The DOI matches its Crossref record; 106 of the 106 references it cites were found in a registry or an index.
A Unifying Mechanism for Mitochondrial Superoxide Production during Ischemia-Reperfusion Injury
Open accessAbstract
Ischemia-reperfusion (IR) injury occurs when blood supply to an organ is disrupted--ischemia--and then restored--reperfusion--leading to a burst of reactive oxygen species (ROS) from mitochondria. It has been tacitly assumed that ROS production during IR is a non-specific consequence of oxygen interacting with dysfunctional mitochondria upon reperfusion. Recently, this view has changed, suggesting that ROS production during IR occurs by a defined mechanism. Here we survey the metabolic factors underlying IR injury and propose a unifying mechanism for its causes that makes sense of the huge amount of disparate data in this area and provides testable hypotheses and new directions for therapies.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“This type of ROS generation occurs when succinate, the substrate for complex II, is present in high concentration and is responsible in vivo for the ROS generated after ischemia upon reperfusion (171, 172).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [172]
In the citing paper
“SUCNR1 ligation on MoDC or the U937 macrophage cell line induces cell migration, suggesting that succinate can act as a chemokine4.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [4]
In the citing paper
“Priming of DCs with succinate and antigen simultaneously, elevates antigen-specific T cell activation, increasing TNFα and IFN-γproduction from these cells4.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [4]
In the citing paper
“SUCNR1 is highly expressed in mouse kidney, liver, spleen, small intestine3, and on dendritic cells (DCs) 4 and ligand binding induces Gi and Gq signalling cascades3.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [4]
In the citing paper
“Extracellular succinate addition also acts in synergy with TLR ligands to increase TNFα and IL-1β expression4 and increases the capacity of DCs to act as antigen presenting cells.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [4]
In the citing paper
“one likely role is as an inflammatory signal, acting via SUCNR14,5,161,162.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [4]
In the citing paper
“Numerous metabolic pathways have been implicated in the metabolic reprogramming of immune cells, in particular those that regulate succinate levels, which, in turn, can influence HIF signaling or other pathways (13,25,40,41).”
From Immunoresponsive Gene 1 and Itaconate Inhibit Succinate Dehydrogenase to Modulate Intracellular Succinate Levels (2016) · cites this paper as [40]
In the citing paper
“Notably, SDH inhibition protected against brain injury after ischemia/reperfusion (40,41), suggesting that inhibition of SDH by endogenously produced itaconate may buffer against potential oxidative damage that can occur under such conditions.”
From Immunoresponsive Gene 1 and Itaconate Inhibit Succinate Dehydrogenase to Modulate Intracellular Succinate Levels (2016) · cites this paper as [40]
Citations
Cites
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207
Self-citationSuccinate is an inflammatory signal that induces IL-1β through HIF-1α
Tannahill, G. M., Curtis, A. M., Adamik, J., Palsson-McDermott, E. M., McGettrick, A. F., Goel, G., Frezza, C., Bernard, N. J., Kelly, B., Foley, N. H., et al. (2013) · Nature · doi:10.1038/nature11986 · Cited by 4,176 · cited 2×
“…probably in conjunction with elevated ROS (Guzy et al., 2008), can stabilize the hypoxia-inducible factors (HIFs) by inhibiting their HIF-α prolyl hydroxylases-mediated degradation, thus leading to activation of a pseudohypoxic response (Selak et al., 2005; Tannahill et al., 2013) (Figure 2).”
BackgroundSelf-citationYellon, D. M., & Hausenloy, D. J. (2007) · New England Journal of Medicine · doi:10.1056/nejmra071667 · Cited by 3,797
Ischemia and reperfusion—from mechanism to translation
Eltzschig, H. K., & Eckle, T. D. L. G. (2011) · Nature Medicine · doi:10.1038/nm.2507 · Cited by 3,468
Sterile inflammation: sensing and reacting to damage
Chen, G. Y., & Nuñez, G. (2010) · Nature Reviews Immunology · doi:10.1038/nri2873 · Cited by 3,051
Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
Chouchani, E. T., Pell, V. R., Gaude, E., Aksentijević, D., Sundier, S. Y., Robb, E. L., Logan, A., Nadtochiy, S. M., Ord, E. N. J., Smith, A. C., et al. (2014) · Nature · doi:10.1038/nature13909 · Cited by 2,907
Self-citationMyocardial ischemia-reperfusion injury: a neglected therapeutic target
Hausenloy, D. J., & Yellon, D. M. (2013) · Journal of Clinical Investigation · doi:10.1172/jci62874 · Cited by 2,357
White, H. D., Norris, R. M., Brown, M. A., Brandt, P. W., Whitlock, R. M. L., & Wild, C. J. (1987) · Circulation · doi:10.1161/01.cir.76.1.44 · Cited by 2,348
Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase
Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108
Reimer, K. A., Lowe, J. E., Rasmussen, M. M., & Jennings, R. B. (1977) · Circulation · doi:10.1161/01.cir.56.5.786 · Cited by 1,944
Cited by
Sorted by citations
Items 201–300 of 751
Activation of Autophagic Flux Blunts Cardiac Ischemia/Reperfusion Injury
Xie, M., Cho, G. W., Kong, Y., Li, D. ‘., Altamirano, F. J., Luo, X., Morales, C. R., Jiang, N., Schiattarella, G. G., May, H. I., et al. (2021) · Circulation Research · doi:10.1161/circresaha.120.318601 · Cited by 46
Huang, Z., Qian, K., Chen, J., Qi, Y., Yifeng, E., Liang, J., & Zhao, L. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.03.018 · Cited by 46
Wang, Y., Xu, Y., Guo, W., Fang, Y., Hu, L., Wang, R., Zhao, R., Guo, D. S., Qi, B., Ren, G., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102537 · Cited by 45
Glutamine metabolism drives succinate accumulation in plasma and the lung during hemorrhagic shock
Slaughter, A. L., D’Alessandro, A., Moore, E. E., Banerjee, A. M., Silliman, C. C., Hansen, K. C., Reisz, J. A., Fragoso, M., Wither, M. J., Bacon, A. W., et al. (2016) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0000000000001256 · Cited by 45
Enhancing Glycolysis Protects against Ischemia-Reperfusion Injury by Reducing ROS Production
Beltran, C., Pardo, R., Bou‐Teen, D., Ruiz‐Meana, M., Villena, J. A., González, I. F., & Barba, I. (2020) · Metabolites · doi:10.3390/metabo10040132 · Cited by 46
Gao, N., Tang, H. C., Gao, L., Tu, G., Luo, H., & Xia, Y. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.04.020 · Cited by 45
The Role of Mitochondria in Immune-Cell-Mediated Tissue Regeneration and Ageing
Su, Y., Wang, P., & Weng, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052668 · Cited by 45
Targeting oxidative stress, a crucial challenge in renal transplantation outcome
Carcy, R., Cougnon, M., Poët, M., Durandy, M., Sicard, A., Counillon, L., Blondeau, N., Hauet, T., Tauc, M., & Pisani, D. F. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.04.023 · Cited by 50
Cryo-EM structures of mitochondrial respiratory complex I from Drosophila melanogaster
Agip, A.-N. A., Chung, I., Sánchez-Martínez, Á., Whitworth, A. J., & Hirst, J. (2023) · eLife · doi:10.7554/elife.84424 · Cited by 45
Fang, W. Y., Wang, G., Tang, L., Su, H., Chen, H., Liao, W., & Xu, J. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13704 · Cited by 44
Can All Major ROS Forming Sites of the Respiratory Chain Be Activated By High FADH 2 /NADH Ratios?
Speijer, D. (2018) · BioEssays · doi:10.1002/bies.201800180 · Cited by 44
Red Blood Cell Metabolic Responses to Torpor and Arousal in the Hibernator Arctic Ground Squirrel
Gehrke, S. A., Rice, S. A., Stefanoni, D., Wilkerson, R. B., Nemkov, T. G., Reisz, J. A., Hansen, K. C., Lucas, A., Cabrales, P., Drew, K. L., et al. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00018 · Cited by 44
Wong, H. S., Monternier, P., & Brand, M. D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.09.006 · Cited by 46
Hypo- and normothermic perfusion of the liver: Which way to go?
Selten, J. W., Schlegel, A. A., de Jonge, J., & Dutkowski, P. (2017) · Best Practice & Research Clinical Gastroenterology · doi:10.1016/j.bpg.2017.04.001 · Cited by 43
Schlegel, A. A., Muller, X., & Dutkowski, P. (2017) · Current Opinion in Organ Transplantation · doi:10.1097/mot.0000000000000472 · Cited by 43
Lu, Y., Kan, H., Wang, Y., Wang, D., Wang, X., Gao, J., & Zhu, L. (2017) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2017.11.023 · Cited by 43
Trewin, A. J., Bahr, L. L., Almast, A., Berry, B. J., Wei, A. Y., Foster, T. H., & Wojtovich, A. P. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7681 · Cited by 43
A reversible mitochondrial complex I thiol switch mediates hypoxic avoidance behavior in C. elegans
Onukwufor, J. O., Farooqi, M. A., Vodičková, A., Koren, S. A., Baldzizhar, A., Berry, B. J., Beutner, G., Porter, G. A., Jr., Belousov, V. V., Grossfield, A. M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30169-y · Cited by 43
Mitochondrial Function and Reactive Oxygen/Nitrogen Species in Skeletal Muscle
Chen, M., Li, Y., Deng, S., Zhao, Y., Lian, Z., & Yu, K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.826981 · Cited by 49
Mathers, K. E., & Staples, J. F. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00052.2019 · Cited by 42
Pharmacology of mitochondrial permeability transition pore inhibitors
Naryzhnaya, N. V., Маслов, Л. Н., & Oeltgen, P. R. (2019) · Drug Development Research · doi:10.1002/ddr.21593 · Cited by 42
Milliken, A. S., Nadtochiy, S. M., & Brookes, P. S. (2022) · Journal of the American Heart Association · doi:10.1161/jaha.122.026135 · Cited by 41
Sander, L. E., & Garaude, J. (2017) · Mitochondrion · doi:10.1016/j.mito.2017.10.008 · Cited by 41
Dubouchaud, H., Walter, L., Rigoulet, M., & Batandier, C. (2018) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-018-9767-7 · Cited by 41
Effects of inhibiting antioxidant pathways on cellular hydrogen sulfide and polysulfide metabolism
Olson, K. R., & Gao, Y. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.02.011 · Cited by 41
Quintana, D. D., Garcia, J. A., Anantula, Y., Rellick, S. L., Engler-Chiurazzi, E. B., Sarkar, S. N., Brown, C. M., & Simpkins, J. W. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-190964 · Cited by 41
Boulghobra, D., Coste, F., Gény, B., & Reboul, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.04.005 · Cited by 42
Hatinguais, R., Pradhan, A., Brown, G. D., Brown, A. J. P., Warris, A., & Shekhova, E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.641495 · Cited by 41
Nanomedicine‐Based Therapeutics for Myocardial Ischemic/Reperfusion Injury
Li, X., Ou, W., Xie, M., Yang, J., Li, Q., & Li, T. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202300161 · Cited by 40
Acute Myocardial Infarction: Molecular Pathogenesis, Diagnosis, and Clinical Management
Zhu, M., Li, Y., Xu, Q., Wang, W., Liu, Y., & Liu, Y. (2025) · MedComm · doi:10.1002/mco2.70418 · Cited by 49
Chemical Conditioning as an Approach to Ischemic Stroke Tolerance: Mitochondria as the Target
Jin, Z., Wu, J., & Yan, L. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030351 · Cited by 40
SMYD2 glutathionylation contributes to degradation of sarcomeric proteins
Godage, D. N. P. M., VanHecke, G. C., Samarasinghe, K. T. G., Feng, H., Hiske, M. A., Holcomb, J., Yang, Z., Jin, J., Chung, C. S., & Ahn, Y. (2018) · Nature Communications · doi:10.1038/s41467-018-06786-x · Cited by 40
Pizzimenti, M., Riou, M., Charles, A., Talha, S., Meyer, A., Andrès, E., Chakfé, N., Lejay, A., & Gény, B. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8122125 · Cited by 40
Zhang, R., Liu, B., Fan, X., Wang, W., Xu, T., Wei, S., Zheng, W., Yuan, Q., Gao, L., Yin, X., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00373 · Cited by 40
Targeting Inflammation and Oxidative Stress as a Therapy for Ischemic Kidney Injury
Andrianova, N. V., Zorov, D. B., & Plotnikov, E. Y. (2020) · Biochemistry (Moscow) · doi:10.1134/s0006297920120111 · Cited by 40
Buchko, M. T., Stewart, C. J., Hatami, S., Himmat, S., Freed, D. H., & Nagendran, J. (2019) · American Journal of Transplantation · doi:10.1111/ajt.15572 · Cited by 39
Macrophage activation as an archetype of mitochondrial repurposing
Jones, A. E., & Divakaruni, A. S. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2019.100838 · Cited by 41
Miljković, J. L., Burger, N., Gawel, J. M., Mulvey, J. F., Norman, A. A. I., Nishimura, T., Tsujihata, Y., Logan, A., Sauchanka, O., Caldwell, S. T., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102429 · Cited by 39
Self-citationArndt, S., Baeza-Garza, C. D., Logan, A., Rosa, T., Wedmann, R., Prime, T. A., Martin, J. L., Saeb‐Parsy, K., Krieg, T., Filipović, M. R., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.784678 · Cited by 38
Self-citationEvolution of peroxisomes illustrates symbiogenesis
Speijer, D. (2017) · BioEssays · doi:10.1002/bies.201700050 · Cited by 38
Reactive Oxygen Species Related Noncoding RNAs as Regulators of Cardiovascular Diseases
Dong, Y., Xu, W., Liu, C., Liu, P., Li, P., & Wang, K. (2019) · International Journal of Biological Sciences · doi:10.7150/ijbs.30464 · Cited by 38
Cellular crosstalk in cardioprotection: Where and when do reactive oxygen species play a role?
Martins‐Marques, T., Rodríguez‐Sinovas, A., & Girão, H. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.044 · Cited by 38
A Case for Hydrogen Sulfide Metabolism as an Oxygen Sensing Mechanism
Olson, K. R. (2021) · Antioxidants · doi:10.3390/antiox10111650 · Cited by 39
ND3 Cys39 in complex I is exposed during mitochondrial respiration
Burger, N., James, A. M., Mulvey, J. F., Hoogewijs, K., Ding, S., Fearnley, I. M., Loureiro, M., Norman, A. A. I., Arndt, S., Mottahedin, A., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.10.010 · Cited by 38
Self-citationAdzigbli, L., Sokolov, E. P., Wimmers, K., Sokolova, I. M., & Ponsuksili, S. (2022) · Scientific Reports · doi:10.1038/s41598-022-24386-0 · Cited by 41
Abe, J., Vujić, A., Prag, H. A., Murphy, M. P., & Krieg, T. (2024) · Basic Research in Cardiology · doi:10.1007/s00395-024-01063-z · Cited by 37
Self-citationJúnior, A. L. G., Tchekalarova, J. D., Atanasova, M., Machado, K. D. C., Rios, M. A. D. S., Paz, M. F. C. J., Găman, M., Găman, A. M., Yele, S., Shill, M. C., et al. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.121 · Cited by 37
Liu, W., Fan, Y., Ding, H., Han, D., Yang, Y., Wu, R., Lv, Y., & Zheng, X. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17062 · Cited by 38
Adzigbli, L., Sokolov, E. P., Ponsuksili, S., & Sokolova, I. M. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.243304 · Cited by 37
Plant-specific features of respiratory supercomplex I + III2 from Vigna radiata
Maldonado, M., Fan, Z., Abe, K. M., & Letts, J. A. (2022) · Nature Plants · doi:10.1038/s41477-022-01306-8 · Cited by 37
Arni, S., Maeyashiki, T., Çıtak, N., Opitz, I., & İnci, İ. (2021) · Cells · doi:10.3390/cells10040748 · Cited by 36
Zhao, Y.-P., Wang, F., Jiang, W., Liu, J., Liu, B., Qi, L., & Zhou, W. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1566338 · Cited by 36
DJ-1: A promising therapeutic candidate for ischemia-reperfusion injury
Lazzari, F. D., Prag, H. A., Gruszczyk, A. V., Whitworth, A. J., & Bisaglia, M. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101884 · Cited by 36
New insights into survival strategies to oxygen deprivation in anoxia‐tolerant vertebrates
Fago, A. (2022) · Acta Physiologica · doi:10.1111/apha.13841 · Cited by 38
Manhas, N., Duong, Q. V., Lee, P., Richardson, J. D., Robertson, J. D., Moxley, M. A., & Bazil, J. N. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014483 · Cited by 36
Protective effects of curcumin on ischemia/reperfusion injury
Mohamadian, M., Parsamanesh, N., Chiti, H., Sathyapalan, T., & Sahebkar, A. (2022) · Phytotherapy Research · doi:10.1002/ptr.7620 · Cited by 35
Bibli, S., Zhou, Z., Zukunft, S., Fißlthaler, B., Andreadou, I., Szabó, C., Brouckaert, P., Fleming, I., & Papapetropoulos, A. (2017) · Cardiovascular Research · doi:10.1093/cvr/cvx058 · Cited by 36
van Golen, R. F., Reiniers, M. J., Marsman, G., Alles, L. K., Rooyen, D. M. V., Petri, B., van der Mark, V. A., van Beek, A. A., Meijer, B., Maas, M. A. W., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.01.014 · Cited by 34
Self-citationSnapshot: Implications for mTOR in Aging-related Ischemia/Reperfusion Injury
Liu, D., Xu, L., Zhang, X., Shi, C., Qiao, S., Ma, Z., & Yuan, J. (2018) · Aging and Disease · doi:10.14336/ad.2018.0501 · Cited by 34
Tomar, N., Zhang, X., Kandel, S. M., Sadri, S., Yang, C., Liang, M., Audi, S. H., Cowley, A. W., & Dash, R. K. (2021) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2021.148518 · Cited by 34
A “Weird” Mitochondrial Fatty Acid Oxidation as a Metabolic “Secret” of Cancer
Zhelev, Z., Aoki, I., Lazarova, D., Vlaykova, T. I., Higashi, T., & Bakalova, R. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2339584 · Cited by 34
Cobley, J. N., & Husi, H. (2020) · Antioxidants · doi:10.3390/antiox9040315 · Cited by 33
Sorby‐Adams, A., Prime, T. A., Miljković, J. L., Prag, H. A., Krieg, T., & Murphy, M. P. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103161 · Cited by 32
Self-citationDuni, Α., Liakopoulos, V., Koutlas, V., Pappas, C., Mitsis, M., & Dounousi, E. C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042157 · Cited by 32
Turco, S. D., Cappello, V., Tapeinos, C., Moscardini, A., Sabatino, L., Battaglini, M., Melandro, F., Torri, F., Martinelli, C., Babboni, S., et al. (2022) · Liver Transplantation · doi:10.1002/lt.26421 · Cited by 32
Kôrge, P., Calmettes, G., John, S., & Weiss, J. N. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768317 · Cited by 32
Viblanc, V. A., Schull, Q., Roth, J. D., Rabdeau, J., Saraux, C., Uhlrich, P., Criscuolo, F., & Dobson, F. S. (2017) · Functional Ecology · doi:10.1111/1365-2435.13032 · Cited by 32
Darius, T., Vergauwen, M., Smith, T. B., Patel, K., Craps, J., Joris, V., Aydın, S., Ury, B., Buémi, A., Meyer, M. D., et al. (2019) · Transplantation · doi:10.1097/tp.0000000000003051 · Cited by 32
Mesenchymal stem cell therapy targeting mitochondrial dysfunction in acute kidney injury
Zhao, L., Hu, C., Zhang, P., Jiang, H., & Chen, J. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1893-4 · Cited by 31
Schumann, A., Schaller, K., Belche, V., Cybulla, M., Grünert, S. C., Moers, N., Sass, J. O., Kaech, A., Hannibal, L., & Spiekerkoetter, U. (2021) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12373 · Cited by 31
Todisco, S., Musio, B., Pesce, V., Cavalluzzi, M. M., Petrosillo, G., Piana, G. L., Sgobba, M. N., Schlosserová, N., Beltrame, L. C., Lorenzo, R. D., et al. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115405 · Cited by 31
Geng, J., Aa, J., Feng, S., Wang, S., Wang, P., Zhang, Y., Ouyang, B., Wang, J.-K., Zhu, Y., Huang, W., et al. (2017) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2017.04.031 · Cited by 31
Key hepatoprotective roles of mitochondria in liver regeneration
Lamanilao, G. G., Doğan, M., Patel, P. S., Azim, S., Patel, D. S., Bhattacharya, S. K., Eason, J. D., Kuscu, C., Kuscu, C., & Bajwa, A. (2023) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00220.2022 · Cited by 30
Li, Y., & Liu, S. (2017) · Medical Science Monitor · doi:10.12659/msm.899855 · Cited by 30
Notch1–Nrf2 signaling crosstalk provides myocardial protection by reducing ROS formation
Zhou, X., Wu, X., Zhu, R.-R., Xu, H., Li, Y.-Y., Xu, Q., Liu, S., Lai, S., Xu, X., Wan, L., et al. (2020) · Biochemistry and Cell Biology · doi:10.1139/bcb-2018-0398 · Cited by 30
A synthetic cell permeable antioxidant protects neurons against acute oxidative stress
Drummond, N. J., Davies, N. O., Lovett, J. E., Miller, M. R., Cook, G., Becker, T., Becker, C. G., McPhail, D. B., & Kunath, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-12072-5 · Cited by 30
Acevedo, A., Jones, A. E., Danna, B. T., Turner, R., Montales, K. P., Benincá, C., Reue, K., Shirihai, O. S., Stiles, L., Wallace, M., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105702 · Cited by 32
Molecular mechanism of the ischemia-induced regulatory switch in mammalian complex I
Grba, D. N., Wright, J. J., Yin, Z., Fisher, W., & Hirst, J. (2024) · Science · doi:10.1126/science.ado2075 · Cited by 29
Gerber, L., Clow, K. A., Katan, T., Emam, M., Leeuwis, R. H. J., Parrish, C. C., & Gamperl, A. K. (2019) · Journal of Experimental Biology · doi:10.1242/jeb.208074 · Cited by 29
Dexpramipexole attenuates myocardial ischemia/reperfusion injury through upregulation of mitophagy
Tang, L., Li, Y., Hu, J., Chen, A., & Mo, Y. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173962 · Cited by 29
Control of Tissue Fibrosis by 5-Methoxytryptophan, an Innate Anti-Inflammatory Metabolite
Wu, K. K. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.759199 · Cited by 29
Mitochondrial Metabolism in Hibernation: Regulation and Implications
Staples, J. F., Mathers, K. E., & Duffy, B. M. (2022) · Physiology · doi:10.1152/physiol.00006.2022 · Cited by 29
Gibbs, E. T., Lerner, C. A., Watson, M. A., Wong, H. S., Gerencser, A. A., & Brand, M. D. (2023) · Biochemical Journal · doi:10.1042/bcj20220611 · Cited by 29
Ding, S., Kim, Y., Huang, K., Um, D. J., Jung, Y., & Kong, H. (2024) · Nano Convergence · doi:10.1186/s40580-024-00423-8 · Cited by 30
Dingfelder, J., Kollmann, D., Rauter, L., Pereyra, D., Kacar, S., Weijler, A. M., Saffarian, T., Tortopis, C., Silberhumer, G. R., Salat, A., et al. (2024) · Liver Transplantation · doi:10.1097/lvt.0000000000000512 · Cited by 28
Improved approach for normothermic machine perfusion of cold stored kidney grafts.
von Horn, C., & Minor, T. (2018) · Europe PMC (PubMed Central) · Cited by 28
Xu, J., Bian, X., Zhao, H., Sun, Y., Tian, Y., Li, X., & Tian, W. (2021) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-021-07215-w · Cited by 28
Binding of Natural Inhibitors to Respiratory Complex I
Schiller, J., & Zickermann, V. (2022) · Pharmaceuticals · doi:10.3390/ph15091088 · Cited by 29
Zhang, F., Li, Z., Gao, P., Zou, J., Cui, Y., Qian, Y., Gu, R., Xu, W., & Hu, J. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1024292 · Cited by 29
Schull, Q., Viblanc, V. A., Stier, A., Saadaoui, H., Lefol, E., Criscuolo, F., Bize, P., & Robin, J. (2016) · Journal of Experimental Biology · doi:10.1242/jeb.145250 · Cited by 31
Wu, J., Li, R., Li, W., Ren, M., Thangthaeng, N., Sumien, N., Liu, R., Yang, S., Simpkins, J. W., Forster, M. J., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.10.008 · Cited by 28
Mitochondrial oxidative stress, calcium and dynamics in cardiac ischaemia‐reperfusion injury
Rozich, E., Ozkurede, U., Pakkiriswami, S., Gemilere, R., Azarin, S. M., & Liu, J. C. (2025) · The Journal of Physiology · doi:10.1113/jp287770 · Cited by 29
Wang, F., Peng, Q., Liu, J., Alolga, R. N., & Zhou, W. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172417 · Cited by 27
XRCC2 repairs mitochondrial DNA damage and fuels malignant behavior in hepatocellular carcinoma
Zhao, Z., He, K., Zhang, Y., Hua, X., Feng, M., Zhao, Z., Sun, Y., Jiang, Y., & Xia, Q. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.04.026 · Cited by 27
Ruhr, I. M., Bierstedt, J., Rhen, T., Das, D., Singh, S. K., Miller, S., Crossley, D. A., & Galli, G. L. J. (2021) · Epigenetics & Chromatin · doi:10.1186/s13072-021-00414-7 · Cited by 27
Abbas, S. H., Ceresa, C. D. L., & Pollok, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25094648 · Cited by 27
Mitochondrial dynamics and quality control regulate proteostasis in neuronal ischemia-reperfusion
Fogo, G. M., Raghunayakula, S., Emaus, K. J., Torres, F. J. T., Shangguan, G., Wider, J. M., Hüttemann, M., & Sanderson, T. H. (2025) · Autophagy · doi:10.1080/15548627.2025.2472586 · Cited by 26
Shitaw, E. E., AlAhmad, M., & Sivaprasadarao, A. (2025) · Antioxidants · doi:10.3390/antiox14070776 · Cited by 26
Protective effects of dexmedetomidine on the survival of random flaps
Fang, M., He, J., Ma, X., Li, W., & Lin, D. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110261 · Cited by 26
Zhou, Z., Ren, X., Zheng, L., Li, A., & Zhou, W. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-021-00895-1 · Cited by 26
Metadata
- Authors
- Chouchani, E. T., Pell, V. R., James, A. M., Work, L. M., Saeb-Parsy, K., Frezza, C., Krieg, T., & Murphy, M. P.
- Affiliations
- Harvard University (US)
- University of Cambridge (GB)
- MRC Mitochondrial Biology Unit (GB)
- University of Glasgow (GB)
- Corresponding author
- Murphy, Michael P.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2016-02
- Volume
- 23
- Issue
- 2
- Pages
- 254-263
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2239083587
- Semantic Scholar
- 05aae81910c5536362646624d7e2848d0da4e591
- Cited by
- 752
- References
- 106
- Citations by year
- 2026: 62 · 2025: 78 · 2024: 63 · 2023: 79 · 2022: 90 · 2021: 104 · 2020: 83 · 2019: 64 · 2018: 58 · 2017: 50 · 2016: 19
- FWCI
- 10.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion)
- Apollo (University of Cambridge) (submittedVersion, cc-by-nc-nd)
- Funders
- British Heart Foundation
- Medical Research Council (MC_UU_12022/6)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- ischemia-reperfusion injury, mitochondrial superoxide production, reactive oxygen species, mitochondrial dysfunction, reperfusion, oxidative stress, metabolic factors, tissue damage
- MeSH terms
- Animals, Electron Transport, Humans, Mitochondria, Models, Biological, Sulfhydryl Compounds, Superoxides, Reperfusion Injury
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