An Antioxidant Response Phenotype Shared between Hereditary and Sporadic Type 2 Papillary Renal Cell Carcinoma
Open accessAbstract
Fumarate hydratase (FH) mutation causes hereditary type 2 papillary renal cell carcinoma (PRCC2). The main effect of FH mutation is fumarate accumulation. The current paradigm posits that the main consequence of fumarate accumulation is HIF-α stabilization. Paradoxically, FH mutation differs from other HIF-α stabilizing mutations, such as VHL and SDH mutations, in its associated tumor types. We identified that fumarate can directly up-regulate antioxidant response element (ARE)-controlled genes. We demonstrated that aldo-keto reductase family 1 member B10 (AKR1B10) is an ARE-controlled gene and is up-regulated upon FH knockdown as well as in FH null cell lines. AKR1B10 overexpression is also a prominent feature in both hereditary and sporadic PRCC2. This phenotype better explains the similarities between hereditary and sporadic PRCC2.
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High fumarate binds glutathione, augmenting ROS signaling and accumulation in vitro and in vivo.
“High concentrations of fumarate bind to glutathione, augmenting ROS signaling and accumulation, as observed in not only in vitro models but also in vivo models136,137.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [137]
Cells lacking FH have high levels of succination on KEAP1, an electrophile sensor and negative regulator of Nrf2.
“Cells lacking FH were shown to have high levels of succination on Kelch-like ECH-associated protein 1 (KEAP1), an electrophile sensor and negative regulator of the transcription factor Nuclear Factor E2-related factor 2 (Nrf2) (Adam et al., 2011; Ooi et al., 2011).”
From Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us? (2012) · cites this paper as Ooi et al., 2011
TH1 and TH17 cells rely heavily on aerobic glycolysis.
“Two pro-inflammatory T cell subsets implicated in the pathogenesis of MS, namely TH1 and TH17 cells, rely heavily on aerobic glycolysis and treatment with DMF or MMF inhibited their development in vitro, as previously reported99,101,102, 49.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [101]
Treatment with DMF or MMF inhibits development of TH1 and TH17 cells in vitro.
“Two pro-inflammatory T cell subsets implicated in the pathogenesis of MS, namely TH1 and TH17 cells, rely heavily on aerobic glycolysis and treatment with DMF or MMF inhibited their development in vitro, as previously reported99,101,102, 49.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [101]
Cites
Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
Benjamini, Y., & Hochberg, Y. (1995) · Journal of the Royal Statistical Society Series B: Statistical Methodology · doi:10.1111/j.2517-6161.1995.tb02031.x · Cited by 109,482 · see citing works
limma: Linear Models for Microarray Data
Smyth, G. K. (2005) · Statistics for Biology and Health · doi:10.1007/0-387-29362-0_23 · Cited by 5,796 · see citing works
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · cited 12× · see citing works
“In cells devoid of VHL function, the E3 ubiquitin ligase complex fails to form and HIF-a accumulates.”
BackgroundInfluentialBioinformatics and Computational Biology Solutions Using R and Bioconductor
Gentleman, R. C., Carey, V. J., Huber, W. K., Irizarry, R. A., & Dudoit, S. (2005) · Statistics in the health sciences · doi:10.1007/0-387-29362-0 · Cited by 3,470 · see citing works
The Multiple Leiomyoma Consortium (2002) · Nature Genetics · doi:10.1038/ng849 · Cited by 1,635 · see citing works
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480 · see citing works
Dysfunctional KEAP1–NRF2 Interaction in Non-Small-Cell Lung Cancer
Singh, A., Misra, V., Thimmulappa, R. K., Lee, H., Ames, S., Hoque, M. O., Herman, J. G., Baylin, S. B., Sidransky, D., Gabrielson, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030420 · Cited by 1,060 · see citing works
Isaacs, J. S., Jung, Y. J., Mole, D. R., Lee, S., Torres-Cabala, C., Chung, Y.-L., Merino, M., Trepel, J., Zbar, B., Toro, J., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.017 · Cited by 958 · see citing works
Pollard, P. J., Brière, J. J., Alam, N. A., Barwell, J., Barclay, E., Wortham, N. C., Hunt, T., Mitchell, M., Olpin, S., Moat, S. J., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi227 · Cited by 865 · see citing works
An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
Chan, K., Han, X.-D., & Kan, Y. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081082098 · Cited by 766 · see citing works
Furukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 746 · see citing works
Shibata, T., Ohta, T., Tong, K. I., Kokubu, A., Odogawa, R., Tsuta, K., Asamura, H., Yamamoto, M., & Hirohashi, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806268105 · Cited by 728 · see citing works
Inherited susceptibility to uterine leiomyomas and renal cell cancer
Launonen, V., Vierimaa, O., Kiuru, M., Isola, J., Roth, S., Pukkala, E., Sistonen, P., Herva, R., & Aaltonen, L. A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051633798 · Cited by 669 · see citing works
McMahon, M. J., Itoh, K., Yamamoto, M. P., Chanas, S. A., Henderson, C. J., McLellan, L. I., Wolf, C. R., Cavin, C., & Hayes, J. D. (2001) · PubMed · Cited by 657 · see citing works
LAU, A., VILLENEUVE, N., Sun, Z., Wong, P. K., & Zhang, D. (2008) · Pharmacological Research · doi:10.1016/j.phrs.2008.09.003 · Cited by 645 · see citing works
Loss of Keap1 Function Activates Nrf2 and Provides Advantages for Lung Cancer Cell Growth
Ohta, T., Iijima, K., Miyamoto, M., Nakahara, I., Tanaka, H., Ohtsuji, M., Suzuki, T., Kobayashi, A., Yokota, J., Sakiyama, T., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-5003 · Cited by 630 · see citing works
Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
Holmgren, A., & Lu, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.083 · Cited by 577 · see citing works
Radjendirane, V., & Jaiswal, A. K. (1998) · Oncogene · doi:10.1038/sj.onc.1202237 · Cited by 566 · see citing works
Inhibition of Hypoxia-inducible Factor (HIF) Hydroxylases by Citric Acid Cycle Intermediates
Koivunen, P., Hirsilä, M., Remes, A. M., Hassinen, I. E., Kivirikko, K. I., & Myllyharju, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610415200 · Cited by 521 · see citing works
A HIF1α Regulatory Loop Links Hypoxia and Mitochondrial Signals in Pheochromocytomas
Dahia, P. L. M., Ross, K. N., Wright, M. E., Hayashida, C. Y., Santagata, S., Barontini, M., Kung, A. L., Sanso, G., Powers, J. F., Tischler, A. S., et al. (2005) · PLoS Genetics · doi:10.1371/journal.pgen.0010008 · Cited by 443 · see citing works
KEAP1 E3 Ligase-Mediated Downregulation of NF-κB Signaling by Targeting IKKβ
Lee, D.-F., Kuo, H.-P., Liu, M., Chou, C.-K., Xia, W., Du, Y., Shen, J., Chen, C.-T., Huo, L., Hsu, M.-C., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.025 · Cited by 399 · see citing works
Vanharanta, S., Buchta, M., McWhinney, S. R., Virta, S. K., Peçzkowska, M., Morrison, C. D., Lehtonen, R., Januszewicz, A., Järvinen, H., Juhola, M., et al. (2004) · The American Journal of Human Genetics · doi:10.1086/381054 · Cited by 389 · see citing works
Molecular basis for the contribution of the antioxidant responsive element to cancer chemoprevention
Hayes, J. D. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00695-4 · Cited by 323 · see citing works
Alam, N. A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg148 · Cited by 323 · see citing works
Nrf1 and Nrf2 Play Distinct Roles in Activation of Antioxidant Response Element-dependent Genes
Ohtsuji, M., Katsuoka, F., Kobayashi, A., Aburatani, H., Hayes, J. D., & Yamamoto, M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804597200 · Cited by 317 · see citing works
Zhang, D. D., Lo, S., Sun, Z., Habib, G. M., Lieberman, M. W., & Hannink, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501279200 · Cited by 299 · see citing works
MacLeod, A. K., McMahon, M. J., Plummer, S. M., Higgins, L. G., Penning, T. M., Igarashi, K., & Hayes, J. D. (2009) · Carcinogenesis · doi:10.1093/carcin/bgp176 · Cited by 297 · see citing works
Gao, L., Wang, J., Sekhar, K. R., Yin, H., Yared, N. F., Schneider, S. N., Sasi, S., Dalton, T. P., Anderson, M. E., Chan, J. Y., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607622200 · Cited by 278 · see citing works
Hypermethylation of the Keap1 gene in human lung cancer cell lines and lung cancer tissues
Wang, R., An, J., Ji, F., Jiao, H., Sun, H., & Zhou, D. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.06.004 · Cited by 261 · see citing works
Increased risk of cancer in patients with fumarate hydratase germline mutation
Lehtonen, H. J., Kiuru, M. H., Ylisaukko‐oja, S. K., Salovaara, R., Herva, R., Koivisto, P., Vierimaa, O., Aittomäki, K., Pukkala, ., Launonen, V., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2005.036400 · Cited by 225 · see citing works
Sudarshan, S., Sourbier, C., Kong, H.-S., Block, K., Romero, V. A. V., Yang, Y., Galindo, C., Mollapour, M., Scroggins, B., Goode, N., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00483-09 · Cited by 217 · see citing works
A mutation of Keap1 found in breast cancer impairs its ability to repress Nrf2 activity
Nioi, P., & Nguyen, T. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.051 · Cited by 212 · see citing works
Rachakonda, G., Xiong, Y., Sekhar, K. R., Stamer, S. L., Liebler, D. C., & Freeman, M. L. (2008) · Chemical Research in Toxicology · doi:10.1021/tx700302s · Cited by 210 · see citing works
Sakurai, A., Nishimoto, M., Himeno, S., Imura, N., Tsujimoto, M., Kunimoto, M., & Hara, S. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20246 · Cited by 207 · see citing works
Alderson, N. L., Wang, Y., Blatnik, M., Frizzell, N., Walla, M. D., Lyons, T. J., Alt, N., Carson, J. A., Nagai, R., Thorpe, S. R., et al. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.03.005 · Cited by 202 · see citing works
Molecular Diagnosis and Therapy of Kidney Cancer
Linehan, W. M., Bratslavsky, G., Pinto, P. A., Schmidt, L. S., Neckers, L., Bottaro, D. P., & Srinivasan, R. (2010) · Annual Review of Medicine · doi:10.1146/annurev.med.042808.171650 · Cited by 166 · see citing works
Linehan, W. M., Pinto, P. A., Srinivasan, R., Merino, M. J., Choyke, P. L., Choyke, L. T., Coleman, J., Toro, J. R., Glenn, G. M., Vocke, C. D., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1870 · Cited by 150 · see citing works
Malec, V., Gottschald, O. R., Li, S., Rose, F., Seeger, W., & Hänze, J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.008 · Cited by 149 · see citing works
Koshikawa, N., Hayashi, J.-I., Nakagawara, A., & Takenaga, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054221 · Cited by 147 · see citing works
Adult Leydig Cell Tumors of the Testis Caused by Germline Fumarate Hydratase Mutations
Carvajal‐Carmona, L. G., Alam, N. A., Pollard, P. J., Jones, A. M., Barclay, E., Wortham, N. C., Pignatelli, M. N., Freeman, A., Pomplun, S., Ellis, I., et al. (2006) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2006-0183 · Cited by 141 · see citing works
Pollard, P. J., El-Bahrawy, M. A., Poulsom, R., Elia, G., Killick, P., Kelly, G. P., Hunt, T., Jeffery, R. E., Seedhar, P., Barwell, J., et al. (2006) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2006-0920 · Cited by 140 · see citing works
Yang, Y., Valera, V., Padilla‐Nash, H. M., Sourbier, C., Vocke, C. D., Vira, M. A., Abu-Asab, M. S., Bratslavsky, G., Tsokos, M., Merino, M. J., et al. (2009) · Cancer Genetics and Cytogenetics · doi:10.1016/j.cancergencyto.2009.08.018 · Cited by 139 · see citing works
Zhang, Y., Crouch, D. H., Yamamoto, M. P., & Hayes, J. D. (2006) · Biochemical Journal · doi:10.1042/bj20060725 · Cited by 124 · see citing works
Succination of Protein Thiols during Adipocyte Maturation
Nagai, R., Brock, J. W. C., Blatnik, M., Baatz, J. E., Bethard, J. R., Walla, M. D., Thorpe, S. R., Baynes, J., & Frizzell, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703551200 · Cited by 122 · see citing works
Blatnik, M., Thorpe, S. R., & Baynes, J. W. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1433.047 · Cited by 109 · see citing works
O′Flaherty, L., Adam, J., Heather, L. C., Zhdanov, A. V., Chung, Y., Miranda, M. X., Croft, J., Olpin, S. E., Clarke, K. J., Pugh, C. W., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq305 · Cited by 108 · see citing works
WU, J. M., Hsieh, T., Lu, X., & Wang, Z. (2006) · Medicinal Chemistry · doi:10.2174/157340606776930709 · Cited by 107 · see citing works
Spencer, S. R., Wilczak, C. A., & Talalay, P. (1990) · PubMed · Cited by 103 · see citing works
Pollard, P., Wortham, N., Barclay, E., Alam, A., Elia, G., Manek, S., Poulsom, R., & Tomlinson, I. (2005) · The Journal of Pathology · doi:10.1002/path.1686 · Cited by 100 · see citing works
Succination of Thiol Groups in Adipose Tissue Proteins in Diabetes
Frizzell, N., Rajesh, M. P., Jepson, M. J., Nagai, R., Carson, J. A., Thorpe, S. R., & Baynes, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019257 · Cited by 99 · see citing works
Visceral pathology of hereditary tyrosinemia type I.
Russo, P., & O’Regan, S. (1990) · PubMed · Cited by 97 · see citing works
Hübner, R., Schwartz, J. D., De, B. P., Ferris, B., Omberg, L., Mezey, J. G., Hackett, N. R., & Crystal, R. G. (2009) · Molecular Medicine · doi:10.2119/molmed.2008.00130 · Cited by 92 · see citing works
Siow, R. C. M., Ishii, T., & Mann, G. E. (2007) · Redox Report · doi:10.1179/135100007x162167 · Cited by 88 · see citing works
Pae, H., Oh, G., Lee, B.-S., Rim, J.-S., Kim, Y., & Chung, H. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.09.010 · Cited by 84 · see citing works
Phase II trial of sunitinib in patients with metastatic non-clear cell renal cell carcinoma
Molina, A. M., Feldman, D. R., Ginsberg, M. S., Kroog, G. S., Tickoo, S. K., Jia, X., Georges, M., Patil, S., Baum, M. S., Reuter, V. E., et al. (2010) · Investigational New Drugs · doi:10.1007/s10637-010-9491-6 · Cited by 84 · see citing works
Kwak, M.-K., Kensler, T. W., & Casero, R. A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00834-9 · Cited by 78 · see citing works
Distinct expression profile in fumarate-hydratase-deficient uterine fibroids
Vanharanta, S., Pollard, P. J., Lehtonen, H. J., Laiho, P., Sjöberg, J., Leminen, A., Aittomäki, K., Arola, J. T., Kruhøffer, M., Orntoft, T. F., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi431 · Cited by 72 · see citing works
Hereditary Leiomyomatosis and Renal Cell Cancer (HLRCC)
Kiuru, M. H., & Launonen, V. (2004) · Current Molecular Medicine · doi:10.2174/1566524043359638 · Cited by 70 · see citing works
Sango, K., Suzuki, T., Yanagisawa, H., Takaku, S., Hirooka, H., Tamura, M., & Watabe, K. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03885.x · Cited by 63 · see citing works
Bellacosa, A., Godwin, A. K., Peri, S., Devarajan, K., Caretti, E., Vanderveer, L., Bove, B. A., Slater, C. M., Zhou, Y., Daly, M. B., et al. (2010) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-09-0078 · Cited by 60 · see citing works
Succination of proteins in diabetes
Frizzell, N., Lima, M., & Baynes, J. (2010) · Free Radical Research · doi:10.3109/10715762.2010.524643 · Cited by 59 · see citing works
Kashkar, H., Deggerich, A., Seeger, J.-M., Yazdanpanah, B., Wiegmann, K., Haubert, D., Pongratz, C., & Krönke, M. (2006) · Blood · doi:10.1182/blood-2006-10-053959 · Cited by 52 · see citing works
Furge, K. A., Tan, M.-H., Dykema, K. J., Kort, E. J., Stadler, W. M., Yao, X., Zhou, M., & Teh, B. T. (2007) · Oncogene · doi:10.1038/sj.onc.1210256 · Cited by 51 · see citing works
Self-citationActivation of the antioxidant response element by specific oxidized metabolites of linoleic acid
Wang, R., Kern, J. T., Goodfriend, T. L., Ball, D. L., & Luesch, H. (2009) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2009.04.008 · Cited by 46 · see citing works
Identification of candidate epigenetic biomarkers for ovarian cancer detection
Lin (2009) · Oncology Reports · doi:10.3892/or_00000509 · Cited by 45 · see citing works
Huang, Y., Luo, J. R., Weng, Y.-I., Mutch, D. G., Goodfellow, P. J., Miller, D. S., & Huang, T. H. ‐. (2010) · Gynecologic Oncology · doi:10.1016/j.ygyno.2010.02.006 · Cited by 44 · see citing works
Sourbier, C., Romero, V. V., Giubellino, A., Yang, Y., Sudarshan, S., Neckers, L., & Linehan, W. M. (2010) · Cell Cycle · doi:10.4161/cc.9.20.13458 · Cited by 27 · see citing works
Flagged first, then by citations
1 of the 68 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
Metabolic Reprogramming: A Cancer Hallmark Even Warburg Did Not Anticipate
Ward, P. S., & Thompson, C. B. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.02.014 · Cited by 3,233 · see citing works
Fundamentals of Cancer Metabolism
DeBerardinis, R. J., & Chandel, N. S. (2016) · Science Advances · doi:10.1126/sciadv.1600200 · Cited by 3,013 · see citing works
Mitochondrial TCA cycle metabolites control physiology and disease
Martínez-Reyes, I., & Chandel, N. S. (2020) · Nature Communications · doi:10.1038/s41467-019-13668-3 · Cited by 2,813 · see citing works
The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis
Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968 · see citing works
The Molecular Mechanisms Regulating the KEAP1-NRF2 Pathway
Baird, L., & Yamamoto, M. P. (2020) · Molecular and Cellular Biology · doi:10.1128/mcb.00099-20 · Cited by 1,600 · see citing works
The Keap1-Nrf2 pathway: Mechanisms of activation and dysregulation in cancer
Kansanen, E., Kuosmanen, S. M., Leinonen, H., & Levonen, A.-L. (2013) · Redox Biology · doi:10.1016/j.redox.2012.10.001 · Cited by 1,313 · see citing works
Comprehensive Molecular Characterization of Papillary Renal-Cell Carcinoma
The Cancer Genome Atlas Research Network (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1505917 · Cited by 1,336 · see citing works
The emerging role of the Nrf2–Keap1 signaling pathway in cancerPreprint
Jaramillo, M. C., & Zhang, D. D. (2013) · Genes & Development · doi:10.1101/gad.225680.113 · Cited by 1,304 · see citing works
Phosphorylation of p62 Activates the Keap1-Nrf2 Pathway during Selective Autophagy
Ichimura, Y., Waguri, S., Sou, Y., Kageyama, S., Hasegawa, J., Ishimura, R., Saito, T., Yang, Y., Kouno, T., Fukutomi, T., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.003 · Cited by 1,205 · see citing works
Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes & Development · doi:10.1101/gad.191056.112 · Cited by 1,188 · see citing works
NRF2 and cancer: the good, the bad and the importance of context
Sporn, M. B., & Liby, K. T. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3278 · Cited by 1,067 · see citing works
Glutamine reliance in cell metabolism
Yoo, H. C., Yu, Y. C., Sung, Y., & Han, J. M. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00504-8 · Cited by 1,021 · see citing works
Molecular basis of the Keap1–Nrf2 system
Suzuki, T., & Yamamoto, M. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.006 · Cited by 995 · see citing works
Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us?
DeBerardinis, R. J., & Thompson, C. B. (2012) · Cell · doi:10.1016/j.cell.2012.02.032 · Cited by 858 · see citing works
Tebay, L. E., Robertson, H., Durant, S. T., Vitale, S. R., Penning, T. M., Dinkova-Kostova, A. T., & Hayes, J. D. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.021 · Cited by 837 · see citing works
Mitochondrial reactive oxygen species and cancer
Sullivan, L. B., & Chandel, N. S. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-17 · Cited by 799 · see citing works
The Cancer Genome Atlas Comprehensive Molecular Characterization of Renal Cell Carcinoma
Ricketts, C. J., de Cubas, A. A., Fan, H., Smith, C. C., Lang, M., Reznik, E., Bowlby, R., Gibb, E. A., Akbani, R., Beroukhim, R., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.075 · Cited by 782 · see citing works
The Roles of NRF2 in Modulating Cellular Iron Homeostasis
Kerins, M. J., & Ooi, A. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7176 · Cited by 741 · see citing works
Self-citationThe Cancer Genome Atlas Comprehensive Molecular Characterization of Renal Cell Carcinoma
Ricketts, C. J., de Cubas, A. A., Fan, H., Smith, C. C., Lang, M., Reznik, E., Bowlby, R., Gibb, E. A., Akbani, R., Beroukhim, R., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.032 · Cited by 737 · see citing works
The Dual Roles of NRF2 in Cancer
Menegon, S., Columbano, A., & Giordano, S. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.05.002 · Cited by 633 · see citing works
The Cancer Genome Atlas of renal cell carcinoma: findings and clinical implications
Linehan, W. M., & Ricketts, C. J. (2019) · Nature Reviews Urology · doi:10.1038/s41585-019-0211-5 · Cited by 629 · see citing works
Singh, A., Venkannagari, S., Oh, K. H., Zhang, Y., Rohde, J. M., Liu, L., Nimmagadda, S., Sudini, K. R., Brimacombe, K. R., Gajghate, S., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00651 · Cited by 624 · see citing works
Fumarate is an epigenetic modifier that elicits epithelial-to-mesenchymal transition
Sciacovelli, M., Gonçalves, E., Johnson, T. I., Zecchini, V. R., da Costa, A. S. H., Gaude, E., Drubbel, A. V., Theobald, S. J., Abbo, S. R., Tran, M. G. B., et al. (2016) · Nature · doi:10.1038/nature19353 · Cited by 584 · see citing works
The KEAP1–NRF2 System in Cancer
Taguchi, K., & Yamamoto, M. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00085 · Cited by 527 · see citing works
Modulating NRF2 in Disease: Timing Is Everything
Dodson, M. B., de la Vega, M. R., Cholanians, A. B., Schmidlin, C. J., Chapman, E., & Zhang, D. D. (2018) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021856 · Cited by 540 · see citing works
Autophagy in the liver: functions in health and disease
Ueno, T., & Komatsu, M. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.185 · Cited by 500 · see citing works
Mitochondrial Dysfunction in Cancer
Boland, M. L., Chourasia, A. H., & Macleod, K. F. (2013) · Frontiers in Oncology · doi:10.3389/fonc.2013.00292 · Cited by 502 · see citing works
Ubiquitin ligases in oncogenic transformation and cancer therapy
Senft, D., Qi, J., & Ronai, Z. A. (2017) · Nature reviews. Cancer · doi:10.1038/nrc.2017.105 · Cited by 490 · see citing works
Regulation of chromatin and gene expression by metabolic enzymes and metabolites
Li, X., Egervári, G., Wang, Y., Berger, S. L., & Lu, Z. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0029-7 · Cited by 486 · see citing works
Glutaminolysis as a target for cancer therapy
Jin, L., Alesi, G. N., & Kang, S. (2016) · Oncogene · doi:10.1038/onc.2015.447 · Cited by 459 · see citing works
Altered metabolite levels in cancer: implications for tumour biology and cancer therapy
Sullivan, L. B., Gui, D. Y., & Heiden, M. G. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.85 · Cited by 406 · see citing works
Oncometabolites: linking altered metabolism with cancer
Yang, M. H., Soga, T., & Pollard, P. J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67228 · Cited by 424 · see citing works
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398 · see citing works
The Keap1–Nrf2 system in cancers: stress response and anabolic metabolism
Mitsuishi, Y., Motohashi, H., & Yamamoto, M. P. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00200 · Cited by 394 · see citing works
Saito, T., Ichimura, Y., Taguchi, K., Suzuki, T., Mizushima, T., Takagi, K., Hirose, Y., Nagahashi, M., Iso, T., Fukutomi, T., et al. (2016) · Nature Communications · doi:10.1038/ncomms12030 · Cited by 364 · see citing works
Transcription factor NRF2 regulates miR-1 and miR-206 to drive tumorigenesis
Singh, A., Happel, C., Manna, S. K., Acquaah-Mensah, G., Carrerero, J., Kumar, S., Nasipuri, P., Krausz, K. W., Wakabayashi, N., Dewi, R., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66353 · Cited by 333 · see citing works
Finley, L. W. S. (2023) · Cell · doi:10.1016/j.cell.2023.01.038 · Cited by 331 · see citing works
The Metabolic Basis of Kidney Cancer
Linehan, W. M., Schmidt, L. S., Crooks, D. R., Wei, D., Srinivasan, R., Lang, M., & Ricketts, C. J. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-1354 · Cited by 336 · see citing works
The Proto-oncometabolite Fumarate Binds Glutathione to Amplify ROS-Dependent Signaling
Sullivan, L. B., Martinez-Garcia, E., Nguyen, H., Mullen, A. R., Dufour, E., Sudarshan, S., Licht, J. D., Deberardinis, R. J., & Chandel, N. S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.05.003 · Cited by 304 · see citing works
Molecular Basis of the KEAP1-NRF2 Signaling Pathway
Suzuki, T., Takahashi, J. A., & Yamamoto, M. P. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.0028 · Cited by 309 · see citing works
Fumarate Is Cardioprotective via Activation of the Nrf2 Antioxidant Pathway
Ashrafian, H., Czibik, G., Bellahcene, M., Aksentijević, D., Smith, A. C., Mitchell, S. J., Dodd, M. S., Kirwan, J., Byrne, J. J., Ludwig, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.01.017 · Cited by 303 · see citing works
The KEAP1-NRF2 pathway: Targets for therapy and role in cancer
Adinolfi, S., Patinen, T., Deen, A. J., Pitkänen, S., Härkönen, J., Kansanen, E., Küblbeck, J., & Levonen, A. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102726 · Cited by 301 · see citing works
Oncogenic KRAS Confers Chemoresistance by Upregulating NRF2
Tao, S., Wang, S., Moghaddam, S. J., Ooi, A., Chapman, E., Wong, P. K., & Zhang, D. D. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1439 · Cited by 291 · see citing works
Self-citationMolecular Mechanism of Cellular Oxidative Stress Sensing by Keap1
Suzuki, T., Muramatsu, A., Saito, R., Iso, T., Shibata, T., Kuwata, K., Kawaguchi, S.-I., Iwawaki, T., Adachi, S., Suda, H., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.047 · Cited by 289 · see citing works
Fumarate induces redox-dependent senescence by modifying glutathione metabolism
Zheng, L., Cardaci, S., Jerby, L., MacKenzie, E. D., Sciacovelli, M., Johnson, T. I., Gaude, E., King, A., Leach, J. D. G., Edrada-Ebel, R., et al. (2015) · Nature Communications · doi:10.1038/ncomms7001 · Cited by 281 · see citing works
NRF2 addiction in cancer cells
Kitamura, H., & Motohashi, H. (2018) · Cancer Science · doi:10.1111/cas.13537 · Cited by 275 · see citing works
Beyond repression of Nrf2: An update on Keap1
Kopacz, A., Klóska, D., Forman, H. J., Józkowicz, A., & Grochot‐Przeczek, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.03.023 · Cited by 262 · see citing works
Trpkov, K., Hes, O., Agaimy, A., Bonert, M., Martínek, P., Magi‐Galluzzi, C., Kristiansen, G., Lüders, C., Nesi, G., Compérat, É., et al. (2016) · The American Journal of Surgical Pathology · doi:10.1097/pas.0000000000000617 · Cited by 259 · see citing works
Defects in mitochondrial metabolism and cancer
Gaude, E., & Frezza, C. (2014) · Cancer & Metabolism · doi:10.1186/2049-3002-2-10 · Cited by 249 · see citing works
Thirty years of NRF2: advances and therapeutic challenges.
Zhang, D. D. (2025) · Nature Reviews Drug Discovery · doi:10.1038/s41573-025-01145-0 · Cited by 282 · see citing works
Tricarboxylic Acid (TCA) Cycle Intermediates: Regulators of Immune Responses
Choi, I., Son, H., & Baek, J.-H. (2021) · Life · doi:10.3390/life11010069 · Cited by 244 · see citing works
p62/ SQSTM 1: ‘Jack of all trades’ in health and cancer
Sánchez‐Martín, P., Saito, T., & Komatsu, M. (2018) · FEBS Journal · doi:10.1111/febs.14712 · Cited by 242 · see citing works
Li, F., He, X., Ye, D., Lin, Y., Yu, H., Yao, C., Huang, L., Zhang, J., Wang, F., Xu, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.10.017 · Cited by 244 · see citing works
Protein Lysine Acylation and Cysteine Succination by Intermediates of Energy Metabolism
Lin, H., Su, X., & He, B. (2012) · ACS Chemical Biology · doi:10.1021/cb3001793 · Cited by 236 · see citing works
Mehine, M. M., Kaasinen, E., Heinonen, H.-R., Mäkinen, N., Kämpjärvi, K., Sarvilinna, N. S., Aavikko, M., Vähärautio, A., Pasanen, A. M., Bützow, R. C., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1518752113 · Cited by 229 · see citing works
Cancer Metabolism: Current Understanding and Therapies
Counihan, J. L., Grossman, E. A., & Nomura, D. K. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00775 · Cited by 229 · see citing works
CRNDE: A Long Non-Coding RNA Involved in CanceR, Neurobiology, and DEvelopment
Ellis, B. C., Molloy, P. L., & Graham, L. D. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00270 · Cited by 228 · see citing works
Molecular and Chemical Regulation of the Keap1-Nrf2 Signaling Pathway
Keum, Y., & Choi, B. Y. (2014) · Molecules · doi:10.3390/molecules190710074 · Cited by 224 · see citing works
Roemeling, C. A. V., Radisky, D. C., Marlow, L. A., Cooper, S. J., Grebe, S. K. G., Anastasiadis, P. Z., Tun, H. W., & Copland, J. A. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0210 · Cited by 223 · see citing works
Linehan, W. M., & Rouault, T. A. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0304 · Cited by 223 · see citing works
Oncometabolites in renal cancer
Yong, C., Stewart, G. D., & Frezza, C. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0210-z · Cited by 212 · see citing works
Hereditary Kidney Cancer Syndromes
Haas, N. B., & Nathanson, K. L. (2013) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2013.10.001 · Cited by 209 · see citing works
Role of Nrf2 in protection against acute kidney injury
Shelton, L. M., Park, B. K., & Copple, I. M. (2013) · Kidney International · doi:10.1038/ki.2013.248 · Cited by 201 · see citing works
Mitochondria as Cellular and Organismal Signaling Hubs
Shen, K., Pender, C. L., Bar‐Ziv, R., Zhang, H., Wickham, K., Willey, E., Durieux, J., Ahmad, Q., & Dillin, A. G. (2022) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-120420-015303 · Cited by 203 · see citing works
The pleiotropic functions of reactive oxygen species in cancer
Wu, K., Zowalaty, A. E. E., Sayin, V. I., & Papagiannakopoulos, T. Y. (2024) · Nature Cancer · doi:10.1038/s43018-024-00738-9 · Cited by 203 · see citing works
The KEAP1–NRF2 System as a Molecular Target of Cancer Treatment
Taguchi, K., & Yamamoto, M. (2020) · Cancers · doi:10.3390/cancers13010046 · Cited by 195 · see citing works
The emerging role of fumarate as an oncometabolite
Yang, M., Soga, T., Pollard, P. J., & Adam, J. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00085 · Cited by 189 · see citing works
NRF2: KEAPing Tumors Protected
Pillai, R., Hayashi, M., Zavitsanou, A.-M., & Papagiannakopoulos, T. Y. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-0922 · Cited by 187 · see citing works
Potential Applications of NRF2 Inhibitors in Cancer Therapy
Panieri, E., & Saso, L. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8592348 · Cited by 185 · see citing works
Roles of Nrf2 in Protecting the Kidney from Oxidative Damage
Nezu, M., & Suzuki, N. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082951 · Cited by 180 · see citing works
Cheng, J., Yan, J., Liu, Y., Shi, J., Wang, H., Zhou, H., Zhou, Y., Zhang, T., Zhao, L., Meng, X., et al. (2023) · Cell Metabolism · doi:10.1016/j.cmet.2023.04.017 · Cited by 182 · see citing works
Oncometabolites: Unconventional triggers of oncogenic signalling cascades
Sciacovelli, M., & Frezza, C. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.025 · Cited by 177 · see citing works
Keap Calm, and Carry on Covalently
Wilson, A. J., Kerns, J. K., Callahan, J. F., & Moody, C. J. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400224q · Cited by 171 · see citing works
Monitoring Keap1–Nrf2 interactions in single live cells
Baird, L., Swift, S., Llères, D., & Dinkova‐Kostova, A. T. (2014) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.03.004 · Cited by 171 · see citing works
Harder, B. G., Jiang, T., Wu, T., Tao, S., de la Vega, M. R., Tian, W., Chapman, E., & Zhang, D. D. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150020 · Cited by 171 · see citing works
Regulation of the Keap1–Nrf2 pathway by p62/SQSTM1
Katsuragi, Y., Ichimura, Y., & Komatsu, M. (2016) · Current Opinion in Toxicology · doi:10.1016/j.cotox.2016.09.005 · Cited by 166 · see citing works
Halofuginone enhances the chemo-sensitivity of cancer cells by suppressing NRF2 accumulation
Tsuchida, K., Tsujita, T., Hayashi, M., Ojima, A., Keleku-Lukwete, N., Katsuoka, F., Otsuki, A., Kikuchi, H., Oshima, Y., Suzuki, M., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.12.041 · Cited by 167 · see citing works
Inhibition of Mitochondrial Aconitase by Succination in Fumarate Hydratase Deficiency
Ternette, N., Yang, M., Laroyia, M., Kitagawa, M., O’Flaherty, L., Wolhulter, K., Igarashi, K., Saito, K., Kato, K., Fischer, R., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.013 · Cited by 158 · see citing works
Fumarate hydratase in cancer: A multifaceted tumour suppressor
Schmidt, C., Sciacovelli, M., & Frezza, C. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.002 · Cited by 163 · see citing works
TCA Cycle Defects and Cancer: When Metabolism Tunes Redox State
Cardaci, S., & Ciriolo, M. R. (2012) · International Journal of Cell Biology · doi:10.1155/2012/161837 · Cited by 162 · see citing works
State of the Science: An Update on Renal Cell Carcinoma
Jonasch, E. W., Futreal, P. A., Davis, I. J., Bailey, S. T., Kim, W. Y., Brugarolas, J., Giaccia, A. J., Kurban, G., Pause, A., Frydman, J., et al. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0117 · Cited by 161 · see citing works
The Role of NRF2/KEAP1 Signaling Pathway in Cancer Metabolism
Song, M.-Y., Lee, D.-Y., Chun, K., & Kim, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094376 · Cited by 166 · see citing works
SQSTM1 Is a Pathogenic Target of 5q Copy Number Gains in Kidney Cancer
Li, L., Shen, C., Nakamura, E., Ando, K., Signoretti, S., Beroukhim, R., Cowley, G. S., Lizotte, P. H., Liberzon, E., Bair, S. M., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.10.025 · Cited by 162 · see citing works
Genetic predisposition to kidney cancer
Schmidt, L. S., & Linehan, W. M. (2016) · Seminars in Oncology · doi:10.1053/j.seminoncol.2016.09.001 · Cited by 160 · see citing works
Ooi, A., Dykema, K., Ansari, A., Petillo, D., Snider, J., Kahnoski, R., Anema, J., Craig, D., Carpten, J., Teh, B.-T., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3227 · Cited by 159 · see citing works
Self-citationBai, X., Chen, Y., Hou, X., Huang, M., & Jin, J. (2016) · Drug Metabolism Reviews · doi:10.1080/03602532.2016.1197239 · Cited by 159 · see citing works
Role of the Keap1–Nrf2 Pathway in Cancer
Leinonen, H. M., Kansanen, E., Pölönen, P., Heinäniemi, M., & Levonen, A. (2014) · Advances in cancer research · doi:10.1016/b978-0-12-420117-0.00008-6 · Cited by 158 · see citing works
Hereditary leiomyomatosis and renal cell carcinoma
Schmidt, L. S., & Linehan, W. M. (2014) · International Journal of Nephrology and Renovascular Disease · doi:10.2147/ijnrd.s42097 · Cited by 155 · see citing works
Epidemiology and Prevention of Renal Cell Carcinoma
Makino, T., Kadomoto, S., Izumi, K., & Mizokami, A. (2022) · Cancers · doi:10.3390/cancers14164059 · Cited by 151 · see citing works
Oncometabolites‐driven tumorigenesis: From genetics to targeted therapy
Morin, A., Letouzé, É., Gimenez‐Roqueplo, A., & Favier, J. (2014) · International Journal of Cancer · doi:10.1002/ijc.29080 · Cited by 150 · see citing works
New and emerging renal entities: a perspective post‐ WHO 2016 classification
Trpkov, K., & Hes, O. (2018) · Histopathology · doi:10.1111/his.13727 · Cited by 147 · see citing works
A catalogue of somatic NRF2 gain-of-function mutations in cancer
Kerins, M. J., & Ooi, A. (2018) · Scientific Reports · doi:10.1038/s41598-018-31281-0 · Cited by 140 · see citing works
Self-citationThe metabolic basis of kidney cancer
Linehan, W. M., & Ricketts, C. J. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.06.002 · Cited by 148 · see citing works
Morandi, A., Taddei, M. L., Chiarugi, P., & Giannoni, E. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00040 · Cited by 139 · see citing works
Tao, S., de la Vega, M. R., Chapman, E., Ooi, A., & Zhang, D. D. (2017) · Molecular Carcinogenesis · doi:10.1002/mc.22745 · Cited by 136 · see citing works
Self-citationMitochondrial metabolites: undercover signalling molecules
Frezza, C. (2017) · Interface Focus · doi:10.1098/rsfs.2016.0100 · Cited by 136 · see citing works
Perspectives of the Nrf-2 signaling pathway in cancer progression and therapy
Basak, P., Sadhukhan, P., Sarkar, P., & Sil, P. C. (2017) · Toxicology Reports · doi:10.1016/j.toxrep.2017.06.002 · Cited by 133 · see citing works
Chinopoulos, C., & Seyfried, T. N. (2018) · ASN NEURO · doi:10.1177/1759091418818261 · Cited by 128 · see citing works
Hsieh, J. J.-D., Le, V., Cao, D., Cheng, E. H. Y., & Creighton, C. J. (2017) · The Journal of Pathology · doi:10.1002/path.5022 · Cited by 126 · see citing works
- Authors
- Ooi, A., Wong, J.-C., Petillo, D., Roossien, D., Perrier-Trudova, V., Whitten, D., Min, B. W. H., Tan, M.-H., Zhang, Z., Yang, X. J., Zhou, M., Gardie, B., Molinié, V., Richard, S., Tan, P. H., Teh, B. T., & Furge, K. A.
- Affiliations
- Van Andel Institute (US)
- National Cancer Centre Singapore (SG)
- Michigan State University (US)
- Northwestern University (US)
- Cleveland Clinic (US)
- Inserm (FR)
- Singapore General Hospital (SG)
- Corresponding author
- Teh, Bin Tean
- Furge, Kyle A.
- ORCID
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 20
- Issue
- 4
- Pages
- 511-523
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W1976949137
- Cited by
- 401
- References
- 68
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 22 · 2023: 23 · 2022: 21 · 2021: 18 · 2020: 33 · 2019: 35 · 2018: 33 · 2017: 32 · 2016: 41 · 2015: 27 · 2014: 26 · 2013: 36 · 2012: 21
- FWCI
- 24.21
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Van Andel Research Institute
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Renal cell carcinoma treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- type 2 papillary renal cell carcinoma, fumarate accumulation, antioxidant response element, AKR1B10, aldo-keto reductase, tumor suppressor mutations
- MeSH terms
- Kelch-Like ECH-Associated Protein 1, Aldo-Keto Reductases, Aldehyde Reductase, Antioxidants, Carcinoma, Renal Cell, Fumarate Hydratase, Humans, Kidney Neoplasms, Phenotype, RNA, Messenger, Gene Expression Regulation, Neoplastic, Response Elements, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Nuclear Respiratory Factor 1, NF-E2-Related Factor 2, Hypoxia-Inducible Factor 1, alpha Subunit
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