The ATP synthase: the understood, the uncertain and the unknown

Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Abrahams, J., Leslie, A. G., Lutter, R., & Walker, J. (1994) · Nature · doi:10.1038/370621a0 · Cited by 2,961

Direct observation of the rotation of F1-ATPase

Noji, H., Yasuda, R., Yoshida, M., & Kinosita, K. (1997) · Nature · doi:10.1038/386299a0 · Cited by 2,216

The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å

Tomitake Tsukihara, A., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1996) · Science · doi:10.1126/science.272.5265.1136 · Cited by 2,102

Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans

Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,019

RESPIRATORY ENZYMES IN OXIDATIVE PHOSPHORYLATION

Chance, B., & Williams, G. R. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57189-7 · Cited by 1,473

Molecular Architecture of the Rotary Motor in ATP Synthase

Stock, D., Leslie, A. G. W., & Walker, J. E. (1999) · Science · doi:10.1126/science.286.5445.1700 · Cited by 1,271

Complete Structure of the 11-Subunit Bovine Mitochondrial Cytochrome bc 1 Complex

Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., & Jap, B. K. (1998) · Science · doi:10.1126/science.281.5373.64 · Cited by 1,253

The binding change mechanism for ATP synthase--some probabilities and possibilities.

Boyer, P. (1993) · Biochimica et Biophysica Acta · doi:10.1016/0005-2728(93)90063-l · Cited by 968

Architecture of succinate dehydrogenase and reactive oxygen species generation

Yankovskaya, V., Horsefield, R., Törnroth, S., Luna-Chavez, C., Miyoshi, H., Léger, C., Byrne, B., Cecchini, G., & Iwata, S. (2003) · Science · doi:10.1126/science.1079605 · Cited by 927

Crystal Structure of Mitochondrial Respiratory Membrane Protein Complex II

Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., & Rao, Z. (2005) · Cell · doi:10.1016/j.cell.2005.05.025 · Cited by 881

Mitochondrial membrane potential

Zorova, L. D., Popkov, V. A., Plotnikov, E. Y., Silachev, D. N., Pevzner, I. B., Jankauskas, S. S., Babenko, V. A., Zorov, S. D., Balakireva, A. V., Juhaszova, M., et al. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.07.009 · Cited by 2,092

Multifaceted mitochondria: moving mitochondrial science beyond function and dysfunction

Monzel, A. S., Enrı́quez, J. A., & Picard, M. A. (2023) · Nature Metabolism · doi:10.1038/s42255-023-00783-1 · Cited by 632

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology

Bernardi, P., Rasola, A., Forte, M. A., & Lippe, G. (2015) · Physiological Reviews · doi:10.1152/physrev.00001.2015 · Cited by 598

Sequence co-evolution gives 3D contacts and structures of protein complexes

Hopf, T. A., Schärfe, C. P. I., Rodrigues, J. P. G. L. M., Green, A. G., Kohlbacher, O., Sander, C., Bonvin, A. M. J. J., & Marks, D. S. (2014) · eLife · doi:10.7554/elife.03430 · Cited by 515

Mitochondria at the crossroads of health and disease

Suomalainen, A., & Nunnari, J. M. (2024) · Cell · doi:10.1016/j.cell.2024.04.037 · Cited by 528

Role of Mitochondrial Calcium and the Permeability Transition Pore in Regulating Cell Death

Bauer, T. M., & Murphy, E. (2020) · Circulation Research · doi:10.1161/circresaha.119.316306 · Cited by 450

Structure and Mechanisms of F-Type ATP Synthases

Kühlbrandt, W. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-110903 · Cited by 445

ATP Synthase

Junge, W., & Nelson, N. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034124 · Cited by 351

Mitochondrial genetic medicine

Wallace, D. C. (2018) · Nature Genetics · doi:10.1038/s41588-018-0264-z · Cited by 344

Mechanisms of mitochondrial respiratory adaptation

Bennett, C. F., Latorre‐Muro, P., & Puigserver, P. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00506-6 · Cited by 322

Mitochondrial disorders of the OXPHOS system

Fernández‐Vizarra, E., & Zeviani, M. (2020) · FEBS Letters · doi:10.1002/1873-3468.13995 · Cited by 323

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM

Zhou, A., Rohou, A. L., Schep, D. G., Bason, J. V., Montgomery, M. G., Walker, J. E., Grigorieff, N., & Rubinstein, J. L. (2015) · eLife · doi:10.7554/elife.10180 · Cited by 298

Structure of the mycobacterial ATP synthase F o rotor ring in complex with the anti-TB drug bedaquiline

Preiß, L., Langer, J. D., Yıldız, Ö., Eckhardt-Strelau, L., Guillemont, J., Koul, A., & Meier, T. W. (2015) · Science Advances · doi:10.1126/sciadv.1500106 · Cited by 305

Architecture of bacterial respiratory chains

Kaila, V. R. I., & Wikström, M. K. F. (2021) · Nature Reviews Microbiology · doi:10.1038/s41579-020-00486-4 · Cited by 297

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

Zhao, J., Benlekbir, S., & Rubinstein, J. L. (2015) · Nature · doi:10.1038/nature14365 · Cited by 283

Assembly of mammalian oxidative phosphorylation complexes I–V and supercomplexes

Signes, A., & Fernandez-Vizarra, E. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170098 · Cited by 267

New Perspectives on Proton Pumping in Cellular Respiration

Wikström, M. K. F., Sharma, V., Kaila, V. R. I., Hosler, J. P., & Hummer, G. (2015) · Chemical Reviews · doi:10.1021/cr500448t · Cited by 262

Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase

He, J., Ford, H. C., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702357114 · Cited by 251

Mitochondrial Respiratory Chain Complexes

Sousa, J. S., D’Imprima, E., & Vonck, J. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-10-7757-9_7 · Cited by 263

2-Hydroxyglutarate Inhibits ATP Synthase and mTOR Signaling

Fu, X., Chin, R., Vergnes, L., Hwang, H., Deng, G., Xing, Y., Pai, M. Y., Li, S., Ta, L. H., Fazlollahi, F., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.06.009 · Cited by 230

Atomic model for the dimeric F O region of mitochondrial ATP synthase

Guo, H., Bueler, S. A., & Rubinstein, J. L. (2017) · Science · doi:10.1126/science.aao4815 · Cited by 225

Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions

Protasoni, M., & Zeviani, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020586 · Cited by 243

Mitochondrial dysfunction in microglia: a novel perspective for pathogenesis of Alzheimer’s disease

Li, Y., Xia, X., Wang, Y., & Zheng, J. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02613-9 · Cited by 231

S- Sulfhydration of ATP synthase by hydrogen sulfide stimulates mitochondrial bioenergetics

Módis, K., Ju, Y., Ahmad, A., Untereiner, A. A., Altaany, Z., Wu, L., Szabó, C., & Wang, R. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.08.023 · Cited by 205

Structure of the dimeric ATP synthase from bovine mitochondria

Spikes, T. E., Montgomery, M. G., & Walker, J. E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2013998117 · Cited by 210

Cryo-EM structure of the entire mammalian F-type ATP synthase

Pinke, G., Zhou, L., & Sazanov, L. A. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0503-8 · Cited by 207

Assembly of the membrane domain of ATP synthase in human mitochondria

He, J., Ford, H. C., Carroll, J., Douglas, C. P. L. C., Gonzales, E., Ding, S., Fearnley, I. M., & Walker, J. E. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722086115 · Cited by 207

Mitochondrial ROS Production Protects the Intestine from Inflammation through Functional M2 Macrophage Polarization

Formentini, L., Santacatterina, F., de Arenas, C. N., Stamatakis, K., Martínez, D. L., Logan, A., Fresno, M., Smits, R., Murphy, M. P., & Cuezva, J. M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.04.036 · Cited by 202

Cryo-EM structure of the mammalian ATP synthase tetramer bound with inhibitory protein IF1

Gu, J., Zhang, L., Zong, S., Guo, R., Liu, T., Yi, J., Wang, P., Zhuo, W., & Yang, M. (2019) · Science · doi:10.1126/science.aaw4852 · Cited by 200

Keeping the home fires burning: AMP-activated protein kinase

Hardie, D. G. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2017.0774 · Cited by 195

Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase

He, J., Carroll, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1711201114 · Cited by 182

Structure of a bacterial ATP synthase

Guo, H., Suzuki, T., & Rubinstein, J. L. (2019) · eLife · doi:10.7554/elife.43128 · Cited by 187

An overview of new antitubercular drugs, drug candidates, and their targets

Bahuguna, A., & Rawat, D. S. (2019) · Medicinal Research Reviews · doi:10.1002/med.21602 · Cited by 179

(Nano)mechanical Motion Triggered by Metal Coordination: from Functional Devices to Networked Multicomponent Catalytic Machinery

Goswami, A., Saha, S., Biswas, P. K., & Schmittel, M. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00159 · Cited by 171

Mammalian Mitochondrial Complex I Structure and Disease-Causing Mutations

Fiedorczuk, K., & Sazanov, L. A. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.06.006 · Cited by 167

Targeting Ferroptosis against Ischemia/Reperfusion Cardiac Injury

Lillo‐Moya, J., Rojas-Solé, C., Muñoz-Salamanca, D., Panieri, E., Saso, L., & Rodrigo, R. (2021) · Antioxidants · doi:10.3390/antiox10050667 · Cited by 166

Alkaliphilic Bacteria with Impact on Industrial Applications, Concepts of Early Life Forms, and Bioenergetics of ATP Synthesis

Preiß, L., Hicks, D. B., Suzuki, S., Meier, T. W., & KRULWICH, T. A. (2015) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2015.00075 · Cited by 161

Shaping the mitochondrial inner membrane in health and disease

Colina-Tenorio, L., Horten, P., Pfanner, N., & Rampelt, H. (2020) · Journal of Internal Medicine · doi:10.1111/joim.13031 · Cited by 156

Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I

Kaila, V. R. I. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2017.0916 · Cited by 152

The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function

Quintana–Cabrera, R., Quirin, C., Glytsou, C., Corrado, M., Urbani, A., Pellattiero, A., Calvo, E., Vázquez, J., Enrı́quez, J. A., Gerle, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05655-x · Cited by 154

The Similarities between Human Mitochondria and Bacteria in the Context of Structure, Genome, and Base Excision Repair System

Boguszewska, K., Szewczuk, M., Kaźmierczak-Barańska, J., & Karwowski, B. T. (2020) · Molecules · doi:10.3390/molecules25122857 · Cited by 152

Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution

Morales‐Ríos, E., Montgomery, M. G., Leslie, A. G. W., & Walker, J. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517542112 · Cited by 142

VDAC Regulation: A Mitochondrial Target to Stop Cell Proliferation

Fang, D., & Maldonado, E. N. (2018) · Advances in cancer research · doi:10.1016/bs.acr.2018.02.002 · Cited by 142

The ATPase Inhibitory Factor 1 (IF1): A master regulator of energy metabolism and of cell survival

García-Bermúdez, J., & Cuezva, J. M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.02.004 · Cited by 141

Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion

Rosenberg, O. S., Dovala, D., Li, X., Connolly, L., Bendebury, A., Finer-Moore, J., Holton, J., Cheng, Y., Stroud, R. M., & Cox, J. S. (2015) · Cell · doi:10.1016/j.cell.2015.03.040 · Cited by 134

Structural basis for power stroke vs. Brownian ratchet mechanisms of motor proteins

Hwang, W., & Karplus, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1818589116 · Cited by 135

Cardiolipin binds selectively but transiently to conserved lysine residues in the rotor of metazoan ATP synthases

Duncan, A. L., Robinson, A. J., & Walker, J. E. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608396113 · Cited by 133

Mitochondrial Morphofunction in Mammalian Cells

Bulthuis, E. P., Adjobo-Hermans, M. J. W., Willems, P. H. G. M., & Koopman, W. J. H. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7534 · Cited by 133

Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase

Carroll, J., He, J., Ding, S., Fearnley, I. M., & Walker, J. E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904005116 · Cited by 132

PKA Phosphorylates the ATPase Inhibitory Factor 1 and Inactivates Its Capacity to Bind and Inhibit the Mitochondrial H+-ATP Synthase

García‐Bermúdez, J., Sánchez‐Aragó, M., Soldevilla, B., del Arco, A., Nuevo‐Tapioles, C., & Cuezva, J. M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.08.052 · Cited by 130

Enhancing photosynthesis in plants: the light reactions

Cardona, T., Shao, S., & Nixon, P. J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170015 · Cited by 129

Assembly Line Polyketide Synthases: Mechanistic Insights and Unsolved Problems

Khosla, C., Herschlag, D., Cane, D. E., & Walsh, C. T. (2014) · Biochemistry · doi:10.1021/bi500290t · Cited by 125

S-glutathionylation reactions in mitochondrial function and disease

Mailloux, R. J., & Willmore, W. G. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00068 · Cited by 130

Who and how in the regulation of mitochondrial cristae shape and function

Quintana–Cabrera, R., Mehrotra, A., Rigoni, G., & Soriano, M. E. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.04.088 · Cited by 124

Optical/electrochemical methods for detecting mitochondrial energy metabolism

Ji, W., Tang, X. X., Du, W., Lu, Y., Wang, N., Wu, Q., Wei, W., Liu, J., Yu, H., Ma, B., et al. (2021) · Chemical Society Reviews · doi:10.1039/d0cs01610a · Cited by 124

The H+-ATP synthase: A gate to ROS-mediated cell death or cell survival

Martínez‐Reyes, I., & Cuezva, J. M. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.03.010 · Cited by 130

Mitochondrial cAMP signaling

Zhang, F., Zhang, L., Qi, Y., & Xu, H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2282-2 · Cited by 129

Automated segmentation and tracking of mitochondria in live-cell time-lapse images

Lefebvre, A. E. Y. T., Ma, D., Kessenbrock, K., Lawson, D. A., & Digman, M. A. (2021) · Nature Methods · doi:10.1038/s41592-021-01234-z · Cited by 121

Arrangement of subunits in intact mammalian mitochondrial ATP synthase determined by cryo-EM

Baker, L. A., Watt, I. N., Runswick, M. J., Walker, J. E., & Rubinstein, J. L. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204935109 · Cited by 120

Bacteriorhodopsin: Would the real structural intermediates please stand up?

Wickstrand, C., Dods, R. H., Royant, A., & Neutze, R. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.05.021 · Cited by 117

Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch

Sobti, M., Walshe, J. L., Wu, D., Ishmukhametov, R. R., Zeng, Y. C., Robinson, C. V., Berry, R. M., & Stewart, A. G. (2020) · Nature Communications · doi:10.1038/s41467-020-16387-2 · Cited by 116

ATP synthase in mycobacteria: Special features and implications for a function as drug target

Lü, P., Lill, H., & Bald, D. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.01.022 · Cited by 115

Mitochondrial ATP synthase is dispensable in blood-stage Plasmodium berghei rodent malaria but essential in the mosquito phase

Sturm, A., Mollard, V., Cozijnsen, A. J., Goodman, C. D., & McFadden, G. I. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1423959112 · Cited by 114

Structure of the human ATP synthase

Lai, Y., Zhang, Y., Zhou, S., Xu, J., Du, Z., Feng, Z., Yu, L., Zhao, Z., Wang, W., Tang, Y., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.04.029 · Cited by 120

Physiological roles of the mitochondrial permeability transition pore

Mnatsakanyan, N., Beutner, G., Porter, G. A., Alavian, K. N., & Jonas, E. A. (2016) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-016-9652-1 · Cited by 120

Vacuolar Transporters – Companions on a Longtime Journey

Martinoia, E. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.01481 · Cited by 111

Evolutionary cell biology: Two origins, one objective

Lynch, M., Field, M. C., Goodson, H. V., Malik, H. S., Pereira‐Leal, J. B., Roos, D. S., Turkewitz, A. P., & Sazer, S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415861111 · Cited by 116

ATP synthase promotes germ cell differentiation independent of oxidative phosphorylation

Teixeira, F. K., Sanchez, C. G., Hurd, T. R., Seifert, J. R. K., Czech, B., Preall, J. B., Hannon, G. J., & Lehmann, R. (2015) · Nature Cell Biology · doi:10.1038/ncb3165 · Cited by 110

Structural mechanisms of cyclophilin D-dependent control of the mitochondrial permeability transition pore

Gutiérrez‐Aguilar, M., & Baines, C. P. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.11.009 · Cited by 110

Emerging concepts in the therapy of mitochondrial disease

Viscomi, C. F., Bottani, E., & Zeviani, M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.001 · Cited by 109

Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes

Toth, A., Meyrat, A., Stoldt, S., Santiago, R., Wenzel, D., Jakobs, S., von Ballmoos, C., & Ott, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917968117 · Cited by 103

Assembly of F1F0-ATP synthases

Rühle, T., & Leister, D. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.02.005 · Cited by 100

High ATP Production Fuels Cancer Drug Resistance and Metastasis: Implications for Mitochondrial ATP Depletion Therapy

Fiorillo, M., Ózsvári, B., Sotgia, F., & Lisanti, M. P. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.740720 · Cited by 104

Why succinate? Physiological regulation by a mitochondrial coenzyme Q sentinel

Murphy, M. P., & Chouchani, E. T. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01004-8 · Cited by 105

Toward Artificial Cells: Novel Advances in Energy Conversion and Cellular Motility

Jeong, S., Nguyen, H. T., Kim, C. H., Ly, M. N., & Shin, K. (2020) · Advanced Functional Materials · doi:10.1002/adfm.201907182 · Cited by 100

The Pancreatic β-Cell: A Bioenergetic Perspective

Nicholls, D. G. (2016) · Physiological Reviews · doi:10.1152/physrev.00009.2016 · Cited by 100

Structure and Mechanism of Respiratory III–IV Supercomplexes in Bioenergetic Membranes

Brzezinski, P., Moe, A., & Ädelroth, P. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00140 · Cited by 97

Structure and mechanism of the proton-driven motor that powers type 9 secretion and gliding motility

James, R. H., Deme, J. C., Kjær, A., Alcock, F., Silale, A., Lauber, F., Johnson, S., Berks, B. C., & Lea, S. M. (2021) · Nature Microbiology · doi:10.1038/s41564-020-00823-6 · Cited by 90

Inhibition of the ATP Synthase Eliminates the Intrinsic Resistance of Staphylococcus aureus towards Polymyxins

Vestergaard, M. R., Nøhr-Meldgaard, K., Bojer, M. S., Nielsen, C. K., Meyer, R. L., Slavetinsky, C. J., Peschel, A., & Ingmer, H. (2017) · mBio · doi:10.1128/mbio.01114-17 · Cited by 92

A Review of the Inhibition of the Mitochondrial ATP Synthase by IF1 in vivo: Reprogramming Energy Metabolism and Inducing Mitohormesis

García-Aguilar, A., & Cuezva, J. M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01322 · Cited by 89

Ndufs4 knockout mouse models of Leigh syndrome: pathophysiology and intervention

van de Wal, M. A. E., Adjobo-Hermans, M. J. W., Keijer, J., Schirris, T. J. J., Homberg, J. R., Wieckowski, M. R., Grefte, S., van Schothorst, E. M., van Karnebeek, C., Quintana, A., et al. (2021) · Brain · doi:10.1093/brain/awab426 · Cited by 93

Phosphate release coupled to rotary motion of F 1 -ATPase

Okazaki, K.-I., & Hummer, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1305497110 · Cited by 88

Mitochondria as Therapeutic Targets in Transplantation

Saeb‐Parsy, K., Martin, J. L., Summers, D. M., Watson, C. J. E., Krieg, T., & Murphy, M. P. (2020) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2020.08.001 · Cited by 88

Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals

Jiko, C., Davies, K. M., Shinzawa‐Itoh, K., Tani, K., Maeda, S., Mills, D. J., Tomitake Tsukihara, A., Fujiyoshi, Y., Kühlbrandt, W., & Gerle, C. (2015) · eLife · doi:10.7554/elife.06119 · Cited by 87

Rotary ATPases—dynamic molecular machines

Stewart, A. G., Laming, E. M., Sobti, M., & Stock, D. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.11.013 · Cited by 85

Iron Dysregulation in Mitochondrial Dysfunction and Alzheimer’s Disease

Onukwufor, J. O., Dirksen, R. T., & Wojtovich, A. P. (2022) · Antioxidants · doi:10.3390/antiox11040692 · Cited by 85

The non-glycosylated isoform of MIC26 is a constituent of the mammalian MICOS complex and promotes formation of crista junctions

Koob, S., Barrera, M., Anand, R., & Reichert, A. S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.03.004 · Cited by 83

The six steps of the complete F1-ATPase rotary catalytic cycle

Sobti, M., Ueno, H., Noji, H., & Stewart, A. G. (2021) · Nature Communications · doi:10.1038/s41467-021-25029-0 · Cited by 82

Exploring membrane respiratory chains

Marreiros, B. C., Calisto, F., Castro, P. J., Duarte, A. M. S., Sena, F. V., Filipa-Silva, A., Sousa, F. M., Teixeira, M. S., Refojo, P. N., & Pereira, M. M. (2016) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2016.03.028 · Cited by 84

High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase

Matthies, D., Zhou, W., Klyszejko, A. L., Anselmi, C., Yıldız, Ö., Brandt, K., Müller, V., Faraldo‐Gómez, J. D., & Meier, T. W. (2014) · Nature Communications · doi:10.1038/ncomms6286 · Cited by 80

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