The B55α Subunit of PP2A Drives a p53-Dependent Metabolic Adaptation to Glutamine Deprivation

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works

The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation

DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088 · see citing works

Beyond aerobic glycolysis: transformed cells can engage in glutamine metabolism that exceeds the requirement for protein and nucleotide synthesis

DeBerardinis, R. J., Mancuso, A., Daikhin, E., Nissim, I., Yudkoff, M., Wehrli, S., & Thompson, C. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709747104 · Cited by 2,622 · see citing works

c-Myc suppression of miR-23a/b enhances mitochondrial glutaminase expression and glutamine metabolism

Gao, P., Tchernyshyov, I., Chang, T.-C., Lee, Y.-S., Kita, K., Ochi, T., Zeller, K. I., De Marzo, A. M., Van Eyk, J. E., Mendell, J. T., et al. (2009) · Nature · doi:10.1038/nature07823 · Cited by 2,124 · see citing works

Myc regulates a transcriptional program that stimulates mitochondrial glutaminolysis and leads to glutamine addiction

Wise, D. R., DeBerardinis, R. J., Mancuso, A., Sayed, N., Zhang, X.-Y., Pfeiffer, H. K., Nissim, I., Daikhin, E., Yudkoff, M., McMahon, S. B., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810199105 · Cited by 2,001 · see citing works

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,890 · see citing works

AMP-activated protein kinase induces a p53-dependent metabolic checkpoint

Jones, R. G., Plas, D. R., Kubek, S., Buzzai, M., Mu, J., Xu, Y., Birnbaum, M. J., & Thompson, C. B. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.03.027 · Cited by 1,619 · see citing works

Glucose-Independent Glutamine Metabolism via TCA Cycling for Proliferation and Survival in B Cells

Le, A., Lane, A. N., Hamaker, M., Bose, S., Gouw, A., Barbi, J., Tsukamoto, T., Rojas, C. J., Slusher, B. S., Zhang, H., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.12.009 · Cited by 1,095 · see citing works

Tumor suppressors and cell metabolism: a recipe for cancer growth

Jones, R. G., & Thompson, C. B. (2009) · Genes & Development · doi:10.1101/gad.1756509 · Cited by 1,085 · see citing works

The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors

Beck, T., & Hall, M. (1999) · Nature · doi:10.1038/45287 · Cited by 990 · see citing works

Systemic Treatment with the Antidiabetic Drug Metformin Selectively Impairs p53-Deficient Tumor Cell Growth

Buzzai, M., Jones, R. G., Amaravadi, R. K., Lum, J. J., DeBerardinis, R. J., Zhao, F., Viollet, B., & Thompson, C. B. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4447 · Cited by 923 · see citing works

Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function

Hu, W., Zhang, C., Wu, R., Sun, Y., Levine, A., & Feng, Z. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001006107 · Cited by 862 · see citing works

Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation

Owusu-Ansah, E., & Banerjee, U. (2009) · Nature · doi:10.1038/nature08313 · Cited by 742 · see citing works

The metabolic profile of tumors depends on both the responsible genetic lesion and tissue type

Yuneva, M. O., Fan, T. W. M., Allen, T. D., Higashi, R. M., Ferraris, D. V., Tsukamoto, T., Matés, J. M., Alonso, F. J., Wang, C., Seo, Y., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.12.015 · Cited by 639 · see citing works

Taking a good look at free radicals in the aging process

Hekimi, S., Lapointe, J., & Wen, Y. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.008 · Cited by 606 · see citing works

Metabolic regulation by p53

Maddocks, O. D. K., & Vousden, K. H. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0735-5 · Cited by 359 · see citing works

Deconstructing p53 transcriptional networks in tumor suppression

Bieging, K. T., & Attardi, L. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.006 · Cited by 194 · see citing works

ROS-Mediated p53 Induction of Lpin1 Regulates Fatty Acid Oxidation in Response to Nutritional Stress

Assaily, W., Rubinger, D. A., Wheaton, K., Lin, Y., Ma, W., Xuan, W., Brown‐Endres, L., Tsuchihara, K., Mak, T. W., & Benchimol, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.038 · Cited by 192 · see citing works

Glutamine: pleiotropic roles in tumor growth and stress resistance

Shanware, N. P., Mullen, A. R., DeBerardinis, R. J., & Abraham, R. T. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0731-9 · Cited by 176 · see citing works

PGC-1α, a Key Modulator of p53, Promotes Cell Survival upon Metabolic Stress

Sen, N., Satija, Y. K., & Das, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.044 · Cited by 164 · see citing works

α4 Is an Essential Regulator of PP2A Phosphatase Activity

Kong, M., Ditsworth, D., Lindsten, T., & Thompson, C. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.025 · Cited by 162 · see citing works

The PP2A-Associated Protein α4 Is an Essential Inhibitor of Apoptosis

Kong, M., Fox, C. J., Mu, J., Solt, L., Xu, A., Cinalli, R. M., Birnbaum, M. J., Lindsten, T., & Thompson, C. B. (2004) · Science · doi:10.1126/science.1100537 · Cited by 149 · see citing works

Free amino acids in normal and neoplastic tissues of mice as studied by paper chromatography.

Roberts, E., & Frankel, S. (1949) · PubMed · Cited by 87 · see citing works

Increased Levels of Hydrogen Peroxide Induce a HIF-1-dependent Modification of Lipid Metabolism in AMPK Compromised C. elegans Dauer Larvae

Xie, M., & Roy, R. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.016 · Cited by 76 · see citing works

Saccharomyces cerevisiae Sit4 Phosphatase Is Active Irrespective of the Nitrogen Source Provided, and Gln3 Phosphorylation Levels Become Nitrogen Source-responsive in a sit4-deleted Strain

Tate, J. J., Feller, A., Dubois, E. L., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606973200 · Cited by 53 · see citing works

EDD Inhibits ATM-mediated Phosphorylation of p53

Ling, S., & Lin, W.-C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182527 · Cited by 44 · see citing works

α4 is highly expressed in carcinogen-transformed human cells and primary human cancers

Chen, L.-P., Lai, Y.-D., Li, D.-C., Zhu, X.-N., Yang, P., Li, W., Zhu, W., Zhao, J., Li, X.-D., Xiao, Y.-M., et al. (2011) · Oncogene · doi:10.1038/onc.2011.20 · Cited by 43 · see citing works

EDD induces cell cycle arrest by increasing p53 levels

Smits, V. A. J. (2012) · Cell Cycle · doi:10.4161/cc.11.4.19154 · Cited by 35 · see citing works

Intranuclear Function for Protein Phosphatase 2A: Pph21 and Pph22 Are Required for Rapamycin-Induced GATA Factor Binding to the DAL5 Promoter in Yeast

Georis, I., Tate, J. J., Feller, A., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00482-10 · Cited by 22 · see citing works

Identification of phosphorylation sites on the E3 ubiquitin ligase UBR5/EDD

Bethard, J. R., Zheng, H., Roberts, L. L., & Eblen, S. T. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.08.023 · Cited by 10 · see citing works

P53 in survival, death and metabolic health: a lifeguard with a licence to kill.

Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080 · see citing works

Glutamine reliance in cell metabolism

Yoo, H. C., Yu, Y. C., Sung, Y., & Han, J. M. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00504-8 · Cited by 1,021 · see citing works

Regulation of cancer cell metabolism: Oncogenic MYC in the driver’s seat

Dong, Y., Tu, R., Liu, H., & Qing, G. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00235-2 · Cited by 405 · see citing works

Regional glutamine deficiency in tumours promotes dedifferentiation through inhibition of histone demethylation

Pan, M., Reid, M. A., Lowman, X. H., Kulkarni, R. P., Tran, T. Q., Liu, X., Yang, Y., Hernandez-Davies, J. E., Rosales, K. K., Li, H., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3410 · Cited by 368 · see citing works

MYC and tumor metabolism: chicken and egg

Dejure, F. R., & Eilers, M. (2017) · The EMBO Journal · doi:10.15252/embj.201796438 · Cited by 240 · see citing works

Regulation of autophagy by coordinated action of mTORC1 and protein phosphatase 2A

Wong, P.-M., Feng, Y., Wang, J., Shi, R., & Jiang, X. (2015) · Nature Communications · doi:10.1038/ncomms9048 · Cited by 239 · see citing works

A Role for p53 in the Adaptation to Glutamine Starvation through the Expression of SLC1A3

Tajan, M., Hock, A. K., Blagih, J., Robertson, N. A., Labuschagne, C. F., Kruiswijk, F., Humpton, T. J., Adams, P. D., & Vousden, K. H. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.005 · Cited by 230 · see citing works

Targeting Glutamine Induces Apoptosis: A Cancer Therapy Approach

Chen, L., & Cui, H. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160922830 · Cited by 184 · see citing works

α-Ketoglutarate attenuates Wnt signaling and drives differentiation in colorectal cancer

Tran, T. Q., Hanse, E. A., Habowski, A. N., Li, H., Ishak Gabra, M. B., Yang, Y., Lowman, X. H., Ooi, A. M., Liao, S. Y., Edwards, R. A., et al. (2020) · Nature Cancer · doi:10.1038/s43018-020-0035-5 · Cited by 161 · see citing works

The role of tumor suppressor p53 in the antioxidant defense and metabolism

Budanov, A. V. (2014) · Subcellular Biochemistry · doi:10.1007/978-94-017-9211-0_18 · Cited by 157 · see citing works

The broken “Off” switch in cancer signaling: PP2A as a regulator of tumorigenesis, drug resistance, and immune surveillance

Ruvolo, P. P. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.08.002 · Cited by 143 · see citing works

Alternative fuels for cancer cells

Keenan, M. M., & Chi, J.-T. (2015) · The Cancer Journal · doi:10.1097/ppo.0000000000000104 · Cited by 131 · see citing works

Tumor suppressive protein phosphatases in human cancer: Emerging targets for therapeutic intervention and tumor stratification

Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works

Myc promotes glutaminolysis in human neuroblastoma through direct activation of glutaminase 2

Xiao, D., Ren, P., Su, H., Yue, M., Xiu, R., Hu, Y., Liu, H., & Qing, G. (2015) · Oncotarget · doi:10.18632/oncotarget.5821 · Cited by 80 · see citing works

Eukaryotic elongation factor-2 kinase (eEF2K) signaling in tumor and microenvironment as a novel molecular target

Karakas, D., & Ozpolat, B. (2020) · Journal of Molecular Medicine · doi:10.1007/s00109-020-01917-8 · Cited by 54 · see citing works

A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment

Wang, X., Garvanska, D. H., Nasa, I., Ueki, Y., Zhang, G., Kettenbach, A. N., Peti, W., Nilsson, J., & Page, R. (2020) · eLife · doi:10.7554/elife.55966 · Cited by 53 · see citing works

The B55α Regulatory Subunit of Protein Phosphatase 2A Mediates Fibroblast Growth Factor-Induced p107 Dephosphorylation and Growth Arrest in Chondrocytes

Kolupaeva, V., Daempfling, L., & Basilico, C. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01730-12 · Cited by 37 · see citing works

Protein phosphatase 2A regulatory subunit B55α functions in mouse oocyte maturation and early embryonic development

Liang, S., Guo, J., Choi, J.-W., Shin, K.-T., Wang, H.-Y., Jo, Y.-J., Kim, N.-H., & Cui, X.-S. (2017) · Oncotarget · doi:10.18632/oncotarget.15927 · Cited by 20 · see citing works

Measuring the Activities of Two-Component Regulatory System Phosphatases

Bourret, R. B., & Silversmith, R. E. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.05.006 · Cited by 3 · see citing works

Faculty Opinions recommendation of Galpha12 directly interacts with PP2A: evidence FOR Galpha12-stimulated PP2A phosphatase activity and dephosphorylation of microtubule-associated protein, tau.

Dhanasekaran, D. N. (2005) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1023160.264844

A specific PP2A regulatory subunit, B56γ, mediates DNA damage‐induced dephosphorylation of p53 at Thr55

Li, H., Cai, X., Shouse, G., Piluso, L. G., & Liu, X. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601519 · Cited by 159 · see citing works

Dephosphorylation of the deinhibitor protein by the PCSH protein phosphatase

Goris, J., Waelkens, E., & Merlevede, W. J. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)80384-7 · Cited by 10 · see citing works

The protein phosphatases involved in cellular regulation. Identification of the inhibitor-2 phosphatases in rabbit skeletal muscle

Tonks, N. K., & Cohen, P. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08522.x · Cited by 331 · see citing works