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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
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Items 801–900 of 999
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Amaegberi, N. V., Семенкова, Г. Н., Kvacheva, Z. B., Lisouskaya, A., Пинчук, С. В., & Шадыро, О. И. (2019) · Cell Biochemistry and Function · doi:10.1002/cbf.3400 · Cited by 13
Ye, D.-J., Kwon, Y., Baek, H., Cho, E.-A., Kwon, T.-U., & Chun, Y. (2019) · Journal of Toxicology and Environmental Health · doi:10.1080/15287394.2019.1635934 · Cited by 13
Kim, H. J., Min, K. H., Lee, H. J., Hwang, Y., & Lee, S. C. (2019) · Journal of Industrial and Engineering Chemistry · doi:10.1016/j.jiec.2019.07.004 · Cited by 12
Ock, J., Lee, H., Ismail, I. A., Lee, H., Kwon, B., Suk, K., Lee, W., & Hong, S. (2010) · Cancer Science · doi:10.1111/j.1349-7006.2010.01781.x · Cited by 13
Flavins and Flavoproteins: Applications in Medicine
Jortzik, E., Wang, L., Ma, J., & Becker, K. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0452-5_7 · Cited by 13
Sita, G., Graziosi, A., Hrelia, P., & Morroni, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011201 · Cited by 13
Iron-silicate-coated porous silicon nanoparticles for in situ ROS self-generation
Um, H., Kang, R. H., & Kim, D. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113273 · Cited by 12
Kaur, C., Sahu, S. K., Bansal, K., DeLiberto, L. K., Zhang, J., Tewari, D., & Bishayee, A. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0442 · Cited by 12
Targeting Lysosomal Thiols for Immunogenic Cancer Cell Death
Arkhypov, A., Klemt, I., Bila, G., Attia, D., Chernii, S. V., Bilyy, R. O., & Mokhir, A. A. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202417509 · Cited by 13
Vickridge, E., Faraco, C. C. F., Samavarchi‐Tehrani, P., Ramdzan, Z. M., Djerir, B., Rahimian, H., Leduy, L., Maréchal, A., Gingras, A., & Nepveu, A. (2022) · NAR Cancer · doi:10.1093/narcan/zcac028 · Cited by 12
Dietary Anthocyanins: Impact on Colorectal Cancer and Mechanisms of Action
Tramer, F., Može, Š., Ayokunle, O., Passamonti, S., & Čvorović, J. (2012) · InTech eBooks · doi:10.5772/27678 · Cited by 12
Reactive oxygen species and cancer
Kong, H., & Chandel, N. S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-818606-0.00030-4 · Cited by 12
Chatterjee, S., Chakraborty, P., Banerjee, K., Sinha, A., Adhikary, A., Das, T., & Choudhuri, S. K. (2013) · BioMetals · doi:10.1007/s10534-013-9637-z · Cited by 12
Transformation, translation and TRAIL: An unexpected intersection
White‐Gilbertson, S. J., Rubinchik, S., & Voelkel‐Johnson, C. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.01.007 · Cited by 12
The Molecular Role of HIF1α Is Elucidated in Chronic Myeloid Leukemia
Singh, V. K., Singh, R., Kushwaha, R., Verma, S. P., Tripathi, A. K., & Mahdi, A. A. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.912942 · Cited by 11
Targeted tumor killing by pomegranate polyphenols: Pro-oxidant role of a classical antioxidant
Mukherjee, S., Gupta, P., Ghosh, S., Choudhury, S., Das, A., Ahir, M., Adhikary, A., & Chattopadhyay, S. (2023) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2023.109283 · Cited by 11
Jara‐Gutiérrez, C., Mercado, L. A., Paz-Araos, M., Howard, C. B., Párraga, M., Escobar, C. D. L. B., Mellado, M., Madrid, A., Montenegro, I., Santana, P., et al. (2024) · BMC Complementary Medicine and Therapies · doi:10.1186/s12906-024-04341-4 · Cited by 11
Cao, S., Li, H., Ye, X., Xing, X., Xie, Y., Zeng, X., Liu, H., Zhong, X., Yang, X., Xing, W., et al. (2024) · European journal of medical research · doi:10.1186/s40001-024-02187-7 · Cited by 11
Glucosinolates and Their Hydrolytic Derivatives: Promising Phytochemicals With Anticancer Potential
Joković, N. M., Pešić, S., Vitorović, J., Bogdanović, A., Sharifi‐Rad, J., & Călina, D. C. (2024) · Phytotherapy Research · doi:10.1002/ptr.8419 · Cited by 11
Yamaguchi, H., Yu, T., Kidachi, Y., Akitaya, T., Yoshida, K., Kamiie, K., Noshita, T., Umetsu, H., & Ryoyama, K. (2011) · Biochimie · doi:10.1016/j.biochi.2011.04.011 · Cited by 11
Induction of apoptosis and suppression of Ras gene expression in MCF human breast cancer cells
Saremy, S., Kolahi, M., Tabandeh, M. R., & Hashemitabar, M. (2021) · Journal of Cancer Research and Therapeutics · doi:10.4103/jcrt.jcrt_624_20 · Cited by 11
Yuan, Z., Yang, Z., Li, W., Wu, A., Su, Z., Jiang, B., & Ganesan, S. (2022) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23138 · Cited by 12
Balakrishnan, V., Sindhu, G., Vinothkumar, V., Ramachandhiran, D., Jawaharlal, S., & Vennila, L. (2022) · Journal of Food Biochemistry · doi:10.1111/jfbc.14465 · Cited by 11
Hasan, A., Khamjan, N. A., Lohani, M., & Mir, S. S. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04424-x · Cited by 11
Silencing thioredoxin induces liver cancer cell senescence under hypoxia
Zhang, T., Liu, H., Zhu, C., Briggs, K. L., Kang, Y., Fleming, J. A., & Curley, S. A. (2012) · Hepatology Research · doi:10.1111/j.1872-034x.2012.00973.x · Cited by 11
Key Roles of Reactive Oxygen and Nitrogen Species
Graves, D. B., & Bauer, G. (2018) · Springer eBooks · doi:10.1007/978-3-319-67627-2_4 · Cited by 11
Dou, C.-Z., Liu, Y., Zhang, L., Chen, S., Hu, C.-Y., Liu, Y., & Zhao, Y. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/8841706 · Cited by 11
Dabbour, N. M., Salama, A. M., Donia, T., Al-Deeb, R. T., Elghane, A. M. A., Badry, K. H., & Loutfy, S. A. (2021) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2021.103022 · Cited by 11
Modulation of reactive oxygen species in cancers: recent advances
Ganesh, J. M., Prerana, P., Dharmarajan, A., Warrier, S. R., & Gandhirajan, R. K. (2022) · Free Radical Research · doi:10.1080/10715762.2022.2133704 · Cited by 12
Øverby, A., Zhao, C., Bones, A. M., & Duan, C. (2014) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12732 · Cited by 11
Oxidative Stress and Drug Resistance in Cancer
Trachootham, D., Zhang, W., & Huang, P. (2009) · Springer eBooks · doi:10.1007/978-0-387-89445-4_7 · Cited by 12
Zhou, J., Chen, X., Feng, S., Luo, S., Pan, Y., Zhong, L., Ji, P., Wang, Z.-R., Ma, S., Li, L., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028930 · Cited by 13
Kang, J., Jeong, Y., Ha, S. K., Lee, H. H., & Lee, K. (2023) · Molecular Biology Reports · doi:10.1007/s11033-022-08130-5 · Cited by 10
Kyriakou, S., Demosthenous, N., Amery, T., Stewart, K. J., Winyard, P. G., Franco, R., Pappa, A., & Panayiotidis, M. I. (2024) · Antioxidants · doi:10.3390/antiox13010082 · Cited by 10
Glucosinolates, isothiocyanates, and their role in the regulation of autophagy and cellular function
Maycotte, P., Illanes, M., & Moreno, D. A. (2024) · Phytochemistry Reviews · doi:10.1007/s11101-024-09944-w · Cited by 10
Sanctis, G. D., Spinelli, M., Vanoni, M., & Sacco, E. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163790 · Cited by 10
Kengen, J., Deglasse, J.-P., Neveu, M.-A. C., Mignion, L., Desmet, C. M., Gourgue, F., Jonas, J., Gallez, B., & Jordan, B. F. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1427236 · Cited by 10
Tucker‐Kellogg, L., Shi, Y., White, J., & Pervaiz, S. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.08.028 · Cited by 10
Liby, K. T. (2013) · Dose-Response · doi:10.2203/dose-response.13-018.liby · Cited by 10
Kawano, Y., Iwama, E., Tsuchihashi, K., Shibahara, D., Harada, T., Tanaka, K., Nagano, O., Saya, H., Nakanishi, Y., & Okamoto, I. (2017) · Lung Cancer · doi:10.1016/j.lungcan.2017.09.008 · Cited by 11
Mima, S., Kakinuma, C., Higuchi, T., Saeki, K., Yamada, T., Uematsu, R., Ishino, M., 鬼頭, 信., Nishikawa, H., Kuniyoshi, H., et al. (2018) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.118.248740 · Cited by 10
Polyphenols in the diet: friend or foe?
Hooper, B., & Frazier, R. A. (2012) · Nutrition Bulletin · doi:10.1111/j.1467-3010.2012.02001.x · Cited by 10
In vivo detection of chemiluminescence to monitor photodynamic threshold dose for tumor treatment
Wei, Y., Song, J., & Chen, Q. (2011) · Photochemical & Photobiological Sciences · doi:10.1039/c0pp00346h · Cited by 10
Benites, J. F., Valderrama, J. A., Taper, H. S., & Calderón, P. B. (2009) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.57.615 · Cited by 10
Corrado, C., Raimondo, S., Flugy, A. M., Fontana, S., Santoro, A., Stassi, G., Marfia, A., Iovino, F., Arlinghaus, R. B., Kohn, E. C., et al. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.10.007 · Cited by 10
Phenethyl isothiocyanate enhances TRAIL-induced apoptosis in oral cancer cells and xenografts
Yeh, C., Ko, H., Hsieh, Y., Wu, K., Kuo, M. Y., & Deng, Y. (2016) · Clinical Oral Investigations · doi:10.1007/s00784-016-1736-0 · Cited by 10
Romo-González, M., Moreno-Paz, S., García‐Hernández, V., Sanchez-Guijo, F. M., & Hernández‐Hernández, Á. (2020) · Antioxidants · doi:10.3390/antiox9010074 · Cited by 10
Tripathi, V., Jaiswal, P., Sahu, K., Majumder, S. K., Kashyap, D., Jha, H. C., Dixit, A. K., & Parmar, H. S. (2022) · Advances in Cancer Biology - Metastasis · doi:10.1016/j.adcanc.2022.100065 · Cited by 9
Zahran, E. M., Mohyeldin, R. H., Refaat, H., Abou‐Zied, H. A., ElNaggar, M. H., Abbas, G. M., Maher, S. A., Saber, E. A., Zarka, M. A., Elrehany, M. A., et al. (2024) · Archiv der Pharmazie · doi:10.1002/ardp.202400684 · Cited by 9
Naveed, T., Ali, S., & Summer, M. (2025) · Medical Oncology · doi:10.1007/s12032-025-02894-z · Cited by 10
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Schmidt, E. E., & Arnér, E. S. J. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_16 · Cited by 9
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Ndombera, F. T. (2017) · Pure and Applied Chemistry · doi:10.1515/pac-2016-1219 · Cited by 9
Bisht, S., Nolting, J., Wenzel, J., Brossart, P., & Feldmann, G. (2019) · Journal of Oncology · doi:10.1155/2019/8701824 · Cited by 9
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Lee, M. K., Zhang, X., Kim, H. J., & Hwang, Y. S. (2021) · Oral Diseases · doi:10.1111/odi.13910 · Cited by 9
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Chen, K., Guo, L., & Wu, C. (2021) · BioEssays · doi:10.1002/bies.202100116 · Cited by 9
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Dong, J., & Liu, B. (2016) · Chemotherapy Open access · doi:10.4172/2167-7700.1000199 · Cited by 9
Hirata, T., Cho, Y., Suzuki, I., Toyoda, T., Akagi, J., Nakamura, Y. K., Numazawa, S., & Ogawa, K. (2019) · The Journal of Toxicological Sciences · doi:10.2131/jts.44.73 · Cited by 9
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Benites, J. F., Valderrama, J. A., Taper, H. S., & Calderón, P. B. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9419-1 · Cited by 9
Wu, L., Chen, X., Huang, L., Tian, J., Ke, F., Xu, J., Chen, Y., & Zheng, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123314 · Cited by 9
Shin, S. Y., Jung, E., Lim, Y., Lee, H.-J., Rhee, J. H., Yoo, M., Ahn, S., & Koh, D. (2022) · Crystals · doi:10.3390/cryst12010108 · Cited by 8
Yamaguchi, H., Kidachi, Y., Kamiie, K., Noshita, T., Umetsu, H., Fuke, Y., & Ryoyama, K. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.06.008 · Cited by 8
Liao, Y., Chen, Y., & Lee, T. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1344-1 · Cited by 8
The oxidoreductase p66Shc acts as tumor suppressor in BRAFV 600E‐transformed cells
Furlan, T., Khalid, S., Nguyen, A.-V., Günther, J., & Troppmair, J. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12199 · Cited by 8
Dai, F., Yan, W., Fu, X., Zheng, Y.-L., Du, Y., Bao, X., Kang, Y., Jin, X., & Zhou, B. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.075 · Cited by 8
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Gomathi, A., Alagumuthu, M., Sai, P. K. J. G., Madhyastha, H., Jayaraj, R., & Muthukaliannan, G. K. (2022) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520622666220523155905 · Cited by 8
Overcoming resistance in chronic myelogenous leukemia
Cooper, S., Giles, F. J., & Savona, M. R. (2009) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428190903267559 · Cited by 8
Nan, K., Zhong, Z., Yue, Y., Zhou, W., Sun, X., Shen, Y., Qu, M., Chen, Z., Gu, J., Sun, C., et al. (2024) · Digestive Diseases and Sciences · doi:10.1007/s10620-023-08213-8 · Cited by 7
Doshi, M., Treglown, K., Copik, A. J., & Gesquiere, A. J. (2013) · BioNanoScience · doi:10.1007/s12668-013-0114-5 · Cited by 7
Antitumor effect of fructose 1,6-bisphosphate and its mechanism in hepatocellular carcinoma cells
Lu, Y.-X., Yu, X.-C., & Zhu, M.-Y. (2013) · Tumor Biology · doi:10.1007/s13277-013-1231-z · Cited by 7
Siddik, Z. H. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-396521-9.00012-7 · Cited by 6
Cai, Z., Zhang, Y., Jiang, L., & Zhu, J. (2021) · 化学学报 · doi:10.6023/a20120583 · Cited by 7
Vernazza, S., Dellacasa, E., Tirendi, S., Pastorino, L., & Bassi, A. M. (2021) · Nanomaterials · doi:10.3390/nano11061365 · Cited by 7
Liu, D., & Liu, A. (2012) · Cell Biochemistry and Function · doi:10.1002/cbf.2912 · Cited by 7
Sheu, M., Chou, P.-Y., Huang, C., Tsai, I., Chien, Y., Lin, S., Tsai, H.-Y., Cheng, H., & Wu, C. (2010) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.2010.05358.x · Cited by 7
Capsaicin Mediated Oxidative Stress in Pancreatic Cancer
Datta, P., Pramanik, K. C., Mehrotra, S., & Srivastava, S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405205-5.00023-4 · Cited by 7
Chao, T. H., Chang, M.-Y., Su, S.-J., & Su, S.-H. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.023 · Cited by 7
Extracellular Albumin Covalently Sequesters Selenocompounds and Determines Cytotoxicity
Zheng, W., Boada, R., He, R., Xiao, T., Ye, F., Simonelli, L., Valiente, M., Zhao, Y. H., & Hassan, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194734 · Cited by 7
Guo, L., Ding, Z., Hu, J., & Liu, S. (2024) · ACS Nano · doi:10.1021/acsnano.4c09232 · Cited by 6
Powolny, A. A., Bommareddy, A., & Singh, S. V. (2011) · Springer eBooks · doi:10.1007/978-94-007-2630-7_12 · Cited by 6
Yamaguchi, H., Yu, T., Noshita, T., Kidachi, Y., Kamiie, K., Yoshida, K., Akitaya, T., Umetsu, H., & Ryoyama, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.265900 · Cited by 6
Ćwikłowska, K., Westhoff, M., Freisinger, S., Dwucet, A., Halatsch, M., Knippschild, U., Debatin, K., Schirmbeck, R., Winiarski, Ł., Oleksyszyn, J., et al. (2018) · Oncology Letters · doi:10.3892/ol.2018.9347 · Cited by 6
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Schmitt, S., & Zischka, H. (2018) · Deutsche Zeitschrift für Onkologie · doi:10.1055/a-0657-4437 · Cited by 6
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Varol, M. (2020) · Springer eBooks · doi:10.1007/978-981-15-7586-0_6 · Cited by 6
Tanikawa, A., Fujihara, T., Nakajima, N., Maeda, Y., Nogata, Y., Yoshimura, E., Okada, Y., Chiba, K., & Kitano, Y. (2022) · Chemistry & Biodiversity · doi:10.1002/cbdv.202200953 · Cited by 6
SHetA2, a New Cancer-Preventive Drug Candidate
Liu, S., Zhou, G., Lo, S. N. H., Louie, M. C., & Rajagopalan, V. (2016) · InTech eBooks · doi:10.5772/65365 · Cited by 6
Microgel Bioreactors for Cancer Cell Targeting by pH-Dependent Generation of Radicals
Majerská, M., Jakubec, M., Klimša, V., Rimpelová, S., Král, V., & Štĕpánek, F. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00531 · Cited by 6
Li, Y., Wei, W., Shen, H.-W., & Hu, W. (2014) · Tumor Biology · doi:10.1007/s13277-013-1597-y · Cited by 6
El-Sheekh, M. M., Kenawy, E., Yousuf, W. E., & Mohamed, T. M. (2024) · Cancer Nanotechnology · doi:10.1186/s12645-024-00291-1 · Cited by 5
Rapid and Robust Quantification of p-Xyleneselenocyanate in Plasma via Derivatization
Zheng, W., Benkessou, F., Twelkmeyer, B., Wang, S., Ginman, T., Ottosson, H., Abedi‐Valugerdi, M., Subirana, M. A., Zhao, Y. H., & Hassan, M. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01426 · Cited by 5
Starving cancer cells to enhances DNA damage and immunotherapy response
Shahi, A., & Kidane, D. (2024) · Oncotarget · doi:10.18632/oncotarget.28595 · Cited by 5
Chattopadhyay, M., Nath, N., Kodela, R., Metkar, S., Soyemi, S. A., & Kashfi, K. (2024) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.124.002240 · Cited by 5
Cai, Y., Wang, Z., Sun, T., Shi, Y., Sun, Y.-L., Huang, P., Su, L., & Jiang, W. (2012) · Oncology Reports · doi:10.3892/or.2012.2207 · Cited by 5
Hu, Z.-Y., Xu, F., Sun, R., CHEN, Y.-F., Zhang, D., Fan, Y., & Sun, J. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2015.3404 · Cited by 5
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Lee, J., Zhang, C., Ko, J.-Y., Lee, J.-S., & Jeon, Y. (2015) · Fisheries and aquatic sciences · doi:10.5657/fas.2015.0035 · Cited by 5
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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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