An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation
Open accessAbstract
BACKGROUND: The gene encoding the serine biosynthesis pathway enzyme PHGDH is located in a region of focal genomic copy number gain in human cancers. Cells with PHGDH amplification are dependent on enzyme expression for proliferation. However, dependence on increased PHGDH expression extends beyond production of serine alone, and further studies of PHGDH function are necessary to elucidate its role in cancer cells. These studies will require a physiologically relevant form of the enzyme for experiments using engineered cell lines and recombinant protein. RESULTS: The addition of an N-terminal epitope tag to PHGDH abolished the ability to support proliferation of PHGDH-amplified cells despite retention of some activity to convert 3-PG to PHP. Introducing an R236E mutation into PHGDH eliminates enzyme activity, and this catalytically inactive enzyme cannot support proliferation of PHGDH-dependent cells, arguing that canonical enzyme activity is required. Tagged and untagged PHGDH exhibit the same intracellular localization and ability to produce D-2-hydroxyglutarate (D-2HG), an error product of PHGDH, arguing that neither mislocalization nor loss of D-2HG production explains the inability of epitope-tagged PHGDH to support proliferation. To enable studies of PHGDH function, we report a method to purify recombinant PHGDH and found that untagged enzyme activity was greater than N-terminally tagged enzyme. Analysis of tagged and untagged PHGDH using size exclusion chromatography and electron microscopy found that an N-terminal epitope tag alters enzyme structure. CONCLUSIONS: Purification of untagged recombinant PHGDH eliminates the need to use an epitope tag for enzyme studies. Furthermore, while tagged PHGDH retains some ability to convert 3PG to PHP, the structural alterations caused by including an epitope tag disrupts the ability of PHGDH to sustain cancer cell proliferation.
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?
Functional PHGDH loss is toxic to tumor cells with PHGDH amplification or high serine biosynthetic flux.
“Functional PHGDH loss is toxic to tumor cells with PHGDH amplification or high serine biosynthetic flux (Locasale et al., 2011; Mattaini et al., 2015; Possemato et al., 2011; Zhang et al., 2017), and small-molecule inhibitors targeting PHGDH have been shown to inhibit serine synthesis and tumor proliferation in vitro and in xenograft cancer models (Mullarky et al., 2016; Pacold et al., 2016; Wang”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Mattaini et al., 2015
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
Smith, D. B., & Johnson, K. S. (1988) · Gene · doi:10.1016/0378-1119(88)90005-4 · Cited by 5,974 · see citing works
EMAN2: An extensible image processing suite for electron microscopy
Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.05.009 · Cited by 2,914 · see citing works
Expression profiling reveals off-target gene regulation by RNAi
Jackson, A. L., Bartz, S. R., Schelter, J., Kobayashi, S. V., Burchard, J., Mao, M., Li, B., Cavet, G., & Linsley, P. S. (2003) · Nature Biotechnology · doi:10.1038/nbt831 · Cited by 2,370 · see citing works
SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
Frank, J., Radermacher, M., Penczek, P. A., Zhu, J., Li, Y., Ladjadj, M., & Leith, A. G. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0030 · Cited by 2,026 · 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
Accurate determination of local defocus and specimen tilt in electron microscopy
Mindell, J. A., & Grigorieff, N. (2003) · Journal of Structural Biology · doi:10.1016/s1047-8477(03)00069-8 · Cited by 1,414 · see citing works
Targeting cancer metabolism: a therapeutic window opens
Heiden, M. G. V. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3504 · Cited by 1,409 · 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
Self-citationHochuli, E., Bannwarth, W., Döbeli, H., Gentz, R., & Stüber, D. (1988) · Nature Biotechnology · doi:10.1038/nbt1188-1321 · Cited by 1,050 · 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
A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification
Hopp, T. P., Prickett, K. S., Price, V. L., Libby, R. T., March, C. J., Cerretti, D. P., Urdal, D. L., & Conlon, P. J. (1988) · Nature Biotechnology · doi:10.1038/nbt1088-1204 · Cited by 959 · see citing works
Field, J. M., Nikawa, J., Broek, D., MACDONALD, B. S., Rodgers, L., Wilson, I. A., Lerner, R. A., & Wigler, M. H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2159 · Cited by 949 · 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
Phosphoglycerate Mutase 1 Coordinates Glycolysis and Biosynthesis to Promote Tumor Growth
Hitosugi, T., Zhou, L., Elf, S., Fan, J., Kang, H., Seo, J. H., Shan, C., Dai, Q., Zhang, L., Xie, J., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.09.020 · Cited by 434 · see citing works
SPARX, a new environment for Cryo-EM image processing
Hohn, M. H., Tang, G., Goodyear, G., Baldwin, P. R., Huang, Z. X., Penczek, P. A., Yang, C., Glaeser, R. M., Adams, P. D., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.07.003 · Cited by 364 · see citing works
Field, J. M., Nikawa, J., Broek, D., MACDONALD, B. S., Rodgers, L., Wilson, I. A., Lerner, R. A., & Wigler, M. H. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2159-2165.1988 · Cited by 330 · see citing works
Affinity chromatography of phosphofructokinase using Cibacron blue F3G-A
Böhme, H.-J., Kopperschläger, G., Schulz, J., & Hofmann, E. (1972) · Journal of Chromatography A · doi:10.1016/s0021-9673(00)83103-9 · Cited by 293 · see citing works
Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
Snell, K. (1984) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(84)90021-9 · Cited by 267 · cited 1× · see citing works
“A linked assay with PSAT was used to interrogate 3-PG and NAD+ to PHP and NADH conversion by PHGDH because the equilibrium of this reaction lies toward 3-PG [23].”
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
Human Phosphoglycerate Dehydrogenase Produces the Oncometabolite d -2-Hydroxyglutarate
Fan, J., Teng, X., Liu, L., Mattaini, K. R., Looper, R., Heiden, M. G. V., & Rabinowitz, J. D. (2014) · ACS Chemical Biology · doi:10.1021/cb500683c · Cited by 201 · see citing works
Self-citationSmall molecule activation of PKM2 in cancer cells induces serine auxotrophy
Kung, C., Hixon, J., Choe, S., Marks, K., Gross, S., Murphy, E., DeLaBarre, B., Cianchetta, G., Sethumadhavan, S., Wang, X., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.07.021 · Cited by 192 · see citing works
Adams, C. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610510200 · Cited by 165 · see citing works
Jarvik, J. W., & Telmer, C. A. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.601 · Cited by 163 · see citing works
PHGDH amplification and altered glucose metabolism in human melanoma
Mullarky, E., Mattaini, K. R., Heiden, M. G. V., Cantley, L. C., & Locasale, J. W. (2011) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2011.00919.x · Cited by 147 · see citing works
Self-citationEnzymic imbalance in serine metabolism in human colon carcinoma and rat sarcoma
Snell, K., Natsumeda, Y., Eble, J., Glover, J., & Weber, G. (1988) · British Journal of Cancer · doi:10.1038/bjc.1988.15 · Cited by 133 · see citing works
Zhao, G., & Winkler, M. E. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.1.232-239.1996 · Cited by 129 · see citing works
Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase
Achouri, Y., Rider, M. H., SCHAFTINGEN, E. V., & Robbi, M. (1997) · Biochemical Journal · doi:10.1042/bj3230365 · Cited by 93 · see citing works
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
Phosphoglycerate dehydrogenase is dispensable for breast tumor maintenance and growth
Chen, J., Chung, F., Yang, G., Pu, M., Gao, H., Jiang, W., Yin, H., Capka, V., Kasibhatla, S., Laffitte, B., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.1540 · Cited by 82 · see citing works
Labrou, N. E., Karagouni, A. D., & Clonis, Y. D. (1995) · Biotechnology and Bioengineering · doi:10.1002/bit.260480314 · Cited by 71 · see citing works
Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase
Dey, S., Grant, G. A., & Sacchettini, J. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414489200 · Cited by 67 · see citing works
Tischendorf, G. W., Zeichhardt, H., & Stöffler, G. (1974) · Molecular and General Genetics MGG · doi:10.1007/bf00267716 · Cited by 66 · see citing works
Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases
Grant, G. A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.10.005 · Cited by 66 · see citing works
Thompson, J. R., Bell, J. K., Bratt, J. M., Grant, G. A., & Banaszak, L. J. (2005) · Biochemistry · doi:10.1021/bi047944b · Cited by 57 · see citing works
Tabatabaie, L., de Koning, T. J., Geboers, A. J. J. M., van den Berg, I. E. T., Berger, R., & Klomp, L. W. J. (2009) · Human Mutation · doi:10.1002/humu.20934 · Cited by 54 · see citing works
Dey, S., Hu, Z., Xu, X. L., Sacchettini, J. C., & Grant, G. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414488200 · Cited by 53 · see citing works
Ali, V., Hashimoto, T., Shigeta, Y., & Nozaki, T. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04195.x · Cited by 47 · see citing works
The Mechanism of Velocity Modulated Allosteric Regulation in D-3-Phosphoglycerate Dehydrogenase
Al-Rabiee, R., Lee, E. J., & Grant, G. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13013 · Cited by 44 · see citing works
The Contribution of Adjacent Subunits to the Active Sites ofd-3-Phosphoglycerate Dehydrogenase
Grant, G. A., Kim, S. J., Xu, X. L., & Hu, Z. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5357 · Cited by 26 · see citing works
Chemical and Physical Properties
Moyer, E. E. (2003) · Springer eBooks · doi:10.1007/978-1-4615-0021-6_2 · Cited by 25 · see citing works
D-3-Phosphoglycerate dehydrogenase from chicken liver. II. Chemical and physical properties.
Grant, G. A., & Bradshaw, R. A. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40881-7 · Cited by 23 · see citing works
Purification and subunit structure of phosphoglycerate dehydrogenase from rabbit liver
Lund, K., Merrill, D. K., & Guynn, R. W. (1986) · Biochemical Journal · doi:10.1042/bj2380919 · Cited by 9 · see citing works
Purification of Muscle Enzymes by Pseudoaffinity Chromatography
Tulsani, N. B., Kumar, A., & Vijayalakshmi, M. A. (1999) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826069908544887 · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Targeting Metabolism for Cancer Therapy
Luengo, A., Gui, D. Y., & Vander Heiden, M. G. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.08.028 · Cited by 971 · see citing works
A PHGDH inhibitor reveals coordination of serine synthesis and one-carbon unit fate
Pacold, M. E., Brimacombe, K. R., Chan, S. H., Rohde, J. M., Lewis, C. A., Swier, L. J. Y. M., Possemato, R., Chen, W. W., Sullivan, L. B., Fiske, B. P., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2070 · Cited by 553 · see citing works
Self-citationThe 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
Self-citationL-2-Hydroxyglutarate production arises from noncanonical enzyme function at acidic pH
Intlekofer, A. M., Wang, B., Liu, H., Shah, H., Carmona-Fontaine, C., Rustenburg, A. S., Salah, S., Gunner, M. R., Chodera, J. D., Cross, J. R., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2307 · Cited by 268 · 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
Self-citationSerine Synthesis via PHGDH Is Essential for Heme Production in Endothelial Cells
Vandekeere, S., Dubois, C., Kalucka, J. M., Sullivan, M. R., García‐Caballero, M., Goveia, J., Chen, R., Diehl, F. F., Bar-Lev, L., Souffreau, J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.06.009 · Cited by 188 · see citing works
Kremer, J. C., Prudner, B. C., Lange, S. E. S., Bean, G. R., Schultze, M., Brashears, C. B., Radyk, M. D., Redlich, N. J., Tzeng, S., Kami, K., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.077 · Cited by 160 · see citing works
Wang, K., Luo, L., Fu, S., Wang, M., Wang, Z., Dong, L., Wu, X., Dai, L., Peng, Y., Shen, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36708-5 · Cited by 133 · see citing works
The complexity of the serine glycine one-carbon pathway in cancer
Reina‐Campos, M., Díaz-Meco, M. T., & Moscat, J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201907022 · Cited by 123 · see citing works
Wu, Y., Tang, L., Huang, H., Yu, Q., Hu, B., Wang, G., Ge, F., Yin, T., Li, S., & Yu, X. (2023) · Nature Communications · doi:10.1038/s41467-023-37094-8 · Cited by 119 · see citing works
Amino acid management in cancer
Tsun, Z.-Y., & Possemato, R. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.08.002 · Cited by 113 · see citing works
The Role of D-3-Phosphoglycerate Dehydrogenase in Cancer
Zhao, X., Fu, J., Du, J., & Xu, W. (2020) · International Journal of Biological Sciences · doi:10.7150/ijbs.41051 · Cited by 90 · see citing works
Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate
Oslund, R., Su, X., Haugbro, M., Kee, J., Esposito, M., David, Y., Wang, B., Ge, E. J., Perlman, D. H., Kang, Y., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2453 · Cited by 87 · see citing works
D-3-Phosphoglycerate Dehydrogenase
Grant, G. A. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00110 · Cited by 82 · 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
Rohde, J. M., Brimacombe, K. R., Liu, L., Pacold, M. E., Yasgar, A., Cheff, D. M., Lee, T. D., Rai, G., Baljinnyam, B., Li, Z., et al. (2018) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2018.02.016 · Cited by 46 · see citing works
The Role of Tumor Metabolic Reprogramming in Tumor Immunity
Zhang, X., Song, W., Gao, Y., Zhang, Y., Zhao, Y., Hao, S., & Ni, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417422 · Cited by 44 · see citing works
Shu, Y., Hao, Y., Feng, J., Liu, H., Li, S., Feng, J., Jiang, Z., Ye, L., Zhou, Y., Sun, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2022111550 · Cited by 39 · see citing works
Phosphoglycerate dehydrogenase is a novel predictor for poor prognosis in gastric cancer
Wu, H. J., Xian, Y., Zhang, S., Wang, X., Jin, Q., & Wang, W. (2016) · OncoTargets and Therapy · doi:10.2147/ott.s105787 · Cited by 36 · see citing works
Wen, X., Kuang, Y., Zhou, L., Yu, B., Chen, Q., Fu, Y., Yan, Z., Guo, H., Lyu, Q., Xie, J., et al. (2018) · Medical Science Monitor · doi:10.12659/msm.906602 · Cited by 34 · see citing works
Warburg and Krebs and related effects in cancer
Unterlass, J. E., & Curtin, N. J. (2019) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2019.4 · Cited by 35 · see citing works
Bi, F., An, Y., Sun, T., You, Y., & Yang, Q. F. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.643129 · Cited by 30 · see citing works
Bruegger, J. J., Smith, B. C., Wynia-Smith, S. L., & Marletta, M. A. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.817700 · Cited by 27 · see citing works
Dimerization of PHGDH via the catalytic unit is essential for its enzymatic function
Xu, H., Qing, X., Wang, Q., Li, C., & Lai, L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100572 · Cited by 17 · see citing works
Increased PHGDH expression promotes aberrant melanin accumulation
Mattaini, K. R., Sullivan, M. R., Lau, A. N., Fiske, B. P., Bronson, R. T., & Heiden, M. G. V. (2019) · BMC Cancer · doi:10.1186/s12885-019-5933-5 · Cited by 13 · see citing works
Self-citationMoonlighting functions of phosphoglycerate dehydrogenase in cancer
Wang, C., An, S., Zhao, L., Li, S., Huang, J., & Ren, W. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115940 · Cited by 11 · see citing works
Paczia, N., Becker‐Kettern, J., Conrotte, J., Cifuente, J. O., Guerin, M. E., & Linster, C. L. (2019) · Biochemistry · doi:10.1021/acs.biochem.8b00990 · Cited by 11 · see citing works
Cheng, B., Peng, P., Chen, S., Liu, R., Li, X., Wang, K., Ma, J., Tang, N., Tang, N., & Huang, A. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02304-w · Cited by 9 · see citing works
Pakarian, P., & Pawelek, P. D. (2016) · Biochimie · doi:10.1016/j.biochi.2016.04.007 · Cited by 9 · see citing works
Modrzejewska, M., Gawroński, M., & Gackowski, D. (2021) · Analytical Biochemistry · doi:10.1016/j.ab.2021.114129 · Cited by 7 · see citing works
Zhong, J., Huang, K., Xie, S., Tan, A., Peng, J., Nie, D., Ma, L., & Li, Y. (2024) · Journal of Cancer · doi:10.7150/jca.90822 · Cited by 6 · see citing works
Glyoxalase 2 Coordinates de Novo Serine Metabolism
Trujillo, M. N., Jennings, E. Q., Farrera, D. O., Kitamura, N., Anderson, C. C., Gehrke, S. A., Reisz, J. A., Johannsen, M., Roede, J. R., D’Alessandro, A., et al. (2025) · ChemBioChem · doi:10.1002/cbic.202401086 · Cited by 6 · see citing works
Synthesis and biological evaluation of innovative thiourea derivatives as PHGDH inhibitors
Xiang, J., Tao, L., Zhou, Y., Tan, Y., Li, Z., Zhao, Y., Sun, Q., & Luo, Y. (2020) · Chemical Papers · doi:10.1007/s11696-020-01188-0 · Cited by 3 · see citing works
Yamamoto, K., Mohri, S., & Furuya, S. (2020) · Archives of Insect Biochemistry and Physiology · doi:10.1002/arch.21751 · Cited by 3 · see citing works
Designing Cyclic-Constrained Peptides to Inhibit Human Phosphoglycerate Dehydrogenase
Qing, X., Wang, Q., Xu, H., Liu, P., & Lai, L. (2023) · Molecules · doi:10.3390/molecules28176430 · Cited by 3 · see citing works
Singh, R. K., Crawford, R. A., Mall, D. P., Pavitt, G. D., & Gerst, J. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.18.585503 · Cited by 2 · see citing works
Chen, J., Xu, M., Liu, Y., Hadi, F., Xue, S., Chien, S., & Zhong, S. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2532234123 · Cited by 1 · see citing works
Mattaini, K. R., Sullivan, M. R., Lau, A. N., Fiske, B. P., Bronson, R. T., & Heiden, M. G. V. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/249250 · Cited by 1 · see citing works
Self-citationBindingDB (2016) · UC San Diego · doi:10.7270/q2h70dn5
- Authors
- Mattaini, K. R., Brignole, E. J., Kini, M., Davidson, S. M., Fiske, B. P., Drennan, C. L., & Vander Heiden, M. G.
- Affiliations
- Koch Institute for Integrative Cancer Research At MIT (US)
- Howard Hughes Medical Institute (US)
- Venue
- Cancer & Metabolism
- Published
- 2015-04-29
- Volume
- 3
- Issue
- 1
- Pages
- 5-5
- ISSN
- 2049-3002 (ISSN-L)
- PMC
- PMC4414297
- OpenAlex
- W1978908743
- Cited by
- 38
- References
- 44
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 1 · 2021: 3 · 2020: 4 · 2019: 5 · 2018: 6 · 2017: 4 · 2016: 4 · 2015: 1
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Cancer & Metabolism (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (1122374, T32GM007287, R01CA168653)
- American Association for Cancer Research
- Burroughs Wellcome Fund
- National Cancer Institute (R01CA168653, P30CA014051, P30-CA-14051)
- National Institute of General Medical Sciences (T32GM007287)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- PHGDH, epitope tagging, recombinant protein purification, enzyme structure, serine biosynthesis, tumor cell proliferation, D-2-hydroxyglutarate, 3-phosphoglycerate
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
