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Serine, glycine and one‑carbon metabolism in cancer (Review)
Open accessAbstract
Serine/glycine biosynthesis and one‑carbon metabolism are crucial in sustaining cancer cell survival and rapid proliferation, and of high clinical relevance. Excessive activation of serine/glycine biosynthesis drives tumorigenesis and provides a single carbon unit for one‑carbon metabolism. One‑carbon metabolism, which is a complex cyclic metabolic network based on the chemical reaction of folate compounds, provides the necessary proteins, nucleic acids, lipids and other biological macromolecules to support tumor growth. Moreover, one‑carbon metabolism also maintains the redox homeostasis of the tumor microenvironment and provides substrates for the methylation reaction. The present study reviews the role of key enzymes with tumor‑promoting functions and important intermediates that are physiologically relevant to tumorigenesis in serine/glycine/one‑carbon metabolism pathways. The related regulatory mechanisms of action of the key enzymes and important intermediates in tumors are also discussed. It is hoped that investigations into these pathways will provide new translational opportunities for human cancer drug development, dietary interventions, and biomarker identification.
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In the citing paper
“Glycolysis supplies one-carbon metabolism through serine biosynthesis from 3-phosphoglycerate [37,49].”
From 20-Hydroxyecdysone Boosts Energy Production and Biosynthetic Processes in Non-Transformed Mouse Cells (2024) · cites this paper as [49]
In the citing paper
“The serine biosynthesis mediated by three enzymes—PSAT1, PHGDH, and PSAT1—“opens the gates” to one-carbon metabolism, whereas its central part—the folate cycle—mediates the re-distribution of one-carbon groups to acceptors [46] (Figure 11).”
From 20-Hydroxyecdysone Confers Antioxidant and Antineoplastic Properties in Human Non-Small Cell Lung Cancer Cells (2023) · cites this paper as [46]
In the citing paper
“Different oncogenes and oncosupressors have a critical impact on these metabolic pathways [20,40,46,47,75,76].”
From 20-Hydroxyecdysone Confers Antioxidant and Antineoplastic Properties in Human Non-Small Cell Lung Cancer Cells (2023) · cites this paper as [46]
In the citing paper
“Transcription factors c-Myc and ATF4 are two master-regulators of glycolysis, respiration, and one-carbon metabolism [44,45,46,49].”
From 20-Hydroxyecdysone Confers Antioxidant and Antineoplastic Properties in Human Non-Small Cell Lung Cancer Cells (2023) · cites this paper as [46]
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2 retracted
Samanta, D., Park, Y., Andrabi, S. A., Shelton, L. M., Gilkes, D. M., & Semenza, G. L. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-0530 · Cited by 242
RetractedmiR-424 targets AKT3 and PSAT1 and has a tumor-suppressive role in human colorectal cancer
Fang, Y., Liang, X. H., Xu, J., & Cai, X. (2018) · Cancer Management and Research · doi:10.2147/cmar.s185789 · Cited by 57
RetractedWarburg, O. (1956) · Science · doi:10.1126/science.123.3191.309 · Cited by 13,425
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
5-Fluorouracil: mechanisms of action and clinical strategies
Longley, D. B., Harkin, D. P., & Johnston, P. G. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1074 · Cited by 5,332
Fundamentals of Cancer Metabolism
DeBerardinis, R. J., & Chandel, N. S. (2016) · Science Advances · doi:10.1126/sciadv.1600200 · Cited by 3,013
The integrated stress response
Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659
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 2,369
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
Chemotherapy and the war on cancer
Chabner, B. A., & Roberts, T. G. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1529 · Cited by 2,231
Kastenhuber, E. R., & Lowe, S. W. (2017) · Cell · doi:10.1016/j.cell.2017.08.028 · Cited by 1,906
The multifaceted roles of fatty acid synthesis in cancer
Röhrig, F., & Schulze, A. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.89 · Cited by 1,651
Stine, Z. E., Walton, Z. E., Altman, B. J., Hsieh, A. L., & Dang, C. V. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0507 · Cited by 1,435
Cancer epigenetics reaches mainstream oncology
Rodríguez‐Paredes, M., & Esteller, M. (2011) · Nature Medicine · doi:10.1038/nm.2305 · Cited by 1,252
HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
David, C. J., Chen, M., Assanah, M., Canoll, P., & Manley, J. L. (2010) · Nature · doi:10.1038/nature08697 · Cited by 1,179
Roesch, A., Fukunaga‐Kalabis, M., Schmidt, E. C., Zabierowski, S. E., Brafford, P. A., Vultur, A., Basu, D., Gimotty, P. A., VOGT, T. M., & Herlyn, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.020 · Cited by 1,177
Quantitative flux analysis reveals folate-dependent NADPH production
Fan, J., Ye, J., Kamphorst, J. J., Shlomi, T., Thompson, C. B., & Rabinowitz, J. D. (2014) · Nature · doi:10.1038/nature13236 · Cited by 1,114
Glucose-Independent Glutamine Metabolism via TCA Cycling for Proliferation and Survival in B Cells
Le, A., Lane, A. N., Hamaker, M., Bose, S., Gouw, A., Barbi, J., Tsukamoto, T., Rojas, C. J., Slusher, B. S., Zhang, H., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.12.009 · Cited by 1,095
Serine and glycine metabolism in cancer
Amelio, I., Cutruzzolà, F., Antonov, A., Agostini, M., & Melino, G. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.004 · Cited by 1,080
NAD(H) and NADP(H) Redox Couples and Cellular Energy Metabolism
Xiao, W., Wang, R., Handy, D. E., & Loscalzo, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7216 · Cited by 1,062
Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells
Maddocks, O. D. K., Berkers, C. R., Mason, S. M., Zheng, L., Blyth, K., Gottlieb, E., & Vousden, K. H. (2013) · Nature · doi:10.1038/nature11743 · Cited by 1,007
Serine and one-carbon metabolism in cancer
Yang, M., & Vousden, K. H. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.81 · Cited by 992
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
Vaupel, P. W., Schmidberger, H., & Mayer, A. (2019) · International Journal of Radiation Biology · doi:10.1080/09553002.2019.1589653 · Cited by 923
Lu, J., Tan, M., & Cai, Q. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.04.001 · Cited by 822
mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle
Ben-Sahra, I., Hoxhaj, G., Ricoult, S. J. H., Asara, J. M., & Manning, B. D. (2016) · Science · doi:10.1126/science.aad0489 · Cited by 795
NRF2 regulates serine biosynthesis in non–small cell lung cancer
DeNicola, G. M., Chen, P.-H., Mullarky, E., Sudderth, J., Hu, Z., Wu, D., Tang, H., Xie, Y., Asara, J. M., Huffman, K. E., et al. (2015) · Nature Genetics · doi:10.1038/ng.3421 · Cited by 768
Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases
Casero, R. A., & Marton, L. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2243 · Cited by 752
Stimulation of de novo pyrimidine synthesis by growth signaling through mTOR and S6K1
Ben-Sahra, I., Howell, J. J., Asara, J. M., & Manning, B. D. (2013) · Science · doi:10.1126/science.1228792 · Cited by 739
Serine is a natural ligand and allosteric activator of pyruvate kinase M2
Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661
Zhang, W. C., Shyh-Chang, N., Yang, H., Rai, A., Umashankar, S., Ma, S., Soh, B. S., Sun, L. L., Tai, B. C., Nga, M. E., et al. (2012) · Cell · doi:10.1016/j.cell.2011.11.050 · Cited by 660
Hosios, A. M., Hecht, V. C., Danai, L. V., Johnson, M. O., Rathmell, J. C., Steinhauser, M. L., Manalis, S. R., & Vander Heiden, M. G. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.02.012 · Cited by 641
Surviving Stress: Modulation of ATF4-Mediated Stress Responses in Normal and Malignant Cells
Wortel, I. M. N., van der Meer, L. T., Kilberg, M. S., & van Leeuwen, F. N. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.07.003 · Cited by 630
Nilsson, R., Jain, M., Madhusudhan, N., Sheppard, N. G., Strittmatter, L., Kampf, C., Huang, J., Asplund, A., & Mootha, V. K. (2014) · Nature Communications · doi:10.1038/ncomms4128 · Cited by 607
Modulating the therapeutic response of tumours to dietary serine and glycine starvation
Maddocks, O. D. K., Athineos, D., Cheung, E. C., Lee, P., Zhang, T., van den Broek, N. J. F., Mackay, G. M., Labuschagne, C. F., Gay, D., Kruiswijk, F., et al. (2017) · Nature · doi:10.1038/nature22056 · Cited by 603
Choline and betaine in health and disease
Ueland, P. M. (2010) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-010-9088-4 · Cited by 598
Serine, but not glycine, supports one-carbon metabolism and proliferation of cancer cells
Labuschagne, C. F., van den Broek, N. J. F., Mackay, G. M., Vousden, K. H., & Maddocks, O. D. K. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.04.045 · Cited by 576
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
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
One-carbon metabolism in cancer
Newman, A. C., & Maddocks, O. D. K. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.118 · Cited by 525
The impact of cellular metabolism on chromatin dynamics and epigenetics
Reid, M. A., Dai, Z., & Locasale, J. W. (2017) · Nature Cell Biology · doi:10.1038/ncb3629 · Cited by 515
One‐carbon metabolism and epigenetics: understanding the specificity
Mentch, S. J., & Locasale, J. W. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12956 · Cited by 510
Activation and repression by oncogenic MYC shape tumour-specific gene expression profiles
Walz, S., Lorenzin, F., Morton, J. P., Wiese, K. E., von Eyß, B., Herold, S., Rycak, L., Dumay‐Odelot, H., Karim, S. A., Bartkuhn, M., et al. (2014) · Nature · doi:10.1038/nature13473 · Cited by 502
NNMT promotes epigenetic remodeling in cancer by creating a metabolic methylation sink
Ulanovskaya, O. A., Zuhl, A. M., & Cravatt, B. F. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1204 · Cited by 454
Serine Catabolism Regulates Mitochondrial Redox Control during Hypoxia
Ye, J., Fan, J., Venneti, S., Wan, Y.-W., Pawel, B. R., Zhang, J., Finley, L. W. S., Lu, C., Lindsten, T., Cross, J. R., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0250 · Cited by 452
Maddocks, O. D. K., Labuschagne, C. F., Adams, P. D., & Vousden, K. H. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.014 · Cited by 452
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 450
DNA methylation: An epigenetic mark of cellular memory
Kim, M., & Costello, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.10 · Cited by 450
Ye, J., Mancuso, A., Tong, X., Ward, P. S., Fan, J., Rabinowitz, J. D., & Thompson, C. B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204176109 · Cited by 426
NADPH production by the oxidative pentose-phosphate pathway supports folate metabolism
Chen, L., Zhang, Z., Hoshino, A., Zheng, H. D., Morley, M. P., Arany, Z. P., & Rabinowitz, J. D. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0043-x · Cited by 426
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 423
Reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway
Ducker, G. S., Chen, L., Morscher, R. J., Ghergurovich, J. M., Esposito, M., Teng, X., Kang, Y., & Rabinowitz, J. D. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.016 · Cited by 419
Diversion of aspartate in ASS1-deficient tumours fosters de novo pyrimidine synthesis
Rabinovich, S., Adler, L., Yizhak, K., Sarver, A., Silberman, A., Agron, S., Stettner, N., Sun, Q., Brandis, A., Helbling, D., et al. (2015) · Nature · doi:10.1038/nature15529 · Cited by 382
Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia
Kikuchi, G., Motokawa, Y., Yoshida, T., & Hiraga, K. (2008) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.84.246 · Cited by 381
Metabolic reprogramming for cancer cells and their microenvironment: Beyond the Warburg Effect
Sun, L., Suo, C., Li, S., Zhang, H., & Gao, P. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.06.005 · Cited by 374
SHMT2 drives glioma cell survival in ischaemia but imposes a dependence on glycine clearance
Kim, D., Fiske, B. P., Birsoy, K., Freinkman, E., Kami, K., Possemato, R. L., Chudnovsky, Y., Pacold, M. E., Chen, W. W., Cantor, J. R., et al. (2015) · Nature · doi:10.1038/nature14363 · Cited by 368
Serine Metabolism Supports Macrophage IL-1β Production
Rodriguez, A. E., Ducker, G. S., Billingham, L. K., Martinez, C. A., Mainolfi, N., Suri, V., Friedman, A. A., Manfredi, M. G., Weinberg, S. E., Rabinowitz, J. D., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.014 · Cited by 349
LKB1 loss links serine metabolism to DNA methylation and tumorigenesis
Kottakis, F., Nicolay, B. N., Roumane, A., Karnik, R., Gu, H., Nagle, J. M., Boukhali, M., Hayward, M. C., Li, Y. Y., Chen, T., et al. (2016) · Nature · doi:10.1038/nature20132 · Cited by 348
Mullarky, E., Lucki, N. C., Beheshti Zavareh, R., Anglin, J. L., Gomes, A. P., Nicolay, B. N., Wong, J. C. Y., Christen, S., Takahashi, H., Singh, P. K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521548113 · Cited by 333
Inhibitors of Protein Methyltransferases and Demethylases
Kanıskan, H. Ü., Martini, M. L., & Jin, J. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00801 · Cited by 327
Histidine catabolism is a major determinant of methotrexate sensitivity
Kanarek, N., Keys, H. R., Cantor, J. R., Lewis, C. A., Chan, S. H., Kunchok, T., Abu-Remaileh, M., Freinkman, E., Schweitzer, L. D., & Sabatini, D. M. (2018) · Nature · doi:10.1038/s41586-018-0316-7 · Cited by 321
Sun, L., Song, L., Wan, Q., Wu, G., Li, X., Wang, Y., Wang, J., Liu, Z., Zhong, X., He, X., et al. (2015) · Cell Research · doi:10.1038/cr.2015.33 · Cited by 313
ATF4-dependent induction of heme oxygenase 1 prevents anoikis and promotes metastasis
Dey, S., Sayers, C. M., Verginadis, I. I., Lehman, S. L., Cheng, Y., Cerniglia, G. J., Tuttle, S. W., Feldman, M. D., Zhang, P. J. L., Fuchs, S. Y., et al. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78031 · Cited by 291
Cancer Cells Tune the Signaling Pathways to Empower de Novo Synthesis of Nucleotides
Villa, E., Ali, E. S., Sahu, U., & Ben‐Sahra, I. (2019) · Cancers · doi:10.3390/cancers11050688 · Cited by 289
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 281
Park, Y., Reyna-Neyra, A., Philippe, L., & Thoreen, C. C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.042 · Cited by 278
Mallik, R., & Chowdhury, T. A. (2018) · Diabetes Research and Clinical Practice · doi:10.1016/j.diabres.2018.05.023 · Cited by 270
ATF4 couples MYC-dependent translational activity to bioenergetic demands during tumour progression
Tameire, F., Verginadis, I. I., Leli, N. M., Polte, C., Conn, C. S., Ojha, R., Salinas, C. S., Chinga, F., Monroy, A. M., Fu, W., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-019-0347-9 · Cited by 269
One-carbon metabolism and epigenetics
Friso, S., Udali, S., Santis, D. D., & Choi, S. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.11.007 · Cited by 267
A Metabolic Function for Phospholipid and Histone Methylation
Ye, C., Sutter, B. M., Wang, Y., Kuang, Z., & Tu, B. P. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.026 · Cited by 266
Tedeschi, P. M., Markert, E. K., Gounder, M. K., Lin, H., Dvorzhinski, D., Dolfi, S. C., Chan, L. L.-Y., Qiu, J., DiPaola, R. S., Hirshfield, K. M., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.393 · Cited by 265
Serine Availability Influences Mitochondrial Dynamics and Function through Lipid Metabolism
Gao, X., Lee, K., Reid, M. A., Sanderson, S. M., Qiu, C., Li, S., Liu, J., & Locasale, J. W. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.017 · Cited by 256
Methyl Donor Micronutrients that Modify DNA Methylation and Cancer Outcome
Mahmoud, A. M., & Ali, M. M. (2019) · Nutrients · doi:10.3390/nu11030608 · Cited by 256
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 250
Ding, J., Li, T., Wang, X., Zhao, E., Choi, J.-H., Yang, L., Zha, Y., Dong, Z., Huang, S., Asara, J. M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.004 · Cited by 246
Winter, S. S., Dunsmore, K. P., Devidas, M., Wood, B. L., Esiashvili, N., Chen, Z., Eisenberg, N., Briegel, N., Hayashi, R. J., Gastier, J. M., et al. (2018) · Journal of Clinical Oncology · doi:10.1200/jco.2018.77.7250 · Cited by 241
MYC-Driven Pathways in Breast Cancer Subtypes
Fallah, Y., Brundage, J., Allegakoen, P., & Shajahan‐Haq, A. N. (2017) · Biomolecules · doi:10.3390/biom7030053 · Cited by 226
Vazquez, A., Kamphorst, J. J., Markert, E. K., Schug, Z. T., Tardito, S., & Gottlieb, E. (2016) · Journal of Cell Science · doi:10.1242/jcs.181016 · Cited by 225
Bose, S., & Le, A. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-77736-8_1 · Cited by 220
The role of DNA methylation in ageing and cancer
Morgan, A. E., Davies, T. J., & Auley, M. T. M. (2018) · Proceedings of The Nutrition Society · doi:10.1017/s0029665118000150 · Cited by 211
Control of Nutrient Stress-Induced Metabolic Reprogramming by PKCζ in Tumorigenesis
Ma, L., Tao, Y., Durán, Á., Lladó, V., Galvez, A. S., Barger, J. F., Castilla, E. A., Chen, J., Yajima, T., Porollo, A., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.028 · Cited by 209
Fine, E. J., Segal-Isaacson, C. J., Feinman, R. D., Herszkopf, S., Romano, M. C., Tomuta, N., Bontempo, A., Negassa, A., & Sparano, J. A. (2012) · Nutrition · doi:10.1016/j.nut.2012.05.001 · Cited by 206
Epstein-Barr-Virus-Induced One-Carbon Metabolism Drives B Cell Transformation
Wang, L. W., Shen, H., Nobre, L., Ersing, I., Paulo, J. A., Trudeau, S., Wang, Z., Smith, N. A., Ma, Y., Reinstadler, B., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.06.003 · Cited by 190
Reina‐Campos, M., Linares, J. F., Durán, Á., Cordes, T., L’Hermitte, A., Badur, M. G., Bhangoo, M. S., Thorson, P. K., Richards, A. C., Rooslid, T., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.018 · Cited by 188
Molecular and cellular mechanisms of chemoresistance in pancreatic cancer
Adamska, A., Elaskalani, O., Emmanouilidi, A., Kim, M. K., Razak, N. B. A., Metharom, P., & Falasca, M. (2017) · Advances in Biological Regulation · doi:10.1016/j.jbior.2017.11.007 · Cited by 186
PHGDH defines a metabolic subtype in lung adenocarcinomas with poor prognosis
Zhang, B., Zheng, A., Hydbring, P., Ambroise, G., Ouchida, A. T., Goiny, M., Vakifahmetoglu-Norberg, H., & Norberg, E. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.05.067 · Cited by 178
A clinical-molecular update on azanucleoside-based therapy for the treatment of hematologic cancers
Diesch, J., Zwick, A., Garz, A.-K., Palau, A., Buschbeck, M., & Götze, K. S. S. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0237-y · Cited by 177
Adams, C. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610510200 · Cited by 173
A landscape of metabolic variation across tumor types
Reznik, E., Luna, A., Aksoy, B. A., Liu, E. M., La, K., Ostrovnaya, I., Creighton, C. J., Hakimi, A. A., & Sander, C. (2018) · Cell Systems · doi:10.1016/j.cels.2017.12.014 · Cited by 172
Carabet, L. A., Rennie, P. S., & Cherkasov, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010120 · Cited by 172
Serine and Functional Metabolites in Cancer
Newman, A. C., & Maddocks, O. D. K. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.05.001 · Cited by 168
KDM4C and ATF4 Cooperate in Transcriptional Control of Amino Acid Metabolism
Zhao, E., Ding, J., Xia, Y., Liu, M., Ye, B., Choi, J.-H., Yan, C., Dong, Z., Huang, S., Zha, Y., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.053 · Cited by 165
Li, S., Swanson, S. K., Gogol, M., Florens, L. A., Washburn, M. P., Workman, J. L., & Suganuma, T. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.024 · Cited by 160
Characterization of the Usage of the Serine Metabolic Network in Human Cancer
Mehrmohamadi, M., Liu, X., Shestov, A. A., & Locasale, J. W. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.026 · Cited by 158
Ou, Y., Wang, S.-J., Jiang, L., Zheng, B., & Gu, W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616359 · Cited by 156
Spatiotemporal compartmentalization of hepatic NADH and NADPH metabolism
Goodman, R. P., Calvo, S. E., & Mootha, V. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm117.000258 · Cited by 150
Gao, S., Ge, A., Xu, S., You, Z., Ning, S., Zhao, Y., & Pang, D. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0648-4 · Cited by 149
PP2A inhibition is a druggable MEK inhibitor resistance mechanism in KRAS-mutant lung cancer cells
Kauko, O., O’Connor, C. M., Kulesskiy, E., Sangodkar, J., Aakula, A., Izadmehr, S., Yetukuri, L., Yadav, B., Padzik, A., Laajala, T. D., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aaq1093 · Cited by 149
Luan, W., Wang, Y., Chen, X., Shi, Y., Wang, J., Zhang, J., Qian, J., Li, R., Tao, T., Wei, W., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3514 · Cited by 146
Chromatin-Bound MDM2 Regulates Serine Metabolism and Redox Homeostasis Independently of p53
Riscal, R., Schrepfer, E., Arena, G., Cissé, M. Y., Bellvert, F., Heuillet, M., Rambow, F., Bonneil, É., Sabourdy, F., Vincent, C., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.033 · Cited by 146
The MYC Enhancer-ome: Long-Range Transcriptional Regulation of MYC in Cancer
Lancho, O., & Herranz, D. (2018) · Trends in cancer · doi:10.1016/j.trecan.2018.10.003 · Cited by 143
Serine deprivation enhances antineoplastic activity of biguanides
Gravel, S.-P., Hulea, L., Toban, N., Birman, E., Blouin, M.-J., Zakikhani, M., Zhao, Y., Topisirovic, I., St-Pierre, J., & Pollak, M. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-2643-t · Cited by 138
Fedirko, V., Lukanova, A., Bamia, C., Trichopolou, A., Trépo, E., Nöthlings, U., Schlesinger, S., Aleksandrova, K., Boffetta, P., Tjønneland, A. M., et al. (2012) · Annals of Oncology · doi:10.1093/annonc/mds434 · Cited by 133
The Impact of One Carbon Metabolism on Histone Methylation
Serefidou, M., Venkatasubramani, A. V., & Imhof, A. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00764 · Cited by 131
p73 regulates serine biosynthesis in cancer
Amelio, I., Markert, E. K., Rufini, A., Antonov, A. V., Sayan, B. S., Tucci, P., Agostini, M., Mineo, T. C., Levine, A. J., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2013.456 · Cited by 126
The complexity of the serine glycine one-carbon pathway in cancer
Reina‐Campos, M., Díaz-Meco, M. T., & Moscat, J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201907022 · Cited by 125
Nishimura, T., Nakata, A., Chen, X., Nishi, K., Meguro‐Horike, M., Sasaki, S., Kita, K., Horike, S., Saitoh, K., Kato, K., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0589-1 · Cited by 115
Cell cycle regulation of folate‐mediated one‐carbon metabolism
Lan, X., Field, M. S., & Stover, P. J. (2018) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1426 · Cited by 113
Xia, Y., Ye, B., Ding, J., Yu, Y., Alptekin, A., Thangaraju, M., Prasad, P. D., Ding, Z., Park, E. J., Choi, J.-H., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3541 · Cited by 108
Role of the ISR-ATF4 pathway and its cross talk with Nrf2 in mitochondrial quality control
Kasai, S., Yamazaki, H., Tanji, K., Engler, M. J., Matsumiya, T., & Itoh, K. (2018) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.18-37 · Cited by 107
Zhang, C., Liu, J., Zhao, Y., Yue, X., Zhu, Y., Wang, X., Wu, H., Blanco, F., Li, S., Bhanot, G., et al. (2016) · eLife · doi:10.7554/elife.10727 · Cited by 106
Mitochondrial One-Carbon Pathway Supports Cytosolic Folate Integrity in Cancer Cells
Zheng, Y., Lin, T.-Y., Lee, G., Paddock, M. N., Momb, J., Cheng, Z., Li, Q., Fei, D. L., Stein, B. D., Ramsamooj, S., et al. (2018) · Cell · doi:10.1016/j.cell.2018.09.041 · Cited by 106
Ross, K. C., Andrews, A. J., Marion, C. D., Yen, T. J., & Bhattacharjee, V. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-16-0798 · Cited by 99
Crystal Structure of the Emerging Cancer Target MTHFD2 in Complex with a Substrate-Based Inhibitor
Gustafsson, R., Jemth, A., Gustafsson, N., Färnegårdh, K., Loseva, O., Wiita, E., Bonagas, N., Dahllund, L., Llona‐Minguez, S., Häggblad, M., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-1476 · Cited by 97
Daunorubicin/Cytarabine Liposome: A Review in Acute Myeloid Leukaemia
Blair, H. A. (2018) · Drugs · doi:10.1007/s40265-018-1022-3 · Cited by 96
Serine and one-carbon metabolism, a bridge that links mTOR signaling and DNA methylation in cancer
Zeng, J., Wu, W. K. K., Wang, H., & Li, X. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104352 · Cited by 96
The Role of D-3-Phosphoglycerate Dehydrogenase in Cancer
Zhao, X., Fu, J., Du, J., & Xu, W. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.41051 · Cited by 93
MYC Modulation around the CDK2/p27/SKP2 Axis
Hydbring, P., Castell, A., & Larsson, L. (2017) · Genes · doi:10.3390/genes8070174 · Cited by 92
Méndez‐Lucas, A., Li, X., Hu, J., Che, L., Song, X., Jia, J., Wang, J., Xie, C., Driscoll, P. C., Tschaharganeh, D. F., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0498 · Cited by 90
Liu, B., Jia, Y., Cao, Y., Wu, S., Jiang, H., Sun, X., Ma, J., Yin, X., Mao, A., & Shang, M. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000445633 · Cited by 75
An early Myc‐dependent transcriptional program orchestrates cell growth during B‐cell activation
Tesi, A., de Pretis, S., Furlan, M., Filipuzzi, M., Morelli, M. J., Andronache, A., Doni, M., Verrecchia, A., Pelizzola, M., Amati, B. B., et al. (2019) · EMBO Reports · doi:10.15252/embr.201947987 · Cited by 73
Serine Supports IL-1β Production in Macrophages Through mTOR Signaling
Chen, S., Xia, Y., He, F., Fu, J., Xin, Z., Deng, B., He, L., Zhou, X., & Ren, W. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01866 · Cited by 73
NRF2 SUMOylation promotes de novo serine synthesis and maintains HCC tumorigenesis
Guo, H., Xu, J., Zheng, Q., He, J., Zhou, W., Wang, K., Huang, X., Fan, Q., Ma, J., Cheng, J., et al. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.09.010 · Cited by 72
PAK4 regulates G6PD activity by p53 degradation involving colon cancer cell growth
Zhang, X., Zhang, X., Li, Y., Shao, Y., Xiao, J., Zhu, G., & Li, F. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.85 · Cited by 67
Shin, M., Momb, J., & Appling, D. R. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0173-0 · Cited by 66
The PHGDH enigma: Do cancer cells only need serine or also a redox modulator?
Li, A. M., & Ye, J. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.01.036 · Cited by 65
Writing and erasing MYC ubiquitination and SUMOylation
Chen, Y., Sun, X., Sears, R. C., & Dai, M. (2019) · Genes & Diseases · doi:10.1016/j.gendis.2019.05.006 · Cited by 64
Albrecht, L. V., Bui, M. H., & Robertis, E. M. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820161116 · Cited by 63
Bolusani, S., Young, B. A., Cole, N., Tibbetts, A. S., Momb, J., Bryant, J. D., Solmonson, A., & Appling, D. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.196840 · Cited by 58
The epigenetics of tumour initiation: cancer stem cells and their chromatin
Avgustinova, A., & Benitah, S. A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.01.003 · Cited by 58
p53‐mediated adaptation to serine starvation is retained by a common tumour‐derived mutant
Humpton, T. J., Hock, A. K., Maddocks, O. D. K., & Vousden, K. H. (2018) · Cancer & Metabolism · doi:10.1186/s40170-018-0191-6 · Cited by 58
Xu, D., Dai, W., Kutzler, L., Lacko, H. A., Jefferson, L. S., Dennis, M. D., & Kimball, S. R. (2019) · Journal of Nutrition · doi:10.1093/jn/nxz309 · Cited by 57
Menin regulates the serine biosynthetic pathway in Ewing sarcoma
Svoboda, L. K., Teh, S. S. K., Sud, S., Kerk, S. A., Zebolsky, A. L., Treichel, S., Thomas, D. G., Halbrook, C. J., Lee, H., Kremer, D. M., et al. (2018) · The Journal of Pathology · doi:10.1002/path.5085 · Cited by 52
Ravez, S., Spillier, Q., Marteau, R., Féron, O., & Frédérick, R. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01167 · Cited by 50
Hughey, C. C., Trefts, E., Bracy, D. P., James, F. D., Donahue, E. P., & Wasserman, D. H. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002568 · Cited by 49
Zhang, W. C., Shyh‐Chang, N., He, Y., Rai, A., Umashankar, S., Ma, S., Soh, B.-S., Sun, L. L., Tai, B. C., Nga, M. E., et al. (2012) · Cell · doi:10.1016/j.cell.2012.02.024 · Cited by 48
Konno, M., Asai, A., Kawamoto, K., Nishida, N., Satoh, T., Doki, Y., Mori, M., & Ishii, H. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.3885 · Cited by 47
Quantitation of Cellular Metabolic Fluxes of Methionine
Shlomi, T., Fan, J., Tang, B., Kruger, W. D., & Rabinowitz, J. D. (2014) · Analytical Chemistry · doi:10.1021/ac4032093 · Cited by 46
Ser, Z., Gao, X., Johnson, C., Mehrmohamadi, M., Liu, X., Li, S., & Locasale, J. W. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.035 · Cited by 46
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Walker, A. K. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.10.004 · Cited by 46
Calise, S. J., Purich, D. L., Nguyen, T. M., Saleem, D. A., Krueger, C., Yin, J. D., & Chan, E. K. L. (2016) · Journal of Cell Science · doi:10.1242/jcs.183400 · Cited by 45
Wang, S., Peng, Z., Wang, S., Yang, L., Chen, Y., Kong, X., Song, S., Pei, P., Tian, C., Yan, H., et al. (2018) · Cell Research · doi:10.1038/s41422-018-0008-8 · Cited by 45
How can we best monitor 5-FU administration to maximize benefit to risk ratio?
Goirand, F., Lemaitre, F., Launay, M., Tron, C., Chatelut, É., Boyer, J.-C., Bardou, M., & Schmitt, A. (2018) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2018.1550484 · Cited by 45
Mazor, K. M., & Stipanuk, M. H. (2016) · Amino Acids · doi:10.1007/s00726-016-2318-9 · Cited by 43
Development of new agents for peripheral T-cell lymphoma
Ito, Y., Makita, S., & Tobinai, K. (2019) · Expert Opinion on Biological Therapy · doi:10.1080/14712598.2019.1572746 · Cited by 37
Pandey, S., Garg, P., Lee, S., Choung, H., Choung, Y., Choung, P., & Chung, J. H. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.07.045 · Cited by 36
Mitochondrial MTHFD isozymes display distinct expression, regulation, and association with cancer
Nilsson, R., Nicolaidou, V., & Koufaris, C. (2019) · Gene · doi:10.1016/j.gene.2019.144032 · Cited by 36
Tripathi, S., Gupta, N., Mahato, M., Gupta, K. C., & Kumar, P. (2013) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2013.11.024 · Cited by 32
Jumonji/Arid1b (Jarid1b) protein modulates human esophageal cancer cell growth
KANO, Y., Konno, M., Ohta, K., Haraguchi, N., Nishikawa, S., Kagawa, Y., Hamabe, A., Hasegawa, S., Ogawa, H., Fukusumi, T., et al. (2013) · Molecular and Clinical Oncology · doi:10.3892/mco.2013.127 · Cited by 32
Knock-down of PSAT1 Enhances Sensitivity of NSCLC Cells to Glutamine-limiting Conditions
Jin, H., Hong, S., Kim, J.-Y., Jang, S., KIM, Y.-S., Sim, J.-H., OH, A.-C., Kim, H., Hong, Y. J., Lee, J., et al. (2019) · Anticancer Research · doi:10.21873/anticanres.13887 · Cited by 30
G9a - An Appealing Antineoplastic Target
Chen, W., Sun, H.-P., Li, D., Wang, Z., You, Q., & Guo, X. (2016) · Current Cancer Drug Targets · doi:10.2174/1568009616666160512145303 · Cited by 29
Al-Baghdadi, R. J. T., Nikonorova, I. A., Mirek, E. T., Wang, Y., Park, J., Belden, W. J., Wek, R. C., & Anthony, T. G. (2017) · Scientific Reports · doi:10.1038/s41598-017-01041-7 · Cited by 27
Mesclon, F., Lambert-Langlais, S., Carraro, V., Parry, L., Hainault, I., Jousse, C., Maurin, A., Bruhat, A., Fafournoux, P., & Avérous, J. (2017) · Oncotarget · doi:10.18632/oncotarget.15828 · Cited by 24
Sowers, M. L., Herring, J. L., Zhang, W., Tang, H. R., Ou, Y., Gu, W. J., & Zhang, K. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.10.026 · Cited by 23
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Konno, M., Koseki, J., Kawamoto, K., Nishida, N., Matsui, H., Dewi, D. L., Ozaki, M., Noguchi, Y., Mimori, K., Gotoh, N., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132789 · Cited by 20
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Hanley, M. P., & Rosenberg, D. W. (2015) · Current Pharmacology Reports · doi:10.1007/s40495-015-0028-8 · Cited by 20
Kim, S. Y., Mi-Na, H. O. N. G., Heo, S., Park, S., Kwon, T. K., Sung, Y. H., Oh, Y., Lee, S., Yi, G., & Kim, I. (2018) · Molecular Carcinogenesis · doi:10.1002/mc.22872 · Cited by 20
Yu, C., Chen, H., Jinbo, C., Feng, Z., Zu, X., & Jian, D. (2018) · Journal of Cancer Research and Therapeutics · doi:10.4103/0973-1482.188434 · Cited by 19
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Robaina, M. C., Mazzoccoli, L., & Klumb, C. E. (2019) · Cells · doi:10.3390/cells8111365 · Cited by 19
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Fukuoka, H., & Kubota, T. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-5526-3_1 · Cited by 16
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Fritsche, M. K., & Knopf, A. (2017) · Genes · doi:10.3390/genes8120384 · Cited by 14
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Mattaini, K. R., Sullivan, M. R., Lau, A. N., Fiske, B. P., Bronson, R. T., & Heiden, M. G. V. (2019) · BMC Cancer · doi:10.1186/s12885-019-5933-5 · Cited by 14
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Kawahata, T., Kawahara, K., Shimokawa, M., Sakiyama, A., Shiraishi, T., Minami, K., Yamamoto, M., Shinsato, Y., Arima, K., Hamada, T., et al. (2020) · Oncology Letters · doi:10.3892/ol.2020.11352 · Cited by 14
Wei, N., Zhang, B., Wang, Y., He, X., Xu, L., Li, G. D., Wang, Y. H., Wang, G. Z., Huang, H., & Li, W. T. (2018) · Clinical & Translational Oncology · doi:10.1007/s12094-018-1942-0 · Cited by 13
Kucharczyk, T., Krawczyk, P. A., Powrózek, T., Kowalski, D. M., Ramlau, R., Kalinka‐Warzocha, E., Knetki‐Wróblewska, M., Winiarczyk, K., Krzakowski, M. J., & Milanowski, J. (2015) · Pathology & Oncology Research · doi:10.1007/s12253-015-9966-z · Cited by 10
Thoreen, C. C., & Park, Y. (2017) · The FASEB Journal · doi:10.1096/fasebj.31.1_supplement.614.32 · Cited by 10
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Metadata
- Authors
- Pan, S., Fan, M., Liu, Z., Li, X., & Wang, H.
- Affiliations
- Henan University (CN)
- Corresponding author
- Li, Xia
- Wang, Huijuan
- ORCID
- Venue
- International Journal of Oncology
- Publisher
- Spandidos Publications
- Published
- 2020-12-11
- Volume
- 58
- Issue
- 2
- Pages
- 158-170
- ISSN
- 1019-6439 (ISSN-L)
- 1791-2423
- PMC
- PMC7864012
- OpenAlex
- W3112083241
- Cited by
- 227
- References
- 166
- Citations by year
- 2026: 58 · 2025: 64 · 2024: 37 · 2023: 36 · 2022: 23 · 2021: 9
- FWCI
- 1.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- International Journal of Oncology (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81872023)
- China Postdoctoral Science Foundation (2018M642742, 81872023)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Health Sciences › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- serine biosynthesis, glycine synthesis, one-carbon metabolism, folate metabolism, cancer metabolism, carcinogenesis, DNA methylation, anticancer drug development, dietary intervention, biomarkers
- MeSH terms
- Warburg Effect, Oncologic, Animals, Antineoplastic Agents, Carbon, Disease Models, Animal, Glycine, Humans, Methylation, Neoplasms, Oxidation-Reduction, Serine, Mice, Metabolic Networks and Pathways, Tumor Microenvironment, Carcinogenesis
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