xie, Y., Song, X., Sun, X., Lotze, M. T., Zeh, H. J., Kang, R., & Tang, D. (2016) · Autophagy · doi:10.1080/15548627.2016.1187366 · Cited by 2,332 · see citing works
Oxidative stress and autophagy: The clash between damage and metabolic needs
Filomeni, G., De Zio, D., & Cecconi, F. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2014.150 · Cited by 2,195 · see citing works
Lu, S. C.-L. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.09.008 · Cited by 2,192 · see citing works
Regulation of glutathione synthesis
Lu, S. C.-L. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.05.005 · Cited by 2,131 · see citing works
Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works
Glutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069 · see citing works
ROS signalling in the biology of cancer
Moloney, J. N., & Cotter, T. G. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.05.023 · Cited by 1,983 · see citing works
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968 · see citing works
Ferroptosis is an autophagic cell death process
Gao, M., Monian, P., Pan, Q., Zhang, W., Xiang, J., & Jiang, X. (2016) · Cell Research · doi:10.1038/cr.2016.95 · Cited by 1,899 · see citing works
Yang, W. S., & Stockwell, B. R. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.02.010 · Cited by 1,876 · see citing works
Glutathione and its role in cellular functions
Sies, H. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00177-x · Cited by 1,735 · see citing works
Regulated necrosis: the expanding network of non-apoptotic cell death pathways
Berghe, T. V., Linkermann, A., Jouan-Lanhouet, S., Walczak, H., & Vandenabeele, P. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3737 · Cited by 1,735 · see citing works
Protein misfolding in the endoplasmic reticulum as a conduit to human disease
Wang, M., & Kaufman, R. J. (2016) · Nature · doi:10.1038/nature17041 · Cited by 1,630 · see citing works
Role of GPX4 in ferroptosis and its pharmacological implication
Seibt, T. M., Proneth, B., & Conrad, M. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.014 · Cited by 1,520 · see citing works
Programmed cell death pathways in cancer: a review of apoptosis, autophagy and programmed necrosis
Ouyang, L., Shi, Z., Zhao, S., Wang, F., Zhou, T., Liu, B., & Bao, J. (2012) · Cell Proliferation · doi:10.1111/j.1365-2184.2012.00845.x · Cited by 1,460 · see citing works
Endoplasmic Reticulum Stress and Oxidative Stress in Cell Fate Decision and Human Disease
Cao, S. S., & Kaufman, R. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5851 · Cited by 1,304 · see citing works
Role of Glutathione in Cancer Progression and Chemoresistance
Traverso, N., Ricciarelli, R., Nitti, M., Marengo, B., Furfaro, A. L., Pronzato, M. A., Marinari, U. M., & Domenicotti, C. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/972913 · Cited by 1,208 · see citing works
Ishimoto, T., Nagano, O., Yae, T., Tamada, M., Motohara, T., Oshima, H., Oshima, M., Ikeda, T., Asaba, R., Yagi, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.038 · Cited by 1,192 · see citing works
The development of the concept of ferroptosis
Hirschhorn, T., & Stockwell, B. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.043 · Cited by 1,052 · see citing works
Apoptosis, autophagy, necroptosis, and cancer metastasis
Su, Z., Yang, Z., Xu, Y., Chen, Y., & Yu, Q. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0321-5 · Cited by 1,039 · see citing works
Global survey of cell death mechanisms reveals metabolic regulation of ferroptosis
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. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2079 · Cited by 1,017 · see citing works
Lewerenz, J., Hewett, S. J., Huang, Y. S., Lambros, M. P., Gout, P. W., Kalivas, P. W., Massie, A., Smolders, I. J., Methner, A., Pergande, M., et al. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4391 · Cited by 996 · see citing works
Mitochondrial Glutathione, a Key Survival Antioxidant
Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works
Glutathione: an overview of biosynthesis and modulation
Anderson, M. E. (1998) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(97)00146-4 · Cited by 917 · see citing works
Reactive oxygen species and cancer paradox: To promote or to suppress?
Galadari, S., Rahman, A. U., Pallichankandy, S., & Thayyullathil, F. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.004 · Cited by 895 · see citing works
Mitochondrial Cristae: Where Beauty Meets Functionality
Cogliati, S., Enriquez, J. A., & Scorrano, L. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.01.001 · Cited by 816 · see citing works
Necroptosis as an alternative form of programmed cell death
Christofferson, D. E., & Yuan, J. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.12.003 · Cited by 771 · see citing works
Dowdle, W. E., Nyfeler, B., Nagel, J., Elling, R. A., Liu, S., Triantafellow, E., Menon, S., Wang, Z., Honda, A., Pardee, G., et al. (2014) · Nature Cell Biology · doi:10.1038/ncb3053 · Cited by 759 · see citing works
RSL3 Drives Ferroptosis Through GPX4 Inactivation and ROS Production in Colorectal Cancer
Sui, X., Zhang, R., Liu, S., Duan, T., Zhai, L., Zhang, M., Han, X., Xiang, Y., Huang, X., Lin, H., et al. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01371 · Cited by 703 · see citing works
To Be or Not to Be? How Selective Autophagy and Cell Death Govern Cell Fate
Green, D. R., & Levine, B. (2014) · Cell · doi:10.1016/j.cell.2014.02.049 · Cited by 687 · see citing works
Iron‐dependent cell death of hepatocellular carcinoma cells exposed to sorafenib
Louandre, C., Ezzoukhry, Z., Godin, C., Barbare, J., Mazière, J., Chauffert, B., & Galmiche, A. (2013) · International Journal of Cancer · doi:10.1002/ijc.28159 · Cited by 602 · see citing works
Chaperone-mediated autophagy is involved in the execution of ferroptosis
Wu, Z., Geng, Y., Lu, X., Shi, Y., Wu, G., Zhang, M., Shan, B., Pan, H., & Yuan, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819728116 · Cited by 582 · see citing works
Multi-targeted prevention of cancer by sulforaphane
Clarke, J., Dashwood, R. H., & Ho, E. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.04.018 · Cited by 567 · see citing works
Ferroptosis Inhibition: Mechanisms and Opportunities
Angeli, J. P. F., Shah, R., Pratt, D. A., & Conrad, M. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.02.005 · Cited by 563 · see citing works
Necroptosis: A Specialized Pathway of Programmed Necrosis
Galluzzi, L., & Kroemer, G. (2008) · Cell · doi:10.1016/j.cell.2008.12.004 · Cited by 561 · cited 1× · see citing works
“Necroptosis is an alternative form of programmed cell death with distinct characters in the mitochondria, lysosome, and plasma membrane, exhibiting a translucent cytoplasm, swelling organelles, increased cell volumes, and disruption of the plasma membrane [76, 77].”
BackgroundArmstrong, J. S., Steinauer, K. K., Hornung, B., Irish, J. M., Lecane, P. S., Birrell, G. W., Peehl, D. M., & Knox, S. J. (2002) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400959 · Cited by 507 · see citing works
Du, J., Wang, T., Li, Y., Zhou, Y., Wang, X., Yu, X., Ren, X., An, Y., Wu, Y., Sun, W., et al. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.011 · Cited by 487 · see citing works
Holmgren, A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.7.2275 · Cited by 477 · see citing works
Meyer, A. J., Brach, T., Marty, L., Kreye, S., Rouhier, N., Jacquot, J., & Hell, R. (2007) · The Plant Journal · doi:10.1111/j.1365-313x.2007.03280.x · Cited by 467 · see citing works
Status of the mitochondrial pool of glutathione in the isolated hepatocyte.
Meredith, M. J., & Reed, D. J. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34844-0 · Cited by 446 · see citing works
The role of NCOA4-mediated ferritinophagy in health and disease
Santana-Codina, N., & Mancias, J. D. (2018) · Pharmaceuticals · doi:10.3390/ph11040114 · Cited by 410 · see citing works
The x cystine/glutamate antiporter: A potential target for therapy of cancer and other diseases
Lo, M., Wang, Y., & Gout, P. W. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21366 · Cited by 399 · see citing works
Glutathione – linking cell proliferation to oxidative stress
Díaz‐Vivancos, P., Simone, A. D., Kiddle, G. A., & Foyer, C. H. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.09.023 · Cited by 392 · see citing works
Circu, M. L., & Aw, T. Y. (2008) · Free Radical Research · doi:10.1080/10715760802317663 · Cited by 392 · see citing works
Induction of ferroptotic cell death for overcoming cisplatin resistance of head and neck cancer
Roh, J., Kim, E. H., Jang, H. J., Park, J. Y., & Shin, D. (2016) · Cancer Letters · doi:10.1016/j.canlet.2016.07.035 · Cited by 375 · see citing works
Louandre, C., Marcq, I., Bouhlal, H., Lachaier, E., Godin, C., Saidak, Z., François, C., Chatelain, D., Debuysscher, V., Barbare, J.-C., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2014.11.014 · Cited by 374 · see citing works
Stoyanovsky, D. A., Tyurina, Y. Y., Shrivastava, I. H., Bahar, İ., Tyurin, V. A., Protchenko, O. V., Jadhav, S., Bolevich, S., Kozlov, A. V., Vladimirov, Y. A., et al. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.008 · Cited by 374 · see citing works
Reactive Oxygen Species in Cancer: A Dance with the Devil
Schumacker, P. T. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.01.007 · Cited by 368 · see citing works
Molecular Targets of Dietary Phenethyl Isothiocyanate and Sulforaphane for Cancer Chemoprevention
Cheung, K. L., & Kong, A. T. (2009) · The AAPS Journal · doi:10.1208/s12248-009-9162-8 · Cited by 365 · see citing works
Autophagy: a barrier or an adaptive response to cancer
Ogier‐Denis, É., & Codogno, P. (2003) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(03)00004-0 · Cited by 365 · see citing works
Miess, H., Dankworth, B., Gouw, A. M., Rosenfeldt, M., Schmitz, W., Jiang, M., Saunders, B., Howell, M., Downward, J., Felsher, D. W., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0315-z · Cited by 361 · see citing works
Advanced cancers: eradication in all cases using 3-bromopyruvate therapy to deplete ATP
Ko, Y. H., Smith, B. L., Wang, Y., Pomper, M. G., Rini, D. A., Torbenson, M. S., Hullihen, J. M., & Pedersen, P. L. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.09.047 · Cited by 352 · see citing works
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349 · see citing works
Glutathione in Cancer Cell Death
Ortega, Á., Mena, S., & Estrela, J. M. (2011) · Cancers · doi:10.3390/cancers3011285 · Cited by 315 · see citing works
Rescue of cells from apoptosis by inhibition of active GSH extrusion
Ghibelli, L., Fanelli, C., Rotilio, G., Lafavia, E., Coppola, S., Colussi, C., Civitareale, P., & Ciriolo, M. R. (1998) · The FASEB Journal · doi:10.1096/fasebj.12.6.479 · Cited by 314 · see citing works
Meng-Shian, C., Wang, S., Hsu, C., Yin, P., Yeh, T.-S., Lee, H., & Tseng, L. (2017) · Oncotarget · doi:10.18632/oncotarget.23055 · Cited by 299 · see citing works
Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
Morgan, B., Ezeriņa, D., Amoako, T. N. E., Riemer, J., Seedorf, M., & Dick, T. P. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1142 · Cited by 288 · see citing works
Mitochondrial lipid trafficking
Tatsuta, T., Scharwey, M., & Langer, T. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.07.011 · Cited by 286 · see citing works
Role of Glutathione in the Regulation of Cisplatin Resistance in Cancer Chemotherapy
Chen, H. H. W., & Kuo, M. T. (2010) · Metal-Based Drugs · doi:10.1155/2010/430939 · Cited by 284 · see citing works
Genetically altered mice to evaluate glutathione homeostasis in health and disease
Dalton, T. P., Chen, Y., Schneider, S. N., Nebert, D. W., & Shertzer, H. G. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.06.040 · Cited by 283 · see citing works
Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
Lash, L. H. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.03.001 · Cited by 280 · see citing works
A nuclear glutathione cycle within the cell cycle
Díaz‐Vivancos, P., Wolff, T., Marković, J., Pallardó, F. V., & Foyer, C. H. (2010) · Biochemical Journal · doi:10.1042/bj20100409 · Cited by 277 · see citing works
Li, L., Lee, T. K. M., Meier, P. J., & Ballatori, N. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16184 · Cited by 277 · see citing works
Franco, R., Panayiotidis, M. I., & Cidlowski, J. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703091200 · Cited by 272 · see citing works
Habib, E., Linher‐Melville, K., Lin, H., & Singh, G. (2015) · Redox Biology · doi:10.1016/j.redox.2015.03.003 · Cited by 272 · see citing works
Hanigan, M. H. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-420117-0.00003-7 · Cited by 271 · see citing works
Ballatori, N., Hammond, C. L., Cunningham, J. B., Krance, S. M., & Marchan, R. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.09.008 · Cited by 247 · see citing works
The fate of extracellular glutathione in the rat☆
Hahn, R., Wendel, A., & Flohé, L. (1978) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(78)90037-5 · Cited by 243 · see citing works
Glutamate Cysteine Ligase Catalysis
Chen, Y., Shertzer, H. G., Schneider, S. N., Nebert, D. W., & Dalton, T. P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504604200 · Cited by 234 · see citing works
Lo, M., Ling, V. W. T., Wang, Y. Z., & Gout, P. W. (2008) · British Journal of Cancer · doi:10.1038/sj.bjc.6604485 · Cited by 222 · see citing works
Kumar, A., Tikoo, S., Maity, S., Sengupta, S., Sengupta, S., Kaur, A., & Bachhawat, A. K. (2012) · EMBO Reports · doi:10.1038/embor.2012.156 · Cited by 213 · see citing works
Phenethyl isothiocyanate: A comprehensive review of anti-cancer mechanisms
Gupta, P., Wright, S. E., Kim, S., & Srivastava, S. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.08.003 · Cited by 212 · see citing works
Selective Autophagy in Cancer Development and Therapy
Đikić, I., Johansen, T., & Kirkin, V. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4027 · Cited by 212 · see citing works
Pseudolaric acid B triggers ferroptosis in glioma cells via activation of Nox4 and inhibition of xCT
Wang, Z., Ding, Y., Wang, X., Lu, S., Wang, C., He, C. H., Wang, L., Piao, M., Chi, G., Luo, Y., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.04.021 · Cited by 211 · see citing works
Intracellular glutathione pools are heterogeneously concentrated
Montero, D., Tachibana, C., Winther, J. R., & Appenzeller‐Herzog, C. (2013) · Redox Biology · doi:10.1016/j.redox.2013.10.005 · Cited by 206 · see citing works
Glutathione Is Recruited into the Nucleus in Early Phases of Cell Proliferation
Marković, J., Borrás, C., Ortega, Á., Sastre, J., Viña, J., & Pallardó, F. V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609582200 · Cited by 195 · see citing works
Under the ROS: Thiol network is the principal suspect for autophagy commitment
Filomeni, G., Desideri, E., Cardaci, S., Rotilio, G., & Ciriolo, M. R. (2010) · Autophagy · doi:10.4161/auto.6.7.12754 · Cited by 192 · see citing works
Okuno, S., Sato, H., Kuriyama-Matsumura, K., Tamba, M., Wang, H., Sohda, S., Hamada, H., Yoshikawa, H., Kondo, T., & Bannai, S. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6600786 · Cited by 191 · see citing works
Molecular targets of isothiocyanates in cancer: Recent advances
Gupta, P., Kim, B., Kim, S., & Srivastava, S. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300684 · Cited by 188 · see citing works
Xc− inhibitor sulfasalazine sensitizes colorectal cancer to cisplatin by a GSH-dependent mechanism
Ma, M.-Z., Chen, G., Wang, P., Lu, W.-H., Zhu, C.-F., Song, M., Yang, J., Wen, S., Xu, R., Hu, Y., et al. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.07.031 · Cited by 188 · see citing works
Nagai, H., Matsumaru, K., Feng, G., & Kaplowitz, N. (2002) · Hepatology · doi:10.1053/jhep.2002.33995 · Cited by 186 · see citing works
Díaz‐Vivancos, P., Dong, Y., Ziegler, K., Marković, J., Pallardó, F. V., Pellny, T. K., VERRIER, P. J., & Foyer, C. H. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04371.x · Cited by 186 · see citing works
Autophagy and Ferroptosis—What Is the Connection?
Kang, R., & Tang, D. (2017) · Current Pathobiology Reports · doi:10.1007/s40139-017-0139-5 · Cited by 185 · see citing works
Mitochondrial Glutathione: Regulation and Functions
Calabrese, G., Morgan, B., & Riemer, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7121 · Cited by 182 · see citing works
Kojer, K., Bien, M., Gangel, H., Morgan, B., Dick, T. P., & Riemer, J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.165 · Cited by 179 · see citing works
Sleire, L., Skeie, B. S., Netland, I. A., Førde, H. E., Dodoo, E., Selheim, F., Leiss, L. W., Heggdal, J., Ph, P., Wang, J., et al. (2015) · Oncogene · doi:10.1038/onc.2015.60 · Cited by 177 · see citing works
Xu, X., Chua, C. C., Kong, J., Kostrzewa, R. M., Kumaraguru, U., Hamdy, R. C., & Chua, B. H. L. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04884.x · Cited by 174 · see citing works
Yu, X., & Long, Y. C. (2016) · Scientific Reports · doi:10.1038/srep30033 · Cited by 171 · see citing works
Role of glutathione transport processes in kidney function
Lash, L. H. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.10.004 · Cited by 170 · see citing works
Anderson, M. E., Bridges, R. J., & Meister, A. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91433-3 · Cited by 165 · see citing works
Disruption of xCT inhibits cancer cell metastasis via the caveolin-1/β-catenin pathway
Chen, R.-S., Song, Y.-M., Zhou, Z.-Y., Tong, T., Li, Y., Fu, M., Guo, X.-L., Dong, L.-J., He, X., Qiao, H.-X., et al. (2008) · Oncogene · doi:10.1038/onc.2008.414 · Cited by 164 · see citing works
Xie, X., Zhao, Y. C., Ma, C., Xu, X., Zhang, Y., Wang, C., Jin, J., Shen, X., Gao, J., Li, N., et al. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13184 · Cited by 155 · see citing works
Khan, M. N., Yi, F., Rasul, A., Li, T., Wang, N., Gao, H., Gao, R., & Ma, T. (2012) · IUBMB Life · doi:10.1002/iub.1068 · Cited by 150 · see citing works
Zou, X., Feng, Z., Li, Y., Wang, Y., Wertz, K., Weber, P., Fu, Y., & Liu, J. (2011) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.05.006 · Cited by 148 · see citing works
Self-citationD'Herde, K. G. M. A., & Krysko, D. V. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2261 · Cited by 142 · see citing works
Larraufie, M., Yang, W. S., Jiang, E., Thomas, A. G., Slusher, B. S., & Stockwell, B. R. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.07.018 · Cited by 135 · see citing works
Toyoda, M., Kaira, K., Ohshima, Y., Ishioka, N. S., Shino, M., Sakakura, K., Takayasu, Y., Takahashi, K., Tominaga, H., Oriuchi, N., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.178 · Cited by 133 · see citing works
Targeting aerobic glycolysis: 3-bromopyruvate as a promising anticancer drug
Cardaci, S., Desideri, E., & Ciriolo, M. R. (2012) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-012-9422-7 · Cited by 132 · see citing works
Hatem, E., Banna, N. E., & Huang, M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7134 · Cited by 126 · see citing works
Wang, J., Luo, B., Li, X., Lu, W., Yang, J., Hu, Y., Huang, P., & Wen, S. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.272 · Cited by 126 · see citing works
The Identification and Structural Characterization of C7orf24 as γ-Glutamyl Cyclotransferase
Oakley, A. J., Yamada, T., Liu, D., Coggan, M., Clark, A. G., & Philip G. Board (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803623200 · Cited by 125 · see citing works
Bachhawat, A. K., Thakur, A., Kaur, J., & Zulkifli, M. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.11.018 · Cited by 125 · see citing works
Disruption of xCT inhibits cell growth via the ROS/autophagy pathway in hepatocellular carcinoma
Guo, W., Zhao, Y., Zhang, Z., Tan, N., Zhao, F., Ge, C., Liang, L., Jia, D., Chen, T., Yao, M., et al. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.07.024 · Cited by 122 · see citing works
Sanguinarine-induced apoptosis is associated with an early and severe cellular glutathione depletion
Débiton, E., Madelmont, J., Legault, J., & Barthomeuf, C. (2003) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-003-0609-9 · Cited by 118 · see citing works
Glutathione participates in the modulation of starvation-induced autophagy in carcinoma cells
Desideri, E., Filomeni, G., & Ciriolo, M. R. (2012) · Autophagy · doi:10.4161/auto.22037 · Cited by 116 · see citing works
Chen, Z., Putt, D. A., & Lash, L. H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1527 · Cited by 116 · see citing works
Molecular and functional analysis of SDCT2, a novel rat sodium-dependent dicarboxylate transporter
Chen, X., Tsukaguchi, H., Chen, X., Berger, U. V., & Hediger, M. A. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5392 · Cited by 105 · see citing works
Glutathione Export during Apoptosis Requires Functional Multidrug Resistance-associated Proteins
Hammond, C. L., Marchan, R., Krance, S. M., & Ballatori, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611019200 · Cited by 103 · see citing works
Söderdahl, T., Enoksson, M., Lundberg, M., Holmgren, A., Ottersen, O. P., Orrenius, S., Bolcsfoldi, G., & Cotgreave, I. A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0259fje · Cited by 99 · see citing works
Guha, P., Dey, A., Sen, R., Chatterjee, M., Chattopadhyay, S., & Bandyopadhyay, S. K. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.171983 · Cited by 97 · see citing works
ChaC2, an Enzyme for Slow Turnover of Cytosolic Glutathione
Kaur, A., Gautam, R., Srivastava, R., Chandel, A., Kumar, A., Karthikeyan, S., & Bachhawat, A. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.727479 · Cited by 97 · see citing works
Benlloch, M., Ortega, Á., Ferrer, P., Segarra, R., Obrador, E., Asensi, M. A., Carretero, J., & Estrela, J. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408531200 · Cited by 92 · see citing works
Häberle, D. A., Wahlländer, A., Sies, H., Linke, I. M., & Lachenmaier, C. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)80558-x · Cited by 92 · see citing works
Chen, G., Chen, Z., Hu, Y., & Huang, P. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4170 · Cited by 88 · see citing works
Ironing out cell death mechanisms
Reed, J. C., & Pellecchia, M. (2012) · Cell · doi:10.1016/j.cell.2012.05.009 · Cited by 87 · see citing works
Brechbuhl, H. M., Kachadourian, R., Min, E., Chan, D. C. F., & Day, B. J. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2011.08.004 · Cited by 86 · see citing works
Wada, F., Koga, H., Akiba, J., Niizeki, T., Iwamoto, H., Ikezono, Y., Nakamura, T., Abe, M., Masuda, A., Sakaue, T., et al. (2018) · Cancer Science · doi:10.1111/cas.13728 · Cited by 81 · see citing works
Narang, V. S., Pauletti, G. M., Gout, P. W., Buckley, D. J., & Buckley, A. R. (2007) · Chemotherapy · doi:10.1159/000100812 · Cited by 78 · see citing works
Kumar, S., Kaur, A., Chattopadhyay, B., & Bachhawat, A. K. (2015) · Biochemical Journal · doi:10.1042/bj20141154 · Cited by 74 · see citing works
Pseudolaric Acids from Pseudolarix kaempferi
Zhou, B., Ying, B., Song, G., Chen, Z. X., Han, J., & Yan, Y. (1983) · Planta Medica · doi:10.1055/s-2007-969944 · Cited by 72 · see citing works
Biogenesis of mitochondrial membrane proteins
Becker, T., Gebert, M., Pfanner, N., & van der Laan, M. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.04.002 · Cited by 70 · see citing works
Inoue, M., & Morino, Y. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89735-6 · Cited by 65 · see citing works
Expression of xCT as a predictor of disease recurrence in patients with colorectal cancer.
Sugano, K., Maeda, K., Ohtani, H., Nagahara, H., Shibutani, M., & Hirakawa, K. (2015) · PubMed · Cited by 65 · see citing works
Broccoli-Derived Sulforaphane and Chemoprevention of Prostate Cancer: From Bench to Bedside
Amjad, A. I., Parikh, R. A., Appleman, L. J., Hahm, E., Singh, K., & Singh, S. V. (2015) · Current Pharmacology Reports · doi:10.1007/s40495-015-0034-x · Cited by 65 · see citing works
GSH depletion enhances adenoviral bax-induced apoptosis in lung cancer cells
Honda, T., Coppola, S., Ghibelli, L., Cho, S. H., Kagawa, S., Spurgers, K. B., Brisbay, S. M., Roth, J. A., Meyn, R. E., Fang, B., et al. (2004) · Cancer Gene Therapy · doi:10.1038/sj.cgt.7700684 · Cited by 56 · see citing works
Habermann, K., Grünewald, L. D., van Wijk, S. J. L., & Fulda, S. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.412 · Cited by 56 · see citing works
Briviba, K., Fraser, G. R., Sies, H., & KETTERER, B. (1993) · Biochemical Journal · doi:10.1042/bj2940631 · Cited by 55 · see citing works
Roh, J., Kim, E. H., Jang, H.-J., & Shin, D. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.01.002 · Cited by 54 · see citing works
Seo, G., Kim, S. K., Byun, Y. J., Oh, E., Jeong, S., Chae, G. T., & Lee, S. (2010) · Free Radical Research · doi:10.3109/10715762.2010.535530 · Cited by 52 · see citing works
Glutathione Depletion Induces Spermatogonial Cell Autophagy
Mancilla, H., Maldonado, R., Cereceda, K., Villarroel‐Espíndola, F., de, M. M., Angulo, C., Castro, M. A., Slebe, J. C., Vera, J. C., Lavandero, S., et al. (2015) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25178 · Cited by 51 · see citing works
Intracellular distribution and depletion of glutathione in rabbit renal proximal tubules
Schnellmann, R. G., Gilchrist, S. M., & Mandel, L. J. (1988) · Kidney International · doi:10.1038/ki.1988.169 · Cited by 49 · see citing works
The role of GSH efflux in staurosporine-induced apoptosis in colonic epithelial cells
Circu, M. L., Stringer, S., Rhoads, C. A., Moyer, M. P., & Aw, T. Y. (2008) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.09.011 · Cited by 48 · see citing works
Ehrke, E., Arend, C., & Dringen, R. (2014) · Journal of Neuroscience Research · doi:10.1002/jnr.23474 · Cited by 44 · see citing works
Cellular and subcellular heterogeneity of glutathione metabolism and transport in rat kidney cells
Lash, L. H., Visarius, T. M., Sall, J. M., Qian, W., & Tokarz, J. J. (1998) · Toxicology · doi:10.1016/s0300-483x(98)00093-6 · Cited by 44 · see citing works
Nanotoxicity of cobalt induced by oxidant generation and glutathione depletion in MCF-7 cells
Akhtar, M. J., Ahamed, M., Alhadlaq, H. A., & Alshamsan, A. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.12.012 · Cited by 40 · see citing works
Lash, L. H., & Putt, D. A. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00155-0 · Cited by 35 · see citing works
Huang, S.-H., Hsu, M.-H., Hsu, S.-C., Yang, J.-S., Huang, W.-W., Huang, A.-C., Hsiao, Y.-P., Yu, C.-C., & Chung, J.-G. (2013) · Human & Experimental Toxicology · doi:10.1177/0960327113491508 · Cited by 32 · see citing works
Sayed, S. M. E., Baghdadi, H., Zolaly, M. A., Almaramhy, H. H., Ayat, M., & Donki, J. G. (2017) · Medical Hypotheses · doi:10.1016/j.mehy.2017.01.014 · Cited by 31 · see citing works
Chauhan, A. K., Min, K., & Kwon, T. K. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3052-7 · Cited by 31 · see citing works
Gordillo, G. M., Biswas, A., Khanna, S., Spieldenner, J. M., Pan, X. J., & Sen, C. K. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.688879 · Cited by 30 · see citing works
Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts
Ott, C., König, J., Höhn, A., Jung, T., & Grune, T. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.492 · Cited by 29 · see citing works
Barattin, R., Perrotton, T., Trompier, D., Lorendeau, D., Pietro, A. D., d′Hardemare, A. D. M., & Baubichon-Cortay, H. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.07.031 · Cited by 25 · see citing works
The Function of Thioredoxin and Glutathione in Deoxyribonucleic Acid Synthesis
Holmgren, A. (1977) · Biochemical Society Transactions · doi:10.1042/bst0050611 · Cited by 24 · see citing works
Yun-feng, Z., Zhang, C., & Suo, Y. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.05.003 · Cited by 22 · see citing works
Kim, J., Yim, J.-H., Cho, J., Kim, J. H., Ko, J., Kim, S., Park, S., & Park, J. (2005) · Endocrinology · doi:10.1210/en.2005-0895 · Cited by 22 · see citing works
Dačević, M., Isaković, A., Podolski-Renić, A., Isakovic, A. M., Stanković, T., Milosevic, Z. C., Rakić, L., Ruždijić, S., & Pešić, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054044 · Cited by 21 · see citing works
Morgan, B. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140101 · Cited by 17 · see citing works
Liu, M., Zhao, Y., & Zhang, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118870 · Cited by 16 · see citing works
Shi, S., Hudson, F. N., Botta, D., McGrath, M. B., White, C. C., Neff‐LaFord, H. D., Dabrowski, M. J., Singh, N. P., & Kavanagh, T. J. (2007) · Cytometry Part A · doi:10.1002/cyto.a.20434 · Cited by 14 · see citing works
Savaskan, N. E., Hahnen, E., & Eyüpoglu, I. Y. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21795 · Cited by 11 · see citing works
Hoang, Y. D., Avakian, A. P., & Luderer, U. (2005) · Reproductive Toxicology · doi:10.1016/j.reprotox.2005.07.011 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Mechanisms of Multidrug Resistance in Cancer Chemotherapy
Bukowski, K., Kciuk, M., & Kontek, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093233 · Cited by 1,770 · see citing works
Niu, B., Liao, K., Zhou, Y., Wen, T., Quan, G., Pan, X., & Wu, C. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121110 · Cited by 1,168 · see citing works
Wang, B., Wang, Y., Zhang, J., Hu, C., Jiang, J., Li, Y., & Peng, Z. (2023) · Archives of Toxicology · doi:10.1007/s00204-023-03476-6 · Cited by 897 · see citing works
ROS-triggered endothelial cell death mechanisms: Focus on pyroptosis, parthanatos, and ferroptosis
Zheng, D., Liu, J., Piao, H., Zhu, Z., Wei, R., & Liu, K. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1039241 · Cited by 573 · see citing works
Self-citationCellular Red-Ox system in health and disease: The latest update
Jena, A. B., Samal, R. R., Bhol, N. K., & Duttaroy, A. K. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114606 · Cited by 561 · see citing works
Targeting glutamine metabolism as a therapeutic strategy for cancer
Jin, J., Byun, J., Choi, Y., & Park, K. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-00971-9 · Cited by 574 · see citing works
Agidigbi, T. S., & Kim, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143576 · Cited by 518 · see citing works
ROS induced lipid peroxidation and their role in ferroptosis
Endale, H. T., Tesfaye, W., & Mengstie, T. A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1226044 · Cited by 423 · see citing works
Tan, M., Yin, Y., Ma, X., Zhang, J., Pan, W., Tan, M., Zhao, Y., Yang, T., Jiang, T., & Li, H. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05645-y · Cited by 214 · see citing works
The role of polyphenols in overcoming cancer drug resistance: a comprehensive review
Dana, P. M., Sadoughi, F., Asemi, Z., & Yousefi, B. (2022) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-021-00301-9 · Cited by 186 · see citing works
The molecular mechanisms of ferroptosis and its role in cardiovascular disease
Zhang, Y., Xin, L., Xiang, M., Shang, C., Wang, Y., Wang, Y., Cui, X., & Lu, Y. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112423 · Cited by 174 · see citing works
The Role of Antioxidants in the Interplay between Oxidative Stress and Senescence
Varesi, A., Chirumbolo, S., Campagnoli, L. I. M., Pierella, E., Piccini, G. B., Carrara, A., Ricevuti, G., Scassellati, C., Bonvicini, C., & Pascale, A. (2022) · Antioxidants · doi:10.3390/antiox11071224 · Cited by 145 · see citing works
Ferroptosis in colorectal cancer: Potential mechanisms and effective therapeutic targets
Wang, Y., Zhang, Z., Sun, W., Zhang, J., Xu, Q., Zhou, X., & Mao, L. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113524 · Cited by 141 · see citing works
Tang, H., Li, C., Zhang, Y., Zheng, H., Cheng, Y., Zhu, J., Chen, X., Zhu, Z., Piao, J., & Li, F. (2020) · Theranostics · doi:10.7150/thno.46771 · Cited by 134 · see citing works
Jin, M., Shi, C., Tian, L., Wu, Y., Hu, C., & Huang, G. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110282 · Cited by 127 · see citing works
Cysteine Depletion, a Key Action to Challenge Cancer Cells to Ferroptotic Cell Death
Daher, B., Vučetić, M., & Pouysségur, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00723 · Cited by 117 · see citing works
Glutathione in Protein Redox Modulation through S-Glutathionylation and S-Nitrosylation
Kalinina, E. V., & Novichkova, M. (2021) · Molecules · doi:10.3390/molecules26020435 · Cited by 117 · see citing works
Qin, Q., Yu, N., Gu, Y., Ke, W., Zhang, Q., Liu, X., Wang, K., & Chen, M. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04911-9 · Cited by 108 · see citing works
Bone Regeneration and Oxidative Stress: An Updated Overview
Bădilă, A. E., Rădulescu, D. M., Ilie, A., Niculescu, A.-G., Grumezescu, A. M., & Rădulescu, A. R. (2022) · Antioxidants · doi:10.3390/antiox11020318 · Cited by 107 · see citing works
Targeting Glutamine Addiction in Gliomas
Obara‐Michlewska, M., & Szeliga, M. (2020) · Cancers · doi:10.3390/cancers12020310 · Cited by 105 · see citing works
Lai, J., Luo, L., & Nguyen, D. D. (2020) · Chemical Engineering Journal · doi:10.1016/j.cej.2020.126190 · Cited by 104 · see citing works
The Mechanism of Ferroptosis and Applications in Tumor Treatment
Lin, X., Ping, J., Wen, Y., & Wu, Y. R. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01061 · Cited by 104 · see citing works
Ferroptosis in Acute Central Nervous System Injuries: The Future Direction?
Shen, L., Lin, D., Li, X., Wu, H., Lenahan, C., Pan, Y., Xu, W., Chen, Y., Shao, A., & Zhang, J. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00594 · Cited by 102 · see citing works
Antioxidant Therapies in Traumatic Brain Injury
Pietro, V. D., Yakoub, K. M., Caruso, G., Lazzarino, G., Signoretti, S., Barbey, A. K., Tavazzi, B., Lazzarino, G., Belli, A., & Amorini, A. M. (2020) · Antioxidants · doi:10.3390/antiox9030260 · Cited by 101 · see citing works
Kan, X., Yin, Y., Song, C., Tan, L., Qiu, X., Liao, Y., Liu, W., Meng, S., Sun, Y., & Ding, C. (2021) · iScience · doi:10.1016/j.isci.2021.102837 · Cited by 99 · see citing works
Activatable Probes for Ratiometric Imaging of Endogenous Biomarkers In Vivo
Fu, Q., Yang, X. P., Wang, M., Zhu, K., Wang, Y., & Song, J. (2024) · ACS Nano · doi:10.1021/acsnano.3c10659 · Cited by 97 · see citing works
Dysregulation of glutathione synthesis in liver disease
Lu, S. C.-L. (2020) · Liver Research · doi:10.1016/j.livres.2020.05.003 · Cited by 96 · see citing works
RB/E2F1 as a Master Regulator of Cancer Cell Metabolism in Advanced Disease
Mandigo, A. C., Yuan, W., Xu, K., Gallagher, P., Pang, A., Guan, Y. F., Shafi, A. A., Thangavel, C., Sheehan, B., Bogdan, D., et al. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1114 · Cited by 94 · see citing works
Cellular Compartmentalization, Glutathione Transport and Its Relevance in Some Pathologies
Vázquez-Meza, H., Vilchis-Landeros, M. M., Vázquez-Carrada, M., Uribe-Ramírez, D., & Matuz-Mares, D. (2023) · Antioxidants · doi:10.3390/antiox12040834 · Cited by 94 · see citing works
Chemical Design of Magnetic Nanomaterials for Imaging and Ferroptosis-Based Cancer Therapy
Xu, W., Guan, G., Yue, R., Dong, Z., Lei, L., Kang, H., & Song, G. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00546 · Cited by 98 · see citing works
Xing, N., Du, Q., Guo, S., Xiang, G., Zhang, Y., Meng, X., Li, X., & Wang, S. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01407-z · Cited by 88 · see citing works
Zhu, J., Amili, M. A., & Guo, S. (2024) · Biomedicines · doi:10.3390/biomedicines12020417 · Cited by 90 · see citing works
Mitochondrial dysfunction-targeted nanosystems for precise tumor therapeutics
Ma, Z., Han, H., & Zhao, Y. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121947 · Cited by 85 · see citing works
Anticancer Potential of Flavonoids: An Overview with an Emphasis on Tangeretin
de Luna, F. C. F., Ferreira, W. A. S., Casseb, S. M. M., & de Oliveira, E. H. C. (2023) · Pharmaceuticals · doi:10.3390/ph16091229 · Cited by 92 · see citing works
GSH and Ferroptosis: Side-by-Side Partners in the Fight against Tumors
Jiang, Y., Glandorff, C., & Sun, M. (2024) · Antioxidants · doi:10.3390/antiox13060697 · Cited by 84 · see citing works
Wada, F., Koga, H., Akiba, J., Niizeki, T., Iwamoto, H., Ikezono, Y., Nakamura, T., Abe, M., Masuda, A., Sakaue, T., et al. (2018) · Cancer Science · doi:10.1111/cas.13728 · Cited by 81 · see citing works
Dzah, C. S., Zhang, H., Gobe, V. A. D., Asante-Donyinah, D., & Duan, Y. (2024) · Advances in Redox Research · doi:10.1016/j.arres.2024.100099 · Cited by 81 · see citing works
An Update on Glutathione's Biosynthesis, Metabolism, Functions, and Medicinal Purposes
Gasmi, A., Nasreen, A., Lenchyk, L. V., Lysiuk, R., Peana, M., Shapovalova, N., Piscopo, S., Komisarenko, M. A., Shanaida, M., Smetanina, K., et al. (2023) · Current Medicinal Chemistry · doi:10.2174/0109298673251025230919105818 · Cited by 80 · see citing works
Xu, X., Sun, Q., Ma, Y., Jiang, X., Niu, N., & Chen, L. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.131881 · Cited by 75 · see citing works
Jasek-Gajda, E., Jurkowska, H., Jasińska, M., & LIS, G. J. (2020) · Antioxidants · doi:10.3390/antiox9070633 · Cited by 73 · see citing works
Piktel, E., Ościłowska, I., Suprewicz, Ł., Depciuch, J., Marcińczyk, N., Chabielska, E., Wolak, P., Wollny, T., Janion, M., Parlińska‐Wojtan, M., et al. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s277014 · Cited by 75 · see citing works
Li, Y., Jiang, L., Zou, Y., Song, Z., & Jin, S. (2020) · Applied Surface Science · doi:10.1016/j.apsusc.2020.148381 · Cited by 65 · see citing works
Öztürk, N., Ceylan, H., & Demir, Y. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23798 · Cited by 64 · see citing works
Targeting ferroptosis using Chinese herbal compounds to treat respiratory diseases
Xu, M., Zhang, D., & Yan, J. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155738 · Cited by 65 · see citing works
Yu, X. Q., Huang, Y., Tao, Y., Fan, L., & Zhang, Y. (2023) · Analytica Chimica Acta · doi:10.1016/j.aca.2023.342060 · Cited by 61 · see citing works
Post-translational Modifications of IκBα: The State of the Art
Wang, X., Peng, H., Huang, Y., Kong, W., Cui, Q., Du, J., & Jin, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.574706 · Cited by 60 · see citing works
Roy, N., & Paira, P. (2024) · ACS Omega · doi:10.1021/acsomega.3c08890 · Cited by 60 · see citing works
Gote, V., Sharma, A. D., & Pal, D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031257 · Cited by 56 · see citing works
ROS regulation in gliomas: implications for treatment strategies
Yang, Y.-C., Zhu, Y., Sun, S.-J., Zhao, C.-J., Bai, Y., Wang, J., & Ma, L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1259797 · Cited by 56 · see citing works
Nanoparticle-Based Delivery Strategies for Combating Drug Resistance in Cancer Therapeutics
Park, S., Lu, G., Zheng, Y., Davison, E. K., & Li, Y. (2025) · Cancers · doi:10.3390/cancers17162628 · Cited by 58 · see citing works
Zhang, Y., Li, J., Dong, X., Meng, D., Zhi, X., Yuan, L., & Yao, L. (2020) · OncoTargets and Therapy · doi:10.2147/ott.s250066 · Cited by 53 · see citing works
Targeting the Redox Landscape in Cancer Therapy
Narayanan, D., Ma, S., & Özcelik, D. (2020) · Cancers · doi:10.3390/cancers12071706 · Cited by 54 · see citing works
Glutathione: Lights and Shadows in Cancer Patients
Marini, H. R., Facchini, B. A., Francia, R. D., Freni, J., Puzzolo, D., Montella, L., Facchini, G., Ottaiano, A., Berretta, M., & Minutoli, L. (2023) · Biomedicines · doi:10.3390/biomedicines11082226 · Cited by 52 · see citing works
Xiong, Y., Wang, Z., Wang, Q., Deng, Q., Chen, J., Wei, J., Yang, X., Yang, X., & Li, Z. (2021) · Theranostics · doi:10.7150/thno.67572 · Cited by 52 · see citing works
Fan, L., Ji, X., Lin, G., Liu, K., Chen, S., Ma, G., Xue, W., Zhang, X., & Wang, L. (2021) · Microchemical Journal · doi:10.1016/j.microc.2021.106202 · Cited by 48 · see citing works
Photodynamic Therapy Combined with Ferroptosis Is a Synergistic Antitumor Therapy Strategy
Huang, Y.-P., Li, X., Zhang, Z., Xiong, L., Wang, Y., & Wen, Y. (2023) · Cancers · doi:10.3390/cancers15205043 · Cited by 47 · see citing works
Progress of stimulus responsive nanosystems for targeting treatment of bacterial infectious diseases
Yang, N., Sun, M., Wang, H., Hu, D., Zhang, A., Khan, S., Chen, Z., Chen, D., & Xie, S. (2024) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2024.103078 · Cited by 46 · see citing works
The Impact of Mitochondrial Fission-Stimulated ROS Production on Pro-Apoptotic Chemotherapy
Ježek, J., Cooper, K. F., & Strich, R. (2021) · Biology · doi:10.3390/biology10010033 · Cited by 45 · see citing works
Deng, P., Li, J., Lu, Y., Hao, R., He, M., Li, M., Tan, M., Gao, P., Wang, L., Hong, H., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.167039 · Cited by 44 · see citing works
Glutathione and glutathione disulfide – their biomedical and pharmaceutical applications
Guan, X. (2023) · Medicinal Chemistry Research · doi:10.1007/s00044-023-03116-9 · Cited by 43 · see citing works
New Insights into the Role of Glutathione in the Mechanism of Fever
Wrotek, S., Sobocińska, J., Kozłowski, H. M., Pawlikowska, M., Jędrzejewski, T., & Dzialuk, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041393 · Cited by 43 · see citing works
Nanotherapeutic approaches to target mitochondria in cancer
Mani, S., Swargiary, G., Tyagi, S., Singh, M., Jha, N. K., & Singh, K. K. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119773 · Cited by 42 · see citing works
Aydemir, D., Hashemkhani, M., Acar, H. Y., & Ulusu, N. N. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05522-3 · Cited by 38 · see citing works
Li, Y., He, P., Liu, Y., Qi, M., & Dong, W. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.708093 · Cited by 41 · see citing works
Non-Enzymatic Antioxidants against Alzheimer’s Disease: Prevention, Diagnosis and Therapy
Varesi, A., Campagnoli, L. I. M., Carrara, A., Pola, I., Floris, E., Ricevuti, G., Chirumbolo, S., & Pascale, A. (2023) · Antioxidants · doi:10.3390/antiox12010180 · Cited by 45 · see citing works
Ferroptosis landscape in prostate cancer from molecular and metabolic perspective
Liang, J., Liao, Y., Wang, P., Yang, K., Wang, Y., Wang, K., Zhong, B., Zhou, D., Cao, Q., Li, J., et al. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01430-0 · Cited by 40 · see citing works
Galata, E., Georgakopoulou, E. A., Kassalia, M.-E., Papadopoulou-Fermeli, N., & Pavlatou, E. A. (2019) · Materials · doi:10.3390/ma12162589 · Cited by 40 · see citing works
Roles of Ferroptosis in Cardiovascular Diseases
Guo, Y., Zhang, W., Zhou, X., Zhao, S., Wang, J., Guo, Y., Liao, Y., Lu, H., Liu, J., Cai, Y., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.911564 · Cited by 39 · see citing works
Self-citationEbselen, a multi-target compound: its effects on biological processes and diseases
Lu, Q., Cai, Y., Xiang, C., Wu, T., Zhao, Y. H., Wang, J., Wang, H. H., & Zou, L. (2021) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2021.14 · Cited by 38 · see citing works
Bayoumi, M., Arafa, M. G., Nasr, M., & Sammour, O. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-99756-1 · Cited by 38 · see citing works
Glutathione‑degrading enzymes in the complex landscape of tumors (Review)
Zhang, T., Yao, C., Zhou, X., Liu, S., Li, Q., Zhu, S., Chen, Z., Hu, D., & Shen, W. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5660 · Cited by 36 · see citing works
Ferroptosis Is a Potential Novel Diagnostic and Therapeutic Target for Patients With Cardiomyopathy
Zhai, Z., Zou, P., Liu, F., Xia, Z., & Li, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.649045 · Cited by 36 · see citing works
Feng, S., Wang, J., Mu, X., Gu, G., Wang, Y., Lu, J., Wang, S., & Zhao, Q. (2022) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2022.113095 · Cited by 36 · see citing works
Wang, L.-L., Mai, Y.-Z., Zheng, M., Yan, G., & Jin, J. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.01.003 · Cited by 35 · see citing works
Diceglie, C., Anelli, G. M., Martelli, C., Serati, A., Dico, A. L., Lisso, F., Parisi, F., Novielli, C., Paleari, R., Cetin, I., et al. (2021) · Nutrients · doi:10.3390/nu13041303 · Cited by 36 · see citing works
Role of LncRNAs in regulating cancer amino acid metabolism
Guo, Y., Lv, B., Liu, R., Dai, Z., Zhang, F., Liang, Y., Yu, B., Zeng, D., Lv, X., & Zhang, Z. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01926-8 · Cited by 35 · see citing works
The Role of Glutathione in Selected Viral Diseases
Wróblewska, J., Wróblewski, M., Hołyńska-Iwan, I., Modrzejewska, M., Nuszkiewicz, J., Wróblewska, W., & Woźniak, A. (2023) · Antioxidants · doi:10.3390/antiox12071325 · Cited by 35 · see citing works
S-Denitrosylation: A Crosstalk between Glutathione and Redoxin Systems
Chakraborty, S., Sircar, E., Bhattacharyya, C., Choudhuri, A., Mishra, A., Dutta, S., Bhatta, S., Sachin, K., & Sengupta, R. (2022) · Antioxidants · doi:10.3390/antiox11101921 · Cited by 36 · see citing works
Yan, L., Shi, J. H., & Zhu, J. (2024) · Discover Oncology · doi:10.1007/s12672-024-01163-1 · Cited by 36 · see citing works
Zheng, Q., Wang, D., Lin, R., & Xu, W. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00112 · Cited by 34 · see citing works
Oxidative-Stress-Related Genes in Osteoporosis: A Systematic Review
León‐Reyes, G., Argoty-Pantoja, A. D., Becerra‐Cervera, A., López-Montoya, P., Rivera‐Paredez, B., & Velázquez‐Cruz, R. (2023) · Antioxidants · doi:10.3390/antiox12040915 · Cited by 33 · see citing works
Su, Z., Yao, C., Tipper, J. L., Yang, L., Xu, X., Chen, X., Guo, B. K., He, B., Xu, X., & Zheng, Y. (2023) · ACS Nano · doi:10.1021/acsnano.3c08267 · Cited by 32 · see citing works
Zou, J., Du, K., Li, S., Lu, L., Mei, J., Lin, W., Deng, M., Wei, W., & Guo, R. (2021) · Genes · doi:10.3390/genes12091305 · Cited by 32 · see citing works
Wu, Y., Wang, D., Lou, Y., Liu, X., Huang, P., Jin, M., & Huang, G. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.112927 · Cited by 32 · see citing works
Wang, L.-L., Zhang, Y., Zheng, M., Wang, X., Wu, X. Z., & Jin, J. (2023) · Chemical Engineering Journal · doi:10.1016/j.cej.2023.143104 · Cited by 32 · see citing works
Revisiting the scavenging activity of glutathione: Free radicals diversity and reaction mechanisms
Luque-Ceballos, J. C., Rodríguez‐Zamora, P., López-Olivos, J. C., & Garzón, I. L. (2023) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2023.114227 · Cited by 31 · see citing works
Devóz, P. P., dos Reis, M. B., Gomes, W. R., Maraslis, F. T., Ribeiro, D. L., Antunes, L. M. G., Batista, B. L., Grotto, D., Reis, R. M., Barbosa, F., et al. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.128758 · Cited by 31 · see citing works
Nanozyme-based cancer theranostics: A scientometric analysis and comprehensive review
Yang, X., Yasinjan, F., Sun, S., Yang, J., Du, Y., Zhang, H., Liang, Y., Geng, H., Wang, Y., Sun, J., et al. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102386 · Cited by 30 · see citing works
GCLC desuccinylation regulated by oxidative stress protects human cancer cells from ferroptosis
Chen, Z., Niu, K., Li, M., Deng, Y., Zhang, J., Wei, D., Wang, J., & Zhao, Y. (2025) · Cell Death and Differentiation · doi:10.1038/s41418-025-01505-8 · Cited by 32 · see citing works
Musaogullari, A., Mandato, A., & Chai, Y.-C. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00998 · Cited by 30 · see citing works
Orlicka-Płocka, M., Fedoruk‐Wyszomirska, A., Gurda, D., Pawelczak, P., Krawczyk, P., Giel-Pietraszuk, M., Framski, G., Ostrowski, T., & Wyszko, E. (2021) · Antioxidants · doi:10.3390/antiox10060950 · Cited by 30 · see citing works
Glutaminolysis dynamics during astrocytoma progression correlates with tumor aggressiveness
Franco, Y. E. M., Alves, M. J. F., Uno, M., Moretti, I. F., Trombetta-Lima, M., Santos, S. D. S., dos Santos, A. F., Arini, G. S., Baptista, M. S., Lerário, A. M., et al. (2021) · Cancer & Metabolism · doi:10.1186/s40170-021-00255-8 · Cited by 27 · see citing works
Chen, T., Chen, J., Zeng, T., Huang, Q., Chen, D., Chen, H., Chen, J., Zheng, B., Wang, M., Chen, S., et al. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.216044 · Cited by 28 · see citing works
Wang, L.-L., Xu, Q., Xie, Y., Zhang, Y., Zheng, M., Li, X.-F., & Jin, J. (2023) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2023.134872 · Cited by 27 · see citing works
Chen, T., Ding, L., Zhao, M., Song, S., Hou, J., Li, X., Li, M., Yin, K., Li, X., & Wang, Z. (2024) · Chinese Medicine · doi:10.1186/s13020-024-00918-w · Cited by 26 · see citing works
Sulfur-Containing Compounds from Plants
Castro, V., Carpena, M., Fraga‐Corral, M., Lopez-Soria, A., García-Pérez, P., Barral-Martinez, M., Pérez-Gregório, R., Cao, H., Simal‐Gándara, J., & Prieto, M. A. (2023) · Springer eBooks · doi:10.1007/978-3-031-18587-8_11 · Cited by 25 · see citing works
Yang, Y., Huangfu, L., Li, H., & Yang, D. (2023) · International Journal of Hyperthermia · doi:10.1080/02656736.2023.2270654 · Cited by 23 · see citing works
Du, K., Gao, X., Feng, Y., Li, J., Wang, H., Lv, S.-L., Wang, P.-Y., Zhang, B., & Qin, X. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112734 · Cited by 25 · see citing works
Fan, Y., Yang, C., Zhou, J., Cheng, X., Dong, Y., Wang, Q., & Wang, Z. (2020) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2020.1850762 · Cited by 25 · see citing works
Mosaddeghi, P., Eslami, M., Farahmandnejad, M., Akhavein, M., Ranjbarfarrokhi, R., Khorraminejad‐Shirazi, M., Shahabinezhad, F., Taghipour, M. J., Dorvash, M., Sakhteman, A., et al. (2021) · Scientific Reports · doi:10.1038/s41598-020-79472-y · Cited by 25 · see citing works
- Authors
- Lv, H., Zhen, C., Liu, J., Yang, P., Hu, L., & Shang, P.
- Affiliations
- Northwestern Polytechnical University (CN)
- Zhejiang Heye Health Technology Co. Ltd., Anji, Zhejiang 313300, China
- Corresponding author
- Shang, Peng
- Venue
- Oxidative Medicine and Cellular Longevity
- Publisher
- Wiley
- Published
- 2019-06-10
- Volume
- 2019
- Pages
- 1-16
- ISSN
- 1942-0994 (ISSN-L)
- 1942-0900
- PMC
- PMC6590529
- OpenAlex
- W2949432489
- Cited by
- 320
- References
- 164
- Citations by year
- 2026: 15 · 2025: 34 · 2024: 78 · 2023: 64 · 2022: 43 · 2021: 46 · 2020: 35 · 2019: 4 · 2018: 1
- FWCI
- 3.50
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Oxidative Medicine and Cellular Longevity (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Northwestern Polytechnical University Foundation for Fundamental Research (3102018JGC012, 3102017OQD111, 51777171, 11872316, 81803032)
- Fundamental Research Funds for the Central Universities (3102018JGC012, 3102017OQD111, 51777171, 11872316, 81803032)
- National Natural Science Foundation of China (3102018JGC012, 3102017OQD111, 51777171, 11872316, 81803032)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- glutathione, glutathione homeostasis, redox homeostasis, oxidative stress, cancer cells, programmed cell death, apoptosis, necroptosis, ferroptosis, autophagy, glutathione depletion, glutathione metabolism
- MeSH terms
- Glutathione, Humans, Neoplasms, Cell Death
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
