What physiological role(s) does the alternative oxidase perform in animals?
Open accessAbstract
Although the alternative oxidase, AOX, was known to be widespread in the animal kingdom by 2004, its exact physiological role in animals remains poorly understood. Here we present what evidence has accumulated thus far, indicating that it may play a role in enabling animals to resist various kinds of stress, including toxins, abnormal oxygen or nutrient levels, protein unfolding, dessication and pathogen attack. Much of our knowledge comes from studies in model organisms, where any benefits from exogenously expressed AOX may be masked by its unregulated expression, which may itself be stressful. The further question arises as to why AOX has been lost from some major crown groups, namely vertebrates, insects and cephalopods, if it plays important roles favouring the survival of other animals. We conclude by presenting some speculative ideas addressing this question, and an outline of how it might be approached experimentally.
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A crucial role in mitigating oxidative stress, as well as other cellular stress conditions, was postulated for AOX in Metazoa.
“A crucial role in mitigating oxidative stress, as well as other cellular stress conditions, was also postulated for AOX in Metazoa (Jacobs and Ballard 2022).”
From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Jacobs and Ballard 2022
AOX is likely an ancient eukaryotic protein with origins that could be traced to the mitochondrial ancestor, but it was lost in several clades, including insects and vertebrates.
“It is likely to be an ancient eukaryotic protein with origins that could be traced to the mitochondrial ancestor, but it was lost in several clades, including insects and vertebrates (Jacobs and Ballard 2022).”
From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Jacobs and Ballard 2022
Cites
Escherichia coli and Salmonella :cellular and molecular biology
Neidhardt, F. C. (1996) · ASM Press eBooks · Cited by 8,197 · see citing works
Mills, E. L., Kelly, B., Logan, A., Costa, A. S. H., Varma, M., Bryant, C. E., Tourlomousis, P., Däbritz, J. H. M., Gottlieb, E., Latorre, I., et al. (2016) · Cell · doi:10.1016/j.cell.2016.08.064 · Cited by 2,291 · see citing works
Self-citationOxidative stress: animal adaptations in nature.
Storey, K. B. (1996) · PubMed · Cited by 699 · see citing works
Vetter, J. (2000) · Toxicon · doi:10.1016/s0041-0101(99)00128-2 · Cited by 665 · see citing works
Scialò, F., Fernández-Ayala, D. J., & Sanz, A. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00428 · Cited by 517 · see citing works
Abele, D., Heise, K., Pörtner, H. O., & Puntarulo, S. (2002) · Journal of Experimental Biology · doi:10.1242/jeb.205.13.1831 · Cited by 487 · see citing works
Mitochondria are physiologically maintained at close to 50 °C
Chrétien, D., Bénit, P., Ha, H., Keipert, S., El‐Khoury, R., Chang, Y., Jastroch, M., Jacobs, H. T., Rustin, P., & Rak, M. (2018) · PLoS Biology · doi:10.1371/journal.pbio.2003992 · Cited by 451 · see citing works
Self-citationThe efficiency and plasticity of mitochondrial energy transduction.
Brand, M. D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330897 · Cited by 406 · see citing works
Jørgensen, B. B. (1982) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1982.0096 · Cited by 357 · see citing works
Salicylic Acid Is an Uncoupler and Inhibitor of Mitochondrial Electron Transport
Norman, C., Howell, K. A., Millar, A. H., Whelan, J., & Day, D. A. (2004) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.031039 · Cited by 279 · see citing works
Cyanogenesis in plants and arthropods
Zagrobelny, M., Bak, S., & Møller, B. L. (2008) · Phytochemistry · doi:10.1016/j.phytochem.2008.02.019 · Cited by 265 · see citing works
Molecular chaperones and proteostasis regulation during redox imbalance
Niforou, K., Cheimonidou, C., & Trougakos, I. P. (2014) · Redox Biology · doi:10.1016/j.redox.2014.01.017 · Cited by 250 · see citing works
PKR Senses Nuclear and Mitochondrial Signals by Interacting with Endogenous Double-Stranded RNAs
Kim, Y., Park, J., Kim, S., Kim, M. A., Kang, M., Kwak, C. S., Kang, M., Kim, B., Rhee, H., & Kim, V. N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.029 · Cited by 242 · see citing works
Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP
Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works
Ecophysiology of Antarctic marine ectotherms: limits to life
Peck, L. S. (2002) · Polar Biology · doi:10.1007/s003000100308 · Cited by 200 · see citing works
Theißen, U. (2003) · Molecular Biology and Evolution · doi:10.1093/molbev/msg174 · Cited by 194 · see citing works
Fernández‐Ayala, D. J. M., Sanz, A., Vartiainen, S., Kemppainen, K. K., Babušiak, M., Mustalahti, E., Costa, R., Tuomela, T., Zeviani, M., Chung, J., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.004 · Cited by 181 · see citing works
Self-citationEnergy crisis: The role of oxidative phosphorylation in acute inflammation and sepsis
Lee, I., & Hüttemann, M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.031 · Cited by 170 · see citing works
Alternative oxidase and plant stress tolerance
Saha, B., Борисович, Б. Г., & Panda, S. K. (2016) · Plant Signaling & Behavior · doi:10.1080/15592324.2016.1256530 · Cited by 160 · see citing works
Marine invertebrate mitochondria and oxidative stress
Abele, D. (2006) · Frontiers in bioscience · doi:10.2741/2115 · Cited by 156 · see citing works
Alternative oxidase in animals: unique characteristics and taxonomic distribution
McDonald, A. E., Vanlerberghe, G. C., & Staples, J. F. (2009) · Journal of Experimental Biology · doi:10.1242/jeb.032151 · Cited by 143 · see citing works
Vanlerberghe, G. C., Martyn, G. D., & Dahal, K. (2016) · Physiologia Plantarum · doi:10.1111/ppl.12451 · Cited by 131 · see citing works
McDonald, A. E., & Vanlerberghe, G. C. (2004) · IUBMB Life · doi:10.1080/1521-6540400000876 · Cited by 118 · see citing works
El‐Khoury, R., Dufour, É., Rak, M., Ramanantsoa, N., Grandchamp, N., Csaba, Z., Duvillié, B., Bénit, P., Gallego, J., Gressèns, P., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003182 · Cited by 116 · see citing works
Self-citationOnukwufor, J. O., Berry, B. J., & Wojtovich, A. P. (2019) · Antioxidants · doi:10.3390/antiox8080285 · Cited by 112 · see citing works
Expression of the alternative oxidase complements cytochrome c oxidase deficiency in human cells
Dassa, E. P., Dufour, É., Gonçalves, S., Paupe, V., Hakkaart, G. A. J., Jacobs, H. T., & Rustin, P. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900001 · Cited by 107 · see citing works
Self-citationMitonuclear Epistasis for Development Time and Its Modification by Diet in Drosophila
Mossman, J. A., Biancani, L. M., Zhu, C.-T., & Rand, D. M. (2016) · Genetics · doi:10.1534/genetics.116.187286 · Cited by 101 · see citing works
Perturbed Redox Signaling Exacerbates a Mitochondrial Myopathy
Doğan, Ş. A., Cerutti, R., Benincá, C., Brea‐Calvo, G., Jacobs, H. T., Zeviani, M., Szibor, M., & Viscomi, C. F. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.07.012 · Cited by 98 · see citing works
Self-citationGilliland, A., Singh, D. P., Hayward, J. M., Moore, C. A., Murphy, A. M., York, C. J., Slator, J., & Carr, J. P. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.102.017640 · Cited by 98 · see citing works
Aw, W. C., Towarnicki, S. G., Melvin, R. G., Youngson, N. A., Garvin, M. R., Hu, Y., Nielsen, S., Thomas, T., Pickford, R., Bustamante, S., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007735 · Cited by 92 · see citing works
Self-citationAntimycin A18 produced by an endophytic Streptomyces albidoflavus isolated from a mangrove plant
Yan, L., Han, N., Zhang, Y., Yu, L., Chen, J., Wei, Y., Li, Q., Tao, L., Zheng, G.-H., Yang, S.-E., et al. (2010) · The Journal of Antibiotics · doi:10.1038/ja.2010.21 · Cited by 90 · see citing works
Metazoans in extreme environments: adaptations of hydrothermal vent and hydrocarbon seep fauna.
McMullin, E. R., Bergquist, D. C., & Fisher, C. R. (2000) · PubMed · Cited by 86 · see citing works
The thermodynamic efficiency of ATP synthesis in oxidative phosphorylation
Nath, S. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.10.002 · Cited by 82 · see citing works
Growth yield and energy distribution
Neijssel, O. M., de Mattos, M. J. T., & Tempest, D. W. (1996) · UvA-DARE (University of Amsterdam) · Cited by 79 · see citing works
Sp185/333: A novel family of genes and proteins involved in the purple sea urchin immune response
Ghosh, J., Buckley, K. M., Nair, S. V., Raftos, D. A., Miller, C., Majeske, A. J., Hibino, T., Rast, J. P., Roth, M. O., & Smith, L. C. (2009) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2009.10.008 · Cited by 79 · see citing works
Responses of invertebrates to temperature and water stress: A polar perspective
Everatt, M. J., Convey, P., Bale, J. S., WORLAND, M. R., & Hayward, S. A. L. (2014) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2014.05.004 · Cited by 72 · see citing works
Klingenspor, M., Fromme, T., Hughes, D. A., Manzke, L. H., Polymeropoulos, E. T., Riemann, T., Trzcionka, M., Hirschberg, V., & Jastroch, M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.006 · Cited by 71 · see citing works
Mitochondrial Sulfide Oxidation in Arenicola Marina
Völkel, S., & Grieshaber, M. K. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00231.x · Cited by 71 · see citing works
Broad AOX expression in a genetically tractable mouse model does not disturb normal physiology
Szibor, M., Dhandapani, P. K., Dufour, É., Holmström, K. M., Zhuang, Y., Salwig, I., Wittig, I., Heidler, J., Gizatullina, Z. Z., Gainutdinov, T. M., et al. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.027839 · Cited by 68 · see citing works
Self-citationSommer, N., Alebrahimdehkordi, N., Pak, O., Knoepp, F., Strielkov, I. V., Scheibe, S., Dufour, É., Andjelković, A., Sydykov, A. S., Saraji, A. A., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba0694 · Cited by 67 · see citing works
Self-citationSzibor, M., Gainutdinov, T. M., Fernández‐Vizarra, E., Dufour, É., Gizatullina, Z. Z., Dębska–Vielhaber, G., Heidler, J., Wittig, I., Viscomi, C. F., Gellerich, F. N., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2019.148137 · Cited by 65 · see citing works
Zhu, Y. J., Lu, J., Wang, J., Chen, F., Leng, F., & Li, H. (2010) · Journal of Integrative Plant Biology · doi:10.1111/j.1744-7909.2010.01004.x · Cited by 60 · see citing works
Context dependency and generality of fever in insects
Stahlschmidt, Z. R., & Adamo, S. A. (2013) · Die Naturwissenschaften · doi:10.1007/s00114-013-1057-y · Cited by 60 · see citing works
El‐Khoury, R., Kemppainen, K. K., Dufour, E., Szibor, M., Jacobs, H. T., & Rustin, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12570 · Cited by 56 · see citing works
Self-citationCyanogenesis in Arthropods: From Chemical Warfare to Nuptial Gifts
Zagrobelny, M., de Castro, É. C. P., Møller, B. L., & Bak, S. (2018) · Insects · doi:10.3390/insects9020051 · Cited by 55 · see citing works
Esposti, M. D., Mentel, M., Martin, W. F., & Sousa, F. L. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00499 · Cited by 49 · see citing works
Yusseppone, M. S., Rocchetta, I., Sabatini, S. E., Luquet, C. M., de Molina, M. D. C. R., Held, C., & Abele, D. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00100 · Cited by 47 · see citing works
Coenzyme Q redox signalling and longevity
Scialò, F., & Sanz, A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.018 · Cited by 46 · see citing works
Response of mitochondrial alternative oxidase (AOX) to light signals
Xu, F., Yuan, S., & Lin, H. (2011) · Plant Signaling & Behavior · doi:10.4161/psb.6.1.14192 · Cited by 44 · see citing works
El‐Khoury, R., Kaulio, E., Lassila, K., Crowther, D. C., Jacobs, H. T., & Rustin, P. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.006 · Cited by 42 · see citing works
Self-citationPace, D. A., & Manahan, D. T. (2007) · Biological Bulletin · doi:10.2307/25066589 · Cited by 42 · see citing works
Redox regulation of mitochondrial sulfide oxidation in the lugworm,Arenicola marina
Hildebrandt, T. M., & Grieshaber, M. K. (2008) · Journal of Experimental Biology · doi:10.1242/jeb.019729 · Cited by 40 · see citing works
Alternative respiratory chain enzymes: Therapeutic potential and possible pitfalls
Saari, S., Garcia, G. S., Bremer, K., Chioda, M. M., Andjelković, A., Debes, P. V., Nikinmaa, M., Szibor, M., Dufour, É., Rustin, P., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.10.012 · Cited by 39 · see citing works
Self-citationUncoupling proteins of invertebrates: A review
Słocińska, M., Barylski, J., & Jarmuszkiewicz, W. (2016) · IUBMB Life · doi:10.1002/iub.1535 · Cited by 36 · see citing works
Kushnirov, V. V., Vishnevskaya, A. B., Alexandrov, I. M., & Ter‐Avanesyan, M. D. (2007) · Prion · doi:10.4161/pri.1.3.4840 · Cited by 36 · see citing works
Collard, M., Ridder, C. D., David, B., Dehairs, F., & Dubois, P. (2014) · Global Change Biology · doi:10.1111/gcb.12735 · Cited by 34 · see citing works
A New Fungicide Produced by a Streptomyces sp. GAAS7310
Chen, G., Lin, B., Lin, Y., Xie, F., Lu, W., & Fong, W. F. (2005) · The Journal of Antibiotics · doi:10.1038/ja.2005.70 · Cited by 31 · see citing works
Liu, M., & Guo, X. (2017) · Scientific Reports · doi:10.1038/s41598-017-10976-w · Cited by 30 · see citing works
The transcriptomic responses of the ark shell, Anadara broughtonii, to sulfide and hypoxia exposure
Wang, Y., Zhou, S., Liu, T., Chen, M., Li, W., & Zhang, X. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-04879-4 · Cited by 29 · see citing works
Expression of Ciona intestinalis AOX causes male reproductive defects in Drosophila melanogaster
Saari, S., Andjelković, A., Garcia, G. S., Jacobs, H. T., & Oliveira, M. T. (2017) · BMC Developmental Biology · doi:10.1186/s12861-017-0151-3 · Cited by 27 · see citing works
Self-citationRespiratory chain signalling is essential for adaptive remodelling following cardiac ischaemia
Szibor, M., Schreckenberg, R., Gizatullina, Z. Z., Dufour, É., Wiesnet, M., Dhandapani, P. K., Dębska–Vielhaber, G., Heidler, J., Wittig, I., Nyman, T. A., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15043 · Cited by 24 · see citing works
Self-citationThe Alternative Oxidase AOX Does Not Rescue the Phenotype oftko25tMutant Flies
Kemppainen, K. K., Kemppainen, E., & Jacobs, H. T. (2014) · G3 Genes Genomes Genetics · doi:10.1534/g3.114.013946 · Cited by 23 · see citing works
Self-citationTward, C. E., Singh, J., Cygelfarb, W., & McDonald, A. E. (2018) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2018.11.003 · Cited by 23 · see citing works
Mitochondrial alternative oxidase contributes to successful tardigrade anhydrobiosis
Wojciechowska, D., Karachitos, A., Roszkowska, M., Rzeźniczak, W., Sobkowiak, R., Kaczmarek, Ł., Kosicki, J. Z., & Kmita, H. (2021) · Frontiers in Zoology · doi:10.1186/s12983-021-00400-5 · Cited by 21 · see citing works
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Salminen, T. S., Cannino, G., Oliveira, M. T., Lillsunde, P., Jacobs, H. T., & Kaguni, L. S. (2019) · G3 Genes Genomes Genetics · doi:10.1534/g3.119.400315 · Cited by 21 · see citing works
Self-citationDhandapani, P. K., Begines-Moreno, I. M., Brea‐Calvo, G., Gärtner, U., Graeber, T. G., Sanchez, G. J., Morty, R. E., Schönig, K., ten Hoeve, J., Wietelmann, A., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-49231-9 · Cited by 19 · see citing works
Self-citationHuang, J., Zhang, L., Li, J., Shi, X., & Zhang, Z. (2013) · Journal of the Marine Biological Association of the United Kingdom · doi:10.1017/s0025315413000696 · Cited by 16 · see citing works
Giordano, L., Aneja, M. K., Sommer, N., Alebrahimdehkordi, N., Saraji, A. A., Weißmann, N., Rudolph, C., Plank, C., Jacobs, H. T., & Szibor, M. (2021) · Gene Therapy · doi:10.1038/s41434-021-00235-z · Cited by 16 · see citing works
Self-citationÁrnason, E. (1991) · Genetics · doi:10.1093/genetics/129.1.145 · Cited by 16 · see citing works
Bremer, K., Yasuo, H., Debes, P. V., & Jacobs, H. T. (2021) · Journal of Experimental Biology · doi:10.1242/jeb.242985 · Cited by 15 · see citing works
Self-citationTurnell, B. R., Kumpitsch, L., & Reinhardt, K. (2021) · Biogerontology · doi:10.1007/s10522-021-09922-1 · Cited by 15 · see citing works
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Saari, S., Kemppainen, E., Tuomela, T., Oliveira, M. T., Dufour, É., & Jacobs, H. T. (2019) · Journal of Experimental Zoology Part A Ecological and Integrative Physiology · doi:10.1002/jez.2274 · Cited by 11 · see citing works
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Dhandapani, P. K., Lyyski, A., Paulin, L. G., Khan, N. A., Suomalainen, A., Auvinen, P., Dufour, É., Szibor, M., & Jacobs, H. T. (2019) · Physiological Reports · doi:10.14814/phy2.14159 · Cited by 11 · see citing works
Self-citationOverexpression of Cerasus humilis ChAOX2 improves the tolerance of Arabidopsis to salt stress
Sun, L., Zhao, X. Y., Ren, J., Yan, S. P., Zhao, X. Y., & Song, X. (2021) · 3 Biotech · doi:10.1007/s13205-021-02871-z · Cited by 10 · see citing works
Landeira-Fernandez, A. M., Galina, A., & MEIS, L. D. (2000) · Journal of Experimental Biology · doi:10.1242/jeb.203.23.3613 · Cited by 10 · see citing works
Streptomyces strains producing mitochondriotoxic antimycin A found in cereal grains
Rasimus, S., Mikkola, R., Andersson, M. A., Jestoi, M. N., & Salkinoja-Salonen, M. S. (2015) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2015.11.007 · Cited by 9 · see citing works
Exogenous Factors May Differentially Influence the Selective Costs of mtDNA Mutations
Aw, W. C., Garvin, M. R., & Ballard, J. W. O. (2018) · Advances in anatomy, embryology and cell biology · doi:10.1007/102_2018_2 · Cited by 5 · see citing works
Self-citationThe Pyrogenic Responses of Invertebrates
Casterlin, M. E., & REYNOLDS, W. W. (1982) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-68569-9_20 · Cited by 4 · see citing works
Systemic impact of the expression of the mitochondrial alternative oxidase on Drosophila developmentPreprint
de Camargo, A. F., Saari, S., Garcia, G. S., Chioda, M. M., Othonicar, M. F., Martins, A. A., Hayashi, G., ten Hoeve, J., Jacobs, H. T., Pinheiro, D. G., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.24.461559 · Cited by 3 · see citing works
Self-citationHan, L., Quan, Z., Han, B., Ding, B., Huang, X., Wang, H., Chang, Y., & Ding, J. (2021) · Journal of Oceanology and Limnology · doi:10.1007/s00343-020-0181-8 · Cited by 2 · see citing works
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Toulis, V., Marfany, G., & Mirra, S. (2025) · Marine Drugs · doi:10.3390/md23080315 · Cited by 5 · see citing works
Rein, K. S., Colon, R., Romagosa, C. R., Ohnikian, N. R., Francis, K. T., & Rein, S. R. (2025) · Marine Drugs · doi:10.3390/md23070291 · Cited by 2 · see citing works
Łabędzka-Dmoch, K., Bui, T. H. D., Piątkowski, J., Dilling, M., Jagiełło, P., Kabza, W., & Golik, P. (2026) · Molecular Biology and Evolution · doi:10.1093/molbev/msag005 · Cited by 1 · see citing works
Wang, Y., Xia, F., Jia, S., Yang, Y., & Zhang, X. (2024) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2024.109953 · Cited by 1 · see citing works
Shao, S., Song, Y., Gao, Y., Cao, Y., Chen, C., Wang, X., Lu, B., Zhang, Y., & Gao, J. (2026) · Horticulturae · doi:10.3390/horticulturae12070810 · Cited by 1 · see citing works
Monesi, N., Fernandes, G. M., Valer, F. B., Uliana, J. V. C., Trinca, V., Azzolini, A. E. C. S., Gorab, E., & Alberici, L. C. (2025) · Biochimie · doi:10.1016/j.biochi.2025.02.007 · Cited by 1 · see citing works
Banerjee, R., Upadhyay, D., Zárybnický, T., Kietz, C., Kuure, S., Fellman, V., Purhonen, J., & Kallijärvi, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.23.612616 · Cited by 1 · see citing works
There is often – but not always – an alternative!
Jacobs, H. T., & Moore, A. L. (2024) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2024.149533 · Cited by 1 · see citing works
Self-citationAbsence of heterosis for hypoxia tolerance in F1 hybrids of Tigriopus californicus
Deconinck, A., Madalone, O., & Willett, C. S. (2024) · Journal of Heredity · doi:10.1093/jhered/esae061
WITHDRAWN: There is often – But not always – An alternative!
Jacobs, H. T., & Moore, A. L. (2024) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2024.149534
Self-citationRetractedRossi, G. S., Venkatesh, S., McDonald, A. E., & Little, A. G. (2026) · Journal of Experimental Biology · doi:10.1242/jeb.252244
- Authors
- Jacobs, H. T., & Ballard, J. W. O.
- Affiliations
- Tampere University (FI)
- The University of Melbourne (AU)
- Corresponding author
- Jacobs, Howard T.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 2022-08
- Volume
- 1863
- Issue
- 6
- Pages
- 148556
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W4221035006
- Cited by
- 25
- References
- 80
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 7 · 2023: 6 · 2022: 4
- FWCI
- 1.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Figshare (submittedVersion, cc-by)
- Tampere University Institutional Repository (Tampere University) (submittedVersion, cc-by)
- La Trobe University (cc-by)
- Funders
- Academy of Finland (283157, 272376, 324730)
- European Research Council (232738)
- Australian Research Council (190102555, 160102575)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Environmental Science › Ecology › Physiological and biochemical adaptations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- alternative oxidase, physiological role, stress tolerance, oxidative stress, protein unfolding, desiccation, pathogen resistance, toxin resistance, mitochondrial respiration, model organisms
- MeSH terms
- Alternative Oxidase, Animals, Ciona intestinalis, Oxidoreductases, Plant Proteins, Mitochondrial Proteins
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