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Supporting Aspartate Biosynthesis Is an Essential Function of Respiration in Proliferating Cells
Open accessAbstract
Mitochondrial respiration is important for cell proliferation; however, the specific metabolic requirements fulfilled by respiration to support proliferation have not been defined. Here, we show that a major role of respiration in proliferating cells is to provide electron acceptors for aspartate synthesis. This finding is consistent with the observation that cells lacking a functional respiratory chain are auxotrophic for pyruvate, which serves as an exogenous electron acceptor. Further, the pyruvate requirement can be fulfilled with an alternative electron acceptor, alpha-ketobutyrate, which provides cells neither carbon nor ATP. Alpha-ketobutyrate restores proliferation when respiration is inhibited, suggesting that an alternative electron acceptor can substitute for respiration to support proliferation. We find that electron acceptors are limiting for producing aspartate, and supplying aspartate enables proliferation of respiration deficient cells in the absence of exogenous electron acceptors. Together, these data argue a major function of respiration in proliferating cells is to support aspartate synthesis.
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“The availability of NAD+ as an electron acceptor enables aspartate synthesis through aspartate aminotransferase and rescues the proliferation of cultured cells with dysfunctions or inhibition of the electron transport system [16,17].”
From Proliferating Astrocytes in Primary Culture Do Not Depend upon Mitochondrial Respiratory Complex I Activity or Oxidative Phosphorylation (2023) · cites this paper as [17]
The cited source says what the claim attributes to it.
In the citing paper
“Despite the prevalence of glycolysis, mitochondrial respiration remains important in proliferating cells, allowing the production of biosynthetic precursors and the generation of electron acceptors that enable aspartate synthesis, for example [9,16,17].”
From Proliferating Astrocytes in Primary Culture Do Not Depend upon Mitochondrial Respiratory Complex I Activity or Oxidative Phosphorylation (2023) · cites this paper as [17]
In the citing paper
“Genetic or epigenetic silencing of ASS1 expression provides an advantage to tumor cells by allowing them to preserve cellular aspartate (Rabinovich et al., 2015), a poorly transported nutrient that can be a critical output of the TCA cycle to support de novo nucleotide synthesis and cell proliferation (Birsoy et al., 2015; Sullivan et al., 2015).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Sullivan et al., 2015
In the citing paper
“However, mitochondrial ATP production appears dispensable for many proliferating cells (Birsoy et al., 2015; Sullivan et al., 2015; Titov et al., 2016).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Sullivan et al., 2015
In the citing paper
“Instead, respiration serves an alternative anabolic role for proliferating cells by regenerating the oxidized form of nicotinamide adenine dinucleotide (NAD+) from the reduced form (NADH) (Birsoy et al., 2015; Sullivan et al., 2015; Titov et al., 2016).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Sullivan et al., 2015
In the citing paper
“For example, eliminating environmental serine, limiting aspartate synthesis via mitochondrial inhibition, and ablating the mitochondrial folate pathway impairs purine biosynthesis (Ducker et al., 2016; Labuschagne et al., 2014; Sullivan et al., 2015).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Sullivan et al., 2015
In the citing paper
“Additionally, glutamine-derived aspartate plays a crucial role in hypoxic environments or environments with electron transport chain (ETC) impairment28.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [28]
In the citing paper
“Aspartate, which is derived from the transamination of glutamine to form glutamate, participates in pyrimidine and purine biosynthesis28.”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [28]
In the citing paper
“Upon ETC dysfunction, the cytosolic steps of the malate–aspartate shuttle can reverse to produce, rather than consume, cytosolic aspartate (42, 43).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [43]
In the citing paper
“Aspartate is used to support protein and nucleotide synthesis in proliferating cells and sustains proliferation in the face of OXPHOS impairment (214).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [214]
In the citing paper
“Time-restricted feeding restores both cycling of metabolic regulators such as cAMP response element-binding protein, mTOR and AMPK, and circadian clock gene expression (214).”
From Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease (2018) · cites this paper as [214]
In the citing paper
“In fact, aspartate biosynthesis has recently been shown to be critically dependent upon a cell’s ability to conduct oxidative phosphorylation (Birsoy et al., 2015; Sullivan et al., 2015).”
From The emerging hallmarks of cancer metabolism (2016) · cites this paper as Sullivan et al., 2015
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Citations
Cites
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
ROS function in redox signaling and oxidative stress
Schieber, M., & Chandel, N. S. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.034 · Cited by 6,931
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704
On Respiratory Impairment in Cancer Cells
Warburg, O. H. (1956) · Science · doi:10.1126/science.124.3215.269 · Cited by 3,472
Otto Warburg's contributions to current concepts of cancer metabolism
Koppenol, W. H., Bounds, P. L., & Dang, C. V. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3038 · Cited by 3,427
Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation
Lunt, S. Y., & Vander Heiden, M. G. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154237 · Cited by 3,057
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
Assessing mitochondrial dysfunction in cells
Brand, M. D., & Nicholls, D. G. (2011) · Biochemical Journal · doi:10.1042/bj20110162 · Cited by 2,436
Wallace, D. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3365 · Cited by 2,404
Brown and beige fat: Development, function and therapeutic potential
Harms, M., & Seale, P. (2013) · Nature Medicine · doi:10.1038/nm.3361 · Cited by 2,328
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Benej, M., Papandreou, I., & Denko, N. C. (2024) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2024.03.004 · Cited by 33
HIF1α-dependent uncoupling of glycolysis suppresses tumor cell proliferation
Urrutia, A. A., Mesa‐Ciller, C., Guajardo-Grence, A., Alkan, H. F., Soro-Arnáiz, I., Vandekeere, A., Campos, A. M. F., Igelmann, S., Fernández-Arroyo, L., Rinaldi, G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114103 · Cited by 31
Metabo-Devo: A metabolic perspective of development
Gándara, L., & Wappner, P. (2018) · Mechanisms of Development · doi:10.1016/j.mod.2018.02.004 · Cited by 31
Zhou, Y., Xu, Z., Quan, D. L., Zhang, F., Zhang, H., Xiao, T., Hou, S., Qiao, H., Harismendy, O., Wang, J. Y. J., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0349-2 · Cited by 31
The Effect of 2-Ketobutyrate on Mitochondrial Substrate-Level Phosphorylation
Bui, D., Ravasz, D., & Chinopoulos, C. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02759-8 · Cited by 27
Palaskas, N. J., Garcia, J. D., Shirazi, R., Shin, D. S., Puig-Saus, C., Braas, D., Ribas, A., & Graeber, T. G. (2019) · Cell Discovery · doi:10.1038/s41421-019-0130-x · Cited by 31
Prostate Cancer Energetics and Biosynthesis
Lin, C., Salzillo, T. C., Bader, D. A., Wilkenfeld, S. R., Awad, D., Pulliam, T. L., Dutta, P., Pudakalakatti, S., Titus, M. A., McGuire, S. E., et al. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-32656-2_10 · Cited by 33
The integrated stress response as a key pathway downstream of mitochondrial dysfunction
Bilen, M., Benhammouda, S., Slack, R. S., & Germain, M. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100555 · Cited by 38
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Xu, W., Patel, C. H., Zhao, L., Sun, I., Oh, M. H., Sun, I.-M., Helms, R. S., Wen, J., & Powell, J. D. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111987 · Cited by 33
Rupprecht, A., Moldzio, R., Mödl, B., & Pohl, E. E. (2019) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2019.03.006 · Cited by 32
Čiapaitė, J., van Roermund, C. W. T., Bosma, M., Gerrits, J., Houten, S. M., IJlst, L., Waterham, H. R., van Karnebeek, C., Wanders, R. J. A., Zwartkruis, F. J. T., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105047 · Cited by 30
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Zhong, X., Wu, H., Ouyang, C., Zhang, W., Shi, Y., Wang, Y.-C., Ann, D. K., Gwack, Y., Shang, W., & Sun, Z. (2023) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-23-0092 · Cited by 31
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Zheng, D., Zhou, H., Wang, H., Zhu, Y., Wu, Y., Li, Q., Li, T., & Liu, L. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02363-0 · Cited by 30
Sosnovski, K. E., Braun, T., Amir, A., Moshel, D., BenShoshan, M., VanDussen, K. L., Levhar, N., Abbas‐Egbariya, H., Beider, K., Ben-Yishay, R., et al. (2023) · Journal of Crohn s and Colitis · doi:10.1093/ecco-jcc/jjad006 · Cited by 30
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Wang, G., Cao, L., Li, S., Zhang, M., Li, Y., Duan, J., Li, Y., Hu, Z., Wu, J., Ni, J., et al. (2024) · npj Biofilms and Microbiomes · doi:10.1038/s41522-024-00582-w · Cited by 29
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Wang, H., Lu, J. L., Kulkarni, S., Zhang, W., Gorka, J. E., Mandel, J. A., Goetzman, E. S., & Prochownik, E. V. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005200 · Cited by 29
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Chinopoulos, C. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113218 · Cited by 29
Wilson, B. C., Boehme, L., Annibali, A., Hodgkinson, A., Carroll, T. S., Oakey, R. J., & Seitan, V. C. (2020) · Nature Communications · doi:10.1038/s41467-020-19205-x · Cited by 29
Metabo-reciprocity in cell mechanics: feeling the demands/feeding the demand
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Fang, H., Xie, A., Du, M., Li, X., Yang, K., Fu, Y., Yuan, X., Fan, R., Yu, W., Zhou, Z., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abl6992 · Cited by 29
Dai, T., Rosario, S. R., Katsuta, E., Dessai, A. S., Paterson, E. J., Novickis, A. T., Gomez, E. C., Zhu, B., Liu, S., Wang, H., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111756 · Cited by 29
Lee, S.-J., Wen, H., An, Y., Cha, J. W., Ko, Y., Hyberts, S. G., & Park, S. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02107 · Cited by 29
Bocca, C., Kane, M. S., Veyrat‐Durebex, C., Chupin, S., Alban, J., Nzoughet, J. K., Mao, M. L., de la Barca, J. M. C., Amati‐Bonneau, P., Bonneau, D., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29972-9 · Cited by 29
Tian, J., Luo, J., Zeng, X., Ke, C., Wang, Y., Liu, Z., Li, L., Zhang, Y., Hu, Z., & Yang, C. (2024) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2023-008226 · Cited by 28
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Gremke, N., Besong, I., Stroh, A., von Wichert, L., Witt, M., Elmshäuser, S., Wanzel, M., Fromm, M. F., Taudte, R. V., Schmatloch, S., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02180-4 · Cited by 31
Exogenous pyruvate facilitates cancer cell adaptation to hypoxia by serving as an oxygen surrogate
Yin, C., He, D., Chen, S., Tan, X., & Sang, N. (2016) · Oncotarget · doi:10.18632/oncotarget.10202 · Cited by 28
Zhang, R., Engel, A. L., Wang, Y., Li, B., Shen, W., Gillies, M. C., Chao, J. R., & Du, J. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00690 · Cited by 28
Zhong, B., Jiang, D., Hong, Y., Li, L., Qiu, L., Yang, R., Jin, X., Song, Y., Chen, C., & Li, B. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00399-x · Cited by 28
Ariyannur, P. S., Xing, G., Barry, E. S., Benford, B., Grunberg, N. E., & Sharma, P. (2021) · Aging and Disease · doi:10.14336/ad.2020.1015 · Cited by 28
Guo, L., Zhang, W., Xie, Y., Chen, X., Olmstead, E. E., Lian, M., Zhang, B., Zaytseva, Y. Y., Evers, B. M., Spielmann, H. P., et al. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0925 · Cited by 30
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Ward, N. P., Poff, A. M., Koutnik, A. P., & D’Agostino, D. P. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180061 · Cited by 30
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Bocca, C., Nzoughet, J. K., Leruez, S., Amati‐Bonneau, P., Ferré, M., Kane, M.-S., Veyrat‐Durebex, C., de la Barca, J. M. C., Chevrollier, A., Homedan, C., et al. (2018) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-23027 · Cited by 27
Shen, Y., Sherman, J. W., Chen, X., & Wang, R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.001379 · Cited by 27
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Gao, J., Guo, Z., Cheng, J., Sun, B. H., Yang, J., Li, H., Wu, S., Dong, F., & Yan, X. (2020) · Scientific Reports · doi:10.1038/s41598-020-78955-2 · Cited by 29
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AspSnFR: A genetically encoded biosensor for real-time monitoring of aspartate in live cells
Hellweg, L., Pfeifer, M., Tarnawski, M., Thing-Teoh, S., Chang, L., Bergner, A., Kress, J., Hiblot, J., Wiedmer, T., Superti‐Furga, G., et al. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.05.002 · Cited by 24
Mutant IDH and non-mutant chondrosarcomas display distinct cellular metabolomes
Pathmanapan, S., Ilkayeva, O., Martin, J. T., Loe, A. K. H., Zhang, H., Zhang, G., Newgard, C. B., Wunder, J. S., & Alman, B. A. (2021) · Cancer & Metabolism · doi:10.1186/s40170-021-00247-8 · Cited by 25
Links between mitochondrial retrograde response and mitophagy in pathogenic cell signalling
Strobbe, D., Sharma, S., & Campanella, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03770-5 · Cited by 24
Metabolic impact of pathogenic variants in the mitochondrial glutamyl‐tRNA synthetase EARS2
Ni, M., Black, L. F., Pan, C., Vu, H., Pei, J., Ko, B., Cai, L., Solmonson, A., Yang, C., Nugent, K. M., et al. (2021) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12387 · Cited by 23
Porto, V., Buceta, D., Domínguez, B., Carneiro, C., Borrajo, E., Fraile, M., Davila‐Ferreira, N., Arias, I. R., Blanco, J. M., Blanco, M. C., et al. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202113028 · Cited by 23
Metabolic reprogramming by miRNAs in the tumor microenvironment: Focused on immunometabolism
Alshahrani, S. H., Ibrahim, Y. S., Jalil, A. T., Altoum, A. A., Achmad, H., Zabibah, R. S., Gabr, G. A., Ramírez‐Coronel, A. A., Alameri, A. A., Qasim, Q. A., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1042196 · Cited by 24
Boykov, I. N., Montgomery, M. M., Hagen, J. T., Aruleba, R. T., McLaughlin, K., Coalson, H. S., Nelson, M. A. M., Pereyra, A. S., Ellis, J. M., Zeczycki, T. N., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-43963-5 · Cited by 23
The redox requirement and regulation during cell proliferation
Zhen, Z., Ren, J., & Zhu, J. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2023.12.010 · Cited by 23
Glutamine Metabolism and Prostate Cancer
Erb, H. H. H., Polishchuk, N., Stasyk, O. V., Kahya, U., Weigel, M. M., & Dubrovska, A. (2024) · Cancers · doi:10.3390/cancers16162871 · Cited by 23
Metformin sensitises hepatocarcinoma cells to methotrexate by targeting dihydrofolate reductase
Wang, Y., Lu, H. J., Sun, L., Chen, X., Wei, H., Suo, C., Feng, J., Yuan, M., Shen, S., Jia, W., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04199-1 · Cited by 22
Bassal, M. A., Samaraweera, S. E., Lim, K. S., Benard, B. A., Bailey, S., Kaur, S., Leo, P., Toubia, J., Thompson-Peach, C. A. L., Nguyen, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30223-9 · Cited by 24
Effects of metabolic cancer therapy on tumor microenvironment
Hyroššová, P., Milošević, M., Škoda, J., Vachtenheim, J., Jr., Rohlena, J., & Rohlenová, K. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.1046630 · Cited by 23
Su, Y., Yang, Y., & Huang, Y. K. (2016) · FEBS Journal · doi:10.1111/febs.13978 · Cited by 22
Asparagine, a critical limiting metabolite during glutamine starvation
Jiang, J., Pavlova, N. N., & Zhang, J. (2018) · Molecular & Cellular Oncology · doi:10.1080/23723556.2018.1441633 · Cited by 22
Audano, M., Pedretti, S., Crestani, M., Caruso, D., Fabiani, E. D., & Mitro, N. (2019) · FEBS Letters · doi:10.1002/1873-3468.13584 · Cited by 22
Madhusudhan, N., Hu, B., Mishra, P., Calva-Moreno, J. F., Patel, K., Boriack, R. L., Ready, J. M., & Nijhawan, D. (2019) · ACS Chemical Biology · doi:10.1021/acschembio.9b00734 · Cited by 22
Novel Mitochondria-targeted Drugs for Cancer Therapy
Fialová, J. L., Raudenská, M., Jakubek, M., Kejík, Z., Pavel Martasek, E., Babula, P., Matkowski, A., Filipenský, P., & Masařík, M. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557520666201118153242 · Cited by 22
Deficiency of malate-aspartate shuttle component SLC25A12 induces pulmonary metastasis
Alkan, H. F., Vesely, P. W., Hackl, H., Foßelteder, J., Schmidt, D. R., Heiden, M. G. V., Pichler, M., Höefler, G., & Bogner‐Strauß, J. G. (2020) · Cancer & Metabolism · doi:10.1186/s40170-020-00232-7 · Cited by 22
del Prado, L., Jaraíz-Rodríguez, M., Agrò, M., Zamora-Dorta, M., Azpiazu, N., Calleja, M., López-Manzaneda, M., de Juan‐Sanz, J., Fernández‐Rodrigo, A., Esteban, J. A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52968-1 · Cited by 21
The role of GOT1 in cancer metabolism
Peng, H., Dou, H., he, S., Xie, Y., Zhang, Q., & Zheng, J. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1519046 · Cited by 21
Metformin inhibits mitochondrial complex I in intestinal epithelium to promote glycaemic control
Sebo, Z. L., Chakrabarty, R. P., Grant, R. A., D’Alessandro, K. B., Koss, A., Blum, J. L. E., Davidson, S. M., Reczek, C. R., & Chandel, N. S. (2026) · Nature Metabolism · doi:10.1038/s42255-026-01530-y · Cited by 21
Physiological impact of in vivo stable isotope tracing on cancer metabolism
Grima-Reyes, M., Martinez-Turtos, A., Abramovich, I., Gottlieb, E., Chiche, J., & Ricci, J. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101294 · Cited by 24
Proleón, Á., Torrejón, D., Urra, F. A., Lazo, F., López-Torres, C., Fuentes-Retamal, S., Quispe, E., Samaniego, L. V. B., Agurto, A., Gavilán, R. G., et al. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.03.111 · Cited by 22
Listeria monocytogenes requires cellular respiration for NAD+ regeneration and pathogenesis
Rivera‐Lugo, R., Deng, D., Anaya-Sanchez, A., Tejedor‐Sanz, S., Tang, E., Reyes Ruiz, V. M., Smith, H. B., Titov, D. V., Sauer, J., Skaar, E. P., et al. (2022) · University of Chicago · doi:10.6082/xrgq5-r4x92 · Cited by 21
Roma, A., Tcheng, M., Ahmed, N., Walker, S., Jayanth, P., Minden, M. D., Hope, K. J., Rao, P. P. N., Luc, J., Doxey, A. C., et al. (2022) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-1032 · Cited by 23
Cabello-Rivera, D., Ortega‐Sáenz, P., Gao, L., Muñoz-Cabello, A. M., Bonilla, V., Schumacker, P. T., & López‐Barneo, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2202178119 · Cited by 21
Metadata
- Authors
- Sullivan, L. B., Gui, D. Y., Hosios, A. M., Bush, L. N., Freinkman, E., & Vander Heiden, M. G.
- Affiliations
- Koch Institute for Integrative Cancer Research At MIT (US)
- Whitehead Institute for Biomedical Research (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 162
- Issue
- 3
- Pages
- 552-563
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4522278
- OpenAlex
- W1553978925
- Cited by
- 1,173
- References
- 55
- Citations by year
- 2026: 106 · 2025: 95 · 2024: 97 · 2023: 120 · 2022: 151 · 2021: 129 · 2020: 128 · 2019: 90 · 2018: 98 · 2017: 75 · 2016: 71 · 2015: 11
- FWCI
- 28.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- U.S. Public Health Service (GG006413)
- National Cancer Institute (P30CA1405141, R01CA168653, P30CA014051)
- National Institute of General Medical Sciences (T32GM007753, T32GM007287)
- 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 › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- mitochondrial respiration, aspartate biosynthesis, cell proliferation, electron acceptors, pyruvate, alpha-ketobutyrate, respiratory chain deficiency, auxotrophy, alternative electron acceptors
- MeSH terms
- Adenosine Triphosphate, Aspartic Acid, Butyrates, Electrons, Humans, Mitochondria, Nucleotides, Cell Respiration, Pyruvic Acid, Cell Line, Tumor, Cell Proliferation
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