The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
CUL3 and NRF2 Mutations Confer an NRF2 Activation Phenotype in a Sporadic Form of Papillary Renal Cell Carcinoma
Published version of a preprint
Abstract
Sustained activation of the stress-regulated transcription factor NRF2 (NFE2L2) is a prominent feature of many types of cancer, implying that mutations driving NRF2 may be important to tumor progression. In hereditary type 2 papillary renal cell carcinoma (PRCC2, also known as hereditary leiomyomatosis and renal cell cancer), NRF2 activation is a direct consequence of the accumulation of intracellular fumarate, a result of fumarate hydratase (FH) inactivation, but it is not clear how NRF2 may be activated in sporadic forms of PRCC2. Here we show that somatic mutations in NRF2, CUL3, and SIRT1 are responsible for driving the NRF2 activation phenotype in sporadic PRCC2. Transcriptome sequencing revealed the expression pattern of mutant alleles of NRF2, CUL3, and SIRT1 and also confirmed NRF2 activation in clinical specimens. Our results show a convergence in somatic mutations in sporadic PRCC2 with FH mutation in hereditary PRCC2. Cancer Res; 73(7); 2044–51. ©2013 AACR.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Some somatic mutations give rise to hyperactive Nrf2, which causes enhanced antioxidant capacity and confers protection of cancer cells from ROS and cancer therapy, thereby leading to cancer cell growth and proliferation, cancer progression, and cancer therapy resistance (e.g., chemoresistance) (Figure 8) [161,162,163,164,165,166,167,168,169,170,171].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [166]
In the citing paper
“most of which have been attributed to loss-of-function mutations in the KEAP1 gene and/or gain-of-function mutations in the NFE2L2 gene encoding Nrf2 [162,163,164,166,167].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [166]
Citations
Cites
R: A Language and Environment for Statistical Computing
R Core Team (2000) · doi:10.32614/r.manuals · Cited by 355,893
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
The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041
Fast and accurate short read alignment with Burrows-Wheeler transform
Li, H., & Durbin, R. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp324 · Cited by 58,607
The variant call format and VCFtools
Danecek, P., Auton, A., Abecasis, G. R., Albers, C. A., Banks, E., DePristo, M. A., Handsaker, R. E., Lunter, G. A., Marth, G., Sherry, S. T., et al. (2011) · Bioinformatics · doi:10.1093/bioinformatics/btr330 · Cited by 16,450
Differential expression analysis for sequence count data
Anders, S., & Huber, W. (2010) · Genome Biology · doi:10.1186/gb-2010-11-10-r106 · Cited by 15,581
Trapnell, C., Roberts, A., Goff, L. A., Pertea, G. M., Kim, D., Kelley, D. R., Pimentel, H., Salzberg, S. L., Rinn, J. L., & Pachter, L. S. (2012) · Nature Protocols · doi:10.1038/nprot.2012.016 · Cited by 12,145
TopHat: discovering splice junctions with RNA-Seq
Trapnell, C., Pachter, L. S., & Salzberg, S. L. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp120 · Cited by 11,682
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Oncogene-induced Nrf2 transcription promotes ROS detoxification and tumorigenesis
DeNicola, G. M., Karreth, F. A., Humpton, T. J., Gopinathan, A., Wei, C., Frese, K., Mangal, D., Yu, K. H., Yeo, C. J., Calhoun, E. S., et al. (2011) · Nature · doi:10.1038/nature10189 · Cited by 2,277
Cited by
Sorted by citations
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
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
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 1,326
Integrated molecular analysis of clear-cell renal cell carcinoma
Sato, Y., Yoshizato, T., Shiraishi, Y., Maekawa, S., Okuno, Y., Kamura, T., Shimamura, T., Sato‐Otsubo, A., Nagae, G., Suzuki, H., et al. (2013) · Nature Genetics · doi:10.1038/ng.2699 · Cited by 1,257
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
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
Tu, W., Wang, H., Li, S., Liu, Q., & Sha, H. (2018) · Aging and Disease · doi:10.14336/ad.2018.0513 · Cited by 727
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 644
The KEAP1–NRF2 System in Cancer
Taguchi, K., & Yamamoto, M. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00085 · Cited by 527
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
Nrf2 in cancers: A double‐edged sword
Wu, S., Lu, H., & Bai, Y. (2019) · Cancer Medicine · doi:10.1002/cam4.2101 · Cited by 479
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 441
Deshmukh, P. H., Unni, S., Krishnappa, G., & Padmanabhan, B. (2016) · Biophysical Reviews · doi:10.1007/s12551-016-0244-4 · Cited by 405
NRF2 as a regulator of cell metabolism and inflammation in cancer
He, F., Antonucci, L., & Karin, M. (2020) · Carcinogenesis · doi:10.1093/carcin/bgaa039 · Cited by 332
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 320
The Nrf2/HO‐1 Axis in Cancer Cell Growth and Chemoresistance
Furfaro, A. L., Traverso, N., Domenicotti, C., Piras, S., Moretta, L., Marinari, U. M., Pronzato, M. A., & Nitti, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1958174 · Cited by 303
Paul, M. K., Bisht, B., Darmawan, D. O., Chiou, R., Ha, V. L., Wallace, W. D., Chon, A. T., Hegab, A. E., Grogan, T., Elashoff, D. A., et al. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.05.009 · Cited by 289
The genomic landscape of hepatoblastoma and their progenies with HCC-like features
Eichenmüller, M., Trippel, F., Kreuder, M., Beck, A., Schwarzmayr, T., Häberle, B., Cairo, S., Leuschner, I., von Schweinitz, D., Strom, T. M., et al. (2014) · Journal of Hepatology · doi:10.1016/j.jhep.2014.08.009 · Cited by 258
Oncogenic potential of Nrf2 and its principal target protein heme oxygenase-1
Na, H., & Surh, Y. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.10.819 · Cited by 203
Regulation of Nrf2/ARE Pathway by Dietary Flavonoids: A Friend or Foe for Cancer Management?
Suraweera, T. L., Rupasinghe, H. P. V., Dellaire, G., & Xu, Z. (2020) · Antioxidants · doi:10.3390/antiox9100973 · Cited by 217
Ge, W., Zhao, K., Wang, X., Li, H., Yu, M., He, M., Xue, X., Zhu, Y., Zhang, C. L., Cheng, Y., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.09.008 · Cited by 188
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 189
An update of Nrf2 activators and inhibitors in cancer prevention/promotion
Pouremamali, F., Pouremamali, A., Dadashpour, M., Soozangar, N., & Jeddi, F. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00906-3 · Cited by 183
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 179
Frank, R., Scheffler, M., Merkelbach‐Bruse, S., Ihle, M. A., Kron, A., Rauer, M., Ueckeroth, F., König, K., Michels, S. Y. F., Fischer, R. N., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3416 · Cited by 167
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
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
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 152
Hyperkalemic hypertension–associated cullin 3 promotes WNK signaling by degrading KLHL3
McCormick, J. A., Yang, C., Zhang, C., Davidge, B., Blankenstein, K. I., Terker, A. S., Yarbrough, B., Meermeier, N. P., Park, H. J., McCully, B. H., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76126 · Cited by 139
Brusatol overcomes chemoresistance through inhibition of protein translation
Harder, B. G., Tian, W., Clair, J. J. L., Tan, A. C., Ooi, A., Chapman, E., & Zhang, D. D. (2016) · Molecular Carcinogenesis · doi:10.1002/mc.22609 · Cited by 138
Self-citationSirtuin and metabolic kidney disease
Wakino, S., Hasegawa, K., & Itoh, H. (2015) · Kidney International · doi:10.1038/ki.2015.157 · Cited by 136
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
Self-citationHsieh, 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 131
Kovac, M. B., Navas, C., Horswell, S. D., Salm, M., Bardella, C., Rowan, A., Stares, M., Castro-Giner, F., Fisher, R. A., de Bruin, E. C., et al. (2015) · Nature Communications · doi:10.1038/ncomms7336 · Cited by 123
The role of natural products in revealing NRF2 function
Zhang, D. D., & Chapman, E. (2020) · Natural Product Reports · doi:10.1039/c9np00061e · Cited by 123
Li, F., Aljahdali, I. A. M., Zhang, R., Nastiuk, K. L., Krolewski, J. J., & Ling, X. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02026-1 · Cited by 114
Targeting ABL1-Mediated Oxidative Stress Adaptation in Fumarate Hydratase-Deficient Cancer
Sourbier, C., Ricketts, C. J., Matsumoto, S., Crooks, D. R., Liao, P., Mannes, P. Z., Yang, Y., Wei, M.-H., Srivastava, G. K., Ghosh, S., et al. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.10.005 · Cited by 109
Reactive Oxygen Species and NRF2 Signaling, Friends or Foes in Cancer?
Wang, R., Liang, L., Matsumoto, M., Iwata, K., Umemura, A., & He, F. (2023) · Biomolecules · doi:10.3390/biom13020353 · Cited by 112
New Strategies in Renal Cell Carcinoma: Targeting the Genetic and Metabolic Basis of Disease
Srinivasan, R., Ricketts, C. J., Sourbier, C., & Linehan, W. M. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2993 · Cited by 111
Saleeb, R., Brimo, F., Farag, M. S., Rompré‐Brodeur, A., Rotondo, F., Beharry, V., Wala, S. J., Plant, P. J., Downes, M. R., Pace, K. T., et al. (2017) · The American Journal of Surgical Pathology · doi:10.1097/pas.0000000000000962 · Cited by 106
Role of Nrf2 and Autophagy in Acute Lung Injury
de la Vega, M. R., Dodson, M. B., Groß, C., Mansour, H. M., Lantz, R. C., Chapman, E., Wang, T., Black, S. M., Garcia, J. G. N., & Zhang, D. D. (2016) · Current Pharmacology Reports · doi:10.1007/s40495-016-0053-2 · Cited by 104
The intricacies of NRF2 regulation in cancer
Schmidlin, C. J., Shakya, A., Dodson, M. B., Chapman, E., & Zhang, D. D. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.016 · Cited by 103
Dysregulation of NRF2 in Cancer: from Molecular Mechanisms to Therapeutic Opportunities
Jung, B.-J., Yoo, H.-S., Shin, S., Park, Y., & Jeon, S. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.195 · Cited by 104
Nuclear Factor Erythroid 2-Related Factor 2 in Regulating Cancer Metabolism
Smolková, K., Mikó, E., Kovàcs, T., Leguina‐Ruzzi, A., Sipos, A., & Bai, P. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8024 · Cited by 101
Dysregulation of the Keap1–Nrf2 pathway in cancer
Leinonen, H. M., Kansanen, E., Pölönen, P., Heinäniemi, M., & Levonen, A. (2015) · Biochemical Society Transactions · doi:10.1042/bst20150048 · Cited by 94
Yang, Q., Li, K., Huang, X., Zhao, C. N., Mei, Y., Li, X., Jiao, L., & Yang, H. (2020) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.11.035 · Cited by 93
Nrf2 and SQSTM1/p62 jointly contribute to mesenchymal transition and invasion in glioblastoma
Pölönen, P., Deen, A. J., Leinonen, H. M., Jyrkkänen, H.-K., Linna-Kuosmanen, S., Mononen, M., Jain, A., Tuomainen, T., Pasonen‐Seppänen, S., Hartikainen, J. M., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0956-6 · Cited by 90
Rare insights into cancer biology
Adam, J., Yang, M., Soga, T., & Pollard, P. J. (2013) · Oncogene · doi:10.1038/onc.2013.222 · Cited by 90
Fabrizio, F. P., Costantini, M., Copetti, M., la Torre, A., Sparaneo, A., Fontana, A., Poeta, M. L., Gallucci, M., Sentinelli, S., Graziano, P., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14492 · Cited by 92
Kim, J.-H., Lee, K.-S., Lee, D.-K., Kim, J., Kwak, S.-N., Ha, K., Choe, J., Won, M., Cho, B. R., Jeoung, D., et al. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5856 · Cited by 88
Functional polymorphisms in Nrf2: implications for human disease
Cho, H., Marzec, J. M., & Kleeberger, S. R. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.012 · Cited by 83
Advances in hereditary leiomyomatosis and renal cell carcinoma (HLRCC) research
Ooi, A. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.10.016 · Cited by 85
Self-citationCullin 3 Ubiquitin Ligases in Cancer Biology: Functions and Therapeutic Implications
Chen, H., & Chen, R. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00113 · Cited by 85
The Regulation of NRF2 by Nutrient-Responsive Signaling and Its Role in Anabolic Cancer Metabolism
Lee, S. B., Sellers, B. N., & DeNicola, G. M. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7356 · Cited by 78
Xu, K., Ma, J., Hall, S. R. R., Peng, R., Yang, H., & Yao, F. (2023) · Theranostics · doi:10.7150/thno.80184 · Cited by 77
A comprehensive characterization of cis -acting splicing-associated variants in human cancerPreprint
Shiraishi, Y., Kataoka, K., Chiba, K., Okada, A., Kogure, Y., Tanaka, H., Ogawa, S., & Miyano, S. (2018) · Genome Research · doi:10.1101/gr.231951.117 · Cited by 72
Shah, N., Zaitseva, L., Bowles, K. M., MacEwan, D. J., & Rushworth, S. A. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.152 · Cited by 69
Precision medicine from the renal cancer genome
Riazalhosseini, Y., & Lathrop, M. G. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.133 · Cited by 69
Chakraborty, S., Balan, M., Flynn, E. A., Zurakowski, D., Choueiri, T. K., & Pal, S. (2019) · Oncogenesis · doi:10.1038/s41389-018-0116-9 · Cited by 65
Understanding the role of NRF2-regulated miRNAs in human malignancies
Shah, N., Rushworth, S. A., Murray, M. Y., Bowles, K. M., & MacEwan, D. J. (2013) · Oncotarget · doi:10.18632/oncotarget.1181 · Cited by 63
The Succinated Proteome of FH-Mutant Tumours
Yang, M. H., Ternette, N., Su, H., Dabiri, R., Kessler, B. M., Adam, J., Teh, B. T., & Pollard, P. J. (2014) · Metabolites · doi:10.3390/metabo4030640 · Cited by 60
Self-citationFabrizio, F. P., Sparaneo, A., Trombetta, D., & Muscarella, L. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2492063 · Cited by 60
Vanneste, M., Feddersen, C. R., Varzavand, A., Zhu, E. Y., Foley, T. M., Zhao, L. Q., Holt, K. H., Milhem, M. M., Piper, R. C., Stipp, C. S., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00442 · Cited by 58
Levings, D. C., Wang, X., Kohlhase, D., Bell, D. A., & Slattery, M. G. (2018) · Redox Biology · doi:10.1016/j.redox.2018.07.026 · Cited by 53
Targeted therapy of esophageal squamous cell carcinoma: the NRF2 signaling pathway as target
Ma, S., Paiboonrungruan, C., Yan, T., Williams, K. P., Major, M. B., & Chen, X. L. (2018) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13681 · Cited by 54
Association of Nrf2 with airway pathogenesis: lessons learned from genetic mouse models
Cho, H., & Kleeberger, S. R. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1557-y · Cited by 53
Payandeh, Z., Tazehkand, A. P., Barati, G., Pouremamali, F., Kahroba, H., Baradaran, B., & Samadi, N. (2020) · Biochimie · doi:10.1016/j.biochi.2020.09.014 · Cited by 54
Schiavoni, V., Emanuelli, M., Milanese, G., Galosi, A. B., Pompei, V., Salvolini, E., & Campagna, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252413239 · Cited by 51
Panieri, E., & Saso, L. (2021) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8146 · Cited by 46
Su, D., Stamatakis, L., Singer, E. A., & Srinivasan, R. (2014) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000069 · Cited by 47
The KEAP1-NRF2 System and Esophageal Cancer
Hirose, W., Oshikiri, H., Taguchi, K., & Yamamoto, M. P. (2022) · Cancers · doi:10.3390/cancers14194702 · Cited by 48
Molecular pathways in renal cell carcinoma
Su, D., Singer, E. A., & Srinivasan, R. (2015) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000186 · Cited by 46
Multifaceted Roles of the KEAP1–NRF2 System in Cancer and Inflammatory Disease Milieu
Panda, H., Wen, H., Suzuki, M., & Yamamoto, M. P. (2022) · Antioxidants · doi:10.3390/antiox11030538 · Cited by 46
Iwaya, T., Endo, F., Yaegashi, M., Sasaki, N., Fujisawa, R., Hiraki, H., Akiyama, Y., Sasaki, A., Suzuki, Y., Masuda, M., et al. (2020) · Gastroenterology · doi:10.1053/j.gastro.2020.09.035 · Cited by 43
Integrated epigenomic profiling reveals endogenous retrovirus reactivation in renal cell carcinoma
Siebenthall, K. T., Miller, C. P., Vierstra, J. D., Mathieu, J., Tretiakova, M., Reynolds, A. P., Sandstrom, R. S., Rynes, E., Neph, S. J., Haugen, E., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.01.063 · Cited by 42
Nrf2 Is a Potential Modulator for Orchestrating Iron Homeostasis and Redox Balance in Cancer Cells
Zhang, L., Zhang, J., Jin, Y., Yao, G., Zhao, H., Qiao, P., & Wu, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.728172 · Cited by 45
Insights into the Genetic Basis of the Renal Cell Carcinomas from The Cancer Genome Atlas
Haake, S. M., Weyandt, J. D., & Rathmell, W. K. (2016) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-16-0115 · Cited by 41
GULP1 regulates the NRF2-KEAP1 signaling axis in urothelial carcinoma
Hayashi, M., Guida, E., Inokawa, Y., Goldberg, R. L., Reis, L. O., Ooki, A., Pilli, M., Sadhukhan, P., Woo, J., Choi, W., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aba0443 · Cited by 41
Association of nanoparticles and Nrf2 with various oxidative stress-mediated diseases
Thiruvengadam, R., Venkidasamy, B., Samynathan, R., Rajakumar, G., Thiruvengadam, M., & Kim, J. H. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110535 · Cited by 40
Ghosh, S., Dutta, N., Banerjee, P., Gajbhiye, R. L., SARENG, H. R., Kapse, P., Pal, S., Burdelya, L. G., Mandal, N. C., Ravichandiran, V., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.05.037 · Cited by 36
Renal cell carcinoma: translational aspects of metabolism and therapeutic consequences
Yang, O. C. Y., Maxwell, P. H., & Pollard, P. J. (2013) · Kidney International · doi:10.1038/ki.2013.245 · Cited by 38
Smoker extracellular vesicles influence status of human bronchial epithelial cells
Héliot, A., Landkocz, Y., Saint-Georges, F. R., Gosset, P., Billet, S., Shirali, P., Courcot, D., & Martin, P. J. (2016) · International Journal of Hygiene and Environmental Health · doi:10.1016/j.ijheh.2016.12.010 · Cited by 39
Filtering through the role of NRF2 in kidney disease
Schmidlin, C. J., Dodson, M. B., & Zhang, D. D. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01177-2 · Cited by 36
TCA cycle-derived oncometabolites in cancer and the immune microenvironment
Sarkar, S., Chang, C.-I., Jean, J., & Wu, M. (2025) · Journal of Biomedical Science · doi:10.1186/s12929-025-01186-y · Cited by 39
NRF2 Regulation by Noncoding RNAs in Cancers: The Present Knowledge and the Way Forward
Fabrizio, F. P., Sparaneo, A., & Muscarella, L. A. (2020) · Cancers · doi:10.3390/cancers12123621 · Cited by 36
Tracing Renal Cell Carcinomas back to the Nephron
Lindgren, D., Sjölund, J., & Axelson, H. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.05.003 · Cited by 40
Role of the KEAP1-NRF2 Axis in Renal Cell Carcinoma
Clerici, S., & Boletta, A. (2020) · Cancers · doi:10.3390/cancers12113458 · Cited by 36
Fabrizio, F. P., Sparaneo, A., Centra, F., Trombetta, D., Storlazzi, C. T., Graziano, P., Maiello, E., Fazio, V. M., & Muscarella, L. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112697 · Cited by 30
Small Molecular Nrf2 Inhibitors as Chemosensitizers for Cancer Therapy
Lin, H., Qiao, Y., Yang, H., Nan, Q., Qu, W., Feng, F., Liu, W., Chen, Y., & Sun, H. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2019-0285 · Cited by 30
Rooper, L. M., Thompson, L. D. �., Gagan, J., Hwang, J. S. G., London, N. R., Mikula, M. W., Stevens, T. M., & Bishop, J. A. (2022) · Modern Pathology · doi:10.1038/s41379-022-01068-w · Cited by 30
Cullin 3 and Its Role in Tumorigenesis
Chen, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_12 · Cited by 29
Testa, U., Pelosi, E., & Castelli, G. (2020) · Medicines · doi:10.3390/medicines7080044 · Cited by 30
Chen, Z., Rong, L., Huang, D. F., & Jiang, Q. L. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.171 · Cited by 27
Novel NRF2 ‐activated cancer treatments utilizing synthetic lethality
Baird, L., Kensler, T. W., & Yamamoto, M. P. (2022) · IUBMB Life · doi:10.1002/iub.2680 · Cited by 26
NRF2: Master regulator of cellular homeostasis and therapeutic vulnerability in cancer
Chen, W.-T., McKee, N. W., Kuhnell, D., & Dodson, M. B. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104050 · Cited by 29
Yamaguchi, Y., Kamai, T., Higashi, S., Murakami, S., Arai, K., Shirataki, H., & Yoshida, K. (2019) · BMC Cancer · doi:10.1186/s12885-019-6347-0 · Cited by 25
Chronic arsenic exposure enhances metastatic potential via NRF2-mediated upregulation of SOX9
Schmidlin, C. J., Zeng, T., Liu, P., Wei, Y., Dodson, M. B., Chapman, E., & Zhang, D. D. (2020) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2020.115138 · Cited by 23
Zhang, C., Li, L., Zhang, Y., & Zeng, C. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.686556 · Cited by 20
Mechanisms used by cancer cells to tolerate drug-induced replication stress
Segeren, H. A., & Westendorp, B. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215804 · Cited by 23
Tasaki, M., Kuroiwa, Y., Inoue, T., Hibi, D., Matsushita, K., Kijima, A., Maruyama, S., Nishikawa, A., & Umemura, T. (2013) · Experimental and Toxicologic Pathology · doi:10.1016/j.etp.2013.07.003 · Cited by 21
Metadata
- Authors
- Ooi, A., Dykema, K., Ansari, A., Petillo, D., Snider, J., Kahnoski, R., Anema, J., Craig, D., Carpten, J., Teh, B.-T., & Furge, K. A.
- Affiliations
- Van Andel Institute (US)
- Venue
- Cancer Research
- Published
- 2013-04-01
- Volume
- 73
- Issue
- 7
- Pages
- 2044-2051
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- OpenAlex
- W2135514225
- Cited by
- 159
- References
- 35
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 6 · 2023: 7 · 2022: 13 · 2021: 9 · 2020: 19 · 2019: 17 · 2018: 13 · 2017: 11 · 2016: 12 · 2015: 20 · 2014: 13 · 2013: 8
- FWCI
- 7.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Health Sciences › Medicine › Oncology › Renal cell carcinoma treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- papillary renal cell carcinoma, Nrf2 activation, CUL3, NRF2 mutation, SIRT1, fumarate hydratase, hereditary leiomyomatosis and renal cell carcinoma, somatic mutations, fumarate accumulation, tumor progression
- MeSH terms
- Kelch-Like ECH-Associated Protein 1, Amino Acid Sequence, Carcinoma, Renal Cell, Cells, Cultured, Humans, Immunoenzyme Techniques, Kidney Neoplasms, Kidney Tubules, Proximal, Molecular Sequence Data, Mutation, Phenotype, Biomarkers, Tumor, Blotting, Western, Sequence Homology, Amino Acid, Oligonucleotide Array Sequence Analysis, Gene Expression Profiling, Cullin Proteins, Intracellular Signaling Peptides and Proteins, NF-E2-Related Factor 2, Sirtuin 1, High-Throughput Nucleotide Sequencing
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