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Volumn 214, Issue 3, 2016, Pages 249-257

The importance of serine metabolism in cancer

Author keywords

[No Author keywords available]

Indexed keywords

SERINE; NUCLEOTIDE; PHOSPHOGLYCERATE DEHYDROGENASE;

EID: 84980041497     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201604085     Document Type: Review
Times cited : (300)

References (82)
  • 1
    • 0030890811 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase
    • Achouri, Y., M.H. Rider, E.V. Schaftingen, and M. Robbi. 1997. Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase. Biochem. J. 323:365-370. http://dx.doi.org/10.1042/bj3230365.
    • (1997) Biochem. J , vol.323 , pp. 365-370
    • Achouri, Y.1    Rider, M.H.2    Schaftingen, E.V.3    Robbi, M.4
  • 3
    • 34447121352 scopus 로고    scopus 로고
    • Role of the transcription factor ATF4 in the anabolic actions of insulin and the anti-anabolic actions of glucocorticoids
    • Adams, C.M. 2007. Role of the transcription factor ATF4 in the anabolic actions of insulin and the anti-anabolic actions of glucocorticoids. J. Biol. Chem. 282:16744-16753. http://dx.doi.org/10.1074/jbc.M610510200.
    • (2007) J. Biol. Chem , vol.282 , pp. 16744-16753
    • Adams, C.M.1
  • 6
    • 84957899529 scopus 로고    scopus 로고
    • mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle
    • Ben-Sahra, I., G. Hoxhaj, S.J. Ricoult, J.M. Asara, and B.D. Manning. 2016. mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle. Science. 351:728-733. http://dx.doi.org/10.1126/science.aad0489.
    • (2016) Science , vol.351 , pp. 728-733
    • Ben-Sahra, I.1    Hoxhaj, G.2    Ricoult, S.J.3    Asara, J.M.4    Manning, B.D.5
  • 8
    • 79251517382 scopus 로고    scopus 로고
    • Regulation of cancer cell metabolism
    • Cairns, R.A., I.S. Harris, and T.W. Mak. 2011. Regulation of cancer cell metabolism. Nat. Rev. Cancer. 11:85-95. http://dx.doi.org/10.1038/nrc2981.
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 85-95
    • Cairns, R.A.1    Harris, I.S.2    Mak, T.W.3
  • 10
    • 84891913582 scopus 로고    scopus 로고
    • Phosphoglycerate dehydrogenase is dispensable for breast tumor maintenance and growth
    • Chen, J., F. Chung, G. Yang, M. Pu, H. Gao, W. Jiang, H. Yin, V. Capka, S. Kasibhatla, B. Laffitte, et al. 2013. Phosphoglycerate dehydrogenase is dispensable for breast tumor maintenance and growth. Oncotarget. 4:2502-2511. http://dx.doi.org/10.18632/oncotarget.1540.
    • (2013) Oncotarget , vol.4 , pp. 2502-2511
    • Chen, J.1    Chung, F.2    Yang, G.3    Pu, M.4    Gao, H.5    Jiang, W.6    Yin, H.7    Capka, V.8    Kasibhatla, S.9    Laffitte, B.10
  • 11
    • 0014470830 scopus 로고
    • The effects of dietary protein on the hepatic enzymes of serine metabolism in the rabbit
    • Cheung, G.P., J.P. Cotropia, and H.J. Sallach. 1969. The effects of dietary protein on the hepatic enzymes of serine metabolism in the rabbit. Arch. Biochem. Biophys. 129:672-682. http://dx.doi.org/10.1016/0003-9861(69)90227-6.
    • (1969) Arch. Biochem. Biophys , vol.129 , pp. 672-682
    • Cheung, G.P.1    Cotropia, J.P.2    Sallach, H.J.3
  • 13
    • 40749099894 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a phosphotyrosine-binding protein
    • Christofk, H.R., M.G. Vander Heiden, N. Wu, J.M. Asara, and L.C. Cantley. 2008b. Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature. 452:181-186. http://dx.doi.org/10.1038/nature06667.
    • (2008) Nature , vol.452 , pp. 181-186
    • Christofk, H.R.1    Vander Heiden, M.G.2    Wu, N.3    Asara, J.M.4    Cantley, L.C.5
  • 16
    • 0014887484 scopus 로고
    • Two enzymes of serine metabolism in rat liver and hepatomas
    • Davis, J.L., H.J. Fallon, and H.P. Morris. 1970. Two enzymes of serine metabolism in rat liver and hepatomas. Cancer Res. 30:2917-2920.
    • (1970) Cancer Res , vol.30 , pp. 2917-2920
    • Davis, J.L.1    Fallon, H.J.2    Morris, H.P.3
  • 17
    • 75149148563 scopus 로고    scopus 로고
    • Q's next: The diverse functions of glutamine in metabolism, cell biology and cancer
    • DeBerardinis, R.J., and T. Cheng. 2010. Q's next: The diverse functions of glutamine in metabolism, cell biology and cancer. Oncogene. 29:313-324. http://dx.doi.org/10.1038/onc.2009.358.
    • (2010) Oncogene , vol.29 , pp. 313-324
    • DeBerardinis, R.J.1    Cheng, T.2
  • 19
    • 17644426079 scopus 로고    scopus 로고
    • D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes
    • Dey, S., Z. Hu, X.L. Xu, J.C. Sacchettini, and G.A. Grant. 2005. D-3-phosphoglycerate dehydrogenase from Mycobacterium tuberculosis is a link between the Escherichia coli and mammalian enzymes. J. Biol. Chem. 280:14884-14891. http://dx.doi.org/10.1074/jbc.M414488200.
    • (2005) J. Biol. Chem , vol.280 , pp. 14884-14891
    • Dey, S.1    Hu, Z.2    Xu, X.L.3    Sacchettini, J.C.4    Grant, G.A.5
  • 20
    • 84889684498 scopus 로고    scopus 로고
    • The histone H3 methyltransferase G9A epigenetically activates the serine-glycine synthesis pathway to sustain cancer cell survival and proliferation
    • Ding, J., T. Li, X. Wang, E. Zhao, J.H. Choi, L. Yang, Y. Zha, Z. Dong, S. Huang, J.M. Asara, et al. 2013. The histone H3 methyltransferase G9A epigenetically activates the serine-glycine synthesis pathway to sustain cancer cell survival and proliferation. Cell Metab. 18:896-907. http://dx.doi.org/10.1016/j.cmet.2013.11.004.
    • (2013) Cell Metab , vol.18 , pp. 896-907
    • Ding, J.1    Li, T.2    Wang, X.3    Zhao, E.4    Choi, J.H.5    Yang, L.6    Zha, Y.7    Dong, Z.8    Huang, S.9    Asara, J.M.10
  • 21
    • 84975455372 scopus 로고    scopus 로고
    • Reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway
    • Ducker, G.S., L. Chen, R.J. Morscher, J.M. Ghergurovich, M. Esposito, X. Teng, Y. Kang, and J.D. Rabinowitz. 2016. Reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway. Cell Metab. 23:1140-1153. http://dx.doi.org/10.1016/j.cmet.2016.04.016.
    • (2016) Cell Metab , vol.23 , pp. 1140-1153
    • Ducker, G.S.1    Chen, L.2    Morscher, R.J.3    Ghergurovich, J.M.4    Esposito, M.5    Teng, X.6    Kang, Y.7    Rabinowitz, J.D.8
  • 22
    • 0019493184 scopus 로고
    • The role of serine hydroxymethyltransferase in cell proliferation: DNA synthesis from serine following mitogenic stimulation of lymphocytes
    • Eichler, H.G., R. Hubbard, and K. Snell. 1981. The role of serine hydroxymethyltransferase in cell proliferation: DNA synthesis from serine following mitogenic stimulation of lymphocytes. Biosci. Rep. 1:101-106. http://dx.doi.org/10.1007/BF01117006.
    • (1981) Biosci. Rep , vol.1 , pp. 101-106
    • Eichler, H.G.1    Hubbard, R.2    Snell, K.3
  • 23
    • 0020958437 scopus 로고
    • Structural and kinetic differences between the M2 type pyruvate kinases from lung and various tumors
    • Eigenbrodt, E., S. Leib, W. Kramer, R.R. Friis, and W. Schoner. 1983. Structural and kinetic differences between the M2 type pyruvate kinases from lung and various tumors. Biomed. Biochim. Acta. 42:S278-S282.
    • (1983) Biomed. Biochim. Acta , vol.42 , pp. S278-S282
    • Eigenbrodt, E.1    Leib, S.2    Kramer, W.3    Friis, R.R.4    Schoner, W.5
  • 24
    • 84964994281 scopus 로고    scopus 로고
    • Serine biosynthesis and transport defects
    • El-Hattab, A.W. 2016. Serine biosynthesis and transport defects. Mol. Genet. Metab. 118:153-159. http://dx.doi.org/10.1016/j.ymgme.2016.04.010.
    • (2016) Mol. Genet. Metab , vol.118 , pp. 153-159
    • El-Hattab, A.W.1
  • 25
    • 84902332213 scopus 로고    scopus 로고
    • Quantitative flux analysis reveals folate-dependent NAD PH production
    • Fan, J., J. Ye, J.J. Kamphorst, T. Shlomi, C.B. Thompson, and J.D. Rabinowitz. 2014. Quantitative flux analysis reveals folate-dependent NAD PH production. Nature. 510:298-302. http://dx.doi.org/10.1038/nature13236.
    • (2014) Nature , vol.510 , pp. 298-302
    • Fan, J.1    Ye, J.2    Kamphorst, J.J.3    Shlomi, T.4    Thompson, C.B.5    Rabinowitz, J.D.6
  • 26
  • 27
    • 84874274833 scopus 로고    scopus 로고
    • Allosteric regulation of PKM2 allows cellular adaptation to different physiological states
    • Gui, D.Y., C.A. Lewis, and M.G. Vander Heiden. 2013. Allosteric regulation of PKM2 allows cellular adaptation to different physiological states. Sci. Signal. 6:pe7. http://dx.doi.org/10.1126/scisignal.2003925.
    • (2013) Sci. Signal , vol.6
    • Gui, D.Y.1    Lewis, C.A.2    Vander Heiden, M.G.3
  • 29
    • 0037064008 scopus 로고    scopus 로고
    • Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses
    • Herbig, K., E.P. Chiang, L.R. Lee, J. Hills, B. Shane, and P.J. Stover. 2002. Cytoplasmic serine hydroxymethyltransferase mediates competition between folate-dependent deoxyribonucleotide and S-adenosylmethionine biosyntheses. J. Biol. Chem. 277:38381-38389. http://dx.doi.org/10.1074/jbc.M205000200.
    • (2002) J. Biol. Chem , vol.277 , pp. 38381-38389
    • Herbig, K.1    Chiang, E.P.2    Lee, L.R.3    Hills, J.4    Shane, B.5    Stover, P.J.6
  • 32
    • 80053902441 scopus 로고    scopus 로고
    • Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
    • Hung, Y.P., J.G. Albeck, M. Tantama, and G. Yellen. 2011. Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab. 14:545-554. http://dx.doi.org/10.1016/j.cmet.2011.08.012.
    • (2011) Cell Metab , vol.14 , pp. 545-554
    • Hung, Y.P.1    Albeck, J.G.2    Tantama, M.3    Yellen, G.4
  • 33
    • 0017261388 scopus 로고
    • Inhibition of chicken pyruvate kinases by amino acids
    • Ibsen, K.H., and S.W. Marles. 1976. Inhibition of chicken pyruvate kinases by amino acids. Biochemistry. 15:1073-1079. http://dx.doi.org/10.1021/bi00650a018.
    • (1976) Biochemistry , vol.15 , pp. 1073-1079
    • Ibsen, K.H.1    Marles, S.W.2
  • 34
    • 0000796646 scopus 로고
    • Pathway of serine formation from carbohydrate in rat liver
    • Ichihara, A., and D.M. Greenberg. 1955. Pathway of serine formation from carbohydrate in rat liver. Proc. Natl. Acad. Sci. USA. 41:605-609. http://dx.doi.org/10.1073/pnas.41.9.605.
    • (1955) Proc. Natl. Acad. Sci. USA , vol.41 , pp. 605-609
    • Ichihara, A.1    Greenberg, D.M.2
  • 35
    • 84948094800 scopus 로고    scopus 로고
    • Pyruvate kinase: Function, regulation and role in cancer
    • Israelsen, W.J., and M.G. Vander Heiden. 2015. Pyruvate kinase: Function, regulation and role in cancer. Semin. Cell Dev. Biol. 43:43-51. http://dx.doi.org/10.1016/j.semcdb.2015.08.004.
    • (2015) Semin. Cell Dev. Biol , vol.43 , pp. 43-51
    • Israelsen, W.J.1    Vander Heiden, M.G.2
  • 38
    • 84888236467 scopus 로고    scopus 로고
    • Expression and clinical significance of phosphoglycerate dehydrogenase and squamous cell carcinoma antigen in cervical cancer
    • Jing, Z., W. Heng, D. Aiping, Q. Yafei, and Z. Shulan. 2013. Expression and clinical significance of phosphoglycerate dehydrogenase and squamous cell carcinoma antigen in cervical cancer. Int. J. Gynecol. Cancer. 23:1465-1469. http://dx.doi.org/10.1097/IGC.0b013e3182a0c068.
    • (2013) Int. J. Gynecol. Cancer , vol.23 , pp. 1465-1469
    • Jing, Z.1    Heng, W.2    Aiping, D.3    Yafei, Q.4    Shulan, Z.5
  • 40
    • 84964670673 scopus 로고    scopus 로고
    • Asparagine promotes cancer cell proliferation through use as an amino acid exchange factor
    • Krall, A.S., S. Xu, T.G. Graeber, D. Braas, and H.R. Christofk. 2016. Asparagine promotes cancer cell proliferation through use as an amino acid exchange factor. Nat. Commun. 7:11457. http://dx.doi.org/10.1038/ncomms11457.
    • (2016) Nat. Commun , vol.7 , pp. 11457
    • Krall, A.S.1    Xu, S.2    Graeber, T.G.3    Braas, D.4    Christofk, H.R.5
  • 42
    • 84901263663 scopus 로고    scopus 로고
    • Serine, but not glycine, supports one-carbon metabolism and proliferation of cancer cells
    • Labuschagne, C.F., N.J. van den Broek, G.M. Mackay, K.H. Vousden, and O.D. Maddocks. 2014. Serine, but not glycine, supports one-carbon metabolism and proliferation of cancer cells. Cell Reports. 7:1248-1258. http://dx.doi.org/10.1016/j.celrep.2014.04.045.
    • (2014) Cell Reports , vol.7 , pp. 1248-1258
    • Labuschagne, C.F.1    van den Broek, N.J.2    Mackay, G.M.3    Vousden, K.H.4    Maddocks, O.D.5
  • 45
    • 84880425659 scopus 로고    scopus 로고
    • Phosphoglycerate dehydrogenase induces glioma cells proliferation and invasion by stabilizing forkhead box M1
    • Liu, J., S. Guo, Q. Li, L. Yang, Z. Xia, L. Zhang, Z. Huang, and N. Zhang. 2013. Phosphoglycerate dehydrogenase induces glioma cells proliferation and invasion by stabilizing forkhead box M1. J. Neurooncol. 111:245-255. http://dx.doi.org/10.1007/s11060-012-1018-x
    • (2013) J. Neurooncol , vol.111 , pp. 245-255
    • Liu, J.1    Guo, S.2    Li, Q.3    Yang, L.4    Xia, Z.5    Zhang, L.6    Huang, Z.7    Zhang, N.8
  • 46
    • 84881177291 scopus 로고    scopus 로고
    • Serine, glycine and one-carbon units: Cancer metabolism in full circle
    • Locasale, J.W. 2013. Serine, glycine and one-carbon units: Cancer metabolism in full circle. Nat. Rev. Cancer. 13:572-583. http://dx.doi.org/10.1038/nrc3557.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 572-583
    • Locasale, J.W.1
  • 48
    • 80054046029 scopus 로고    scopus 로고
    • Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation
    • Lunt, S.Y., and M.G. Vander Heiden. 2011. Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation. Annu. Rev. Cell Dev. Biol. 27:441-464. http://dx.doi.org/10.1146/annurev-cellbio-092910-154237.
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 441-464
    • Lunt, S.Y.1    Vander Heiden, M.G.2
  • 50
    • 84872905650 scopus 로고    scopus 로고
    • Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells
    • Maddocks, O.D., C.R. Berkers, S.M. Mason, L. Zheng, K. Blyth, E. Gottlieb, and K.H. Vousden. 2013. Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells. Nature. 493:542-546. http://dx.doi.org/10.1038/nature11743.
    • (2013) Nature , vol.493 , pp. 542-546
    • Maddocks, O.D.1    Berkers, C.R.2    Mason, S.M.3    Zheng, L.4    Blyth, K.5    Gottlieb, E.6    Vousden, K.H.7
  • 51
    • 84957427247 scopus 로고    scopus 로고
    • Serine metabolism supports the methionine cycle and DNA/RNA methylation through de novo ATP synthesis in cancer cells
    • Maddocks, O.D., C.F. Labuschagne, P.D. Adams, and K.H. Vousden. 2016. Serine metabolism supports the methionine cycle and DNA/RNA methylation through de novo ATP synthesis in cancer cells. Mol. Cell. 61:210-221. http://dx.doi.org/10.1016/j.molcel.2015.12.014.
    • (2016) Mol. Cell , vol.61 , pp. 210-221
    • Maddocks, O.D.1    Labuschagne, C.F.2    Adams, P.D.3    Vousden, K.H.4
  • 52
    • 84948117747 scopus 로고    scopus 로고
    • An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation
    • Mattaini, K.R., E.J. Brignole, M. Kini, S.M. Davidson, B.P. Fiske, C.L. Drennan, and M.G. Vander Heiden. 2015. An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation. Cancer Metab. 3:5. http://dx.doi.org/10.1186/s40170-015-0131-7.
    • (2015) Cancer Metab , vol.3 , pp. 5
    • Mattaini, K.R.1    Brignole, E.J.2    Kini, M.3    Davidson, S.M.4    Fiske, B.P.5    Drennan, C.L.6    Vander Heiden, M.G.7
  • 53
    • 84923186422 scopus 로고    scopus 로고
    • Famine versus feast: Understanding the metabolism of tumors in vivo
    • Mayers, J.R., and M.G. Vander Heiden. 2015. Famine versus feast: Understanding the metabolism of tumors in vivo. Trends Biochem. Sci. 40:130-140. http://dx.doi.org/10.1016/j.tibs.2015.01.004.
    • (2015) Trends Biochem. Sci , vol.40 , pp. 130-140
    • Mayers, J.R.1    Vander Heiden, M.G.2
  • 56
    • 0034854417 scopus 로고    scopus 로고
    • ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini
    • Muthuswamy, S.K., D. Li, S. Lelievre, M.J. Bissell, and J.S. Brugge. 2001. ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini. Nat. Cell Biol. 3:785-792. http://dx.doi.org/10.1038/ncb0901-785.
    • (2001) Nat. Cell Biol , vol.3 , pp. 785-792
    • Muthuswamy, S.K.1    Li, D.2    Lelievre, S.3    Bissell, M.J.4    Brugge, J.S.5
  • 57
    • 84859261025 scopus 로고    scopus 로고
    • Mouse genetics suggests cell-context dependency for Myc-regulated metabolic enzymes during tumorigenesis
    • Nilsson, L.M., T.Z. Forshell, S. Rimpi, C. Kreutzer, W. Pretsch, G.W. Bornkamm, and J.A. Nilsson. 2012. Mouse genetics suggests cell-context dependency for Myc-regulated metabolic enzymes during tumorigenesis. PLoS Genet. 8:e1002573. http://dx.doi.org/10.1371/journal.pgen.1002573.
    • (2012) PLoS Genet , vol.8
    • Nilsson, L.M.1    Forshell, T.Z.2    Rimpi, S.3    Kreutzer, C.4    Pretsch, W.5    Bornkamm, G.W.6    Nilsson, J.A.7
  • 62
    • 0000008924 scopus 로고
    • The pathway and control of serine biosynthesis in Escherichia coli
    • Pizer, L.I. 1963. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238:3934-3944.
    • (1963) J. Biol. Chem , vol.238 , pp. 3934-3944
    • Pizer, L.I.1
  • 65
    • 84913285138 scopus 로고
    • Evidence for a specific alanine-hydroxypyruvic transaminase
    • W.D. McElroy, and B. Glass, editors. Johns Hopkins, Baltimore
    • Sallach, H.J. 1955. Evidence for a specific alanine-hydroxypyruvic transaminase. In Amino Acid Metabolism. W.D. McElroy, and B. Glass, editors. Johns Hopkins, Baltimore. 782-796.
    • (1955) Amino Acid Metabolism , pp. 782-796
    • Sallach, H.J.1
  • 67
    • 0021191196 scopus 로고
    • Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
    • Snell, K. 1984. Enzymes of serine metabolism in normal, developing and neoplastic rat tissues. Adv. Enzyme Regul. 22:325-400. http://dx.doi.org/10.1016/0065-2571(84)90021-9.
    • (1984) Adv. Enzyme Regul , vol.22 , pp. 325-400
    • Snell, K.1
  • 68
    • 0022643088 scopus 로고
    • Enzymic imbalance in serine metabolism in rat hepatomas
    • Snell, K., and G. Weber. 1986. Enzymic imbalance in serine metabolism in rat hepatomas. Biochem. J. 233:617-620. http://dx.doi.org/10.1042/bj2330617.
    • (1986) Biochem. J , vol.233 , pp. 617-620
    • Snell, K.1    Weber, G.2
  • 69
    • 0023655502 scopus 로고
    • The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture
    • Snell, K., Y. Natsumeda, and G. Weber. 1987. The modulation of serine metabolism in hepatoma 3924A during different phases of cellular proliferation in culture. Biochem. J. 245:609-612. http://dx.doi.org/10.1042/bj2450609.
    • (1987) Biochem. J , vol.245 , pp. 609-612
    • Snell, K.1    Natsumeda, Y.2    Weber, G.3
  • 70
    • 0014164744 scopus 로고
    • A view of the comparison of the regulation of enzymes in mammalian and microbial systems
    • Suda, M. 1967. A view of the comparison of the regulation of enzymes in mammalian and microbial systems. Adv. Enzyme Regul. 5:181-209. http://dx.doi.org/10.1016/0065-2571(67)90016-7.
    • (1967) Adv. Enzyme Regul , vol.5 , pp. 181-209
    • Suda, M.1
  • 71
    • 84938234308 scopus 로고    scopus 로고
    • Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells
    • Sullivan, L.B., D.Y. Gui, A.M. Hosios, L.N. Bush, E. Freinkman, and M.G. Vander Heiden. 2015. Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells. Cell. 162:552-563. http://dx.doi.org/10.1016/j.cell.2015.07.017.
    • (2015) Cell , vol.162 , pp. 552-563
    • Sullivan, L.B.1    Gui, D.Y.2    Hosios, A.M.3    Bush, L.N.4    Freinkman, E.5    Vander Heiden, M.G.6
  • 72
    • 77955616558 scopus 로고    scopus 로고
    • Compartmentalization of mammalian folate-mediated one-carbon metabolism
    • Tibbetts, A.S., and D.R. Appling. 2010. Compartmentalization of mammalian folate-mediated one-carbon metabolism. Annu. Rev. Nutr. 30:57-81. http://dx.doi.org/10.1146/annurev.nutr.012809.104810.
    • (2010) Annu. Rev. Nutr , vol.30 , pp. 57-81
    • Tibbetts, A.S.1    Appling, D.R.2
  • 73
    • 50549185131 scopus 로고
    • The biosynthetic pathway of serine in Salmonella typhimurium
    • Umbarger, H.E., and M.A. Umbarger. 1962. The biosynthetic pathway of serine in Salmonella typhimurium. Biochim. Biophys. Acta. 62:193-195. http://dx.doi.org/10.1016/0006-3002(62)90515-2.
    • (1962) Biochim. Biophys. Acta , vol.62 , pp. 193-195
    • Umbarger, H.E.1    Umbarger, M.A.2
  • 75
    • 80052242132 scopus 로고    scopus 로고
    • Targeting cancer metabolism: A therapeutic window opens
    • Vander Heiden, M.G. 2011. Targeting cancer metabolism: A therapeutic window opens. Nat. Rev. Drug Discov. 10:671-684. http://dx.doi.org/10.1038/nrd3504.
    • (2011) Nat. Rev. Drug Discov , vol.10 , pp. 671-684
    • Vander Heiden, M.G.1
  • 76
    • 77649305610 scopus 로고    scopus 로고
    • The common feature of leukemia-associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting a-ketoglutarate to 2-hydroxyglutarate
    • Ward, P.S., J. Patel, D.R. Wise, O. Abdel-Wahab, B.D. Bennett, H.A. Coller, J.R. Cross, V.R. Fantin, C.V. Hedvat, A.E. Perl, et al. 2010. The common feature of leukemia-associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting a-ketoglutarate to 2-hydroxyglutarate. Cancer Cell. 17:225-234. http://dx.doi.org/10.1016/j.ccr.2010.01.020.
    • (2010) Cancer Cell , vol.17 , pp. 225-234
    • Ward, P.S.1    Patel, J.2    Wise, D.R.3    Abdel-Wahab, O.4    Bennett, B.D.5    Coller, H.A.6    Cross, J.R.7    Fantin, V.R.8    Hedvat, C.V.9    Perl, A.E.10
  • 77
    • 84885357137 scopus 로고    scopus 로고
    • Exploiting the bad eating habits of Ras-driven cancers
    • White, E. 2013. Exploiting the bad eating habits of Ras-driven cancers. Genes Dev. 27:2065-2071. http://dx.doi.org/10.1101/gad.228122.113.
    • (2013) Genes Dev , vol.27 , pp. 2065-2071
    • White, E.1
  • 78
    • 84860793042 scopus 로고    scopus 로고
    • Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation
    • Ye, J., A. Mancuso, X. Tong, P.S. Ward, J. Fan, J.D. Rabinowitz, and C.B. Thompson. 2012. Pyruvate kinase M2 promotes de novo serine synthesis to sustain mTORC1 activity and cell proliferation. Proc. Natl. Acad. Sci. USA. 109:6904-6909. http://dx.doi.org/10.1073/pnas.1204176109.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6904-6909
    • Ye, J.1    Mancuso, A.2    Tong, X.3    Ward, P.S.4    Fan, J.5    Rabinowitz, J.D.6    Thompson, C.B.7
  • 80
    • 9144270452 scopus 로고    scopus 로고
    • Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase gene causes severe neurodevelopmental defects and results in embryonic lethality
    • Yoshida, K., S. Furuya, S. Osuka, J. Mitoma, Y. Shinoda, M. Watanabe, N. Azuma, H. Tanaka, T. Hashikawa, S. Itohara, and Y. Hirabayashi. 2004. Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase gene causes severe neurodevelopmental defects and results in embryonic lethality. J. Biol. Chem. 279:3573-3577. http://dx.doi.org/10.1074/jbc.C300507200.
    • (2004) J. Biol. Chem , vol.279 , pp. 3573-3577
    • Yoshida, K.1    Furuya, S.2    Osuka, S.3    Mitoma, J.4    Shinoda, Y.5    Watanabe, M.6    Azuma, N.7    Tanaka, H.8    Hashikawa, T.9    Itohara, S.10    Hirabayashi, Y.11
  • 81
    • 0029671184 scopus 로고    scopus 로고
    • A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria
    • Zhao, G., and M.E. Winkler. 1996. A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178:232-239.
    • (1996) J. Bacteriol , vol.178 , pp. 232-239
    • Zhao, G.1    Winkler, M.E.2
  • 82
    • 84919797513 scopus 로고    scopus 로고
    • Phosphoglycerate dehydrogenase: Potential therapeutic target and putative metabolic oncogene
    • Zogg, C.K. 2014. Phosphoglycerate dehydrogenase: Potential therapeutic target and putative metabolic oncogene. J. Oncol. 2014:524101. http://dx.doi.org/10.1155/2014/524101.
    • (2014) J. Oncol , vol.2014
    • Zogg, C.K.1


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