Tracing compartmentalized NADPH metabolism in the cytosol and mitochondria of mammalian cells

Cancer-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 · 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

Association of reactive oxygen species levels and radioresistance in cancer stem cells

Diehn, M., Cho, R. W., Lobo, N. A., Kalisky, T., Dorie, M. J., Kulp, A. N., Qian, D., Lam, J. S., Ailles, L. E., Wong, M., et al. (2009) · Nature · doi:10.1038/nature07733 · Cited by 2,555 · see citing works

The Common Feature of Leukemia-Associated IDH1 and IDH2 Mutations Is a Neomorphic Enzyme Activity Converting α-Ketoglutarate to 2-Hydroxyglutarate

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 · cited 2× · see citing works

Glutamine supports pancreatic cancer growth through a KRAS-regulated metabolic pathway

Son, J., Lyssiotis, C. A., Ying, H., Wang, X., Hua, S., Ligorio, M., Perera, R. M., Ferrone, C. R., Mullarky, E., Shyh-Chang, N., et al. (2013) · Nature · doi:10.1038/nature12040 · Cited by 1,990 · see citing works

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 · see citing works

Metabolite profiling identifies a key role for glycine in rapid cancer cell proliferation

Jain, M., Nilsson, R., Sharma, S., Madhusudhan, N., Kitami, T., Souza, A. L., Kafri, R., Kirschner, M. W., Clish, C. B., & Mootha, V. K. (2012) · Science · doi:10.1126/science.1218595 · Cited by 1,403 · see citing works

Bcl-xL Regulates the Membrane Potential and Volume Homeostasis of Mitochondria

Heiden, M. G. V., Chandel, N. S., Williamson, E. K., Schumacker, P. T., & Thompson, C. B. (1997) · Cell · doi:10.1016/s0092-8674(00)80450-x · Cited by 1,378 · see citing works

AMPK regulates NADPH homeostasis to promote tumour cell survival during energy stress

Jeon, S.-M., Chandel, N. S., & Hay, N. (2012) · Nature · doi:10.1038/nature11066 · Cited by 1,132 · see citing works

Antioxidant and oncogene rescue of metabolic defects caused by loss of matrix attachment

Schafer, Z. T., Grassian, A. R., Song, L., Jiang, Z., Gerhart-Hines, Z., Irie, H. Y., Gao, S., Puigserver, P., & Brugge, J. S. (2009) · Nature · doi:10.1038/nature08268 · Cited by 1,031 · see citing works

Hypoxia promotes isocitrate dehydrogenase-dependent carboxylation of α-ketoglutarate to citrate to support cell growth and viability

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 · see citing works

The power to reduce: pyridine nucleotides—small molecules with a multitude of functions

Pollak, N., Dölle, C., & Ziegler, M. (2007) · Biochemical Journal · doi:10.1042/bj20061638 · Cited by 730 · see citing works

Compartmentalization of Mammalian Folate-Mediated One-Carbon Metabolism

Tibbetts, A. S., & Appling, D. R. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104810 · Cited by 692 · cited 16× · see citing works

Metabolite Transport in Mitochondria

LaNoue, K. F., & Schoolwerth, A. C. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004255 · Cited by 622 · see citing works

Metabolic enzyme expression highlights a key role for MTHFD2 and the mitochondrial folate pathway in cancer

Nilsson, R., Jain, M., Madhusudhan, N., Sheppard, N. G., Strittmatter, L., Kampf, C., Huang, J., Asplund, A., & Mootha, V. K. (2014) · Nature Communications · doi:10.1038/ncomms4128 · Cited by 607 · see citing works

Reciprocal regulation of p53 and malic enzymes modulates metabolism and senescence

Jiang, P., Du, W., Mancuso, A., Wellen, K. E., & Yang, X. (2013) · Nature · doi:10.1038/nature11776 · Cited by 491 · see citing works

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 · see citing works

INCA: a computational platform for isotopically non-stationary metabolic flux analysis

Young, J. D. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btu015 · Cited by 398 · see citing works

Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia

Kikuchi, G., Motokawa, Y., Yoshida, T., & Hiraga, K. (2008) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.84.246 · Cited by 381 · see citing works

Understanding metabolic regulation and its influence on cell physiology

Metallo, C. M., & Vander Heiden, M. G. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.018 · Cited by 367 · see citing works

Reductive glutamine metabolism is a function of the α-ketoglutarate to citrate ratio in cells

Fendt, S.-M., Bell, E. L., Keibler, M. A., Olenchock, B. A., Mayers, J. R., Wasylenko, T. M., Vokes, N. I., Guarente, L., Heiden, M. G. V., & Stephanopoulos, G. (2013) · Nature Communications · doi:10.1038/ncomms3236 · Cited by 364 · see citing works

A single lentiviral vector platform for microRNA-based conditional RNA interference and coordinated transgene expression

Shin, K.-J., Wall, E. A., Zavzavadjian, J. R., Santat, L. A., Liu, J., Hwang, J., Rebres, R. A., Roach, T. I. A., Seaman, W. E., Simon, M. I., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606179103 · Cited by 332 · see citing works

Pathways and Subcellular Compartmentation of NAD Biosynthesis in Human Cells

Nikiforov, A., Dölle, C., Niere, M., & Ziegler, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213298 · Cited by 326 · see citing works

Futile Cycles in the Metabolism of Glucose

Katz, J. J., & Rognstad, R. (1976) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152810-2.50013-9 · Cited by 324 · see citing works

High Precision Isotope Ratio Monitoring Techniques in Mass Spectrometry

Brand, W. A. (1996) · Journal of Mass Spectrometry · doi:10.1002/(sici)1096-9888(199603)31:3 · Cited by 299 · see citing works

The Pentose Cycle, Triose Phosphate Isomerization, and Lipogenesis in Rat Adipose Tissue

Katz, J. J., Landau, B. R., & Bartsch, G. E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96899-7 · Cited by 280 · see citing works

IDH1 mutations alter citric acid cycle metabolism and increase dependence on oxidative mitochondrial metabolism

Grassian, A. R., Parker, S. J., Davidson, S. M., Divakaruni, A. S., Green, C. R., Zhang, X., Slocum, K. L., Pu, M., Lin, F., Vickers, C., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-0772-t · Cited by 280 · see citing works

Contribution of serine, folate and glycine metabolism to the ATP, NADPH and purine requirements of cancer cells

Tedeschi, P. M., Markert, E. K., Gounder, M. K., Lin, H., Dvorzhinski, D., Dolfi, S. C., Chan, L. L.-Y., Qiu, J., DiPaola, R. S., Hirshfield, K. M., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.393 · Cited by 261 · see citing works

Proton‐translocating transhydrogenase and NAD‐ and NADP‐linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria

Sazanov, L. A., & Jackson, J. B. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00370-x · Cited by 205 · see citing works

NAD Kinase Levels Control the NADPH Concentration in Human Cells

Pollak, N., Niere, M., & Ziegler, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704442200 · Cited by 197 · see citing works

Identification of a de novo thymidylate biosynthesis pathway in mammalian mitochondria

Anderson, D. D., Quintero, C. M., & Stover, P. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103623108 · Cited by 186 · see citing works

The Potential for Isocitrate Dehydrogenase Mutations to Produce 2-Hydroxyglutarate Depends on Allele Specificity and Subcellular Compartmentalization

Ward, P. S., Lü, C., Cross, J. R., Abdel-Wahab, O. I., Levine, R. L., Schwartz, G. K., & Thompson, C. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.435495 · Cited by 181 · see citing works

Doxycycline Alters Metabolism and Proliferation of Human Cell Lines

Ahler, E., Sullivan, W. J., Cass, A. A., Braas, D., York, A. G., Bensinger, S. J., Graeber, T. G., & Christofk, H. R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064561 · Cited by 170 · see citing works

Biochemistry of Cultured Mammalian Cells

Levintow, L., & Eagle, H. (1961) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.30.070161.003133 · Cited by 129 · see citing works

Evidence for electrogenic aspartate transport in rat liver mitochondria

LaNoue, K. F., Meijer, A. J., & Brouwer, A. (1974) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(74)90337-3 · Cited by 113 · see citing works

In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units.

Barlowe, C. K., & Appling, D. R. (1988) · PubMed · Cited by 110 · see citing works

Stereospecificity for Nicotinamide Nucleotides in Enzymatic and Chemical Hydride Transfer Reaction

You, K.-S., & Oppenheimer, N. J. (1985) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238509113625 · Cited by 104 · see citing works

Transfer of reducing equivalents into mitochondria by the interconversions of proline and Δ1-pyrroline-5-carboxylate

Hagedorn, C. H., & Phang, J. M. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90010-3 · Cited by 91 · see citing works

Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase

Rendina, A. R., Hermes, J. D., & Cleland, W. W. (1984) · Biochemistry · doi:10.1021/bi00320a056 · Cited by 67 · see citing works

Glycoconjugates as noninvasive probes of intrahepatic metabolism: pathways of glucose entry into compartmentalized hepatic UDP-glucose pools during glycogen accumulation.

Hellerstein, M. K., Greenblatt, D. J., & Munro, H. N. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.18.7044 · Cited by 66 · see citing works

13C-flux Analysis Reveals NADPH-balancing Transhydrogenation Cycles in Stationary Phase of Nitrogen-starving Bacillus subtilis

Rühl, M., Coq, D. L., Aymerich, S., & Sauer, U. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366492 · Cited by 62 · see citing works

Isotopomer spectral analysis of triglyceride fatty acid synthesis in 3T3-L1 cells

Kharroubi, A., Masterson, T. M., Aldaghlas, T., Kennedy, K. A., & Kelleher, J. K. (1992) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1992.263.4.e667 · Cited by 62 · see citing works

Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1- 13 C]-Glycolaldehyde in D 2 O

Go, M. K., Amyes, T. L., & Richard, J. P. (2009) · Biochemistry · doi:10.1021/bi900636c · Cited by 58 · see citing works

Effect of vitamin B6 availability on serine hydroxymethyltransferase in MCF-7 cells

Perry, C. A., Yu, S., Chen, J., Matharu, K., & Stover, P. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.005 · Cited by 56 · see citing works

Isotope Discrimination Effects in the Metabolism of Tritiated Glucose

Katz, J. J., Rognstad, R., & Kemp, R. G. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97600-3 · Cited by 53 · see citing works

Hexose-6-phosphate dehydrogenase: linking endocrinology and metabolism in the endoplasmic reticulum

Bánhegyi, G., Csala, M., & Benedetti, A. (2008) · Journal of Molecular Endocrinology · doi:10.1677/jme-08-0156 · Cited by 49 · see citing works

Modeling cellular compartmentation in one‐carbon metabolism

Scotti, M., Stella, L., Shearer, E. J., & Stover, P. J. (2013) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1209 · Cited by 46 · see citing works

Futile cycling in glucose metabolism

Katz, J. J., & Rognstad, R. (1978) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(78)90980-5 · Cited by 44 · see citing works

Maintenance of luminal NADPH in the endoplasmic reticulum promotes the survival of human neutrophil granulocytes

Kardon, T., Senesi, S., Marcolongo, P., Legeza, B., Bánhegyi, G., Mandl, J., Fulceri, R., & Benedetti, A. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.045 · Cited by 28 · see citing works

IDH1 and IDH2 have critical roles in 2-hydroxyglutarate production in D-2-hydroxyglutarate dehydrogenase depleted cells

Matsunaga, H., Futakuchi-Tsuchida, A., Takahashi, M., ISHIKAWA, T., Tsuji, M., & Ando, O. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.002 · Cited by 28 · see citing works

Altered redox state of luminal pyridine nucleotides facilitates the sensitivity towards oxidative injury and leads to endoplasmic reticulum stress dependent autophagy in HepG2 cells

Száraz, P., Bánhegyi, G., & Benedetti, A. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.10.004 · Cited by 25 · see citing works

Metabolic loss of deuterium from isotopically labeled glucose

Ben‐Yoseph, O., Kingsley, P. B., & Ross, B. D. (1994) · Magnetic Resonance in Medicine · doi:10.1002/mrm.1910320317 · Cited by 24 · see citing works

Glycerol Phosphate Shuttle in Virus-Transformed Cells in Culture

Bissell, M. J., Rambeck, W., White, R. C., & Bassham, J. A. (1976) · Science · doi:10.1126/science.175441 · Cited by 22 · see citing works

Fundamentals of Cancer Metabolism

DeBerardinis, R. J., & Chandel, N. S. (2016) · Science Advances · doi:10.1126/sciadv.1600200 · Cited by 3,013 · see citing works

One-Carbon Metabolism in Health and Disease

Ducker, G. S., & Rabinowitz, J. D. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2016.08.009 · Cited by 2,239 · see citing works

Understanding the Intersections between Metabolism and Cancer Biology

Heiden, M. G. V., & DeBerardinis, R. J. (2017) · Cell · doi:10.1016/j.cell.2016.12.039 · Cited by 2,316 · see citing works

The PI3K–AKT network at the interface of oncogenic signalling and cancer metabolism

Hoxhaj, G., & Manning, B. D. (2020) · Nature Reviews Cancer · doi:10.1038/s41568-019-0216-7 · Cited by 2,137 · see citing works

The multifaceted contributions of mitochondria to cellular metabolism

Spinelli, J. B., & Haigis, M. C. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0124-1 · Cited by 1,935 · see citing works

The return of metabolism: biochemistry and physiology of the pentose phosphate pathway

Stincone, A., Prigione, A., Cramer, T., Wamelink, M. M. C., Campbell, K., Cheung, E., Olin‐Sandoval, V., Grüning, N., Krüger, A., Tauqeer Alam, M., et al. (2015) · Biological Reviews · doi:10.1111/brv.12140 · Cited by 1,576 · see citing works

Mitochondrial ROS in cancer: initiators, amplifiers or an Achilles' heel?

Sabharwal, S. S., & Schumacker, P. T. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3803 · Cited by 1,643 · see citing works

The role of ROS in tumour development and progression

Cheung, E. C., & Vousden, K. H. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-021-00435-0 · Cited by 1,622 · see citing works

Metabolic pathways promoting cancer cell survival and growth

Boroughs, L. K., & DeBerardinis, R. J. (2015) · Nature Cell Biology · doi:10.1038/ncb3124 · Cited by 1,459 · see citing works

Targeting mitochondria metabolism for cancer therapy

Weinberg, S. E., & Chandel, N. S. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1712 · Cited by 1,385 · see citing works

Oxidative stress inhibits distant metastasis by human melanoma cells

Piskounova, E., Agathocleous, M., Murphy, M. M., Hu, Z., Huddlestun, S. E., Zhao, Z., Leitch, A. M., Johnson, T. M., DeBerardinis, R. J., & Morrison, S. J. (2015) · Nature · doi:10.1038/nature15726 · Cited by 1,269 · see citing works

Supporting aspartate biosynthesis is an essential function of respiration in proliferating cells

Sullivan, L. B., Gui, D. Y., Hosios, A. M., Bush, L. N., Freinkman, E., & Vander Heiden, M. G. (2015) · Cell · doi:10.1016/j.cell.2015.07.017 · Cited by 1,173 · see citing works

ROS homeostasis and metabolism: a dangerous liason in cancer cells

Panieri, E., & Santoro, M. M. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.105 · Cited by 1,156 · see citing works

Reprogramming glucose metabolism in cancer: can it be exploited for cancer therapy?

Hay, N. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.77 · Cited by 1,123 · see citing works

Targeting Metabolism for Cancer Therapy

Luengo, A., Gui, D. Y., & Vander Heiden, M. G. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.08.028 · Cited by 971 · see citing works

Serine and one-carbon metabolism in cancer

Yang, M., & Vousden, K. H. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.81 · Cited by 992 · see citing works

Regulation of mammalian nucleotide metabolism and biosynthesis

Lane, A. N., & Fan, T. W.-M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv047 · Cited by 959 · see citing works

mTORC1 induces purine synthesis through control of the mitochondrial tetrahydrofolate cycle

Ben-Sahra, I., Hoxhaj, G., Ricoult, S. J. H., Asara, J. M., & Manning, B. D. (2016) · Science · doi:10.1126/science.aad0489 · Cited by 795 · see citing works

Metabolomics and Isotope Tracing

Jang, C., Chen, L., & Rabinowitz, J. D. (2018) · Cell · doi:10.1016/j.cell.2018.03.055 · Cited by 841 · see citing works

Nrf2, the Master Regulator of Anti-Oxidative Responses

Vomund, S., Schäfer, A., Parnham, M., Brüne, B., & Von Knethen, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122772 · Cited by 752 · see citing works

Hypoxia and Metabolic Adaptation of Cancer Cells

Eales, K. L., Hollinshead, K. E. R., & Tennant, D. A. (2016) · Oncogenesis · doi:10.1038/oncsis.2015.50 · Cited by 724 · see citing works

Amino acids rather than glucose account for the majority of cell mass in proliferating mammalian cells

Hosios, A. M., Hecht, V. C., Danai, L. V., Johnson, M. O., Rathmell, J. C., Steinhauser, M. L., Manalis, S. R., & Vander Heiden, M. G. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.02.012 · Cited by 641 · see citing works

The pentose phosphate pathway in health and disease

TeSlaa, T. A., Ralser, M., Fan, J., & Rabinowitz, J. D. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00863-2 · Cited by 690 · see citing works

Keap1 loss promotes Kras-driven lung cancer and results in dependence on glutaminolysis

Romero, R., Sayin, V. I., Davidson, S. M., Bauer, M. R., Singh, S. X., LeBoeuf, S. E., Karakousi, T. R., Ellis, D. C., Bhutkar, A., Sánchez-Rivera, F. J., et al. (2017) · Nature Medicine · doi:10.1038/nm.4407 · Cited by 652 · see citing works

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 623 · see citing works

The Complex Interplay between Antioxidants and ROS in Cancer

Harris, I. S., & DeNicola, G. M. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.03.002 · Cited by 638 · see citing works

Reductive carboxylation supports redox homeostasis during anchorage-independent growth

Jiang, L., Shestov, A. A., Swain, P., Yang, C., Parker, S. J., Wang, Q. A., Terada, L. S., Adams, N. D., McCabe, M. T., Pietrak, B., et al. (2016) · Nature · doi:10.1038/nature17393 · Cited by 582 · see citing works

Cystine transporter regulation of pentose phosphate pathway dependency and disulfide stress exposes a targetable metabolic vulnerability in cancer

Liu, X., Olszewski, K. L., Zhang, Y., Lim, E. W., Shi, J., Zhang, X., Zhang, J., Lee, H., Koppula, P., Lei, G., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0496-x · Cited by 599 · see citing works

The Two Faces of Reactive Oxygen Species in Cancer

Reczek, C. R., & Chandel, N. S. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-041916-065808 · Cited by 602 · see citing works

Redox regulation of the immune response

Morris, G., Gevezova, M., Sarafian, V. S., & Maes, M. H. J. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-022-00902-0 · Cited by 600 · see citing works

Endothelial Cell Metabolism

Eelen, G., de Zeeuw, P., Treps, L., Harjes, U., Wong, B. W., & Carmeliet, P. (2017) · Physiological Reviews · doi:10.1152/physrev.00001.2017 · Cited by 591 · see citing works

A New View into the Regulation of Purine Metabolism: The Purinosome

Pedley, A. M., & Benkovic, S. J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.09.009 · Cited by 580 · see citing works

2-Hydroxyglutarate produced by neomorphic IDH mutations suppresses homologous recombination and induces PARP inhibitor sensitivity

Sulkowski, P. L., Corso, C. D., Robinson, N. D., Scanlon, S. E., Purshouse, K. R., Bai, H., Liu, Y., Sundaram, R. K., Hegan, D. C., Fons, N. R., et al. (2017) · Science Translational Medicine · doi:10.1126/scitranslmed.aal2463 · Cited by 556 · see citing works

ROS in Cancer: The Burning Question

Chio, I. I. C., & Tuveson, D. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.03.004 · Cited by 532 · see citing works

Increased demand for NAD(+) relative to ATP drives aerobic glycolysis

Luengo, A., Li, Z., Gui, D. Y., Sullivan, L. B., Zagorulya, M., Do, B. T., Ferreira, R., Naamati, A., Ali, A., Lewis, C. A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.012 · Cited by 547 · see citing works

Mitochondria as playmakers of apoptosis, autophagy and senescence

Abate, M., Festa, A., Falco, M., Lombardi, A., Luce, A., Grimaldi, A., Zappavigna, S., Sperlongano, P., Irace, C., Caraglia, M., et al. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.022 · Cited by 543 · see citing works

Inhibition of acetyl-CoA carboxylase suppresses fatty acid synthesis and tumor growth of non-small-cell lung cancer in preclinical models

Svensson, R. U., Parker, S. J., Eichner, L. J., Kolar, M. J., Wallace, M., Brun, S. N., Lombardo, P. S., Van Nostrand, J. L., Hutchins, A., Vera, L., et al. (2016) · Nature Medicine · doi:10.1038/nm.4181 · Cited by 536 · see citing works

Metabolic heterogeneity confers differences in melanoma metastatic potential

Tasdogan, A., Faubert, B., Ramesh, V., Ubellacker, J. M., Shen, B., Solmonson, A., Murphy, M. M., Gu, Z., Gu, W., Martin, M., et al. (2020) · Nature · doi:10.1038/s41586-019-1847-2 · Cited by 509 · see citing works

One-carbon metabolism in cancer

Newman, A. C., & Maddocks, O. D. K. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.118 · Cited by 509 · see citing works

Metabolomics: A Primer

Liu, X., & Locasale, J. W. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.01.004 · Cited by 453 · see citing works

Serine Catabolism Regulates Mitochondrial Redox Control during Hypoxia

Ye, J., Fan, J., Venneti, S., Wan, Y.-W., Pawel, B. R., Zhang, J., Finley, L. W. S., Lu, C., Lindsten, T., Cross, J. R., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0250 · Cited by 452 · see citing works

Reversal of cytosolic one-carbon flux compensates for loss of the mitochondrial folate pathway

Ducker, G. S., Chen, L., Morscher, R. J., Ghergurovich, J. M., Esposito, M., Teng, X., Kang, Y., & Rabinowitz, J. D. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.04.016 · Cited by 419 · see citing works

NADPH production by the oxidative pentose-phosphate pathway supports folate metabolism

Chen, L., Zhang, Z., Hoshino, A., Zheng, H. D., Morley, M. P., Arany, Z. P., & Rabinowitz, J. D. (2019) · Nature Metabolism · doi:10.1038/s42255-019-0043-x · Cited by 419 · see citing works

The importance of serine metabolism in cancer

Mattaini, K. R., Sullivan, M. R., & Heiden, M. G. V. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604085 · Cited by 409 · see citing works

Mitochondria as biosynthetic factories for cancer proliferation

Ahn, C. S., & Metallo, C. M. (2015) · Cancer & Metabolism · doi:10.1186/s40170-015-0128-2 · Cited by 399 · see citing works

Metabolic Reprogramming in Glioma

Strickland, M., & Stoll, E. A. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00043 · Cited by 350 · see citing works

Serine Metabolism Supports Macrophage IL-1β Production

Rodriguez, A. E., Ducker, G. S., Billingham, L. K., Martinez, C. A., Mainolfi, N., Suri, V., Friedman, A. A., Manfredi, M. G., Weinberg, S. E., Rabinowitz, J. D., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.014 · Cited by 346 · see citing works

Environment dictates dependence on mitochondrial complex I for NAD+ and aspartate production and determines cancer cell sensitivity to metformin

Gui, D. Y., Sullivan, L. B., Luengo, A., Hosios, A. M., Bush, L. N., Gitego, N., Davidson, S. M., Freinkman, E., Thomas, C. J., & Vander Heiden, M. G. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.006 · Cited by 323 · see citing works

Fatty acid synthesis is required for breast cancer brain metastasis

Ferraro, G. B., Ali, A., Luengo, A., Kodack, D. P., Deik, A., Abbott, K. L., Bezwada, D., Blanc, L., Prideaux, B., Jin, X., et al. (2021) · Nature Cancer · doi:10.1038/s43018-021-00183-y · Cited by 328 · see citing works

Histidine catabolism is a major determinant of methotrexate sensitivity

Kanarek, N., Keys, H. R., Cantor, J. R., Lewis, C. A., Chan, S. H., Kunchok, T., Abu-Remaileh, M., Freinkman, E., Schweitzer, L. D., & Sabatini, D. M. (2018) · Nature · doi:10.1038/s41586-018-0316-7 · Cited by 321 · see citing works

Serine restriction alters sphingolipid diversity to constrain tumour growth

Muthusamy, T., Cordes, T., Handzlik, M. K., You, L., Lim, E. W., Gengatharan, J. M., Pinto, A. F. M., Badur, M. G., Kolar, M. J., Wallace, M., et al. (2020) · Nature · doi:10.1038/s41586-020-2609-x · Cited by 315 · see citing works

Environmental cystine drives glutamine anaplerosis and sensitizes cancer cells to glutaminase inhibition

Muir, A., Danai, L. V., Gui, D. Y., Waingarten, C. Y., Lewis, C. A., & Vander Heiden, M. G. (2017) · eLife · doi:10.7554/elife.27713 · Cited by 311 · see citing works

Low glycaemic diets alter lipid metabolism to influence tumour growth

Lien, E. C., Westermark, A. M., Zhang, Y., Yuan, C., Li, Z., Lau, A. N., Sapp, K. M., Wolpin, B. M., & Heiden, M. G. V. (2021) · Nature · doi:10.1038/s41586-021-04049-2 · Cited by 311 · see citing works

A non-canonical tricarboxylic acid cycle underlies cellular identity

Arnold, P. K., Jackson, B. T., Paras, K. I., Brunner, J. S., Hart, M. L., Newsom, O. J., Alibeckoff, S. P., Endress, J., Drill, E., Sullivan, L. B., et al. (2022) · Nature · doi:10.1038/s41586-022-04475-w · Cited by 304 · see citing works

ROS homeostasis and metabolism: a critical liaison for cancer therapy

Kim, J., Kim, J., & Bae, J. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.119 · Cited by 295 · see citing works

Regulation of Substrate Utilization by the Mitochondrial Pyruvate Carrier

Vacanti, N. M., Divakaruni, A. S., Green, C. R., Parker, S. J., Henry, R. R., Ciaraldi, T. P., Murphy, A. N., & Metallo, C. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.024 · Cited by 277 · see citing works

Limited Environmental Serine and Glycine Confer Brain Metastasis Sensitivity to PHGDH Inhibition

Ngo, B., Kim, E., Osorio-Vasquez, V., Doll, S., Bustraan, S., Liang, R. J., Luengo, A., Davidson, S. M., Ali, A., Ferraro, G. B., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1228 · Cited by 268 · see citing works

Optical imaging of metabolic dynamics in animals

Shi, L., Zheng, C., Shen, Y., Chen, Z., Silveira, E. S., Zhang, L., Wei, M., Liu, C., de Sena-Tomás, C., Targoff, K. L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05401-3 · Cited by 271 · see citing works

Cancer, Oxidative Stress, and MetastasisPreprint

Gill, J. G., Piskounova, E., & Morrison, S. J. (2016) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2016.81.030791 · Cited by 269 · see citing works

Genomic deletion of malic enzyme 2 confers collateral lethality in pancreatic cancer

Dey, P., Baddour, J., Muller, F., Wu, C. C., Wang, H., Liao, W.-T., Lan, Z., Chen, A., Gutschner, T., Kang, Y., et al. (2017) · Nature · doi:10.1038/nature21052 · Cited by 264 · see citing works

A guide to 13C metabolic flux analysis for the cancer biologist

Antoniewicz, M. R. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0060-y · Cited by 264 · see citing works

Human SHMT inhibitors reveal defective glycine import as a targetable metabolic vulnerability of diffuse large B-cell lymphoma

Ducker, G. S., Ghergurovich, J. M., Mainolfi, N., Suri, V., Jeong, S. K., Hsin-Jung Li, S., Friedman, A., Manfredi, M. G., Gitai, Z., Kim, H., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1706617114 · Cited by 261 · see citing works

Serine Availability Influences Mitochondrial Dynamics and Function through Lipid Metabolism

Gao, X., Lee, K., Reid, M. A., Sanderson, S. M., Qiu, C., Li, S., Liu, J., & Locasale, J. W. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.017 · Cited by 249 · see citing works

SFXN1 is a mitochondrial serine transporter required for one-carbon metabolism

Kory, N., Wyant, G. A., Prakash, G., de Bos, J. U., Bottanelli, F., Pacold, M. E., Chan, S. H., Lewis, C. A., Wang, T., Keys, H. R., et al. (2018) · Science · doi:10.1126/science.aat9528 · Cited by 246 · see citing works

Increased Serine Synthesis Provides an Advantage for Tumors Arising in Tissues Where Serine Levels Are Limiting

Sullivan, M. R., Mattaini, K. R., Dennstedt, E. A., Nguyen, A. A., Sivanand, S., Reilly, M. F., Meeth, K. M., Muir, A., Darnell, A. M., Bosenberg, M., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.02.015 · Cited by 242 · see citing works

Loss of succinate dehydrogenase activity results in dependency on pyruvate carboxylation for cellular anabolism

Lussey-Lepoutre, C., Hollinshead, K. E. R., Ludwig, C., Menara, M., Morin, A., Castro-Vega, L.-J., Parker, S. J., Janin, M., Martinelli, C., Ottolenghi, C., et al. (2015) · Nature Communications · doi:10.1038/ncomms9784 · Cited by 227 · see citing works

Activation of the NRF2 antioxidant program generates an imbalance in central carbon metabolism in cancer

Sayin, V. I., LeBoeuf, S. E., Singh, S. X., Davidson, S. M., Biancur, D., Guzelhan, B. S., Alvarez, S. W., Wu, W. L., Karakousi, T. R., Zavitsanou, A. M., et al. (2017) · eLife · doi:10.7554/elife.28083 · Cited by 231 · see citing works

Methods and advances in metabolic flux analysis: a mini-review

Antoniewicz, M. R. (2015) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-015-1585-x · Cited by 236 · see citing works

SHMT2 Desuccinylation by SIRT5 Drives Cancer Cell Proliferation

Yang, X. P., Wang, Z., Li, X., Liu, B., Liu, M., Liu, L., Chen, S., Ren, M., Wang, Y., Yu, M., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1912 · Cited by 231 · see citing works

NADH Shuttling Couples Cytosolic Reductive Carboxylation of Glutamine with Glycolysis in Cells with Mitochondrial Dysfunction

Gaude, E., Schmidt, C., Gammage, P. A., Dugourd, A. J. F., Blacker, T. S., Peak‐Chew, S., Sáez-Rodríguez, J., O'Neill, J. S., Szabadkai, G., Minczuk, M. A., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.034 · Cited by 229 · see citing works

The Role of Mitochondria in Inflammation: From Cancer to Neurodegenerative Disorders

Missiroli, S., Genovese, I., Perrone, M., Vezzani, B., Vitto, V. A. M., & Giorgi, C. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9030740 · Cited by 231 · see citing works

Formate metabolism in health and disease

Pietzke, M., Meiser, J., & Vazquez, A. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2019.05.012 · Cited by 218 · see citing works

Arginine Methylation of MDH1 by CARM1 Inhibits Glutamine Metabolism and Suppresses Pancreatic Cancer

Wang, Y.-P., Zhou, W., Wang, J., Huang, X., Zuo, Y., Wang, T.-S., Gao, X. J., Xu, Y., Zou, S., Liu, Y., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.028 · Cited by 226 · see citing works

Cancer Metabolism: Current Understanding and Therapies

Counihan, J. L., Grossman, E. A., & Nomura, D. K. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00775 · Cited by 229 · see citing works

Cancer metabolism at a glance

Vazquez, A., Kamphorst, J. J., Markert, E. K., Schug, Z. T., Tardito, S., & Gottlieb, E. (2016) · Journal of Cell Science · doi:10.1242/jcs.181016 · Cited by 225 · see citing works

Cell Clustering Promotes a Metabolic Switch that Supports Metastatic Colonization

Labuschagne, C. F., Cheung, E. C., Blagih, J., Domart, M., & Vousden, K. H. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.07.014 · Cited by 223 · see citing works

Serine, glycine and one‑carbon metabolism in cancer (Review)

Pan, S., Fan, M., Liu, Z., Li, X., & Wang, H. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5158 · Cited by 227 · see citing works

Netrin G1 Promotes Pancreatic Tumorigenesis through Cancer-Associated Fibroblast–Driven Nutritional Support and Immunosuppression

Francescone, R. A., III, Costa, D. B. V., Franco‐Barraza, J., Wagner, J., Muir, A., Lau, A. N., Gabitova, L., Pazina, T., Gupta, S., Luong, T., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-0775 · Cited by 222 · see citing works

Switching to the cyclic pentose phosphate pathway powers the oxidative burst in activated neutrophils

Britt, E. C., Lika, J., Giese, M. A., Schoen, T. J., Seim, G. L., Huang, Z., Lee, P. Y., Anna Huttenlocher, A., & Fan, J. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00550-8 · Cited by 221 · see citing works

Enzyme promiscuity drives branched-chain fatty acid synthesis in adipose tissues

Wallace, M., Green, C. R., Roberts, L. S., Lee, Y. M., McCarville, J. L., Sánchez-Gurmaches, J., Meurs, N., Gengatharan, J. M., Hover, J. D., Phillips, S. A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0132-2 · Cited by 207 · see citing works

Cytosolic Aspartate Availability Determines Cell Survival When Glutamine Is Limiting

Alkan, H. F., Walter, K. E., Luengo, A., Madreiter‐Sokolowski, C. T., Stryeck, S., Lau, A. N., Zoughbi, W. A., Lewis, C. A., Thomas, C. J., Höefler, G., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.021 · Cited by 205 · see citing works

Guidelines on experimental methods to assess mitochondrial dysfunction in cellular models of neurodegenerative diseases

Connolly, N. M. C., Theurey, P., Ádám‐Vizi, V., Bazan, N. G., Bernardi, P., Bolaños, J. P., Culmsee, C., Dawson, V. L., Deshmukh, M., Duchen, M. R., et al. (2017) · Cell Death and Differentiation · doi:10.1038/s41418-017-0020-4 · Cited by 208 · see citing works

MCART1/SLC25A51 is required for mitochondrial NAD transport

Kory, N., uit de Bos, J., van der Rijt, S., Jankovic, N., Güra, M., Arp, N., Pena, I. A., Prakash, G., Chan, S. H., Kunchok, T., et al. (2020) · Science Advances · doi:10.1126/sciadv.abe5310 · Cited by 205 · see citing works

Isocitrate Dehydrogenase Mutation and ( <i>R</i> )-2-Hydroxyglutarate: From Basic Discovery to Therapeutics Development

Dang, L., & Su, S.-S. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044732 · Cited by 204 · see citing works

KRAS4A directly regulates hexokinase 1

Amendola, C. R., Mahaffey, J. P., Parker, S. J., Ahearn, I. M., Chen, W.-C., Zhou, M., Court, H., Shi, J., Mendoza, S. L., Morten, M. J., et al. (2019) · Nature · doi:10.1038/s41586-019-1832-9 · Cited by 203 · see citing works

Spectral tracing of deuterium for imaging glucose metabolism

Zhang, L., Shi, L., Shen, Y., Miao, Y., Wei, M., Qian, N., Liu, Y., & Min, W. (2019) · Nature Biomedical Engineering · doi:10.1038/s41551-019-0393-4 · Cited by 198 · see citing works

Mitochondrial metabolism in astrocytes regulates brain bioenergetics, neurotransmission and redox balance

Rose, J., Brian, C., Pappa, A., Panayiotidis, M. I., & Franco, R. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.536682 · Cited by 196 · see citing works

MESH1 is a cytosolic NADPH phosphatase that regulates ferroptosis

Ding, C. C., Rose, J., Sun, T., Wu, J., Chen, P., Lin, C., Yang, W., Chen, K., Lee, H., Xu, E., et al. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0181-1 · Cited by 189 · see citing works

Famine versus feast: understanding the metabolism of tumors in vivo

Mayers, J. R., & Heiden, M. G. V. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.01.004 · Cited by 185 · see citing works

NADPH debt drives redox bankruptcy: SLC7A11/xCT-mediated cystine uptake as a double-edged sword in cellular redox regulation

Liu, X., Zhang, Y., Zhuang, L., Olszewski, K. L., & Gan, B. (2020) · Genes & Diseases · doi:10.1016/j.gendis.2020.11.010 · Cited by 184 · see citing works

Lactate and glutamine support NADPH generation in cancer cells under glucose deprived conditions

Ying, M., You, D., Zhu, X., Cai, L., Zeng, S., & Hu, X. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102065 · Cited by 182 · see citing works

Mitochondrial NADP(H) generation is essential for proline biosynthesis

Zhu, J., Schwörer, S., Berisa, M., Kyung, Y. J., Ryu, K. W., Yi, J.-M., Jiang, X., Cross, J. R., & Thompson, C. B. (2021) · Science · doi:10.1126/science.abd5491 · Cited by 179 · see citing works

Serine one-carbon catabolism with formate overflow

Meiser, J., Tumanov, S., Maddocks, O., Labuschagne, C. F., Athineos, D., Van Den Broek, N., Mackay, G. M., Gottlieb, E., Blyth, K., Vousden, K., et al. (2016) · Science Advances · doi:10.1126/sciadv.1601273 · Cited by 174 · see citing works

HIF-driven SF3B1 induces KHK-C to enforce fructolysis and heart disease

Mirtschink, P., Krishnan, J., Grimm, F., Sarre, A., Hörl, M., Kayikci, M., Fankhauser, N., Christinat, Y., Cortijo, C., Feehan, O., et al. (2015) · Nature · doi:10.1038/nature14508 · Cited by 173 · see citing works

Adipose tissue mTORC2 regulates ChREBP-driven de novo lipogenesis and hepatic glucose metabolism

Tang, Y., Wallace, M., Sánchez-Gurmaches, J., Hsiao, W., Li, H., Lee, P. L., Vernia, S., Metallo, C. M., & Guertin, D. A. (2016) · Nature Communications · doi:10.1038/ncomms11365 · Cited by 171 · see citing works

Metabolic rewiring in melanoma

Ratnikov, B. I., Scott, D. A., Osterman, A. L., Smith, J. W., & Ronai, Z. A. (2016) · Oncogene · doi:10.1038/onc.2016.198 · Cited by 168 · see citing works

Mitochondrial NAD + /NADH Redox State and Diabetic Cardiomyopathy

Berthiaume, J. M., Kurdys, J., Muntean, D. M., & Rosca, M. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7415 · Cited by 168 · see citing works

Serine and Functional Metabolites in Cancer

Newman, A. C., & Maddocks, O. D. K. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.05.001 · Cited by 168 · see citing works

Targeting MTHFD2 in acute myeloid leukemia

Pikman, Y., Puissant, A., Alexe, G., Furman, A. A., Chen, L. M., Frumm, S. M., Ross, L. S., Fenouille, N., Bassil, C. F., Lewis, C. A., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151574 · Cited by 157 · see citing works

Activation of Oxidative Stress Response in Cancer Generates a Druggable Dependency on Exogenous Non-essential Amino Acids

LeBoeuf, S. E., Wu, W. L., Karakousi, T. R., Karadal, B., Jackson, S. R., Davidson, S. M., Wong, K.-K., Koralov, S. B., Sayin, V. I., & Papagiannakopoulos, T. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2019.11.012 · Cited by 150 · see citing works

Deuterium Tracing to Interrogate Compartment-Specific NAD(P)H Metabolism in Cultured Mammalian Cells

Lim, E. W., Parker, S. J., & Metallo, C. M. (2019) · Methods in molecular biology · doi:10.1007/978-1-0716-0159-4_4 · Cited by 8 · see citing works

Cytosolic and mitochondrial NADPH fluxes are independently regulated

Niu, X., Stancliffe, E., Gelman, S. J., Wang, L., Schwaiger-Haber, M., Rowles, J. L., Shriver, L. P., & Patti, G. J. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01283-9 · Cited by 60 · see citing works

Toward Quantitative Understanding of Compartmentalized NADPH Metabolism in Cancer Cells

Moon, S. J. (2022) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 1 · see citing works

[20] Rapid separation of particulate and soluble fractions from isolated cell preparations (digitonin and cell cavitation procedures)

Zuurendonk, P. F., Tischler, M. E., Akerboom, T. P. M., van der Meer, R., WILLIAMSON, J. R., & Tager, J. M. (1979) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(79)56023-6 · Cited by 46 · see citing works

Metabolic control and compartmentation in single living cells

Kohen, E., Kohen, C., Hirschberg, J., Wouters, A. W., Thorell, B., Westerhoff, H. V., & Charyulu, K. K. N. (1983) · Cell Biochemistry and Function · doi:10.1002/cbf.290010103 · Cited by 24 · see citing works