The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Understanding Metabolic Regulation and Its Influence on Cell Physiology
Open accessAbstract
Metabolism impacts all cellular functions and plays a fundamental role in biology. In the last century, our knowledge of metabolic pathway architecture and the genomic landscape of disease has increased exponentially. Combined with these insights, advances in analytical methods for quantifying metabolites and systems approaches to analyze these data now provide powerful tools to study metabolic regulation. Here we review the diverse mechanisms cells use to adapt metabolism to specific physiological states and discuss how metabolic flux analyses can be applied to identify important regulatory nodes to understand normal and pathological cell physiology.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Succinate inhibits HIF-1␣ signaling through inhibition of PHD2 but can also impact the activity of numerous ␣-ketoglutarate-dependent dioxygenases (42,43).”
From Immunoresponsive Gene 1 and Itaconate Inhibit Succinate Dehydrogenase to Modulate Intracellular Succinate Levels (2016) · cites this paper as [43]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836
Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535
Insulin signalling and the regulation of glucose and lipid metabolism
Saltiel, A. R., & Kahn, C. R. (2001) · Nature · doi:10.1038/414799a · Cited by 5,326
Regulation of cancer cell metabolism
Cairns, R. A., Harris, I. S., & Mak, T. W. (2011) · Nature Reviews Cancer · doi:10.1038/nrc2981 · Cited by 4,744
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · cited 1×
“…the hypoxia-inducible factor (HIF) transcription factor complex a subunit is short when oxygen levels are high because the protein is hydroxylated by the EGLN proteins, recognized by the von Hippel Lindau E3 ubiquitin ligase, and targeted for degradation (Ivan et al., 2001; Jaakkola et al., 2001).”
BackgroundCancer-associated IDH1 mutations produce 2-hydroxyglutarate
Dang, L., White, D. W., Gross, S., Bennett, B. D., Bittinger, M. A., Driggers, E. M., Fantin, V. R., Jang, H. G., Jin, S., Keenan, M. C., et al. (2009) · Nature · doi:10.1038/nature08617 · Cited by 4,154
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
Kim, J.-W., Tchernyshyov, I., Semenza, G. L., & Dang, C. V. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.002 · Cited by 3,905
Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333
Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.
Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251 · cited 1×
“M.G.V.H. is supported by the Burroughs Wellcome Fund, the Damon Runyon Cancer Research Foundation, the Smith Family Foundation, and the National Cancer Institute.”
MethodXu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875
Figueroa, M. E., Abdel-Wahab, O., Lu, C., Ward, P. S., Patel, J., Shih, A., Li, Y., Bhagwat, N., Vasanthakumar, A., Fernandez, H. F., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.11.015 · Cited by 2,766
Phosphorylation of ULK1 (hATG1) by AMP-Activated Protein Kinase Connects Energy Sensing to Mitophagy
Egan, D. F., Shackelford, D. B., Mihaylova, M. M., Gelino, S., Kohnz, R. A., Mair, W., Vasquez, D. S., Joshi, A., Gwinn, D. M., Taylor, R., et al. (2011) · Science · doi:10.1126/science.1196371 · Cited by 2,600
A conserved family of prolyl-4-hydroxylases that modify HIF
Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491
HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., & Denko, N. C. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.01.012 · Cited by 2,267
Histone demethylation by a family of JmjC domain-containing proteins
Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,244
The transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation
Wang, R., Dillon, C. P., Shi, L. Z., Milasta, S., Carter, R., Finkelstein, D., McCormick, L. L., Fitzgerald, P., Chi, H., Munger, J., et al. (2011) · Immunity · doi:10.1016/j.immuni.2011.09.021 · Cited by 2,140 · cited 1×
“Although mutant IDH1 activity is significantly lower than that of the wildtype enzyme, the lack of appreciable enzyme capacity to eliminate 2HG causes this metabolite to accumulate to millimolar levels within tumors (Dang et al., 2009; Gross et al., 2010; Ward et al., 2010).”
BackgroundOncogenic Kras maintains pancreatic tumors through regulation of anabolic glucose metabolism
Ying, H., Kimmelman, A. C., Lyssiotis, C. A., Hua, S., Chu, G. C., Fletcher-Sananikone, E., Locasale, J. W., Son, J., Zhang, H., Coloff, J. L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.01.058 · Cited by 2,043
Ward, P. S., Patel, J., Wise, D. R., Abdel-Wahab, O., Bennett, B. D., Coller, H. A., Cross, J. R., Fantin, V. R., Hedvat, C. V., Perl, A. E., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.01.020 · Cited by 2,020
TIGAR, a p53-Inducible Regulator of Glycolysis and Apoptosis
Bensaad, K., Tsuruta, A., Selak, M. A., Vidal, M. N. C., Nakano, K., Bartrons, R., Gottlieb, E., & Vousden, K. H. (2006) · Cell · doi:10.1016/j.cell.2006.05.036 · Cited by 2,019
IDH mutation impairs histone demethylation and results in a block to cell differentiation
Lu, C., Ward, P. S., Kapoor, G. S., Rohle, D., Turcan, S., Abdel-Wahab, O., Edwards, C. R., Khanin, R., Figueroa, M. E., Melnick, A., et al. (2012) · Nature · doi:10.1038/nature10860 · Cited by 1,985
Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
Chandel, N. S., Maltepe, E., Goldwasser, E., Mathieu, C. E., Simon, M. C., & Schumacker, P. T. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.20.11715 · Cited by 1,926
Regulation of cellular metabolism by protein lysine acetylation
Zhao, S., Xu, W., Jiang, W., Yu, W., Lin, Y., Zhang, T., Yao, J., Zhou, L., Zeng, Y., Li, H., et al. (2010) · Science · doi:10.1126/science.1179689 · Cited by 1,910
Li, Y., Xu, S., Mihaylova, M. M., Zheng, B., Hou, X., Jiang, B., Park, O., Luo, Z., Lefai, É., Shyy, J. Y.-J., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.009 · Cited by 1,840
Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
Metallo, C. M., Gameiro, P. A., Bell, E. L., Mattaini, K. R., Yang, J., Hiller, K., Jewell, C. M., Johnson, Z. R., Irvine, D. J., Guarente, L., et al. (2012) · Nature · doi:10.1038/nature10602 · Cited by 1,791
Self-citationAMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638
Growth factor regulation of autophagy and cell survival in the absence of apoptosis
Lum, J. J., Bauer, D. E., Kong, M., Harris, M. H., Li, C., Lindsten, T., & Thompson, C. B. (2005) · Cell · doi:10.1016/j.cell.2004.11.046 · Cited by 1,487
Nrf2 Redirects Glucose and Glutamine into Anabolic Pathways in Metabolic Reprogramming
Mitsuishi, Y., Taguchi, K., Kawatani, Y., Shibata, T., Nukiwa, T., Aburatani, H., Yamamoto, M., & Motohashi, H. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.05.016 · Cited by 1,395 · cited 5×
“Multiple Regulatory Events Converge on the Oxidative Pentose Phosphate Pathway The oxidative pentose phosphate pathway (PPP; red arrows) generates NADPH to maintain reduced glutathione, combat reactive oxygen species (ROS), and maintain redox homeostasis.”
BackgroundInfluentialReductive carboxylation supports growth in tumour cells with defective mitochondria
Mullen, A. R., Wheaton, W. W., Jin, E. S., Chen, P.-H., Sullivan, L. B., Cheng, T., Yang, Y., Linehan, W. M., Chandel, N. S., & DeBerardinis, R. J. (2012) · Nature · doi:10.1038/nature10642 · Cited by 1,328
Anastasiou, D., Poulogiannis, G., Asara, J. M., Boxer, M. B., Jiang, J., Shen, M., Bellinger, G., Sasaki, A. T., Locasale, J. W., Auld, D. S., et al. (2011) · Science · doi:10.1126/science.1211485 · Cited by 1,218
Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes & Development · doi:10.1101/gad.191056.112 · Cited by 1,188 · cited 1×
“Succinate and fumarate abundances increase with oncogenic loss-of-function mutations in the TCA cycle enzymes SDH and FH, and both metabolites can affect dioxygenase activity (Xiao et al., 2012).”
BackgroundGlucose-Independent Glutamine Metabolism via TCA Cycling for Proliferation and Survival in B Cells
Le, A., Lane, A. N., Hamaker, M., Bose, S., Gouw, A., Barbi, J., Tsukamoto, T., Rojas, C. J., Slusher, B. S., Zhang, H., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.12.009 · Cited by 1,095
The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
Chowdhury, R., Yeoh, K. K., Tian, Y., Hillringhaus, L., Bagg, E. A., Rose, N. R., Leung, I. K. H., Li, X. S., Woon, E. C. Y., Yang, M., et al. (2011) · The EMBO Reports · doi:10.1038/embor.2011.43 · Cited by 1,035
Wise, D. R., Ward, P. S., Shay, J. E. S., Cross, J. R., Gruber, J. J., Sachdeva, U. M., Platt, J. M., DeMatteo, R. G., Simon, M. C., & Thompson, C. B. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1117773108 · Cited by 975
Nature and Development of Lactic Dehydrogenases
Cahn, R. D., Zwilling, E., Kaplan, N. O., & Levine, L. (1962) · Science · doi:10.1126/science.136.3520.962 · Cited by 943
Cellular Metabolism and Disease: What Do Metabolic Outliers Teach Us?
DeBerardinis, R. J., & Thompson, C. B. (2012) · Cell · doi:10.1016/j.cell.2012.02.032 · Cited by 858
A Mitochondrial Pyruvate Carrier Required for Pyruvate Uptake in Yeast, Drosophila , and Humans
Bricker, D. K., Taylor, E. B., Schell, J. C., Orsak, T., Boutron, A., Chen, Y.-C., Cox, J. E., Cardon, C. M., Van Vranken, J. G., Dephoure, N., et al. (2012) · Science · doi:10.1126/science.1218099 · Cited by 843
p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
Jiang, P., Du, W., Wang, X., Mancuso, A., Gao, X., Wu, M., & Yang, X. (2011) · Nature Cell Biology · doi:10.1038/ncb2172 · Cited by 834
Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis
Anastasiou, D., Yu, Y., Israelsen, W. J., Jiang, J.-K., Boxer, M. B., Hong, B. S., Tempel, W., Dimov, S., Shen, M., Jha, A., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1060 · Cited by 816
Self-citationTransport of Energy in Muscle: The Phosphorylcreatine Shuttle
Bessman, S. P., & Geiger, P. J. (1981) · Science · doi:10.1126/science.6450446 · Cited by 758
Identification and Functional Expression of the Mitochondrial Pyruvate Carrier
Herzig, S., Raemy, E., Montessuit, S., Veuthey, J.-L., Zamboni, N., Westermann, B., Kunji, E. R. S., & Martinou, J.-C. (2012) · Science · doi:10.1126/science.1218530 · Cited by 747
Gross, S., Cairns, R. A., Minden, M. D., Driggers, E. M., Bittinger, M. A., Jang, H. G., Sasaki, M., Jin, S., Schenkein, D. P., Su, S. M., et al. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20092506 · Cited by 736
Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation
Koivunen, P., Lee, S., Duncan, C. G., Lopez, G., Lu, G., Ramkissoon, S., Losman, J. A., Joensuu, P., Bergmann, U., Gross, S., et al. (2012) · Nature · doi:10.1038/nature10898 · Cited by 727
Ayala, J. E., Samuel, V. T., Morton, G. J., Obici, S., Croniger, C. M., Shulman, G. I., Wasserman, D. H., & McGuinness, O. P. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.006239 · Cited by 722
Phosphofructokinase 1 Glycosylation Regulates Cell Growth and Metabolism
Yi, W., Clark, P. M., Mason, D. E., Keenan, M. C., Hill, C., Goddard, W. A., Peters, E. C., Driggers, E. M., & Hsieh‐Wilson, L. C. (2012) · Science · doi:10.1126/science.1222278 · Cited by 696
Metabolic networks in motion: 13C‐based flux analysis
Sauer, U. (2006) · Molecular Systems Biology · doi:10.1038/msb4100109 · Cited by 681
Sunny, N. E., Parks, E. J., Browning, J. D., & Burgess, S. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.11.004 · Cited by 672
Evidence for an Alternative Glycolytic Pathway in Rapidly Proliferating Cells
Heiden, M. G. V., Locasale, J. W., Swanson, K. D., Sharfi, H., Heffron, G. J., Amador‐Noguez, D., Christofk, H. R., Wagner, G., Rabinowitz, J. D., Asara, J. M., et al. (2010) · Science · doi:10.1126/science.1188015 · Cited by 648
Munger, J. C., Bennett, B. D., Parikh, A., Feng, X., McArdle, J., RABITZ, H. A., Shenk, T. E., & Rabinowitz, J. D. (2008) · Nature Biotechnology · doi:10.1038/nbt.1500 · Cited by 641
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
Marin-Valencia, I., Yang, C., Mashimo, T., Cho, S., Baek, H., Yang, X.-L., Rajagopalan, K. N., Maddie, M., Vemireddy, V., Zhao, Z., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.05.001 · Cited by 529
IDH1(R132H) mutation increases murine haematopoietic progenitors and alters epigenetics
Sasaki, M., Knobbe, C. B., Munger, J. C., Lind, E. F., Brenner, D., Brüstle, A., Harris, I. S., Holmes, R., Wakeham, A., Haight, J., et al. (2012) · Nature · doi:10.1038/nature11323 · Cited by 513
Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
Hung, Y. P., Albeck, J. G., Tantama, M., & Yellen, G. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.08.012 · Cited by 509
Determination of confidence intervals of metabolic fluxes estimated from stable isotope measurements
Antoniewicz, M. R., Kelleher, J. K., & Stephanopoulos, G. N. (2006) · Metabolic Engineering · doi:10.1016/j.ymben.2006.01.004 · Cited by 451
Fan, T. W. ‐., Lane, A. N., Higashi, R. M., Farag, M. A., Gao, H. T., Bousamra, M., & Miller, D. M. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-41 · Cited by 438
Selective distribution of lactate dehydrogenase isoenzymes in neurons and astrocytes of human brain
Bittar, P. G., Charnay, Y., Pellerin, L., Bouras, C., & Magistretti, P. J. (1996) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199611000-00001 · Cited by 423
Itaconic acid is a mammalian metabolite induced during macrophage activation
Strelko, C. L., Lu, W., Dufort, F. J., Seyfried, T. N., Chiles, T. C., Rabinowitz, J. D., & Roberts, M. F. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2070889 · Cited by 391
Stromal control of cystine metabolism promotes cancer cell survival in chronic lymphocytic leukaemia
Zhang, W., Trachootham, D., Liu, J., Chen, G., Pelicano, H., Garcı́a-Prieto, C., Lu, W., Burger, J. A., Croce, C. M., Plunkett, W. K., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2432 · Cited by 364
Comparative Metabolic Flux Profiling of Melanoma Cell Lines
Scott, D. A., Richardson, A. D., Filipp, F. V., Knutzen, C. A., Chiang, G. G., Ronai, Z. A., Osterman, A. L., & Smith, J. W. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.282046 · Cited by 328
Cellular concentrations of enzymes and their substrates
Albe, K. R., Butler, M. H., & Wright, B. E. (1990) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(05)80266-8 · Cited by 318
AMPK: Lessons from transgenic and knockout animals
Viollet, B. (2009) · Frontiers in bioscience · doi:10.2741/3229 · Cited by 314
Roodhart, J. M. L., Daenen, L. G. M., Stigter, E. C. A., Prins, H.-J., Gerrits, J., Houthuijzen, J. M., Gerritsen, M. G., Schipper, H. S., Backer, M. J. G., van Amersfoort, M., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.08.010 · Cited by 305
Sasaki, M., Knobbe, C. B., Itsumi, M., Elia, A. J., Harris, I. S., Chio, I. I. C., Cairns, R. A., McCracken, S., Wakeham, A., Haight, J., et al. (2012) · Genes & Development · doi:10.1101/gad.198200.112 · Cited by 296
Evaluation of 13C isotopic tracers for metabolic flux analysis in mammalian cells
Metallo, C. M., Walther, J. L., & Stephanopoulos, G. (2009) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2009.07.010 · Cited by 280
6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE: A METABOLIC SIGNALING ENZYME
Pilkis, S. J., Claus, T. H., Kurland, I. J., & Lange, A. J. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.004055 · Cited by 278
Kung, H.-N., Marks, J. R., & Chi, J.-T. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002229 · Cited by 277
Roche, T. E., & Hiromasa, Y. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-6380-z · Cited by 265
The regulation of the release of ketone bodies by the liver
Krebs, H. A. (1966) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(66)90027-6 · Cited by 259
Choo, A. Y., Kim, S. G., Heiden, M. G. V., Mahoney, S. J., Vu, H., Yoon, S.-O., Cantley, L. C., & Blenis, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.007 · Cited by 258
Tumor imaging using hyperpolarized 13 C magnetic resonance spectroscopy
Brindle, K. M., Bohndiek, S. E., Gallagher, F. A., & Kettunen, M. I. (2011) · Magnetic Resonance in Medicine · doi:10.1002/mrm.22999 · Cited by 252
Jacobus, W. E. (1985) · Annual Review of Physiology · doi:10.1146/annurev.ph.47.030185.003423 · Cited by 246
Muscle Amino Acid Metabolism and Gluconeogenesis
Ruderman, N. B. (1975) · Annual Review of Medicine · doi:10.1146/annurev.me.26.020175.001333 · Cited by 217
Metabolic flux analysis in mammalian cell culture
Quek, L., Dietmair, S., Krömer, J. O., & Nielsen, L. K. (2009) · Metabolic Engineering · doi:10.1016/j.ymben.2009.09.002 · Cited by 216
R�os, S., Santos, C. R., Moco, S., Baenke, F., Kelly, G. P., Howell, M. T., Zamboni, N., & Schulze, A. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-11-0234 · Cited by 201
Olsen, C. P., & Gilst, M. R. V. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.08.007 · Cited by 193
Mass isotopomer study of the nonoxidative pathways of the pentose cycle with [1,2-13C2]glucose
Lee, W. P., Boros, L. G., Puigjaner, J., Bassilian, S., Lim, S. K., & Cascante, M. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.274.5.e843 · Cited by 183
Use of 2H2O for estimating rates of gluconeogenesis. Application to the fasted state.
Landau, B. R., Wahren, J., Chandramouli, V., Schumann, W. C., Ekberg, K., & Kalhan, S. C. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117635 · Cited by 173
Consoli, A., Kennedy, F., Miles, J., & Gerich, J. (1987) · Journal of Clinical Investigation · doi:10.1172/jci113206 · Cited by 170
Endocrine Control of Metabolism
Randle, P. J. (1963) · Annual Review of Physiology · doi:10.1146/annurev.ph.25.030163.001451 · Cited by 164
13C metabolic flux analysis in complex systems
Zamboni, N. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.08.009 · Cited by 156
Merritt, M. E., Harrison, C. E., Sherry, A. D., Malloy, C. R., & Burgess, S. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111247108 · Cited by 150
Dzeja, P. P., Zeleznikar, R. J., & Goldberg, N. D. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_13 · Cited by 137
Dzeja, P. P., Zeleznikar, R. J., & Goldberg, N. D. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006859632730 · Cited by 135
Reactivating HIF prolyl hydroxylases under hypoxia results in metabolic catastrophe and cell death
Tennant, D. A., Frezza, C., MacKenzie, E. D., Nguyen, Q., Zheng, L., Selak, M. A., Roberts, D. L., Dive, C., Watson, D. G., Aboagye, E. O., et al. (2009) · Oncogene · doi:10.1038/onc.2009.250 · Cited by 122
Isotopomer studies of gluconeogenesis and the Krebs cycle with 13C-labeled lactate.
Katz, J. J., Wals, P. A., & Lee, W. N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74421-4 · Cited by 118
Boros, L. G., Lee, P. W. N., Brandes, J. L., Cascante, M., Muscarella, P., Schirmer, W. J., Melvin, W. S., & Ellison, E. C. (1998) · Medical Hypotheses · doi:10.1016/s0306-9877(98)90178-5 · Cited by 111
Maier, K., Hofmann, U., Reuß, M., & Mauch, K. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21746 · Cited by 97
Hellerstein, M. K. (2004) · Metabolic Engineering · doi:10.1016/j.ymben.2003.10.005 · Cited by 96
Isotopically nonstationary 13C flux analysis of Myc-induced metabolic reprogramming in B-cells
Murphy, T. A., Dang, C. V., & Young, J. D. (2012) · Metabolic Engineering · doi:10.1016/j.ymben.2012.07.008 · Cited by 92
Allosteric Properties of Skeletal Muscle Pyruvate Kinase
Carminatti, H., de Asúa, L. J., Leiderman, B., & Rozengurt, E. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45884-5 · Cited by 83
Regulation of pentose phosphate pathway dehydrogenases by NADP+/NADPH ratios
Holten, D. D., Procsal, D. A., & Chang, H.-L. (1976) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(76)91164-5 · Cited by 80
Newsholme, P. (1979) · Journal of Molecular and Cellular Cardiology · doi:10.1016/0022-2828(79)90480-2 · Cited by 77
Liang, Y. T., Buettger, C. W., Berner, D. K., & Matschinsky, F. M. (1997) · Diabetologia · doi:10.1007/s001250050783 · Cited by 71
Khairallah, M., Labarthe, F., Bouchard, B., Danialou, G., Petrof, B. J., & Rosiers, C. D. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00942.2003 · Cited by 67
Holleran, A. L., Briscoe, D. A., Fiskum, G., & Kelleher, J. K. (1995) · Molecular and Cellular Biochemistry · doi:10.1007/bf01076071 · Cited by 53
Zonation of acetate labeling across the liver: implications for studies of lipogenesis by MIDA
Puchowicz, M. A., Bederman, I. R., Comte, B., Yang, D., David, F., Stone, E. C., Jabbour, K., Wasserman, D. H., & Brunengraber, H. (1999) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1999.277.6.e1022 · Cited by 42
Pentose cycle activity in muscle from fetal, neonatal and infant rhesus monkeys
Beatty, C. H., Basinger, G. M., & Bocek, R. M. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90413-9 · Cited by 26
Insulin and muscle amino acid balance
Cahill, G. F., Aoki, T. T., Brennan, M. F., & Müller, W. (1972) · Proceedings of The Nutrition Society · doi:10.1079/pns19720042 · Cited by 21
Flagged first, then by citations
Cited by
Sorted by citations
Metabolomics: beyond biomarkers and towards mechanisms
Johnson, C. H., Ivanisevic, J., & Siuzdak, G. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.25 · Cited by 2,829
Identification of bioactive metabolites using activity metabolomics
Rinschen, M. M., Ivanisevic, J., Giera, M., & Siuzdak, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0108-4 · Cited by 1,008
Moussaieff, A., Rouleau, M., Kitsberg, D., Cohen, M., Levy, G., Barasch, D., Nemirovski, A., Shen-Orr, S., Laevsky, I., Amit, M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.002 · Cited by 666
A roadmap for interpreting 13C metabolite labeling patterns from cells
Buescher, J. M., Antoniewicz, M. R., Boros, L. G., Burgess, S. C., Brunengraber, H., Clish, C. B., DeBerardinis, R. J., Féron, O., Frezza, C., Ghesquière, B., et al. (2015) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2015.02.003 · Cited by 644
Tracing compartmentalized NADPH metabolism in the cytosol and mitochondria of mammalian cells
Lewis, C. A., Parker, S. J., Fiske, B. P., McCloskey, D., Gui, D. Y., Green, C. R., Vokes, N. I., Feist, A. M., Vander Heiden, M. G., & Metallo, C. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.008 · Cited by 562
Metadata
- Authors
- Metallo, C. M., & Vander Heiden, M. G.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Metallo, Christian M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2013-02
- Volume
- 49
- Issue
- 3
- Pages
- 388-398
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3569837
- OpenAlex
- W2024399152
- Cited by
- 367
- References
- 100
- Citations by year
- 2026: 26 · 2025: 39 · 2024: 36 · 2023: 24 · 2022: 25 · 2021: 37 · 2020: 35 · 2019: 31 · 2018: 25 · 2017: 16 · 2016: 19 · 2015: 24 · 2014: 23 · 2013: 6
- FWCI
- 2.26
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc)
- Funders
- American Cancer Society (70-002)
- Damon Runyon Cancer Research Foundation
- Richard and Susan Smith Family Foundation
- Burroughs Wellcome Fund
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- metabolic regulation, cell physiology, metabolic flux analysis, metabolic adaptation, metabolite quantification, metabolic disorders
- MeSH terms
- Animals, Cell Physiological Phenomena, Cells, Glycolysis, Humans, Models, Biological, Metabolic Networks and Pathways
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review