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Spare respiratory capacity, oxidative stress and excitotoxicity
Abstract
Chronic exposure to glutamate (glutamate excitotoxicity) exacerbates neuronal damage in the aftermath of stroke and is implicated in a variety of neurodegenerative disorders. Mitochondria play a central role in the survival or death of the exposed neuron. Calcium, oxidative stress and ATP insufficiency play closely interlocked roles that may be investigated with primary neuronal cultures.
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“Under increased workload, stress, or nutrient limitation, cells engage this reserve capacity to generate more energy and promote cell viability (14, 15).”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [15]
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Cites
Glutamate and the pathophysiology of hypoxic–ischemic brain damage
Rothman, S. M., & Olney, J. W. (1986) · Annals of Neurology · doi:10.1002/ana.410190202 · Cited by 2,428
Korshunov, S. S., Skulachev, V. P., & Starkov, A. A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01159-9 · Cited by 1,727
Glutamate neurotoxicity in cortical cell culture
Choi, D. W., Maulucci-Gedde, M., & Kriegstein, A. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-02-00357.1987 · Cited by 1,506
NMDA-dependent superoxide production and neurotoxicity
Lafon‐Cazal, M., Pietri, S., Culcasi, M., & Bockaert, J. (1993) · Nature · doi:10.1038/364535a0 · Cited by 1,183
Glutamate release in severe brain ischaemia is mainly by reversed uptake
Rossi, D. J., Oshima, T., & Attwell, D. (2000) · Nature · doi:10.1038/35002090 · Cited by 1,128
The release and uptake of excitatory amino acids
Nicholls, D. G., & Attwell, D. (1990) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(90)90129-v · Cited by 1,092
Self-citationNovelli, A., Reilly, J. A., Lysko, P. G., & Henneberry, R. C. (1988) · Brain Research · doi:10.1016/0006-8993(88)90765-2 · Cited by 961
Mayer, M. L., & Westbrook, G. L. (1987) · The Journal of Physiology · doi:10.1113/jphysiol.1987.sp016883 · Cited by 943
Glutamate-induced neuron death requires mitochondrial calcium uptake
Stout, A. K., Raphael, H. M., Kanterewicz, B. I., Klann, E., & Reynolds, I. J. (1998) · Nature Neuroscience · doi:10.1038/1577 · Cited by 630
The mitochondrial permeability transition from in vitro artifact to disease target
Bernardi, P., Krauskopf, A., Basso, E., Petronilli, V., Blalchy‐Dyson, E., Di Lisa, F., & Forte, M. A. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05213.x · Cited by 627
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- Wabnitz, 2006, The permeability transition pore is not a prerequisite for glutamate-induced calcium deregulation and mitochondrial depolarization in brain neurons, Biol. Membr., 22, 346
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van der Windt, G. J. W., Everts, B., Chang, C.-H., Curtis, J. D., Freitas, T. C., Amiel, E., Pearce, E. J., & Pearce, E. L. (2012) · Immunity · doi:10.1016/j.immuni.2011.12.007 · Cited by 1,540
Mitochondrial Dynamics Controls T Cell Fate through Metabolic Programming
Buck, M. D., O’Sullivan, D., Geltink, R. I. K., Curtis, J. D., Chang, C., Sanin, D. E., Qiu, J., Kretz, O., Braas, D., van der Windt, G. J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.05.035 · Cited by 1,491
Fueling Immunity: Insights into Metabolism and Lymphocyte Function
Pearce, E. L., Poffenberger, M. C., Chang, C.-H., & Jones, R. G. (2013) · Science · doi:10.1126/science.1242454 · Cited by 1,363
Kawalekar, O. U., O’Connor, R. S., Fraietta, J. A., Guo, L., McGettigan, S. E., Posey, A. D., Patel, P. R., Guedan, S., Scholler, J., Keith, B., et al. (2016) · Immunity · doi:10.1016/j.immuni.2016.01.021 · Cited by 1,267
Patsoukis, N., Bardhan, K., Chatterjee, P., Sari, D., Liu, B., Bell, L. N., Karoly, E. D., Freeman, G. J., Petkova, V., Seth, P., et al. (2015) · Nature Communications · doi:10.1038/ncomms7692 · Cited by 1,249
Mitochondria are the powerhouses of immunity
Mills, E. L., Kelly, B., & O'Neill, L. A. J. (2017) · Nature Immunology · doi:10.1038/ni.3704 · Cited by 1,161
Metabolic switching and fuel choice during T‐cell differentiation and memory development
van der Windt, G. J. W., & Pearce, E. L. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01150.x · Cited by 563
Mookerjee, S. A., Gerencser, A. A., Nicholls, D. G., & Brand, M. D. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.774471 · Cited by 550
Self-citationCD8 memory T cells have a bioenergetic advantage that underlies their rapid recall ability
van der Windt, G. J. W., O’Sullivan, D., Everts, B., Huang, S. C.-C., Buck, M. D., Curtis, J. D., Chang, C.-H., Smith, A. M., Ai, T., Faubert, B., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221740110 · Cited by 523
Analysis and Interpretation of Microplate-Based Oxygen Consumption and pH Data
Divakaruni, A. S., Paradyse, A. R., Ferrick, D. A., Murphy, A. N., & Jastroch, M. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-801415-8.00016-3 · Cited by 543
The Regulation and Physiology of Mitochondrial Proton Leak
Divakaruni, A. S., & Brand, M. D. (2011) · Physiology · doi:10.1152/physiol.00046.2010 · Cited by 514
Brain lactate metabolism: the discoveries and the controversies
Dienel, G. A. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.175 · Cited by 479
Calcium‐dependent mitochondrial function and dysfunction in neurons
Pivovarova, N. B., & Andrews, S. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07754.x · Cited by 389
Marchetti, P., Fovez, Q., Germain, N., Khamari, R., & Kluza, J. (2020) · The FASEB Journal · doi:10.1096/fj.202000767r · Cited by 321
Neuronal vulnerability, pathogenesis, and Parkinson's disease
Sulzer, D., & Surmeier, D. J. (2012) · Movement Disorders · doi:10.1002/mds.25095 · Cited by 323
Loss of the Tumor Suppressor LKB1 Promotes Metabolic Reprogramming of Cancer Cells via HIF-1α
Faubert, B., Vincent, E. E., Griss, T., Samborska, B., Izreig, S., Svensson, R. U., Mamer, O. A., Avizonis, D., Shackelford, D. B., Shaw, R. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312570111 · Cited by 278
Mitochondrial Dysfunction in Airway Disease
Prakash, Y. S., Pabelick, C. M., & Sieck, G. C. (2017) · CHEST Journal · doi:10.1016/j.chest.2017.03.020 · Cited by 267
Pfleger, J. M., He, M., & Abdellatif, M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.202 · Cited by 251
Role of sigma-1 receptors in neurodegenerative diseases
Nguyen, L., Lucke-Wold, B. P., Mookerjee, S. A., Cavendish, J. Z., Robson, M. J., Scandinaro, A. L., & Matsumoto, R. R. (2014) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2014.12.005 · Cited by 236
Clinical and Molecular Characteristics of Mitochondrial Dysfunction in Autism Spectrum Disorder
Rose, S., Niyazov, D. M., Rossignol, D. A., Goldenthal, M. J., Kahler, S. G., & Frye, R. E. (2018) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-018-0352-x · Cited by 237
Measuring Bioenergetics in T Cells Using a Seahorse Extracellular Flux Analyzer
van der Windt, G. J. W., Chang, C., & Pearce, E. L. (2016) · Current Protocols in Immunology · doi:10.1002/0471142735.im0316bs113 · Cited by 189
Neuronal vulnerability, pathogenesis, and Parkinson's disease
Sulzer, D., & Surmeier, D. J. (2013) · Movement Disorders · doi:10.1002/mds.25187 · Cited by 184
Rose, S., Frye, R. E., Slattery, J., Wynne, R., Tippett, M., Pavliv, O., Melnyk, S., & James, S. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085436 · Cited by 168
Fueling and Imaging Brain Activation
Dienel, G. A. (2012) · ASN NEURO · doi:10.1042/an20120021 · Cited by 175
Buskiewicz, I. A., Montgomery, T. L., Yasewicz, E. C., Huber, S. A., Murphy, M. P., Hartley, R. C., Kelly, R., Crow, M. K., Perl, A., Budd, R. C., et al. (2016) · Science Signaling · doi:10.1126/scisignal.aaf1933 · Cited by 181
Determining Maximum Glycolytic Capacity Using Extracellular Flux Measurements
Mookerjee, S. A., Nicholls, D. G., & Brand, M. D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0152016 · Cited by 167
Self-citationLi, W., Qiu, S., Chen, J., Jiang, S., Chen, W., Jiang, J., Wang, F., Si, W., Shu, Y., Wei, P., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.07.011 · Cited by 167
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Divakaruni, A. S., Wallace, M., Buren, C., Martyniuk, K. M., Andreyev, A. Y., Li, E., Fields, J. A., Cordes, T., Reynolds, I. J., Bloodgood, B. L., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201612067 · Cited by 169
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Divakaruni, A. S., & Jastroch, M. (2022) · Nature Metabolism · doi:10.1038/s42255-022-00619-4 · Cited by 162
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Cichocki, F. M., Wu, C., Zhang, B., Felices, M., Tesi, B., Tuininga, K., Dougherty, P., Taras, E., Hinderlie, P., Blazar, B. R., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20172168 · Cited by 131
Frye, R. E., Rose, S., Chacko, J., Wynne, R., Bennuri, S. C., Slattery, J. C., Tippett, M., Delhey, L., Melnyk, S., Kahler, S. G., et al. (2016) · Translational Psychiatry · doi:10.1038/tp.2016.189 · Cited by 130
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Dmitriev, R. I., Zhdanov, A. V., Nolan, Y. M., & Papkovsky, D. B. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.08.065 · Cited by 117
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Vasconcelos, A. R., dos Santos, N. B., Scavone, C., & Munhoz, C. D. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00033 · Cited by 113
Dhingra, A., Jayas, R., Afshar, P., Guberman, M., Maddaford, G. G., Gerstein, J., Lieberman, B., Nepon, H., Margulets, V., Dhingra, R., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.010 · Cited by 108
Rojas, F., González, D., Cortés, N., Ampuero, E., Hernández, D. E., Fritz, E., Abarzúa, S., Martinez, A. N., Elorza, Á. A., Alvarez, A. R., et al. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00203 · Cited by 97
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Fraser, K. A., Schenkel, J. M., Jameson, S. C., Vezys, V., & Masopust, D. (2013) · Immunity · doi:10.1016/j.immuni.2013.07.003 · Cited by 92
Norberg, E., Lako, A., Chen, P.-H., Stanley, I. A., Zhou, F., Ficarro, S. B., Chapuy, B., Chen, L., Rodig, S. J., Shin, D. H., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.116 · Cited by 87
Changing the energy of an immune response.
Delmastro-Greenwood, M. M., & Piganelli, J. D. (2013) · Europe PMC (PubMed Central) · Cited by 84
Wong, L. R., & Ho, P. C. (2017) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12836 · Cited by 79
Rose, S., Frye, R. E., Slattery, J., Wynne, R. A., Tippett, M., Melnyk, S., & James, S. J. (2015) · Translational Psychiatry · doi:10.1038/tp.2015.29 · Cited by 78
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Surmeier, D. J., & Sulzer, D. (2013) · Prion · doi:10.4161/pri.23582 · Cited by 74
Keuper, M., Jastroch, M., Yi, C., Fischer‐Posovszky, P., Wabitsch, M., Tschöp, M. H., & Hofmann, S. M. (2013) · The FASEB Journal · doi:10.1096/fj.13-238725 · Cited by 76
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Corrado, M., Edwards-Hicks, J., Villa, M., Flachsmann, L. J., Sanin, D. E., Jacobs, M. M. E., Baixauli, F., Stanczak, M. A., Anderson, E., Azuma, M., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.11.003 · Cited by 70
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Rose, S., Frye, R. E., Slattery, J. M., Wynne, R. A., Tippett, M., Melnyk, S., & James, S. J. (2014) · Translational Psychiatry · doi:10.1038/tp.2014.15 · Cited by 69
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Barbosa, D. J., Capela, J. P., Feio‐Azevedo, R., Gomes, A., Bastos, M. D. L., & Carvalho, F. D. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1478-9 · Cited by 70
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Zelickson, B. R., Benavides, G. A., Johnson, M. S., Chacko, B. K., Venkatraman, A., Landar, A. L., Betancourt, A. M., Bailey, S. M., & Darley-Usmar, V. M. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.09.011 · Cited by 66
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Yang, C., Wong, C.-M., Wei, J., Chung, A. C. K., & Cai, Z. (2018) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2018.07.087 · Cited by 62
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Mancini, Ö. K., Lora, M., Cuillerier, A., Shum‐Tim, D., Hamdy, R. C., Burelle, Y., Servant, M. J., Stochaj, U., & Colmegna, I. (2017) · Circulation Research · doi:10.1161/circresaha.117.311400 · Cited by 56
Lin, H., Naito, K., Oh, Y., Farber, G., Kanaan, G. N., Valaperti, A., Dawood, F., Zhang, L., Li, G. H., Smyth, D. R., et al. (2020) · Circulation · doi:10.1161/circulationaha.119.041213 · Cited by 54
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Park, B. V., & Pan, F. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.07.027 · Cited by 58
Aravamudan, B., Thompson, M., Sieck, G. C., Vassallo, R., Pabelick, C. M., & Prakash, Y. S. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25508 · Cited by 52
Navneet, S., Zhao, J., Wang, J., Mysona, B. A., Barwick, S. R., Kaidery, N. A., SAUL, A. B., Kaddour‐Djebbar, I., Bollag, W. B., Thomas, B., et al. (2019) · Redox Biology · doi:10.1016/j.redox.2019.101199 · Cited by 53
High density lipoproteins selectively promote the survival of human regulatory T cells
Rueda, C. M., Rodríguez-Perea, A. L., Moreno‐Fernandez, M. E., Jackson, C. M., Melchior, J., Davidson, W. S., & Chougnet, C. A. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m072835 · Cited by 57
Nickens, K. P., Wikström, J. D., Shirihai, O. S., Patierno, S. R., & Ceryak, S. M. (2013) · Mitochondrion · doi:10.1016/j.mito.2013.09.005 · Cited by 54
Lee, W.-H., Higuchi, H., Ikeda, S., Macke, E. L., Takimoto, T., Pattnaik, B. R., Liu, C., Chu, L.-F., Siepka, S. M., Krentz, K. J., et al. (2016) · eLife · doi:10.7554/elife.19264 · Cited by 52
Rose, S., Wynne, R. A., Frye, R. E., Melnyk, S., & James, S. J. (2015) · Journal of Toxicology · doi:10.1155/2015/573701 · Cited by 46
Clerc, P., Young, C. A., Bordt, E. A., Grigore, A. M., Fiskum, G. M., & Polster, B. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079982 · Cited by 45
Regulation of T cell immunity by cellular metabolism
Hu, Z., Zou, Q., & Su, B. (2018) · Frontiers of Medicine · doi:10.1007/s11684-018-0668-2 · Cited by 43
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Moult, P. R. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371317 · Cited by 43
Caiola, E., Falcetta, F., Giordano, S., Marabese, M., Garassino, M. C., Broggini, M., Pastorelli, R., & Brunelli, L. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0954-5 · Cited by 41
Jaber, S. M., Bordt, E. A., Bhatt, N. M., Lewis, D. M., Gerecht, S., Fiskum, G., & Polster, B. M. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.09.003 · Cited by 40
DiNuzzo, M., Dienel, G. A., Behar, K. L., Petroff, O. A. C., Benveniste, H., Hyder, F., Giove, F., Michaeli, S., Mangia, S., Herculano‐Houzel, S., et al. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15839 · Cited by 40
Dhingra, R., & Kirshenbaum, L. A. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.310 · Cited by 39
Metabolic reprogramming and apoptosis sensitivity: Defining the contours of a T cell response
Voss, K., Larsen, S. E., & Snow, A. L. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.08.033 · Cited by 38
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Nanjireddy, P., Olejniczak, S. H., & Buxbaum, N. P. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1121565 · Cited by 39
Nicholls, D. G., Brand, M. D., & Gerencser, A. A. (2014) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-014-9573-9 · Cited by 36
Self-citationAkrami, M., Menzies, R. J., Chamoto, K., Miyajima, M., Suzuki, R., Sato, H., Nishii, A., Tomura, M., Fagarasan, S., & Honjo, T. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2010981117 · Cited by 35
Surin, A. M., Khiroug, S. S., Gorbacheva, L. R., Khodorov, B. I., Pinelis, V. G., & Khiroug, L. (2013) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00102 · Cited by 36
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Gusdon, A. M., & Chu, C. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3763 · Cited by 34
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Rao, G., Murphy, B., Dey, A., Dwivedi, S. K. D., Zhang, Y., Roy, R. V., Chakraborty, P. K., Bhattacharya, R., & Mukherjee, P. (2020) · The FASEB Journal · doi:10.1096/fj.202000173r · Cited by 33
Altintas, M. M., DiBartolo, S., Tadros, L., Samelko, B., & Wasse, H. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.629239 · Cited by 32
Jones, A. E., Li, S., Acevedo, A., Veliova, M., Shirihai, O. S., Stiles, L., & Divakaruni, A. S. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00235.2020 · Cited by 33
Qiu, L., Yu, H., & Liang, F. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13251 · Cited by 29
Forget, M., Haymaker, C., Dennison, J. B., Toth, C., Maiti, S. N., Fulbright, O. J., Cooper, L. J. N., Hwu, P., Radvanyi, L. G., & Bernatchez, C. (2015) · OncoImmunology · doi:10.1080/2162402x.2015.1057386 · Cited by 30
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Chen, Z., Dudek, J., Maack, C., & Hofmann, U. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114597 · Cited by 31
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Aggarwal, A., Aggarwal, P., Khatak, M., & Khatak, S. (2010) · International Journal of Pharma and Bio Sciences · Cited by 30
Mancini, G., Dias, C., Lourenço, C. F., Laranjinha, J. A. N., Bem, A. F. D., & Ledo, A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210122 · Cited by 31
Nicotine affects mitochondrial structure and function in human airway smooth muscle cells
Borkar, N. A., Thompson, M. A., Bartman, C. M., Sathish, V., Prakash, Y. S., & Pabelick, C. M. (2023) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00158.2023 · Cited by 28
Jafri, A. J. A., Arfuzir, N. N. N., Lambuk, L., Iezhitsa, I. N., Agarwal, R., Agarwal, P., Razali, N., Krasilnikova, A. V., Kharitonova, M. V., Demidov, V. A., et al. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.09.005 · Cited by 28
Sarin, M., Wang, Y., Zhang, F., Rothermund, K., Zhang, Y., Lu, J. L., Sims‐Lucas, S., Beer–Stolz, D., Houten, B. V., Vockley, J., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.201 · Cited by 30
Thompson, E. A., Beura, L. K., Nelson, C. E., Anderson, K. G., & Vezys, V. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501797 · Cited by 27
Firgany, A. E. L., & Sarhan, N. R. (2020) · Acta Histochemica · doi:10.1016/j.acthis.2020.151554 · Cited by 27
Huang, Y., Kwan, K. K., Leung, K. W., Yao, P., Wang, H., Dong, T. T.-X., & Tsim, K. W. K. (2018) · Journal of Ginseng Research · doi:10.1016/j.jgr.2018.02.002 · Cited by 27
Immunobiology of chimeric antigen receptor T cells and novel designs
Walsh, Z. H., Yang, Y., & Kohler, M. E. (2019) · Immunological Reviews · doi:10.1111/imr.12794 · Cited by 27
Frye, R. E., Rose, S., Wynne, R. A., Bennuri, S. C., Blossom, S. J., Gilbert, K. M., Heilbrun, L. P., & Palmer, R. F. (2017) · Scientific Reports · doi:10.1038/s41598-017-04821-3 · Cited by 25
DHA Protects Against Zinc Mediated Alterations in Neuronal Cellular Bioenergetics
McGee, S. L., Sadli, N., Morrison, S., Swinton, C., & Suphioglu, C. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000331724 · Cited by 23
Evaluation of a Serum-Free Medium for Human Epithelial and Stromal Cell Culture
Caneparo, C., Chabaud, S., Fradette, J., & Bolduc, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231710035 · Cited by 26
NAD+ maintenance attenuates light induced photoreceptor degeneration
Bai, S., & Sheline, C. T. (2012) · Experimental Eye Research · doi:10.1016/j.exer.2012.12.007 · Cited by 22
Zhou, Y., Al-Saaidi, R. A., Guerra, P. F., Freude, K., Olsen, R. K. J., Jensen, U. B., Gregersen, N., Hyttel, P., Bolund, L., Aagaard, L., et al. (2016) · Stem Cells and Development · doi:10.1089/scd.2016.0162 · Cited by 21
Jeon, Y. H., He, M., Austin, J., Shin, H., Pfleger, J. M., & Abdellatif, M. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109866 · Cited by 20
Tian, H., Chai, D., Wang, G., Wang, Q., Sun, N., Jiang, G., Li, H., Song, J., Fang, L., Wang, M., et al. (2023) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-023-03407-5 · Cited by 21
Metadata
- Authors
- Nicholls, D. G.
- Affiliations
- Buck Institute for Research on Aging (US)
- Corresponding author
- Nicholls, David G.
- ORCID
- Nicholls, David G.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2009-11-19
- Volume
- 37
- Issue
- 6
- Pages
- 1385-1388
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2077752542
- Cited by
- 161
- References
- 32
- Citations by year
- 2026: 10 · 2025: 5 · 2024: 7 · 2023: 10 · 2022: 8 · 2021: 3 · 2020: 17 · 2019: 4 · 2018: 8 · 2017: 12 · 2016: 15 · 2015: 11 · 2014: 13 · 2013: 14 · 2012: 12
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- National Institute on Aging (R01 AG2 1440, P01AG025901)
- National Institute of Neurological Disorders and Stroke (R01 NS4 1908)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroprotection in Cerebral Ischemia
- Keywords
- glutamate excitotoxicity, spare respiratory capacity, oxidative stress, mitochondria, stroke, neurodegeneration, calcium, neuronal survival, primary neuronal cultures
- MeSH terms
- Adenosine Triphosphate, Animals, Mitochondria, Neurons, Neurotoxins, Receptors, N-Methyl-D-Aspartate, Receptors, Glutamate, Oxidative Stress, Glutamic Acid, Cell Respiration
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