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Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity
Open accessAbstract
Otto Warburg's theory on the origins of cancer postulates that tumor cells have defects in mitochondrial oxidative phosphorylation and therefore rely on high levels of aerobic glycolysis as the major source of ATP to fuel cellular proliferation (the Warburg effect). This is in contrast to normal cells, which primarily utilize oxidative phosphorylation for growth and survival. Here we report that the major function of glucose metabolism for Kras-induced anchorage-independent growth, a hallmark of transformed cells, is to support the pentose phosphate pathway. The major function of glycolytic ATP is to support growth under hypoxic conditions. Glutamine conversion into the tricarboxylic acid cycle intermediate alpha-ketoglutarate through glutaminase and alanine aminotransferase is essential for Kras-induced anchorage-independent growth. Mitochondrial metabolism allows for the generation of reactive oxygen species (ROS) which are required for Kras-induced anchorage-independent growth through regulation of the ERK MAPK signaling pathway. We show that the major source of ROS generation required for anchorage-independent growth is the Q o site of mitochondrial complex III. Furthermore, disruption of mitochondrial function by loss of the mitochondrial transcription factor A (TFAM) gene reduced tumorigenesis in an oncogenic Kras-driven mouse model of lung cancer. These results demonstrate that mitochondrial metabolism and mitochondrial ROS generation are essential for Kras-induced cell proliferation and tumorigenesis.
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“Providing cells with αKG, oxaloacetate, or pyruvate is sufficient to rescue cancer cell proliferation in conditions of glutamine starvation, confirming that glutamine supports proliferation by replenishing depleted TCA cycle intermediates, a process termed anaplerosis (Altman et al., 2016; Weinberg et al., 2010; Yuneva et al., 2007).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Weinberg et al., 2010
In the citing paper
“However, KRAS has also been shown to promote cancer cell growth by stimulating alanine aminotransferase activity, leading to high levels of α-ketoglutarate for the TCA cycle and mitochondrial ROS generation, which was required for mutant KRAS-driven tumorigenesis in a mouse model of lung cancer64.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [64]
In the citing paper
“A low level of reactive oxygen species (ROS) activates tumorigenic growth signaling; however, when the level exceeds the cellular redox capacity, ROS can damage macromolecules such as proteins, lipids and nucleotides55.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [55]
In the citing paper
“Correspondingly, in K-Ras mutant cells, the oxygen consumption rate and ATP generation are enhanced by glutamine, contributing to tumorigenesis55.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [55]
In the citing paper
“Notably, alanine levels were significantly decreased in Mpc knockdown cells, highlighting a role for mitochondrial pyruvate and mitochondrial alanine aminotransferase (ALT2) in mediating glutamine anaplerosis which was previously described in cancer cells (Weinberg et al., 2010).”
From Regulation of Substrate Utilization by the Mitochondrial Pyruvate Carrier (2014) · cites this paper as Weinberg et al., 2010
In the citing paper
“Another study reported that mitochondrial ROS are necessary for the KRAS (Kirsten rat sarcoma virus)—induced anchored-independent growth of lung cancer.”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Weinberg et al. 2010
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Cites
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088
On Respiratory Impairment in Cancer Cells
Warburg, O. H. (1956) · Science · doi:10.1126/science.124.3215.269 · Cited by 3,472
The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth
Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820
DeBerardinis, R. J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S., & Thompson, C. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709747104 · Cited by 2,622
Gao, P., Tchernyshyov, I., Chang, T.-C., Lee, Y.-S., Kita, K., Ochi, T., Zeller, K. I., De Marzo, A. M., Van Eyk, J. E., Mendell, J. T., et al. (2009) · Nature · doi:10.1038/nature07823 · Cited by 2,124
Wise, D. R., DeBerardinis, R. J., Mancuso, A., Sayed, N., Zhang, X.-Y., Pfeiffer, H. K., Nissim, I., Daikhin, E., Yudkoff, M., McMahon, S. B., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810199105 · Cited by 2,001
Hypoxia, HIF1 and glucose metabolism in the solid tumour
Denko, N. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2468 · Cited by 1,707
Fantin, V. R., St-Pierre, J., & Leder, P. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.04.023 · Cited by 1,635
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Redox control of glutamine utilization in cancer
Alberghina, L., & Gaglio, D. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.513 · Cited by 150
Chinopoulos, C. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23196 · Cited by 148
Rohlenová, K., Sachaphibulkij, K., Štursa, J., Bezawork‐Geleta, A., Blecha, J., Endaya, B., Werner, L., Černý, J., Zobalová, R., Goodwin, J., et al. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6677 · Cited by 144
Sormendi, S., & Wielockx, B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00040 · Cited by 147
Cheng, C.-W., Kuo, C.-Y., Fan, C.-C., Fang, W.-C., Jiang, S. S., Yk, L., Wang, T.-Y., Kao, M.-C., & Lee, A. Y.-L. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.204 · Cited by 142
DNA Damage in Cancer Therapeutics: A Boon or a Curse?
Khanna, A. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3247 · Cited by 142
Kalyanaraman, B., Hardy, M., Podsiadły, R., Cheng, G., & Zielonka, J. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.021 · Cited by 140
Self-citationMitochondrial Genome Instability and ROS Enhance Intestinal Tumorigenesis in APC Mice
Woo, D. K., Green, P. D., Santos, J. H., D’Souza, A. D., Walther, Z., Martin, W. D., Christian, B. E., Chandel, N. S., & Shadel, G. S. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.10.003 · Cited by 138
Self-citationMitochondrial Abnormality Facilitates Cyst Formation in Autosomal Dominant Polycystic Kidney Disease
Ishimoto, Y., Inagi, R., Yoshihara, D., Kugita, M., Nagao, S., Shimizu, A., Takeda, N., Wake, M., Honda, K., Zhou, J., et al. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00337-17 · Cited by 139
Using Seahorse Machine to Measure OCR and ECAR in Cancer Cells
Zhang, J., & Zhang, Q. H. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9027-6_18 · Cited by 140
A break in mitochondrial endosymbiosis as a basis for inflammatory diseases
Murphy, M. P., & O’Neill, L. A. J. (2024) · Nature · doi:10.1038/s41586-023-06866-z · Cited by 138
Obre, E., & Rossignol, R. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.12.008 · Cited by 137
Balliet, R. M., Capparelli, C., Guido, C., Pestell, T. G., Martinez‐Outschoorn, U., Zhao, L., Whitaker‐Menezes, D., Chiavarina, B., Pestell, R. G., Howell, A., et al. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18254 · Cited by 138
The many faces of Janus kinase
Seavey, M. M., & Dobrzański, P. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.12.024 · Cited by 136
Biochemical Underpinnings of Immune Cell Metabolic Phenotypes
Olenchock, B. A., Rathmell, J. C., & Heiden, M. G. V. (2017) · Immunity · doi:10.1016/j.immuni.2017.04.013 · Cited by 141
Targeting mitochondria in cancer: current concepts and immunotherapy approaches
Pustylnikov, S., Costabile, F., Beghi, S., & Facciabene, A. (2018) · Translational research · doi:10.1016/j.trsl.2018.07.013 · Cited by 142
CRISPR screens in physiologic medium reveal conditionally essential genes in human cells
Rossiter, N. J., Huggler, K. S., Adelmann, C. H., Keys, H. R., Soens, R. W., Sabatini, D. M., & Cantor, J. R. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.02.005 · Cited by 138
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Yuan, Y., Li, H., Wang, P., Chen, L., Guo, D. S., Jiang, H., He, B., Qin, S., Wang, K., Li, N., et al. (2021) · Science China Life Sciences · doi:10.1007/s11427-021-1999-2 · Cited by 140
Glutamine metabolism in breast cancer and possible therapeutic targets
Li, S., Zeng, H., Fan, J., Wang, X., Xu, C., Li, Y., Tu, J., Nephew, K. P., & Long, X. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115464 · Cited by 143
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Kawada, K., Toda, K., & Sakai, Y. (2017) · International Journal of Clinical Oncology · doi:10.1007/s10147-017-1156-4 · Cited by 140
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Uras, I. Z., Moll, H. P., & Casanova, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124325 · Cited by 138
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Mitra, K. (2013) · BioEssays · doi:10.1002/bies.201300011 · Cited by 134
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Still, E. R., & Yuneva, M. O. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.113 · Cited by 142
Ren, Y., Wang, R., Weng, S., Xu, H., Zhang, Y., Chen, S., Liu, S., Ba, Y., Zhou, Z., Luo, P., et al. (2023) · Molecular Cancer · doi:10.1186/s12943-023-01831-w · Cited by 149
Hypoxia Dictates Metabolic Rewiring of Tumors: Implications for Chemoresistance
Belisario, D. C., Kopecka, J., Pasino, M., Akman, M., De Smaele, E., Donadelli, M., & Riganti, C. (2020) · Cells · doi:10.3390/cells9122598 · Cited by 133
Mitochondria in cancer: at the crossroads of life and death
Fogg, V. C., Lanning, N. J., & MacKeigan, J. P. (2011) · 癌症:英文版 · doi:10.5732/cjc.011.10018 · Cited by 139
Targeting ROS-Mediated Crosstalk Between Autophagy and Apoptosis in Cancer
Gao, L., Loveless, J., Shay, C., & Teng, Y. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-42667-5_1 · Cited by 135
Diers, A. R., Broniowska, K. A., Chang, C.-F., & Hogg, N. (2012) · Biochemical Journal · doi:10.1042/bj20120294 · Cited by 133
Cheng, G., Zielonka, J., McAllister, D. M., Mackinnon, A. C., Joseph, J., Dwinell, M. B., & Kalyanaraman, B. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-285 · Cited by 132
Self-citationHe, Z., Xu, Q., Newland, B., Foley, R., Lara‐Sáez, I., Curtin, J. F., & Wang, W. (2021) · Journal of Materials Chemistry B · doi:10.1039/d1tb00728a · Cited by 134
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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
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Shanware, N. P., Bray, K., & Abraham, R. T. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134717 · Cited by 136
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Yamada, Y., Satrialdi, S., Hibino, M., Sasaki, D., Abe, J., & Harashima, H. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.09.010 · Cited by 129
Dong, C., Dai, X., Wang, X., Lu, Q., Chen, L., Song, X., Ding, L., Huang, H., Feng, W., Chen, Y., et al. (2022) · Advanced Materials · doi:10.1002/adma.202205680 · Cited by 130
Metabolic reprogramming and its clinical implication for liver cancer
Yang, F., Hilakivi-Clarke, L. A., Shaha, A., Wang, Y., Wang, X., Deng, Y., Lai, J., & Kang, N. (2023) · Hepatology · doi:10.1097/hep.0000000000000005 · Cited by 140
Chinopoulos, C., & Seyfried, T. N. (2018) · ASN NEURO · doi:10.1177/1759091418818261 · Cited by 130
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Rasola, A., Neckers, L., & Picard, D. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.03.005 · Cited by 129
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Caldez, M. J., Van Hul, N., Koh, H. W. L., Teo, X. Q., Fan, J. J., Tan, P. Y., Dewhurst, M. R., Too, P. G., Talib, S. Z. A., Chiang, B. E., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.09.020 · Cited by 133
Redox signaling: Potential arbitrator of autophagy and apoptosis in therapeutic response
Zhang, L., Wang, K., Lei, Y., Li, Q., Nice, E. C., & Huang, C. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.08.030 · Cited by 127
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Wang, P., Ma, W., Park, J., Celi, F. S., Arena, R. A., Choi, J. W., Ali, Q. A., Tripodi, D., Zhuang, J., Lago, C. U., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1214091 · Cited by 128
Amplification of USP13 drives ovarian cancer metabolism
Han, C., Yang, L., Choi, H. H., Baddour, J., Achreja, A., Liu, Y., Li, Y., Li, J., Wan, G., Huang, C., et al. (2016) · Nature Communications · doi:10.1038/ncomms13525 · Cited by 127
Glutaminase inhibitor CB-839 synergizes with carfilzomib in resistant multiple myeloma cells
Thompson, R. M., Dytfeld, D., Reyes, L., Robinson, R. M., Smith, B. M., Manevich, Y., Jakubowiak, A. J., Komarnicki, M. A., Przybyłowicz-Chalecka, A., Szczepaniak, T., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16262 · Cited by 126
Koundinya, M., Sudhalter, J., Courjaud, A., Lionne, B., Touyer, G., Bonnet, L., Menguy, I., Schreiber, I., Perrault, C., Vougier, S., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.03.005 · Cited by 123
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Boyle, K. A., Wickle, J. V., Hill, R. B., Marchese, A., Kalyanaraman, B., & Dwinell, M. B. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001469 · Cited by 130
Self-citationOshima, N., Ishida, R., Kishimoto, S., Beebe, K. E., Brender, J., Yamamoto, K., Urban, D. J., Rai, G., Johnson, M. S., Benavides, G. A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.01.039 · Cited by 130
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Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
Wang, Y., Wang, F., Wang, L., Qiu, S., Yao, Y., Yan, C., Xiong, X., Chen, X., Ji, Q., Cao, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109516 · Cited by 125
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Shvedova, A. A., Yanamala, N. V. K., Kisin, E. R., Tkach, A. V., Murray, A. R., Hubbs, A. F., Chirila, M. M., Keohavong, P., Sycheva, L. P., Kagan, V. E., et al. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00167.2013 · Cited by 124
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Jeong, S. M., Lee, A., Lee, J., & Haigis, M. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525949 · Cited by 121
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Freyre‐Fonseca, V., Delgado‐Buenrostro, N. L., Gutiérrez-Cirlos, E. B., Calderón-Torres, C. M., Cabellos-Avelar, T., Sánchez-Pérez, Y., Pinzón, E., Torres, I., Molina‐Jijón, E., & Zazueta, C. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.01.025 · Cited by 123
Song, I.-S., Jeong, Y. J., Jeong, S. H., Heo, H. J., Kim, H. K., Bae, K. B., Park, Y., Kim, S. U., Kim, J., Kim, N., et al. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.06.007 · Cited by 123
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Policastro, L. L., Ibañez, I. L., Notcovich, C., Duran, H. A., & Podhajcer, O. L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4367 · Cited by 120
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Hu, S., Feng, J., Wang, M., Wufuer, R., Liu, K., Zhang, Z., & Zhang, Y. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102470 · Cited by 123
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Purohit, V., Simeone, D. M., & Lyssiotis, C. A. (2019) · Cancers · doi:10.3390/cancers11070955 · Cited by 121
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Yuan, L., Sheng, X., Willson, A. K., Roque, D. R., Stine, J. E., Guo, H., Jones, H. M., Zhou, C., & Bae-Jump, V. L. (2015) · Endocrine Related Cancer · doi:10.1530/erc-15-0192 · Cited by 116
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Chang, J. Y., Yi, H., Kim, H.-W., & Shong, M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.12.008 · Cited by 117
Hollinshead, K. E. R., Parker, S. J., Eapen, V. V., Encarnación-Rosado, J., Sohn, A. S. W., Oncu, T., Cammer, M., Mancias, J. D., & Kimmelman, A. C. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108231 · Cited by 118
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Wang, H., Wang, L., Zhang, Y., Wang, J., Deng, Y., & Lin, D. (2016) · Cancer Cell International · doi:10.1186/s12935-016-0280-y · Cited by 113
Toda, K., Kawada, K., Iwamoto, M., Inamoto, S., Sasazuki, T., Shirasawa, S., Hasegawa, S., & Sakai, Y. (2016) · Neoplasia · doi:10.1016/j.neo.2016.09.004 · Cited by 113
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Jeong, S. M., Hwang, S., & Seong, R. H. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.02.023 · Cited by 112
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Xu, L., Lin, D., Yin, D., & Koeffler, H. P. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1107-0 · Cited by 114
Chang, C.-W., Chen, Y., Chou, S.-H., Han, C., Chen, Y., Yang, C.-C., Huang, C., & Lo, J. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0626 · Cited by 113
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Metadata
- Authors
- Weinberg, F., Hamanaka, R., Wheaton, W. W., Weinberg, S., Joseph, J., Lopez, M., Kalyanaraman, B., Mutlu, G. M., Budinger, G. R. S., & Chandel, N. S.
- Affiliations
- Northwestern University (US)
- Division of Pulmonary and Critical Care, Department of Medicine,
- Medical College of Wisconsin (US)
- Department of Biophysics and Free Radical Research Center, Medical College of Wisconsin, Milwaukee, WI 53226
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-04-26
- Volume
- 107
- Issue
- 19
- Pages
- 8788-8793
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2889315
- OpenAlex
- W1982330633
- Cited by
- 1,742
- References
- 29
- Citations by year
- 2026: 63 · 2025: 100 · 2024: 124 · 2023: 122 · 2022: 149 · 2021: 154 · 2020: 137 · 2019: 138 · 2018: 111 · 2017: 108 · 2016: 100 · 2015: 113 · 2014: 89 · 2013: 77 · 2012: 77
- FWCI
- 23.58
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 BX000201)
- LUNGevity Foundation
- Respiratory Health Association of Metropolitan Chicago
- Respiratory Health Association
- National Institutes of Health
- National Heart, Lung, and Blood Institute (P01HL071643)
- National Cancer Institute (R01CA125112, R01CA152810, R01CA123067, CA125112, P30CA060553, T32CA070085, T32CA009560)
- National Institute of Environmental Health Sciences (ES 013995, ES015024, R01ES013995, R01ES015024)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- KRAS, mitochondrial metabolism, reactive oxygen species, pentose phosphate pathway, aerobic glycolysis, Warburg effect, anchorage-independent growth, glutaminase, alpha-ketoglutarate, TCA cycle, ERK signaling, mitochondrial complex III, TFAM, lung cancer, carcinogenesis, hypoxia
- MeSH terms
- Aerobiosis, Animals, Cell Adhesion, Cell Transformation, Neoplastic, Glutamine, Glycolysis, Humans, Lung Neoplasms, Mitochondria, Oxidative Phosphorylation, Pentose Phosphate Pathway, Electron Transport Complex III, Proto-Oncogene Proteins p21(ras), Reactive Oxygen Species, HCT116 Cells, Extracellular Signal-Regulated MAP Kinases, Cell Proliferation, Mice
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