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Glycolysis: A multifaceted metabolic pathway and signaling hub
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Glycolysis is a highly conserved metabolic pathway responsible for the anaerobic production of adenosine triphosphate (ATP) from the breakdown of glucose molecules. While serving as a primary metabolic pathway in prokaryotes, glycolysis is also utilized by respiring eukaryotic cells, providing pyruvate to fuel oxidative metabolism. Furthermore, glycolysis is the primary source of ATP production in multiple cellular states (e.g., hypoxia) and is particularly important in maintaining bioenergetic homeostasis in the most abundant cell type in the human body, the erythrocyte. Beyond its role in ATP production, glycolysis also functions as a signaling hub, producing several metabolic intermediates which serve roles in both signaling and metabolic processes. These signals emanating from the glycolytic pathway can profoundly impact cell function, phenotype, and fate and have previously been overlooked. In this review, we will discuss the role of the glycolytic pathway as a source of signaling molecules in eukaryotic cells, emphasizing the newfound recognition of glycolysis' multifaceted nature and its importance in maintaining cellular homeostasis, beyond its traditional role in ATP synthesis.
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“Even under hypoxic conditions, glycolysis remains the predominant pathway for ATP generation in tumor cells (11).”
From Bioinformatics-based identification of glycolysis-related signatures associated with drug resistance and prognosis in lung adenocarcinoma (2026) · cites this paper as [11]
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Cites
Metabolic regulation of gene expression by histone lactylation
Zhang, D., Tang, Z., Huang, H., Zhou, G., Cui, C., Weng, Y., Liu, W., Kim, S., Lee, S., Perez-Neut, M., et al. (2019) · Nature · doi:10.1038/s41586-019-1678-1 · Cited by 4,371
Aerobic glycolysis: Meeting the metabolic requirements of cell proliferation
Lunt, S. Y., & Vander Heiden, M. G. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154237 · Cited by 3,057
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927
Mammalian Sirtuins: Biological Insights and Disease Relevance
Haigis, M. C., & Sinclair, D. A. (2010) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092250 · Cited by 2,085
AMPK: Mechanisms of Cellular Energy Sensing and Restoration of Metabolic Balance
Garcia, D., & Shaw, R. J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.032 · Cited by 2,061
LDHA-Associated Lactic Acid Production Blunts Tumor Immunosurveillance by T and NK Cells
Brand, A., Singer, K., Koehl, G. E., Kolitzus, M., Schoenhammer, G., Thiel, A., Matos, C., Bruss, C., Klobuch, S., Peter, K., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.011 · Cited by 2,039
Activation of a metabolic gene regulatory network downstream of mTOR complex 1
Düvel, K., Yecies, J. L., Menon, S., Raman, P., Lipovsky, A. I., Souza, A. L., Triantafellow, E., Ma, Q., Gorski, R., Cleaver, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.022 · Cited by 2,020
Sirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008
Inhibitory effect of tumor cell-derived lactic acid on human T cells
Fischer, K., Hoffmann, P., Voelkl, S., Meidenbauer, N., Ammer, J., Edinger, M., Gottfried, E., Schwarz, S., Rothe, G., Hoves, S., et al. (2007) · Blood · doi:10.1182/blood-2006-07-035972 · Cited by 1,946
Glucose feeds the TCA cycle via circulating lactate
Hui, S., Ghergurovich, J. M., Morscher, R. J., Jang, C., Teng, X., Lu, W., Esparza, L. A., Reya, T., Zhan, L., Yanxiang Guo, J., et al. (2017) · Nature · doi:10.1038/nature24057 · Cited by 1,721
Nucleotides released by apoptotic cells act as a find-me signal to promote phagocytic clearance
Elliott, M. R., Chekeni, F. B., Trampont, P. C., Lazarowski, E. R., Kadl, A., Walk, S. F., Park, D., Woodson, R. I., Ostankovich, M., Sharma, P., et al. (2009) · Nature · doi:10.1038/nature08296 · Cited by 1,654
Targeting lactate-fueled respiration selectively kills hypoxic tumor cells in mice
Sonveaux, P., Végran, F., Schroeder, T., Wergin, M., Verrax, J., Rabbani, Z. N., Saedeleer, C. J. D., Kennedy, K. M., Diepart, C., Jordan, B. F., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36843 · Cited by 1,635
Physiology and Pathophysiology of Purinergic Neurotransmission
Burnstock, G. (2007) · Physiological Reviews · doi:10.1152/physrev.00043.2006 · Cited by 1,609
NAD+ and sirtuins in aging and disease
Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481
Phosphoenolpyruvate Is a Metabolic Checkpoint of Anti-tumor T Cell Responses
Ho, P.-C., Bihuniak, J. D., Macintyre, A. N., Staron, M., Liu, X., Amezquita, R., Tsui, Y.-C., Cui, G., Micevic, G., Perales, J. C., et al. (2015) · Cell · doi:10.1016/j.cell.2015.08.012 · Cited by 1,462
NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Xie, N., Zhang, L., Gao, W. Q., Huang, C., Huber, P., Zhou, X., Li, C. L., Shen, G., & Zou, B. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00311-7 · Cited by 1,147
(ADP-ribose)n participates in DNA excision repair
Durkacz, B. W., Omidiji, O., Gray, D. A., & Shall, S. (1980) · Nature · doi:10.1038/283593a0 · Cited by 1,123
Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
Rutter, J., Reick, M., Wu, L. C., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1060698 · Cited by 1,059
Complexes of sequential metabolic enzymes
Srere, P. A. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.000513 · Cited by 1,058
Regulation of glycolysis by the hypoxia-inducible factor (HIF): Implications for cellular physiology
Kierans, S. J., & Taylor, C. T. (2021) · The Journal of Physiology · doi:10.1113/jp280572 · Cited by 1,015
Self-citationATP as a biological hydrotrope
Patel, A., Malinovska, L., Saha, S., Wang, J., Alberti, S., Krishnan, Y., & Hyman, A. A. (2017) · Science · doi:10.1126/science.aaf6846 · Cited by 1,002
Yu, J., Chai, P., Xie, M., Ge, S., Ruan, J., Fan, X., & Jia, R. (2021) · Genome biology · doi:10.1186/s13059-021-02308-z · Cited by 981
The sirtuin family in health and disease
Wu, Q., Zhang, T., Chen, H., Yu, X., Lv, J.-L., Liu, Y., Liu, Y., Zheng, G., Zhao, J.-Q., Wei, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01257-8 · Cited by 928
Structure of mammalian AMPK and its regulation by ADP
Xiao, B., Sanders, M. J., Underwood, E., Heath, R., Mayer, F. V., Carmena, D., Jing, C., Walker, P. A., Eccleston, J. F., Haire, L. F., et al. (2011) · Nature · doi:10.1038/nature09932 · Cited by 926
ATP Release Guides Neutrophil Chemotaxis via P2Y2 and A3 Receptors
Chen, Y., Corriden, R., Inoue, Y., Yip, L., Hashiguchi, N., Zinkernagel, A. S., Nizet, V., Insel, P. A., & JUNGER, W. G. (2006) · Science · doi:10.1126/science.1132559 · Cited by 882
Pan, R.-Y., He, L., Zhang, J., Liu, X., Liao, Y., Gao, J., Liao, Y., Yan, Y., Li, Q., Zhou, X., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.02.013 · Cited by 862
Marsin, A.-S., Bertrand, L., Rider, M. H., Deprez, J., Beauloye, C., Vincent, M. F., den Berghe, G. V., Carling, D., & Hue, L. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00742-9 · Cited by 853
Cell–cell and intracellular lactate shuttles
Brooks, G. A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.178350 · Cited by 833
Haas, R., Smith, J., Rocher-Ros, V., Nadkarni, S., Montero‐Melendez, T., D’Acquisto, F., Bland, E. J., Bombardieri, M., Pitzalis, C., Perretti, M., et al. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002202 · Cited by 800
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763
Scott, J. W., Hawley, S. A., Green, K. A., Anis, M., Stewart, G., Scullion, G. A., Norman, D. G., & Hardie, D. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci19874 · Cited by 754
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
Hassa, P. O., Haenni, S. S., Elser, M., & Hottiger, M. O. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00040-05 · Cited by 719
Multifaceted roles of glycolytic enzymes
Kim, J., & Dang, C. V. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.01.005 · Cited by 692
Investigating the mechanism for AMP activation of the AMP-activated protein kinase cascade
Sanders, M. J., Grondin, P., Hegarty, B. D., Snowden, M. A., & Carling, D. (2007) · Biochemical Journal · doi:10.1042/bj20061520 · Cited by 677
NBS1 lactylation is required for efficient DNA repair and chemotherapy resistance
Chen, H., Li, Y., Li, H., Chen, X., Fu, H., Mao, D., Chen, W., Lan, L., Wang, C., Hu, K., et al. (2024) · Nature · doi:10.1038/s41586-024-07620-9 · Cited by 639
Calorie restriction extends yeast life span by lowering the level of NADH
Lin, S.-J., Ford, E., Haigis, M., Liszt, G., & Guarente, L. (2004) · Genes & Development · doi:10.1101/gad.1164804 · Cited by 632
Ca 2+ -Induced Ca 2+ Release in Sea Urchin Egg Homogenates: Modulation by Cyclic ADP-Ribose
Galione, A., Lee, H. C., & Busa, W. B. (1991) · Science · doi:10.1126/science.1909457 · Cited by 621
Regulation of Corepressor Function by Nuclear NADH
Zhang, Q., Piston, D. W., & Goodman, R. H. (2002) · Science · doi:10.1126/science.1069300 · Cited by 620
Extracellular ATP triggers and maintains asthmatic airway inflammation by activating dendritic cells
Idzko, M., Hammad, H., van Nimwegen, M., Kool, M., Willart, M. A. M., Muskens, F., Hoogsteden, H. C., Luttmann, W., Ferrari, D., Virgilio, F. D., et al. (2007) · Nature Medicine · doi:10.1038/nm1617 · Cited by 620
AMPK is a direct adenylate charge-regulated protein kinase
Oakhill, J. S., Steel, R., Chen, Z.-P., Scott, J. W., Ling, N., Tam, S., & Kemp, B. E. (2011) · Science · doi:10.1126/science.1200094 · Cited by 612
Liu, C., Wu, J., Zhu, J., Kuei, C., Yu, J., Shelton, J., Sutton, S. W., Li, X., Yun, S. J., Mirzadegan, T., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806409200 · Cited by 606
Opperdoes, F. R., & Borst, P. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80476-6 · Cited by 600
Carling, D., Zammit, V. A., & Hardie, D. G. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80292-2 · Cited by 599
Brizel, D. M., Schroeder, T., Scher, R. L., Walenta, S., Clough, R. W., Dewhirst, M. W., & Mueller‐Klieser, W. (2001) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/s0360-3016(01)01630-3 · Cited by 596
Structural basis for AMP binding to mammalian AMP-activated protein kinase
Xiao, B., Heath, R., Saiu, P., Leiper, F. C., Leone, P., Jing, C., Walker, P. A., Haire, L., Eccleston, J. F., Davis, C. T., et al. (2007) · Nature · doi:10.1038/nature06161 · Cited by 591
Garcia, C. K., Goldstein, J. L., Pathak, R., Anderson, R. G. W., & Brown, M. S. (1994) · Cell · doi:10.1016/0092-8674(94)90361-1 · Cited by 588
Hoque, R., Farooq, A., Ghani, A., Gorelick, F. S., & Mehal, W. Z. (2014) · Gastroenterology · doi:10.1053/j.gastro.2014.03.014 · Cited by 576
Clapper, D. L., Walseth, T. F., Dargie, P. J., & Lee, H. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47970-7 · Cited by 568
Kim, M. Y., Mauro, S. A., Gévry, N. Y., Lis, J. T., & Kraus, W. L. (2004) · Cell · doi:10.1016/j.cell.2004.11.002 · Cited by 551
Gu, J., Zhou, J., Chen, Q., Xu, X., Gao, J., Li, X., Shao, Q., Zhou, B., Zhou, H., Wei, S., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110986 · Cited by 529
Blood lactate is an important energy source for the human brain.
van Hall, G., Stømstad, M., Rasmussen, P., Jans, Ø., Zaar, M., Gam, C., Quistorff, B., Secher, N. H., & Nielsen, H. B. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.35 · Cited by 522
Structural Determination of a Cyclic Metabolite of NAD+ with Intracellular Ca2+-mobilizing Activity
Lee, H. C., Walseth, T. F., Bratt, G. T., Hayes, R., & Clapper, D. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94230-4 · Cited by 480
Suter, M., Riek, U., Tuerk, R. D., Schlattner, U., Wallimann, T., & Neumann, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606357200 · Cited by 473
Irizarry-Caro, R. A., McDaniel, M. M., Overcast, G. R., Jain, V. G., Troutman, T. D., & Pasare, C. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009778117 · Cited by 472
Release of ATP from human erythrocytes in response to a brief period of hypoxia and hypercapnia
Bergfeld, G. R., & Forrester, T. (1992) · Cardiovascular Research · doi:10.1093/cvr/26.1.40 · Cited by 453
The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation
Sweetlove, L. J., & Fernie, A. R. (2018) · Nature Communications · doi:10.1038/s41467-018-04543-8 · Cited by 433
Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
Campanella, M. E., Chu, H., & Low, P. S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409741102 · Cited by 407
Reciprocal Binding of PARP-1 and Histone H1 at Promoters Specifies Transcriptional Outcomes
Krishnakumar, R., Gamble, M. J., Frizzell, K. M., Berrocal, J. G., Kininis, M., & Kraus, W. L. (2008) · Science · doi:10.1126/science.1149250 · Cited by 382
Gertz, E. W., Wisneski, J. A., Stanley, W. C., & Neese, R. A. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113822 · Cited by 379
Enzymes of Glycolysis Are Functionally Associated with the Mitochondrion in Arabidopsis Cells
Giegé, P., Heazlewood, J. L., Roessner, U., Millar, A. H., Fernie, A. R., Leaver, C. J., & Sweetlove, L. J. (2003) · The Plant Cell · doi:10.1105/tpc.012500 · Cited by 378
Lactate Limits T Cell Proliferation via the NAD(H) Redox State
Quinn, W. J., Jiao, J., TeSlaa, T. A., Stadanlick, J. E., Wang, Z., Wang, L., Akimova, T., Angelin, A., Schäfer, P. M., Cully, M. D., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108500 · Cited by 376
Widespread reorganization of metabolic enzymes into reversible assemblies upon nutrient starvation
Narayanaswamy, R., Levy, M., Tsechansky, M., Stovall, G. M., O’Connell, J. D., Mirrielees, J. A., Ellington, A. D., & Marcotte, E. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812771106 · Cited by 368
Lactate Receptor Sites Link Neurotransmission, Neurovascular Coupling, and Brain Energy Metabolism
Lauritzen, K. H., Morland, C., Puchades, M. A., Holm‐Hansen, S., Hagelin, E. M. V., Lauritzen, F., Attramadal, H., Storm‐Mathisen, J., GJEDDE, A. H., & Bergersen, L. H. (2013) · Cerebral Cortex · doi:10.1093/cercor/bht136 · Cited by 367
Perraud, A.-L., Takanishi, C. L., Shen, B. W., Kang, S. J., Smith, M., Schmitz, C., Knowles, H. M., Ferraris, D. V., Li, W., Zhang, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m411446200 · Cited by 362
Lactate enhances motility of tumor cells and inhibits monocyte migration and cytokine release
Goetze, K. (2011) · International Journal of Oncology · doi:10.3892/ijo.2011.1055 · Cited by 356
Cell Surface Lactate Receptor GPR81 Is Crucial for Cancer Cell Survival
Roland, C. L., Arumugam, T., Deng, D., Liu, S. H., Philip, B., Gomez, S., Burns, W. R., Ramachandran, V., Wang, H., Cruz‐Monserrate, Z., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0319 · Cited by 345
Latham, T., Mackay, C. L., Sproul, D., Karim, M., Culley, J., Harrison, D. J., Hayward, L., Langridge‐Smith, P. R. R., Gilbert, N., & Ramsahoye, B. H. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks066 · Cited by 340
Oakhill, J. S., Chen, Z., Scott, J. W., Steel, R., Castelli, L. A., Ling, N. X. Y., Macaulay, S. L., & Kemp, B. E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009705107 · Cited by 337
Lactic Acid: No Longer an Inert and End-Product of Glycolysis
Sun, S., Li, H., Chen, J., & Qian, Q. (2017) · Physiology · doi:10.1152/physiol.00016.2017 · Cited by 331
Lactate metabolism is associated with mammalian mitochondria
Chen, Y.-J., Mahieu, N. G., Huang, X., Singh, M., Crawford, P. A., Johnson, S. L., Gross, R. W., Schaefer, J., & Patti, G. J. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2172 · Cited by 326
Brown, T. P., Bhattacharjee, P., Ramachandran, S., Sivaprakasam, S., Ristić, B., Sikder, M. O. F., & Ganapathy, V. (2020) · Oncogene · doi:10.1038/s41388-020-1216-5 · Cited by 322
Role of GPR81 in lactate-mediated reduction of adipose lipolysis
Cai, T., Ren, N., Jin, L., Cheng, K., Kash, S. F., Chen, R., Wright, S. D., Taggart, A. K. P., & Waters, M. G. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.088 · Cited by 305
Autocrine regulation of T‐cell activation by ATP release and P2X 7 receptors
Yip, L., Woehrle, T., Corriden, R., Hirsh, M., Chen, Y., Inoue, Y., Ferrari, V., Insel, P. A., & JUNGER, W. G. (2009) · The FASEB Journal · doi:10.1096/fj.08-126458 · Cited by 303
Apicella, M., Giannoni, E., Fiore, S., Ferrari, K. J., Fernández-Pérez, D., Isella, C., Granchi, C., Minutolo, F., Sottile, A., Comoglio, P. M., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.08.006 · Cited by 299
Becker, L. M., O’Connell, J. T., Vo, A. P., Cain, M. P., Tampe, D., Bizarro, L., Sugimoto, H., McGow, A. K., Asara, J. M., Lovisa, S., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107701 · Cited by 296
Yang, X., Lu, Y., Hang, J., Zhang, J., Zhang, T., Huo, Y., Liu, J., Lai, S., Luo, D., Wang, L., et al. (2020) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-20-0111 · Cited by 289
Active muscle and whole body lactate kinetics after endurance training in men
Bergman, B. C., Wolfel, E. E., Butterfield, G. E., Lopaschuk, G. D., Casazza, G. A., Horning, M. A., & Brooks, G. A. (1999) · Journal of Applied Physiology · doi:10.1152/jappl.1999.87.5.1684 · Cited by 280
Graham, J. W. A., Williams, T. C. R., Morgan, M., Fernie, A. R., Ratcliffe, R. G., & Sweetlove, L. J. (2007) · The Plant Cell · doi:10.1105/tpc.107.053371 · Cited by 276
Jiang, J., Huang, D., Jiang, Y., Hou, J., Tian, M., Li, J., Sun, L., Zhang, Y., Zhang, T., Li, Z., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.647559 · Cited by 274
Glycolytic enzymes localize to synapses under energy stress to support synaptic function
Jang, S., Nelson, J. C., Bend, E. G., Rodríguez-Laureano, L., Tueros, F. G., Cartagenova, L., Underwood, K., Jorgensen, E. M., & Colón-Ramos, D. A. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.011 · Cited by 270
The purinergic receptor P2RX7 directs metabolic fitness of long-lived memory CD8+ T cells
da Silva, H. B., Beura, L. K., Wang, H., Hanse, E. A., Gore, R., Scott, M. C., Walsh, D., Block, K. E., Fonseca, R., Yan, Y., et al. (2018) · Nature · doi:10.1038/s41586-018-0282-0 · Cited by 259
The Hexosamine Biosynthesis Pathway: Regulation and Function
Paneque, A., Fortus, H., Zheng, J., Werlen, G., & Jacinto, E. (2023) · Genes · doi:10.3390/genes14040933 · Cited by 257
Lactate promotes glioma migration by TGF-β2–dependent regulation of matrix metalloproteinase-2
Baumann, F., Leukel, P., Doerfelt, A., Beier, C. P., Dettmer, K., Oefner, P. J., Kastenberger, M., Kreutz, M. P., Nickl‐Jockschat, T., Bogdahn, U., et al. (2008) · Neuro-Oncology · doi:10.1215/15228517-2008-106 · Cited by 256
Bioluminescence detection of ATP release mechanisms in epithelia
Taylor, A. L., Kudlow, B. A., Marrs, K. L., Gruenert, D. C., Guggino, W. B., & Schwiebert, E. M. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.5.c1391 · Cited by 245
Dihydroxyacetone phosphate signals glucose availability to mTORC1
Orozco, J. M., Krawczyk, P. A., Scaria, S. M., Cangelosi, A. L., Chan, S. H., Kunchok, T., Lewis, C. A., & Sabatini, D. M. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0250-5 · Cited by 242
The Spatial Organization of Metabolism Within the Plant Cell
Sweetlove, L. J., & Fernie, A. R. (2013) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-050312-120233 · Cited by 238
la Sala, A., Ferrari, D., Corinti, S., Cavani, A., Virgilio, F. D., & Girolomoni, G. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.3.1611 · Cited by 232
The mechanism of RNA 5′ capping with NAD+, NADH and desphospho-CoA
Bird, J. G., Zhang, Y., Tian, Y., Panova, N., Barvík, I., Greene, L., Liu, M., Buckley, B., Krásný, L., Lee, J. K., et al. (2016) · Nature · doi:10.1038/nature18622 · Cited by 232
Correlation of high lactate levels in human cervical cancer with incidence of metastasis.
Schwickert, G., Walenta, S., Sundfør, K., Rofstad, E. K., & Mueller-Klieser, W. (1995) · PubMed · Cited by 225
Samuvel, D. J., Sundararaj, K. P., Nareika, A., Lopes-Virella, M. F., & Huang, Y. Q. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802059 · Cited by 223
Lactate Modulates the Activity of Primary Cortical Neurons through a Receptor-Mediated Pathway
Bozzo, L., Puyal, J., & Chatton, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071721 · Cited by 222
Lactate extraction during net lactate release in legs of humans during exercise
Stanley, W. C., Gertz, E. W., Wisneski, J. A., Neese, R. A., Morris, D. L., & Brooks, G. A. (1986) · Journal of Applied Physiology · doi:10.1152/jappl.1986.60.4.1116 · Cited by 215
Glycolytic Enzymes Coalesce in G Bodies under Hypoxic Stress
Jin, M., Fuller, G. G., Han, T., Yao, Y., Alessi, A. F., Freeberg, M. A., Roach, N. P., Moresco, J. J., Karnovsky, A., Baba, M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.082 · Cited by 208
Wagner, W., Ciszewski, W. M., & Kania, K. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0114-x · Cited by 202
Gallagher, C., Carpenter, K. L. H., Grice, P., Howe, D. J., Mason, A., Timofeev, I. S., Menon, D. K., Kirkpatrick, P. J., Pickard, J. D., Sutherland, G. R., et al. (2009) · Brain · doi:10.1093/brain/awp202 · Cited by 201
Liberti, M. V., Dai, Z., Wardell, S. E., Baccile, J. A., Liu, X., Gao, X., Baldi, R. M., Mehrmohamadi, M., Johnson, M. O., Madhukar, N. S., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.017 · Cited by 201
Quennet, V., Yaromina, A., Zips, D., Rosner, A., Walenta, S., Baumann, M. A., & Mueller‐Klieser, W. (2006) · Radiotherapy and Oncology · doi:10.1016/j.radonc.2006.08.012 · Cited by 197
Ranganathan, P. V., Shanmugam, A., Swafford, D., Suryawanshi, A. S., Bhattacharjee, P., Hussein, M. S., Koni, P. A., Prasad, P. D., Kurago, Z., Thangaraju, M., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1700604 · Cited by 196
Histone lactylation links metabolism and gene regulation
Izzo, L., & Wellen, K. E. (2019) · Nature · doi:10.1038/d41586-019-03122-1 · Cited by 195
Extracellular ATP and TNF-α Synergize in the Activation and Maturation of Human Dendritic Cells
Schnurr, M. M., Then, F., Galambos, P., Scholz, C., Siegmund, B., Endres, S., & Eigler, A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.8.4704 · Cited by 194
Increased release of ATP from endothelial cells during acute inflammation
Bodin, P., & Burnstock, G. (1998) · Inflammation Research · doi:10.1007/s000110050341 · Cited by 193
Extracellular ATP in T-lymphocyte activation: possible role in effector functions.
Filippini, A., Taffs, R. E., & Sitkovsky, M. V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.21.8267 · Cited by 193
Disposal of blood [1-13c] lactate in humans during rest and exercise
Mazzeo, R. S., Brooks, G. A., Schoeller, D. A., & Budinger, T. F. (1986) · Journal of Applied Physiology · doi:10.1152/jappl.1986.60.1.232 · Cited by 189
NAD(+)-dependent repair of damaged DNA by human cell extracts.
Satoh, M. S., Poirier, G. G., & Lindahl, T. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53346-9 · Cited by 188
Wu, S., & Wei, Y. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.09.014 · Cited by 182
Sirtuins and their Biological Relevance in Aging and Age-Related Diseases
Zhao, L., Cao, J., Hu, K., He, X., Dou, Y., Tong, T., & Han, L. (2020) · Aging and Disease · doi:10.14336/ad.2019.0820 · Cited by 178
Yegutkin, G. G., Bodin, P., & Burnstock, G. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703136 · Cited by 176
The Role of Mammalian Sirtuins in the Regulation of Metabolism, Aging, and Longevity
Satoh, A., Stein, L. R., & Imai, S. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-21631-2_7 · Cited by 175
Shangguan, X., He, J., Ma, Z., Zhang, W., Ji, Y., Shen, K., Yue, Z., Li, W., Xin, Z., Zheng, Q., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22163-7 · Cited by 173
Ambiquitous enzymes: Variation in intracellular distribution as a regulatory mechanism
Wilson, J. E. (1978) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(78)80029-2 · Cited by 171
Regulation of NF-κB signalling by the mono-ADP-ribosyltransferase ARTD10
Verheugd, P., Forst, A. H., Milke, L., Herzog, N., Feijs, K. L. H., Kremmer, E., Kleine, H. O., & Lüscher, B. (2013) · Nature Communications · doi:10.1038/ncomms2672 · Cited by 169
Errea, A. J., Cayet, D., Marchetti, P., Tang, C., Kluza, J., Offermanns, S., Sirard, J., & Rumbo, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163694 · Cited by 168
Tumor-derived lactate and myeloid-derived suppressor cells: Linking metabolism to cancer immunology
Husain, Z., Seth, P., & Sukhatme, V. P. (2013) · OncoImmunology · doi:10.4161/onci.26383 · Cited by 164
Entelis, N., Brandina, I., Kamenski, P. A., Krasheninnikov, I. A., Martin, R. P., & Tarassov, I. (2006) · Genes & Development · doi:10.1101/gad.385706 · Cited by 162
Brain Hexokinase, the Prototype Ambiquitous Enzyme
Wilson, J. E. (1980) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152816-4.50005-4 · Cited by 160
Ratter, J. M., Rooijackers, H. M. M., Hooiveld, G. J. E. J., Hijmans, A., de Galan, B. E., Tack, C. J., & Stienstra, R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02564 · Cited by 158
Maintained exercise‐enhanced brain executive function related to cerebral lactate metabolism in men
Hashimoto, T., Tsukamoto, H., Takenaka, S., Olesen, N. D., Petersen, L. G., Sørensen, H., Nielsen, H. B., Secher, N. H., & Ogoh, S. (2018) · The FASEB Journal · doi:10.1096/fj.201700381rr · Cited by 156
Endurance training increases gluconeogenesis during rest and exercise in men
Bergman, B. C., Horning, M. A., Casazza, G. A., Wolfel, E. E., Butterfield, G. E., & Brooks, G. A. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.278.2.e244 · Cited by 153
Lactate: a multifunctional signaling molecule
Lee, T.-Y. (2021) · Journal of Yeungnam Medical Science · doi:10.12701/yujm.2020.00892 · Cited by 142
Interaction of the aldolase and the membrane of human erythrocytes
Strapazon, E., & Steck, T. L. (1977) · Biochemistry · doi:10.1021/bi00632a025 · Cited by 142
Srinivas, S. R., Gopal, E., Zhuang, L., Itagaki, S., Martin, P. M., Fei, Y.-J., Ganapathy, V., & Prasad, P. D. (2005) · Biochemical Journal · doi:10.1042/bj20050927 · Cited by 141
Kang, J., Lim, L., Lu, Y., & Song, J. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000327 · Cited by 139
Gluconeogenesis and hepatic glycogenolysis during exercise at the lactate threshold
Emhoff, C.-A. W., Messonnier, L. A., Horning, M. A., Fattor, J. A., Carlson, T. J., & Brooks, G. A. (2013) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01202.2012 · Cited by 139
Identification of a multienzyme complex for glucose metabolism in living cells
Kohnhorst, C. L., Kyoung, M., Jeon, M., Schmitt, D. L., Kennedy, E. L., Ramirez, J., Bracey, S. M., Luu, B. T., Russell, S. J., & An, S. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.783050 · Cited by 138
The GAPDH redox switch safeguards reductive capacity and enables survival of stressed tumour cells
Talwar, D., Miller, C. G., Großmann, J. L., Szyrwiel, Ł., Schwecke, T., Demichev, V., Mikecin, A., Mayakonda, A., Lutsik, P., Veith, C., et al. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00781-3 · Cited by 137
Elucidation of signaling and functional activities of an orphan GPCR, GPR81
Ge, H., Weiszmann, J., Reagan, J. D., Gupte, J., Baribault, H., Gyuris, T., Chen, J., Tian, H., & Li, Y. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m700513-jlr200 · Cited by 131
Enolase takes part in a macromolecular complex associated to mitochondria in yeast
Brandina, I., Graham, J. W. A., Guillier, C., Entelis, N., Krasheninnikov, I. A., Sweetlove, L. J., Tarassov, I., & Martin, R. P. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.07.001 · Cited by 128
Lactic acid delays the inflammatory response of human monocytes
Peter, K., Rehli, M., Singer, K., Renner, K., & Kreutz, M. P. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.005 · Cited by 127
Autocrine Regulation of Macrophage Activation via Exocytosis of ATP and Activation of P2Y11 Receptor
Sakaki, H., Tsukimoto, M., Harada, H., Moriyama, Y., & Kojima, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059778 · Cited by 122
Flight muscle function in Drosophila requires colocalization of glycolytic enzymes.
Wojtas, K. M., Slepecky, N. B., von Kalm, L., & Sullivan, D. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.9.1665 · Cited by 121
Harun-Or-Rashid, M., & Inman, D. M. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1346-7 · Cited by 121
Compartmentation of enzymes in a microbody, the glycosome, is essential inTrypanosoma brucei
Guerra‐Giraldez, C., Quijada, L., & CLAYTON, C. E. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.13.2651 · Cited by 117
Kang, J., Lim, L., & Song, J. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.014 · Cited by 114
Myocardial glucose and lactate metabolism during rest and atrial pacing in humans
Bergman, B. C., Tsvetkova, T. O., Lowes, B. D., & Wolfel, E. E. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2008.168286 · Cited by 111
Paolini, L., Adam, C., Beauvillain, C., Preisser, L., Blanchard, S., Pignon, P., Seegers, V., Chevalier, L.-M., Campone, M., Wernert, R., et al. (2020) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-18-0749 · Cited by 103
The role of poly(ADP-ribosyl)ation in epigenetic events
Quénet, D., Ramy, R. E., Schreiber, V., & Dantzer, F. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.07.023 · Cited by 100
Campanella, M. E., Chu, H., Wandersee, N. J., Peters, L. L., Mohandas, N., Gilligan, D. M., & Low, P. S. (2008) · Blood · doi:10.1182/blood-2008-03-146159 · Cited by 99
Modulation of sarcoplasmic reticulum Ca2+ release by glycolysis in cat atrial myocytes
Kockskämper, J., Zima, A. V., & Blatter, L. A. (2005) · The Journal of Physiology · doi:10.1113/jphysiol.2004.078782 · Cited by 91
Ultrastructural Localization of Glycolytic Enzymes on Sarcoplasmic Reticulum Vesicles
Xu, K. Y., & Becker, L. C. (1998) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549804600401 · Cited by 91
Bird, J. G., Basu, U., Kuster, D., Ramachandran, A., Grudzien‐Nogalska, E., Towheed, A., Wallace, D. C., Kiledjian, M., Temiakov, D., Patel, S. S., et al. (2018) · eLife · doi:10.7554/elife.42179 · Cited by 89
NADH inhibition of SIRT1 links energy state to transcription during time-restricted feeding
Levine, D. C., Kuo, H.-Y., Hong, H., Cedernaes, J., Hepler, C., Wright, A. G., Sommars, M. A., Kobayashi, Y., Marcheva, B., Gao, P., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00498-1 · Cited by 88
Kennedy, L. H., Glesaaen, E. R., Palibrk, V., Pannone, M., Wang, W., Al-Jabri, A., Suganthan, R., Meyer, N., Austbø, M. L., Lin, X., et al. (2022) · eLife · doi:10.7554/elife.76451 · Cited by 82
Song, J. (2021) · Protein Science · doi:10.1002/pro.4079 · Cited by 79
CapZyme-Seq Comprehensively Defines Promoter-Sequence Determinants for RNA 5′ Capping with NAD+
Vvedenskaya, I. O., Bird, J. G., Zhang, Y., Zhang, Y., Jiao, X., Barvı́k, I., Krásný, L., Kiledjian, M., Taylor, D. M., Ebright, R. H., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.014 · Cited by 77
Cori, C. F., & Cori, G. T. (1946) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.15.070146.001205 · Cited by 76
ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues
Dang, M., Lim, L., Kang, J., & Song, J. (2021) · Communications Biology · doi:10.1038/s42003-021-02247-2 · Cited by 73
Elevated lactic acid is a negative prognostic factor in metastatic lung cancer
Vlachostergios, P. J., Oikonomou, K. G., Gibilaro, E., & Apergis, G. A. (2015) · Cancer Biomarkers · doi:10.3233/cbm-150514 · Cited by 72
Supramolecular organization of glycolytic enzymes
Kurganov, B. I., Np, S., & Ls, M. (1985) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(85)80086-2 · Cited by 71
Glycolytic Enzyme Interactions with Yeast and Skeletal Muscle F-Actin
Waingeh, V. F., Gustafson, C. D., Kozliak, E. I., Lowe, S. L., Knull, H. R., & Thomasson, K. A. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.070052 · Cited by 70
The malate-aspartate shuttle is important for de novo serine biosynthesis
Broeks, M. H., Meijer, N. W. F., Westland, D., Bosma, M., Gerrits, J., German, H. M., Čiapaitė, J., van Karnebeek, C., Wanders, R. J. A., Zwartkruis, F. J. T., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113043 · Cited by 69
On the association of glycolytic components in skeletal muscle extracts
Clarke, F. M., & Masters, C. J. (1974) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(74)90270-8 · Cited by 66
Lambertus, M., Øverberg, L. T., Andersson, K. A., Hjelden, M. S., Hadzic, A., Haugen, Ø. P., Storm‐Mathisen, J., Bergersen, L. H., Geiseler, S. J., & Morland, C. (2020) · Acta Physiologica · doi:10.1111/apha.13587 · Cited by 65
Diversification of NAD biological role : the importance of location
Stefano, M. D., & Conforti, L. (2013) · FEBS Journal · doi:10.1111/febs.12433 · Cited by 62
Kierans, S. J., Fagundes, R. R., Malkov, M. I., Sparkes, R., Dillon, E., Smolenski, A., Faber, K. N., & Taylor, C. T. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208117120 · Cited by 61
Self-citationATP-induced activation of human B lymphocytes via P2-purinoceptors
Padeh, S., Cohen, A., & Roifman, C. M. (1991) · The Journal of Immunology · doi:10.4049/jimmunol.146.5.1626 · Cited by 59
Spatial Reorganization of Saccharomyces cerevisiae Enolase To Alter Carbon Metabolism under Hypoxia
Miura, N., Shinohara, M., Tatsukami, Y., Sato, Y., Morisaka, H., Kuroda, K., & Ueda, M. (2013) · Eukaryotic Cell · doi:10.1128/ec.00093-13 · Cited by 57
Arrivault, S., Guenther, M., Florian, A., Encke, B., Feil, R., Vosloh, D., Lunn, J. E., Sulpice, R., Fernie, A. R., Stitt, M., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.038190 · Cited by 57
To, W. K. L., Kumar, P., & Marshall, J. M. (2015) · Placenta · doi:10.1016/j.placenta.2015.04.005 · Cited by 52
Extracellular Adenine Nucleotides Inhibit the Activation of Human CD4+ T Lymphocytes
Duhant, X., Schandené, L., Bruyns, C., Gonzalez, N. S., Goldman, M., Boeynaems, J., & Communi, D. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.1.15 · Cited by 50
Wolf, B. A., Colca, J. R., Comens, P. G., TURK, J. W., & McDaniel, M. L. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66560-3 · Cited by 49
Jovanović, S., & Jovanović, A. (2005) · Diabetes · doi:10.2337/diabetes.54.2.383 · Cited by 46
Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line
Rakus, D., Mamczur, P., Gizak, A., Duś, D., & Dżugaj, A. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.209 · Cited by 42
Molecular functions of moonlighting proteins in cell metabolic processes
Werelusz, P., Galiniak, S., & Mołoń, M. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119598 · Cited by 35
Phosphoenolpyruvate regulates the Th17 transcriptional program and inhibits autoimmunity
Huang, T.-Y., Hirota, M., Sasaki, D., Kalra, R. S., Chien, H.-C., Tamai, M., Sarkar, S., Mi, Y., Miyagi, M., Seto, Y., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112205 · Cited by 33
HIF1α-dependent uncoupling of glycolysis suppresses tumor cell proliferation
Urrutia, A. A., Mesa‐Ciller, C., Guajardo-Grence, A., Alkan, H. F., Soro-Arnáiz, I., Vandekeere, A., Campos, A. M. F., Igelmann, S., Fernández-Arroyo, L., Rinaldi, G., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114103 · Cited by 31
Moonlight functions of glycolytic enzymes in cancer
Шегай, П. В., Shatova, O. P., Zabolotneva, A. A., Shestopalov, A. V., & Каприн, А. Д. (2023) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2023.1076138 · Cited by 30
Cooper, A. J. L., Sheu, K. R., Burke, J. R., Strittmatter, W. J., & Blass, J. P. (1998) · Developmental Neuroscience · doi:10.1159/000017344 · Cited by 29
Kholodenko, B. Ν., Westerhoff, H. V., & Cascante, M. (1996) · Biochemical Journal · doi:10.1042/bj3130921 · Cited by 28
Dang, M., Li, T., Zhou, S., & Song, J. (2022) · Communications Biology · doi:10.1038/s42003-022-04293-w · Cited by 27
Ambiquitous Behavior—A Biological Phenomenon of General Significance?
Nemat‐Gorgani, M., & Wilson, J. E. (1980) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152816-4.50006-6 · Cited by 26
A novel mechanism for ATP to enhance the functional oligomerization of TDP-43 by specific binding
Wang, L., Lim, L., Dang, M., & Song, J. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.006 · Cited by 23
Patterns of spatiotemporal organization in an "ambiquitous" enzyme model.
Marmillot, P., Hervagault, J. F., & Welch, G. R. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.24.12103 · Cited by 20
Seok, S. M., Park, T. Y., Park, H.-S., Baik, E. J., & Lee, S. (2015) · International Immunopharmacology · doi:10.1016/j.intimp.2015.03.029 · Cited by 20
Henderson, A. R. (1969) · British Journal of Anaesthesia · doi:10.1093/bja/41.3.245 · Cited by 16
Size-Specific Modulation of a Multienzyme Glucosome Assembly during the Cell Cycle
Jeon, M., Schmitt, D. L., Kyoung, M., & An, S. (2023) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.3c00037 · Cited by 13
ATP induces folding of ALS-causing C71G-hPFN1 and nascent hSOD1
Kang, J., Lim, L., & Song, J. (2023) · Communications Chemistry · doi:10.1038/s42004-023-00997-0 · Cited by 13
[Therapeutic experiences with Budd-Chiari syndrome: report of 100 cases].
Wang, Z. G. (1989) · PubMed · Cited by 1
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Decoding microglial immunometabolism: a new frontier in Alzheimer's disease research
Jung, E. S., Choi, H., & Mook-Jung, I. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00825-0 · Cited by 124
Wu, G., Chong, J. W. R., Khoo, K. S., Tang, D. Y. Y., & Show, P. L. (2025) · Biotechnology for Biofuels and Bioproducts · doi:10.1186/s13068-025-02679-6 · Cited by 33
Cao, Z., Zhou, Q., An, J., Guo, X., Jia, X., & Qiu, Y. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s525651 · Cited by 30
Zhou, J., Hu, S., Ouyang, Y., Kong, Y., & Liu, M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1736492 · Cited by 23
Choi, J. Y., Ha, N. G., Lee, W. J., & Boo, Y. C. (2025) · Antioxidants · doi:10.3390/antiox14040498 · Cited by 24
Metadata
- Authors
- Kierans, S. J., & Taylor, C. T.
- Affiliations
- University College Dublin (IE)
- Corresponding author
- Taylor, Cormac T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2024-11
- Volume
- 300
- Issue
- 11
- Pages
- 107906
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC11605472
- OpenAlex
- W4403659524
- Cited by
- 198
- References
- 182
- Citations by year
- 2026: 125 · 2025: 72 · 2024: 1
- FWCI
- 8.13
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Taighde Éireann – Research Ireland (22/FFP-A/10523)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
- Keywords
- glycolysis, metabolic intermediates, ATP production, erythrocytes, hypoxia, bioenergetic homeostasis, pyruvate, eukaryotic cells, cellular homeostasis, cell fate
- MeSH terms
- Adenosine Triphosphate, Animals, Energy Metabolism, Glycolysis, Homeostasis, Humans, Signal Transduction, Metabolic Networks and Pathways
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