Glutamine Transport and Mitochondrial Metabolism in Cancer Cell Growth
Open accessAbstract
The concept that cancer is a metabolic disease is now well acknowledged: many cancer cell types rely mostly on glucose and some amino acids, especially glutamine for energy supply. These findings were corroborated by over-expression of plasma membrane nutrient transporters, such as the glucose transporters GLUTs and some amino acid transporters such as ASCT2, LAT1 and ATB0,+, which became promising targets for pharmacological intervention. On the basis of their sodium dependent transport modes, ASCT2 and ATB0+ have the capacity to sustain glutamine need of cancer cells; while LAT1, that is sodium independent will have the role of providing cancer cells with some amino acids with plausible signaling roles. According to the metabolic reprogramming of many types of cancer cells, glucose is mainly catabolized by aerobic glycolysis in tumors, while the fate of Glutamine is completed at mitochondrial level where the enzyme Glutaminase converts Glutamine to Glutamate. Glutamine rewiring in cancer cells is heterogeneous. For example, Glutamate is converted to -Ketoglutarate giving rise to a truncated form of Krebs cycle. This reprogrammed pathway leads to the production of ATP mainly at substrate level and regeneration of reducing equivalents needed for cells growth, redox balance and metabolic energy. Few studies on hypothetical mitochondrial transporter for Glutamine are reported and indirect evidences suggested its presence. Pharmacological compounds able to inhibit Glutamine metabolism may represent novel drugs for cancer treatments. Interestingly, well acknowledged targets for drugs are the Glutamine transporters of plasma membrane and the key enzyme Glutaminase.
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Glutamine is transported into cells through plasma membrane glutamine transporters such as SLC1A5, SLC38A1, and SLC38A2.
“Glutamine is transported into cells through plasma membrane glutamine transporters such as SLC1A5, SLC38A1, and SLC38A217”
From Glutamine reliance in cell metabolism (2020) · cites this paper as [17]
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Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works
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 · see citing works
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509 · see citing works
The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950 · see citing works
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398 · see citing works
Gao, P., Tchernyshyov, I., Chang, T.-C., Lee, Y.-S., Kita, K., Ochi, T., Zeller, K. I., De Marzo, A. M., Van Eyk, J. E., Mendell, J. T., et al. (2009) · Nature · doi:10.1038/nature07823 · Cited by 2,124 · see citing works
From Krebs to clinic: glutamine metabolism to cancer therapy
Altman, B. J., Stine, Z. E., & Dang, C. V. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.71 · Cited by 2,119 · see citing works
Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy
Nicklin, P., Bergman, P., Zhang, B., Triantafellow, E., Wang, H., Nyfeler, B., Yang, H., Hild, M., Kung, C., Wilson, C., et al. (2009) · Cell · doi:10.1016/j.cell.2008.11.044 · Cited by 1,798 · 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
Serine starvation induces stress and p53-dependent metabolic remodelling in cancer cells
Maddocks, O. D. K., Berkers, C. R., Mason, S. M., Zheng, L., Blyth, K., Gottlieb, E., & Vousden, K. H. (2013) · Nature · doi:10.1038/nature11743 · Cited by 1,007 · see citing works
Wang, S., Tsun, Z., Wolfson, R. L., Shen, K., Wyant, G., Plovanich, M. E., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 772 · see citing works
Amino acid transporters ASCT2 and LAT1 in cancer: partners in crime?
Fuchs, B. C., & Bode, B. (2005) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2005.04.005 · Cited by 717 · see citing works
SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1
Rebsamen, M., Pochini, L., Stasyk, T., de Araújo, M. E. G., Galluccio, M., Kandasamy, R. K., Snijder, B., Fauster, A., Rudashevskaya, E. L., Bruckner, M., et al. (2015) · Nature · doi:10.1038/nature14107 · Cited by 673 · see citing works
Self-citationCancer cell metabolism: the essential role of the nonessential amino acid, glutamine
Zhang, J., Pavlova, N. N., & Thompson, C. B. (2017) · The EMBO Journal · doi:10.15252/embj.201696151 · Cited by 651 · 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
Tardito, S., Oudin, A., Ahmed, S. U., Fack, F., Keunen, O., Zheng, L., Miletic, H., Sakariassen, P. Ø., Weinstock, A., Wagner, A., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3272 · Cited by 557 · see citing works
Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
Mastroberardino, L., Spindler, B., Pfeiffer, R., Skelly, P. J., Loffing, J., Shoemaker, C. B., & Verrey, F. (1998) · Nature · doi:10.1038/26246 · Cited by 557 · see citing works
Utsunomiya‐Tate, N., Endou, H., & Kanai, Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.25.14883 · Cited by 532 · see citing works
Molecular mechanisms of glutamine action
Curi, R., Lagranha, C. J., Doi, S. Q., Sellitti, D. F., Procopio, J., Pithon‐Curi, T. C., Corless, M., & Newsholme, P. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20339 · Cited by 497 · see citing works
Amino acid homeostasis and signalling in mammalian cells and organisms
Bröer, S., & Bröer, A. (2017) · Biochemical Journal · doi:10.1042/bcj20160822 · Cited by 496 · see citing works
Oncogenic K‐Ras decouples glucose and glutamine metabolism to support cancer cell growth
Gaglio, D., Metallo, C. M., Gameiro, P. A., Hiller, K., Danna, L. S., Balestrieri, C., Alberghina, L., Stephanopoulos, G., & Chiaradonna, F. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.56 · Cited by 492 · see citing works
Bhutia, Y. D., Babu, E., Ramachandran, S., & Ganapathy, V. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-3745 · Cited by 483 · see citing works
Pyruvate carboxylase is required for glutamine-independent growth of tumor cells
Cheng, T., Sudderth, J., Yang, C., Mullen, A. R., Jin, E. S., Matés, J. M., & DeBerardinis, R. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016627108 · Cited by 475 · see citing works
Impaired Amino Acid Transport at the Blood Brain Barrier Is a Cause of Autism Spectrum Disorder
Tărlungeanu, D. C., Deliu, E., Dotter, C. P., Kara, M., Janiesch, P. C., Scalise, M., Galluccio, M., Tesulov, M., Morelli, E., Sonmez, F. M., et al. (2016) · Cell · doi:10.1016/j.cell.2016.11.013 · Cited by 367 · see citing works
Self-citationWang, Q., Hardie, R., Hoy, A. J., van Geldermalsen, M., Gao, D., Fazli, L., Sadowski, M. C., Balaban, S., Schreuder, M., Nagarajah, R., et al. (2015) · The Journal of Pathology · doi:10.1002/path.4518 · Cited by 338 · see citing works
Glutamine transporters in mammalian cells and their functions in physiology and cancer
Bhutia, Y. D., & Ganapathy, V. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.017 · Cited by 326 · see citing works
SLC6 transporters: Structure, function, regulation, disease association and therapeutics
Pramod, A. B., Foster, J. D., Carvelli, L., & Henry, L. K. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.07.002 · Cited by 317 · see citing works
Cynober, L. A. (2002) · Nutrition · doi:10.1016/s0899-9007(02)00780-3 · Cited by 303 · see citing works
Seow, H. F., Bröer, S., Bröer, A., Bailey, C. G., Potter, S. J., Cavanaugh, J. A., & Rasko, J. E. J. (2004) · Nature Genetics · doi:10.1038/ng1406 · Cited by 274 · see citing works
Bröer, A., Rahimi, F., & Bröer, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700534 · Cited by 252 · see citing works
Pochini, L., Scalise, M., Galluccio, M., & Indiveri, C. (2014) · Frontiers in Chemistry · doi:10.3389/fchem.2014.00061 · Cited by 250 · see citing works
Self-citationRecent Molecular Advances in Mammalian Glutamine Transport
Bode, B. P. (2001) · Journal of Nutrition · doi:10.1093/jn/131.9.2475s · Cited by 245 · see citing works
ASCT2/SLC1A5 controls glutamine uptake and tumour growth in triple-negative basal-like breast cancer
van Geldermalsen, M., Wang, Q., Nagarajah, R., Marshall, A., Thoeng, A., Gao, D., Ritchie, W., Feng, Y., Bailey, C. G., Deng, N., et al. (2015) · Oncogene · doi:10.1038/onc.2015.381 · Cited by 235 · see citing works
The SLC38 family of sodium–amino acid co-transporters
Bröer, S. (2013) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-013-1393-y · Cited by 224 · see citing works
LAPTM4b recruits the LAT1-4F2hc Leu transporter to lysosomes and promotes mTORC1 activation
Milkereit, R., Persaud, A. K., Vanoaica, L., Guetg, A., Verrey, F., & Rotin, D. (2015) · Nature Communications · doi:10.1038/ncomms8250 · Cited by 205 · see citing works
A Tale of Two Glutaminases: Homologous Enzymes with Distinct Roles in Tumorigenesis
Katt, W. P., Lukey, M. J., & Cerione, R. A. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0190 · Cited by 179 · see citing works
Drug-induced amino acid deprivation as strategy for cancer therapy
Fung, M. K. L., & Chan, G. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0509-9 · Cited by 172 · see citing works
Wang, Q., Bailey, C. G., Ng, C., Tiffen, J. C., Thoeng, A., Minhas, V., Lehman, M., Hendy, S. C., Buchanan, G., Nelson, C. C., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1821 · Cited by 168 · see citing works
Targeting SLC1a5 ‐mediated glutamine dependence in non‐small cell lung cancer
Hassanein, M., Qian, J., Hoeksema, M. D., Wang, J., Jacobovitz, M. R., Ji, X., Harris, F. T., Harris, B. K., Boyd, K. L., Chen, H., et al. (2015) · International Journal of Cancer · doi:10.1002/ijc.29535 · Cited by 168 · see citing works
Gaglio, D., Soldati, C., Vanoni, M., Alberghina, L., & Chiaradonna, F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004715 · Cited by 164 · see citing works
Transporters in Drug Development and Clinical Pharmacology
Giacomini, K. M., & Sm, H. (2013) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2013.86 · Cited by 151 · see citing works
LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter
Napolitano, L., Scalise, M., Galluccio, M., Pochini, L., Albanese, L. M., & Indiveri, C. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.08.004 · Cited by 149 · see citing works
Self-citationRobey, R. B., Weisz, J., Kuemmerle, N. B., Salzberg, A. C., Berg, A. S., Brown, D. G., Maurer, L. L., Palorini, R., Al‐Mulla, F., Al-Temaimi, R. A., et al. (2015) · Carcinogenesis · doi:10.1093/carcin/bgv037 · Cited by 138 · see citing works
Gupta, N., Miyauchi, S., Martindale, R. G., Herdman, A. V., Podolsky, R. H., Miyake, K., Mager, S., Prasad, P. D., Ganapathy, M. E., & Ganapathy, V. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2005.04.002 · Cited by 135 · see citing works
Amino acid transporter SLC6A14 is a novel and effective drug target for pancreatic cancer
Coothankandaswamy, V., Cao, S., Xu, Y., Prasad, P. D., Singh, P. K., Reynolds, C. P., Yang, S., Ogura, J., Ganapathy, V., & Bhutia, Y. D. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13616 · Cited by 132 · see citing works
Glutaminase regulation in cancer cells: a druggable chain of events
Katt, W. P., & Cerione, R. A. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.10.008 · Cited by 130 · see citing works
Rosilio, C., Nebout, M., Imbert, V., Griessinger, E., Neffati, Z., Benadiba, J., Hagenbeek, T. J., Spits, H., Reverso, J., Ambrosetti, D., et al. (2014) · Leukemia · doi:10.1038/leu.2014.338 · Cited by 128 · see citing works
Icard, P., & Lincet, H. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.07.001 · Cited by 123 · see citing works
Li, L., Di, X., Zhang, S., Kan, Q., Liu, H., Lu, T., Wang, Y., Fu, Q., Sun, J., & He, Z. (2016) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2016.01.041 · Cited by 115 · see citing works
Damiani, C., Colombo, R., Gaglio, D., Mastroianni, F., Pescini, D., Westerhoff, H. V., Mauri, G., Vanoni, M., & Alberghina, L. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005758 · Cited by 112 · see citing works
Up-regulation of the amino acid transporter ATB0,+ (SLC6A14) in carcinoma of the cervix
Gupta, N., Prasad, P. D., Ghamande, S. A., Martin, P. M., Herdman, A. V., Martindale, R. G., Podolsky, R. H., Mager, S., Ganapathy, M. E., & Ganapathy, V. (2005) · Gynecologic Oncology · doi:10.1016/j.ygyno.2005.08.016 · Cited by 109 · see citing works
Plasma-free amino acid profiles are predictors of cancer and diabetes development
Bi, X., & Henry, C. J. (2017) · Nutrition and Diabetes · doi:10.1038/nutd.2016.55 · Cited by 106 · see citing works
Zhu, Y., Li, T., da Silva, S. R., Lee, J. J., Lu, C., Eoh, H., Jung, J. U., & Gao, S. (2017) · mBio · doi:10.1128/mbio.01179-17 · Cited by 92 · see citing works
Babu, E., Bhutia, Y. D., Ramachandran, S., Gnana‐Prakasam, J. P., Prasad, P. D., Thangaraju, M., & Ganapathy, V. (2015) · Biochemical Journal · doi:10.1042/bj20150437 · Cited by 90 · see citing works
Mitochondrial Chemical Biology: New Probes Elucidate the Secrets of the Powerhouse of the Cell
Wisnovsky, S., Lei, E. K., Jean, S. R., & Kelley, S. O. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.06.012 · Cited by 88 · see citing works
Li, L., Di, X., Wu, M., Sun, Z., Zhong, L., Wang, Y., Fu, Q., Kan, Q., Sun, J., & He, Z. (2016) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2016.11.012 · Cited by 84 · see citing works
Honjo, H., Kaira, K., Miyazaki, T., Yokobori, T., Kanai, Y., Nagamori, S., Oyama, T., Asao, T., & Kuwano, H. (2016) · Journal of Surgical Oncology · doi:10.1002/jso.24160 · Cited by 83 · see citing works
Xu, M., Sakamoto, S., Matsushima, J., Kimura, T., Ueda, T., Mizokami, A., Kanai, Y., & Ichikawa, T. (2015) · The Journal of Urology · doi:10.1016/j.juro.2015.11.071 · Cited by 81 · see citing works
ASCT2 regulates glutamine uptake and cell growth in endometrial carcinoma
Marshall, A. D., van Geldermalsen, M., Otte, N. J., Lum, T., Vellozzi, M., Thoeng, A., Pang, A., Nagarajah, R., Zhang, B. K., Wang, Q., et al. (2017) · Oncogenesis · doi:10.1038/oncsis.2017.70 · Cited by 79 · see citing works
Napolitano, L., Scalise, M., Koyioni, M., Koutentis, P. A., Catto, M., Eberini, I., Parravicini, C., Palazzolo, L., Pisani, L., Galluccio, M., et al. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.07.006 · Cited by 78 · see citing works
Self-citationClinical Role of ASCT2 (SLC1A5) in KRAS-Mutated Colorectal Cancer
Toda, K., Nishikawa, G., Iwamoto, M., Itatani, Y., Takahashi, R., Sakai, Y., & Kawada, K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081632 · Cited by 77 · see citing works
Glutamine activates STAT3 to control cancer cell proliferation independently of glutamine metabolism
Cacace, A., Sboarina, M., Vazeille, T., & Sonveaux, P. (2017) · Oncogene · doi:10.1038/onc.2016.364 · Cited by 76 · see citing works
Novel therapeutic approaches targeting L-type amino acid transporters for cancer treatment
Hayashi, K., & Anzai, N. (2017) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v9.i1.21 · Cited by 76 · see citing works
Glutamine transport. From energy supply to sensing and beyond
Scalise, M., Pochini, L., Galluccio, M., & Indiveri, C. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.006 · Cited by 74 · see citing works
Self-citationOppedisano, F., Catto, M., Koutentis, P. A., Nicolotti, O., Pochini, L., Koyioni, M., Introcaso, A., Michaelidou, S. S., Carotti, A., & Indiveri, C. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.09.011 · Cited by 72 · see citing works
Self-citationThe MYC mRNA 3′‐UTR couples RNA polymerase II function to glutamine and ribonucleotide levels
Dejure, F. R., Royla, N., Herold, S., Kalb, J., Walz, S., Ade, C. P., Mastrobuoni, G., Vanselow, J. T., Schlösser, A., Wolf, E., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201796662 · Cited by 69 · see citing works
Colas, C., Grewer, C. T., Otte, N. J., Gameiro, A. M., Albers, T., Singh, K., Shere, H., Bonomi, M., Holst, J., & Schlessinger, A. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004477 · Cited by 67 · see citing works
Scalise, M., Pochini, L., Giangregorio, N., Tonazzi, A., & Indiveri, C. (2013) · Pharmaceutics · doi:10.3390/pharmaceutics5030472 · Cited by 67 · see citing works
Self-citationPingitore, P., Pochini, L., Scalise, M., Galluccio, M., Hedfalk, K., & Indiveri, C. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.05.034 · Cited by 67 · see citing works
Self-citationTransport mechanism and regulatory properties of the human amino acid transporter ASCT2 (SLC1A5)
Scalise, M., Pochini, L., Panni, S., Pingitore, P., Hedfalk, K., & Indiveri, C. (2014) · Amino Acids · doi:10.1007/s00726-014-1808-x · Cited by 67 · see citing works
Self-citationPrognostic significance of L-type amino acid transporter 1 (LAT1) expression in cutaneous melanoma
Shimizu, A., Kaira, K., Kato, M., Yasuda, M., Takahashi, A., Tominaga, H., Oriuchi, N., Nagamori, S., Kanai, Y., Oyama, T., et al. (2015) · Melanoma Research · doi:10.1097/cmr.0000000000000181 · Cited by 64 · see citing works
Liu, Y., Liu, Y., An, H., Chang, Y., Zhang, W., Zhu, Y., Xu, L., & Xu, J. (2015) · Scientific Reports · doi:10.1038/srep16954 · Cited by 63 · see citing works
A novel glutaminase isoform in mammalian tissues
Rosa, V. Y. D. L., Campos-Sandoval, J. A., Martín‐Rufián, M., Cardona, C., Matés, J. M., Segura, J. A., Alonso, F. J., & Márquez, J. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.02.021 · Cited by 61 · see citing works
Indiveri, C., ABRUZZO, G., Stipani, I., & Palmieri, F. (1998) · Biochemical Journal · doi:10.1042/bj3330285 · Cited by 56 · see citing works
Self-citationAlbers, T., Marsiglia, W. M., Thomas, T., Gameiro, A. M., & Grewer, C. T. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.075648 · Cited by 52 · see citing works
Liu, W., Chen, H., Wong, N. W., Haynes, W., Baker, C. M., & Wang, X. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.02.025 · Cited by 52 · see citing works
Cysteine is not a substrate but a specific modulator of human ASCT2 (SLC1A5) transporter
Scalise, M., Pochini, L., Pingitore, P., Hedfalk, K., & Indiveri, C. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.10.011 · Cited by 49 · see citing works
Self-citationLAT-1 activity of meta-substituted phenylalanine and tyrosine analogs
Augustyn, E., Finke, K., Zur, A. A., Hansen, L., Heeren, N., Chien, H., Lin, L., Giacomini, K. M., Colas, C., Schlessinger, A., et al. (2016) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2016.04.023 · Cited by 47 · see citing works
LAT1 is a putative therapeutic target in endometrioid endometrial carcinoma
Marshall, A. D., van Geldermalsen, M., Otte, N. J., Anderson, L. A., Lum, T., Vellozzi, M., Zhang, B. K., Thoeng, A., Wang, Q., Rasko, J. E. J., et al. (2016) · International Journal of Cancer · doi:10.1002/ijc.30371 · Cited by 47 · see citing works
Lu, J., Chen, M., Tao, Z., Gao, S., Li, Y., Cao, Y., Lu, C., & Zou, X. (2017) · OncoTarget · doi:10.18632/oncotarget.19479 · Cited by 46 · see citing works
Bak, L. K., Ziemińska, E., Waagepetersen, H. S., Schousboe, A., & Albrecht, J. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9471-1 · Cited by 44 · see citing works
Alberghina, L., Gaglio, D., Gelfi, C., Moresco, R. M., Mauri, G., Bertolazzi, P., Messa, C., Gilardi, M. C., Chiaradonna, F., & Vanoni, M. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00362 · Cited by 43 · see citing works
Mitochondrial dysfunction and potential anticancer therapy
LLeonart, M. E., Grodzicki, R., Graifer, D. M., & Lyakhovich, A. (2017) · Medicinal Research Reviews · doi:10.1002/med.21459 · Cited by 43 · see citing works
Nikkuni, O., Kaira, K., Toyoda, M., Shino, M., Sakakura, K., Takahashi, K., Tominaga, H., Oriuchi, N., Suzuki, M., Iijima, M., et al. (2015) · Pathology & Oncology Research · doi:10.1007/s12253-015-9954-3 · Cited by 41 · see citing works
Glutaminolysis and carcinogenesis of oral squamous cell carcinoma
Cetindis, M., Biegner, T., Munz, A., Teriete, P., Reinert, S., & Grimm, M. R. (2015) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/s00405-015-3543-7 · Cited by 39 · see citing works
Glutamine transport in submitochondrial particles
Sastrasinh, S., & Sastrasinh, M. (1989) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1989.257.6.f1050 · Cited by 38 · see citing works
LAT1 acts as a crucial transporter of amino acids in human thymic carcinoma cells
Hayashi, K., Jutabha, P., Maeda, S., Yothaisong, S., Ouchi, M., Endou, H., Fujita, T., Chida, M., & Anzai, N. (2016) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2016.07.006 · Cited by 33 · see citing works
Kasai, N., Sasakawa, A., Hosomi, K., Poh, T. W., Chua, B. L., Yong, W. P., So, J. B. Y., Chan, S. L., Soong, R. C. T., Kono, K., et al. (2017) · Europe PMC (PubMed Central) · Cited by 29 · see citing works
Glutamine Transport in Normal and Acidotic Rat Kidney Mitochondria
Atlante, A., Passarella, S., Minervini, G. M., & Quagliariello, E. (1994) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1994.1513 · Cited by 28 · see citing works
Transcriptomic and Immunohistochemical Profiling of SLC6A14 in Pancreatic Ductal Adenocarcinoma
Penheiter, A. R., Erdogan, S., Murphy, S. J., Hart, S. N., Lima, J. F., Rohakhtar, F. R., O’Brien, D. R., Bamlet, W. R., Wuertz, R. E., Smyrk, T. C., et al. (2015) · BioMed Research International · doi:10.1155/2015/593572 · Cited by 26 · see citing works
Expression of human heteromeric amino acid transporters in the yeast Pichia pastoris
Costa, M., Rosell, A., Álvarez-Marimon, E., Zorzano, A., Fotiadis, D., & Palacı́n, M. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2012.10.003 · Cited by 26 · see citing works
Bjersand, K., Seidal, T., Poromaa, I. S., Åkerud, H., & Skírnisdóttir, I. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179363 · Cited by 22 · see citing works
Yanagisawa, N., Satoh, T., Hana, K., Ichinoe, M., Nakada, N., Endou, H., Okayasu, I., & Murakumo, Y. (2015) · Cancer Biomarkers · doi:10.3233/cbm-150486 · Cited by 20 · see citing works
Targeting cancer metabolism at the plasma membrane by limiting amino acid access through SLC6A14
McCracken, A. N., & Edinger, A. L. (2015) · Biochemical Journal · doi:10.1042/bj20150721 · Cited by 19 · see citing works
Wang, J., Fei, X., Wu, W., Chen, X., Su, L., Zhu, Z., & Zhou, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166147 · Cited by 18 · see citing works
Right on TARGET: glutamine metabolism in cancer
Ratnikov, B. I., Jeon, Y. J., Smith, J. W., & Ronai, Z. A. (2015) · Oncoscience · doi:10.18632/oncoscience.205 · Cited by 15 · see citing works
Chiotellis, A., Herde, A. M., Weyermann, K., Leutwiler, D. S., Schibli, R., Ametamey, S. M., Krämer, S. D., & Mu, L. (2014) · Amino Acids · doi:10.1007/s00726-014-1754-7 · Cited by 11 · see citing works
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Glutamine reliance in cell metabolism
Yoo, H. C., Yu, Y. C., Sung, Y., & Han, J. M. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00504-8 · Cited by 1,021 · see citing works
Energy metabolism in health and diseases
Liu, H., Wang, S., Wang, J., Guo, X., Song, Y., Fu, K., Gao, Z., Liu, D., He, W., & Yang, L. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02141-x · Cited by 438 · see citing works
Mitochondria: It is all about energy
Casanova, A., Wevers, A., Ledesma, S. N., & Pruimboom, L. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1114231 · Cited by 335 · see citing works
Scalise, M., Galluccio, M., Console, L., Pochini, L., & Indiveri, C. (2018) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00243 · Cited by 283 · see citing works
Self-citationThe Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology
Scalise, M., Pochini, L., Console, L., Losso, M. A., & Indiveri, C. (2018) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00096 · Cited by 267 · see citing works
Self-citationA Review of the Alleged Health Hazards of Monosodium Glutamate
Zanfirescu, A., Ungurianu, A., Tsatsakis, A. M., Nițulescu, G. M., Kouretas, D., Veskoukis, A. S., Tsoukalas, D., Engin, A. B., Aschner, M., & Margina, D. M. (2019) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12448 · Cited by 288 · see citing works
Emerging roles of Myc in stem cell biology and novel tumor therapies
Yoshida, G. J. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0835-y · Cited by 244 · see citing works
Targeting Glutamine Metabolism and Redox State for Leukemia Therapy
Gregory, M. A., Nemkov, T. G., Park, H. J., Zaberezhnyy, V., Gehrke, S. A., Adane, B., Jordan, C. T., Hansen, K. C., D’Alessandro, A., & DeGregori, J. V. (2019) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-3223 · Cited by 173 · see citing works
Therapeutic targeting of glutaminolysis as an essential strategy to combat cancer
Matés, J. M., Paola, F. J. D., Campos-Sandoval, J. A., Mazurek, S., & Márquez, J. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.012 · Cited by 164 · see citing works
Sodium homeostasis in the tumour microenvironment
Leslie, T. K., James, A. D., Zaccagna, F., Grist, J. T., Deen, S. S., Kennerley, A. J., Riemer, F., Kaggie, J. D., Gallagher, F. A., Gilbert, F. J., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2019.07.001 · Cited by 141 · see citing works
Wang, B., Pei, J., Xu, S.-N., Liu, J., & Yu, J.-M. (2024) · Journal of experimental & clinical cancer research : CR · doi:10.1186/s13046-024-02994-0 · Cited by 129 · see citing works
Oxidative stress and antioxidants in the pathophysiology of malignant melanoma
Obrador, E., Liu-Smith, F., Dellinger, R. W., Salvador, R., Meyskens, F. L., & Estrela, J. M. (2019) · Biological Chemistry · doi:10.1515/hsz-2018-0327 · Cited by 119 · see citing works
Valdebenito, S., Malik, S., Luu, R. H., Loudig, O. D., Mitchell, M. I., Okafo, G. N., Bhat, K., Prideaux, B., & Eugenín, E. A. (2021) · Scientific Reports · doi:10.1038/s41598-021-93775-8 · Cited by 120 · see citing works
Banerjee, A., Mukherjee, S., & Maji, B. (2021) · Toxicology Reports · doi:10.1016/j.toxrep.2021.04.009 · Cited by 103 · see citing works
Bonanomi, M., Salmistraro, N., Porro, D., Pinsino, A., Colangelo, A. M., & Gaglio, D. (2022) · Chemosphere · doi:10.1016/j.chemosphere.2022.134947 · Cited by 105 · see citing works
Could ketogenic diet “starve” cancer? Emerging evidence
Barrea, L., Caprio, M., Tuccinardi, D., Moriconi, E., Renzo, L. D., Muscogiuri, G., Colao, A., Savastano, S., & on behalf of the Obesity Programs of nutrition, E. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1847030 · Cited by 102 · see citing works
Glutamine addiction in tumor cell: oncogene regulation and clinical treatment
Li, X., Peng, X., Li, Y., Wei, S., He, G., Liu, J., Li, X., Yang, S., Dai, L., Lin, W., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-023-01449-x · Cited by 99 · see citing works
Purinergic Signaling in the Hallmarks of Cancer
Campos‐Contreras, A. D. R., Díaz‐Muñoz, M., & Vázquez‐Cuevas, F. G. (2020) · Cells · doi:10.3390/cells9071612 · Cited by 94 · see citing works
Jiang, H., Zhang, N., Tang, T., Feng, F., Sun, H., & Qu, W. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104844 · Cited by 88 · see citing works
Pochini, L., Galluccio, M., Scalise, M., Console, L., & Indiveri, C. (2018) · SLAS DISCOVERY · doi:10.1177/2472555218812821 · Cited by 83 · see citing works
Self-citationZhou, Q., Lin, W., Wang, C., Sun, F., Ju, S., Chen, Q., Wang, Y., Chen, Y., Li, H., Wang, L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30559-2 · Cited by 80 · see citing works
Nilsson, A., Haanstra, J. R., Engqvist, M. K. M., Gerding, A., Bakker, B. M., Klingmüller, U., Teusink, B., & Nielsen, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1919250117 · Cited by 71 · see citing works
Prasad, P., Ghosh, S., & Roy, S. S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03818-6 · Cited by 72 · see citing works
Lobetyolin induces apoptosis of colon cancer cells by inhibiting glutamine metabolism
He, W., Tao, W., Zhang, F., Jie, Q., He, Y., Zhu, W., Tan, J., Shen, W., Li, L., Yang, Y., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15009 · Cited by 68 · see citing works
Targeting the Mitochondrial Metabolic Network: A Promising Strategy in Cancer Treatment
Frattaruolo, L., Brindisi, M., Curcio, R., Marra, F., Dolce, V., & Cappello, A. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176014 · Cited by 66 · see citing works
Glutamine Metabolism Drives Growth in Advanced Hormone Receptor Positive Breast Cancer
Demas, D. M., Demo, S. D., Fallah, Y., Clarke, R. C., Nephew, K. P., Althouse, S. K., Sandusky, G. E., He, W., & Shajahan‐Haq, A. N. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00686 · Cited by 66 · see citing works
Okanishi, H., Ohgaki, R., Okuda, S., Endou, H., & Kanai, Y. (2020) · Cancer Science · doi:10.1111/cas.14756 · Cited by 66 · see citing works
The Development of Novel Drug Treatments for Stroke Patients: A Review
Frank, D., Zlotnik, A. A., Boyko, M., & Gruenbaum, B. F. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105796 · Cited by 63 · see citing works
Lopes, C., Pereira, C., & Medeiros, R. (2021) · Cancers · doi:10.3390/cancers13020203 · Cited by 63 · see citing works
How Autophagy Shapes the Tumor Microenvironment in Ovarian Cancer
Ferraresi, A., Girone, C., Esposito, A., Vidoni, C., Vallino, L., Secomandi, E., Dhanasekaran, D. N., & Isidoro, C. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.599915 · Cited by 61 · see citing works
KRAS mutation: The booster of pancreatic ductal adenocarcinoma transformation and progression
Zhang, Z., Zhang, H., Liao, X., & Tsai, H. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1147676 · Cited by 62 · see citing works
Targeting glutamine metabolism as a potential target for cancer treatment
Zou, W., Han, Z., Wang, Z., & Liu, Q. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03430-7 · Cited by 59 · see citing works
Sequence Features of Mitochondrial Transporter Protein Families
Gyimesi, G., & Hediger, M. A. (2020) · Biomolecules · doi:10.3390/biom10121611 · Cited by 56 · see citing works
RETRACTED: The interplay between monosodium glutamate (MSG) consumption and metabolic disorders
Kayode, O. T., Bello, J. A., Oguntola, J. A., Kayode, A. A. A., & Olukoya, D. K. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e19675 · Cited by 57 · see citing works
RetractedAmino Acid Transporter SLC6A14 (ATB0,+) – A Target in Combined Anti-cancer Therapy
Nałęcz, K. A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.594464 · Cited by 57 · see citing works
Metabolic reprogramming as a feast for virus replication
Polčicová, K., Baďurová, L., & Tomášková, J. (2020) · Acta Virologica · doi:10.4149/av_2020_210 · Cited by 57 · see citing works
Emerging Hallmarks of Metabolic Reprogramming in Prostate Cancer
Lasorsa, F. M., di Meo, N. A., Rutigliano, M., Ferro, M., Terracciano, D., Tătaru, O. S., Battaglia, M., Ditonno, P., & Lucarelli, G. T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24020910 · Cited by 56 · see citing works
Arif, T., Paul, A., Krelin, Y., Shteinfer‐Kuzmine, A., & Shoshan‐Barmatz, V. (2018) · Cancers · doi:10.3390/cancers10120499 · Cited by 55 · see citing works
Metabolic Reprogramming in Cancer: Implications for Immunosuppressive Microenvironment
Aden, D., Sureka, N., Zaheer, S., Chaurasia, J. K., & Zaheer, S. (2024) · Immunology · doi:10.1111/imm.13871 · Cited by 54 · see citing works
Metabolic regulation of prostate cancer heterogeneity and plasticity
Peitzsch, C., Gorodetska, I., Klusa, D., Shi, Q., Alves, T. C., Pantel, K., & Dubrovska, A. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.12.002 · Cited by 53 · see citing works
Pool, L., Wijdeveld, L. F. J. M., de Groot, N. M. S., & Brundel, B. J. J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168463 · Cited by 52 · see citing works
Lipid Catabolism and ROS in Cancer: A Bidirectional Liaison
Castelli, S., Falco, P. D., Ciccarone, F., Desideri, E., & Ciriolo, M. R. (2021) · Cancers · doi:10.3390/cancers13215484 · Cited by 53 · see citing works
Tumor metabolic reprogramming in lung cancer progression (Review)
Li, X., Liu, M., Liu, H., & Chen, J. (2022) · Oncology Letters · doi:10.3892/ol.2022.13407 · Cited by 52 · see citing works
The multifaceted roles of mitochondria at the crossroads of cell life and death in cancer
Fontana, F., & Limonta, P. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.09.024 · Cited by 52 · see citing works
Amino acid transporters: Emerging roles in drug delivery for tumor-targeting therapy
Zhang, L., Sui, C., Yang, W., & Luo, Q. (2020) · Asian Journal of Pharmaceutical Sciences · doi:10.1016/j.ajps.2019.12.002 · Cited by 51 · see citing works
miR‐145 inhibits glutamine metabolism through c‐myc/GLS1 pathways in ovarian cancer cells
Li, J., Li, X., Wu, L., Pei, M., Li, H., & Jiang, Y. (2019) · Cell Biology International · doi:10.1002/cbin.11182 · Cited by 47 · see citing works
LKB1 and cancer: The dual role of metabolic regulation
Li, T., & Zhu, H. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110872 · Cited by 47 · see citing works
Gilteritinib Inhibits Glutamine Uptake and Utilization in FLT3 -ITD–Positive AML
Thomas, M. E. Z., Lu, X., Talebi, Z., Jeon, J. Y., Buelow, D. R., Gibson, A. A., Uddin, M. E., Brinton, L. T., Nguyen, J., Collins, M., et al. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0071 · Cited by 46 · see citing works
Beyond the Warburg Effect: N-Myc Contributes to Metabolic Reprogramming in Cancer Cells
Yoshida, G. J. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.00791 · Cited by 46 · see citing works
Daneshmandi, S., Choi, J. E., Qi, Y., MacDonald, C. R., Pandey, M. R., Goruganthu, M., Roberts, N. T., Singh, P. K., Higashi, R. M., Lane, A. N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47096-9 · Cited by 45 · see citing works
Membrane Transporters for Amino Acids as Players of Cancer Metabolic Rewiring
Scalise, M., Console, L., Rovella, F., Galluccio, M., Pochini, L., & Indiveri, C. (2020) · Cells · doi:10.3390/cells9092028 · Cited by 45 · see citing works
Self-citationMorris, D. R., Qu, Y., Agrawal, A. S., Garofalo, R. P., & Casola, A. (2020) · Viruses · doi:10.3390/v12101088 · Cited by 45 · see citing works
Wetzel, T. J., Erfan, S. C., Figueroa, L. D., Wheeler, L. M., & Ananieva, E. A. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1186539 · Cited by 43 · see citing works
Dual Inhibitions on Glucose/Glutamine Metabolisms for Nontoxic Pancreatic Cancer Therapy
Xu, Y., Yu, Z., Fu, H., Guo, Y., Hu, P., & Shi, J. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c00111 · Cited by 43 · see citing works
Targeting fuel pocket of cancer cell metabolism: A focus on glutaminolysis
Sharma, S., Agnihotri, N., & Kumar, S. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114943 · Cited by 42 · see citing works
The Novel Roles of Connexin Channels and Tunneling Nanotubes in Cancer Pathogenesis
Valdebenito, S., Lou, E., Baldoni, J., Okafo, G. N., & Eugenín, E. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051270 · Cited by 41 · see citing works
Fan, Y., Xue, H., Li, Z., Huo, M., Gao, H., & Guan, X. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1345522 · Cited by 40 · see citing works
Phytochemicals Target Multiple Metabolic Pathways in Cancer
Shuvalov, O. Y., Kirdeeva, Y., Daks, A. A., Fedorova, O., Parfenyev, S. E., Simon, H., & Barlev, N. A. (2023) · Antioxidants · doi:10.3390/antiox12112012 · Cited by 43 · see citing works
Unraveling the Peculiar Features of Mitochondrial Metabolism and Dynamics in Prostate Cancer
Fontana, F., Anselmi, M., & Limonta, P. (2023) · Cancers · doi:10.3390/cancers15041192 · Cited by 39 · see citing works
ASCT1 and ASCT2: Brother and Sister?
Scalise, M., Console, L., Cosco, J., Pochini, L., Galluccio, M., & Indiveri, C. (2021) · SLAS discovery : advancing life sciences R & D · doi:10.1177/24725552211030288 · Cited by 35 · see citing works
Self-citationTFEB Supports Pancreatic Cancer Growth through the Transcriptional Regulation of Glutaminase
Kim, J. H., Lee, J., Cho, Y.-R., Lee, S., Sung, G., Shin, D., Choi, K., & Son, J. (2021) · Cancers · doi:10.3390/cancers13030483 · Cited by 35 · see citing works
Progress in research on the role of amino acid metabolic reprogramming in tumour therapy: A review
Wang, D., & Wan, X. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113923 · Cited by 34 · see citing works
High expression of SLC38A1 predicts poor prognosis in patients with de novo acute myeloid leukemia
Li, Y., Shao, H., Da, Z., Pan, J., & Fu, B. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28632 · Cited by 34 · see citing works
Non-Coding RNAs as Key Regulators of Glutaminolysis in Cancer
Ortiz-Pedraza, Y., Muñoz-Bello, J. O., Olmedo‐Nieva, L., Contreras‐Paredes, A., Martínez-Ramírez, I., Langley, E., & Lizano, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082872 · Cited by 34 · see citing works
Guarino, F., Zinghirino, F., Mela, L., Pappalardo, X. G., Ichas, F., Pinto, V. D., & Messina, A. A. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148289 · Cited by 34 · see citing works
Targeting Pulmonary Fibrosis by SLC1A5-Dependent Glutamine Transport Blockade
Choudhury, M., Schaefbauer, K. J., Kottom, T. J., Yi, E. S., Tschumperlin, D. J., & LIMPER, A. H. (2023) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2022-0339oc · Cited by 32 · see citing works
The Human Transient Receptor Potential Melastatin 2 Ion Channel Modulates ROS Through Nrf2
Bao, L., Festa, F., Freet, C. S., Lee, J. P., Hirschler‐Laszkiewicz, I., Chen, S.-J., Keefer, K. A., Wang, H., Patterson, A. D., Cheung, J. Y., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50661-8 · Cited by 32 · see citing works
Zhang, C., Hu, Y., Zhang, Y., Ma, W.-D., Song, Y., Quan, X.-H., Guo, X., & Wang, C. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119365 · Cited by 32 · see citing works
Cohen, A. S., Grudzinski, J., Smith, G. T., Peterson, T. E., Whisenant, J. G., Hickman, T. L., Ciombor, K. K., Cardin, D. B., Eng, C., Goff, L. W., et al. (2021) · Journal of Nuclear Medicine · doi:10.2967/jnumed.120.261594 · Cited by 32 · see citing works
Stirred suspension bioreactors maintain naïve pluripotency of human pluripotent stem cells
Rohani, L., Borys, B. S., Razian, G., Naghsh, P., Liu, S., Johnson, A. A., Machiraju, P., Holland, H., Lewis, I. A., Groves, R. A., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01218-3 · Cited by 31 · see citing works
ATP modulates SLC7A5 (LAT1) synergistically with cholesterol
Cosco, J., Scalise, M., Colas, C., Galluccio, M., Martini, R., Rovella, F., Mazza, T., Ecker, G. F., & Indiveri, C. (2020) · Scientific Reports · doi:10.1038/s41598-020-73757-y · Cited by 31 · see citing works
Self-citationMetabolic and oncogenic adaptations to pyruvate dehydrogenase inactivation in fibroblasts
Wang, H., Lu, J. L., Kulkarni, S., Zhang, W., Gorka, J. E., Mandel, J. A., Goetzman, E. S., & Prochownik, E. V. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005200 · Cited by 29 · see citing works
Aria, H., Rezaei, M., Nazem, S., Daraei, A., Nikfar, G., Mansoori, B., Bahmanyar, M., Tavassoli, A., Vakil, M. K., & Mansoori, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.947885 · Cited by 26 · see citing works
Antunes, A. P. D. O. L., Carmo, F., Pinto, S., Andrade, N., & Martel, F. (2022) · PharmaNutrition · doi:10.1016/j.phanu.2022.100320 · Cited by 27 · see citing works
Lee, S. R., ROH, J., Ryu, J., Shin, H., & Hong, E. (2022) · Cell & Bioscience · doi:10.1186/s13578-021-00740-z · Cited by 26 · see citing works
The Role of Metabolic Plasticity in Blood and Brain Stem Cell Pathophysiology
Libby, C. J., McConathy, J., Darley-Usmar, V. M., & Hjelmeland, A. B. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1169 · Cited by 25 · see citing works
Insights into the Transport Cycle of LAT1 and Interaction with the Inhibitor JPH203
Brunocilla, C., Console, L., Rovella, F., & Indiveri, C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24044042 · Cited by 24 · see citing works
Self-citationMetabolic Changes in Polycystic Kidney Disease as a Potential Target for Systemic Treatment
Haumann, S., Müller, R., & Liebau, M. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176093 · Cited by 23 · see citing works
Tumor metabolism rewiring in epithelial ovarian cancer
Wang, M., Zhang, J., & Wu, Y. (2023) · Journal of Ovarian Research · doi:10.1186/s13048-023-01196-0 · Cited by 23 · see citing works
Homology Modeling Informs Ligand Discovery for the Glutamine Transporter ASCT2
Garibsingh, R. A., Otte, N. J., Ndaru, E., Colas, C., Grewer, C. T., Holst, J., & Schlessinger, A. (2018) · Frontiers in Chemistry · doi:10.3389/fchem.2018.00279 · Cited by 23 · see citing works
Wang, X., Xiao-xia, Y., Peng-Fei, S., Zong-Xue, Z., & Xiu-li, G. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175323 · Cited by 23 · see citing works
Zhang, J., Chen, M., Yang, Y., Liu, Z., Guo, W., Xiang, P., Zeng, Z., Wang, D., & Xiong, W. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.31349 · Cited by 23 · see citing works
Scalise, M., Pochini, L., Cosco, J., Aloe, E., Mazza, T., Console, L., Esposito, A., & Indiveri, C. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00110 · Cited by 22 · see citing works
Self-citationAlternative Energy: Breaking Down the Diverse Metabolic Features of Lung Cancers
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- Authors
- Scalise, M., Pochini, L., Galluccio, M., Console, L., & Indiveri, C.
- Affiliations
- University of Calabria (IT)
- Institute of Biomembranes, Bioenergetics and Molecular Biotechnologies (IT)
- Corresponding author
- Indiveri, Cesare
- Venue
- Frontiers in Oncology
- Publisher
- Frontiers Media SA
- Published
- 2017-12-11
- Volume
- 7
- Pages
- 306-306
- ISSN
- 2234-943X (ISSN-L)
- PMC
- PMC5770653
- OpenAlex
- W2773957517
- Cited by
- 183
- References
- 98
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 19 · 2023: 22 · 2022: 24 · 2021: 23 · 2020: 34 · 2019: 18 · 2018: 13
- FWCI
- 1.78
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Oncology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive of Doctoral Theses and Digital Collections (University of Calabria) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministero dell’Istruzione, dell’Università e della Ricerca (PON_01_00937)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- 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
- Keywords
- glutamine transport, mitochondrial metabolism, cancer cell growth, cancer metabolism, glutamine metabolism, glutaminase, glutamate, alpha-ketoglutarate, TCA cycle, metabolic reprogramming, aerobic glycolysis, amino acid transporters, ASCT2, LAT1, GLUT transporters
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