Cited by 614ATP Synthase and ATPases ResearchPhotosynthetic Processes and MechanismsMitochondrial Function and Pathology

The DOI matches its Crossref record; 121 of the 123 references it cites were found in a registry or an index.

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

Walker, John E.·2013·Biochemical Society Transactions

DOI 10.1042/bst20110773

Open this paper in CoChat — free account

Abstract

The ATP synthases are multiprotein complexes found in the energy-transducing membranes of bacteria, chloroplasts and mitochondria. They employ a transmembrane protonmotive force, Δp, as a source of energy to drive a mechanical rotary mechanism that leads to the chemical synthesis of ATP from ADP and Pi. Their overall architecture, organization and mechanistic principles are mostly well established, but other features are less well understood. For example, ATP synthases from bacteria, mitochondria and chloroplasts differ in the mechanisms of regulation of their activity, and the molecular bases of these different mechanisms and their physiological roles are only just beginning to emerge. Another crucial feature lacking a molecular description is how rotation driven by Δp is generated, and how rotation transmits energy into the catalytic sites of the enzyme to produce the stepping action during rotation. One surprising and incompletely explained deduction based on the symmetries of c-rings in the rotor of the enzyme is that the amount of energy required by the ATP synthase to make an ATP molecule does not have a universal value. ATP synthases from multicellular organisms require the least energy, whereas the energy required to make an ATP molecule in unicellular organisms and chloroplasts is higher, and a range of values has been calculated. Finally, evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria. Here the enzymes form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.

Integrity signals

Registry

Crossref · 10.1042/bst20110773

Cites

121 of 121 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

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
Self-citation
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
Self-citation
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

Flagged first, then by citations

Show all 123 references

2 of the 123 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Mitchell, 1993, David Keilin's respiratory chain concept and its chemiosmotic consequences, 295

Sorted by citations

Items 501–600 of 603

Artificial DNA-nano/microparticle motors: Factors governing speed, run length, and unidirectionality revealed by geometry-based kinetic simulations
Harashima, T., & Iino, R. (2026) · Biophysical Journal · doi:10.1016/j.bpj.2026.09.041 · Cited by 1
Mitochondrial complex I in focus: mechanisms and therapeutic strategies of urinary system diseases
Yu, F., Li, Y., Qu, R., Wang, Z., An, W., Chen, Y., Yue, Z., & Wang, W. J. (2026) · Frontiers in Physiology · doi:10.3389/fphys.2026.1753159 · Cited by 1
Emerging Roles of Adenosine Metabolism in Astrocytes During Brain Injury
Zhu, S., Zhong, S., Lin, X. P., Zhao, C., & Li, Y. (2026) · CNS Neuroscience & Therapeutics · doi:10.1002/cns.70889 · Cited by 1
Mitochondrial permeability transition in redox homeostasis and ferroptosis
Guo, L. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113244 · Cited by 1
A comparison of the innate flexibilities of six chains in F1-ATPase with identical secondary and tertiary folds; 3 active enzymes and 3 structural proteins
Tirion, M. M. (2016) · Structural Dynamics · doi:10.1063/1.4967226 · Cited by 1
Dynamic modulation of transthylakoid electric potential by chloroplast ATP synthases
Lyu, H., & Zuo, Y.-S. (2024) · Biochimie · doi:10.1016/j.biochi.2024.01.007 · Cited by 1
Engineering of IF1‐susceptive bacterial F1‐ATPase
Hatasaki, Y. C., Kobayashi, R., Watanabe, R. R., Hara, M., Ueno, H., & Noji, H. (2024) · Protein Science · doi:10.1002/pro.4942 · Cited by 1
Biological Energy Transformation
Knoflacher, M. (2024) · Springer eBooks · doi:10.1007/978-3-662-69423-7_7 · Cited by 1
ATP synthesis of Enterococcus hirae V-ATPase driven by sodium motive force
Otomo, A., Zhu, L. G. H., Okuni, Y., Yamamoto, M., & Iino, R. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108422 · Cited by 1
Activation of Bacterial F-ATPase by LDAO: Deciphering the Molecular Mechanism
Bruman, S. M., Zubareva, V. M., Shugaeva, T. E., Lapashina, A. S., & Feniouk, B. A. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297924602600 · Cited by 1
Evolution and regulatory diversification of plastid F1FO-ATP synthase
Kohzuma, K., Muraoka, S., Kumazawa, M., & Ifuku, K. (2025) · Plant and Cell Physiology · doi:10.1093/pcp/pcaf100 · Cited by 1
Mitochondrial Calcium Uptake in Activation of the Permeability Transition Pore and Cell Death
Solesio, M. E., & Pavlov, E. V. (2017) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-319-55539-3_4 · Cited by 2
Motion and Nanomechanical Effects in Supramolecular Catalysts
Schmittel, M., Goswami, A., Paul, I., & Biswas, P. K. (2020) · Advances in atom and single molecule machines · doi:10.1007/978-3-030-56777-4_13 · Cited by 1
Структурно-функциональные аспекты терморегуляции электронного транспорта и синтеза АТР в хлоропластах
Vershubskii, A. V., & Tikhonov, A. N. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521010097 · Cited by 1
Characterization of inner mitochondrial membrane architecture
Barbot, M. (2016) · doi:10.53846/goediss-5829 · Cited by 1
Visualizing movements in E. coli F 1 F o ATP synthase indicates how the F 1 and F o motors are coupledPreprint
Sobti, M., Walshe, J. L., Ishmukhametov, R. R., & Stewart, A. G. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/622084 · Cited by 1
Subunit epsilon of E. coli F 1 F o ATP synthase attenuates enzyme activity by modulating central stalk flexibilityPreprint
Sobti, M., Walshe, J. L., Zeng, Y. C., Ishmukhametov, R. R., & Stewart, A. G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.320408 · Cited by 1
Obtenção de anticorpos monoclonais murinos contra antígenos de Staphylococcus aureus resistentes à meticilina por imunização subtrativa
Simões, A. C. (2015) · Americanae (AECID Library)
From chemiosmotic redox loops to proton motive molecular machines
Wikström, M. K. F. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.05.139
A potassium “transporter” regulated by the ATP/ADP ratio
Morais-Cabral, J. H. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.05.135
Bioenergetics in Mitochondria, Bacteria and Chloroplasts
MacMillan, F., & Meier, T. W. (2013)
The Mitochondrial Permeability Transition Pore, the c‐Subunit of the F1FoATP Synthase, Cellular Development, and Synaptic Efficiency
Jonas, E. A., Porter, G. A., Beutner, G., Mnatsakanyan, N., & Alavian, K. N. (2015) · Wiley eBooks · doi:10.1002/9781119017127.ch2
Conversion of the ATP synthase subunit c into a hydrophilic pore
Kulik, D. (2016) · University Library - University of Saskatchewan (University of Saskatchewan)
Functional Characterization of Human ADCK3 and ADCK4, Mitochondrial Atypical Kinases
Wheeler, B. (2015) · QSpace (Queen's University Library)
Isolation and functional studies of the F-type ATP synthase from spinach chloroplasts and Heliobacterium modesticaldum
Yang, J.-H. (2015)
TOPOLOGÍA Y FUNCIÓN DE LAS SUBUNIDADES INTRÍNSECAS DE LA MEMBRANA DE LAS F 1 F O -ATP SINTASA MITOCONDRIALES
Sánchez-Vásquez, L., & González‐Halphen, D. (2017) · TIP Revista Especializada en Ciencias Químico-Biológicas · doi:10.1016/j.recqb.2017.04.004
The elastic transfer model of angular rate modulation in F1-ATPase stalling and controlled rotation experiments
Volkán-Kacsó, S. (2017) · Modern Physics Letters B · doi:10.1142/s0217984917300022
Computational Structural Biology of Macromolecular Interactions
Rodrigues, J. G. L. M. (2014) · Utrecht University Repository (Utrecht University)
The Design and Synthesis of Novel AOX and cytochrome bc 1 complex inhibitors which act as Phytopathogenic Fungicides
Misselbrook, J. (2019) · Sussex Research Online (University of Sussex) · doi:10.13140/rg.2.2.22947.40486
Structures of an intact yeast V-ATPase alone and in complex with bacterial effector VopQPreprint
Peng, W., Fernandez, J., Casey, A. K., Kinch, L. N., Tomchick, D. R., & Orth, K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.16.207225
Insights into the biogenesis of the human mitochondrial ribosomal large subunit – Characterisation of mL44 and mL45
Hanitsch, E. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8315
Enzymatic and structural insights into the mycobacterial alkylhydroperoxide reductase subunit C and repurposing of an antimalaria compound inhibiting the mycobacterial cytochrome BCC oxidase for tuberculosis disease
Chong, S. S. M. (2020) · doi:10.32657/10356/143914
Organelle Genomics: The Chloroplast Genome of Amaranth
Ramaraj, T., & Ponniah, S. K. (2021) · Compendium of plant genomes · doi:10.1007/978-3-030-72365-1_2
Expression of the cyanobacterial F 0 F 1 ATP synthase inhibitor AtpΘ depends on small basic DNA-binding proteins and differential mRNA stabilityPreprint
Song, K., Hagemann, M., Georg, J., Maaß, S., Becher, D., & Hess, W. R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.11.17.468837
Development of an experimental and computational platform for enhanced characterization of modified peptides and proteins in environmental proteomics
Sharma, R. (2014)
ATP合酶旋转催化的一种新机制
刘, 佳., 昌, 增., & 付, 新. (2016) · Scientia Sinica Vitae · doi:10.1360/05scls-2015-0312
References
(2013) · Elsevier eBooks · doi:10.1016/b978-0-12-388425-1.00023-3
Faculty Opinions recommendation of F1F0-ATP Synthase Inhibitory Factor 1 in the Normal Pancreas and in Pancreatic Ductal Adenocarcinoma: Effects on Bioenergetics, Invasion and Proliferation.
Curci, S., & Colella, M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733703416.793549717
Effects of a two-year health-enhancing physical activity program on skeletal muscle protein profiles in people with rheumatoid arthritisPreprint
Ossipova, E., Idborg, H., Fridén, C., Jakobsson, P., Kosek, E., Malm, C., Nordgren, B., Opava, C. H., Tegner, Y., Vanluyten, J., et al. (2020) · Research Square · doi:10.21203/rs.3.rs-46096/v1
Assembly, super-assembly and impared assembly of the mitochondrial electron trasport chain: in situ validation of the plasticity model
Martín-García, E. (2018) · doi:10.4321/repisalud.6486
Mitochondrial Electron Transport
Prochaska, L. J., Pokalsky, C. N., Alnajjar, K. S., & Cvetkov, T. L. (2018) · Springer eBooks · doi:10.1007/978-3-642-35943-9_25-1
Faculty Opinions recommendation of Three-Dimensional Analysis of Mitochondrial Crista Ultrastructure in a Patient with Leigh Syndrome by In Situ Cryoelectron Tomography.
Carazo, J. M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733717981.793549192
ATP Proton Pumps. Function and Regulation
Cortassa, S. C., Aon, M. A., Juhaszova, M., & Sollott, S. J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00201-7
A 3-Dimensional Hypothesis of Oxidative Phosphorylation
Knight, V. A. (2023) · Vascular Cell · doi:10.24238/13221-14-1-215
Proteomic Analysis of Urine from Youths Indulging in GamingPreprint
Yang, M., Liu, Y., Shen, Z., Wang, H., & Gao, Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.26.581984
The Origin of Cells
Lynch, M. (2024) · Oxford University Press eBooks · doi:10.1093/oso/9780192847287.003.0002
Stepwise Dissipative Control of Multimodal Motion in a Silver(I) Catenate
Elramadi, E., Kundu, S., Mondal, D., Paululat, T., & Schmittel, M. (2024) · Angewandte Chemie · doi:10.1002/ange.202404444
Additional file 2 of A quantitative proteomics analysis for small molecule Stemazole’s effect on human neural stem cells
Li, H., Zhang, Y., Zhang, J., Zhao, C., Zhu, Y., & Han, M. (2020) · Figshare · doi:10.6084/m9.figshare.13357649
Additional file 3 of A quantitative proteomics analysis for small molecule Stemazole’s effect on human neural stem cells
Li, H., Zhang, Y., Zhang, J., Zhao, C., Zhu, Y., & Han, M. (2020) · Figshare · doi:10.6084/m9.figshare.13357652
ATP synthase of E. coli: F1-ATPase activity is functionally decoupled from the proton-transporting complex (FO) by tributyltin
Milgrom, Y. M., & Duncan, T. M. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150705
A very versatile molecular machine
Manson, M. D. (2024) · Journal of Bacteriology · doi:10.1128/jb.00351-24
Fundamental Physiological Processes in Cyanobacteria
Waditee‐Sirisattha, R., & Kageyama, H. (2025) · Microorganisms for sustainability · doi:10.1007/978-981-96-5330-0_2
Liquid Intelligence: A Public Framework for Structured Water, Energy Coherence, and Biological ResiliencePreprint
Decker, M., & Decker, N. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5254823
A Salmonella type I toxin promotes systemic infection by inhibiting F o F 1 ATP synthasePreprint
Kim, S., Kim, S., & Lee, E. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.26.656083
Effect of Ionic Strength on Chloroplast ATP Synthase
Minaeva, A. V., Osipov, S. D., & Vlasov, A. V. (2025) · Biochemistry (Moscow) Supplement Series A Membrane and Cell Biology · doi:10.1134/s199074782570014x
A single-cell atlas inclusive of age-related menopause reveals global tissue and ovarian remodelingPreprint
VanBenschoten, H. M., Nugmanova, Z., Olmsted, A. M., Huang, R., Annepureddy, L. D., Gingerich, I. K., Kratka, C. E., Duncan, F. E., Kholod, O., & Goods, B. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.20.660779
Proton Channels in the Context of Human Diseases
Sagsoz, M. E. (2025) · Recent trends in pharmacology. · doi:10.62425/rtpharma.1771654
Synergistic inactivation of Aspergillus niger spores by low-dose ClO2 and photocatalysis via interfacial electron transfer
Wang, J., Cao, R., Niu, J., Huang, D., Zhang, W., & Li, Y. (2025) · Water Research · doi:10.1016/j.watres.2025.125132
Mitochondrial genome assembly and analysis of Cercis chinensis: insights into an economically valuable ornamental species
Wang, M., Yang, R., Wang, M., Li, J., & Huang, C. (2025) · BMC Plant Biology · doi:10.1186/s12870-025-07904-w
Additional file 1 of A quantitative proteomics analysis for small molecule Stemazole’s effect on human neural stem cells
Li, H., Zhang, Y., Zhang, J., Zhao, C., Zhu, Y., & Han, M. (2020) · Figshare · doi:10.6084/m9.figshare.13357646
Additional file 1 of An HSP90 cochaperone Ids2 maintains the stability of mitochondrial DNA and ATP synthase
Jiang, P.-H., Hou, C.-Y., & Teng, S.-C. (2021) · Figshare · doi:10.6084/m9.figshare.16994438
Additional file 4 of A quantitative proteomics analysis for small molecule Stemazole’s effect on human neural stem cells
Li, H., Zhang, Y., Zhang, J., Zhao, C., Zhu, Y., & Han, M. (2020) · Figshare · doi:10.6084/m9.figshare.13357655
Additional file 5 of An HSP90 cochaperone Ids2 maintains the stability of mitochondrial DNA and ATP synthase
Jiang, P.-H., Hou, C.-Y., & Teng, S.-C. (2021) · Figshare · doi:10.6084/m9.figshare.16994450
Catabolism
Achal, V. (2025) · Springer eBooks · doi:10.1007/978-981-95-1610-0_4
Spin-dependent magnetosensitivity of enzymatic synthesis of adenosine triphosphate in strong magnetic fields
Berdinskiy, V. L., & Shevchenko, U. G. (2025) · Russian Chemical Bulletin · doi:10.1007/s11172-025-4759-3
Mitochondrial Reticulum in Skeletal Muscles: Proven and Hypothetical Functions
Bakeeva, L. E., Vays, V. B., Vangeli, I. M., Eldarov, C. M., Popkov, V. A., Zorova, L. D., Zorov, S. D., & Zorov, D. B. (2025) · Biochemistry (Moscow) · doi:10.1134/s000629792560190x
Single-molecule Observation and Torque Measurement of Rotary Molecular Motor Using Optically Asymmetric Janus Nanoparticle
Otomo, A., & Iino, R. (2025) · Seibutsu Butsuri · doi:10.2142/biophys.65.322
Cell Painting reveals polypharmacological activity on the V-ATPase by the F-ATPase inhibitor Cyhexatin
Hecker, F. A., Grohs, M., Koenig, T., Niehaus, K., Gnutt, D., & Geibel, S. (2026) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2026.106978
Arenobufagin suppresses lung cancer cell growth by disrupting mitochondrial function and inducing relocalization of ATP synthase
Yan, Y., Zhou, X., Gu, M., Ding, Y., Zhao, X., Zhou, Z., & Ke, J. (2026) · Toxicon · doi:10.1016/j.toxicon.2026.109067
Respiration in Terrestrial Organisms
Amthor, J. S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-21964-1.00196-8
Reversal of ATP synthase is a key attribute accompanying cellular differentiation of Trypanosoma brucei insect forms
Kunzová, M., Doleželová, E., Moos, M., Panicucci, B., & Zı́ková, A. (2026) · Communications Biology · doi:10.1038/s42003-026-09933-z
Variabilité glycémique : exploration in vitro des fonctions cellulaires et mitochondriales sur la lignée de cardiomyocyte HL-1
Mordel, P. (2017) · theses.fr (ABES) · doi:10.70675/bf54e0a3z7d52z4a54zbc78ze2ef44479be7
Utilisation du modèle levure pour la recherche de voies thérapeutiques contre le syndrome de Barth
de Tilques, M. D. T. (2017) · theses.fr (ABES) · doi:10.70675/db54cf9cz39cdz47d7z9aabz808ab0c7b1c7
Recherche et études de marqueurs précoces permettant de déterminer l'état de fraicheur de filets de poissons
Cléach, J. (2018) · theses.fr (ABES) · doi:10.70675/498c30b7z90a8z42f0za685zba48bfefb8d7
PGC-1α régule un programme onco-métabolique capable de réprimer l’agressivité du cancer de la prostate
Kaminski, L. (2018) · theses.fr (ABES) · doi:10.70675/7f6ae88bz4f3cz49d3zafcdz8682254b2be3
Mitochondrial metabolic remodeling in the progression of dilated cardiomyopathy
Vargas, L. (2021) · theses.fr (ABES) · doi:10.70675/2b0e60a0z336az4b99za7bazf7f8f4fb9d74
Structural and functional studies of acyl carrier protein post-translational moifications in mycobacterial type I polyketide synthases
Nguyen, M. C. (2019) · theses.fr (ABES) · doi:10.70675/23ca750fzfd75z4bb2z8801z42c9db0270af
Bases métaboliques du développement neuronal : rôles de la kinase NUAK1 dans la régulation des mitochondries axonales
Lanfranchi, M. (2021) · theses.fr (ABES) · doi:10.70675/247335b1zba7fz4005zafbdzdc43c088d75f
Macrophages respiratory supercomplexes and metabolic reprogramming upon anti-bacterial immunity
Tioli, G. (2021) · theses.fr (ABES) · doi:10.70675/e73a8229zb994z494dz981dz835d152203d8
Syndrome de Barth et recherche de voies thérapeutiques
Almyre, C. (2024) · theses.fr (ABES) · doi:10.70675/6de95820z84d7z467ez9477zb31adc2ae471
APOBEC3, cytidine deaminases at the crossroads of cellular stress, viral editing and tumorigenesis
Raymond, K. A. (2024) · theses.fr (ABES) · doi:10.70675/c5baf2e0zc96dz4512zbe80zf87de14d5dbd
The Caenorhabditis elegans mitochondrial electron transport chain: its role in adaptation, longevity, and biotechnology
Cruz, E. Y. H., & Uribe‐Carvajal, S. (2026) · Experimental Cell Research · doi:10.1016/j.yexcr.2026.115026
Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro
Walus, M., Kida, E., & Golabek, A. A. (2026) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2026.110130
Plastic leachates drive conjugative transfer of antibiotic resistance genes
Chen, Y., Yu, K., Sun, Y., Yan, Y., Yin, G., Wang, J., Li, X., Tang, S., Pronyk, P., & Xia, Y. (2026) · Environmental Science and Ecotechnology · doi:10.1016/j.ese.2026.100705
Comparative analysis of mitochondrial genome of Gaultheria (Ericaceae) provides insights into their adaptation to high elevation
Zhao, J., Lin, Y.-J., Yu, Y., & Lu, L. (2026) · BMC Plant Biology · doi:10.1186/s12870-026-08757-7
Imaging mitochondrial electric flickers in intact cells with a membrane-anchored indicator
Ren, W., Zhang, L., Li, L., Li, M., Wang, Z., Zhou, F., Lin, Z., Chen, Z., Wang, X., Xi, P., et al. (2026) · PhotoniX · doi:10.1186/s43074-026-00245-3
The role of metabolic reprogramming in oocyte development: research progress and prospects
Li, Y., Liu, Y., & Jin, J. (2026) · Frontiers in Reproductive Health · doi:10.3389/frph.2026.1803167
OPA1 Requires ATP Synthase Activity and Oligomerization to Mitigate Prion-Induced Mitochondrial Dysfunction, Oxidative Stress, and Neuronal Apoptosis
Wu, W., Zhang, X., Jiang, M., Zhao, D., Yang, L., & Ma, N. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05960-3
Mitochondrial dysfunction in muscle cells induced by snoring vibrations
Stål, P., El‐Habta, R., Qian, Y.-C., Zhu, S., Williams, C., Mateus, A., Gilthorpe, J. D., & Shah, F. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102174
Arbuscular mycorrhiza provides postanthesis benefits to maximize wheat grain yield and nitrogen concentration
Zhou, J., Huang, B., Yang, R., Berckx, F., Gui, H., Fransson, P. M. A., Rillig, M. C., Reynolds, M. P., Xie, J., Razavi, B. S., et al. (2026) · New Phytologist · doi:10.1111/nph.71353
CIRBP maintains skeletal muscle mitochondrial energy homeostasis via mt-ATP6 to ameliorate sarcopenia
Wang, Z., Guo, Y., Hu, Z., Zhang, H., & Liu, Q. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154183
Experimental and computational insights into mitochondrial permeability transition and pro-apoptotic signaling induced by the methanol fraction of Daniellia oliveri leaves in male Wistar rats
Achem, J., Ogunyemi, O. M., Banwo, O. G., Onyiba, C. I., Bolarin, O. L., Olanlokun, J. O., & Olorunsogo, O. O. (2025) · Egyptian Journal of Basic and Applied Sciences · doi:10.1080/2314808x.2026.2696700
High‐throughput mutational analysis of F 1 ‐ ATPase by integrated cell‐free protein synthesis and single‐molecule rotation assay
Taguchi, M., Oya, T., Ueno, H., & Noji, H. (2026) · Protein Science · doi:10.1002/pro.70699
Biological characteristics of ATP5A1 and its pathogenic mechanisms in human diseases: advances in clinical translation
Shu-yin, Y., Deng, Q., Gao, H.-J., Liu, H.-D., Tang, H., Wang, Q., Liu, Y.-M., & Yan, Q.-B. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1862366
Mitochondrial Complex V Dysfunction in Neurodegeneration: Secondary Bystander or Primary Driver?
Harris, K. E., Lascaratos, G., & Chau, K. (2026) · Brain Sciences · doi:10.3390/brainsci16080890
Functional discrepancy between F-type and A-type rotary ion-translocating ATPases in acid tolerance of Streptococcus anginosus
Sekiya, M., Ishikawa, T., Oyake, M., Shimoyama, Y., Sasaki, M., & Nakanishi‐Matsui, M. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110983
Tissue-wide metabolic buffering confers resilience to mitochondrial dysfunctionPreprint
Petridi, S., Dhawanjewar, A. S., Dubal, D., Chandrasegaram, R., Dickmänken, H., Bala-Muraly, N., Wilson, B. A., Eve, T., Marzullo, B. P., Hynes-Allen, A. M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.08.27.747448
Proteome-wide crosslinking mass spectrometry reveals novel components of essential complexes in ToxoplasmaPreprint
Butterworth, S., Gin, A. L., Shikha, S., Tengganu, I. F., Rush, J., Duraisingh, T., Sodeinde, V., Lemgruber, L., Schulte, F., Hu, K., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.01.748362
ATP synthase subunits e and g are essential for Ca2+ homeostasis and development in Drosophila melanogaster independent of oxidative phosphorylation
Frigo, E., Santalla, M., Brischigliaro, M., Nata, F. B., Tommasin, L., Rossini, M., Komarov, D., Ferro, S., Pendin, D., Marin, O., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01869-5
The lower γ region supports forward rotation in the latter half of the 80° substep of F 1 ‐ ATPase
Uchiyama, T., Ueno, H., Sobti, M., Furlong, E., Brown, S. H. J., Stewart, A. G., & Noji, H. (2026) · Protein Science · doi:10.1002/pro.70803

Authors: Walker, J. E.
Affiliations: MRC Mitochondrial Biology Unit (GB)
Corresponding author: Walker, John E.
ORCID: Walker, John E.
Venue: Biochemical Society Transactions
Publisher: Portland Press Ltd.
Published: 2013-01-29
Volume: 41
Issue: 1
Pages: 1-16
ISSN: 0300-5127 (ISSN-L)
1470-8752
DOI: 10.1042/bst20110773
OpenAlex: W2104675030
Cited by: 614
References: 123
Citations by year: 2026: 39 · 2025: 44 · 2024: 48 · 2023: 39 · 2022: 47 · 2021: 56 · 2020: 61 · 2019: 46 · 2018: 52 · 2017: 42 · 2016: 42 · 2015: 54 · 2014: 30 · 2013: 13
FWCI: 4.36
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Society Transactions (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords: ATP synthase, proton motive force, rotary mechanism, ATP production, enzyme regulation, mitochondrial ATP synthase, chloroplast ATP synthase, bacterial ATP synthase, supramolecular complexes
MeSH terms: Hydrolysis, Models, Molecular, Protein Conformation, ATP Synthetase Complexes, Uncertainty

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks