In vivo regulation of monomer-tetramer conversion of pyruvate kinase subtype M2 by glucose is mediated via fructose 1,6-bisphosphate

Methods of Enzymatic Analysis

(1974) · Elsevier eBooks · doi:10.1016/b978-0-12-091304-6.x5001-0 · Cited by 6,786 · see citing works

HORMONAL REGULATION OF MAMMALIAN GLUCOSE TRANSPORT

Simpson, I. A., & Cushman, S. W. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.005211 · Cited by 398 · see citing works

[25] Pyruvate kinase isozymes from rat

Imamura, K., & Tanaka, T. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(82)90121-5 · Cited by 142 · see citing works

An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1,6-bisphosphate

Ashizawa, K., McPhie, P., Lin, K., & Cheng, S. Y. (1991) · Biochemistry · doi:10.1021/bi00243a010 · Cited by 101 · see citing works

Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase.

Kato, H., Fukuda, T., Parkison, C., McPhie, P., & Cheng, S.-Y. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7861 · Cited by 99 · see citing works

Hormone and DNA binding activity of a purified human thyroid hormone nuclear receptor expressed in Escherichia coli.

Lin, K., Fukuda, T., & Cheng, S.-Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34100-6 · Cited by 56 · see citing works

Characterization of a membrane-associated 3,3',5-triiodo-L-thyronine binding protein by use of monoclonal antibodies

HASUMURA, S., Kitagawa, S., Lovelace, E., Willingham, M. C., Pastan, I. H., & Cheng, S.-Y. (1986) · Biochemistry · doi:10.1021/bi00372a014 · Cited by 41 · see citing works

A cellular 3,3',5-triiodo-L-thyronine binding protein from a human carcinoma cell line. Purification and characterization.

Kitagawa, S., Obata, T., HASUMURA, S., Pastan, I. H., & Cheng, S.-Y. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61442-5 · Cited by 35 · see citing works

A cytoplasmic thyroid hormone binding protein: characterization using monoclonal antibodies

Obata, T., Fukuda, T., Willingham, M. C., Liang, C., & Cheng, S. Y. (1989) · Biochemistry · doi:10.1021/bi00428a030 · Cited by 15 · see citing works

Regulation of thyroid hormone binding to its cytosolic binding protein by L-α-alanine

Ashizawa, K., Kato, H., McPhie, P., & Cheng, S.-Y. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(90)92065-8 · Cited by 10 · see citing works

The nucleotide sequence of a full length cDNA encoding rat pituitary pyruvate kinase

Parkison, C., Kato, H., & Cheng, S.-Y. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.17.7106 · Cited by 5 · see citing works

Antibodies against the human cellular 3,3′,5‐triiodo‐L‐thyronine‐binding protein (p58)

Obata, T., Fukuda, T., & Cheng, S. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80630-6 · Cited by 4 · see citing works

Metabolic Reprogramming: A Cancer Hallmark Even Warburg Did Not Anticipate

Ward, P. S., & Thompson, C. B. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.02.014 · Cited by 3,233 · see citing works

Pyruvate kinase M2 regulates Hif-1α activity and IL-1β induction and is a critical determinant of the Warburg effect in LPS-activated macrophages

Palsson-McDermott, E. M., Curtis, A. M., Goel, G., Lauterbach, M. A. R., Sheedy, F. J., Gleeson, L. E., van den Bosch, M. W. M., Quinn, S. R., Domingo-Fernandez, R., Johnston, D. G. W., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2014.12.005 · Cited by 1,397 · see citing works

Regulation of pyruvate metabolism and human disease

Gray, L. R., Tompkins, S. C., & Taylor, E. B. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1539-2 · Cited by 951 · see citing works

Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis

Anastasiou, D., Yu, Y., Israelsen, W. J., Jiang, J.-K., Boxer, M. B., Hong, B. S., Tempel, W., Dimov, S., Shen, M., Jha, A., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1060 · Cited by 816 · see citing works

Pyruvate kinase type M2 and its role in tumor growth and spreading

Mazurek, S., Boschek, C. B., Hugo, F., & Eigenbrodt, E. (2005) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2005.04.009 · Cited by 812 · see citing works

Pyruvate Kinase M2 Regulates Gene Transcription by Acting as a Protein Kinase

Gao, X., Wang, H., Yang, J. J., Liu, X., & Liu, Z.-R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.001 · Cited by 772 · see citing works

Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells

Mazurek, S. (2011) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.02.005 · Cited by 694 · see citing works

Serine is a natural ligand and allosteric activator of pyruvate kinase M2

Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., et al. (2012) · Nature · doi:10.1038/nature11540 · Cited by 661 · see citing works

PKM2, function and expression and regulation

Zhang, Z., Deng, X., Liu, Y., Liu, Y., Sun, L., & Chen, F. (2019) · Cell & Bioscience · doi:10.1186/s13578-019-0317-8 · Cited by 504 · see citing works

Evolution of glycolysis

Fothergill‐Gilmore, L. A., & Michels, P. A. M. (1993) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(93)90001-z · Cited by 458 · see citing works

Structural Basis for Tumor Pyruvate Kinase M2 Allosteric Regulation and Catalysis ,

Dombrauckas, J. D., Santarsiero, B. D., & Mesecar, A. D. (2005) · Biochemistry · doi:10.1021/bi0474923 · Cited by 414 · see citing works

PKM2 contributes to cancer metabolism

Wong, N., Ojo, D., Yan, J., & Tang, D. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.01.031 · Cited by 348 · see citing works

Pyruvate kinase type M2 promotes tumour cell exosome release via phosphorylating synaptosome-associated protein 23

Wei, Y., Wang, D., Jin, F., Bian, Z., Li, L., Liang, H., Li, M., Shi, L., Pan, C., Zhu, D., et al. (2017) · Nature Communications · doi:10.1038/ncomms14041 · Cited by 311 · see citing works

Rocking cell metabolism: revised functions of the key glycolytic regulator PKM2 in cancer

Chaneton, B., & Gottlieb, E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.04.003 · Cited by 294 · see citing works

Modulation of type M 2 pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein

Zwerschke, W., Mazurek, S., Massimi, P., Banks, L., EIGENBRODT, E., & Jansen‐Dürr, P. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1291 · Cited by 257 · see citing works

PKM2, a Central Point of Regulation in Cancer Metabolism

Wong, N., Melo, J. D., & Tang, D. (2013) · International Journal of Cell Biology · doi:10.1155/2013/242513 · Cited by 243 · see citing works

Quinoline 3-sulfonamides inhibit lactate dehydrogenase A and reverse aerobic glycolysis in cancer cells

Billiard, J., Dennison, J. B., Briand, J., Annan, R. S., Chai, D., Colón, M., Dodson, C. S., Gilbert, S. A., Greshock, J. D., Jing, J., et al. (2013) · Cancer & Metabolism · doi:10.1186/2049-3002-1-19 · Cited by 242 · see citing works

Pyruvate Kinase M2: Multiple Faces for Conferring Benefits on Cancer Cells

Tamada, M., Suematsu, M., & Saya, H. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-0859 · Cited by 239 · see citing works

Pyruvate kinase M2-specific siRNA induces apoptosis and tumor regression

Goldberg, M. S., & Sharp, P. A. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111487 · Cited by 232 · see citing works

Metabolism of activated T lymphocytes

Maciolek, J. A., Pasternak, J. A., & Wilson, H. L. (2014) · Current Opinion in Immunology · doi:10.1016/j.coi.2014.01.006 · Cited by 224 · see citing works

Cancer metabolism in space and time: Beyond the Warburg effect

Danhier, P., Bański, P., Payen, V. L., Grasso, D., Ippolito, L., Sonveaux, P., & Porporato, P. E. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.02.001 · Cited by 214 · see citing works

Targeting Protein-Protein Interaction by Small Molecules

Jin, L., Wang, W., & Fang, G. (2014) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-140028 · Cited by 195 · see citing works

Small 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

Diverting Glycolysis to Combat Oxidative Stress

Mullarky, E., & Cantley, L. C. (2015) · Springer eBooks · doi:10.1007/978-4-431-55651-0_1 · Cited by 189 · see citing works

Pyruvate kinase M2 and cancer: an updated assessment

Iqbal, M. A., Gupta, V., Prakasam, G., Mazurek, S., & Bamezai, R. N. K. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.011 · Cited by 189 · see citing works

An overview of structure, function, and regulation of pyruvate kinases

Schormann, N., Hayden, K. L., Lee, P. Y. K., Banerjee, S., & Chattopadhyay, D. (2019) · Protein Science · doi:10.1002/pro.3691 · Cited by 187 · see citing works

M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation

Morgan, H. P., O’Reilly, F. J., Wear, M. A., O’Neill, J. R., Fothergill‐Gilmore, L. A., Hupp, T. R., & Walkinshaw, M. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217157110 · Cited by 180 · see citing works

The multifaceted regulation and functions of PKM2 in tumor progression

Li, Z., Yang, P., & Li, Z. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.07.008 · Cited by 175 · see citing works

Cancer Metabolism and Drug Resistance

Rahman, M., & Hasan, M. R. (2015) · Metabolites · doi:10.3390/metabo5040571 · Cited by 168 · see citing works

Posttranslational Modifications of Pyruvate Kinase M2: Tweaks that Benefit Cancer

Prakasam, G., Iqbal, M. A., Bamezai, R. N. K., & Mazurek, S. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00022 · Cited by 153 · see citing works

Aerobic Glycolysis by Proliferating Cells: Protection against Oxidative Stress at the Expense of Energy Yield

Brand, K. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022498714522 · Cited by 153 · see citing works

The Role of Phosphometabolites in Cell Proliferation, Energy Metabolism, and Tumor Therapy

Mazurek, S., Boschek, C. B., & EIGENBRODT, E. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022490512705 · Cited by 147 · see citing works

Nuclear localization of soluble CTP:phosphocholine cytidylyltransferase.

Wang, Y., Sweitzer, T. D., Weinhold, P. A., & Kent, C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53405-0 · Cited by 142 · see citing works

Understanding the Central Role of Citrate in the Metabolism of Cancer Cells and Tumors: An Update

Icard, P., Coquerel, A., Wu, Z., Gligorov, J., Fuks, D., Fournel, L., Lincet, H., & Simula, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126587 · Cited by 139 · see citing works

Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

Gui, D. Y., Lewis, C. A., & Heiden, M. G. V. (2013) · Science Signaling · doi:10.1126/scisignal.2003925 · Cited by 122 · see citing works

p73 regulates serine biosynthesis in cancer

Amelio, I., Markert, E. K., Rufini, A., Antonov, A. V., Sayan, B. S., Tucci, P., Agostini, M., Mineo, T. C., Levine, A. J., & Melino, G. (2013) · Oncogene · doi:10.1038/onc.2013.456 · Cited by 121 · see citing works

Three rounds (1R/2R/3R) of genome duplications and the evolution of the glycolytic pathway in vertebrates

Steinke, D., Hoegg, S., Brinkmann, H., & Meyer, A. (2006) · BMC Biology · doi:10.1186/1741-7007-4-16 · Cited by 122 · see citing works

Parkin Regulates the Activity of Pyruvate Kinase M2

Liu, K., Li, F., Han, H., Chen, Y., Mao, Z., Luo, J., Zhao, Y., Zheng, B., Gu, W. J., & Zhao, W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.703066 · Cited by 120 · see citing works

Hallmarks of Pulmonary Hypertension: Mesenchymal and Inflammatory Cell Metabolic Reprogramming

D’Alessandro, A., Kasmi, K. C. E., Plecitá‐Hlavatá, L., Ježek, P., Li, M., Zhang, H., Gupte, S. A., & Stenmark, K. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7217 · Cited by 110 · see citing works

The PKM2 activator TEPP‐46 suppresses kidney fibrosis via inhibition of the EMT program and aberrant glycolysis associated with suppression of HIF‐1α accumulation

Liu, H., Takagaki, Y., Kumagai, A., Kanasaki, K., & Koya, D. (2020) · Journal of Diabetes Investigation · doi:10.1111/jdi.13478 · Cited by 104 · see citing works

Effect of Extracellular AMP on Cell Proliferation and Metabolism of Breast Cancer Cell Lines with High and Low Glycolytic Rates

Mazurek, S., Michel, A., & EIGENBRODT, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.8.4941 · Cited by 105 · see citing works

Using the yeast two‐hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth

Williams, J. M., Chen, G. C., Zhu, L., & Rest, R. F. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00670.x · Cited by 103 · see citing works

Oncogenic Kinase–Induced PKM2 Tyrosine 105 Phosphorylation Converts Nononcogenic PKM2 to a Tumor Promoter and Induces Cancer Stem–like Cells

Zhou, Z., Li, M., Zhang, L., Zhao, H., Şahin, Ö., Chen, J., Zhao, J. J., Songyang, Z., & Yu, D. (2018) · Cancer Research · doi:10.1158/0008-5472.can-17-2726 · Cited by 102 · see citing works

Fascin promotes lung cancer growth and metastasis by enhancing glycolysis and PFKFB3 expression

Lin, S., Li, Y., Wang, D., Huang, C., Marino, D., Bollt, O., Wu, C., Taylor, M. D., Li, W., DeNicola, G. M., et al. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.07.025 · Cited by 99 · see citing works

The Pancreatic β-Cell: A Bioenergetic Perspective

Nicholls, D. G. (2016) · Physiological Reviews · doi:10.1152/physrev.00009.2016 · Cited by 95 · see citing works

Glucose Catabolism in Liver Tumors Induced by c-MYC Can Be Sustained by Various PKM1/PKM2 Ratios and Pyruvate Kinase Activities

Méndez‐Lucas, A., Li, X., Hu, J., Che, L., Song, X., Jia, J., Wang, J., Xie, C., Driscoll, P. C., Tschaharganeh, D. F., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0498 · Cited by 89 · see citing works

The Trypanocidal Drug Suramin and Other Trypan Blue Mimetics Are Inhibitors of Pyruvate Kinases and Bind to the Adenosine Site

Morgan, H. P., McNae, I. W., Nowicki, M. W., Zhong, W., Michels, P. A. M., Auld, D. S., Fothergill‐Gilmore, L. A., & Walkinshaw, M. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.212613 · Cited by 84 · see citing works

Direct Measurements of Oscillatory Glycolysis in Pancreatic Islet β-Cells Using Novel Fluorescence Resonance Energy Transfer (FRET) Biosensors for Pyruvate Kinase M2 Activity

Merrins, M. J., Dyke, A. R. V., Mapp, A. K., Rizzo, M. A., & Satin, L. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.508127 · Cited by 80 · see citing works

Lapachol inhibits glycolysis in cancer cells by targeting pyruvate kinase M2

Babu, M. S., Mahanta, S. K., Lakhter, A. J., Hato, T., Paul, S., & Naidu, S. R. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191419 · Cited by 80 · see citing works

Isotype‐specific inhibitors of the glycolytic key regulator pyruvate kinase subtype M2 moderately decelerate tumor cell proliferation

Spoden, G. A., Mazurek, S., Morandell, D., Bacher, N., Ausserlechner, M. J., Jansen‐Dürr, P., EIGENBRODT, E., & Zwerschke, W. (2008) · International Journal of Cancer · doi:10.1002/ijc.23512 · Cited by 79 · see citing works

Non-canonical functions of enzymes facilitate cross-talk between cell metabolic and regulatory pathways

Snaebjornsson, M. T., & Schulze, A. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0065-6 · Cited by 77 · see citing works

Multiple functions of pyruvate kinase M2 in various cell types

Lee, Y.-B., Min, J. K., Kim, J., Cap, K. C., Islam, R., Hossain, A. J., Dogsom, O., Hamza, A., Mahmud, S., Choi, D. R., et al. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30536 · Cited by 76 · see citing works

O-GlcNAcase targets pyruvate kinase M2 to regulate tumor growth

Singh, J. P., Qian, K., Lee, J.-S., Zhou, J., Han, X., Zhang, B., Ong, Q., Ni, W., Jiang, M., Ruan, H., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0975-3 · Cited by 77 · see citing works

Identification of anti-retinal antibodies in patients with age-related macular degeneration

Morohoshi, K., Ohbayashi, M., Patel, N., Chong, V. N., Bird, A. C., & Ono, S. J. (2012) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2012.03.007 · Cited by 77 · see citing works

Pyruvate Kinase Type M2: A Key Regulator Within the Tumour Metabolome and a Tool for Metabolic Profiling of Tumours

Mazurek, S. (2008) · Ernst Schering Research Foundation workshop/Ernst Schering Foundation Symposium proceedings · doi:10.1007/2789_2008_091 · Cited by 76 · see citing works

Pharmacologic Activation of PKM2 Slows Lung Tumor Xenograft Growth

Parnell, K. M., Foulks, J. M., Nix, R. N., Clifford, A., Bullough, J., LUO, B. H., Senina, A. V., Vollmer, D., Liu, J., McCarthy, V., et al. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0026 · Cited by 72 · see citing works

Human cytomegalovirus encoded chemokine receptor US28 activates the HIF-1α/PKM2 axis in glioblastoma cells

de Wit, R. H., Mujić-Delić, A., van Senten, J. R., Fraile‐Ramos, A., Siderius, M. H., & Smit, M. J. (2016) · Oncotarget · doi:10.18632/oncotarget.11817 · Cited by 67 · see citing works

Reciprocal Regulation of Protein Kinase and Pyruvate Kinase Activities of Pyruvate Kinase M2 by Growth Signals

Gao, X., Wang, H., Yang, J. J., Chen, J., Jie, J., Li, L., Zhang, Y., & Liu, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.448753 · Cited by 66 · see citing works

An allostatic mechanism for M2 pyruvate kinase as an amino-acid sensor

Yuan, M., McNae, I. W., Chen, Y., Blackburn, E. A., Wear, M. A., Michels, P. A. M., Fothergill‐Gilmore, L. A., Hupp, T. R., & Walkinshaw, M. D. (2018) · Biochemical Journal · doi:10.1042/bcj20180171 · Cited by 66 · see citing works

Pyruvate kinase isoform M2 impairs cognition in systemic lupus erythematosus by promoting microglial synaptic pruning via the β-catenin signaling pathway

Lu, L., Wang, H., Liu, X., Tan, L., Qiao, X., Ni, J., Sun, Y., Liang, J., Hou, Y., & Dou, H. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02279-9 · Cited by 63 · see citing works

Targeting Pyruvate Kinase M2 Phosphorylation Reverses Aggressive Cancer Phenotypes

Apostolidi, M., Vathiotis, I. A., Muthusamy, V., Gaule, P., Gassaway, B. M., Rimm, D. L., & Rinehart, J. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-4190 · Cited by 65 · see citing works

Mitochondrial GTP Links Nutrient Sensing to β Cell Health, Mitochondrial Morphology, and Insulin Secretion Independent of OxPhos

Jesinkey, S. R., Madiraju, A. K., Alves, T. C., Yarborough, O. H., CARDONE, R. L., Zhao, X., Parsaei, Y., Nasiri, A. R., Butrico, G. M., Liu, X., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.058 · Cited by 60 · see citing works

PKM2 inhibitor shikonin suppresses TPA‐induced mitochondrial malfunction and proliferation of skin epidermal JB6 cells

Li, W., Liu, J., & Zhao, Y. (2012) · Molecular Carcinogenesis · doi:10.1002/mc.21988 · Cited by 57 · see citing works

Regulation of glycolysis in brown adipocytes by HIF-1α

Basse, A. L., Isidor, M. S., Winther, S., Skjoldborg, N. B., Murholm, M., Andersen, E. S., Pedersen, S. B., Wolfrum, C., Quistorff, B., & Hansen, J. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-04246-y · Cited by 54 · see citing works

Conditional Epitopes: Is Your Antibody Always Specific?

Willingham, M. C. (1999) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549904701002 · Cited by 57 · see citing works

Activators of PKM2 in Cancer Metabolism

Warner, S. L., Carpenter, K. J., & Bearss, D. J. (2014) · Future Medicinal Chemistry · doi:10.4155/fmc.14.70 · Cited by 57 · see citing works

Pyruvate Kinase Inhibits Proliferation during Postnatal Cerebellar Neurogenesis and Suppresses Medulloblastoma Formation

Tech, K., Tikunov, A. P., Farooq, H., Morrissy, A. S., Meidinger, J., Fish, T., Green, S. C., Liu, H., Li, Y., Mungall, A. J. J., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-3304 · Cited by 52 · see citing works

Discovery of 3-(trifluoromethyl)-1H-pyrazole-5-carboxamide activators of the M2 isoform of pyruvate kinase (PKM2)

Xu, Y., Liu, X., Saunders, M., Pearce, S., Foulks, J. M., Parnell, K. M., Clifford, A., Nix, R. N., Bullough, J., Hendrickson, T. F., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.12.028 · Cited by 51 · see citing works

Regulation of thyroid hormone receptor-mediated transcription by a cytosol protein.

Ashizawa, K., & Cheng, S.-Y. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.19.9277 · Cited by 51 · see citing works

New pyridin-3-ylmethyl carbamodithioic esters activate pyruvate kinase M2 and potential anticancer lead compounds

Zhang, Y., Liu, B., Wu, X., Li, R., Ning, X., Liu, Y., Liu, Z., Ge, Z., Li, R., & Yin, Y. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.05.041 · Cited by 49 · see citing works

Functional cross-talk between allosteric effects of activating and inhibiting ligands underlies PKM2 regulation

Macpherson, J. A., Theisen, A., Masino, L., Fets, L., Driscoll, P. C., Encheva, V., Snijders, A. P., Martin, S. R., Kleinjung, J., Barran, P. E., et al. (2019) · eLife · doi:10.7554/elife.45068 · Cited by 48 · see citing works

Crystal Structure of a Complex of Escherichia coli Glycerol Kinase and an Allosteric Effector Fructose 1,6-Bisphosphate,

Ormö, M., Bystrom, C. E., & Remington, S. J. (1998) · Biochemistry · doi:10.1021/bi981616s · Cited by 47 · see citing works

Elevation of serum pyruvate kinase M2 (PKM2) in IBD and its relationship to IBD indices

Almousa, A. A., Morris, M. W., Fowler, S. A., Jones, J., & Alcorn, J. (2017) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2017.12.007 · Cited by 46 · see citing works

Energy Metabolism on Mitochondrial Maturation and Its Effects on Cardiomyocyte Cell Fate

Persad, K. L., & Lopaschuk, G. D. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.886393 · Cited by 47 · see citing works

The Genomes of Two Billfishes Provide Insights into the Evolution of Endothermy in Teleosts

Wu, B., Feng, C., Zhu, C., Xu, W., Yuan, Y., Hu, M., Yuan, K., Li, Y., Ren, Y., Zhou, Y., et al. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab035 · Cited by 42 · see citing works

In vitro effect of extracellular AMP on MCF‐7 breast cancer cells: Inhibition of glycolysis and cell proliferation

Hugo, F., Mazurek, S., Zander, U. C., & EIGENBRODT, E. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041530315 · Cited by 44 · see citing works

Pyruvate kinase M2 regulates mitochondrial homeostasis in cisplatin-induced acute kidney injury

Xie, W., He, Q., Zhang, Y., Xu, X., Wen, P., Cao, H., Zhou, Y., Luo, J., Yang, J., & Jiang, L. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06195-z · Cited by 44 · see citing works

Stress eating and tuning out: Cancer cells re-wire metabolism to counter stress

Stine, Z. E., & Dang, C. V. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.844093 · Cited by 43 · see citing works

Determining the quantitative relationship between glycolysis and GAPDH in cancer cells exhibiting the Warburg effect

Zhu, X., Jin, C., Pan, Q., & Hu, X. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100369 · Cited by 42 · see citing works

Ca 2+ Effects on ATP Production and Consumption Have Regulatory Roles on Oscillatory Islet Activity

McKenna, J. P., Ha, J., Merrins, M. J., Satin, L. S., Sherman, A., & Bertram, R. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2015.11.3526 · Cited by 40 · see citing works

SUMOylation disassembles the tetrameric pyruvate kinase M2 to block myeloid differentiation of leukemia cells

Li, X., Jiang, Y., Zhang, X., Wang, X., Wei, R., Qin, K., & Lu, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03400-9 · Cited by 37 · see citing works

A Novel Role for Pyruvate Kinase M2 as a Corepressor for P53 during the DNA Damage Response in Human Tumor Cells

Li, X., Wang, X., Wang, X., Liu, S.-H., Ding, X., Chen, G., & Lu, Y. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737056 · Cited by 36 · see citing works

Long non‐coding RNA VAL facilitates PKM2 enzymatic activity to promote glycolysis and malignancy of gastric cancer

Dai, T., Zhang, X., Zhou, X., Hu, X., Huang, X., Xing, F., Tian, H., & Li, Y. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.1088 · Cited by 36 · see citing works

Sepsis-induced changes in pyruvate metabolism: insights and potential therapeutic approaches

Nuyttens, L., Vandewalle, J., & Libert, C. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00155-6 · Cited by 36 · see citing works

A critical review of the role of M2PYK in the Warburg effect

Harris, R. A., & Fenton, A. W. (2019) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2019.01.004 · Cited by 32 · see citing works

Verification of Endometrial Tissue Biomarkers Previously Discovered Using Mass Spectrometry-Based Proteomics by Means of Immunohistochemistry in a Tissue Microarray Format

Dubé, V., Grigull, J., DeSouza, L. V., Ghanny, S., Colgan, T. J., Romaschin, A. D., & Siu, K. W. M. (2007) · Journal of Proteome Research · doi:10.1021/pr070087o · Cited by 33 · see citing works

Metabolic modulation of cancer: a new frontier with great translational potential

Kinnaird, A. S., & Michelakis, E. D. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1250-2 · Cited by 32 · see citing works

G9a inhibition induced PKM2 regulates autophagic responses

Ahmad, F., Dixit, D., Joshi, S. D., & Sen, E. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.07.009 · Cited by 32 · see citing works

Enhancing Mitochondrial Respiration Suppresses Tumor Promoter TPA-Induced PKM2 Expression and Cell Transformation in Skin Epidermal JB6 Cells

Wittwer, J. A., Robbins, D. F., Wang, F., Codarin, S., Shen, X., Kevil, C. G., Huang, T., Remmen, H. V., Richardson, A., & Zhao, Y. (2011) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-11-0028 · Cited by 31 · see citing works

Pyruvate kinase M2 phosphorylates H2AX and promotes genomic instability in human tumor cells

Li, X., Qin, K., Wang, X., Wang, X., Zhou, A., Chen, G., & Lu, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.22621 · Cited by 31 · see citing works

Intestinal epithelial PKM2 serves as a safeguard against experimental colitis via activating β-catenin signaling

Sun, X., Yao, L., Liang, H., Wang, D., He, Y., Yao, W., Ye, L., Wang, K., Li, L., Chen, J., et al. (2019) · Mucosal Immunology · doi:10.1038/s41385-019-0197-6 · Cited by 31 · see citing works

Microglia PKM2 Mediates Neuroinflammation and Neuron Loss in Mice Epilepsy through the Astrocyte C3-Neuron C3R Signaling Pathway

Li, X., Zhou, R., Peng, H., Peng, J., Li, Q., & Mei, M. (2023) · Brain Sciences · doi:10.3390/brainsci13020262 · Cited by 30 · see citing works

PGAMgnam Style: A Glycolytic Switch Controls Biosynthesis

Chaneton, B., & Gottlieb, E. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.014 · Cited by 30 · see citing works

TEPP-46-Based AIE Fluorescent Probe for Detection and Bioimaging of PKM2 in Living Cells

Wang, D., Li, C., Zhu, Y., Song, Y., Lu, S., Sun, H., Hao, H., & Xu, X. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c02529 · Cited by 29 · see citing works

Cancer metabolism control by natural products: Pyruvate kinase M2 targeting therapeutics

El‐Far, A. H., Jaouni, S. K. A., Li, X., & Fu, J. (2022) · Phytotherapy Research · doi:10.1002/ptr.7534 · Cited by 29 · see citing works

Identification of Candidate Biomarker Proteins Released by Human Endometrial and Cervical Cancer Cells Using Two-Dimensional Liquid Chromatography/Tandem Mass Spectrometry

Li, H., DeSouza, L. V., Ghanny, S., Li, W., Romaschin, A. D., Colgan, T. J., & Siu, K. W. M. (2007) · Journal of Proteome Research · doi:10.1021/pr0700798 · Cited by 29 · see citing works

Physiogenomic comparison of edema and BMI in patients receiving rosiglitazone or pioglitazone

Ruaño, G., Bernene, J. L., Windemuth, A., Bower, B., Wencker, D., Seip, R. L., Kocherla, M., Holford, T. R., Petit, W. A., & Hanks, S. (2008) · Clinica Chimica Acta · doi:10.1016/j.cca.2008.10.009 · Cited by 28 · see citing works

A review on the emerging roles of pyruvate kinase M2 in anti-leukemia therapy

Yang, G., Wu, J., Leung, C., Ma, D., & Chen, J. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.10.213 · Cited by 27 · see citing works

Cancer‐associated mutations in human pyruvate kinase M2 impair enzyme activity

Liu, V. M., Howell, A. J., Hosios, A. M., Li, Z., Israelsen, W. J., & Heiden, M. G. V. (2019) · FEBS Letters · doi:10.1002/1873-3468.13648 · Cited by 26 · see citing works

A short review on cross-link between pyruvate kinase (PKM2) and Glioblastoma Multiforme

Verma, H., Cholia, R. P., Kaur, S., Dhiman, M., & Mantha, A. K. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00690-y · Cited by 26 · see citing works

Modulation of the phosphorylation state of rat liver pyruvate kinase by allosteric effectors and insulin.

Claus, T. H., El‐Maghrabi, M. R., & Pilkis, S. J. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)36025-3 · Cited by 101 · see citing works

Reciprocal Regulation of Protein Kinase and Pyruvate Kinase Activities of Pyruvate Kinase M2 by Growth Signals

Gao, X., Wang, H., Yang, J. J., Chen, J., Jie, J., Li, L., Zhang, Y., & Liu, Z. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.448753 · Cited by 66 · see citing works

An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1,6-bisphosphate

Ashizawa, K., McPhie, P., Lin, K., & Cheng, S. Y. (1991) · Biochemistry · doi:10.1021/bi00243a010 · Cited by 101 · see citing works

Phosphorylation of pyruvate kinase type K is restricted to the dimeric form

Weernink, P. A. O., Rijksen, G., Mascini, E. M., & Saal, G. E. J. (1992) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(92)90337-d · Cited by 20 · see citing works

Fructose 2,6 bisphosphate promotes the monomer-tetramer conservation of Leishmania mexicana amazonensis pyruvate kinase type two.

Ponte‐Sucre, A., & Ramı́rez, J. L. (1993) · PubMed