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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–272 of 272
Uittenbogaard, M. N., Wang, H., Zhang, V. W., Wong, L. C., Brantner, C. A., Gropman, A. L., & Chiaramello, A. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.01.022 · Cited by 17
Testosterone Decreases Placental Mitochondrial Content and Cellular Bioenergetics
Mishra, J. S., Blesson, C. S., & Kumar, S. (2020) · Biology · doi:10.3390/biology9070176 · Cited by 16
Mitochondrial Dysfunction in Mitochondrial Medicine: Current Limitations, Pitfalls, and Tomorrow
Guéguen, N., Lenaers, G., Reynier, P., Weissig, V., & Edeas, M. A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1266-8_1 · Cited by 17
Kim, C., Potluri, P., Khalil, A., Gaut, D. L., McManus, M. J., Compton, S. L., Wallace, D. C., & Yadava, N. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.003 · Cited by 14
Self-citationChu‐Tan, J. A., Rutar, M., Saxena, K., Wu, Y., Howitt, L., Valter, K., Provis, J. M., & Natoli, R. (2016) · International Journal of Photoenergy · doi:10.1155/2016/2734139 · Cited by 14
Mechanism of neem limonoids-induced cell death in cancer: Role of oxidative phosphorylation
Yadav, N., Kumar, S., Kumar, R., Srivastava, P., Sun, L., Rapali, P., Marlowe, T. A., Schneider, A., Inigo, J. R., O’Malley, J., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.028 · Cited by 14
Self-citationYKL-40 and the Cellular Metabolic Profile in Parkinson’s Disease
Gevezova, M., Kazakova, M., Trenova, A. G., & Sarafian, V. S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216297 · Cited by 15
Ataxin-3 Links NOD2 and TLR2 Mediated Innate Immune Sensing and Metabolism in Myeloid Cells
Chapman, T., Corridoni, D., Shiraishi, S., Pandey, S., Aulicino, A., Wigfield, S., Costa, M. D. C., Thézénas, M., Paulson, H. L., Fischer, R., et al. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01495 · Cited by 13
Pandey, A. K., Sarkar, S., Yadav, S. K., Yadav, S., Srikrishna, S., Siddiqui, M. H., Parmar, D., & Yadav, S. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02667-5 · Cited by 13
Liu, Y., Li, C., Li, X., Tang, P., Liu, P., Hou, C., Zhang, X., & Li, R. (2017) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2017.4834 · Cited by 13
Mao, H., & Ding, L. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7853 · Cited by 12
Uittenbogaard, M. N., Brantner, C. A., Fang, Z., Wong, L. C., Gropman, A. L., & Chiaramello, A. (2018) · Mitochondrion · doi:10.1016/j.mito.2018.06.001 · Cited by 12
Ricci, V., Martinotti, G., Mosca, A., & Maina, G. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1740079 · Cited by 11
Mancini, G., Martins, W. C., de Oliveira, J., Bem, A. F. D., & Tasca, C. I. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02026-w · Cited by 12
Rigotto, G., Zentilin, L., Pozzan, T., & Basso, E. (2021) · Cells · doi:10.3390/cells10082046 · Cited by 12
Vidyadharan, V. A., Betancourt, A., Smith, C., Yallampalli, C., & Blesson, C. S. (2022) · Nutrients · doi:10.3390/nu14061158 · Cited by 10
Uittenbogaard, M. N., Gropman, A. L., Brantner, C. A., & Chiaramello, A. (2018) · Clinical Case Reports · doi:10.1002/ccr3.1868 · Cited by 11
Salazar, C., Barros, M., Elorza, Á. A., & Ruíz, L. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010389 · Cited by 9
Lee, S. Y., Kang, M.-G., Lee, S., Yoon, S. S., Cho, Y., Min, D., Ann, D., Shin, J., Paik, Y., & Jo, D. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107326 · Cited by 9
Beck, B. H., & Fuller, S. A. (2012) · Journal of Aquatic Animal Health · doi:10.1080/08997659.2012.720637 · Cited by 8
Ferrari, F., Gorini, A., & Villa, R. F. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1482-0 · Cited by 8
Altered Bioenergetics of Blood Cell Sub-Populations in Acute Pancreatitis Patients
Morton, J. C., Armstrong, J. A., Sud, A., Tepikin, A. V., Sutton, R., & Criddle, D. N. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8122201 · Cited by 8
Schuh, R. A., Matthews, C. C., & Fishman, P. S. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21772 · Cited by 8
Musthafa, T., Nizami, S. K., Mishra, A., Hasan, G., & Gopurappilly, R. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70059 · Cited by 7
Michelini, L. G. B., Figueira, T. R., Siqueira‐Santos, E. S., & Castilho, R. F. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.01.030 · Cited by 7
Hatoková, Z., Evinová, A., & Račay, P. (2023) · Toxicology in Vitro · doi:10.1016/j.tiv.2023.105652 · Cited by 5
Mazur, H. M., Merlavsky, V. M., Manko, B. O., & Manko, V. V. (2019) · The Ukrainian Biochemical Journal · doi:10.15407/ubj91.06.005 · Cited by 5
Contrasting consequences of podocyte insulin-like growth factor 1 receptor inhibition
Hurcombe, J., Barrington, F., Marchetti, M., Betin, V. M. S., Bowen, E. E., Lay, A. C., Ni, L., Dayalan, L., Pope, R. J. P., Brinkkoetter, P. T., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109749 · Cited by 5
Lores‐Arnaiz, S., Karadayian, A. G., Gutnisky, A., & Arnaiz, G. R. D. L. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14232 · Cited by 5
Radhakrishnan, S., Norley, J., Wendt, S., LeRoy, N. J., Hall, H., Norcross, S., Doan, S., Snaider, J. M., MacVicar, B. A., Weake, V. M., et al. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00342 · Cited by 5
Xia, M., Wang, T., Wang, Y., Hu, T., Chen, D., & Wang, B. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1436059 · Cited by 4
Impact of MnTBAP and Baricitinib Treatment on Hutchinson–Gilford Progeria Fibroblasts
Vehns, E., Arnold, R., & Djabali, K. (2022) · Pharmaceuticals · doi:10.3390/ph15080945 · Cited by 5
Jekabsons, M. B. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10020702 · Cited by 4
Mitochondria, Sodium, and Calcium in Neuronal Dysfunction
Nicholls, D. G. (2011) · Springer eBooks · doi:10.1007/978-0-85729-701-3_7 · Cited by 4
Self-citationEnergetic costs of cellular and therapeutic control of stochastic mtDNA populationsPreprint
Hoitzing, H., Gammage, P. A., Minczuk, M. A., Johnston, I. G., & Jones, N. S. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/145292 · Cited by 4
O2-Sensitive Probes Based on Phosphorescent Metalloporphyrins
Dmitriev, R. I., & Papkovsky, D. B. (2012) · SpringerBriefs in biochemistry and molecular biology · doi:10.1007/978-3-0348-0525-4_1 · Cited by 3
Moro, L., Rech, G., Linazzi, A. M., dos Santos, T. G., & de Oliveira, D. L. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147498 · Cited by 3
Immune Cell Metabolic Fitness for Life
Bittman, K. S. (2022) · Antibodies · doi:10.3390/antib11020032 · Cited by 2
Respiratory Syncytial Virus Infections Induce Hypermetabolism in Pediatric Upper AirwaysPreprint
Rezinciuc, S., Bezavada, L., Bahadoran, A., Ingels, J. F., Kim, Y.-Y., Cormier, S. A., DeVincenzo, J. P., Shulkin, B. L., & Smallwood, H. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.18.200964 · Cited by 2
Lv, J., Yao, X., Liu, S., Li, Y., Hu, W., & Li, X. (2025) · Biomaterials Advances · doi:10.1016/j.bioadv.2025.214569 · Cited by 1
de Moura, M. B., Hahm, E., Houten, B. V., & Singh, S. V. (2013) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4614-9227-6_8 · Cited by 1
Akbari, H., Ayati, M. H., Vaghasloo, M. A., & Karimi, M. (2022) · Journal of Family Medicine and Primary Care · doi:10.4103/jfmpc.jfmpc_1890_21 · Cited by 1
Mitochondrial Dysfunction and Protein Aggregation in the Cybrid Cell Model of Parkinson's Disease
Cronin-Furman, E. N. (2013) · doi:10.18130/v3dz3t · Cited by 1
Manifestations of Drug Toxicity on Mitochondria in the Nervous System
Reynolds, I. J. (2008) · Wiley eBooks · doi:10.1002/9780470372531.ch8
Mechanisms of Ischemic Induced Neuronal Death and Ischemic Tolerance
Lehotský, J., Pavlikova, M., Straka, S., Kovalská, M., Kaplán, P., & Tatarkov�, Z. (2012) · InTech eBooks · doi:10.5772/32112
Brandhorst, S. (2013) · DuEPublico (University of Duisburg-Essen)
Common mtDNA Polymorphisms and Neurodegenerative Disorders
Elson, J. L., & Samuels, D. C. (2011) · Springer eBooks · doi:10.1007/978-0-85729-701-3_4
Rojas-Martinez, J. C. (2009) · Texas ScholarWorks (Texas Digital Library)
Expression of AIF and CGRP markers in epiphysis and thymus during aging
Linkova, N. S., Katanugina, A. S., & Khavinson, V. K. (2012) · Advances in Gerontology · doi:10.1134/s2079057012030083
Analysis of copy number variation and disease mechanisms underlying Parkinson’s disease
van der Merwe, C. (2016) · SUNScholar (Stellenbosch University)
Manifestations of Drug Toxicity on Mitochondria in the Nervous System
Prehn, J. H. M., & Llorente‐Folch, I. (2018) · Wiley eBooks · doi:10.1002/9781119329725.ch9
Kaur, A. (2018) · Springer theses · doi:10.1007/978-3-319-73405-7_6
Comparative Analysis of the Mitochondrial Physiology of Pancreatic b
Patel, P., Gouvin, L. M., Brown, M., Khalil, A., Henchey, E., & Heuck, A. P. (2014)
., A. A., Goel, M., ., B. C., & ., R. P. (2019) · Indian Journal of Child Health · doi:10.32677/ijch.2019.v06.i08.004
Cytoprotection by a naturally occurring variant of ATP5G1 in Arctic ground squirrelsPreprint
Singhal, N. S., Bai, M., Lee, E. M., Luo, S., Cook, K. R., & Dengke, K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.31.929018
Molecular mechanisms regulating CD8+ T cell differentiation following external cues
Cullen, J. G. (2018) · Minerva Access (University of Melbourne)
Li, X., Ingram, T. L., Wang, Y., Derecka, K., Courtier, N., Piana, M., Hardy, I. C. W., Chakrabarti, L., & Stöger, R. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.14.296053
Cerebrovascular Dysfunction and Degeneration in Alzheimer’s Disease Pathophysiology
Quintana, D. D. (2020) · The Research Repository @ WVU (West Virginia University) · doi:10.33915/etd.7941
The Environmental Contribution to Redox Dyshomeostasis in Parkinson’s Disease
Garza-Lombó, C., & Franco, R. (2022) · Molecular and integrative toxicology · doi:10.1007/978-3-030-87451-3_4
Reduced insulin signalling in neurons induces sex-specific health benefitsPreprint
Baghdadi, M., Nespital, T., Mesaros, A., Buschbaum, S., Withers, D. J., Grönke, S., & Partridge, L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.19.508502
Rosa, R. S., Mendonça, A. P. M., Oliveira, M., de Carvalho, D. B., Vázquez, L., & de Oliveira, M. F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.25.690158
Rosa, R. S., Mendonça, A. P. M., Oliveira, M. P., de Carvalho, D. B., Vázquez, L., & Oliveira, M. F. (2026) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2026.104948
Yasuhara, S., You, Z., & Tamura, D. A. A. T. (2026) · IntechOpen eBooks · doi:10.5772/intechopen.1015862 · Cited by 1
Rogers, G. W., & Will, Y. (2026) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2026.2697796
Arias-Carrión, Ó., Guerra‐Crespo, M., Soto-Rojas, L. O., Valle, Y., Ortega‐Robles, E., & Ortuño‐Sahagún, D. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1886917 · Cited by 2
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