The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Spare Respiratory Capacity Rather Than Oxidative Stress Regulates Glutamate Excitotoxicity after Partial Respiratory Inhibition of Mitochondrial Complex I with Rotenone
Open accessAbstract
Partial inhibition of mitochondrial respiratory complex I by rotenone reproduces aspects of Parkinson's disease in rodents. The hypothesis that rotenone enhancement of neuronal cell death is attributable to oxidative stress was tested in an acute glutamate excitotoxicity model using primary cultures of rat cerebellar granule neurons. As little as 5 n m rotenone increased mitochondrial superoxide (O 2·−) levels and potentiated glutamate-induced cytoplasmic Ca 2+deregulation, the first irreversible stage of necrotic cell death. However, the potent cell-permeant O 2·−trap manganese tetrakis (N-ethylpyridinium-2yl) porphyrin failed to prevent the effects of the inhibitor. The bioenergetic consequences of rotenone addition were quantified by monitoring cell respiration. Glutamate activation of NMDA receptors used the full respiratory capacity of the in situ mitochondria, and >80% of the glutamate-stimulated respiration was attributable to increased cellular ATP demand. Rotenone at 20 n m inhibited basal and carbonyl cyanide p-trifluoromethoxyphenylhydrazone-stimulated cell respiration and caused respiratory failure in the presence of glutamate. ATP synthase inhibition by oligomycin was also toxic in the presence of glutamate. We conclude that the cell vulnerability in the rotenone model of partial complex I deficiency under these specific conditions is primarily determined by spare respiratory capacity rather than oxidative stress.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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 [14]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases
Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Li, N., Ragheb, K., Lawler, G., Sturgis, J., Rajwa, B. P., Melendez, J. A., & Robinson, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210432200 · Cited by 1,465
Mitochondria and neuronal survival
Nicholls, D. G., & Budd, S. L. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.315 · Cited by 1,243
Self-citationNMDA-dependent superoxide production and neurotoxicity
Lafon‐Cazal, M., Pietri, S., Culcasi, M., & Bockaert, J. (1993) · Nature · doi:10.1038/364535a0 · Cited by 1,183
Mitochondria and neuronal activity
Kann, O., & Kovács, R. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00222.2006 · Cited by 871
Keeney, P. M., Xie, J., Capaldi, R., & Bennett, J. P. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0984-06.2006 · Cited by 765
Schapira, A. H. V. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68970-8 · Cited by 617
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
Kudin, A. P., Bimpong‐Buta, N., Vielhaber, S., Elger, C. E., & Kunz, W. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310341200 · Cited by 514
Budd, S. L., & Nicholls, D. G. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67062282.x · Cited by 435
Self-citation
Cited by
Sorted by citations
Assessing mitochondrial dysfunction in cells
Brand, M. D., & Nicholls, D. G. (2011) · Biochemical Journal · doi:10.1042/bj20110162 · Cited by 2,436
Self-citationMitochondrial respiratory capacity is a critical regulator of CD8+ T cell memory development
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
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
Dong, X.-X., Wang, Y., & Qin, Z.-H. (2009) · Acta Pharmacologica Sinica · doi:10.1038/aps.2009.24 · Cited by 1,297
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
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
Brain Glucose Metabolism: Integration of Energetics with Function
Dienel, G. A. (2018) · Physiological Reviews · doi:10.1152/physrev.00062.2017 · Cited by 911
Exner, N., Lutz, A. K., Haass, C., & Winklhofer, K. F. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.170 · Cited by 677
Bordt, E. A., Clerc, P., Roelofs, B. A., Saladino, A. J., Tretter, L., Ádám‐Vizi, V., Cherok, E., Khalil, A., Yadava, N., Ge, S. X., et al. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.02.020 · Cited by 605
Self-citationThe role of mitochondria in insulin resistance and type 2 diabetes mellitus
Szendroedi, J., Phielix, E., & Roden, M. (2012) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.138 · Cited by 600
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-citationSuperoxide Dismutase Mimics: Chemistry, Pharmacology, and Therapeutic Potential
Batinic̈‐Haberle, I., Reboucas, J. S., & Spasojević, I. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2876 · Cited by 539
Integration of cellular bioenergetics with mitochondrial quality control and autophagy
Hill, B. G., Benavides, G. A., Lancaster, J. R., Ballinger, S. W., Dell’Italia, L., Zhang, J., & Darley-Usmar, V. M. (2012) · Biological Chemistry · doi:10.1515/hsz-2012-0198 · Cited by 495
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
Figueira, T. R., de Barros, M. H., Camargo, A. A., Castilho, R. F., Ferreira, J. C. B., Kowaltowski, A. J., Sluse, F. E., de Souza-Pinto, N. C., & Vercesi, A. E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4729 · Cited by 430
Crompton, J. G., Sukumar, M., Roychoudhuri, R., Clever, D. C., Gros, A., Eil, R. L., Tran, E., Hanada, K., Yu, Z., Palmer, D. C., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-2277 · Cited by 354
Marchetti, P., Fovez, Q., Germain, N., Khamari, R., & Kluza, J. (2020) · The FASEB Journal · doi:10.1096/fj.202000767r · Cited by 321
Hill, B. G., Dranka, B. P., Zou, L., Chatham, J. C., & Darley-Usmar, V. M. (2009) · Biochemical Journal · doi:10.1042/bj20090934 · Cited by 284
Toxin Models of Mitochondrial Dysfunction in Parkinson's Disease
Martinez, T. N., & Greenamyre, J. T. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4033 · Cited by 279
Mitochondrial involvement and oxidative stress in temporal lobe epilepsy
Rowley, S. D., & Patel, M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.02.002 · Cited by 257
Pfleger, J. M., He, M., & Abdellatif, M. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.202 · Cited by 251
Fukui, H., & Moraes, C. T. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.02.008 · Cited by 250
Wang, W., Osenbroch, P. Ø., Skinnes, R., Esbensen, Y., Bjørås, M., & Eide, L. (2010) · Stem Cells · doi:10.1002/stem.542 · Cited by 242
Positron emission tomography and functional characterization of a complete PBR/TSPO knockout
Banati, R. B., Middleton, R. J., Chan, R., Hatty, C. R., Wai-Ying Kam, W., Quin, C., Graeber, M. B., Parmar, A., Zahra, D., Callaghan, P., et al. (2014) · Nature Communications · doi:10.1038/ncomms6452 · Cited by 241
Optical probes and techniques for O2 measurement in live cells and tissue
Dmitriev, R. I., & Papkovsky, D. B. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0914-0 · Cited by 231
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
Is There a Link between Mitochondrial Reserve Respiratory Capacity and Aging?
Desler, C., Hansen, T. L., Frederiksen, J. H., Espersen, M. L. M., Singh, K. K., & Rasmussen, L. J. (2012) · Journal of Aging Research · doi:10.1155/2012/192503 · Cited by 237
Mitochondrial calcium function and dysfunction in the central nervous system
Nicholls, D. G. (2009) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.03.010 · Cited by 213
Self-citationSchneider, L. E., Giordano, S. S., Zelickson, B. R., Johnson, M. S., Benavides, G. A., Ouyang, X., Fineberg, N. S., Darley-Usmar, V. M., & Zhang, J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.08.030 · Cited by 210
Choi, S. W., Gerencser, A. A., & Nicholls, D. G. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06055.x · Cited by 204
Self-citationOxidative Stress and Energy Crises in Neuronal Dysfunction
Nicholls, D. G. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.002 · Cited by 205
Self-citationMeasuring 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
Peng, H., Wang, Q., Lou, T., Qin, J., Jung, S. Y., Shetty, V., Li, F., Wang, Y., Feng, X., Mitch, W. E., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01646-6 · Cited by 197
Bioenergetics of cerebral ischemia: A cellular perspective
Hertz, L. (2008) · Neuropharmacology · doi:10.1016/j.neuropharm.2008.05.023 · Cited by 196
Xiao, D., Powolny, A. A., de Moura, M. B., Kelley, E. E., Bommareddy, A., Kim, S., Hahm, E., Normolle, D. P., Houten, B. V., & Singh, S. V. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.063255 · Cited by 176
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
Dienel, G. A. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24015 · Cited by 168
Li, 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
Anandhan, A., Jacome, M. S., Lei, S., Hernández-Franco, P., Pappa, A., Panayiotidis, M. I., Powers, R., & Franco, R. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.009 · Cited by 165
Spare respiratory capacity, oxidative stress and excitotoxicity
Nicholls, D. G. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371385 · Cited by 161
Self-citationSiddiqui, A., Rivera, S., Castro, M. D. R., Acevedo‐Torres, K., Rane, A., Torres‐Ramos, C. A., Nicholls, D. G., Andersen, J. K., & Ayala‐Torres, S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.06.008 · Cited by 154
Self-citationOxidative Stress in Parkinson’s Disease: Potential Benefits of Antioxidant Supplementation
Percário, S., Barbosa, A. D. S., Varela, E. L. P., Gomes, A. R. Q., Ferreira, M. E. S., Moreira, T. D. N. A., & Dolabela, M. F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2360872 · Cited by 158
Sansbury, B. E., Jones, S. P., Riggs, D. W., Darley-Usmar, V. M., & Hill, B. G. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.12.002 · Cited by 149
Xun, Z., Rivera, S., Ayala‐Peña, S., Lim, J. I., Budworth, H., Skoda, E. M., Robbins, P. D., Niedernhofer, L. J., Wipf, P., & McMurray, C. T. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.10.001 · Cited by 155
C9orf72 regulates energy homeostasis by stabilizing mitochondrial complex I assembly
Wang, T., Liu, H., Itoh, K., Oh, S., Zhao, L., Murata, D., Sesaki, H., Härtung, T., Na, C. H., & Wang, J. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.01.005 · Cited by 154
Ju, W., Perkins, G. A., Keun-young Kim, A., Bastola, T., Choi, W.-Y., & Choi, S. (2022) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2022.101136 · Cited by 152
Siracusa, R., Scuto, M. C., Fusco, R., Salinaro, A. T., Ontario, M. L., Crea, R., Paola, R. D., Cuzzocrea, S., & Calabrese, V. (2020) · Antioxidants · doi:10.3390/antiox9090824 · Cited by 147
Role of oxidative DNA damage in mitochondrial dysfunction and Huntington’s disease pathogenesis
Ayala‐Peña, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.017 · Cited by 147
Esterházy, D., King, M. S., Yakovlev, G., & Hirst, J. (2008) · Biochemistry · doi:10.1021/bi702243b · Cited by 144
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
Shaltouki, A., Sivapatham, R., Pei, Y., Gerencser, A. A., Momčilović, O., Rao, M. S., & Zeng, X. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.02.019 · Cited by 131
Mitochondrial Structure, Function and Dynamics Are Temporally Controlled by c-Myc
Graves, J. A., Wang, Y., Sims‐Lucas, S., Cherok, E., Rothermund, K. D., Branca, M. F., Elster, J. D., Beer–Stolz, D., Houten, B. V., Vockley, J. E., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037699 · Cited by 128
Perez, J. N., Hill, B. G., Benavides, G. A., Dranka, B. P., & Darley-Usmar, V. M. (2010) · Biochemical Journal · doi:10.1042/bj20100090 · Cited by 125
PGC-1α controls mitochondrial biogenesis and dynamics in lead-induced neurotoxicity
Dabrowska, A. F., Venero, J. L., Iwasawa, R., Hankir, M. K., Rahman, S., Boobis, A. R., & Hajji, N. (2015) · Aging · doi:10.18632/aging.100790 · Cited by 126
Loss of OPA1 disturbs cellular calcium homeostasis and sensitizes for excitotoxicity
Kushnareva, Y. E., Gerencser, A. A., Bossy, B., Ju, W.-K., White, A. D., Waggoner, J., Ellisman, M. H., Perkins, G. A., & Bossy‐Wetzel, E. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.128 · Cited by 115
Zhao, L., Liu, Y., Zhang, S., Wei, L., Cheng, H., Wang, J., & Wang, J. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04821-w · Cited by 115
Zhu, J., Gusdon, A. M., Çimen, H., Houten, B. V., Koç, E., & Chu, C. T. (2012) · Cell Death and Disease · doi:10.1038/cddis.2012.46 · Cited by 109
Tauroursodeoxycholic Acid Prevents Retinal Degeneration in Transgenic P23H Rats
Fernández‐Sánchez, L., Lax, P., Pinilla, I., Martín‐Nieto, J., & Cuenca, N. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-7496 · Cited by 110
Unravelling mitochondrial pathways to P arkinson's disease
Celardo, I., Martins, L. M., & Gandhi, S. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12433 · Cited by 105
Bajpai, R., Sharma, A., Achreja, A., Edgar, C. L., Wei, C., Siddiqa, A., Gupta, V. A., Matulis, S. M., McBrayer, S. K., Mittal, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15051-z · Cited by 103
Martínez, E. M. G., Sanz‐Blasco, S., Karachitos, A., Bández, M. J., Fernández-Gómez, F.-J., Perez‐Alvarez, S., de Mera, R. M. M.-F., Jordán, M. J., Aguirre, N., Galindo, M. F., et al. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.07.028 · Cited by 103
Armstrong, J. A., Cash, N. J., Ouyang, Y., Morton, J. C., Chvanov, M., Latawiec, D., Awais, M., Tepikin, A. V., Sutton, R., & Criddle, D. N. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003200 · Cited by 105
Rueda, C. B., Llorente‐Folch, I., Traba, J., Amigo, I., González‐Sánchez, P., Contreras, L., Juaristi, I., Martínez-Valero, P., Pardo, B., del Arco, A., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.04.003 · Cited by 100
Yang, J., Tadokoro, T., Keijzers, G., Mattson, M. P., & Bohr, V. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082883 · Cited by 94
Rotenone induces neuronal death by microglial phagocytosis of neurons
Emmrich, J., Hornik, T. C., Neher, J. J., & Brown, G. C. (2013) · FEBS Journal · doi:10.1111/febs.12401 · Cited by 93
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
Fumarate hydratase is a critical metabolic regulator of hematopoietic stem cell functions
Guitart, A. V., Panagopoulou, T. I., Villacreces, A., Vukovic, M., Sepulveda, C., Allen, L., Carter, R. N., van de Lagemaat, L. N., Morgan, M., Giles, P., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20161087 · Cited by 86
Freestone, P. S., Chung, K. K. H., Guatteo, E., Mercuri, N. B., Nicholson, L. F. B., & Lipski, J. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06990.x · Cited by 85
Kong, Y. X. G., Bergen, N. V., Bui, B. V., Chrysostomou, V., Vingrys, A. J., Trounce, I. A., & Crowston, J. G. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.026 · Cited by 85
Measuring mitochondrial respiration in intact single muscle fibers
Schuh, R. A., Jackson, K. C., Khairallah, R. J., Ward, C. W., & Spangenburg, E. E. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00229.2011 · Cited by 85
Ghițu, A., Schwiebs, A., Radeke, H. H., Avram, Ș., Zupkó, I., Bor, A., Pavel, I. Z., Dehelean, C. A., Oprean, C., Bojin, F. M., et al. (2019) · Nutrients · doi:10.3390/nu11040858 · Cited by 82
DJ-1 knock-down impairs astrocyte mitochondrial function
Larsen, N. J., Ambrosi, G., Mullett, S. J., Berman, S. B., & Hinkle, D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.016 · Cited by 82
MicroRNAs Regulate Mitochondrial Function in Cerebral Ischemia-Reperfusion Injury
Hu, Y. H., Deng, H., Xu, S., & Zhang, J. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161024895 · Cited by 81
A combined in vitro approach to improve the prediction of mitochondrial toxicants
Eakins, J. A., Bauch, C., Woodhouse, H. J., Park, B. J., Bevan, S. J., Dilworth, C., & Walker, P. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.03.016 · Cited by 79
Fluorescent probes for in vitro and in vivo quantification of hydrogen peroxide
Ye, S., Hu, J. J., Zhao, Q. A., & Yang, D. (2020) · Chemical Science · doi:10.1039/d0sc04888g · Cited by 80
Mitochondrial and Bioenergetic Dysfunction in Trauma-Induced Painful Peripheral Neuropathy
Lim, T. K. Y., Rone, M. B., Lee, S., Antel, J. P., & Zhang, J. (2015) · Molecular Pain · doi:10.1186/s12990-015-0057-7 · Cited by 78
Rodríguez‐Rocha, H., García‐García, A., Pickett, C. S., Li, S., Jones, J., Chen, H., Webb, B., Choi, J. H., Zhou, Y., Zimmerman, M. C., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.021 · Cited by 80
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
Ramanathan, R., Kiyimba, F., Gonzalez, J. M., Mafi, G. G., & DeSilva, U. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c01884 · Cited by 83
Amadoro, G., Corsetti, V., Florenzano, F., Atlante, A., Bobba, A., Nicolin, V., Nori, S. L., & Calissano, P. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00018 · Cited by 77
Nicoletti, V., Palermo, G., Prete, E. D., Mancuso, M., & Ceravolo, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.636506 · Cited by 75
Xun, Z., Lee, D. Y., Lim, J. I., Canaria, C. A., Barnebey, A., Yanonne, S., & McMurray, C. T. (2012) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2012.01.008 · Cited by 73
Assaying Mitochondrial Respiration as an Indicator of Cellular Metabolism and Fitness
Smolina, N., Bruton, J. D., Kostareva, A. A., & Sejersen, T. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6960-9_7 · Cited by 73
Colorectal cancer cells respond differentially to autophagy inhibition in vivo
Lauzier, A., Normandeau-Guimond, J., Vaillancourt‐Lavigueur, V., Boivin, V., Charbonneau, M., Rivard, N., Scott, M. S., Dubois, C. M., & Jean, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-47659-7 · Cited by 75
Retained features of embryonic metabolism in the adult MRL mouse
Naviaux, R. K., Le, T. P., Bedelbaeva, K., Leferovich, J. M., Gourevitch, D., Sachadyn, P., Zhang, X., Clark, L. D., & Heber‐Katz, E. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2008.11.164 · Cited by 72
Yamamoto, H., Morino, K., Lemecha, M., Taishi, I., Kiriyama, K., Ikami, T., & Maegawa, H. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1735841 · Cited by 73
Beyond autophagy: a novel role for autism-linked Wdfy3 in brain mitophagy
Napoli, E., Song, G., Panoutsopoulos, A. A., Riyadh, M. A., Kaushik, G., Halmai, J. A. N. M., Levenson, R., Zarbalis, K. S., & Giulivi, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-29421-7 · Cited by 73
Oxidative stress induces mitochondrial dysfunction in a subset of autistic lymphoblastoid cell lines
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
Deletion of a Neuronal Drp1 Activator Protects against Cerebral Ischemia
Flippo, K. H., Lin, Z., Dickey, A. S., Zhou, X., Dhanesha, N., Walters, G. C., Liu, Y., Merrill, R. A., Meller, R., Simon, R. P., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1926-19.2020 · Cited by 72
Cerqueira, F. M., da Cunha, F. M., Laurindo, F. R. M., & Kowaltowski, A. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.01.011 · Cited by 71
Methylene Blue Provides Behavioral and Metabolic Neuroprotection Against Optic Neuropathy
Rojas, J. C., John, J. M., Lee, J., & Gonzalez-Lima, F. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9027-z · Cited by 71
Excitotoxicity Revisited: Mitochondria on the Verge of a Nervous Breakdown
Plotegher, N., Filadi, R., Pizzo, P., & Duchen, M. R. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2021.01.001 · Cited by 65
Reactive oxygen species regulation by AIF- and complex I-depleted brain mitochondria
Chinta, S. J., Rane, A., Yadava, N., Andersen, J. K., Nicholls, D. G., & Polster, B. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.010 · Cited by 64
Self-citationRačay, P., Tatarková, Z., Chomová, M., Hatok, J., Kaplán, P., & Dobrota, D. (2009) · Neurochemical Research · doi:10.1007/s11064-009-9934-7 · Cited by 62
Mitochondrial Dysfunction Impairs Tumor Suppressor p53 Expression/Function
Compton, S. L., Kim, C. G., Griner, N. B., Potluri, P., Scheffler, I. E., Sen, S., Jerry, D. J., Schneider, S. S., & Yadava, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163063 · Cited by 62
Self-citationOrgan reserve, excess metabolic capacity, and aging
Atamna, H., Tenore, A., Lui, F., & Dhahbi, J. M. (2018) · Biogerontology · doi:10.1007/s10522-018-9746-8 · Cited by 72
Rueda, C. B., Traba, J., Amigo, I., Llorente‐Folch, I., González‐Sánchez, P., Pardo, B., Esteban, J. A., del Arco, A., & Satrústegui, J. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2702-14.2015 · Cited by 62
Human cytomegalovirus infection increases mitochondrial biogenesis
Kaarbø, M., Ager-Wick, E., Osenbroch, P. Ø., Kilander, A., Skinnes, R., Müller, F., & Eide, L. (2011) · Mitochondrion · doi:10.1016/j.mito.2011.08.008 · Cited by 60
Platelets from pulmonary hypertension patients show increased mitochondrial reserve capacity
Nguyen, Q. L., Corey, C. G., White, P., Watson, A. M. M., Gladwin, M. T., Simon, M. A. M., & Shiva, S. (2017) · JCI Insight · doi:10.1172/jci.insight.91415 · Cited by 60
Metadata
- Authors
- Yadava, N., & Nicholls, D. G.
- Affiliations
- Buck Institute for Research on Aging (US)
- Corresponding author
- Nicholls, David G.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2007-07-04
- Volume
- 27
- Issue
- 27
- Pages
- 7310-7317
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6794596
- OpenAlex
- W2061113435
- Cited by
- 272
- References
- 39
- Citations by year
- 2026: 5 · 2025: 3 · 2024: 3 · 2023: 6 · 2022: 14 · 2021: 11 · 2020: 23 · 2019: 15 · 2018: 17 · 2017: 22 · 2016: 22 · 2015: 15 · 2014: 15 · 2013: 17 · 2012: 24
- FWCI
- 5.04
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (R01 AG2 1440, R01AG021440)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- rotenone, mitochondrial complex I deficiency, Parkinson's disease model, glutamate excitotoxicity, oxidative stress, spare respiratory capacity, mitochondrial superoxide, manganese porphyrin, necrosis, NMDA receptor, ATP demand, mitochondrial respiration, oligomycin, ATP synthase inhibition, cerebellar granule cells
- MeSH terms
- Animals, Mitochondria, Rotenone, Cell Death, Rats, Wistar, Oxidative Stress, Excitatory Amino Acid Agonists, Glutamic Acid, Cell Respiration, Electron Transport Complex I, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
