Glycolysis: A multifaceted metabolic pathway and signaling hub
Open accessAbstract
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.
“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]
The section “Glycolysis and its contribution to metabolism” says glycolysis is the primary source of ATP in cells experiencing hypoxia. It does not make that ATP-generation claim specifically about tumor cells, so the tumor-cell qualification goes beyond what the passage states. (LLM, conf=0.83)
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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 · see citing works
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 · see citing works
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 1,997 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Physiology and Pathophysiology of Purinergic Neurotransmission
Burnstock, G. (2007) · Physiological Reviews · doi:10.1152/physrev.00043.2006 · Cited by 1,579 · see citing works
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 · see citing works
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 · see citing works
(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 · see citing works
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 1,078 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 990 · see citing works
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 955 · see citing works
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 · see citing works
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 891 · see citing works
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 · see citing works
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 858 · see citing works
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 818 · see citing works
Cell–cell and intracellular lactate shuttles
Brooks, G. A. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.178350 · Cited by 803 · see citing works
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 782 · see citing works
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 · see citing works
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 · see citing works
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 682 · see citing works
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 682 · see citing works
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 660 · see citing works
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 · see citing works
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 622 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Opperdoes, F. R., & Borst, P. (1977) · FEBS Letters · doi:10.1016/0014-5793(77)80476-6 · Cited by 600 · see citing works
Carling, D., Zammit, V. A., & Hardie, D. G. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80292-2 · Cited by 599 · see citing works
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 · see citing works
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 · see citing works
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 587 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 510 · see citing works
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 · see citing works
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 · see citing works
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 465 · see citing works
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 · see citing works
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 421 · see citing works
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 · see citing works
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 · see citing works
Gertz, E. W., Wisneski, J. A., Stanley, W. C., & Neese, R. A. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113822 · Cited by 379 · see citing works
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 · see citing works
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 370 · see citing works
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 · see citing works
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 358 · see citing works
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 356 · see citing works
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 · see citing works
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 331 · see citing works
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 328 · see citing works
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 · see citing works
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 321 · see citing works
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 319 · see citing works
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 310 · see citing works
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 · see citing works
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 · see citing works
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 293 · see citing works
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 284 · see citing works
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 · see citing works
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 278 · see citing works
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 · see citing works
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 · see citing works
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 266 · see citing works
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 · see citing works
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 252 · see citing works
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 247 · see citing works
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 245 · see citing works
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 · see citing works
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 230 · see citing works
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 226 · see citing works
The mechanism of RNA 5′ capping with NAD+, NADH and desphospho-CoA
Bird, J. G., Zhang, Y., Tian, Y., Panova, N., Barvı́k, I., Greene, L., Liu, M., Buckley, B., Krásný, L., Lee, J. K., et al. (2016) · Nature · doi:10.1038/nature18622 · Cited by 226 · see citing works
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 · see citing works
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 220 · see citing works
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 · see citing works
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 211 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 196 · see citing works
Histone lactylation links metabolism and gene regulation
Izzo, L., & Wellen, K. E. (2019) · Nature · doi:10.1038/d41586-019-03122-1 · Cited by 195 · see citing works
Wagner, W., Ciszewski, W. M., & Kania, K. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0114-x · Cited by 194 · see citing works
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 · see citing works
Increased release of ATP from endothelial cells during acute inflammation
Bodin, P., & Burnstock, G. (1998) · Inflammation Research · doi:10.1007/s000110050341 · Cited by 193 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 188 · see citing works
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 · see citing works
Yegutkin, G. G., Bodin, P., & Burnstock, G. (2000) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0703136 · Cited by 176 · see citing works
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 174 · see citing works
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 · see citing works
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 171 · see citing works
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 · see citing works
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 162 · see citing works
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 · see citing works
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 161 · see citing works
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 160 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 150 · see citing works
Interaction of the aldolase and the membrane of human erythrocytes
Strapazon, E., & Steck, T. L. (1977) · Biochemistry · doi:10.1021/bi00632a025 · Cited by 142 · see citing works
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 · see citing works
Kang, J., Lim, L., Lu, Y., & Song, J. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000327 · Cited by 139 · see citing works
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 · see citing works
Lactate: a multifunctional signaling molecule
Lee, T.-Y. (2021) · Journal of Yeungnam Medical Science · doi:10.12701/yujm.2020.00892 · Cited by 136 · see citing works
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 135 · see citing works
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 133 · see citing works
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 127 · see citing works
Enolase takes part in a macromolecular complex associated to mitochondria in yeast.
Brandina, I., Graham, J., Lemaître-Guillier, C., Entelis, N., Krasheninnikov, I., Sweetlove, L., Tarassov, I., & Martin, R. (2006) · Biochimica et Biophysica Acta · doi:10.1016/j.bbabio.2006.07.001 · Cited by 126 · see citing works
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 123 · see citing works
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 · see citing works
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 · see citing works
Harun-Or-Rashid, M., & Inman, D. M. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1346-7 · Cited by 121 · see citing works
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 · see citing works
Kang, J., Lim, L., & Song, J. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.09.014 · Cited by 114 · see citing works
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 · see citing works
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 · see citing works
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 96 · see citing works
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 94 · see citing works
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 · see citing works
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 · see citing works
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 85 · see citing works
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 81 · see citing works
Song, J. (2021) · Protein Science · doi:10.1002/pro.4079 · Cited by 80 · see citing works
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 · see citing works
Cori, C. F., & Cori, G. T. (1946) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.15.070146.001205 · Cited by 76 · see citing works
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 76 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 62 · see citing works
Diversification of NAD biological role : the importance of location
Stefano, M. D., & Conforti, L. (2013) · FEBS Journal · doi:10.1111/febs.12433 · Cited by 61 · see citing works
ATP-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 · see citing works
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 · see citing works
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 56 · see citing works
Self-citationArrivault, S., Guenther, M., Florian, A., Encke, B., Feil, R., Vosloh, D., Lunn, J. E., Ronan Sulpice, A., Fernie, A. R., Stitt, M., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.038190 · Cited by 56 · see citing works
To, W. K. L., Kumar, P., & Marshall, J. M. (2015) · Placenta · doi:10.1016/j.placenta.2015.04.005 · Cited by 52 · see citing works
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 · see citing works
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 · see citing works
Jovanović, S., & Jovanović, A. (2005) · Diabetes · doi:10.2337/diabetes.54.2.383 · Cited by 46 · see citing works
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 · see citing works
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 · see citing works
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 32 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Kholodenko, B. Ν., Westerhoff, H. V., & Cascante, M. (1996) · Biochemical Journal · doi:10.1042/bj3130921 · Cited by 28 · see citing works
Dang, M., Li, T., Zhou, S., & Song, J. (2022) · Communications Biology · doi:10.1038/s42003-022-04293-w · Cited by 27 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Henderson, A. R. (1969) · British Journal of Anaesthesia · doi:10.1093/bja/41.3.245 · Cited by 16 · see citing works
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 · see citing works
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 · see citing works
[Therapeutic experiences with Budd-Chiari syndrome: report of 100 cases].
Wang, Z. G. (1989) · PubMed · Cited by 1 · see citing works
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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 · see citing works
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 32 · see citing works
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 28 · see citing works
Zhou, J., Hu, S., Ouyang, Y., Kong, Y., & Liu, M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1736492 · Cited by 23 · see citing works
Choi, J. Y., Ha, N. G., Lee, W. J., & Boo, Y. C. (2025) · Antioxidants · doi:10.3390/antiox14040498 · Cited by 24 · see citing works
Immune cell metabolic dysfunction in Parkinson’s disease
Mark, J. R., & Tansey, M. G. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00827-y · Cited by 20 · see citing works
Jiang, X., Wu, A., Yan, J., Chen, J., Wen, Y., Wu, H., Yan, N., Yang, Z., Liu, F., & Li, P. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.114907 · Cited by 17 · see citing works
Tang, Q., Zhang, Y., Huang, J. G., & Zhou, R. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116962 · Cited by 17 · see citing works
Yi, T., Shen, L., Luo, W., & Wang, P. (2025) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2025.123319 · Cited by 15 · see citing works
The return of metabolism: biochemistry and physiology of glycolysis
Grüning, N., Agostini, F., Caldana, C., Hartl, J., Heinemann, M., Keller, M. A., Krüsemann, J. L., Lamperti, C., Linster, C. L., Lindner, S. N., et al. (2025) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.70104 · Cited by 16 · see citing works
Xi, L., Wang, Z., Chen, Y., & Li, Q. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010148 · Cited by 14 · see citing works
Wei, K.-S., Tang, J., Xu, C., Yang, L., Tang, J., Wu, S., Zhao, Y., Di, H., Yu, X., Liang, K., et al. (2025) · Industrial Crops and Products · doi:10.1016/j.indcrop.2025.122304 · Cited by 13 · see citing works
Lactate and lactylation in the kidneys: Current advances and prospects (Review)
Li, X., Hu, L., Hu, Q., & Jin, H. (2025) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2025.5562 · Cited by 13 · see citing works
Integrated Multi-Omics Analysis Reveals Key Regulators of Bovine Oocyte Maturation
Kassim, Y., Sheng, H., Xu, G., Jin, H., Iqbal, T. H., Elashry, M., & Zhang, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26093973 · Cited by 12 · see citing works
Xu, A., Xie, L., Ouyang, Y., Liu, P., Xiao, Y., Wang, Y., Liu, J., Liu, B., Gao, B., & Zhu, D. (2025) · LWT · doi:10.1016/j.lwt.2025.118191 · Cited by 11 · see citing works
Yang, Y., Tian, X., Chen, J., Liu, J., Jiang, H., Liu, L., Qu, S., Wu, M., Wang, J., Chen, Y., et al. (2025) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2025-011948 · Cited by 11 · see citing works
Histone lactylation: a new target for overcoming immune evasion and therapy resistance
Ghadyani, F., Zandi, P., & Ghafouri‐Fard, S. (2025) · Medical Oncology · doi:10.1007/s12032-025-02940-w · Cited by 11 · see citing works
Liu, M., Wang, M., Fu, X., Song, F., Zhou, F., Li, T., & Wang, J. (2025) · Metabolites · doi:10.3390/metabo15020097 · Cited by 9 · see citing works
Pan, S., Zhang, Z., Liu, Z., Wu, L., Gao, Q., & Cai, H. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.144359 · Cited by 9 · see citing works
Li, M., Ma, Y. C., Wang, S., Zheng, H., Yang, C., Duan, A., Zhou, B., Shang, J., Liang, X., & Yang, X. (2025) · Cells · doi:10.3390/cells14110832 · Cited by 8 · see citing works
Meng, Q., Song, Q., Meng, X., Wang, X., & Cong, J. (2025) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2025.111602 · Cited by 9 · see citing works
Xiao, D., Zou, M. Q., & Huang, M. (2025) · Materials Science and Engineering B · doi:10.1016/j.mseb.2025.118647 · Cited by 8 · see citing works
Keller, I., & Neuhaus, H. E. (2025) · Journal of Plant Physiology · doi:10.1016/j.jplph.2025.154600 · Cited by 8 · see citing works
Luo, W. F., He, X., Chen, Y., Xu, Y., Zhuang, Y., Ding, Y., & Fan, X. (2025) · Foods · doi:10.3390/foods14173112 · Cited by 8 · see citing works
Pyruvate Kinase M2 Role in Cardiovascular Repair
Rihan, M., Zangi, L., & Magadum, A. (2025) · Cells · doi:10.3390/cells14201623 · Cited by 8 · see citing works
Influence of exercise training on nitric oxide pathways and their physiological effects
Benjamim, C. J. R., Bailey, S. J., Gonçalves, L. D. S., Burleigh, M. C., Siervo, M., Coggan, A. R., & Bescós, R. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104041 · Cited by 8 · see citing works
Chen, Y., Wang, X., Lu, L., Zhang, B., Yang, H., Zhao, S., Wang, Z., Wang, L., Peng, Q., & Xue, B. (2025) · Animals · doi:10.3390/ani15081152 · Cited by 8 · see citing works
HcTRET1 is critical for epidermal chitin synthesis in Hyphantria cunea
Liu, D., Zou, C., Zhang, S., Wang, Z., Yu, J., Nan, Y., & Dong, Z. (2025) · Insect Molecular Biology · doi:10.1111/imb.12994 · Cited by 7 · see citing works
The role of glycolysis in inflammation
Dehantschutter, E. T., & Taylor, C. T. (2026) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00113.2026 · Cited by 7 · see citing works
Self-citationMechanisms underlying low mutation rates in mammalian oocytes and preimplantation embryos
Dudko, N., Dobrucki, J. W., & Fulka, J. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf760 · Cited by 5 · see citing works
Lim, H., Denison, M. I. J., Natarajan, S., Lee, K., Oh, C., & Park, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010335 · Cited by 5 · see citing works
Cell-free DNA: plays an essential role in early diagnosis and immunotherapy of pancreatic cancer
Wen, Y., Zhao, G., & Dai, C. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1546332 · Cited by 5 · see citing works
Potential of exudate metabolites to predict microbial populations in beef
Hong, H., Kim, H.-J., Kim, H., Ismail, A., Choi, M., & Jo, C. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116814 · Cited by 5 · see citing works
Methods and Guidelines for Metabolism Studies: Applications to Cancer Research
Li, M., Amend, S. R., & Pienta, K. J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178466 · Cited by 6 · see citing works
Weiß, L., Turner, M. E., Qin, Z., Bäck, M., & Aïkawa, E. (2026) · European Heart Journal - Valvular and Structural Heart Disease · doi:10.1093/ehjvshd/xwag018 · Cited by 4 · see citing works
Degradation of the Molecular Basis of Life During the Aging Process
Błaszczyk, J. W. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052419 · Cited by 4 · see citing works
Feng, D.-D., Yang, C., Orr, M. C., & Zhang, A. (2025) · BMC Genomics · doi:10.1186/s12864-025-11524-x · Cited by 4 · see citing works
Laws, M. J., Kramer, S., Gonyea, T., Huff, J., Edwards, L., Tarvainen, I., Damdimopoulou, P., & Flaws, J. A. (2025) · Reproductive Toxicology · doi:10.1016/j.reprotox.2025.108938 · Cited by 4 · see citing works
Fang, W. B., Kozai, Y., Acevedo, D. S., Brodine, R., Gorrepati, H. S., Arviso, N., Cote, P., Thompson, A., Gerdes, Z., Espinoza, A., et al. (2025) · Cancer Biology & Therapy · doi:10.1080/15384047.2025.2535824 · Cited by 4 · see citing works
Solar-driven catalytic platforms for closed-loop carbon cycling: CO2 assisting biomass conversion
Jiang, J., Wang, Y., Li, Y.-J., Huang, J., Zhang, W., Wang, D., Xu, D., Fu, D., Zhang, P., Wang, L., et al. (2025) · Bioresource Technology · doi:10.1016/j.biortech.2025.133789 · Cited by 4 · see citing works
Liu, B., Chen, G., Mo, H., Liang, X., Su, X., Lu, F., Lin, Q., Liu, X., Deng, J., & Zhang, D. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157055 · Cited by 3 · see citing works
Targeting Glycolysis for Spinal Cord Injury: Regulatory Mechanisms and Therapeutic Prospects.
Qian, S., Shi, C., Wang, B., Guo, Y., Dan, L., Dang, Z., Zhao, X.-W., Gao, F., Yang, Y., Shen, J., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00604 · Cited by 3 · see citing works
Liu, J., Tan, D., Qiu, H., Liang, Y., Wu, H., Yu, Y., & Zhao, H. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1674444 · Cited by 3 · see citing works
Karpova, N. S., Fefilova, E., Daks, A. A., Parfenyev, S. E., Nazarov, A., Barlev, N. A., & Shuvalov, O. Y. (2025) · Pharmaceuticals · doi:10.3390/ph18111717 · Cited by 4 · see citing works
Wang, Y., Zhou, T., Bai, S., Wang, S., Wang, Y., Wang, W., Zhou, Y., Tian, J., Qin, X., & Gao, X. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121451 · Cited by 3 · see citing works
Doeven, T., Glenthøj, A. B., Grace, R. F., & van Beers, E. J. (2026) · The Lancet · doi:10.1016/s0140-6736(26)00150-9 · Cited by 4 · see citing works
Suswidiantoro, V., Tang, K. S., Rahman, K., Puteri, M. U., Wahyuni, T., Ariestanti, D. M., James, R. J., Yan, C. C., Kato, M., & Saputri, F. C. (2026) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2026.101248 · Cited by 4 · see citing works
Sun, Y., Jiang, Y., Zhang, Z., An, C., Lyu, Y., Xie, Y. H., Wei, H., Liu, X., Irshad, S., Wang, X., et al. (2026) · Industrial Crops and Products · doi:10.1016/j.indcrop.2026.123205 · Cited by 3 · see citing works
Zhang, W., Wang, Y., Sun, T., Wu, H., Zhao, L., Lu, J., Hu, B., Geng, X., & Chen, G. (2026) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2026.114402 · Cited by 3 · see citing works
Moon, C. Y., Shin, S., Lee, J., Kim, S., Lee, S., & Kang, H. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152488 · Cited by 3 · see citing works
Fortis, S. P., Grier, A., Reisz, J. A., Dzieciątkowska, M., Cendali, F. I., Kauffman, V., Morton, D. H., & D’Alessandro, A. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00166 · Cited by 3 · see citing works
Gupta, P. K., Li, L. Z., Singh, D. K., Nova, S., Arias‐Mendoza, F., Orlovskiy, S., Chawla, S., NELSON, D. S., Farwell, M. D., & Nath, K. (2025) · Academic Radiology · doi:10.1016/j.acra.2025.01.035 · Cited by 2 · see citing works
Mohamed, H., Naz, T., Li, S., Wang, X., Saeed, T., Eltoukhy, A., Khalid, H., Ramadan, A. S., Awad, M. F., Liu, Q., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143998 · Cited by 2 · see citing works
Scheelings, T. F., Kodikara, S., Beale, D. J., Van, T. T. H., Moore, R. J., & Skerratt, L. F. (2025) · Microbial Ecology · doi:10.1007/s00248-025-02556-7 · Cited by 2 · see citing works
Miteva‐Staleva, J., Krumova, E. T., & Angelova, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199308 · Cited by 2 · see citing works
Mishra, D., Saxena, R., Deepak, Yadav, R., & Mishra, D. P. (2025) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2025.104050 · Cited by 2 · see citing works
Yan, X.-L., Huang, Y.-L., Yang, S.-M., Chen, G.-Z., Lin, J.-Q., Guan, Y., Zhu, J.-H., Chen, X.-F., & Li, X. (2025) · Investigative Ophthalmology and Visual Science · doi:10.1167/iovs.66.14.43 · Cited by 2 · see citing works
Jiang, X. Y., Liu, Y., Wang, S., Ke, X., Shang, Q., Li, F., Yu, Z., Xu, L., Tian, X., & Chu, J. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.170722 · Cited by 2 · see citing works
Wei, J., Jiang, J., Li, C., Wang, G., Wulan, J., Yang, H., Shen, F., Ye, D., Li, K., Li, X., et al. (2026) · Chemical Science · doi:10.1039/d5sc08242k · Cited by 2 · see citing works
Metabolism of tumor infiltrating T cells
Ertl, H. C. J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1711328 · Cited by 2 · see citing works
l-Fucose: a dietary sugar with multifaceted potential in the biology and therapy of cancer
Bitaraf, A., Jimenez, M. C., Kakirde, C., & Lau, E. K. (2026) · Nature reviews. Cancer · doi:10.1038/s41568-025-00901-z · Cited by 2 · see citing works
Niu, S.-Q., Li, T., Bao, X.-W., Qian, X.-L., Yang, F., Wu, S., Li, S.-Y., Liang, L.-L., Bai, J., Liu, S.-J., et al. (2026) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2026.111089 · Cited by 2 · see citing works
Dönmez, E. M., Fabrizius, A., & Siebert, U. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1738836 · Cited by 2 · see citing works
A Flawed Conjecture Keeps Haunting Brain Energy Metabolism Research
Schurr, A. (2026) · NeuroSci · doi:10.3390/neurosci7030049 · Cited by 3 · see citing works
Discovery of phage defense systems through component modularity networksPreprint
van den Berg, D. F., Costa, A. R., Esser, J. Q., Muralidharan, A., van den Bossche, H., & Brouns, S. J. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.30.679545 · Cited by 2 · see citing works
The Citric Acid Cycle: Historical Discovery, Biochemical Mechanisms, and Its Impact on Life Sciences
Lan, L. (2025) · Journal of Contemporary Medical Practice · doi:10.53469/jcmp.2025.07(03).37 · Cited by 1 · see citing works
The role of SIRT2 in homeostatic medicine and aging intervention
Li, Y., Han, L., Fu, Y., Zhang, Y., Zou, Z., Luo, J., Tang, X., Tian, L., Lu, Y., Huang, Y., et al. (2025) · Oral Science and Homeostatic Medicine · doi:10.26599/oshm.2025.9610009 · Cited by 1 · see citing works
Heterogeneity in somatic cell nuclear transfer embryo reprogramming across mammalian species
Li, W., Liu, Y., Wang, L., Dilixiati, A., Cheng, Z., Chang, Z., Ma, X., He, Z., Liang, Y., Wang, Y., et al. (2025) · Biology of Reproduction · doi:10.1093/biolre/ioaf133 · Cited by 1 · see citing works
Wen, X., Bou, G., He, Q., Liu, Q., Yi, M., & Ren, H. (2025) · Proteomes · doi:10.3390/proteomes13030033 · Cited by 1 · see citing works
Promotion of HIV clearance by sensitization of HIV reservoirs to cell death
Li, M., Sun, B.-C., Dong, J., Lǐ, J., Minze, L. J., Chen, M., Cheng, C., & Wang, J. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1600741 · Cited by 1 · see citing works
Singh, L. K., & Sharma, B. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147084 · Cited by 1 · see citing works
Enhanced Bacterial Cellulose Production Using Hempseed Meal: Optimal Conditions and Properties
Orpool, S., Kamthai, S., Siriwoharn, T., Khaw-on, P., Deenu, A., & Naruenartwongsakul, S. (2025) · BioTech · doi:10.3390/biotech14030066 · Cited by 1 · see citing works
Yang, S., Wang, Y., Ai, J., Wu, Q., Zang, S., Deng, J., Li, R., Dao, J., Zhang, Z., Zhao, Y., et al. (2025) · Industrial Crops and Products · doi:10.1016/j.indcrop.2025.121834 · Cited by 1 · see citing works
Song, G., Zhao, S., Zhao, K., Liu, R., Hu, C., & van Loosdrecht, M. C. M. (2025) · Resources Conservation and Recycling · doi:10.1016/j.resconrec.2025.108578 · Cited by 1 · see citing works
YY1: Master regulator of metabolic reprogramming in cancer
Akram, R., Hosea, R., Zhao, F., Górecki, A., Figiel, M., Wu, S., & Kasim, V. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189505 · Cited by 1 · see citing works
Chota, A., Sarbadhikary, P., Abrahamse, H., & George, B. P. A. (2025) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.70042 · Cited by 1 · see citing works
Cheng, J., Xiang, L., Wang, Y., Pan, L., Guo, Z., & Lu, S. (2026) · BMC Plant Biology · doi:10.1186/s12870-025-08090-5 · Cited by 1 · see citing works
Kato, H., Yamaoka, I., & Kubota, H. (2026) · npj Systems Biology and Applications · doi:10.1038/s41540-026-00658-7 · Cited by 1 · see citing works
Zou, G., Jiang, Y., Ma, R., Li, S., & Zhang, C. (2026) · Clinical & Translational Oncology · doi:10.1007/s12094-026-04286-9 · Cited by 1 · see citing works
Majumdar, N., Pokharel, B. R., Williams, F., Rajput, S., Cook, P., & Akula, S. M. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07922-8 · Cited by 1 · see citing works
Yao, B.-F., Tan, J.-M., Xing, H.-N., Luo, X., & Peng, J. (2026) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2026.178740 · Cited by 1 · see citing works
Liu, C., Jiang, L., Wang, P., Hu, Y., Zheng, Y., Lu, L., Lü, J., Mao, Y., & Liu, P. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1717779 · Cited by 1 · see citing works
Selective elimination of myeloid HIV reservoirs by targeting pro-survival pathways
Li, M., Sun, B., Minze, L. J., Graviss, E. A., Vasquez, M., Zhao, H., Gelman, B. B., Chen, M., & Wang, J. (2026) · Journal of Infection · doi:10.1016/j.jinf.2026.106733 · Cited by 1 · see citing works
Yang, L., Song, L., Lu, Z., Yao, X., Wang, J., Zeng, Y., Ren, W., Luo, P., & Meng, J. (2026) · Biology · doi:10.3390/biology15080621 · Cited by 1 · see citing works
Park, S., Kim, S., Kim, S.-K., Kim, S.-K., Park, J.-S., Hwang, S., & Kim, S. R. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00486-0 · Cited by 1 · see citing works
Zheng, L., Niu, W., Xie, X.-F., Vu, T., & Du, G.-W. (2026) · Science Advances · doi:10.1126/sciadv.aea8724 · Cited by 1 · see citing works
Excess glucose shapes mitochondrial metabolism and redox state in human primary white adipocytes
Herbers, E., Moisio, K., Torregrosa‐Muñumer, R., Karppinen, J. E., Heinonen, S., van der Kolk, B. W., Hassinen, A., Peltoniemi, H. H., Tuominen, R., Pirinen, E., et al. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.05.321 · Cited by 1 · see citing works
Metabolic Brain Disorders: Prodromes, Symptoms, and Syndromes
Błaszczyk, J. W. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27125190 · Cited by 1 · see citing works
Biotransformation of Microcystin-LR in marine sediments: Mechanism and global potential
Rehman, A., Wang, X., Yousaf, M., Wang, J., & Li, Z. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.142754 · Cited by 1 · see citing works
Álvarez, J. V., Lis-López, L., Rodrigues, D., Pena, C., Bravo, S. B., Díaz-Tomé, V., Cuello-Rodríguez, S., López-Valverde, L., Rodiño‐Janeiro, B. K., Colon, C., et al. (2026) · Drug Delivery and Translational Research · doi:10.1007/s13346-026-02130-9 · Cited by 1 · see citing works
Xiao, N., Yan, H., Xi, Y., Xu, Y., Zhang, J., Li, Z., & Xie, Z. (2026) · Cells · doi:10.3390/cells15121122 · Cited by 1 · see citing works
Papaneophytou, C. P., & Petrou, C. C. (2026) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl49369 · Cited by 1 · see citing works
Singh, H., Purwar, A., & Taliyan, R. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117127 · Cited by 1 · see citing works
Regulation and clinical manifestations of gluconeogenesis dysfunction
Bobok, N. (2026) · npj Metabolic Health and Disease · doi:10.1038/s44324-026-00120-6 · Cited by 1 · see citing works
Sobral, C., Afonso, J., Correia‐Pinto, J., Baltazar, F., & Nogueira-Silva, C. (2026) · Journal of Clinical Medicine · doi:10.3390/jcm15155774 · Cited by 1 · see citing works
Firdaus, Z., Khanal, S., Washington, A. M., Solverson, J. K., Doskey, L. C., Xiao, Y., Yaqubi, M., Pereyra, D., Heimbach, J. K., Taner, T., et al. (2026) · Hepatology · doi:10.1097/hep.0000000000001833 · Cited by 1 · see citing works
Phatak, P. S., Mathivathanan, S., Shah, D., Suresh, I., Shejo, M., Das, S. K., & Varahan, S. (2026) · Genetics · doi:10.1093/genetics/iyag211 · Cited by 1 · see citing works
Albihlal, W. S., Matia‐González, A. M., Schmidt, T., Mayer, W., Bryant, J., Bushell, M., Niessing, D., Barberis, M., Schmidt, A., Heinisch, J. J., et al. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag184 · Cited by 1 · see citing works
Singh, T., Bridgeman, E., Baker, A. J., Noblet, H. A., Yang, K. Y., Kang, S., Lim, K. H., Lee, S. S., Amundsen, N. M., Lee, Y., et al. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107246 · Cited by 1 · see citing works
Zheng, Q., Liu, Y., Li, T., Zhang, X., Geng, Y., Chen, Z., Zhou, J., Fan, W., Wang, Y., Zhang, L., et al. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1871582
“Even under hypoxic conditions, glycolysis remains the predominant pathway for ATP generation in tumor cells (11).”
- 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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