Reprogramming of serine, glycine and one-carbon metabolism in cancer

Hallmarks of Cancer: The Next Generation

Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · 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

The metabolism of tumors in the body

Warburg, O., Wind, F., & Negelein, E. (1927) · Journal of General Physiology · doi:10.1085/jgp.8.6.519 · Cited by 4,416 · see citing works

Cancer-associated IDH1 mutations produce 2-hydroxyglutarate

Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154 · see citing works

An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336 · 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

The Common Feature of Leukemia-Associated IDH1 and IDH2 Mutations Is a Neomorphic Enzyme Activity Converting α-Ketoglutarate to 2-Hydroxyglutarate

Ward, P. S., Patel, J., Wise, D. R., Abdel-Wahab, O., Bennett, B. D., Coller, H. A., Cross, J. R., Fantin, V. R., Hedvat, C. V., Perl, A. E., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.01.020 · Cited by 2,020 · see citing works

Temporary Remissions in Acute Leukemia in Children Produced by Folic Acid Antagonist, 4-Aminopteroyl-Glutamic Acid (Aminopterin)

Farber, S., Diamond, L. K., Mercer, R. D., Sylvester, R. F., & Wolff, J. A. (1948) · New England Journal of Medicine · doi:10.1056/nejm194806032382301 · Cited by 1,806 · see citing works

Functional genomics reveal that the serine synthesis pathway is essential in breast cancer

Possemato, R., Marks, K. M., Shaul, Y. D., Pacold, M. E., Kim, D., Birsoy, K., Sethumadhavan, S., Woo, H.-K., Jang, H. G., Jha, A. K., et al. (2011) · Nature · doi:10.1038/nature10350 · Cited by 1,683 · see citing works

NRF2 and the Hallmarks of Cancer

Rojo de la Vega, M., Chapman, E., & Zhang, D. D. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.03.022 · Cited by 1,672 · see citing works

Serine, glycine and one-carbon units: cancer metabolism in full circle

Locasale, J. W. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3557 · Cited by 1,671 · see citing works

Metabolite profiling identifies a key role for glycine in rapid cancer cell proliferation

Jain, M., Nilsson, R., Sharma, S., Madhusudhan, N., Kitami, T., Souza, A. L., Kafri, R., Kirschner, M. W., Clish, C. B., & Mootha, V. K. (2012) · Science · doi:10.1126/science.1218595 · Cited by 1,403 · see citing works

An essential role of the mitochondrial electron transport chain in cell proliferation is to enable aspartate synthesis

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

MYC, Metabolism, and Cancer

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 1,375 · see citing works

Oxidative stress inhibits distant metastasis by human melanoma cells

Piskounova, E., Agathocleous, M., Murphy, M. M., Hu, Z., Huddlestun, S. E., Zhao, Z., Leitch, A. M., Johnson, T. M., DeBerardinis, R. J., & Morrison, S. J. (2015) · Nature · doi:10.1038/nature15726 · Cited by 1,269 · see citing works

Inhibition of Pyruvate Kinase M2 by Reactive Oxygen Species Contributes to Cellular Antioxidant Responses

Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B., Jiang, J., Shen, M., Bellinger, G., Sasaki, A. T., Locasale, J. W., Auld, D. S., et al. (2011) · Science · doi:10.1126/science.1211485 · Cited by 1,196 · see citing works

Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells

Sullivan, L. B., Gui, D. Y., Hosios, A. M., Bush, L. N., Freinkman, E., & Vander Heiden, M. G. (2015) · Cell · doi:10.1016/j.cell.2015.07.017 · Cited by 1,173 · see citing works

Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis

Locasale, J. W., Grassian, A. R., Melman, T., Lyssiotis, C. A., Mattaini, K. R., Bass, A. J., Heffron, G., Metallo, C. M., Muranen, T., Sharfi, H., et al. (2011) · Nature Genetics · doi:10.1038/ng.890 · Cited by 1,120 · see citing works

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 · see citing works

Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment

Schafer, Z. T., Grassian, A. R., Song, L., Jiang, Z., Gerhart-Hines, Z., Irie, H. Y., Gao, S., Puigserver, P., & Brugge, J. S. (2009) · Nature · doi:10.1038/nature08268 · Cited by 1,031 · see citing works

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 · see citing works

Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response

Lu, P. D., Harding, H. P., & Ron, D. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200408003 · Cited by 1,006 · see citing works

The 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

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 · see citing works

Multi-omics analysis identifies ATF4 as a key regulator of the mitochondrial stress response in mammals

Quirós, P. M., Prado, M. A., Zamboni, N., D’Amico, D., Williams, R. W., Finley, D., Gygi, S. P., & Auwerx, J. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201702058 · Cited by 832 · see citing works

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 · see citing works

NFS1 undergoes positive selection in lung tumours and protects cells from ferroptosis

Alvarez, S. W., Sviderskiy, V. O., Terzi, E. M., Papagiannakopoulos, T., Moreira, A. L., Adams, S., Sabatini, D. M., Birsoy, K., & Possemato, R. (2017) · Nature · doi:10.1038/nature24637 · Cited by 787 · see citing works

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 747 · see citing works

Histone Methylation Dynamics and Gene Regulation Occur through the Sensing of One-Carbon Metabolism

Mentch, S. J., Mehrmohamadi, M., Huang, L., Liu, X., Gupta, D., Mattocks, D. A. L., Padilla, P. G., Ables, G. P., Bamman, M. M., Thalacker‐Mercer, A. E., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.024 · Cited by 706 · see citing works

Compartmentalization of Mammalian Folate-Mediated One-Carbon Metabolism

Tibbetts, A. S., & Appling, D. R. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104810 · Cited by 692 · see citing works

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 · see citing works

Glycine decarboxylase activity drives non-small cell lung cancer tumor-initiating cells and tumorigenesis

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 · see citing works

Serine is an essential metabolite for effector T cell expansion

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

Dietary methionine influences therapy in mouse cancer models and alters human metabolism

Gao, X., Sanderson, S. M., Dai, Z., Reid, M. A., Cooper, D. E., Lu, M., Richie, J. P., Ciccarella, A., Calcagnotto, A., Mikhael, P. G., et al. (2019) · Nature · doi:10.1038/s41586-019-1437-3 · Cited by 657 · see citing works

Influence of Threonine Metabolism on <i>S</i> -Adenosylmethionine and Histone Methylation

Shyh-Chang, N., Locasale, J. W., Lyssiotis, C. A., Zheng, Y., Teo, R. Y., Ratanasirintrawoot, S., Zhang, J., Onder, T., Unternaehrer, J. J., Zhu, H., et al. (2013) · Science · doi:10.1126/science.1226603 · Cited by 638 · see citing works

Metabolic enzyme expression highlights a key role for MTHFD2 and the mitochondrial folate pathway in cancer

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 · see citing works

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 · 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

LY231514, a pyrrolo[2,3-d]pyrimidine-based antifolate that inhibits multiple folate-requiring enzymes.

Shih, C., Chen, V. J., Gossett, L. S., Gates, S. B., MacKellar, W. C., Habeck, L. L., Shackelford, K. A., Mendelsohn, L. G., Soose, D. J., Patel, V. F., et al. (1997) · PubMed · Cited by 560 · 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

Thymidylate synthetase - a target enzyme in cancer chemotherapy

Danenberg, P. V. (1977) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(77)90001-4 · Cited by 504 · see citing works

UPRmt regulation and output: a stress response mediated by mitochondrial-nuclear communication

Melber, A., & Haynes, C. M. (2018) · Cell Research · doi:10.1038/cr.2018.16 · Cited by 488 · see citing works

Toward a better understanding of methotrexate

Kremer, J. M. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20278 · Cited by 478 · 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

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 · see citing works

Serine Metabolism Supports the Methionine Cycle and DNA/RNA Methylation through De Novo ATP Synthesis in Cancer Cells

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 440 · 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

Methionine is a metabolic dependency of tumor-initiating cells

Wang, Z., Yip, L. Y., Lee, J. H. J., Wu, Z., Chew, H. Y., Chong, P. K. W., Teo, C. C., Ang, H. Y.-K., Peh, K. L. E., Yuan, J. X., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0423-5 · Cited by 425 · see citing works

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 · see citing works

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 419 · see citing works

Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation

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 410 · see citing works

Uber den Stoffwechsel der Karzinomezellen

Warburg, O. (1924) · Medical Entomology and Zoology · Cited by 401 · see citing works

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 · see citing works

Spatiotemporal Control of Acetyl-CoA Metabolism in Chromatin Regulation

Sivanand, S., Viney, I. A., & Wellen, K. E. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.004 · Cited by 356 · see citing works

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 · see citing works

Folic Acid and Risk of Prostate Cancer: Results From a Randomized Clinical Trial

Figueiredo, J. C., Grau, M. V., Haile, R. W., Sandler, R. S., Summers, R. W., Bresalier, R. S., Burke, C. A., McKeown‐Eyssen, G., & Baron, J. A. (2009) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djp019 · Cited by 340 · see citing works

cMyc-mediated activation of serine biosynthesis pathway is critical for cancer progression under nutrient deprivation conditions

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 311 · see citing works

High in vivo rates of methionine biosynthesis in transformed human and malignant rat cells auxotrophic for methionine.

Hoffman, R. M., & Erbe, R. W. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.5.1523 · Cited by 300 · see citing works

Mitochondrial myopathy induces a starvation-like response

Tyynismaa, H., Carroll, C. J., Raimundo, N., Ahola-Erkkilä, S., Wenz, T., Ruhanen, H., Guse, K., Hemminki, A., Peltola-Mjøsund, K. E., Tulkki, V., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq310 · Cited by 300 · see citing works

Pemetrexed: biochemical and cellular pharmacology, mechanisms, and clinical applications

Chattopadhyay, S., Moran, R. G., & Goldman, I. D. (2007) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0343 · Cited by 283 · 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

Human SHMT inhibitors reveal defective glycine import as a targetable metabolic vulnerability of diffuse large B-cell lymphoma

Ducker, G. S., Ghergurovich, J. M., Mainolfi, N., Suri, V., Jeong, S. K., Hsin-Jung Li, S., Friedman, A., Manfredi, M. G., Gitai, Z., Kim, H., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706617114 · Cited by 261 · see citing works

SFXN1 is a mitochondrial serine transporter required for one-carbon metabolism

Kory, N., Wyant, G. A., Prakash, G., de Bos, J. U., Bottanelli, F., Pacold, M. E., Chan, S. H., Lewis, C. A., Wang, T., Keys, H. R., et al. (2018) · Science · doi:10.1126/science.aat9528 · Cited by 246 · see citing works

Metabolism, Activity, and Targeting of D- and L-2-Hydroxyglutarates

Ye, D., Guan, K.-L., & Xiong, Y. (2018) · Trends in Cancer · doi:10.1016/j.trecan.2017.12.005 · Cited by 242 · see citing works

Effect of folic acid supplementation on genomic DNA methylation in patients with colorectal adenoma

Pufulete, M., Abbadi, R. A.-G., Khushal, A., Appleby, P., Harris, N., Gout, S., Emery, P. W., & Sanders, T. A. B. (2005) · Gut · doi:10.1136/gut.2004.054718 · Cited by 239 · see citing works

SHMT2 Desuccinylation by SIRT5 Drives Cancer Cell Proliferation

Yang, X. P., Wang, Z., Li, X., Liu, B., Liu, M., Liu, L., Chen, S., Ren, M., Wang, Y., Yu, M., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1912 · Cited by 231 · see citing works

Serine Catabolism Feeds NADH when Respiration Is Impaired

Yang, L., García‐Cañaveras, J. C., Chen, Z., Wang, L., Liang, L., Jang, C., Mayr, J. A., Zhang, Z., Ghergurovich, J. M., Zhan, L., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.017 · Cited by 213 · see citing works

Nrf2- and ATF4-Dependent Upregulation of xCT Modulates the Sensitivity of T24 Bladder Carcinoma Cells to Proteasome Inhibition

Ye, P., Mimura, J., Okada, T., Sato, H., Liu, T., Maruyama, A., Οhyama, C., & Itoh, K. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00221-14 · Cited by 209 · see citing works

A Functional Screen for Myc-Responsive Genes Reveals Serine Hydroxymethyltransferase, a Major Source of the One-Carbon Unit for Cell Metabolism

Nikiforov, M. A., Chandriani, S. J., O’Connell, B. C., Petrenko, O., Kotenko, I., Beavis, A. J., Sedivy, J. M., & Cole, M. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5793-5800.2002 · Cited by 201 · see citing works

Serine Catabolism by SHMT2 Is Required for Proper Mitochondrial Translation Initiation and Maintenance of Formylmethionyl-tRNAs

Minton, D. R., Nam, M., McLaughlin, D. J., Shin, J., Bayraktar, E. C., Alvarez, S., Sviderskiy, V. O., Papagiannakopoulos, T. Y., Sabatini, D. M., Birsoy, K., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.024 · Cited by 192 · see citing works

Modulation of Redox Homeostasis by Inhibition of MTHFD2 in Colorectal Cancer: Mechanisms and Therapeutic Implications

Ju, H., Lu, Y., Chen, D.-L., Zuo, Z.-X., Liu, Z., Wu, Q.-N., Mo, H., Wang, Z., Wang, D., Pu, H., et al. (2018) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djy160 · Cited by 189 · see citing works

Increased Serine and One-Carbon Pathway Metabolism by PKCλ/ι Deficiency Promotes Neuroendocrine Prostate Cancer

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 187 · see citing works

Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria

Anderson, D. D., Quintero, C. M., & Stover, P. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103623108 · Cited by 186 · see citing works

Analysis of Myc Bound Loci Identified by CpG Island Arrays Shows that Max Is Essential for Myc-Dependent Repression

Mao, D. Y. L., Watson, J. D., Yan, P. S., Baršytė-Lovejoy, D., Khosravi, F., Wong, W. W.-L., Farnham, P., Huang, T. H. ‐., & Penn, L. Z. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00297-5 · Cited by 183 · see citing works

From methotrexate to pemetrexed and beyond. A review of the pharmacodynamic and clinical properties of antifolates

Walling, J. (2006) · Investigational New Drugs · doi:10.1007/s10637-005-4541-1 · Cited by 182 · see citing works

Serine one-carbon catabolism with formate overflow

Meiser, J., Tumanov, S., Maddocks, O., Labuschagne, C. F., Athineos, D., Van Den Broek, N., Mackay, G. M., Gottlieb, E., Blyth, K., Vousden, K., et al. (2016) · Science Advances · doi:10.1126/sciadv.1601273 · Cited by 174 · see citing works

Targeting MTHFD2 in acute myeloid leukemia

Pikman, Y., Puissant, A., Alexe, G., Furman, A. A., Chen, L. M., Frumm, S. M., Ross, L. S., Fenouille, N., Bassil, C. F., Lewis, C. A., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151574 · Cited by 157 · see citing works

Mechanisms of methotrexate resistance in osteosarcoma.

Guo, W., Healey, J. H., Meyers, P. A., Ladanyi, M., Huvos, A. G., Bertino, J. R., & Gorlick, R. G. (1999) · PubMed · Cited by 152 · see citing works

Defective respiration and one-carbon metabolism contribute to impaired naïve T cell activation in aged mice

Ron‐Harel, N., Notarangelo, G., Ghergurovich, J. M., Paulo, J. A., Sage, P. T., Santos, D., Satterstrom, F. K., Gygi, S. P., Rabinowitz, J. D., Sharpe, A. H., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804149115 · Cited by 150 · see citing works

Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor

Davis, S. R., Stacpoole, P. W., Williamson, J., Kick, L. S., Quinlivan, E. P., Coats, B. S., Shane, B., Bailey, L. B., & Gregory, J. F. (2004) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00351.2003 · Cited by 149 · see citing works

Cytoplasmic Serine Hydroxymethyltransferase Regulates the Metabolic Partitioning of Methylenetetrahydrofolate but Is Not Essential in Mice

MacFarlane, A. J., Liu, X., Perry, C. A., Flodby, P., Allen, R. H., Stabler, S. P., & Stover, P. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802671200 · Cited by 148 · see citing works

Methionine metabolism influences genomic architecture and gene expression through H3K4me3 peak width

Dai, Z., Mentch, S. J., Gao, X., Nichenametla, S. N., & Locasale, J. W. (2018) · Nature Communications · doi:10.1038/s41467-018-04426-y · Cited by 132 · see citing works

SHMT1 knockdown induces apoptosis in lung cancer cells by causing uracil misincorporation

Paone, A., Marani, M., Fiascarelli, A., Rinaldo, S., Giardina, G., Contestabile, R., Paiardini, A., & Cutruzzolà, F. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.482 · Cited by 129 · see citing works

The Action of Pteroylglutamic Conjugates on Man

Farber, S., Cutler, E. C., Hawkins, J. W., Harrison, J., Peirce, E. C., & Lenz, G. G. (1947) · Science · doi:10.1126/science.106.2764.619 · Cited by 128 · see citing works

Effects of folate supplementation on two provisional molecular markers of colon cancer: a prospective, randomized trial

Kim, Y.-I., Baik, H. W., Fawaz, K. A., Knox, T. A., Lee, Y., Norton, R. A., Libby, E. D., & Mason, J. B. (2001) · The American Journal of Gastroenterology · doi:10.1111/j.1572-0241.2001.03474.x · Cited by 128 · see citing works

Serine Hydroxymethyltransferase Anchors de Novo Thymidylate Synthesis Pathway to Nuclear Lamina for DNA Synthesis

Anderson, D. D., Woeller, C. F., Chiang, E. I., Shane, B., & Stover, P. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.333120 · Cited by 124 · see citing works

Effect of folate supplementation on DNA methylation of rectal mucosa in patients with colonic adenomas: correlation with nutrient intake

Cravo, M. L., Pinto, A. G., Chaves, P. P., da Cruz, J. A. L., Lage, P., Leitão, C. N., & Mira, F. C. (1998) · Clinical Nutrition · doi:10.1016/s0261-5614(98)80304-x · Cited by 122 · see citing works

Global DNA and p53 Region-Specific Hypomethylation in Human Colonic Cells Is Induced by Folate Depletion and Reversed by Folate Supplementation

Wasson, G. R., McGlynn, A. P., McNulty, H., O'Reilly, S. L., McKelvey‐Martin, V. J., McKerr, G., Strain, J., Scott, J. M., & Downes, C. S. (2006) · Journal of Nutrition · doi:10.1093/jn/136.11.2748 · Cited by 122 · see citing works

Mitochondrial C1-Tetrahydrofolate Synthase (MTHFD1L) Supports the Flow of Mitochondrial One-carbon Units into the Methyl Cycle in Embryos

Pike, S., Rajendra, R., Artzt, K., & Appling, D. R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.079855 · Cited by 120 · see citing works

Increased formate overflow is a hallmark of oxidative cancer

Meiser, J., Schuster, A. M., Pietzke, M., Voorde, J. V., Athineos, D., Oizel, K., Burgos-Barragan, G., Wit, N., Dhayade, S., Morton, J. P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03777-w · Cited by 119 · see citing works

MTHFD2 links RNA methylation to metabolic reprogramming in renal cell carcinoma

Green, N. H., Galvan, D. L., Badal, S. S., Chang, B. H., LeBleu, V. S., Long, J., Jonasch, E., & Danesh, F. R. (2019) · Oncogene · doi:10.1038/s41388-019-0869-4 · Cited by 117 · see citing works

The folate-coupled enzyme MTHFD2 is a nuclear protein and promotes cell proliferation

Gustafsson Sheppard, N., Jarl, L., Mahadessian, D., Strittmatter, L., Schmidt, A., Madhusudan, N., Tegnér, J., Lundberg, E. K., Asplund, A., Jain, M., et al. (2015) · Scientific Reports · doi:10.1038/srep15029 · Cited by 115 · see citing works

High-throughput RNAi screening for novel modulators of vimentin expression identifies MTHFD2 as a regulator of breast cancer cell migration and invasion

Lehtinen, L., Ketola, K., Mäkelä, R., Mpindi, J.-P., Viitala, M., Kallioniemi, O., & Iljin, K. (2012) · Oncotarget · doi:10.18632/oncotarget.756 · Cited by 109 · see citing works

Primed, constant infusion with [2H3]serine allows in vivo kinetic measurement of serine turnover, homocysteine remethylation, and transsulfuration processes in human one-carbon metabolism

Gregory, J. F., Cuskelly, G. J., Shane, B., Toth, J. P., Baumgartner, T. G., & Stacpoole, P. W. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/72.6.1535 · Cited by 108 · see citing works

A strategy for identifying transcription factor binding sites reveals two classes of genomic c-Myc target sites

Haggerty, T. J., Zeller, K. I., Osthus, R. C., Wonsey, D. R., & Dang, C. V. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0931346100 · Cited by 106 · see citing works

How pyridoxal 5′‐phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state

Giardina, G., Brunotti, P., Fiascarelli, A., Cicalini, A., Costa, M. G. S., Buckle, A. M., di Salvo, M. L., Giorgi, A., Marani, M., Paone, A., et al. (2015) · FEBS Journal · doi:10.1111/febs.13211 · Cited by 104 · see citing works

Proteomic profiling of breast cancer metabolism identifies SHMT2 and ASCT2 as prognostic factors

Bernhardt, S., Bayerlová, M., Vetter, M., Wachter, A., Mitra, D., Hanf, V., Lantzsch, T., Uleer, C., Peschel, S., John, J., et al. (2017) · Breast Cancer Research · doi:10.1186/s13058-017-0905-7 · Cited by 101 · see citing works

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 · see citing works

Regulation of the Balance of One-carbon Metabolism inSaccharomyces cerevisiae

Piper, M. D. W., Hong, S.-P., Ball, G. E., & Dawes, I. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004248200 · Cited by 94 · see citing works

Resistance Mechanisms to Methotrexate in Tumors

Bertino, J. R., Göker, E., Gorlick, R. G., Li, W. W., & Banerjee, D. (1996) · Stem Cells · doi:10.1002/stem.140005 · Cited by 93 · see citing works

Mouse Genetics Suggests Cell-Context Dependency for Myc-Regulated Metabolic Enzymes during Tumorigenesis

Nilsson, L. M., Plym Forshell, T. Z., Rimpi, S., Kreutzer, C., Pretsch, W., Bornkamm, G. W., & Nilsson, J. A. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002573 · Cited by 85 · see citing works

The natural product carolacton inhibits folate-dependent C1 metabolism by targeting FolD/MTHFD

Fu, C., Sikandar, A., Donner, J., Zaburannyi, N., Herrmann, J. E., Reck, M., Wagner‐Döbler, I., Koehnke, J., & Müller, R. (2017) · Nature Communications · doi:10.1038/s41467-017-01671-5 · Cited by 84 · see citing works

Metabolic Profiling Reveals a Dependency of Human Metastatic Breast Cancer on Mitochondrial Serine and One-Carbon Unit Metabolism

Li, A. M., Ducker, G. S., Li, Y., Seoane, J. A., Xiao, Y., Melemenidis, S., Zhou, Y., Liu, L., Vanharanta, S., Graves, E. E., et al. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0606 · Cited by 84 · see citing works

Downregulating serine hydroxymethyltransferase 2 (SHMT2) suppresses tumorigenesis in human hepatocellular carcinoma

Woo, C. C., Chen, W. C., Teo, X. Q., Radda, G. K., & Lee, P. T. H. (2016) · Oncotarget · doi:10.18632/oncotarget.10415 · Cited by 82 · see citing works

Identification of miR-193b Targets in Breast Cancer Cells and Systems Biological Analysis of Their Functional Impact

Leivonen, S., Rokka, A., Östling, P., Kohonen, P. J., Corthals, G. L., Kallioniemi, O., & Perälä, M. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.005322 · Cited by 76 · see citing works

IDH3α regulates one-carbon metabolism in glioblastoma

May, J., Kouri, F. M., Hurley, L., Liu, J., Tommasini-Ghelfi, S., Ji, Y., Gao, P., Calvert, A. E., Lee, A., Chandel, N. S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aat0456 · Cited by 75 · see citing works

The Structure of Chicken Liver Xanthine Dehydrogenase

Nishino, T., Nöda, K., Amaya, Y., Sato, A., & Nishino, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2818 · Cited by 74 · see citing works

MTHFD2 overexpression predicts poor prognosis in renal cell carcinoma and is associated with cell proliferation and vimentin-modulated migration and invasion

Lin, H., Huang, B., Wang, H., Liu, X., Hong, Y., Qiu, S., & Zheng, J. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000495402 · Cited by 73 · see citing works

Proximity‐dependent labeling methods for proteomic profiling in living cells

Chen, C., & Perrimon, N. (2017) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.272 · Cited by 72 · see citing works

Carbon-13 NMR detection of folate-mediated serine and glycine synthesis in vivo in Saccharomyces cerevisiae

Pasternack, L. B., Laude, D. A., & Appling, D. R. (1992) · Biochemistry · doi:10.1021/bi00152a005 · Cited by 68 · see citing works

Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase

Shin, M., Momb, J., & Appling, D. R. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0173-0 · Cited by 66 · see citing works

EIF2A promotes cell survival during paclitaxel treatment in vitro and in vivo

Chen, L., He, J., Zhou, J., Xiao, Z. Q., Ding, N., Duan, Y., Li, W., & Sun, L. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14469 · Cited by 64 · see citing works

The importance of mitochondrial folate enzymes in human colorectal cancer

Miyo, M., Konno, M., Colvin, H. S., Nishida, N., Koseki, J., Kawamoto, K., Tsunekuni, K., Nishimura, J., Hata, T., Takemasa, I., et al. (2016) · Oncology Reports · doi:10.3892/or.2016.5264 · Cited by 60 · see citing works

Novel Pyrrolo[3,2- d ]pyrimidine Compounds Target Mitochondrial and Cytosolic One-carbon Metabolism with Broad-spectrum Antitumor Efficacy

Dekhne, A. S., Shah, K., Ducker, G. S., Katinas, J. M., Wong-Roushar, J., Nayeen, M. J., Doshi, A., Ning, C., Bao, X., Frühauf, J., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0037 · Cited by 59 · see citing works

A pyrazolopyran derivative preferentially inhibits the activity of human cytosolic serine hydroxymethyltransferase and induces cell death in lung cancer cells

Marani, M., Paone, A., Fiascarelli, A., Macone, A., Gargano, M., Rinaldo, S., Giardina, G., Pontecorvi, V., Koes, D. R., McDermott, L. A., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.6726 · Cited by 57 · see citing works

EWS/FLI is a Master Regulator of Metabolic Reprogramming in Ewing Sarcoma

Tanner, J. M., Bensard, C., Wei, P., Krah, N. M., Schell, J. C., Gardiner, J. D., Schiffman, J. D., Lessnick, S. L., & Rutter, J. P. (2017) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0182 · Cited by 57 · see citing works

MTHFD1L, A Folate Cycle Enzyme, Is Involved in Progression of Colorectal Cancer

Agarwal, S., Behring, M. P., Hale, K., Diffalha, S. A., Wang, K., Manne, U., & Varambally, S. (2019) · Translational Oncology · doi:10.1016/j.tranon.2019.07.011 · Cited by 55 · see citing works

Mice deficient in the Shmt2 gene have mitochondrial respiration defects and are embryonic lethal

Tani, H., Ohnishi, S., Shitara, H., Mito, T., Yamaguchi, M., Yonekawa, H., Hashizume, O., Ishikawa, K., Nakada, K., & Hayashi, J. (2018) · Scientific Reports · doi:10.1038/s41598-017-18828-3 · Cited by 54 · see citing works

No Effect of Folic Acid Supplementation on Global DNA Methylation in Men and Women with Moderately Elevated Homocysteine

Jung, A. Y., Smulders, Y. M., Verhoef, P., Kok, F. J., Blom, H. J., Kok, R. M., Kampman, E., & Durga, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024976 · Cited by 48 · see citing works

miR-615-5p prevents proliferation and migration through negatively regulating serine hydromethyltransferase 2 (SHMT2) in hepatocellular carcinoma

Wu, X., Deng, L., Tang, D., Ying, G., Yao, X., Liu, F., & Gui, L. (2015) · Tumor Biology · doi:10.1007/s13277-015-4506-8 · Cited by 47 · see citing works

Protein interaction and functional data indicate MTHFD2 involvement in RNA processing and translation

Koufaris, C., & Nilsson, R. (2018) · Cancer & Metabolism · doi:10.1186/s40170-018-0185-4 · Cited by 44 · see citing works

Properties of Tetrahydropteroylpentaglutamate Bound to 10-Formyltetrahydrofolate Dehydrogenase

Kim, D. W., Huang, T. H., Schirch, D. M., & Schirch, V. (1996) · Biochemistry · doi:10.1021/bi9619684 · Cited by 41 · see citing works

Mitochondrial serine hydroxymethyltransferase 2 is a potential diagnostic and prognostic biomarker for human glioma

Wang, B., Wang, W., Zhu, Z., Zhang, X., Tang, F., Wang, D., Liu, X., Xiao-ling, Y. A. N., & Zhuang, H. (2017) · Clinical Neurology and Neurosurgery · doi:10.1016/j.clineuro.2017.01.005 · Cited by 40 · see citing works

Positive correlation between expression level of mitochondrial serine hydroxymethyltransferase and breast cancer grade

Yin, K. (2015) · OncoTargets and Therapy · doi:10.2147/ott.s82433 · Cited by 29 · see citing works

DNA hypomethylation of CBS promoter induced by folate deficiency is a potential noninvasive circulating biomarker for colorectal adenocarcinomas

Xue, G., Lu, C., Pan, S., Zhang, Y., Miao, H., Shan, S., Zhu, X., & Zhang, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.17988 · Cited by 18 · see citing works

Disruption of the mouse Shmt2 gene confers embryonic anaemia via foetal liver-specific metabolomic disorders

Tani, H., Mito, T., Velagapudi, V., Ishikawa, K., Umehara, M., Nakada, K., Suomalainen, A., & Hayashi, J. (2019) · Scientific Reports · doi:10.1038/s41598-019-52372-6 · Cited by 14 · see citing works

A bacterial pan-genome makes gene essentiality strain-dependent and evolvable

Rosconi, F., Rudmann, E., Li, J., Surujon, D., Anthony, J. S., Frank, M. W., Jones, D. S., Rock, C. O., Rosch, J. W., Johnston, C. D., et al. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01208-7 · Cited by 122 · see citing works

SHMT2-mediated mitochondrial serine metabolism drives 5-FU resistance by fueling nucleotide biosynthesis

Pranzini, E., Pardella, E., Muccillo, L., Leo, A., Nesi, I., Santi, A., Parri, M., Zhang, T., Uribe, A. H., Lottini, T., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111233 · Cited by 105 · see citing works

Regulatory mechanisms of one-carbon metabolism enzymes

Petrova, B., Maynard, A. G., Wang, P., & Kanarek, N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105457 · Cited by 103 · see citing works

Targeting serine-glycine-one-carbon metabolism as a vulnerability in cancers

Sun, W. Y., Liu, R., Gao, X., Lin, Z., Tang, H., Cui, H., & Zhao, E. (2023) · Biomarker Research · doi:10.1186/s40364-023-00487-4 · Cited by 82 · see citing works

Dissecting the Crosstalk between NRF2 Signaling and Metabolic Processes in Cancer

DeBlasi, J. M., & DeNicola, G. M. (2020) · Cancers · doi:10.3390/cancers12103023 · Cited by 80 · see citing works

ADH1C inhibits progression of colorectal cancer through the ADH1C/PHGDH /PSAT1/serine metabolic pathway

Li, S., Hong, Y., Wan, L., Liu, J.-Y., Ren, L., Yang, Y., Ge, B., Zhang, Y., Fu, W.-Q., Zheng, X., et al. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00894-7 · Cited by 60 · see citing works

A review of small-molecule inhibitors of one-carbon enzymes: SHMT2 and MTHFD2 in the spotlight

Cuthbertson, C. R., Arabzada, Z., Bankhead, A., Kyani, A., & Neamati, N. (2021) · ACS Pharmacology &amp; Translational Science · doi:10.1021/acsptsci.0c00223 · Cited by 57 · see citing works

Factors Determining Epithelial-Mesenchymal Transition in Cancer Progression

Tomecka, P., Kunachowicz, D., Górczyńska, J., Gebuza, M., Kuźnicki, J., Skinderowicz, K., & Choromańska, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168972 · Cited by 58 · see citing works

Metabolomics and the Multi-Omics View of Cancer

Wishart, D. S. (2022) · Metabolites · doi:10.3390/metabo12020154 · Cited by 51 · see citing works

Serine Metabolic Reprogramming in Tumorigenesis, Tumor Immunity, and Clinical Treatment

Wang, S., Xiaoxue, Y., Guanbin, S., Yang, L., Junyu, J., & Liu, W. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.05.007 · Cited by 45 · see citing works

Target enzymes in serine‐glycine‐one‐carbon metabolic pathway for cancer therapy

Sun, W. Y., Zhao, E., & Cui, H. (2022) · International Journal of Cancer · doi:10.1002/ijc.34353 · Cited by 39 · see citing works

Amino acid metabolism in glioblastoma pathogenesis, immune evasion, and treatment resistance

Srivastava, S., Anbiaee, R., Houshyari, M., Laxmi, L., Sridhar, S. B., Ashique, S., Hussain, M. S., Kumar, S., Taj, T., Akbarnejad, Z., et al. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03721-1 · Cited by 33 · see citing works

One-carbon metabolism supports S-adenosylmethionine and m6A methylation to control the osteogenesis of bone marrow stem cells and bone formation

Zhang, W., Bai, Y., Hao, L., Zhao, Y., Zhang, L., Ding, W., Qi, Y., & Xu, Q. (2024) · Journal of Bone and Mineral Research · doi:10.1093/jbmr/zjae121 · Cited by 32 · see citing works

Metformin Is a Pyridoxal-5′-phosphate (PLP)-Competitive Inhibitor of SHMT2

Tramonti, A., Cuyàs, E., Encinar, J. A., Pietzke, M., Paone, A., Verdura, S., Arbusà, A., Martı́n-Castillo, B., Giardina, G., Joven, J., et al. (2021) · Cancers · doi:10.3390/cancers13164009 · Cited by 31 · see citing works

The Ubiquitin–Proteasome System in Tumor Metabolism

Wang, J., Xiang, Y., Fan, M., Fang, S., & Hua, Q. (2023) · Cancers · doi:10.3390/cancers15082385 · Cited by 31 · see citing works

The role of serine metabolism in lung cancer: From oncogenesis to tumor treatment

Zhou, X., Tian, C., Cao, Y., Zhao, M., & Wang, K. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2022.1084609 · Cited by 30 · see citing works

Metabolic Profiles of Cancer Stem Cells and Normal Stem Cells and Their Therapeutic Significance

Stouras, I., Vasileiou, M., Kanatas, P., Tziona, E., Tsianava, C., & Theocharis, S. (2023) · Cells · doi:10.3390/cells12232686 · Cited by 28 · see citing works

The interactions and biological pathways among metabolomics products of patients with coronary heart disease

Chu, C., Liu, S., Nie, L., Hu, H., Liu, Y., & Yang, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116305 · Cited by 28 · see citing works

Metabolic reprogramming in cancer: signaling pathways and therapeutic targets

Dong, S., & Lei, X. (2026) · Molecular Cancer · doi:10.1186/s12943-026-02582-0 · Cited by 28 · see citing works

Biochemical Mechanisms Associating Alcohol Use Disorders with Cancers

Rodriguez, F. D., & Coveñas, R. (2021) · Cancers · doi:10.3390/cancers13143548 · Cited by 27 · see citing works

Transcriptional Activation of Chac1 and Other Atf4-Target Genes Induced by Extracellular l-Serine Depletion is negated with Glycine Consumption in Hepa1-6 Hepatocarcinoma Cells

Hamano, M., Tomonaga, S., Osaki, Y., Oda, H., Kato, H., & Furuya, S. (2020) · Nutrients · doi:10.3390/nu12103018 · Cited by 25 · see citing works

Research progress of hyperthermia in tumor therapy by influencing metabolic reprogramming of tumor cells

Yang, Y., Huangfu, L., Li, H., & Yang, D. (2023) · International Journal of Hyperthermia · doi:10.1080/02656736.2023.2270654 · Cited by 23 · see citing works

Mechanism underlying circRNA dysregulation in the TME of digestive system cancer

Wu, Z., Yu, X., Zhang, S., He, Y., & Guo, W. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.951561 · Cited by 22 · see citing works

Upregulation of SHMT2 Promotes Tumor Growth and Poor Prognosis of Breast Cancer through Activating VEGF and MAPK Signaling PathwayPreprint

Xie, S.-Y., Shi, D., Ouyang, Y. Q., Cheng, X.-Y., Chen, X., Jiang, T., Xia, W., Guo, L., & Lin, H. (2021) · Research Square · doi:10.21203/rs.3.rs-1016628/v1 · Cited by 22 · see citing works

Asparagine: A key metabolic junction in targeted tumor therapy

Wang, X., Gong, W., Xiong, X., Jia, X., & Xu, J. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107292 · Cited by 21 · see citing works

ABCC2 induces metabolic vulnerability and cellular ferroptosis via enhanced glutathione efflux in gastric cancer

Wang, Y., Gan, X., Cheng, X., Jia, Y., Wang, G., Tang, X., Du, H., Li, X., Liu, X., Xing, X., et al. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1754 · Cited by 21 · see citing works

Oncogenic viral infection and amino acid metabolism in cancer progression: Molecular insights and clinical implications

Liu, N., Shi, F., Yang, L., Liao, W., & Cao, Y. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188724 · Cited by 21 · see citing works

Hsa_circ_0062682 Promotes Serine Metabolism and Tumor Growth in Colorectal Cancer by Regulating the miR-940/PHGDH Axis

Sun, S., Li, C., Cui, K., Liu, B., Zhou, M., Cao, Y., Zhang, J., Bian, Z., Fei, B., & Huang, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.770006 · Cited by 21 · see citing works

PHGDH promotes esophageal squamous cell carcinoma progression via Wnt/β-catenin pathway

Duan, X., Chen, Y., Zhang, K., Chen, W., Zhao, J., Dai, X., Cao, W., Dong, Z., Mo, S., & Lü, J. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110736 · Cited by 20 · see citing works

Tissue-Specific Metabolic Reprogramming during Wound-Induced Organ Formation in Tomato Hypocotyl Explants

Larriba, E., Sánchez‐García, A. B., Martínez‐Andújar, C., Albacete, A. A., & Pérez‐Pérez, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810112 · Cited by 19 · see citing works

The emerging role of deubiquitylating enzymes as therapeutic targets in cancer metabolism

Tu, R., Ma, J., Zhang, P., Kang, Y., Xiong, X., Zhu, J., Li, M., & Zhang, C. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02524-y · Cited by 20 · see citing works

Aging impairs CD8 T cell responses in adoptive T-cell therapy against solid tumors

Kadyrzhanova, G., Tamai, M., Sarkar, S., Kalra, R. S., & Ishikawa, H. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1484303 · Cited by 18 · see citing works

Overexpression of SFXN1 indicates poor prognosis and promotes tumor progression in lung adenocarcinoma

Chen, L., Kang, Y., Jiang, Y., You, J., Huang, C.-T., Xu, X., & Chen, F. (2022) · Pathology - Research and Practice · doi:10.1016/j.prp.2022.154031 · Cited by 18 · see citing works

Folate Metabolism in Hepatocellular Carcinoma. What Do We Know So Far?

Quevedo-Ocampo, J., Escobedo‐Calvario, A., Souza-Arroyo, V., Miranda-Labra, R. U., Bucio, L., Gutiérrez‐Ruíz, M. C., Chávez-Rodríguez, L., & Gómez-Quiroz, L. E. (2022) · Technology in Cancer Research & Treatment · doi:10.1177/15330338221144446 · Cited by 18 · see citing works

HOXD8 suppresses renal cell carcinoma growth by upregulating SHMT1 expression

Yang, Y., Zhang, M., Zhao, Y., Deng, T., Zhou, X. Y., Qian, H., Wang, M., Zhang, C., Huo, Z., Mao, Z., et al. (2023) · Cancer Science · doi:10.1111/cas.15982 · Cited by 18 · see citing works

Protein lipoylation in cancer: metabolic reprogramming and therapeutic potential

Li, S., Liu, Y., Hu, W., Deng, A., Ren, X., Chen, L., Lu, Y., Wu, Y., Huang, H., Cao, J., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02718-z · Cited by 17 · see citing works

Interplay between mTOR and Purine Metabolism Enzymes and Its Relevant Role in Cancer

Allegrini, S., Camici, M., Garcia‐Gil, M., Pesi, R., & Tozzi, M. G. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126735 · Cited by 17 · see citing works

Ailanthone Inhibits Proliferation, Migration and Invasion of Osteosarcoma Cells by Downregulating the Serine Biosynthetic Pathway

Zhang, Y., Gong, R., Liu, Y., Sun, X., Liang, J., Zhou, Y., Wang, Y., Yu, W., Wang, Y., Tang, L., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.842406 · Cited by 16 · see citing works

Role of long non-coding RNAs in metabolic reprogramming of gastrointestinal cancer cells

Wang, K., Lu, Y., Li, H., Zhang, J., Ju, Y., & Ouyang, M. (2024) · Cancer Cell International · doi:10.1186/s12935-023-03194-0 · Cited by 16 · see citing works

Metabolic reprograming of cancer as a therapeutic target

Furukawa, T., Tabata, S., Minami, K., Yamamoto, M., Kawahara, K., & Tanimoto, A. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130301 · Cited by 15 · see citing works

DNA Methylation and Its Role in Personalized Nutrition: Mechanisms, Clinical Insights, and Future Perspectives

Hussain, S. A., Sarker, M. I. M., Liu, Y., & Jin, T. Z. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020566 · Cited by 14 · see citing works

Discovery of Myeloid-Derived Suppressor Cell-Specific Metabolism by Metabolomic and Lipidomic Profiling

Kim, J., Lee, H., Choi, H., & Min, H. (2023) · Metabolites · doi:10.3390/metabo13040477 · Cited by 14 · see citing works

One-carbon metabolizing enzyme ALDH1L1 influences mitochondrial metabolism through 5-aminoimidazole-4-carboxamide ribonucleotide accumulation and serine depletion, contributing to tumor suppression

Sasaki, M., Yamamoto, K., Ueda, T., Irokawa, H., Takeda, K., Sekine, R., Itoh, F., Tanaka, Y., Kuge, S., & Shibata, N. (2023) · Scientific Reports · doi:10.1038/s41598-023-38142-5 · Cited by 14 · see citing works

Hypoxia controls the expression of genes responsible for serine synthesis in U87MG cells on ERN1-dependent manner

Sliusar, M. Y., Minchenko, D. O., Khita, O. O., Tsymbal, D. O., Viletska, Y. M., Luzina, O. Y., Danilovskyi, S. V., Ratushna, O. O., & Minchenko, О. H. (2023) · Endocrine Regulations · doi:10.2478/enr-2023-0028 · Cited by 14 · see citing works

SHMT2 regulates serine metabolism to promote the progression and immunosuppression of papillary renal cell carcinoma

Kong, W., Wang, Z., Chen, N., Mei, Y., Li, Y., & Yue, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.914332 · Cited by 14 · see citing works

New Emerging Therapeutic Strategies Based on Manipulation of the Redox Regulation Against Therapy Resistance in Cancer

Nazari, A., Osati, P., Fakhr, S. S., Faghihkhorasani, F., Ghanaatian, M., Faghihkhorasani, F., Rezaei‐Tazangi, F., Far, N. P., Shourideh, A., Ebrahimi, N., et al. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0491 · Cited by 13 · see citing works

Causal associations between liver traits and Colorectal cancer: a Mendelian randomization study

Ni, Y., Wang, W., Liu, Y., & Jiang, Y. (2023) · BMC Medical Genomics · doi:10.1186/s12920-023-01755-w · Cited by 13 · see citing works

The enzymes of serine synthesis pathway in cancer metastasis

Li, L., Qin, Y., & Chen, Y. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119697 · Cited by 13 · see citing works

PSAT1 promotes the progression of colorectal cancer by regulating Hippo-YAP/TAZ-ID1 axis via AMOT

Tang, M., Song, K., Xie, D., Yuan, X., Wang, Y., Li, Z., Lu, X., Guo, L., Zhu, X., Xiong, L., et al. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05194-8 · Cited by 13 · see citing works

Targeting mitochondrial homeostasis as a cancer treatment strategy: current status and future prospects

Zhong, H., Pan, R., Ouyang, Y., Xiao, T., Gu, W., Yang, H., Wang, H., Li, H., Peng, T., & Chen, P. (2026) · Molecular Cancer · doi:10.1186/s12943-026-02571-3 · Cited by 13 · see citing works

SHMT as a Potential Therapeutic Target for Renal Cell Carcinoma

Situ, Y., Zhang, J., Liao, W., Liang, Q., Lu, L., Xu, Q., Chen, J., Lu, X., Cui, Y., Shao, Z., et al. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2809196 · Cited by 12 · see citing works

Cancer-associated fibroblasts derived fibronectin extra domain A promotes sorafenib resistance in hepatocellular carcinoma cells by activating SHMT1

Dong, Y., Chen, Y., Wang, Y., Zhao, X., Zi, R., Hao, J., Ding, Q., Jiang, H., Wang, X., Lu, F., et al. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101330 · Cited by 12 · see citing works

Current status of cancer starvation therapy

Li, J., Dandan, T. O. N. G., & Lin, J. (2022) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2021-0297 · Cited by 12 · see citing works

Serine hydroxymethyltransferase 2 predicts unfavorable outcomes in multiple cancer: a systematic review and meta-analysis

Du, J., Huang, Y., Jing, S., Pei, Y., Qian, Y., & Zeng, Y. (2022) · Translational Cancer Research · doi:10.21037/tcr-21-2485 · Cited by 12 · see citing works

ATF4/MYC Regulates MTHFD2 to Promote NSCLC Progression by Mediating Redox Homeostasis

Gao, Y., Feng, L., Zhang, L., Geng, J., & Zhang, E. (2022) · Disease Markers · doi:10.1155/2022/7527996 · Cited by 12 · see citing works

Vital role of SHMT2 in diverse disease

Ma, W., Liu, R., Zhao, K., & Zhong, J. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.05.108 · Cited by 11 · see citing works

Upregulation of serine metabolism enzyme PSAT1 predicts poor prognosis and promotes proliferation, metastasis and drug resistance of clear cell renal cell carcinoma

Ye, J., Huang, X., Tian, S., Wang, J., Wang, H., Feng, H., Zhao, X., Cao, S., Xuan, Y., Li, X., et al. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.113977 · Cited by 11 · see citing works

Knockdown of ERN1 disturbs the expression of phosphoserine aminotransferase 1 and related genes in glioblastoma cells

Minchenko, О. H., Sliusar, M. Y., Khikhlo, Y. P., Halkin, O. V., Viletska, Y. M., Khita, O. O., & Minchenko, D. O. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110104 · Cited by 11 · see citing works

The Pivotal Role of One-Carbon Metabolism in Neoplastic Progression During the Aging Process

Majumder, A., Bano, S., & Nayak, K. B. (2024) · Biomolecules · doi:10.3390/biom14111387 · Cited by 11 · see citing works

S-adenosylmethionine deficit disrupts very low-density lipoprotein metabolism promoting liver lipid accumulation in mice

Luque-Urbano, M. R., Fernández‐Ramos, D., Lopitz‐Otsoa, F., de Juan, V. G., Bizkarguenaga, M., Castro-Espadas, L., Hermoso-Martínez, U., Barbier‐Torres, L., Lu, S. C.-L., Millet, Ó., et al. (2025) · Journal of Lipid Research · doi:10.1016/j.jlr.2025.100794 · Cited by 11 · see citing works

The role and research progress of serine metabolism in tumor cells

Lyu, H., Bao, S., Cai, L., Wang, M., Liu, Y., Sun, Y., & Hu, X. S. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1509662 · Cited by 11 · see citing works

Metabolomic Profiling of Breast Cancer Patients Undergoing Neoadjuvant Chemotherapy for Predicting Disease-Free and Overall Survival

Talarico, M. C. R., Derchain, S., da Silva, L. F., Sforça, M. L., Rocco, S. A., Cardoso, M. R., & Sarian, L. O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168639 · Cited by 10 · see citing works

Asparagine as a signal for glutamine sufficiency via asparagine synthetase: a fresh evidence-based framework in physiology and oncology

Olawuni, B., & Bode, B. P. (2024) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00316.2024 · Cited by 10 · see citing works

New insights into the dule roles CDK12 in human cancers: Mechanisms and interventions for cancer therapy

Dai, W., Xie, D., Huang, H., Li, J., Guo, C., Cao, F., Yang, L., Zhong, C., & Liu, S. (2024) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2024.101173 · Cited by 10 · see citing works

SFXN3 is Associated with Poor Clinical Outcomes and Sensitivity to the Hypomethylating Therapy in Non-M3 Acute Myeloid Leukemia Patients

Dong, Y., Jin, F., Wang, J., Li, Q., Huang, Z., Xia, L., & Yang, M. (2023) · Current Gene Therapy · doi:10.2174/1566523223666230724121515 · Cited by 10 · see citing works

NMR Metabolomics of Primary Ovarian Cancer Cells in Comparison to Established Cisplatin-Resistant and -Sensitive Cell Lines

Ghini, V., Sorbi, F., Fambrini, M., & Magherini, F. (2024) · Cells · doi:10.3390/cells13080661 · Cited by 10 · see citing works

YY2/PHGDH axis suppresses tumorigenesis by inhibiting tumor cell de novo serine biosynthesis

Li, J., Luo, X., Wei, M., Li, Z., Li, Y., Zhao, H., Miyagishi, M., Kasim, V., & Wu, S. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115006 · Cited by 9 · see citing works

Inhibition of signaling protein ERN1 increases the sensitivity of serine synthesis gene expressions to glucose and glutamine deprivations in U87MG glioblastoma cells

Minchenko, О. H., Sliusar, M. Y., Khita, O. O., Minchenko, D. O., Viletska, Y. M., Halkin, O. V., Levadna, L. O., Cherednychenko, A. A., & Khikhlo, Y. P. (2024) · Endocrine Regulations · doi:10.2478/enr-2024-0010 · Cited by 9 · see citing works

Analysis of microarray and single-cell RNA-seq identifies gene co-expression, cell–cell communication, and tumor environment associated with metabolite interconversion enzyme in prostate cancer

Karoii, D. H., Abroudi, A. S., Forghani, N., Bavandi, S., Djamali, M., Baghaei, H., Shafaeitilaki, S., & HasanZadeh, E. (2025) · Discover Oncology · doi:10.1007/s12672-025-01926-4 · Cited by 9 · see citing works

Targeting amino acid in tumor therapy

Ge, M., Xu, Y., Cui, L., Huang, E., Liu, Z., & Yin, K. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1582116 · Cited by 8 · see citing works

Ailanthone: A multi-targeting Quassinoid from Ailanthus altissima for broad-spectrum cancer therapy - a comprehensive review of mechanisms, pharmacokinetics, and clinical prospects

Huang, Y.-J., Chen, H., Jiang, Y., Meng, Z., She, C., Miao, Z., & Fan, Y. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120716 · Cited by 8 · see citing works

Serine-associated one-carbon metabolic reprogramming: a new anti-cancer therapeutic strategy

Zhang, J., Bai, J., Chen, G., Wang, J., Cheng, Y., Zhao, J., & Xiong, H. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1184626 · Cited by 8 · see citing works

Serine Metabolism Regulates the Replicative Senescence of Human Dental Pulp Cells through Histone Methylation

Zhou, S., Cui, J., & Shi, Y. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46040179 · Cited by 8 · see citing works

A study on the significance of serine hydroxymethyl transferase expression and its role in bladder cancer

Su, S.-W., Chen, X., Wang, G., Li, P., Yang, T., Fang, K.-W., Wu, J., & Li, J. (2024) · Scientific Reports · doi:10.1038/s41598-024-58618-2 · Cited by 8 · see citing works

Effect of Carbon Ion Radiation Induces Bystander Effect on Metastasis of A549 Cells and Metabonomic Correlation Analysis

Yang, Z., Zhang, Q., Luo, H., Shao, L., Liu, R., Kong, Y., Zhao, X., Geng, Y., Li, C., & Wang, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.601620 · Cited by 8 · see citing works

Cellular Signaling of Amino Acid Metabolism in Prostate Cancer

Yao, P., Cao, S., Zhu, Z., Wen, Y., Guo, Y., Liang, W., & Xie, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020776 · Cited by 7 · see citing works

Rapid prediction of cervical cancer and high-grade precursor lesions: An integrated approach using low-field 1H NMR and chemometric analysis

Leão, L. Q. D. S., de Andrade, J. C., Marques, G. M., Guimarães, C. C., de Albuquerque, R. D. F. V., Silva, A. S. E., de Araujo, K. P., de Oliveira, M. P., Gonçalves, A. F., Figueiredo, H. F., et al. (2025) · Clinica Chimica Acta · doi:10.1016/j.cca.2025.120346 · Cited by 7 · see citing works

Endoplasmic reticulum stress-dependent regulation of the expression of serine hydroxymethyltransferase 2 in glioblastoma cells

Minchenko, О. H., Sliusar, M. Y., Khita, O. O., Viletska, Y. M., Luzina, O. Y., Danilovskyi, S. V., & Minchenko, D. O. (2024) · Endocrine Regulations · doi:10.2478/enr-2024-0016 · Cited by 6 · see citing works

Phase-dependent hepatotoxicity of Aluminum oxide nanoparticles mediated through the intestinal microbiota

Li, M., Deng, F., Dong, L., Wang, X., Jiang, H., Yao, S., Chen, Y., Duan, L., Du, H., Qin, G., et al. (2025) · Environment International · doi:10.1016/j.envint.2025.109398 · Cited by 6 · see citing works

Per- and polyfluoroalkyl substances (PFASs) exposure and gastric cancer risk: Insights from exposome-metabolome profiling

Zhu, J., Li, S., Li, X., Wang, L., & Ling-bin, D. (2025) · Environmental Technology & Innovation · doi:10.1016/j.eti.2025.104242 · Cited by 4 · see citing works

Recent progress in serine metabolism reprogramming in tumors and strategies for serine deprivation

Liu, H., & Liu, Y. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1669565 · Cited by 4 · see citing works

PHGDH phosphorylation mediated by WNK1 serves as a dual marker of metabolic vulnerability and responsiveness to oxaliplatin treatment

Fang, S., Jin, G., Yan, M., Song, Y., Zhao, S., Zhang, C., Shao, Y. W., Zhao, K., Liu, M., Wang, Z., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2525213123 · Cited by 4 · see citing works

Synergistic effects of low-dose arsenic and N-methyl-N′-nitro-N-nitrosoguanidine co-exposure by altering gut microbiota and intestinal metabolic profile in rats

Wang, K., Lin, X., Wang, T., Zhang, X., Cheng, W., Xu, F., Wang, L., Li, B., Wang, M., Wang, W., et al. (2023) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2023.115195 · Cited by 4 · see citing works

Interplay of serum taurine, S-adenosylmethionine, and cysteine levels in cancer risk: a prospective study

Liu, C., Liu, T., Wei, Y., Shi, J., Deng, L., Song, M., & Shi, H. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1507125 · Cited by 3 · see citing works

Longitudinal serum metabolomics predicts therapeutic outcome in acute myeloid leukemia

Cai, Q., Liu, W., Yan, C., Li, J., Huang, Y., Li, X. O., Yang, Q., Wei, X., Yang, H., Zhang, G., et al. (2025) · Translational Oncology · doi:10.1016/j.tranon.2025.102567 · Cited by 3 · see citing works

Novel machine‐learning bioinformatics reveal distinct metabolic alterations for enhanced colorectal cancer diagnosis and monitoring

Xu, R., Jung, H., Choueiry, F., Zhang, S., Pearlman, R., Hampel, H., Jin, N. Y., Li, J., & Zhu, J. (2025) · iMetaOmics. · doi:10.1002/imo2.70003 · Cited by 3 · see citing works

The Global mRNA Expression Profiles of Inhibiting PHGDH Induced Cisplatin Resistance in Gastric Cancer.

Pan, K., Zhao, X., & Xu, W. (2022) · PubMed Central · doi:10.22074/cellj.2022.8046 · Cited by 3 · see citing works

Expression, Prognostic Value, and Immune Infiltration of MTHFD Family in Bladder Cancer

Zheng, B. S., Wang, S. D., Zhang, J., & Ge, C. G. (2023) · Current Cancer Drug Targets · doi:10.2174/1568009623666230804152603 · Cited by 3 · see citing works

Transcriptome analysis reveals effects of leukemogenic SHP2 mutations in biosynthesis of amino acids signaling

Zhao, Y., Chang, Z., Hu, B., Zhang, Q., Zhang, D., He, C., Guo, Y., Peng, Z., Chen, C., & Chen, Y. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1090542 · Cited by 3 · see citing works

Amino Acid Metabolism of the Skin: Control by Specific Enzymes and Contribution to Protective Functions

Dörner, C., Steinbinder, J., Sachslehner, A. P., Sukseree, S., & Eckhart, L. (2025) · Metabolites · doi:10.3390/metabo15090601 · Cited by 2 · see citing works

Genetic variations in amino acid metabolism-related genes are associated with risk of papillary thyroid carcinoma: a case-control study

Meng, H., Xiao, Z., Wang, Q., Li, D., & Li, Z. (2025) · BMC Endocrine Disorders · doi:10.1186/s12902-025-02034-8 · Cited by 2 · see citing works

PSAT1 knockdown mediated VDAC1 oligomerization promotes ferroptosis and suppresses cell proliferation in esophageal squamous cell carcinoma

Ren, R., Fan, T., Li, Y., Li, C., Jin, F., Gao, H. Y., Wang, X., Xu, Y., Li, X., Li, S., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.148112 · Cited by 2 · see citing works

Quercetin's antitumor effect in bladder cancer: Synergistic regulation of gut microbiota and l-serine metabolic pathway

Zhai, Z., Yang, F., Feng, R., Zhang, H., Wang, J., Zuo, H., Yang, X., Ye, M., Xu, H., Hu, J., et al. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.03.034 · Cited by 2 · see citing works

In Silico Prediction of Metabolic Fluxes in Cancer Cells with Altered S-adenosylmethionine Decarboxylase Activity

Доценко, О. И., & Shtofel, D. K. (2020) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-020-00949-8 · Cited by 2 · see citing works

HER2-low Breast Cancer: Salivary Metabolic Features and Therapeutic Perspectives

Bel’skaya, L. V. (2025) · Frontiers in Bioscience-Scholar · doi:10.31083/fbs36652 · Cited by 2 · see citing works

SFXN3 is a Prognostic Marker and Promotes the Growth of Acute Myeloid Leukemia

Jin, F., He, L., Wang, J., Zhang, Y., & Yang, M. (2024) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-024-01326-5 · Cited by 2 · see citing works

Metabolic Reprogramming in Kidney Cancer: Implications for Therapy

Edo, E. T. (2025) · annals of urologic oncology · doi:10.32948/auo.2025.06.02 · Cited by 2 · see citing works

Metabolic Rewiring in Cancer: Understanding the Complexity of Metabolic Networks

Sharma, A., Negi, N., Sharma, I., & Sobti, R. C. (2024) · Springer eBooks · doi:10.1007/978-981-99-6263-1_27 · Cited by 1 · see citing works

Microbiota–Metabolite–Host Crosstalk Mediates the Impact of Dietary Energy Levels on Colonic Homeostasis in High-Altitude Ruminants

Yu, Q., Li, N., Bao, P., Huang, C., Zheng, Q., Wang, T., Ma, C., Deng, J., Jiang, F., Jia, J., et al. (2025) · Animals · doi:10.3390/ani15192929 · Cited by 1 · see citing works

Multifunctionality analysis of serine hydroxymethyltransferases from human and Escherichia coli

Hayashi, M., Sakai‐Kato, K., & Miyamoto, T. (2025) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2025.141107 · Cited by 1 · see citing works

Targeting serine-glycine-one-carbon metabolism as a vulnerability in cancers

Sun, W. Y., Liu, R., Gao, X., Lin, Z., Tang, H., Cui, H., & Zhao, E. (2023) · Biomarker Research · doi:10.1186/s40364-023-00487-4 · Cited by 82 · see citing works

Serine, glycine and one‑carbon metabolism in cancer (Review)

Pan, S., Fan, M., Liu, Z., Li, X., & Wang, H. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5158 · Cited by 227 · see citing works

Target enzymes in serine‐glycine‐one‐carbon metabolic pathway for cancer therapy

Sun, W. Y., Zhao, E., & Cui, H. (2022) · International Journal of Cancer · doi:10.1002/ijc.34353 · Cited by 39 · see citing works

Serine, glycine and one-carbon units: cancer metabolism in full circle

Locasale, J. W. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3557 · Cited by 1,671 · see citing works

Serine Hydroxymethyltransferase in Cancer Cells

Гаврилюк, Л. А. (2025) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750824601371