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.
“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]
Mitochondrial respiration remains important in proliferating cells, allowing production of biosynthetic precursors and electron acceptors that enable aspartate synthesis.
“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]
Genetic or epigenetic silencing of ASS1 provides an advantage to tumor cells by allowing them to preserve cellular aspartate, a poorly transported nutrient that can be a critical output of the TCA cycle to support de novo nucleotide synthesis and cell proliferation.
“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
Mitochondrial ATP production appears dispensable for many proliferating cells.
“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
Respiration serves an anabolic role for proliferating cells by regenerating NAD+ from NADH.
“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
Eliminating environmental serine, limiting aspartate synthesis via mitochondrial inhibition, and ablating the mitochondrial folate pathway impair purine biosynthesis.
“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
Glutamine-derived aspartate plays a crucial role in hypoxic environments or environments with electron transport chain impairment.
“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]
Aspartate derived from transamination of glutamine to form glutamate participates in pyrimidine and purine biosynthesis.
“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]
Upon ETC dysfunction, the cytosolic steps of the malate-aspartate shuttle can reverse to produce cytosolic aspartate.
“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]
Aspartate is used to support protein and nucleotide synthesis in proliferating cells and sustains proliferation in the face of OXPHOS impairment.
“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]
Time-restricted feeding restores both cycling of metabolic regulators such as cAMP response element-binding protein, mTOR and AMPK, and circadian clock gene expression.
“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]
Aspartate biosynthesis is critically dependent on a cell's ability to conduct oxidative phosphorylation.
“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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Cites
Warburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425 · see citing works
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 · see citing works
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 · see citing works
On Respiratory Impairment in Cancer Cells
Warburg, O. H. (1956) · Science · doi:10.1126/science.124.3215.269 · Cited by 3,472 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Assessing mitochondrial dysfunction in cells
Brand, M. D., & Nicholls, D. G. (2011) · Biochemical Journal · doi:10.1042/bj20110162 · Cited by 2,436 · see citing works
Wallace, D. C. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3365 · Cited by 2,404 · see citing works
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 · see citing works
Williamson, D., Lund, P., & Krebs, H. (1967) · Biochemical Journal · doi:10.1042/bj1030514 · Cited by 1,871 · see citing works
Mitochondrial metabolism and ROS generation are essential for Kras-mediated tumorigenicity
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. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003428107 · Cited by 1,742 · see citing works
Human Cells Lacking mtDNA: Repopulation with Exogenous Mitochondria by Complementation
King, M. P., & Attardi, G. M. (1989) · Science · doi:10.1126/science.2814477 · Cited by 1,659 · see citing works
Birsoy, K., Wang, T., Chen, W. W., Freinkman, E., Abu-Remaileh, M., & Sabatini, D. M. (2015) · Cell · doi:10.1016/j.cell.2015.07.016 · Cited by 1,388 · see citing works
Self-citationHuman cells lacking mtDNA: repopulation with exogenous mitochondria by complementation
(1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90040-d · Cited by 1,386 · see citing works
The impact of O2 availability on human cancer
Bertout, J. A., Patel, S. A., & Simon, M. C. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2540 · Cited by 1,365 · see citing works
Reductive carboxylation supports growth in tumour cells with defective mitochondria
Mullen, A. R., Wheaton, W. W., Jin, E. S., Chen, P.-H., Sullivan, L. B., Cheng, T., Yang, Y., Linehan, W. M., Chandel, N. S., & DeBerardinis, R. J. (2012) · Nature · doi:10.1038/nature10642 · Cited by 1,328 · see citing works
Self-citationNewmeyer, D. D., & Ferguson-Miller, S. M. (2003) · Cell · doi:10.1016/s0092-8674(03)00116-8 · Cited by 1,268 · see citing works
Glutamine and cancer: cell biology, physiology, and clinical opportunities
Hensley, C. T., Wasti, A. T., & DeBerardinis, R. J. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69600 · Cited by 1,262 · see citing works
Metformin inhibits mitochondrial complex I of cancer cells to reduce tumorigenesis
Wheaton, W. W., Weinberg, S. E., Hamanaka, R. B., Soberanes, S., Sullivan, L. B., Anso, E., Glasauer, A., Dufour, E., Mutlu, G. M., Budigner, G. S., et al. (2014) · eLife · doi:10.7554/elife.02242 · Cited by 1,105 · see citing works
Self-citationThe Metabolism of Carcinoma Cells
Warburg, O. H. (1925) · The Journal of Cancer Research · doi:10.1158/jcr.1925.148 · Cited by 1,005 · see citing works
mtDNA mutations increase tumorigenicity in prostate cancer
Petros, J. A., Baumann, A. K., Ruiz‐Pesini, E., Amin, M. B., Sun, C. Q., Hall, J., Lim, S.-D., Issa, M. M., Flanders, W. D., Hosseini, S. H., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408894102 · Cited by 834 · see citing works
Tan, A. S., Baty, J. W., Dong, L.-F., Bezawork-Geleta, A., Endaya, B., Goodwin, J., Bajzikova, M., Kovarova, J., Peterka, M., Yan, B., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.003 · Cited by 785 · see citing works
Cancer metabolism: facts, fantasy, and fiction
Zu, X. L., & Guppy, M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.11.136 · Cited by 618 · see citing works
Mitochondrial tumour suppressors: a genetic and biochemical update
Gottlieb, E., & Tomlinson, I. P. M. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1737 · Cited by 617 · see citing works
Shackelford, D. B., Abt, E., Gerken, L., Vasquez, D. S., Seki, A., Leblanc, M., Wei, L., Fishbein, M. C., Czernin, J., Mischel, P. S., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2012.12.008 · Cited by 585 · see citing works
Tracing compartmentalized NADPH metabolism in the cytosol and mitochondria of mammalian cells
Lewis, C. A., Parker, S. J., Fiske, B. P., McCloskey, D., Gui, D. Y., Green, C. R., Vokes, N. I., Feist, A. M., Vander Heiden, M. G., & Metallo, C. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.008 · Cited by 562 · see citing works
Self-citationOn respiratory impairment in cancer cells
Weinhouse, S. (1956) · Science · doi:10.1126/science.124.3215.267 · Cited by 554 · see citing works
Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
Hung, Y. P., Albeck, J. G., Tantama, M., & Yellen, G. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.012 · Cited by 509 · see citing works
Zhao, Y., Hu, Q., Cheng, F., Su, N., Wang, A., Zou, Y., Hu, H., Chen, X., Hai‐Meng, Z. H. O. U., Huang, X., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.009 · Cited by 434 · see citing works
Fan, J., Kamphorst, J. J., Mathew, R., Chung, M. K., White, E., Shlomi, T., & Rabinowitz, J. D. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.65 · Cited by 428 · see citing works
Heterogeneity of tumor-induced gene expression changes in the human metabolic network
Hu, J., Locasale, J. W., Bielas, J. H., O'Sullivan, J., Sheahan, K., Cantley, L. C., Heiden, M. G. V., & Vitkup, D. (2013) · Nature Biotechnology · doi:10.1038/nbt.2530 · Cited by 407 · see citing works
Uber den Stoffwechsel der Karzinomezellen
Warburg, O. (1924) · Medical Entomology and Zoology · Cited by 401 · see citing works
Reductive glutamine metabolism is a function of the α-ketoglutarate to citrate ratio in cells
Fendt, S.-M., Bell, E. L., Keibler, M. A., Olenchock, B. A., Mayers, J. R., Wasylenko, T. M., Vokes, N. I., Guarente, L., Heiden, M. G. V., & Stephanopoulos, G. (2013) · Nature Communications · doi:10.1038/ncomms3236 · Cited by 364 · see citing works
[27] Isolation of human cell lines lacking mitochondrial DNA
King, M. P., & Attardi, G. M. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)64029-4 · Cited by 355 · see citing works
Mullen, A. R., Hu, Z., Shi, X., Jiang, L., Boroughs, L. K., Kovacs, Z., Boriack, R., Rakheja, D., Sullivan, L. B., Linehan, W. M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.037 · Cited by 337 · see citing works
Self-citationSchleyer, M., SCHMIDT, B., & Neupert, W. (1982) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1982.tb06657.x · Cited by 298 · see citing works
Pyruvate Kinase Isoform Expression Alters Nucleotide Synthesis to Impact Cell Proliferation
Lunt, S. Y., Muralidhar, V., Hosios, A. M., Israelsen, W. J., Gui, D. Y., Newhouse, L., Ogrodzinski, M. P., Hecht, V. C., Xu, K., Acevedo, P. N. M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.027 · Cited by 259 · see citing works
Self-citationZhang, X., Fryknäs, M., Hernlund, E., Fayad, W., Milito, A. D., Olofsson, M. H., Gogvadze, V. G., Dang, L. H., Påhlman, S., Kunz‐Schughart, L. A., et al. (2014) · Nature Communications · doi:10.1038/ncomms4295 · Cited by 253 · see citing works
Park, J. S., Sharma, L. K., Li, H., Xiang, R., Holstein, D. M., Wu, J., Lechleiter, J. D., Naylor, S. L., Deng, J. J., Lü, J., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp069 · Cited by 243 · see citing works
Glutamine: a major energy source for cultured mammalian cells.
Zielke, H. R., Zielke, C. L., & Pt, O. (1984) · PubMed · Cited by 240 · see citing works
Famine versus feast: understanding the metabolism of tumors in vivo
Mayers, J. R., & Heiden, M. G. V. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.01.004 · Cited by 185 · see citing works
Membrane Potential-Driven Protein Import into Mitochondria
Geissler, A., Krimmer, T., Bömer, U., Guiard, B., Rassow, J., & Pfanner, N. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.11.3977 · Cited by 144 · see citing works
On auxotrophy for pyrimidines of respiration‐deficient chick embryo cells
Gregoire, M., Morais, R., Quilliam, M. A., & GRAVEL, D. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08249.x · Cited by 110 · see citing works
NAD+ as a Signaling Molecule Modulating MetabolismPreprint
Cantó, C., & Auwerx, J. H. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2012.76.010439 · Cited by 109 · see citing works
(1994) · PubMed · Cited by 109 · see citing works
The pathway of glutamine and glutamate oxidation in isolated mitochondria from mammalian cells
Kovačević, Z. (1971) · Biochemical Journal · doi:10.1042/bj1250757 · Cited by 95 · see citing works
Chen, W. W., Birsoy, K., Mihaylova, M. M., Snitkin, H., Stasinski, I., Yücel, B., Bayraktar, E. C., Carette, J. E., Clish, C. B., Brummelkamp, T. R., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.046 · Cited by 79 · see citing works
Hayashi, J., Takemitsu, M., & Nonaka, I. (1992) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01233159 · Cited by 70 · see citing works
den Bogert, C. V., Spelbrink, J. N., & Dekker, L. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041520323 · Cited by 45 · see citing works
Howell, N., & Sager, R. (1979) · Somatic Cell and Molecular Genetics · doi:10.1007/bf01542645 · Cited by 41 · see citing works
Pyruvate blocks expression of sensitivity to antimycin A and chloramphenicol
Harris, M. (1980) · Somatic Cell Genetics · doi:10.1007/bf01538969 · Cited by 30 · see citing works
Löffler, M., & Schneider, F. (1982) · Molecular and Cellular Biochemistry · doi:10.1007/bf00227608 · Cited by 15 · see citing works
Kroll, W., Loffler, M., & Schneider, F. (1983) · Zeitschrift für Naturforschung C · doi:10.1515/znc-1983-7-818 · Cited by 5 · see citing works
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The emerging hallmarks of cancer metabolism
Pavlova, N. N., & Thompson, C. B. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.12.006 · Cited by 5,926 · see citing works
The Warburg Effect: How Does it Benefit Cancer Cells?
Liberti, M. V., & Locasale, J. W. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.001 · Cited by 5,150 · 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
Understanding the Intersections between Metabolism and Cancer Biology
Heiden, M. G. V., & DeBerardinis, R. J. (2017) · Cell · doi:10.1016/j.cell.2016.12.039 · Cited by 2,316 · see citing works
One-Carbon Metabolism in Health and Disease
Ducker, G. S., & Rabinowitz, J. D. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.009 · Cited by 2,239 · see citing works
From Krebs to clinic: glutamine metabolism to cancer therapy
Altman, B. J., Stine, Z. E., & Dang, C. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.71 · Cited by 2,119 · see citing works
The multifaceted contributions of mitochondria to cellular metabolism
Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935 · see citing works
Vyas, S., Zaganjor, E., & Haigis, M. C. (2016) · Cell · doi:10.1016/j.cell.2016.07.002 · Cited by 1,735 · see citing works
Multi-dimensional Roles of Ketone Bodies in Fuel Metabolism, Signaling, and Therapeutics
Puchalska, P., & Crawford, P. A. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.12.022 · Cited by 1,617 · see citing works
The hallmarks of cancer metabolism: still emerging
Pavlova, N. N., Zhu, J., & Thompson, C. B. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.01.007 · Cited by 1,418 · see citing works
Birsoy, K., Wang, T., Chen, W. W., Freinkman, E., Abu-Remaileh, M., & Sabatini, D. M. (2015) · Cell · doi:10.1016/j.cell.2015.07.016 · Cited by 1,388 · see citing works
Self-citationMitochondrial metabolism and cancer
Porporato, P. E., Filigheddu, N., Pedro, J. M. B., Kroemer, G., & Galluzzi, L. (2017) · Cell Research · doi:10.1038/cr.2017.155 · Cited by 1,292 · see citing works
Zong, W., Rabinowitz, J. D., & White, E. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.011 · Cited by 1,287 · see citing works
Metabolic regulation of cell growth and proliferation
Zhu, J., & Thompson, C. B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0123-5 · Cited by 1,106 · 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
Targeting Metabolism for Cancer Therapy
Luengo, A., Gui, D. Y., & Vander Heiden, M. G. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.08.028 · Cited by 971 · see citing works
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Molina, J. R., Sun, Y., Protopopova, M., Gera, S., Bandi, M., Bristow, C., McAfoos, T., Morlacchi, P., Ackroyd, J., Agip, A.-N. A., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0052-4 · Cited by 928 · see citing works
Glutaminolysis: A Hallmark of Cancer Metabolism
Yang, L., Venneti, S., & Nagrath, D. (2017) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071516-044546 · Cited by 859 · see citing works
Lieu, E. L., Nguyen, T. A., Rhyne, S., & Kim, J. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0375-3 · Cited by 827 · see citing works
Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease
Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787 · see citing works
Mitochondrial Metabolism as a Target for Cancer Therapy
Vasan, K., Werner, M., & Chandel, N. S. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.06.019 · Cited by 746 · see citing works
Environment impacts the metabolic dependencies of Ras-driven non-small cell lung cancer
Davidson, S. M., Papagiannakopoulos, T., Olenchock, B. A., Heyman, J. E., Keibler, M. A., Luengo, A., Bauer, M. R., Jha, A. K., O’Brien, J. P., Pierce, K. A., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.01.007 · Cited by 737 · see citing works
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Ma, E. H., Bantug, G., Griss, T., Condotta, S., Johnson, R. M., Samborska, B., Mainolfi, N., Suri, V., Guak, H., Balmer, M. L., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.12.011 · Cited by 657 · see citing works
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Metabolites and the Tumour Microenvironment: From Cellular Mechanisms to Systemic Metabolism
Elia, I., & Haigis, M. C. (2021) · Nature Metabolism · doi:10.1038/s42255-020-00317-z · Cited by 651 · see citing works
Cancer cell metabolism: the essential role of the nonessential amino acid, glutamine
Zhang, J., Pavlova, N. N., & Thompson, C. B. (2017) · The EMBO Journal · doi:10.15252/embj.201696151 · Cited by 651 · see citing works
Mitochondrial metabolism promotes adaptation to proteotoxic stress
Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645 · see citing works
Multifaceted mitochondria: moving mitochondrial science beyond function and dysfunction
Monzel, A. S., Enrı́quez, J. A., & Picard, M. A. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00783-1 · Cited by 618 · see citing works
Bordt, E. A., Clerc, P., Roelofs, B. A., Saladino, A. J., Tretter, L., Ádám‐Vizi, V., Cherok, E., Khalil, A., Yadava, N., Ge, S. X., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.020 · Cited by 598 · see citing works
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Mayers, J. R., Torrence, M. E., Danai, L. V., Papagiannakopoulos, T., Davidson, S. M., Bauer, M. R., Lau, A. N., Ji, B. W., Dixit, P. D., Hosios, A. M., et al. (2016) · Science · doi:10.1126/science.aaf5171 · Cited by 582 · see citing works
Self-citationVardhana, S. A., Hwee, M. A., Berisa, M., Wells, D. K., Yost, K. E., King, B., Smith, M., Herrera, P. S., Chang, H. Y., Satpathy, A. T., et al. (2020) · Nature Immunology · doi:10.1038/s41590-020-0725-2 · Cited by 575 · see citing works
A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate
Pacold, M. E., Brimacombe, K. R., Chan, S. H., Rohde, J. M., Lewis, C. A., Swier, L. J. Y. M., Possemato, R., Chen, W. W., Sullivan, L. B., Fiske, B. P., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2070 · Cited by 553 · see citing works
Self-citationIncreased demand for NAD(+) relative to ATP drives aerobic glycolysis
Luengo, A., Li, Z., Gui, D. Y., Sullivan, L. B., Zagorulya, M., Do, B. T., Ferreira, R., Naamati, A., Ali, A., Lewis, C. A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.012 · Cited by 547 · see citing works
Self-citationRegulation and function of the mammalian tricarboxylic acid cycle
Arnold, P. K., & Finley, L. W. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102838 · Cited by 535 · see citing works
Kuntz, E. M., Baquero, P., Michie, A. M., Dunn, K. M., Tardito, S., Holyoake, T. L., Helgason, G. V., & Gottlieb, E. (2017) · Nature Medicine · doi:10.1038/nm.4399 · Cited by 533 · see citing works
Titov, D. V., Cracan, V., Goodman, R. P., Peng, J., Grabarek, Z., & Mootha, V. K. (2016) · Science · doi:10.1126/science.aad4017 · Cited by 518 · see citing works
TCA Cycle and Mitochondrial Membrane Potential Are Necessary for Diverse Biological Functions
Martínez‐Reyes, I., Diebold, L. P., Kong, H., Schieber, M., Huang, H., Hensley, C. T., Mehta, M., Wang, T., Santos, J. H., Woychik, R. P., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.12.002 · Cited by 512 · see citing works
Energy metabolism and inflammation in brain aging and Alzheimer’s disease
Yin, F., Sancheti, H., Patil, I., & Cadenas, E. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.200 · Cited by 538 · see citing works
New aspects of amino acid metabolism in cancer
Vettore, L. A., Westbrook, R. L., & Tennant, D. A. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0620-5 · Cited by 503 · see citing works
Absolute quantification of matrix metabolites reveals the dynamics of mitochondrial metabolism
Chen, W. W., Freinkman, E., Wang, T., Birsoy, K., & Sabatini, D. M. (2016) · Cell · doi:10.1016/j.cell.2016.07.040 · Cited by 500 · see citing works
Self-citationBernardi, P., Gerle, C., Halestrap, A. P., Jonas, E. A., Karch, J. M., Mnatsakanyan, N., Pavlov, E. V., Sheu, S., & Soukas, A. A. (2023) · Cell Death and Differentiation · doi:10.1038/s41418-023-01187-0 · Cited by 482 · see citing works
Metabolic pathways in T cell activation and lineage differentiation
Almeida, L., Lochner, M., Berod, L., & Sparwasser, T. D. (2016) · Seminars in Immunology · doi:10.1016/j.smim.2016.10.009 · Cited by 475 · see citing works
Metabolic recycling of ammonia via glutamate dehydrogenase supports breast cancer biomass
Spinelli, J. B., Yoon, H., Ringel, A. E., Jeanfavre, S., Clish, C. B., & Haigis, M. C. (2017) · Science · doi:10.1126/science.aam9305 · Cited by 468 · see citing works
Aspartate is a limiting metabolite for cancer cell proliferation under hypoxia and in tumours
Garcia-Bermudez, J., Baudrier, L., La, K., Zhu, X. G., Fidelin, J., Sviderskiy, V. O., Papagiannakopoulos, T., Molina, H., Snuderl, M., Lewis, C. A., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0118-z · Cited by 442 · see citing works
Mitochondrial dysfunction remodels one-carbon metabolism in human cells
Bao, X. R., Ong, S., Goldberger, O., Peng, J., Sharma, R., Thompson, D. A., Vafai, S. B., Cox, A. G., Marutani, E., Ichinose, F., et al. (2016) · eLife · doi:10.7554/elife.10575 · Cited by 439 · see citing works
Vascular stiffness mechanoactivates YAP/TAZ-dependent glutaminolysis to drive pulmonary hypertension
Bertero, T., Oldham, W. M., Cottrill, K. A., Pisano, S., Vanderpool, R. R., Yu, Q., Zhao, J., Tai, Y., Tang, Y., Zhang, Y.-Y., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci86387 · Cited by 438 · see citing works
Mitochondrial Biogenesis and Proteome Remodeling Promote One-Carbon Metabolism for T Cell Activation
Ron-Harel, N., Santos, D., Ghergurovich, J. M., Sage, P. T., Reddy, A., Lovitch, S. B., Dephoure, N., Satterstrom, F. K., Sheffer, M., Spinelli, J. B., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.007 · Cited by 429 · see citing works
The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
Sweetlove, L. J., & Fernie, A. R. (2018) · Nature Communications · doi:10.1038/s41467-018-04543-8 · Cited by 421 · see citing works
Olivares, O., Mayers, J. R., Gouirand, V., Torrence, M. E., Gicquel, T., Borge, L., Lac, S., Roques, J., Lavaut, M.-N., Berthezène, P., et al. (2017) · Nature Communications · doi:10.1038/ncomms16031 · Cited by 413 · see citing works
The importance of serine metabolism in cancer
Mattaini, K. R., Sullivan, M. R., & Heiden, M. G. V. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604085 · Cited by 409 · see citing works
Yap, T. A., Daver, N. G., Mahendra, M., Zhang, J., Kamiya-Matsuoka, C., Meric‐Bernstam, F., Kantarjian, H. M., Ravandi, F., Collins, M., Francesco, M. E. D., et al. (2023) · Nature Medicine · doi:10.1038/s41591-022-02103-8 · Cited by 408 · 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
Self-citationTumor-Stroma Mechanics Coordinate Amino Acid Availability to Sustain Tumor Growth and Malignancy
Bertero, T., Oldham, W. M., Grasset, E. M., Bourget, I., Boulter, E., Pisano, S., Hofman, P., Bellvert, F., Meneguzzi, G., Bulavin, D. V., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.09.012 · Cited by 393 · see citing works
The ERK and JNK pathways in the regulation of metabolic reprogramming
Papa, S., Choy, P. M., & Bubici, C. (2018) · Oncogene · doi:10.1038/s41388-018-0582-8 · Cited by 381 · see citing works
Guo, J. Y., Teng, X., Laddha, S. V., Ma, S., Nostrand, S. C. V., Yang, Y., Khor, S., Chan, C. S., Rabinowitz, J. D., & White, E. (2016) · Genes & Development · doi:10.1101/gad.283416.116 · Cited by 373 · see citing works
Mitochondrial ubiquinol oxidation is necessary for tumour growth
Martínez‐Reyes, I., Cardona, L. R., Kong, H., Vasan, K., McElroy, G. S., Werner, M., Kihshen, H. G., Reczek, C. R., Weinberg, S. E., Gao, P., et al. (2020) · Nature · doi:10.1038/s41586-020-2475-6 · Cited by 368 · see citing works
Ma, E. H., Verway, M. J., Johnson, R. M., Roy, D. G., Steadman, M., Hayes, S., Williams, K. S., Sheldon, R. D., Samborska, B., Kosinski, P. A., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.09.003 · Cited by 364 · see citing works
Mitochondrial electron transport chain is necessary for NLRP3 inflammasome activation
Billingham, L. K., Stoolman, J. S., Vasan, K., Rodriguez, A. E., Poor, T. A., Szibor, M., Jacobs, H. T., Reczek, C. R., Rashidi, A., Zhang, P., et al. (2022) · Nature Immunology · doi:10.1038/s41590-022-01185-3 · Cited by 360 · see citing works
The pyruvate-lactate axis modulates cardiac hypertrophy and heart failure
Cluntun, A. A., Badolia, R., Lettlová, S., Parnell, K. M., Shankar, T. S., Diakos, N., Olson, K. A., Taleb, I., Tatum, S. M., Berg, J. A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.12.003 · Cited by 345 · see citing works
As Extracellular Glutamine Levels Decline, Asparagine Becomes an Essential Amino Acid
Pavlova, N. N., Hui, S., Ghergurovich, J. M., Fan, J., Intlekofer, A. M., White, R. M., Rabinowitz, J. D., Thompson, C. B., & Zhang, J. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.12.006 · Cited by 341 · see citing works
Aspartate is an endogenous metabolic limitation for tumour growth
Sullivan, L. B., Luengo, A., Danai, L. V., Bush, L. N., Diehl, F. F., Hosios, A. M., Lau, A. N., Elmiligy, S., Malstrom, S. E., Lewis, C. A., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0125-0 · Cited by 339 · see citing works
Self-citationMitochondrial fusion supports increased oxidative phosphorylation during cell proliferation
Yao, C.-H., Wang, R., Wang, Y., Kung, C.-P., Weber, J. D., & Patti, G. J. (2019) · eLife · doi:10.7554/elife.41351 · Cited by 338 · see citing works
LIN28 Regulates Stem Cell Metabolism and Conversion to Primed Pluripotency
Zhang, J., Ratanasirintrawoot, S., Chandrasekaran, S., Wu, Z., Ficarro, S. B., Yu, C., Ross, C. A., Cacchiarelli, D., Xia, Q., Seligson, M. T., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.05.009 · Cited by 334 · see citing works
Metabolic signaling in T cells
Shyer, J. A., Flavell, R. A., & Bailis, W. (2020) · Cell Research · doi:10.1038/s41422-020-0379-5 · Cited by 334 · see citing works
Finley, L. W. S. (2023) · Cell · doi:10.1016/j.cell.2023.01.038 · Cited by 331 · see citing works
Gui, D. Y., Sullivan, L. B., Luengo, A., Hosios, A. M., Bush, L. N., Gitego, N., Davidson, S. M., Freinkman, E., Thomas, C. J., & Vander Heiden, M. G. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.006 · Cited by 323 · see citing works
Self-citationControl of intestinal stem cell function and proliferation by mitochondrial pyruvate metabolism
Schell, J. C., Wisidagama, D. R., Bensard, C., Zhao, H., Wei, P., Tanner, J., Flores, A., Mohlman, J., Sorensen, L. K., Earl, C. S., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3593 · Cited by 322 · see citing works
Rewiring urea cycle metabolism in cancer to support anabolism
Keshet, R., Szlosarek, P. W., Carracedo, A., & Erez, A. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0054-z · Cited by 322 · see citing works
Lou, T., Sethuraman, D., Dospoy, P. D., Srivastva, P., Kim, H. S., Kim, J., Ma, X., Chen, P.-H., Huffman, K. E., Frink, R. E., et al. (2015) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-14-0287 · Cited by 315 · see citing works
Metabolomics and mass spectrometry imaging reveal channeled de novo purine synthesis in cells
Pareek, V., Tian, H., Winograd, N., & Benkovic, S. J. (2020) · Science · doi:10.1126/science.aaz6465 · Cited by 312 · see citing works
Muir, A., Danai, L. V., Gui, D. Y., Waingarten, C. Y., Lewis, C. A., & Vander Heiden, M. G. (2017) · eLife · doi:10.7554/elife.27713 · Cited by 311 · see citing works
Self-citationLow glycaemic diets alter lipid metabolism to influence tumour growth
Lien, E. C., Westermark, A. M., Zhang, Y., Yuan, C., Li, Z., Lau, A. N., Sapp, K. M., Wolpin, B. M., & Heiden, M. G. V. (2021) · Nature · doi:10.1038/s41586-021-04049-2 · Cited by 311 · see citing works
The mitochondrial respiratory chain is essential for haematopoietic stem cell function
Ansó, E., Weinberg, S. E., Diebold, L. P., Thompson, B. J., Malinge, S., Schumacker, P. T., Liu, X., Zhang, Y., Shao, Z., Steadman, M., et al. (2017) · Nature Cell Biology · doi:10.1038/ncb3529 · Cited by 310 · see citing works
A non-canonical tricarboxylic acid cycle underlies cellular identity
Arnold, P. K., Jackson, B. T., Paras, K. I., Brunner, J. S., Hart, M. L., Newsom, O. J., Alibeckoff, S. P., Endress, J., Drill, E., Sullivan, L. B., et al. (2022) · Nature · doi:10.1038/s41586-022-04475-w · Cited by 304 · see citing works
Self-citationBeckervordersandforth, R., Ebert, B., Schäffner, I., Moss, J., Fiebig, C., Shin, J., Moore, D. L., Ghosh, L., Trinchero, M. F., Stockburger, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.017 · Cited by 303 · see citing works
Slow TCA flux and ATP production in primary solid tumours but not metastases
Bartman, C. R., Weilandt, D. R., Shen, Y., Lee, W. D., Han, Y., TeSlaa, T., Jankowski, C. S. R., Samarah, L., Park, N. R., da Silva-Diz, V., et al. (2023) · Nature · doi:10.1038/s41586-022-05661-6 · Cited by 299 · see citing works
Bajzíková, M., Kovářová, J., Coelho, A. R., Boukalová, Š., Oh, S., Rohlenová, K., Švec, D., Hubáčková, S., Endaya, B., Judasová, K., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.10.014 · Cited by 296 · see citing works
Dong, L., Kovářová, J., Bajzíková, M., Bezawork‐Geleta, A., Švec, D., Endaya, B., Sachaphibulkij, K., Coelho, A. R., Šebková, N., Růžičková, A., et al. (2017) · eLife · doi:10.7554/elife.22187 · Cited by 294 · see citing works
Differential Glutamate Metabolism in Proliferating and Quiescent Mammary Epithelial Cells
Coloff, J. L., Murphy, J. P., Braun, C. R., Harris, I. S., Shelton, L. M., Kami, K., Gygi, S. P., Selfors, L. M., & Brugge, J. S. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.03.016 · Cited by 288 · see citing works
α-Ketoglutarate Accelerates the Initial Differentiation of Primed Human Pluripotent Stem Cells
TeSlaa, T., Chaikovsky, A. C., Lipchina, I., Escobar, S. L., Hochedlinger, K., Huang, J., Graeber, T. G., Braas, D., & Teitell, M. A. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.002 · Cited by 287 · see citing works
Mitochondrial translation requires folate-dependent tRNA methylation
Morscher, R. J., Ducker, G. S., Li, H., Mayer, J., Gitai, Z., Sperl, W., & Rabinowitz, J. D. (2018) · Nature · doi:10.1038/nature25460 · Cited by 278 · see citing works
Metformin as an Anticancer Agent
Vancura, A., Bu, P., Bhagwat, M., Zeng, J., & Vancurova, I. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.07.006 · Cited by 274 · see citing works
The functional roles of TCA cycle metabolites in cancer
Eniafe, J., & Jiang, S. (2021) · Oncogene · doi:10.1038/s41388-020-01639-8 · Cited by 274 · see citing works
The Influence of Metabolism on Drug Response in Cancer
Zaal, E. A., & Berkers, C. R. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00500 · Cited by 272 · see citing works
Fueling the Cell Division Cycle
Salazar‐Roa, M., & Malumbres, M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.08.009 · Cited by 270 · see citing works
Asparagine couples mitochondrial respiration to ATF4 activity and tumor growth
Krall, A. S., Mullen, P. J., Surjono, F., Momcilovic, M., Schmid, E. W., Halbrook, C. J., Thambundit, A., Mittelman, S. D., Lyssiotis, C. A., Shackelford, D. B., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.02.001 · Cited by 266 · see citing works
Kodama, M. (2020) · Institutional Repositories DataBase (IRDB) · Cited by 263 · see citing works
Baccelli, I., Gareau, Y., Lehnertz, B., Gingras, S., Spinella, J.-F., Corneau, S., Mayotte, N., Girard, S., Fréchette, M., Blouin-Chagnon, V., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.06.003 · Cited by 257 · see citing works
MYC promotes tryptophan uptake and metabolism by the kynurenine pathway in colon cancerPreprint
Venkateswaran, N., Lafita‐Navarro, M. C., Hao, Y.-H., Kilgore, J. A., Perez‐Castro, L., Braverman, J., Borenstein‐Auerbach, N., Kim, M. G., Lesner, N. P., Mishra, P., et al. (2019) · Genes & Development · doi:10.1101/gad.327056.119 · Cited by 254 · see citing works
Glutamine Metabolism Regulates Proliferation and Lineage Allocation in Skeletal Stem Cells
Yu, Y., Newman, H., Shen, L., Sharma, D., Hu, G., Mirando, A. J., Zhang, H., Knudsen, E., Zhang, G.-F., Hilton, M. J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.016 · Cited by 253 · see citing works
Lactate activates the mitochondrial electron transport chain independently of its metabolism
Cai, X., Ng, C., Jones, O., Fung, T. S., Ryu, K. W., Li, D., & Thompson, C. B. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.09.034 · Cited by 253 · see citing works
Borst, P. (2020) · IUBMB Life · doi:10.1002/iub.2367 · Cited by 252 · see citing works
Kalyanaraman, B. (2017) · Redox Biology · doi:10.1016/j.redox.2017.04.018 · Cited by 246 · see citing works
The Warburg effect: a signature of mitochondrial overload
Wang, Y., & Patti, G. J. (2023) · Trends in Cell Biology · doi:10.1016/j.tcb.2023.03.013 · Cited by 243 · see citing works
Sullivan, M. R., Mattaini, K. R., Dennstedt, E. A., Nguyen, A. A., Sivanand, S., Reilly, M. F., Meeth, K. M., Muir, A., Darnell, A. M., Bosenberg, M., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.02.015 · Cited by 242 · see citing works
Mick, E., Titov, D. V., Skinner, O. S., Sharma, R., Jourdain, A. A., & Mootha, V. K. (2020) · eLife · doi:10.7554/elife.49178 · Cited by 241 · see citing works
Heterogeneity in Cancer Metabolism: New Concepts in an Old Field
Gentric, G., Mieulet, V., & Mechta‐Grigoriou, F. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6750 · Cited by 237 · see citing works
Distinct modes of mitochondrial metabolism uncouple T cell differentiation and function
Bailis, W., Shyer, J. A., Zhao, J., García‐Cañaveras, J. C., Khazal, F. J. A., Qu, R., Steach, H. R., Bielecki, P., Khan, O. M., Jackson, R. P., et al. (2019) · Nature · doi:10.1038/s41586-019-1311-3 · Cited by 233 · see citing works
Coordinative metabolism of glutamine carbon and nitrogen in proliferating cancer cells under hypoxia
Wang, Y., Bai, C., Ruan, Y., Liu, M., Chu, Q., Qiu, L., Yang, C., & Li, B. (2019) · Nature Communications · doi:10.1038/s41467-018-08033-9 · Cited by 232 · see citing works
A Role for p53 in the Adaptation to Glutamine Starvation through the Expression of SLC1A3
Tajan, M., Hock, A. K., Blagih, J., Robertson, N. A., Labuschagne, C. F., Kruiswijk, F., Humpton, T. J., Adams, P. D., & Vousden, K. H. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.005 · Cited by 230 · see citing works
- 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 · 2014: 1
- 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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