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Selective killing of oncogenically transformed cells through a ROS-mediated mechanism by β-phenylethyl isothiocyanate
Open accessAbstract
Reactive oxygen species (ROS) stimulate cell proliferation and induce genetic instability, and their increase in cancer cells is often viewed as an adverse event. Here, we show that such abnormal increases in ROS can be exploited to selectively kill cancer cells using beta-phenylethyl isothiocyanate (PEITC). Oncogenic transformation of ovarian epithelial cells with H-Ras(V12) or expression of Bcr-Abl in hematopoietic cells causes elevated ROS generation and renders the malignant cells highly sensitive to PEITC, which effectively disables the glutathione antioxidant system and causes severe ROS accumulation preferentially in the transformed cells due to their active ROS output. Excessive ROS causes oxidative mitochondrial damage, inactivation of redox-sensitive molecules, and massive cell death. In vivo, PEITC exhibits therapeutic activity and prolongs animal survival.
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“Indeed, this seems to be the case as compounds that raise ROS levels can effectively and selectively kill a variety of tumor cell lines 31, 74, 75.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [75]
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Cites
Bcl-2 functions in an antioxidant pathway to prevent apoptosis
Hockenbery, D. M., Oltvai, Z. N., Yin, X., Milliman, C. L., & Korsmeyer, S. J. (1993) · Cell · doi:10.1016/0092-8674(93)80066-n · Cited by 3,402
NF-κB: linking inflammation and immunity to cancer development and progression
Karin, M., & Greten, F. R. (2005) · Nature reviews. Immunology · doi:10.1038/nri1703 · Cited by 3,175
Production of large amounts of hydrogen peroxide by human tumor cells.
Szatrowski, T. P., & Nathan, C. (1991) · PubMed · Cited by 2,504
ROS stress in cancer cells and therapeutic implications
Pelicano, H., Carney, D. A., & Huang, P. (2004) · Drug Resistance Updates · doi:10.1016/j.drup.2004.01.004 · Cited by 2,031
Crucial role of p53-dependent cellular senescence in suppression of Pten-deficient tumorigenesis
Chen, Z., Trotman, L. C., Shaffer, D., Lin, H.-K., Dotan, Z. A., Niki, M., Koutcher, J. A., Scher, H. I., Ludwig, T., Gerald, W., et al. (2005) · Nature · doi:10.1038/nature03918 · Cited by 1,993
Self-citationMitogenic Signaling Mediated by Oxidants in Ras-Transformed Fibroblasts
Irani, K., Xia, Y., Zweier, J. L., Sollott, S. J., Der, C. J., Fearon, E. R., Sundaresan, M., Finkel, T., & Goldschmidt-Clermont, P. J. (1997) · Science · doi:10.1126/science.275.5306.1649 · Cited by 1,588
Rac1b and reactive oxygen species mediate MMP-3-induced EMT and genomic instability
Radisky, D. C., Levy, D. D., Littlepage, L. E., Liu, H., Nelson, C. M., Fata, J. E., Leake, D., Godden, E. L., Albertson, D. G., Angela Nieto, M., et al. (2005) · Nature · doi:10.1038/nature03688 · Cited by 1,284
Mechanisms of BCR–ABL in the pathogenesis of chronic myelogenous leukaemia
Ren, R. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1567 · Cited by 1,078
c-Myc Can Induce DNA Damage, Increase Reactive Oxygen Species, and Mitigate p53 Function
Vafa, O., Wade, M., Kern, S., Beeche, M., Pandita, T. K., Hampton, G. M., & Wahl, G. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00520-8 · Cited by 876
Superoxide dismutase as a target for the selective killing of cancer cells
Huang, P., Li, F., Oldham, E. A., Keating, M. J., & Plunkett, W. K. (2000) · Nature · doi:10.1038/35030140 · Cited by 846
Research works printed but not linked: 1
- Vereecque, 1999, A new murine aggressive leukemic model, Leuk. Res., 23, 415
Cited by
Sorted by citations
Items 101–200 of 999
Lluis, J. M., Buricchi, F., Chiarugi, P., Morales, A., & Fernández-Checa, J. C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0515 · Cited by 218
ROS-Mediated Cancer Cell Killing through Dietary Phytochemicals
NavaneethaKrishnan, S., Rosales, J. L., & Lee, K. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9051542 · Cited by 224
Chan, D. W., Liu, V. W. S., Tsao, G. S., Yao, K., Furukawa, T., Chan, K. K. L., & Ngan, H. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn167 · Cited by 215
Fucoxanthin induces apoptosis in human leukemia HL-60 cells through a ROS-mediated Bcl-xL pathway
Kim, K., Heo, S., Kang, S., Ahn, G., & Jeon, Y. (2010) · Toxicology in Vitro · doi:10.1016/j.tiv.2010.05.023 · Cited by 213
Iron and Reactive Oxygen Species: Friends or Foes of Cancer Cells?
Bystrom, L. M., Guzman, M. L., & Rivella, S. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5014 · Cited by 212
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 216
Targeting SOD1 reduces experimental non–small-cell lung cancer
Glasauer, A., Sena, L. A., Diebold, L. P., Mazar, A. P., & Chandel, N. S. (2013) · Journal of Clinical Investigation · doi:10.1172/jci71714 · Cited by 215
Glucose deprivation activates a metabolic and signaling amplification loop leading to cell death
Graham, N. A., Tahmasian, M., Kohli, B., Komisopoulou, E., Zhu, M. X., Vivanco, I., Teitell, M. A., Wu, H., Ribas, A., Lo, R. S., et al. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.20 · Cited by 211
Involvement of Cytochrome P450 in Reactive Oxygen Species Formation and Cancer
Hrycay, E. G., & Bandiera, S. M. (2015) · Advances in pharmacology · doi:10.1016/bs.apha.2015.03.003 · Cited by 234
Gain of Nrf2 Function in Non-Small-Cell Lung Cancer Cells Confers Radioresistance
Singh, A., Bodas, M., Wakabayashi, N., Bunz, F., & Biswal, S. S. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3219 · Cited by 217
Larasati, Y. A., Yoneda‐Kato, N., Nakamae, I., Yokoyama, T., Meiyanto, E., & Kato, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-20179-6 · Cited by 216
DNA damage by lipid peroxidation products: Implications in cancer, inflammation and autoimmunity
Gentile, F., Arcaro, A., Pizzimenti, S., Daga, M., Cetrangolo, G. P., Dianzani, C., Lepore, A., Graf, M., Ames, P. R. J., & Barrera, G. (2017) · AIMS Genetics · doi:10.3934/genet.2017.2.103 · Cited by 205
Effective elimination of fludarabine-resistant CLL cells by PEITC through a redox-mediated mechanism
Trachootham, D., Zhang, H., Zhang, W., Feng, L., Du, M., Zhou, Y. N., Chen, Z., Pelicano, H., Plunkett, W. K., Wierda, W. G., et al. (2008) · Blood · doi:10.1182/blood-2008-04-149815 · Cited by 210
Targeted iron oxide nanoparticles for the enhancement of radiation therapy
Hauser, A. K., Mitov, M. I., Daley, E. F., McGarry, R. C., Anderson, K. W., & Hilt, J. Z. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.07.032 · Cited by 202
Oxidation-responsive polymers for biomedical applications
Song, C., Du, F., & Li, Z. (2014) · Journal of Materials Chemistry B · doi:10.1039/c3tb21725f · Cited by 204
Redox Control of Liver Function in Health and Disease
Marí, M., Colell, A., Morales, A., von Montfort, C., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2634 · Cited by 203
Covalent Binding to Tubulin by Isothiocyanates
Mi, L., Xiao, Z., Hood, B. L., Dakshanamurthy, S., Wang, X., Govind, S., Conrads, T. P., Veenstra, T. D., & Chung, F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802330200 · Cited by 200
Targeting Cancer Cell Mitochondria as a Therapeutic Approach
Wen, S., Zhu, D., & Huang, P. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.190 · Cited by 206
Panngom, K., Baik, K. Y., Nam, M., Han, J. H., Rhim, H. C., & Choi, E. H. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.168 · Cited by 199
VDAC1: from structure to cancer therapy
Shoshan‐Barmatz, V., & Mizrachi, D. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00164 · Cited by 200
TIGAR Is Required for Efficient Intestinal Regeneration and Tumorigenesis
Cheung, E. C., Athineos, D., Lee, P., Ridgway, R. A., Lambie, W., Nixon, C., Strathdee, D., Blyth, K., Sansom, O. J., & Vousden, K. H. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.001 · Cited by 193
Epi-drugs to fight cancer: From chemistry to cancer treatment, the road ahead
Mai, A., & Altucci, L. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.020 · Cited by 192
Antioxidants: Friends or foe in prevention or treatment of cancer: The debate of the century
Saeidnia, S., & Abdollahi, M. R. (2013) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2013.05.004 · Cited by 190
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 191
The mitochondrial citrate transporter, CIC, is essential for mitochondrial homeostasis
Catalina-Rodriguez, O., Kolukula, V. K., Tomita, Y. A., Preet, A., Palmieri, F., Wellstein, A., Byers, S. W., Giaccia, A. J., Glasgow, E. F., Albanese, C., et al. (2012) · Oncotarget · doi:10.18632/oncotarget.714 · Cited by 190
Browsing the oldest antioxidant enzyme: catalase and its multiple regulation in cancer
Galasso, M., Gambino, S., Romanelli, M. G., Donadelli, M., & Scupoli, M. T. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.06.010 · Cited by 184
Lin, L., Wang, J., Song, J., Liu, Y., Zhu, G., Dai, Y., Shen, Z., Tian, R., Song, J., Wang, Z., et al. (2019) · Theranostics · doi:10.7150/thno.39831 · Cited by 184
Chou, W.-C., Lei, W.-C., Ko, B., Hou, H.-A., Chen, C.-Y., Tang, J.-L., Yao, M., Tsay, W., Wu, S.-J., Huang, S.-Y., et al. (2010) · Leukemia · doi:10.1038/leu.2010.267 · Cited by 180
Bioactive food components and cancer risk reduction
Stan, S. D., Kar, S., Stoner, G. D., & Singh, S. V. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21623 · Cited by 176
Xiao, D., Powolny, A. A., de Moura, M. B., Kelley, E. E., Bommareddy, A., Kim, S., Hahm, E., Normolle, D. P., Houten, B. V., & Singh, S. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063255 · Cited by 176
Cancer chemoprevention with dietary isothiocyanates mature for clinical translational research
Singh, S. V., & Singh, K. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs216 · Cited by 180
Durantini, A. M., Greene, L. E., Lincoln, R., Martínez, S. R., & Cosa, G. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10288 · Cited by 179
Ma, Y., Ha, C. S., Hwang, S. W., Lee, H. J., Kim, G., Lee, K.-W., & Song, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091947 · Cited by 176
Connections between metabolism and epigenetics in cancers
Thakur, C., & Chen, F. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.006 · Cited by 176
Pro-Oxidant Natural Products as Anticancer Agents
Martı́n-Cordero, C., León‐González, A. J., Calderón‐Montaño, J. M., Burgos‐Morón, E., & López‐Lázaro, M. (2012) · Current Drug Targets · doi:10.2174/138945012802009044 · Cited by 171
BODIPYs in antitumoral and antimicrobial photodynamic therapy: An integrating review
Agazzi, M. L., Ballatore, M. B., Durantini, A. M., Durantini, E. N., & Tomé, A. C. (2019) · Journal of Photochemistry and Photobiology C Photochemistry Reviews · doi:10.1016/j.jphotochemrev.2019.04.001 · Cited by 170
Xiao, D., Powolny, A. A., & Singh, S. V. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802529200 · Cited by 170
Cancer Chemoprevention by Targeting the Epigenome
Huang, P.-H., Plass, C., & Gerhäuser, C. (2011) · Current Drug Targets · doi:10.2174/138945011798184155 · Cited by 168
Sulforaphane inhibits multiple inflammasomes through an Nrf2-independent mechanism
Greaney, A. J., Maier, N. K., Leppla, S. H., & Moayeri, M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3a0415-155rr · Cited by 167
Events associated with apoptotic effect of p-Coumaric acid in HCT-15 colon cancer cells
Jaganathan, S. K. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i43.7726 · Cited by 163
Oliva, C. R., Moellering, D. R., Gillespie, G. Y., & Griguer, C. E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024665 · Cited by 164
Targeting Metabolic–Redox Circuits for Cancer Therapy
Wang, K., Jiang, J., Lei, Y., Zhou, S., Wei, Y., & Huang, C. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.01.001 · Cited by 162
Nair, S., Wenge, L. I., & Kong, A. T. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00549.x · Cited by 163
Wang, Y., Wu, Y., Luo, K., Liu, Y., Zhou, M., Yan, S., Shi, H., & Cai, Y. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.04.013 · Cited by 160
Mitochondria, cholesterol and cancer cell metabolism
Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2016) · Clinical and Translational Medicine · doi:10.1186/s40169-016-0106-5 · Cited by 166
Shukla, S., & Gupta, S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.007 · Cited by 163
Lee, G., Won, H., Lee, Y.-M., Choi, J.-W., Oh, T.-I., Jang, J.-H., Choi, D., Lim, B. O., Kim, Y. J., Park, J., et al. (2016) · Scientific Reports · doi:10.1038/srep18928 · Cited by 166
Switching Akt: from survival signaling to deadly response
Łoś, M., Maddika, S., Erb, B., & Schulze‐Osthoff, K. (2009) · BioEssays · doi:10.1002/bies.200900005 · Cited by 164
Zhao, J. L., Cao, X., Liu, X., Wang, Z., Zhang, C., White, J. C., & Xing, B. (2016) · Nanotoxicology · doi:10.1080/17435390.2016.1206149 · Cited by 158
Widodo, N., Priyandoko, D., Shah, N., Wadhwa, R., & Kaul, S. C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013536 · Cited by 161
Lee, M. (2015) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v6.i3.148 · Cited by 152
Warburg Effect and Redox Balance
Hamanaka, R. B., & Chandel, N. S. (2011) · Science · doi:10.1126/science.1215637 · Cited by 154
Drugging the addict: non‐oncogene addiction as a target for cancer therapy
Nagel, R., Semenova, E. A., & Berns, A. J. M. (2016) · EMBO Reports · doi:10.15252/embr.201643030 · Cited by 161
Zhang, D., Wei, Y., Chen, K., Zhang, X., Xu, X., Shi, Q., Han, S., Chen, X., Gong, H., Li, X., et al. (2014) · Advanced Healthcare Materials · doi:10.1002/adhm.201400299 · Cited by 153
Lu, W., Hu, Y., Chen, G., Chen, Z., Zhang, H., Wang, F., Feng, L., Pelicano, H., Wang, H., Keating, M. J., et al. (2012) · PLoS Biology · doi:10.1371/journal.pbio.1001326 · Cited by 152
Qi, X.-F., Zheng, L., Lee, K.-J., Kim, D.-H., Kim, C.-S., Cai, D.-Q., Wu, Z., Qin, J.-W., Yu, Y., & Sk, K. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.44 · Cited by 151
The Role of STAT-3 in the Induction of Apoptosis in Pancreatic Cancer Cells by Benzyl Isothiocyanate
Sahu, R. P., & Srivastava, S. (2009) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djn470 · Cited by 150
Flaherty, R. L., Owen, M., Fagan-Murphy, A., Intabli, H., Healy, D., Patel, A., Allen, M. C., Patel, B. A., & Flint, M. S. (2017) · Breast Cancer Research · doi:10.1186/s13058-017-0823-8 · Cited by 159
ROS-activated Anticancer Prodrugs: a New Strategy for tumor-specific Damage
Peng, X., & Gandhi, V. V. (2012) · Therapeutic Delivery · doi:10.4155/tde.12.61 · Cited by 148
Mandal, P. K., Schneider, M., Kölle, P., Kuhlencordt, P., Förster, H., Beck, H., Bornkamm, G. W., & Conrad, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-1509 · Cited by 147
Redox Paradox: A Novel Approach to Therapeutics-Resistant Cancer
Chaiswing, L., Clair, W. H. S., & Clair, D. K. S. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7485 · Cited by 149
Won, H. J., Ryplida, B., Kim, S. G., Lee, G., Ryu, J. H., & Park, S. Y. (2020) · ACS Nano · doi:10.1021/acsnano.0c02517 · Cited by 146
Reddy, N. M., Kleeberger, S. R., Bream, J. H., Fallon, P. G., Kensler, T. W., Yamamoto, M. P., & Reddy, S. P. (2008) · Oncogene · doi:10.1038/onc.2008.188 · Cited by 144
Oxidative stress-based cytotoxicity of delphinidin and cyanidin in colon cancer cells
Čvorović, J., Tramer, F., Granzotto, M., Candussio, L., Decorti, G., & Passamonti, S. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.019 · Cited by 139
Nie, X., Xia, L., Wang, H., Chen, G., Wu, B., Zeng, T., Hong, C., Wang, L., & You, Y. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b11291 · Cited by 138
Ju, H.-Q., Gocho, T., Aguilar, M., Wu, M., Zhuang, Z.-N., Fu, J., Yanaga, K., Huang, P., & Chiao, P. J. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0420 · Cited by 137
Biological targets of isothiocyanates
Brown, K., & Hampton, M. B. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.06.004 · Cited by 138
Redox Control of Leukemia: From Molecular Mechanisms to Therapeutic Opportunities
Irwin, M. E., Valle, N. R.-D., & Chandra, J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4258 · Cited by 146
Physiological role of phospholipid hydroperoxide glutathione peroxidase in mammals
Conrad, M., Schneider, M., Seiler, A., & Bornkamm, G. W. (2007) · Biological Chemistry · doi:10.1515/bc.2007.130 · Cited by 136
Rai, P., Young, J. J., Burton, D. G. A., Giribaldi, M. G., Önder, T. T., & Weinberg, R. A. (2010) · Oncogene · doi:10.1038/onc.2010.520 · Cited by 138
Ralph, S. J., Moreno-Sánchez, R., Neuzil, J., & Rodríguez-Enríquez, S. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0566-7 · Cited by 126
Voltage-Dependent Anion Channel 1 As an Emerging Drug Target for Novel Anti-Cancer Therapeutics
Shoshan‐Barmatz, V., Krelin, Y., Shteinfer‐Kuzmine, A., & Arif, T. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00154 · Cited by 135
Chen, W., Zhao, Z., Li, L., Wu, B., Chen, S., Zhou, H., Wang, Y., & Li, Y. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.013 · Cited by 133
Metabolic alterations in cancer cells and therapeutic implications
Hammoudi, N., Ahmed, K. B. R., Garcı́a-Prieto, C., & Huang, P. (2011) · 癌症:英文版 · doi:10.5732/cjc.011.10267 · Cited by 137
Ren, J.-G., Seth, P., Ye, H., Guo, K., Hanai, J., Husain, Z., & Sukhatme, V. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-04626-4 · Cited by 138
Are peroxiredoxins tumor suppressors?
Neumann, C. A., & Fang, Q. (2007) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2007.04.007 · Cited by 133
Hatem, E., Banna, N. E., & Huang, M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7134 · Cited by 127
Dong, L., Freeman, R., Liu, J., Zobalová, R., Marín‐Hernández, Á., Stantic, M., Rohlena, J., Vališ, K., Rodríguez‐Enríquez, S., Butcher, B., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2439 · Cited by 126
Lee, S., Lim, M., Kim, M., Yu, C., Yun, Y., Ahn, J., & Song, J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.038 · Cited by 127
Wu, R. P., Hayashi, T., Cottam, H. B., Jin, G., Yao, S., Wu, C. C. N., Rosenbach, M., Corr, M., Schwab, R. B., & Carson, D. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002890107 · Cited by 126
Qu, Y., Wang, J., Ray, P., Guo, H., Huang, J., Shin-Sim, M., Bukoye, B. A., Liu, B., Lee, A. V., Lin, X., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci43144 · Cited by 128
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 127
Zhu, C., Hu, W., Wu, H., & Hu, X. (2014) · Scientific Reports · doi:10.1038/srep05029 · Cited by 124
Hekmatshoar, Y., Nakhle, J., Galloni, M., & Vignais, M. (2018) · Biochemical Journal · doi:10.1042/bcj20170712 · Cited by 127
Nitric Oxide Induces Cell Death by Regulating Anti-Apoptotic BCL-2 Family Members
Snyder, C. M., Shroff, E. H., Liu, J., & Chandel, N. S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007059 · Cited by 123
Phytoagents for Cancer Management: Regulation of Nucleic Acid Oxidation, ROS, and Related Mechanisms
Lee, W.-L., Huang, J.-Y., & Shyur, L. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/925804 · Cited by 126
Chen, W., Su, H., Xu, Y., Bao, T., & Zheng, X. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.10.024 · Cited by 125
Targeting Thioredoxin Reductase by Parthenolide Contributes to Inducing Apoptosis of HeLa Cells
Duan, D., Zhang, J., Yao, J., Liu, Y., & Fang, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700591 · Cited by 125
Micro-RNA-155 is induced by K-Ras oncogenic signal and promotes ROS stress in pancreatic cancer
Wang, P., Zhu, C.-F., Ma, M.-Z., Chen, G., Song, M., Zeng, Z.-L., Lu, W.-H., Yang, J., Wen, S., Chiao, P. J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4125 · Cited by 126
Ghosh, A. K., Secreto, C. R., Boysen, J. C., Sassoon, T., Shanafelt, T. D., Mukhopadhyay, D., & Kay, N. E. (2010) · Blood · doi:10.1182/blood-2010-09-305649 · Cited by 120
Wu, H., Wang, Y., Ying, M., Jin, C., Li, J., & Hu, X. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00595-3 · Cited by 122
Nrf2-driven TERT regulates pentose phosphate pathway in glioblastoma
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Metadata
- Authors
- Trachootham, D., Zhou, Y., Zhang, H., Demizu, Y., Chen, Z., Pelicano, H., Chiao, P. J., Achanta, G., Arlinghaus, R. B., Liu, J., & Huang, P.
- Affiliations
- Thammasat University (TH)
- The University of Texas MD Anderson Cancer Center (US)
- Corresponding author
- Huang, Peng
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 10
- Issue
- 3
- Pages
- 241-252
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W1993238109
- Cited by
- 1,080
- References
- 43
- Citations by year
- 2026: 13 · 2025: 26 · 2024: 36 · 2023: 40 · 2022: 59 · 2021: 54 · 2020: 50 · 2019: 58 · 2018: 58 · 2017: 68 · 2016: 83 · 2015: 59 · 2014: 83 · 2013: 65 · 2012: 73
- FWCI
- 16.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (CA-16 672)
- National Cancer Institute (CA-16672, CA085563, R01CA109041, CA109041, R01CA085563, R01CA100428, CA100428, P30CA016672)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- reactive oxygen species, selective cytotoxicity, oncogenic transformation, H-Ras V12, BCR-ABL, glutathione antioxidant system, oxidative stress, ovarian epithelial cells, hematopoietic cells, cancer cell death, cancer therapy
- MeSH terms
- Animals, Antioxidants, Cell Line, Cell Transformation, Neoplastic, Glutathione, Humans, Neoplasms, Oncogene Protein p21(ras), Survival Rate, Fusion Proteins, bcr-abl, Cell Death, Reactive Oxygen Species, Isothiocyanates, Xenograft Model Antitumor Assays, Mice
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