ATF3 promotes the serine synthesis pathway and tumor growth under dietary serine restriction
Open accessAbstract
The serine synthesis pathway (SSP) involving metabolic enzymes phosphoglycerate dehydrogenase (PHGDH), phosphoserine aminotransferase 1 (PSAT1), and phosphoserine phosphatase (PSPH) drives intracellular serine biosynthesis and is indispensable for cancer cells to grow in serine-limiting environments. However, how SSP is regulated is not well understood. Here, we report that activating transcription factor 3 (ATF3) is crucial for transcriptional activation of SSP upon serine deprivation. ATF3 is rapidly induced by serine deprivation via a mechanism dependent on ATF4, which in turn binds to ATF4 and increases the stability of this master regulator of SSP. ATF3 also binds to the enhancers/promoters of PHGDH, PSAT1, and PSPH and recruits p300 to promote expression of these SSP genes. As a result, loss of ATF3 expression impairs serine biosynthesis and the growth of cancer cells in the serine-deprived medium or in mice fed with a serine/glycine-free diet. Interestingly, ATF3 expression positively correlates with PHGDH expression in a subset of TCGA cancer samples.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
ATF3 regulates serine biosynthesis by increasing PHGDH, PSAT1, and PSPH.
“regulates serine biosynthesis by increasing PHGDH, PSAT1, and PSPH [38]”
From 20-Hydroxyecdysone Boosts Energy Production and Biosynthetic Processes in Non-Transformed Mouse Cells (2024) · cites this paper as [38]
Different oncogenes and oncosuppressors have a critical impact on these metabolic pathways.
“Different oncogenes and oncosupressors have a critical impact on these metabolic pathways [20,40,46,47,75,76].”
From 20-Hydroxyecdysone Confers Antioxidant and Antineoplastic Properties in Human Non-Small Cell Lung Cancer Cells (2023) · cites this paper as [47]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Genome engineering using the CRISPR-Cas9 system
Ran, F. A., Hsu, P. D., Wright, J., Agarwala, V., Scott, D. A., & Zhang, F. (2013) · Nature Protocols · doi:10.1038/nprot.2013.143 · Cited by 11,133 · see citing works
Histone H3K27ac separates active from poised enhancers and predicts developmental state
Creyghton, M. P., Cheng, A. W., Welstead, G. G., Kooistra, T., Carey, B. W., Steine, E. J., Hanna, J., Lodato, M. A., Frampton, G. M., Sharp, P. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016071107 · Cited by 4,302 · 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
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
Modification of Enhancer Chromatin: What, How, and Why?
Calo, E., & Wysocka, J. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.038 · Cited by 1,457 · 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
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
Discovery of a selective catalytic p300/CBP inhibitor that targets lineage-specific tumours
Lasko, L. M., Jakob, C. G., Edalji, R. P., Qiu, W., Montgomery, D., Digiammarino, E. L., Hansen, T. M., Risi, R. M., Frey, R., Manaves, V., et al. (2017) · Nature · doi:10.1038/nature24028 · Cited by 858 · see citing works
ATF3 promotes erastin-induced ferroptosis by suppressing system Xc–
Wang, L., Liu, Y., Du, T., Yang, H., Lei, L., Guo, M., Ding, H., Zhang, J., Wang, H., Chen, X., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0380-z · Cited by 820 · see citing works
Self-citationHai, T., & Hartman, M. G. (2001) · Gene · doi:10.1016/s0378-1119(01)00551-0 · Cited by 808 · see citing works
Systems biology approaches identify ATF3 as a negative regulator of Toll-like receptor 4
Gilchrist, M., Thorsson, V., Li, B., Rust, A., Korb, M., Kennedy, K. A., Hai, T., Bolouri, H., & Aderem, A. (2006) · Nature · doi:10.1038/nature04768 · Cited by 782 · 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
Bowers, E. M., Yan, G., Mukherjee, C., Orry, A., Wang, L., Holbert, M. A., Crump, N. T., Hazzalin, C. A., Liszczak, G., Yuan, H., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.03.006 · Cited by 666 · see citing works
Hai, T., Wolfgang, C. D., Marsee, D. K., Allen, A. E., & Sivaprasad, U. (1999) · Europe PMC (PubMed Central) · Cited by 629 · see citing works
Surviving Stress: Modulation of ATF4-Mediated Stress Responses in Normal and Malignant Cells
Wortel, I. M. N., van der Meer, L. T., Kilberg, M. S., & van Leeuwen, F. N. (2017) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2017.07.003 · Cited by 613 · see citing works
ATF4-dependent transcription mediates signaling of amino acid limitation
Kilberg, M. S., Shan, J., & Su, N. Y. (2009) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2009.05.008 · Cited by 595 · 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
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
Jiang, H.-Y., Wek, S. A., McGrath, B. C., Lü, D., Hai, T., Harding, H. P., Wang, X., Ron, D., Cavener, D. R., & Wek, R. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.1365-1377.2004 · Cited by 504 · see citing works
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
The importance of serine metabolism in cancer
Mattaini, K. R., Sullivan, M. R., & Heiden, M. G. V. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604085 · Cited by 409 · see citing works
Wang, Q., Mora-Jensen, H. I., Weniger, M. A., Pérez‐Galán, P., Wolford, C. C., Hai, T., Ron, D., Chen, W., Trenkle, W. C., Wiestner, A. U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807611106 · Cited by 343 · see citing works
Wang, F., Marshall, C. B., & Ikura, M. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1254-4 · Cited by 311 · see citing works
Opposing roles for calcineurin and ATF3 in squamous skin cancer
Wu, X., Nguyen, B.-C., Dziunycz, P., Chang, S. E., Brooks, Y., Lefort, K., Hofbauer, G. F. L., & Dotto, G. P. (2010) · Nature · doi:10.1038/nature08996 · Cited by 301 · see citing works
Limited Environmental Serine and Glycine Confer Brain Metastasis Sensitivity to PHGDH Inhibition
Ngo, B., Kim, E., Osorio-Vasquez, V., Doll, S., Bustraan, S., Liang, R. J., Luengo, A., Davidson, S. M., Ali, A., Ferraro, G. B., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1228 · Cited by 268 · see citing works
Ding, J., Li, T., Wang, X., Zhao, E., Choi, J.-H., Yang, L., Zha, Y., Dong, Z., Huang, S., Asara, J. M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.11.004 · Cited by 244 · see citing works
Self-citationPark, Y., Reyna‐Neyra, A., Philippe, L., & Thoreen, C. C. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.042 · Cited by 242 · see citing works
Sullivan, M. R., Mattaini, K. R., Dennstedt, E. A., Nguyen, A. A., Sivanand, S., Reilly, M. F., Meeth, K. M., Muir, A., Darnell, A. M., Bosenberg, M., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.02.015 · Cited by 242 · see citing works
Masuoka, H. C., & Townes, T. M. (2002) · Blood · doi:10.1182/blood.v99.3.736 · Cited by 231 · see citing works
Crawford, R. R., Prescott, E. T., Sylvester, C. F., Higdon, A. N., Shan, J., Kilberg, M. S., & Mungrue, I. N. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.635144 · Cited by 221 · see citing works
Activating transcription factor 3, a stress sensor, activates p53 by blocking its ubiquitination
Yan, C., Lü, D., Hai, T., & Boyd, D. D. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600712 · Cited by 214 · see citing works
Self-citationNegative Regulation of TLR-Signaling Pathways by Activating Transcription Factor-3
Whitmore, M., Iparraguirre, A., Kubelka, L., Weninger, W., Hai, T., & Williams, B. R. G. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.3622 · Cited by 212 · see citing works
A potential dichotomous role of ATF3, an adaptive-response gene, in cancer development
Yin, X. H., DeWille, J. W., & Hai, T. (2007) · Oncogene · doi:10.1038/sj.onc.1210861 · Cited by 209 · see citing works
Gargiulo, G., Cesaroni, M., Serresi, M., de Vries, N., Hulsman, D., Bruggeman, S. W. M., Lancini, C., & van Lohuizen, M. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.03.030 · Cited by 180 · see citing works
Combinatorial bZIP dimers display complex DNA-binding specificity landscapes
Rodríguez‐Martínez, J. A., Reinke, A. W., Bhimsaria, D., Keating, A. E., & Ansari, A. Z. (2017) · eLife · doi:10.7554/elife.19272 · Cited by 175 · see citing works
KDM4C and ATF4 Cooperate in Transcriptional Control of Amino Acid Metabolism
Zhao, E., Ding, J., Xia, Y., Liu, M., Ye, B., Choi, J.-H., Yan, C., Dong, Z., Huang, S., Zha, Y., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.053 · Cited by 162 · see citing works
Self-citationOu, Y., Wang, S.-J., Jiang, L., Zheng, B., & Gu, W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616359 · Cited by 154 · see citing works
gadd153/Chop10 , a Potential Target Gene of the Transcriptional Repressor ATF3
Wolfgang, C. D., Chen, B. P. C., Martindale, J. L., Holbrook, N. J., & Hai, T. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6700 · Cited by 153 · see citing works
Dichotomous engagement of HDAC3 activity governs inflammatory responses
Nguyen, H. C. B., Adlanmerini, M., Hauck, A. K., & Lazar, M. A. (2020) · Nature · doi:10.1038/s41586-020-2576-2 · Cited by 150 · see citing works
Chromatin-Bound MDM2 Regulates Serine Metabolism and Redox Homeostasis Independently of p53
Riscal, R., Schrepfer, E., Arena, G., Cissé, M. Y., Bellvert, F., Heuillet, M., Rambow, F., Bonneil, É., Sabourdy, F., Vincent, C., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.033 · Cited by 139 · see citing works
Yuan, X., Yu, L., Li, J., Xie, G., Rong, T., Zhang, L. N., Chen, J., Meng, Q., Irving, A. T., Wang, D., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3879 · Cited by 138 · see citing works
Transcription factor ATF3 links host adaptive response to breast cancer metastasis
Wolford, C. C., McConoughey, S. J., Jalgaonkar, S. P., Leon, M. E., Merchant, A. S., Dominick, J. L., Yin, X. H., Chang, Y.-S., Zmuda, E. J., O'Toole, S. A., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64410 · Cited by 127 · see citing works
Pan, Y., Chen, H., Siu, F., & Kilberg, M. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304574200 · Cited by 112 · see citing works
Zhao, J. C., Li, X., Guo, M., Yu, J., & Yan, C. (2016) · BMC Genomics · doi:10.1186/s12864-016-2664-8 · Cited by 111 · see citing works
Self-citationXia, Y., Ye, B., Ding, J., Yu, Y., Alptekin, A., Thangaraju, M., Prasad, P. D., Ding, Z., Park, E. J., Choi, J.-H., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-3541 · Cited by 108 · see citing works
Self-citationTranscriptional Autorepression of the Stress-inducible GeneATF3
Wolfgang, C. D., Liang, G., Okamoto, Y., Allen, A. E., & Hai, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909637199 · Cited by 105 · see citing works
Lassot, I., Estrabaud, E., Emiliani, S., Benkirane, M., Bénarous, R., & Margottin-Goguet, F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505294200 · Cited by 99 · see citing works
Lee, S. H., Krisanapun, C., & Baek, S. J. (2010) · Carcinogenesis · doi:10.1093/carcin/bgq016 · Cited by 98 · see citing works
Liu, J., Zhang, C., Wu, H., Sun, X., Li, Y., HUANG, S. H., Yue, X., Lu, S., Shen, Z., Su, X., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci132876 · Cited by 98 · see citing works
Jan, Y., Tsai, H., Yang, C., Huang, M.-S., Yang, Y., Lai, T., Lee, C.-H., Jeng, Y., Huang, C. F., Su, J.-L., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-1842 · Cited by 91 · see citing works
Liu, W., Iiizumi, M., Okuda, H., Kobayashi, A., Watabe, M., Pai, S. K., Pandey, P. R., Xing, F., Fukuda, K., Modur, V., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.232637 · Cited by 88 · see citing works
Hackl, C., Lang, S. A., Moser, C., Mori, A., Fichtner‐Feigl, S., Hellerbrand, C., Dietmeier, W., Schlitt, H. J., Geissler, E. K., & Stoeltzing, O. (2010) · BMC Cancer · doi:10.1186/1471-2407-10-668 · Cited by 86 · see citing works
ATF3 Regulates the Stability of p53: A Link to Cancer
Yan, C., & Boyd, D. D. (2006) · Cell Cycle · doi:10.4161/cc.5.9.2714 · Cited by 80 · see citing works
Self-citationLoss of ATF3 promotes Akt activation and prostate cancer development in a Pten knockout mouse model
Wang, Z., Xu, D., Ding, H.-F., Kim, J., Zhang, J., Hai, T., & Yan, C. (2014) · Oncogene · doi:10.1038/onc.2014.426 · Cited by 69 · see citing works
Self-citationDi Marcantonio, D., Martinez, E., Kanefsky, J. S., Huhn, J. M., Gabbasov, R., Gupta, A., Krais, J. J., Peri, S., Tan, Y., Skorski, T., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.05.008 · Cited by 67 · 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
MDM2 Mediates Ubiquitination and Degradation of Activating Transcription Factor 3
Mo, P., Wang, H., Lu, H., Boyd, D. D., & Yan, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132597 · Cited by 56 · see citing works
Self-citationThiaville, M. M., Dudenhausen, E. E., Zhong, C., Pan, Y., & Kilberg, M. S. (2008) · Biochemical Journal · doi:10.1042/bj20071252 · Cited by 50 · see citing works
The stress-responsive gene ATF3 regulates the histone acetyltransferase Tip60
Cui, H., Guo, M., Xu, D. M., Ding, Z., Zhou, G., Ding, H., Zhang, J., Tang, Y., & Yan, C. (2015) · Nature Communications · doi:10.1038/ncomms7752 · Cited by 46 · see citing works
Self-citationThe Stress Response Mediator ATF3 Represses Androgen Signaling by Binding the Androgen Receptor
Wang, H., Jiang, M., Cui, H., Chen, M., Buttyan, R., Hayward, S. W., Hai, T., Wang, Z., & Yan, C. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00159-12 · Cited by 44 · see citing works
Self-citationCompetitive ubiquitination activates the tumor suppressor p53
Li, X., Guo, M., Cai, L., Du, T., Liu, Y., Ding, H., Wang, H., Zhang, J., Chen, X., & Yan, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0463-x · Cited by 41 · see citing works
Self-citationAtf3 deficiency promotes genome instability and spontaneous tumorigenesis in mice
Wang, Z., He, Y. D., Deng, W., Lang, L., Yang, H., Jin, B., Kolhe, R. B., Ding, H.-F., Zhang, J., Hai, T., et al. (2017) · Oncogene · doi:10.1038/onc.2017.310 · Cited by 40 · see citing works
Self-citationLee, S., Krisanapun, C., & Baek, S. J. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.928.11 · Cited by 39 · see citing works
Epitope tagging of endogenous genes in diverse human cell lines
Kim, J.-S., Bonifant, C. L., Bunz, F., Lane, W. S., & Waldman, T. A. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn566 · Cited by 36 · see citing works
Emerging roles of ATF3 in the suppression of prostate cancer
Wang, Z., & Yan, C. (2015) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1010948 · Cited by 28 · see citing works
Self-citationWang, Z., Kim, J., Teng, Y., Ding, H.-F., Zhang, J., Hai, T., Cowell, J. K., & Yan, C. (2015) · Oncogene · doi:10.1038/onc.2015.417 · Cited by 19 · see citing works
Self-citation
Flagged first, then by citations
1 of the 67 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Metabolic reprogramming, sensing, and cancer therapy
Mao, Y., Xia, Z., Xia, W., & Jiang, P. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115064 · Cited by 168 · see citing works
The integrated stress response in metabolic adaptation
Ryoo, H. D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107151 · Cited by 120 · see citing works
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
Serine signaling governs metabolic homeostasis and health
He, L., Ding, Y., Zhou, X., Li, T., & Yin, Y. (2023) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2023.03.001 · Cited by 98 · see citing works
Yun, H. J., Li, M., Guo, D. S., Jeon, S. M., Park, S. H., Lim, J. S., Lee, S. B., Liu, R. R., Du, L., Kim, S., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02927-3 · Cited by 95 · see citing works
PHGDH: a novel therapeutic target in cancer
Lee, C. M., Hwang, Y., Kim, M., Park, Y.-C., Kim, H., & Fang, S. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01268-1 · Cited by 81 · see citing works
NSUN2 promotes colorectal cancer progression by enhancing SKIL mRNA stabilization
Zou, S., Huang, Y., Yang, Z., Zhang, J., Meng, M., Zhang, Y., Feng, J., Sun, R., Li, W., Wang, W., et al. (2024) · Clinical and Translational Medicine · doi:10.1002/ctm2.1621 · Cited by 75 · see citing works
Self-citationCycling back to folate metabolism in cancer
Lee, Y., Vousden, K. H., & Hennequart, M. (2024) · Nature Cancer · doi:10.1038/s43018-024-00739-8 · Cited by 65 · see citing works
Kosakamoto, H., Okamoto, N., Aikawa, H., Sugiura, Y., Suematsu, M., Niwa, R., Miura, M., & Obata, F. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00608-7 · Cited by 46 · see citing works
Tombari, C., Zannini, A., Bertolio, R., Pedretti, S., Audano, M., Triboli, L., Cancila, V., Vacca, D., Caputo, M., Donzelli, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42458-1 · Cited by 51 · see citing works
Azuma, K., Xiang, H., Tagami, T., Kasajima, R., KATO, Y. O., Karakawa, S., Kikuchi, S., Imaizumi, A., Matsuo, N., Ishii, H., et al. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2021-004420 · Cited by 45 · see citing works
Yoon, B. K., Kim, H., Oh, T. G., Oh, S. K., Jo, S., Kim, M., Chun, K.-H., Hwang, N., Lee, S., Jin, S., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2217826120 · Cited by 45 · see citing works
Pancreatic cancer: molecular pathogenesis and emerging therapeutic strategies
Rozengurt, E., & Eibl, G. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02499-y · Cited by 47 · 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
Activating transcription factor 4: a regulator of stress response in human cancers
Wu, D., & Liang, J. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1370012 · Cited by 41 · see citing works
Chan, F.-F., Kwan, K. K., Seoung, D.-H., Chin, D. W., Ng, I. O., Wong, C. C., & Wong, C. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.10.025 · Cited by 40 · 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
Imbalanced unfolded protein response signaling contributes to 1-deoxysphingolipid retinal toxicity
Rosarda, J. D., Giles, S., Harkins-Perry, S. R., Mills, E. A., Friedlander, M., Wiseman, R. L., & Eade, K. (2023) · Nature Communications · doi:10.1038/s41467-023-39775-w · Cited by 35 · see citing works
A comprehensive review on signaling attributes of serine and serine metabolism in health and disease
Wu, D., Zhang, K., Khan, F. A., Pandupuspitasari, N. S., Guan, K., Sun, F., & Huang, C. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.129607 · Cited by 33 · 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
Transcription factor NKX2–1 drives serine and glycine synthesis addiction in cancer
Heylen, E., Verstraete, P., Aerschot, L. V., Geeraerts, S. L., Venken, T., Timcheva, K., Nittner, D., Verbeeck, J., Royaert, J., Gijbels, M. J., et al. (2023) · British Journal of Cancer · doi:10.1038/s41416-023-02216-y · Cited by 30 · see citing works
Epigenetic developmental mechanisms underlying sex differences in cancer
Rubin, J. B., Abou-Antoun, T., Ippolito, J. E., Llaci, L., Marquez, C., Wong, J. P., & Yang, L. (2024) · Journal of Clinical Investigation · doi:10.1172/jci180071 · Cited by 28 · see citing works
ASCT2 is a major contributor to serine uptake in cancer cells
Conger, K. O., Chidley, C., Ozgurses, M., Zhao, H., Kim, Y., Semina, S. E., Burns, P. A., Rawat, V., Lietuvninkas, L., Sheldon, R., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114552 · Cited by 25 · see citing works
Cordes, T., Kuna, R. S., McGregor, G. H., Khare, S., Gengatharan, J. M., Muthusamy, T., & Metallo, C. M. (2022) · Journal of Lipid Research · doi:10.1016/j.jlr.2022.100281 · Cited by 26 · see citing works
Badu, P., Baniulyte, G., Sammons, M. A., & Pager, C. T. (2024) · Journal of Virology · doi:10.1128/jvi.01055-24 · Cited by 23 · see citing works
Shuvalov, O., Kirdeeva, Y., Fefilova, E., Netsvetay, S., Zorin, M., Vlasova, Y., Fedorova, O., Daks, A., Parfenyev, S., & Barlev, N. (2023) · Metabolites · doi:10.3390/metabo13050656 · Cited by 21 · see citing works
Chen, Z., Xu, J., Fang, K., Jiang, H., Leng, Z., Wu, H., Zhang, Z., Wang, Z., Li, Z., Sun, M., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-024-02016-8 · Cited by 19 · see citing works
Zhao, X., Chen, C., Qiu, H., Liu, J., Shao, N., Guo, M., Jiang, Y., Zhao, J., & Xu, L. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107666 · Cited by 17 · see citing works
Amino acids metabolism: a potential target for cancer treatment
Ren, S., Zhou, X., Wang, Z., & Yuan, K. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02523-3 · Cited by 18 · see citing works
Xing, R., Liu, R., Man, Y., Liu, C., Zhang, Y., Gao, H., & Yang, W. (2025) · Cell Discovery · doi:10.1038/s41421-024-00758-w · Cited by 15 · see citing works
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
Identification of ATF3 as a novel protective signature of quiescent colorectal tumor cells
Lü, X., Zhong, L., Lindell, E., Veanes, M., Guo, J., Zhao, M., Salehi, M., Swartling, F. J., Chen, X., Sjöblom, T., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06204-1 · Cited by 13 · see citing works
Self-citationTFTG: A comprehensive database for human transcription factors and their targets
Zhou, X., Zhou, L., Qian, F., Chen, J., Zhang, Y., Yu, Z., Zhang, J., Yang, Y., Li, Y., Song, C., et al. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.04.036 · Cited by 12 · see citing works
Self-citationUnleashing metabolic power for axonal regeneration
Yang, X.-Y., & Zhou, B. (2024) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2024.07.001 · Cited by 12 · see citing works
Luo, P., Wang, F., Li, J., Liu, G., Qin, X., Yan, B., Cao, X., Liu, B., Wang, Y., Wu, G., et al. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110134 · Cited by 12 · see citing works
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
Huang, H., Mu, Y., Huang, Y., Ji, B., Wang, Y., Chen, C., Chen, Y., Luo, Z., Li, S., Zhang, Z., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59490-y · Cited by 11 · see citing works
Luo, X., Ge, J., Liu, J., Liu, Z., Bi, C., & Lan, S. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113136 · Cited by 11 · see citing works
MicroRNA regulation of the serine synthesis pathway in endocrine-resistant breast cancer cells
Petri, B. J., Piell, K. M., Wilt, A. E., Howser, A. D., Winkler, L., Whitworth, M. R., Valdés, B., Lehman, N. L., Clem, B. F., & Klinge, C. M. (2023) · Endocrine Related Cancer · doi:10.1530/erc-23-0148 · Cited by 15 · see citing works
Cis-Regulatory Elements in Mammals
Liu, X., Chen, M., Qu, X., Liu, W., Dou, Y., Liu, Q., Shi, D., Jiang, M., & Li, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms25010343 · Cited by 10 · see citing works
Metabolism and mRNA translation: a nexus of cancer plasticity
Tang, X., Li, K., Wang, Y., Rocchi, S., Shen, S., & Cerezo, M. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.10.009 · Cited by 10 · see citing works
Eduardo, M. B., Cottone, G., McCloskey, C. W., Liu, S., Palma, F. R., Zappia, M. P., Islam, A. B. M. M. K., Gao, P., Setya, J., Dennis, S., et al. (2025) · Science Advances · doi:10.1126/sciadv.ads9182 · Cited by 11 · see citing works
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
Vitamin B2 and B3 nutrigenomics reveals a therapy for NAXD disease
Garg, A., Blume, S. Y., Huynh, H., Barrios, A. M., Karabulut, O. O., Zhao, Q., Midha, A. D., Turner, A. W., Resnick, B. V., Chen, X., et al. (2026) · Cell · doi:10.1016/j.cell.2026.01.022 · Cited by 9 · see citing works
Self-citationMinchenko, 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
Su, P., Yang, Y., & Zheng, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1779543 · Cited by 8 · see citing works
Wang, H., Fan, M., Liu, S., Qu, M., Hou, X., Hou, J., Xu, Y., Shang, X., Liu, C., He, M., et al. (2024) · BMC Cancer · doi:10.1186/s12885-024-13304-4 · Cited by 8 · see citing works
Self-citationLin, Z., Chang, C., Zhao, S., Fang, L., & Wang, P. (2025) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2025.0115 · Cited by 8 · see citing works
Tsai, C., Yu, M., Lee, Y., Feng, K.-C., Wu, C.-H., Li, Y.-C., Cheng, M., Lin, S., Huang, S.-F., Lin, T., et al. (2025) · Cancer Gene Therapy · doi:10.1038/s41417-025-00951-3 · Cited by 6 · see citing works
Yu, M., Hong, Y., Pan, Q., Zheng, P., He, Y., Zhu, W., Xu, S., & Lv, Q. (2026) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03627-w · Cited by 6 · see citing works
Wei, E., He, P., Wang, R., Xu, S., Zhang, Y., Wang, Q., Tang, X., & Shen, Z. (2023) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2023.105568 · Cited by 6 · see citing works
ASCT2 is the primary serine transporter in cancer cellsPreprint
Conger, K. O., Chidley, C., Ozgurses, M., Zhao, H., Kim, Y., Semina, S. E., Burns, P. A., Rawat, V., Sheldon, R., Ben-Sahra, I., et al. (2023) · bioRxiv · doi:10.1101/2023.10.09.561530 · Cited by 5 · see citing works
Hao, L., Li, B., Lü, S., An, Z.-C., Yin, Z.-Y., Du, Z., & Wang, H.-Q. (2026) · Journal of Biomedical Science · doi:10.1186/s12929-025-01205-y · Cited by 5 · see citing works
Ma, T., Ma, J., Wang, Y., Kui, X., Liu, J., Han, C., Wei, W., Lin, Z., & Song, X. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117182 · Cited by 5 · see citing works
Serine-Driven Metabolic Plasticity Drives Adaptive Resilience in Pancreatic Cancer Cells
Bonanomi, M., Mallia, S., Scalise, M., Aramini, T., Baldassari, F., Brivio, E., Conte, F., Dico, A. L., Bonas, M., Porro, D., et al. (2025) · Antioxidants · doi:10.3390/antiox14070833 · 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
Xia, P., Shuang, S., Fu, D., Liu, L., Yang, D., Guo, Y., Tian, Y., Ji, P., Yuan, X., Tian, Y., et al. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01307-2 · Cited by 4 · see citing works
Amino Acids Supplementation in Cancer: What Do We Feed, the Patient or the Tumor?
Corsetti, G., Pasini, E., Romano, C., & Dioguardi, F. (2025) · Nutrients · doi:10.3390/nu17172813 · Cited by 4 · see citing works
Diether, N. E., Kommadath, A., Fouhse, J. M., Zijlstra, R. T., Stothard, P., & Willing, B. P. (2024) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00146.2024 · Cited by 4 · see citing works
Li, Q., Meng, W., Xie, C., Wang, F., Deng, Y., Chen, K., Li, Y., Li, Y. H., Wen, Y., Zhu, J., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.140764 · Cited by 3 · see citing works
Self-citationMetabolic remodeling and immune evasion in glioblastoma: a focus on serine and lipid networks
Jiang, D., Wang, C., Zhao, Y., & Li, Y. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1676560 · Cited by 3 · see citing works
Metabolic Vulnerabilities as a Therapeutic Target in Breast Cancer
Guo, S., & Addison, C. (2026) · Current Oncology · doi:10.3390/curroncol33020129 · Cited by 4 · see citing works
Chen, S., Chang, K., Lin, W.-Y., Hsu, S.-Y., Sung, H., Lin, Y.-H., Feng, T., Hou, C., & Juang, H. (2024) · Biomedical Journal · doi:10.1016/j.bj.2024.100756 · Cited by 3 · see citing works
Wang, J., Zhang, X., Zhan, S., Han, F., Wang, Q., Liu, Y., & Huang, Z. (2024) · Journal of Nutrition · doi:10.1016/j.tjnut.2024.10.041 · Cited by 3 · see citing works
Wang, M., Sun, G., Fan, Y., Sima, G., Sun, X., Qiu, T., & Li, X. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01621-x · Cited by 3 · see citing works
Self-citationDrivers of de novo Serine/Glycine synthesis in acute leukemia
Verstraete, P., Keersmaecker, K. D., & Kampen, K. R. (2023) · FEBS Letters · doi:10.1002/1873-3468.14700 · Cited by 3 · see citing works
Li, Y., Chen, Y., Wang, J.-W., Wu, H.-H., Hsu, H., Ho, D., Yang, C., & Tian, Y. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118032 · Cited by 2 · see citing works
Hashimoto, T., Saito, S., Ohata, M., & Okuwaki, M. (2025) · FEBS Journal · doi:10.1111/febs.70124 · Cited by 2 · see citing works
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
Self-citationMinchenko, О. H., Kulish, Y. V., Viletska, Y. M., Khita, O. O., Rudnytska, O. V., Kozynkevych, H. E., & Minchenko, D. O. (2024) · Endocrine Regulations · doi:10.2478/enr-2024-0029 · Cited by 2 · see citing works
Cordes, T., Kuna, R. S., McGregor, G. H., Khare, S., Gengatharan, J. M., Muthusamy, T., & Metallo, C. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.19.476986 · Cited by 2 · see citing works
Regulation of RNA methylation by therapy treatment, promotes tumor survivalPreprint
Bukhari, S. I. A., Truesdell, S. S., Datta, C., Choudhury, P., Wu, K. Q., Shrestha, J., Maharjan, R., Plotsker, E., Elased, R. K., Laisa, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.19.540602 · Cited by 2 · see citing works
Chlamydia trachomatis L2 434/Bu readily activates glycolysis under hypoxia for efficient metabolism
Li, R., Zhang, S., Otsuguro, S., Nagao, M., Matsuda, A., Thapa, J., Okubo, T., Maenaka, K., Higashi, H., & Yamaguchi, H. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150461 · Cited by 1 · see citing works
The serine synthesis pathway is indispensable for glioblastoma growth and malignancy
Yun, H. J., Liu, R. R., & Lee, J. (2025) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-025-00247-1 · Cited by 1 · see citing works
Weng, X., Luo, J., Xu, J., Huang, S., Hu, J., & Tang, Z. (2025) · Pancreas · doi:10.1097/mpa.0000000000002613 · Cited by 1 · see citing works
Daniel, M. M., & Andwey, G. H. (2026) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.71007 · Cited by 1 · see citing works
Targeting FOXM1/PSAT1 axis by Brusatol inhibits lung cancer malignant progression
Ou, S., Wang, X., Sun, Y., Liang, Y., Bai, J., Han, C., & Song, J. (2026) · Pathology - Research and Practice · doi:10.1016/j.prp.2026.156365 · Cited by 1 · see citing works
Zhou, X., Zhao, M., Cao, Y., Zhou, X., & Wang, K. (2026) · Cancer Medicine · doi:10.1002/cam4.71780 · Cited by 1 · see citing works
Lin, H., Chen, H.-H., Lin, Y.-P., Li, H.-F., Lin, J.-H., Lee, K., & Tseng, T. (2026) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00006.2026 · Cited by 1 · see citing works
Xi, C., Pang, J., Oliaeimotlagh, M., Mao, R., Zhi, W., Jones, K., Hu, T., Shi, H., Ande, S., Horuzsko, A., et al. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-09052-x · Cited by 1 · see citing works
Self-citationCCDC86-BHLHE40-ATF3 axis promotes aerobic glycolysis and tumor development in glioma
Liu, J., Du, D., Huang, Y., Tian, J., Wang, X., Chen, L., & Wang, F. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101643 · Cited by 1 · see citing works
Eduardo, M. B., Cottone, G., McCloskey, C. W., Liu, S., Zappia, M. P., Benevolenskaya, E. V., Islam, A. B. M. M. K., Frolov, M. V., Palma, F. R., Gao, P., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.21.581404 · Cited by 1 · see citing works
Serine auxotrophy is a targetable vulnerability driven by PSAT1 suppression in AMLPreprint
Sinanidis, I., Tsakiroglou, P., Dubner, B. G., Foertsch, R., Gondek, J., Choi, I., Paun, B. C., Zhao, L., Ghiaur, G., & Dalton, W. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.13.651470 · Cited by 1 · see citing works
Mathematical modelling of carbohydrate and protein metabolism in muscle
Alharbi, B. M., Williams, H. E., Parr, T., Brameld, J. M., Fallaize, C. J., & Wattis, J. A. D. (2025) · Mathematical Biosciences · doi:10.1016/j.mbs.2025.109455
Eduardo, M. B., Islam, A. B. M. M. K., McCloskey, C. W., Zappia, M. P., Frolov, M. V., Khokha, R., Benevolenskaya, E. V., Khan, S. A., & Clare, S. E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.01.679891
Serine metabolism reprogramming in cancer: a multi-tiered regulatory framework
Yuan, Y., Wang, K., Jin, Y., & Han, T. (2025) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2025188
Yun, H. J., Li, M., Guo, D., Jeon, S. M., Park, S. H., Lim, J. S., Lee, S. B., Liu, R., Du, L., Kim, S.-H., et al. (2023) · Figshare · doi:10.6084/m9.figshare.24819674
Gao, J., Yang, Y., Chang, X., Wang, X., Zhang, Z., Shi, S., Liu, Y., Su, J., Chen, Z., Sun, R., et al. (2026) · Cancer Cell International · doi:10.1186/s12935-026-04171-z
Serine Hydroxymethyltransferase in Cancer Cells
Гаврилюк, Л. А. (2025) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750824601371
Rewiring of de novo serine synthesis supports tumorigenesis under deficiency of TET2
Zheng, K., Rao, K., Lü, X., Yang, M., Wu, H., Ai, Z., & He, J. (2026) · British Journal of Cancer · doi:10.1038/s41416-026-03526-7
Dong, Y., Zheng, J., Dong, X., Lv, Y., Xu, Z., Ye, C., Zhu, S., Dong, H., & Lv, Y. (2026) · Food and Chemical Toxicology · doi:10.1016/j.fct.2026.116274
Metabolic targeting of cyst(e)ine enhances carboplatin responsiveness in ovarian cancer
Yoon, I., Oh, S., Park, S. Y., Park, J., Jang, H., Park, E., You, K. A., Kim, K., Hwang, S., Kim, H. Y., et al. (2026) · Cancer & Metabolism · doi:10.1186/s40170-026-00450-5
Dutti, G. B., Mangialardi, K., Rasola, S., Sebastio, L., Tarantini, F., Cumbo, C., Anelli, L., Zagaria, A., Coccaro, N., Minervini, A., et al. (2026) · Genes · doi:10.3390/genes17080954
Sun, C., Wu, S., Li, Z., Huang, C., & Wu, D. (2026) · Biochemical Pharmacology · doi:10.1016/j.bcp.2026.118376
Serine auxotrophy is a targetable vulnerability driven by PSAT1 suppression in AML
Sinanidis, I., Tsakiroglou, P., Dubner, B. G., Foertsch, R., Gondek, J., Choi, I., Paun, B. C., Supeanu, T., Zhao, L., Ghiaur, G., et al. (2026) · Leukemia · doi:10.1038/s41375-026-03176-x · Cited by 1 · see citing works
- Authors
- Li, X., Gracilla, D., Cai, L., Zhang, M., Yu, X., Chen, X., Zhang, J., Long, X., Ding, H.-F., & Yan, C.
- Affiliations
- Augusta University (US)
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute (US)
- Corresponding author
- Yan, Chunhong
- ORCID
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2021-09
- Volume
- 36
- Issue
- 12
- Pages
- 109706
- ISSN
- 2211-1247 (ISSN-L)
- PMC
- PMC8491098
- OpenAlex
- W3199501069
- Cited by
- 98
- References
- 67
- Citations by year
- 2026: 20 · 2025: 25 · 2024: 26 · 2023: 20 · 2022: 7
- FWCI
- 5.26
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion, other-oa)
- PubMed Central (acceptedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (R01CA139107, R01CA190429, R01CA236890, R01CA240966, R01HL122686, R01HL139794)
- U.S. Department of Defense (W81XWH1910587)
- 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 › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- ATF3, serine synthesis pathway, serine biosynthesis, PHGDH, PSAT1, phosphoserine phosphatase, ATF4, P300, transcriptional regulation, tumor growth, cancer metabolism, protein stability
- MeSH terms
- Transaminases, Animals, Humans, Male, Mice, Nude, Neoplasms, Phosphoric Monoester Hydrolases, Promoter Regions, Genetic, Protein Binding, Serine, Transplantation, Heterologous, Gene Expression Regulation, Neoplastic, Cell Line, Tumor, Phosphoglycerate Dehydrogenase, p300-CBP Transcription Factors, Mice, Activating Transcription Factor 3, Activating Transcription Factor 4, Biosynthetic Pathways, Protein Stability
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review