Amino acid metabolism, redox balance and epigenetic regulation in cancer
Open accessAbstract
Amino acids act as versatile nutrients driving cell growth and survival, especially in cancer cells. Amino acid metabolism comprises numerous metabolic networks and is closely linked with intracellular redox balance and epigenetic regulation. Reprogrammed amino acid metabolism has been recognized as a ubiquitous feature in tumour cells. This review outlines the metabolism of several primary amino acids in cancer cells and highlights the pivotal role of amino acid metabolism in sustaining redox homeostasis and regulating epigenetic modification in response to oxidative and genetic stress in cancer cells.
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One-carbon metabolism links glycolysis with biosynthetic processes that result in DNA and RNA biosynthesis, protein biosynthesis, and maintenance of the redox and methylation states of cells.
“As serine is derived from glycolysis intermediate 3-phosphoglycerate, one-carbon metabolism links glycolysis with different biosynthetic processes that result in DNA and RNA biosynthesis, protein biosynthesis, and the maintenance of the redox and methylation states of cells [51,52].”
From 20-Hydroxyecdysone Boosts Energy Production and Biosynthetic Processes in Non-Transformed Mouse Cells (2024) · cites this paper as [52]
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1 retracted
Wu, Y., Hu, Z., Hu, S., et al. (2019) · Cancer Biomarkers · doi:10.3233/cbm-190022 · Cited by 13 · see citing works
RetractedHallmarks of Cancer: New Dimensions
Hanahan, D. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1059 · Cited by 9,887 · see citing works
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
Reactive oxygen species (ROS) as pleiotropic physiological signalling agents
Sies, H., & Jones, D. P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0230-3 · Cited by 5,335 · see citing works
Metabolic reprogramming and cancer progression
Faubert, B., Solmonson, A., & DeBerardinis, R. J. (2020) · Science · doi:10.1126/science.aaw5473 · Cited by 2,740 · see citing works
Hayes, J. D., Dinkova-Kostova, A. T., & Tew, K. D. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.06.001 · Cited by 2,654 · see citing works
Cystine transporter SLC7A11/xCT in cancer: ferroptosis, nutrient dependency, and cancer therapy
Koppula, P., Zhuang, L., & Gan, B. (2020) · Protein & Cell · doi:10.1007/s13238-020-00789-5 · Cited by 2,546 · see citing works
Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252 · 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
Tryptophan metabolism as a common therapeutic target in cancer, neurodegeneration and beyond
Platten, M., Nollen, E. A. A., Röhrig, U. F., Fallarino, F., & Opitz, C. A. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0016-5 · Cited by 1,586 · see citing works
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
Black, J. C., Rechem, C. V., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,318 · see citing works
Cysteine depletion induces pancreatic tumor ferroptosis in mice
Badgley, M. A., Kremer, D. M., Maurer, H. C., DelGiorno, K. E., Lee, H.-J., Purohit, V., Sagalovskiy, I. R., Ma, A., Kapilian, J., Firl, C. E. M., et al. (2020) · Science · doi:10.1126/science.aaw9872 · Cited by 1,294 · 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
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 · see citing works
Self-citationGlutaminolysis: 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
Neinast, M. D., Murashige, D., & Arany, Z. P. (2018) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020518-114455 · Cited by 727 · see citing works
DNA methylation and histone modifications: teaming up to silence genes
Fuks, F. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.08.002 · Cited by 643 · see citing works
Liu, X., Olszewski, K. L., Zhang, Y., Lim, E. W., Shi, J., Zhang, X., Zhang, J., Lee, H., Koppula, P., Lei, G., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0496-x · Cited by 599 · see citing works
Methionine metabolism in health and cancer: a nexus of diet and precision medicine
Sanderson, S. M., Gao, X., Dai, Z., & Locasale, J. W. (2019) · Nature reviews. Cancer · doi:10.1038/s41568-019-0187-8 · Cited by 572 · see citing works
Dispensable and Indispensable Amino Acids for Humans
Reeds, P. J. (2000) · Journal of Nutrition · doi:10.1093/jn/130.7.1835s · Cited by 511 · see citing works
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 509 · see citing works
Emerging Roles for Branched-Chain Amino Acid Metabolism in Cancer
Sivanand, S., & Heiden, M. G. V. (2020) · Cancer Cell · doi:10.1016/j.ccell.2019.12.011 · Cited by 488 · see citing works
Protein arginine methylation: from enigmatic functions to therapeutic targeting
Wu, Q., Schapira, M., Arrowsmith, C. H., & Baršytė-Lovejoy, D. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00159-8 · Cited by 444 · see citing works
Labadie, B. W., Bao, R., & Luke, J. J. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-2882 · Cited by 413 · see citing works
Cancer progression by reprogrammed BCAA metabolism in myeloid leukaemia
Hattori, A., Tsunoda, M., Konuma, T., Kobayashi, M., Nagy, T., Glushka, J., Tayyari, F., McSkimming, D., Kannan, N., Tojo, A., et al. (2017) · Nature · doi:10.1038/nature22314 · Cited by 401 · see citing works
Jin, L., Li, D., Alesi, G. N., Fan, J., Kang, H., Zhou, L., Boggon, T. J., Jin, P., Yi, H. L., Wright, E., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2014.12.006 · Cited by 371 · see citing works
BCAT1 restricts αKG levels in AML stem cells leading to IDHmut-like DNA hypermethylation
Raffel, S., Falcone, M., Kneisel, N., Hansson, J., Wang, W., Lutz, C., Bullinger, L., Poschet, G., Nonnenmacher, Y., Barnert, A., et al. (2017) · Nature · doi:10.1038/nature24294 · Cited by 354 · see citing works
xCT: A Critical Molecule That Links Cancer Metabolism to Redox Signaling
Liu, J., Xia, X., & Huang, P. (2020) · Molecular Therapy · doi:10.1016/j.ymthe.2020.08.021 · Cited by 348 · see citing works
Wang, Q., Hardie, R., Hoy, A. J., van Geldermalsen, M., Gao, D., Fazli, L., Sadowski, M. C., Balaban, S., Schreuder, M., Nagarajah, R., et al. (2015) · The Journal of Pathology · doi:10.1002/path.4518 · Cited by 338 · see citing works
Jin, L., Chun, J., Pan, C., Kumar, A., Zhang, G., Ha, Y., Li, D., Alesi, G. N., Kang, Y., Zhou, L., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.025 · Cited by 329 · see citing works
Asparagine synthetase: Function, structure, and role in disease
Lomelino, C. L., Andring, J. T., McKENNA, R. V., & Kilberg, M. S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.819060 · Cited by 309 · see citing works
Branched-chain amino acids in disease
White, P. J., & Newgard, C. B. (2019) · Science · doi:10.1126/science.aav0558 · Cited by 303 · see citing works
Tryptophan in health and disease
Comai, S., Bertazzo, A., Brughera, M., & Crotti, S. (2020) · Advances in clinical chemistry · doi:10.1016/bs.acc.2019.08.005 · Cited by 300 · see citing works
Ericksen, R. E., Lim, S. L., McDonnell, E., Shuen, W. H., Vadiveloo, M. K., White, P. J., Ding, Z., Kwok, R., Lee, P., Radda, G. K., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2018.12.020 · Cited by 295 · see citing works
Mukhopadhyay, S., Goswami, D., Adiseshaiah, P. P., Burgan, W., Yi, M., Guerin, T. M., Kozlov, S. V., Nissley, D. V., & McCormick, F. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-1363 · Cited by 279 · see citing works
Protein arginine methyltransferases: promising targets for cancer therapy
Hwang, J. W., Cho, Y., Bae, G., Kim, S., & Kim, Y. K. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00613-y · Cited by 274 · see citing works
Cysteine metabolic circuitries: druggable targets in cancer
Bonifácio, V. D. B., Pereira, S. A., Serpa, J., & Vicente, J. B. (2020) · British Journal of Cancer · doi:10.1038/s41416-020-01156-1 · Cited by 269 · 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
Dimou, A. D., Tsimihodimos, V., & Bairaktari, E. T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23074022 · Cited by 264 · see citing works
GOT1 inhibition promotes pancreatic cancer cell death by ferroptosis
Kremer, D. M., Nelson, B. S., Lin, L., Yarosz, E. L., Halbrook, C. J., Kerk, S. A., Sajjakulnukit, P., Myers, A. L., Thurston, G., Hou, S. W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24859-2 · Cited by 262 · see citing works
DJ-1 suppresses ferroptosis through preserving the activity of S-adenosyl homocysteine hydrolase
Cao, J., Chen, X., Li, J., Lu, B., Meng, Y. G., Zhu, D., Zhu, H., He, Q., Yang, B., & Ying, M. (2020) · Nature Communications · doi:10.1038/s41467-020-15109-y · Cited by 258 · see citing works
System Xc−: a key regulatory target of ferroptosis in cancer
Liu, M.-R., Zhu, W.-T., & Pei, D. (2021) · Investigational New Drugs · doi:10.1007/s10637-021-01070-0 · 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
Targeting Epigenetics in Cancer
Bennett, R. L., & Licht, J. D. (2017) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-105106 · Cited by 252 · see citing works
BCAT2-mediated BCAA catabolism is critical for development of pancreatic ductal adenocarcinoma
Li, J., Yin, M., Wang, D., Wang, J., Lei, M., Zhang, Y., Liu, Y., Zhang, L., Zou, S., Hu, L.-P., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-019-0455-6 · Cited by 248 · see citing works
Cystathionine-β-synthase: Molecular Regulation and Pharmacological Inhibition
Zuhra, K., Augsburger, F., Majtán, T., & Szabó, C. (2020) · Biomolecules · doi:10.3390/biom10050697 · Cited by 244 · see citing works
Multifaceted role of branched-chain amino acid metabolism in cancer
Peng, H., Wang, Y., & Luo, W. (2020) · Oncogene · doi:10.1038/s41388-020-01480-z · Cited by 244 · see citing works
Amino acid metabolism in hematologic malignancies and the era of targeted therapy
Tabe, Y., Lorenzi, P. L., & Konopleva, M. Y. (2019) · Blood · doi:10.1182/blood.2019001034 · Cited by 238 · see citing works
ASCT2/SLC1A5 controls glutamine uptake and tumour growth in triple-negative basal-like breast cancer
van Geldermalsen, M., Wang, Q., Nagarajah, R., Marshall, A., Thoeng, A., Gao, D., Ritchie, W., Feng, Y., Bailey, C. G., Deng, N., et al. (2015) · Oncogene · doi:10.1038/onc.2015.381 · Cited by 235 · see citing works
Chandel, N. S. (2021) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a040584 · Cited by 229 · see citing works
Li, T., Tan, Y., Chen, Y., Zheng, X., Wang, W., Liao, K. L., Mo, H., Lin, J., Yang, W., Piao, H., et al. (2022) · Gut · doi:10.1136/gutjnl-2022-326928 · Cited by 217 · see citing works
PHGDH heterogeneity potentiates cancer cell dissemination and metastasis
Rossi, M., Altea-Manzano, P., Demicco, M., Doglioni, G., Bornes, L., Fukano, M., Vandekeere, A., Cuadros, A. M., Fernández-García, J., Riera-Domingo, C., et al. (2022) · Nature · doi:10.1038/s41586-022-04758-2 · Cited by 213 · see citing works
Gu, Y., de Albuquerque, C. P., Braas, D., Zhang, W., Villa, G. R., Bi, J., Ikegami, S., Masui, K., Gini, B., Yang, H., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.030 · Cited by 210 · see citing works
Zhu, Z., Achreja, A., Meurs, N., Animasahun, O., Owen, S., Mittal, A., Parikh, P., Lo, T.-W., Franco-Barraza, J., Shi, J., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0226-5 · Cited by 204 · see citing works
Daher, B., Parks, S. K., Durivault, J., Cormerais, Y., Baidarjad, H., Tambutté, É., Pouysségur, J., & Vučetić, M. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3855 · Cited by 203 · see citing works
Li, W., He, Y., Yang, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-21963-1 · Cited by 193 · see citing works
Upadhyayula, P. S., Higgins, D. M. O., Mela, A., Banu, M. A., Dovas, A., Zandkarimi, F., Patel, P. R., Mahajan, A., Humala, N., Nguyen, T. T. T., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36630-w · Cited by 191 · see citing works
Villa, E., Sahu, U., O’Hara, B. P., Ali, E. S., Helmin, K. A., Asara, J. M., Gao, P., Singer, B. D., & Ben‐Sahra, I. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.009 · Cited by 186 · see citing works
Kynurenine importation by SLC7A11 propagates anti-ferroptotic signaling
Fiore, A., Zeitler, L., Russier, M., Groß, A., Hiller, M.-K., Parker, J. L., Stier, L. J., Köcher, T., Newstead, S. L., & Murray, P. J. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.007 · Cited by 175 · see citing works
Loss of EZH2 Reprograms BCAA Metabolism to Drive Leukemic Transformation
Gu, Z., Liu, Y., Cai, F., Patrick, M., Zmajkovic, J., Cao, H., Zhang, Y., Tasdogan, A., Chen, M., Qi, L., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0152 · Cited by 173 · see citing works
Asparagine Synthetase in Cancer: Beyond Acute Lymphoblastic Leukemia
Chiu, M., Taurino, G., Bianchi, M. G., Kilberg, M. S., & Bussolati, O. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01480 · Cited by 169 · see citing works
Proline Metabolism in Tumor Growth and Metastatic Progression
D’Aniello, C., Patriarca, E. J., Phang, J. M., & Minchiotti, G. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00776 · Cited by 165 · see citing works
Wang, X., Liu, R., Qu, X., Yu, H. T., Chu, H., Zhang, Y., Zhu, W., Wu, X., Gao, H., Tao, B., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.007 · Cited by 164 · see citing works
Ala, M. (2021) · International Reviews of Immunology · doi:10.1080/08830185.2021.1954638 · Cited by 162 · see citing works
Brait, M., Ling, S., Nagpal, J. K., Chang, X., Park, H. L., Lee, J., Okamura, J., Yamashita, K., Sidransky, D., & Kim, M. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044951 · Cited by 154 · see citing works
Proline metabolism and redox; maintaining a balance in health and disease
Vettore, L. A., Westbrook, R. L., & Tennant, D. A. (2021) · Amino Acids · doi:10.1007/s00726-021-03051-2 · Cited by 154 · see citing works
Zhao, Y., Feng, X., Chen, Y., Selfridge, J. E., Gorityala, S., Du, Z., Wang, J. M., Hao, Y., Cioffi, G., Conlon, R. A., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0600 · Cited by 131 · see citing works
Targeting Tryptophan Catabolism in Cancer Immunotherapy Era: Challenges and Perspectives
Peyraud, F., Guégan, J., Bodet, D., Cousin, S., Bessede, A., & Italiano, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.807271 · Cited by 130 · see citing works
Acetylation promotes BCAT2 degradation to suppress BCAA catabolism and pancreatic cancer growth
Lei, M.-Z., Li, X.-X., Zhang, Y., Li, J.-T., Zhang, F., Wang, Y.-P., Yin, M., Qu, J., & Lei, Q.-Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0168-0 · Cited by 129 · see citing works
Self-citationCysteine Depletion, a Key Action to Challenge Cancer Cells to Ferroptotic Cell Death
Daher, B., Vučetić, M., & Pouysségur, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00723 · Cited by 117 · see citing works
Amino Acid Transporters as Targets for Cancer Therapy: Why, Where, When, and How
Bröer, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176156 · Cited by 112 · see citing works
Sitthideatphaiboon, P., Galán‐Cobo, A., Negrao, M. V., Qu, X. H., Poteete, A., Zhang, F., Liu, D. D., Lewis, W. E., Kemp, H. N., Lewis, J., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-20-2859 · Cited by 112 · see citing works
Newman, A. C., Falcone, M., Uribe, A. H., Zhang, T., Athineos, D., Pietzke, M., Vázquez, A., Blyth, K., & Maddocks, O. D. K. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.019 · Cited by 111 · see citing works
Amino Acid Metabolism in Cancer Drug Resistance
Yoo, H.-C., & Han, J. M. (2022) · Cells · doi:10.3390/cells11010140 · Cited by 105 · see citing works
Asparagine: A Metabolite to Be Targeted in Cancers
Jiang, J., Batra, S., & Zhang, J. (2021) · Metabolites · doi:10.3390/metabo11060402 · Cited by 99 · see citing works
Amino acids and its pharmaceutical applications: A mini review
Bongioanni, A., Bueno, M. S., Mezzano, B. A., Longhi, M. R., & Garnero, C. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.121375 · Cited by 95 · see citing works
Wang, Y., Zhang, J., Ren, S., Sun, D., Huang, H., Wang, H., Jin, Y., Li, F., Zheng, C., Liu, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.026 · Cited by 94 · see citing works
Amino acid deprivation using enzymes as a targeted therapy for cancer and viral infections
Fernandes, H. S., Teixeira, C. S. S., Fernandes, P. A., Ramos, M. J., & Cerqueira, N. M. F. S. A. (2016) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1254194 · Cited by 91 · see citing works
Shen, Y., Hong, J., Asaka, R., Asaka, S., Hsu, F., Rahmanto, Y. S., Jung, J.-G., Chen, Y.-W., Yen, T., Tomaszewski, A., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3971 · Cited by 91 · see citing works
Cystine uptake inhibition potentiates front-line therapies in acute myeloid leukemia
Pardieu, B., Pasanisi, J., Ling, F., Bello, R. D., Penneroux, J., Su, A. H., Joudinaud, R., Chat, L., Wu, H.-C., Duchmann, M., et al. (2022) · Leukemia · doi:10.1038/s41375-022-01573-6 · Cited by 91 · see citing works
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 90 · see citing works
Tryptophan: A Rheostat of Cancer Immune Escape Mediated by Immunosuppressive Enzymes IDO1 and TDO
Kim, M., & Tomek, P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.636081 · Cited by 89 · see citing works
Jeschke, J., O’Hagan, H. M., Zhang, W., Vatapalli, R. J., Calmon, M. F., Danilova, L., Nelkenbrecher, C., Neste, L. V., Bijsmans, I. T. G. W., van Engeland, M., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-3751 · Cited by 87 · see citing works
Targeting extracellular nutrient dependencies of cancer cells
García‐Bermúdez, J., Williams, R. T., Guarecuco, R., & Birsoy, K. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.11.011 · Cited by 87 · see citing works
Recent advances in clinical trials targeting the kynurenine pathway
Pires, A. S., Sundaram, G., Heng, B., Krishnamurthy, S., Brew, B. J., & Guillemin, G. J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108055 · Cited by 84 · see citing works
ZBTB1 Regulates Asparagine Synthesis and Leukemia Cell Response to L-Asparaginase
Williams, R. T., Guarecuco, R., Gates, L. A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.03.008 · Cited by 78 · see citing works
Westbrook, R. L., Bridges, E., Roberts, J., Escribano-Gonzalez, C., Eales, K. L., Vettore, L. A., Walker, P. D., Vera-Sigüenza, E., Rana, H., Cuozzo, F., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110320 · Cited by 78 · see citing works
Peng, B., Li, W., Ding, J., et al. (2020) · Theranostics · doi:10.7150/thno.39241 · Cited by 72 · see citing works
Lee, B., Mahmud, I., Marchica, J., Dereziński, P., Qi, F., Wang, F., Joshi, P. K., Valerio, F., Rivera, I., Patel, V., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-60616-z · Cited by 70 · see citing works
GLS2 is protumorigenic in breast cancers
Dias, M. M., Adamóski, D., dos Reis, L. M., Ascenção, C. F. R., de Oliveira, K. R. S., Mafra, A. C. P., Bastos, A. C. D. S., Quintero, M., Cassago, C. A. D. G., Ferreira, I. M., et al. (2019) · Oncogene · doi:10.1038/s41388-019-1007-z · Cited by 68 · see citing works
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 · see citing works
Kandasamy, P., Zlobec, I., Nydegger, D. T., Pujol‐Giménez, J., Bhardwaj, R., Shirasawa, S., Tsunoda, T., & Hediger, M. A. (2021) · Molecular Oncology · doi:10.1002/1878-0261.12999 · Cited by 60 · see citing works
Huynh, T. Y. L., Zaręba, I., Baszanowska, W., Lewoniewska, S., & Palka, J. A. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03685-y · Cited by 59 · see citing works
Bogner, A. N., Stiers, K. M., & Tanner, J. J. (2021) · Amino Acids · doi:10.1007/s00726-021-02999-5 · Cited by 59 · see citing works
LncRNA XLOC_006390 promotes pancreatic carcinogenesis and glutamate metabolism by stabilizing c-Myc
He, J., Li, F., Zhou, Y., Hou, X., Liu, S., Li, X., Zhang, Y., Jing, X., & Yang, L. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.11.021 · Cited by 54 · see citing works
Self-citationYoshida, T., Yamasaki, S., Kaneko, O., Taoka, N., Tomimoto, Y., Namatame, I., Yahata, T., Kuromitsu, S., Cantley, L. C., & Lyssiotis, C. A. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.11.130 · Cited by 53 · see citing works
Cysteine as a Carbon Source, a Hot Spot in Cancer Cells Survival
Serpa, J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00947 · Cited by 53 · see citing works
Tissue of origin dictates GOT1 dependence and confers synthetic lethality to radiotherapy
Nelson, B. S., Lin, L., Kremer, D. M., Sousa, C. M., Cotta‐Ramusino, C., Myers, A. L., Ramos, J., Gao, T., Kovalenko, I., Wilder-Romans, K., et al. (2020) · Cancer & Metabolism · doi:10.1186/s40170-019-0202-2 · Cited by 51 · see citing works
Activation of MAT2A-RIP1 signaling axis reprograms monocytes in gastric cancer
Zhang, Y., Yang, H., Zhao, J., Wan, P., Hu, Y., Lv, K., Hu, Y., Yang, X., & Ma, M. (2021) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2020-001364 · Cited by 50 · see citing works
Xia, M., Li, X., Diao, Y., Du, B., & Li, Y. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100920 · Cited by 48 · see citing works
Self-citationLiu, H.-Y., Zhang, H.-S., Liu, M.-Y., Li, H., Wang, X., & Wang, M. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108964 · Cited by 48 · see citing works
Self-citationYao, B., Zhu, S., Wei, X., Chen, M., Feng, Y., Li, Z., Xu, X., Zhang, Y., Wang, Y., Zhou, J., et al. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01598-6 · Cited by 48 · see citing works
One-carbon epigenetics and redox biology of neurodegeneration
Coppedè, F. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.12.002 · Cited by 47 · see citing works
Lu, J., Chen, M., Tao, Z., Gao, S., Li, Y., Cao, Y., Lu, C., & Zou, X. (2017) · OncoTarget · doi:10.18632/oncotarget.19479 · Cited by 46 · see citing works
PRMT1 inhibition induces differentiation of colon cancer cells
Plotnikov, A. N., Kozer, N., Cohen, G., Carvalho, S., Duberstein, S., Almog, O., Solmesky, L. J., Shurrush, K. A., Babaev, I., Benjamin, S., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-77028-8 · Cited by 43 · see citing works
Helenius, I. T., Madala, H. R., & Yeh, J.-R. J. (2021) · Biomolecules · doi:10.3390/biom11111666 · Cited by 43 · see citing works
Reprogramming of mitochondrial proline metabolism promotes liver tumorigenesis
Ding, Z., Ericksen, R. E., Lee, Q. Y., & Han, W. (2021) · Amino Acids · doi:10.1007/s00726-021-02961-5 · Cited by 42 · see citing works
Zhang, Y., Chen, S.-W., Zhu, J., et al. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02512-2 · Cited by 41 · see citing works
PYCR, a key enzyme in proline metabolism, functions in tumorigenesis
Li, Y., Bie, J., Song, C., Liu, M., & Luo, J. (2021) · Amino Acids · doi:10.1007/s00726-021-03047-y · Cited by 39 · see citing works
Jin, L., Kiang, K. M. Y., Cheng, S. Y., & Leung, G. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00666-7 · Cited by 38 · see citing works
Raninga, P. V., He, Y., Datta, K. K., Lu, X. M., Maheshwari, U. R., Venkat, P., Mayoh, C., Gowda, H., Kalimutho, M., Hooper, J. D., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.12.011 · Cited by 36 · see citing works
Arginine Methylation in Brain Tumors: Tumor Biology and Therapeutic Strategies
Bryant, J.-P., Heiss, J. D., & Banasavadi‐Siddegowda, Y. (2021) · Cells · doi:10.3390/cells10010124 · Cited by 32 · see citing works
Oudaert, I., Satilmis, H., Vlummens, P., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02250-3 · Cited by 32 · see citing works
MAT2A as Key Regulator and Therapeutic Target in MLLr Leukemogenesis
Secker, K.-A., Bloechl, B., Keppeler, H., Duerr‐Stoerzer, S., Schmid, H., Schneidawind, D., Jeong, J., Hentrich, T., Schulze-Hentrich, J. M., & Schneidawind, C. (2020) · Cancers · doi:10.3390/cancers12051342 · Cited by 31 · see citing works
Targeting the methionine addiction of cancer.
Sedillo, J. C., & Cryns, V. L. (2022) · PubMed Central · Cited by 30 · see citing works
Expanding the Therapeutic World of Tryptophan Metabolism
Wyant, G. A., & Moslehi, J. J. (2022) · Circulation · doi:10.1161/circulationaha.122.059812 · Cited by 28 · see citing works
Proline dehydrogenase in cancer: apoptosis, autophagy, nutrient dependency and cancer therapy
Liu, Y., Mao, C., Liu, S., Xiao, D., Shi, Y., & Tao, Y. (2021) · Amino Acids · doi:10.1007/s00726-021-03032-5 · Cited by 25 · see citing works
Thomas, T. M., Miyaguchi, K., Edwards, L., et al. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-20-0086 · Cited by 24 · see citing works
Pharmacologic approaches to amino acid depletion for cancer therapy
Wilder, C. S., Chen, Z., & DiGiovanni, J. (2021) · Molecular Carcinogenesis · doi:10.1002/mc.23349 · Cited by 23 · see citing works
Serine synthesis influences tamoxifen response in ER+ human breast carcinoma
Metcalf, S. A., Petri, B. J., Kruer, T. L., Green, B., Dougherty, S. M., Wittliff, J. L., Klinge, C. M., & Clem, B. F. (2020) · Endocrine Related Cancer · doi:10.1530/erc-19-0510 · Cited by 21 · see citing works
Ościłowska, I., Rolkowski, K., Baszanowska, W., Huynh, T. Y. L., Lewoniewska, S., Nizioł, M., Sawicka, M., Bielawska, K., Szoka, P., Miltyk, W., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042354 · Cited by 21 · see citing works
Li, D., Yang, Z., Liu, Z., et al. (2020) · Applied immunohistochemistry & molecular morphology · doi:10.1097/pai.0000000000000705 · Cited by 20 · see citing works
Grasping for aspartate in tumour metabolism
Fu, A., & Danial, N. N. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0137-9 · Cited by 19 · see citing works
Yang, Y., Zheng, M., Han, F., Shang, L., Li, M., Gu, X., Li, H., & Chen, L. (2022) · Journal of Molecular Medicine · doi:10.1007/s00109-022-02181-8 · Cited by 19 · see citing works
Methylation of HBP1 by PRMT1 promotes tumor progression by regulating actin cytoskeleton remodeling
Wang, J., Yang, R., Cheng, Y., Zhou, Y., Zhang, T., Wang, S., Li, H., Jiang, W., & Zhang, X. (2022) · Oncogenesis · doi:10.1038/s41389-022-00421-7 · Cited by 18 · see citing works
Yan, S., Qi, C., Song, W., Xu, Q., Gu, L., Sun, W., & Zhang, Y. (2021) · Marine Drugs · doi:10.3390/md19110588 · Cited by 17 · see citing works
1-C Metabolism—Serine, Glycine, Folates—In Acute Myeloid Leukemia
Mahmood, K., & Emadi, A. (2021) · Pharmaceuticals · doi:10.3390/ph14030190 · Cited by 16 · see citing works
Gaglio, D., Bonanomi, M., Valtorta, S., Bharat, R., Ripamonti, M., Conte, F., Fiscon, G., Righi, N., Napodano, E., Papa, F., et al. (2020) · Cancer & Metabolism · doi:10.1186/s40170-020-00227-4 · Cited by 15 · see citing works
Methyl Group Metabolism in Differentiation, Aging, and Cancer
Erichsen, L., Thimm, C., & Santourlidis, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158378 · Cited by 15 · see citing works
Increased Response to Immune Checkpoint Inhibitors with Dietary Methionine RestrictionPreprint
Morehead, L. C., Garg, S., Wallis, K., Siegel, E. R., Tackett, A. J., & Miousse, I. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.05.535695 · Cited by 12 · see citing works
Enhanced Antitumor Effect in Liver Cancer by Amino Acid Depletion-Induced Oxidative Stress
Okuda, K., Umemura, A., Kataoka, S., Yano, K., Takahashi, A., Okishio, S., Taketani, H., Seko, Y., Nishikawa, T., Yamaguchi, K., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.758549 · Cited by 11 · see citing works
Interactions between Radiation and One-Carbon Metabolism
Korimerla, N., & Wahl, D. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031919 · Cited by 11 · see citing works
Jiang, Q., Li, J., Jing, M., Zhang, Y.-X., Zhang, Q.-Q., Cai, C.-B., Wang, D., Qi, H.-W., Li, T., Li, Y., et al. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/8678363 · Cited by 11 · see citing works
Metformin Induces PRODH/POX-Dependent Apoptosis in Breast Cancer Cells
Huynh, T. Y. L., Ościłowska, I., Szoka, Ł., Piktel, E., Baszanowska, W., Bielawska, K., Bucki, R., Miltyk, W., & Palka, J. A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.869413 · Cited by 10 · see citing works
Zhao, X., Wang, L., Lin, H., Wang, J., Fu, J., Zhu, D., & Xu, W. (2022) · PubMed Central · doi:10.22074/cellj.2022.7907 · Cited by 8 · see citing works
Nur, S. M., Mohammed, M. R. S., Zamzami, M. A., Choudhry, H., Ahmad, A., Ateeq, B., Rather, I. A., & Khan, M. I. (2022) · Metabolites · doi:10.3390/metabo12030267 · Cited by 7 · see citing works
Guardamagna, I., Iaria, O., Lonati, L., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032983 · Cited by 4 · see citing works
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Shuvalov, O., Kirdeeva, Y., Fefilova, E., Daks, A., Fedorova, O., Parfenyev, S., Nazarov, A., Vlasova, Y., Krasnov, G. S., & Barlev, N. A. (2024) · Antioxidants · doi:10.3390/antiox13111349 · Cited by 9 · see citing works
- Authors
- Li, X., & Zhang, H.
- Affiliations
- Beijing University of Technology (CN)
- Faculty of Environment and Life Beijing University of Technology Beijing China
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2023-05-19
- Volume
- 291
- Issue
- 3
- Pages
- 412-429
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W4367668286
- Cited by
- 90
- References
- 138
- Citations by year
- 2026: 36 · 2025: 28 · 2024: 21 · 2023: 5
- FWCI
- 2.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Journal (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Natural Science Foundation of Beijing Municipality (7192014)
- National Laboratory of Biomacromolecules (2017kf02)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer and biochemical research
- Keywords
- amino acid metabolism, redox homeostasis, epigenetic regulation, cancer metabolism, cancer cells, oxidative stress, genetic stress, epigenetic modifications, metabolic reprogramming
- MeSH terms
- Amino Acids, Humans, Neoplasms, Oxidation-Reduction, Oxidative Stress, Epigenesis, Genetic
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