The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Open accessAbstract
Mitochondria are double-membraned organelles with variable shapes influenced by metabolic conditions, developmental stage, and environmental stimuli. Their dynamic morphology is a result of regulated and balanced fusion and fission processes. Fusion is crucial for the health and physiological functions of mitochondria, including complementation of damaged mitochondrial DNAs and the maintenance of membrane potential. Mitofusins are dynamin-related GTPases that are essential for mitochondrial fusion. They are embedded in the mitochondrial outer membrane and thought to fuse adjacent mitochondria via combined oligomerization and GTP hydrolysis. However, the molecular mechanisms of this process remain unknown. Here we present crystal structures of engineered human MFN1 containing the GTPase domain and a helical domain during different stages of GTP hydrolysis. The helical domain is composed of elements from widely dispersed sequence regions of MFN1 and resembles the 'neck' of the bacterial dynamin-like protein. The structures reveal unique features of its catalytic machinery and explain how GTP binding induces conformational changes to promote GTPase domain dimerization in the transition state. Disruption of GTPase domain dimerization abolishes the fusogenic activity of MFN1. Moreover, a conserved aspartate residue trigger was found to affect mitochondrial elongation in MFN1, probably through a GTP-loading-dependent domain rearrangement. Thus, we propose a mechanistic model for MFN1-mediated mitochondrial tethering, and our results shed light on the molecular basis of mitochondrial fusion and mitofusin-related human neuromuscular disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“GTP hydrolysis of MFN1 causes a conformational change that allows the OMMs of opposing mitochondria to contact and fuse [61, 62].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [62]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Sheldrick, G. M. (2007) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 88,113
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 320
Mitochondrial dynamics in vascular remodeling and target-organ damage
Zhu, T., Hu, Q., Yuan, Y., Yao, H., Zhang, J., & Qi, J. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1067732 · Cited by 12
Plasticity in salt bridge allows fusion-competent ubiquitylation of mitofusins and Cdc48 recognition
Anton, V., Buntenbroich, I., Schuster, R., Gaedke, F., Simões, T., Altin, S., Calabrese, G., Riemer, J., Schauss, A. C., & Escobar‐Henriques, M. (2019) · Life Science Alliance · doi:10.26508/lsa.201900491 · Cited by 13
Premature senescence and cardiovascular disease following cancer treatments: mechanistic insights
Jain, A., Casanova, D., Padilla, A. V., Paniagua-Bojorges, A., Kotla, S., Ko, K. A., Samanthapudi, V. S. K., Chau, K. M., Nguyen, M. T., Wen, J. J., et al. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1212174 · Cited by 11
Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles
Peñalva, D. A., Monnappa, A. K., Natale, P., & López‐Montero, I. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313609121 · Cited by 11
Mitofusin2 expression is associated with podocyte injury in IgA nephropathy
Tang, X.-L., Yuan, Y., Liang, X., & Jiang, X. (2023) · European journal of medical research · doi:10.1186/s40001-023-01107-5 · Cited by 11
Zeng, S., Zhou, X., Lin, F., Wu, P., Liu, Y., Ma, Y.-B., Jin, X., Ren, H., Jiang, J., Li, H., et al. (2025) · Aquaculture · doi:10.1016/j.aquaculture.2025.742489 · Cited by 10
Pei, W., Dai, L., Li, M., Cao, S., Xiao, Y., Yang, Y., Ma, M., Deng, M., Mo, Y., & Liu, M. (2025) · Biomolecules · doi:10.3390/biom15070970 · Cited by 10
Hepatic ischemia-reperfusion and mitochondrial quality control: potential therapeutic targets
Wang, J., Fu, W., Lü, N., Guo, Z., Ong, S., Shi, H., Zhou, H., Chang, X., & Miao, M. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115267 · Cited by 11
Rapid and quantitative in vitro analysis of mitochondrial fusion and its interplay with apoptosis
Xu, J., Su, L., Han, J., Gao, K., Zhang, M., Wang, S., Chen, C., & Yan, X. (2020) · Talanta · doi:10.1016/j.talanta.2020.121523 · Cited by 10
Mitophagy: A Potential Target for Pressure Overload‐Induced Cardiac Remodelling
Shao, R., Li, J., Qu, T., Liao, Y., & Chen, M. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2849985 · Cited by 11
Sloat, S. R., & Hoppins, S. C. (2022) · Life Science Alliance · doi:10.26508/lsa.202101305 · Cited by 10
Targeting protein interaction networks in mitochondrial dynamics for cancer therapy
Yin, C.-F., Chang, Y., Huang, H., & Juan, H. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.11.006 · Cited by 10
Disrupted Mitochondrial Dynamics Impair Corneal Epithelial Healing in Neurotrophic Keratopathy
Jin, M., Liu, Z., Shi, R., Deng, Y., Lin, J., Zhang, Y., Lin, L., Wang, Y., Shi, Y., Li, C., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031290 · Cited by 9
Zerihun, M., Rubin, S. J. S., Silnitsky, S., & Qvit, N. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417504 · Cited by 9
Li, Y., Yu, X., Xiao, T., Chi, H.-L., Zhu, G., & Kang, Y. (2021) · Cardiovascular Toxicology · doi:10.1007/s12012-021-09641-6 · Cited by 9
Self-citationKelly, C. M., Zeiger, P. J., Narayanan, V., Ramsey, K. M., & Sondermann, H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101438 · Cited by 9
Lv, Y., Chen, L., Li, L., Liao, Z., Fang, Z., Cheng, L., & Peng, F. (2025) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2025.1535401 · Cited by 9
Tolosa-Díaz, A., Almendro‐Vedia, V. G., Natale, P., & López‐Montero, I. (2020) · Biomolecules · doi:10.3390/biom10071085 · Cited by 8
Vlieghe, A., Niort, K., Fumat, H., Guigner, J., Cohen, M. M., & Tareste, D. C. (2023) · Biomolecules · doi:10.3390/biom13091341 · Cited by 8
Yuan, Y., Wu, Y., He, M., & Jiang, X. (2024) · Current Molecular Medicine · doi:10.2174/0115665240310818240531080353 · Cited by 7
Mechanisms of mitochondrial reorganization
Maruyama, T., Hama, Y., & Noda, N. N. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad098 · Cited by 7
Chen, Q., Wang, Y., Jiao, F., Shi, C., Pei, M., Wang, L., & Gong, Z. (2020) · PubMed · doi:10.14670/hh-18-237 · Cited by 7
Hegde, M., Daimary, U. D., Jose, S., Sajeev, A., Chinnathambi, A., Alharbi, S. A., Shakibaei, M., & Kunnumakkara, A. B. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.866473 · Cited by 7
Guo, Z., Wang, Z., Gao, Z., Feng, T., Gao, Y., Yin, Z., Tian, Z., Liu, Y., Mao, X., & Xiang, C. (2023) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-023-09959-6 · Cited by 7
Direct Small Molecule Activation of MitofusinsPreprint
Zacharioudakis, E., Biris, N., Garner, T. P., Chen, Y., Pekson, R., Dhingra, R., Santulli, G., Kirshenbaum, L. A., Kitsis, R. N., & Gavathiotis, E. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/301713 · Cited by 7
Self-citationMitochondrial function maintenance and mitochondrial training in ageing and related diseases
Gao, G., Xie, Z., & Huang, H. (2025) · Journal of Holistic Integrative Pharmacy · doi:10.1016/j.jhip.2025.04.001 · Cited by 6
Wang, D., Lv, Y., Xie, F., Zhao, Y., Ren, B., Jin, S., Zhu, N., Qin, M., Lin, Z., Wang, L., et al. (2026) · Biomaterials · doi:10.1016/j.biomaterials.2026.123985 · Cited by 6
The multifaceted effects of mitochondria in kidney diseases
Xue, J.-L., Ji, J., Zhou, Y., Zhang, Y., Liu, B., Ma, R., & Li, Z. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101957 · Cited by 6
ER-mitochondria tethering and its signaling: A novel therapeutic target in breast cancer
Paidi, C., Nuthalapati, Y., Samudrala, A. S., Bhamidipati, P., Mangam, C., Welch, D. R., Nagaraju, G. P., & Malla, R. R. (2025) · Molecular Therapy Oncology · doi:10.1016/j.omton.2025.200995 · Cited by 6
Mitochondrial dynamics in yeast with repressed adenine nucleotide translocator AAC2
Galkina, K. V., Zyrina, A. N., Golyshev, S. A., Kashko, N. D., Маркова, О. В., Соколов, С. С., Severin, F. F., & Кнорре, Д. А. (2020) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2020.151071 · Cited by 6
From dynamin related proteins structures and oligomers to membrane fusion mediated by mitofusins
Ozeir, M., & Cohen, M. M. (2022) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2022.148913 · Cited by 7
Ruan, X.-H., Ma, T., & Fan, Y. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.05.084 · Cited by 6
Identification and characterization of signal peptide of Mitofusin1 (Mfn1)
Sinha, S., & Aradhyam, G. K. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.12.165 · Cited by 6
Brandner, A. F., Vecchis, D. D., Baaden, M., Cohen, M. M., & Taly, A. (2019) · Data in Brief · doi:10.1016/j.dib.2019.104460 · Cited by 6
SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features
Gewehr, L., Junglas, B., Jilly, R., Franz, J., Zhu, W. E., Weidner, T., Bonn, M., Sachse, C., & Schneider, D. (2023) · Nature Communications · doi:10.1038/s41467-023-37746-9 · Cited by 6
Liu, Y., Chen, Y., Cao, B., Kong, D., Li, J., Li, W., Guo, Y., Yuan, Z., Gao, Y., Zhang, Y., et al. (2024) · Biophysics Reports · doi:10.52601/bpr.2024.240037 · Cited by 5
Self-citationA Molecular Chemical Perspective: Mitochondrial Dynamics Is Not a Bystander of Cartilage Diseases
Wu, J., Zhou, X., Xu, X., & Xie, J. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00706 · Cited by 7
A special latch in yeast mitofusin guarantees mitochondrial fusion by stabilizing self-assembly
Huang, S., Ma, D., Yu, C., Li, J., Tu, X., Huang, Z., Qi, Y., Ou, J.-Y., Feng, J.-X., Yu, B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-64646-x · Cited by 5
Self-citationZhang, Y., Ma, L., Wang, Z., Gao, C., Yang, L., Li, M., Tang, X., Yuan, H., Pang, D., & Ouyang, H. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.134673 · Cited by 5
Iqbal, A., Waseem, H. B., Ali, F., Baammi, S., Faheem, H., Shazly, G. A., Nafidi, H., Sajid, M., Khan, M. S., Akram, H. N., et al. (2024) · Journal of the Indian Chemical Society · doi:10.1016/j.jics.2024.101403 · Cited by 5
Mitochondrial dynamics, biogenesis, mitophagy and oxidative stress in gestational obesity: A review
Rodríguez-Córdoba, K. M., Agreda-Soto, S., Garzón, J. A. C., & Pustovrh, M. C. (2024) · Endocrine and Metabolic Science · doi:10.1016/j.endmts.2024.100205 · Cited by 7
Mitochondrial fusion protein: a new therapeutic target for lung injury diseases
Jia, G., Song, E., Huang, Q., Chen, M., & Liu, G. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1500247 · Cited by 5
Barsa, C., Perrin, J., David, C., Mourier, A., & Rojo, M. (2025) · Scientific Reports · doi:10.1038/s41598-025-93702-1 · Cited by 5
Anisotropic Micro/Nanotopography Regulating Mitochondrial Dynamics in Cardiomyocytes
Liu, Y., Yi, B., Yang, L., Yang, Y., Li, T., Li, X., Cho, J. Y., Zhang, D., Zhou, Q., & Yu, T. (2025) · Research · doi:10.34133/research.0891 · Cited by 5
Membrane fusion by Drosophila atlastin does not require GTP hydrolysis
Crosby, D., & Lee, T. H. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-05-0164 · Cited by 5
Common Energetic and Mechanical Features of Membrane Fusion and Fission Machineries
Tareste, D. C., & Roux, A. (2018) · Springer eBooks · doi:10.1007/978-3-030-00630-3_16 · Cited by 6
Kron, N. S., & Fieber, L. A. (2021) · PLoS ONE · doi:10.1371/journal.pone.0252647 · Cited by 5
Organelle-specific regulation of ferroptosis
Zhang, Y., Liu, M., Li, M., Wu, Y., Xie, M., Liu, X., Lu, H., Zhai, X., & Yang, Y. (2026) · Biology Direct · doi:10.1186/s13062-025-00717-9 · Cited by 4
Hu, M., Guan, S., Fu, X., Wang, K., Gu, B., Liu, X., Liu, X., Yan, Z., Chen, Z., & Liu, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147710 · Cited by 4
Fan, H., Zhao, H., Zhang, P., Yu, P., Ji, Y., Chen, G., Jin, H., Liu, Y., Liu, J., Chen, Z., et al. (2026) · Advanced Science · doi:10.1002/advs.202511406 · Cited by 4
Self-citationMIRO1-mediated mitochondrial fusion is required for stomatal immunity in Arabidopsis
Lu, P., Liu, J., Yu, H., & Li, J. X. (2026) · Nature Plants · doi:10.1038/s41477-026-02224-9 · Cited by 4
Regulation of mitochondrial function during spermatogenesis and sperm maturation
Meng, K., Zhu, Z., Jia, H., Feng, Y., Feng, J., Shen, Y., Jiang, W., Liu, C., Qin, Q., Gao, F., et al. (2026) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-026-00944-6 · Cited by 4
Self-citationExtracellular matrix signals promote actin-dependent mitochondrial elongation and activity
Gatti, P., Mukherjee, P., Talukdar, P. D., Freppel, W., Kasmaie, A., Kanou, J., Chatel‐Chaix, L., Chatterji, U., & Germain, M. (2026) · iScience · doi:10.1016/j.isci.2026.115171 · Cited by 5
You, Y., Wang, X., Li, S., Zhao, X., & Zhang, X. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6513 · Cited by 4
Lys716 in the transmembrane domain of yeast mitofusin Fzo1 modulates anchoring and fusion
Versini, R., Baaden, M., Cavellini, L., Cohen, M. M., Taly, A., & Fuchs, P. F. J. (2024) · Structure · doi:10.1016/j.str.2024.08.017 · Cited by 4
Li, C.-Y., Ding, D., Guo, Y., Fu, Y., Shen, Y., Fu, J., Zhang, C.-X., & Han, F. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06840-5 · Cited by 3
Yang, L., Cui, H., & Yang, L. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.07.043 · Cited by 3
Wu, X., Liu, L., Zhao, R., & Chen, W. (2025) · Immunologic Research · doi:10.1007/s12026-025-09695-6 · Cited by 3
Mitochondrial Homeostasis in Diabetic Cardiomyopathy: From Dysfunction to Therapeutic Strategies
Huang, Y., Zou, W., Jiang, X., Cheng, J., & Zheng, J. (2026) · Antioxidants · doi:10.3390/antiox15030399 · Cited by 4
Targeting mitochondrial dynamics against cancer
Cao, Y., Yang, C.-P., Shen, B., Hu, J., & Gao, S. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.03.006 · Cited by 3
Self-citationPI(3)P regulates mitochondrial dynamics through FGD-dependent actin organization
Zhao, S., Zhang, J., Ma, T., Li, J., Duan, M., Wang, X., Li, M., & Yang, C. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202508040 · Cited by 3
Yan, X., Tian, D., Peng, R., Chen, L., He, Q., Zhou, Q., & Li, Q. (2022) · Tissue and Cell · doi:10.1016/j.tice.2022.101749 · Cited by 3
Buntenbroich, I., Anton, V., Pérez-Hernández, D., Simões, T., Gaedke, F., Schauss, A. C., Dittmar, G. A. G., Riemer, J., & Escobar‐Henriques, M. (2023) · iScience · doi:10.1016/j.isci.2023.107014 · Cited by 3
Niu, M.-M., Guo, H.-X., Li, Y., Chen, S., & Xiang-chen, M. (2025) · Food Bioscience · doi:10.1016/j.fbio.2025.106729 · Cited by 2
Self-citationPeiji, W., Wu, Z., Song, Z., Deng, X., Zhang, Y., & Gong, X. (2026) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2026.1778855 · Cited by 2
Shi, X., Zhang, C., Long, Y., Chen, J., 任丽华, & Shi, R. (2026) · Cancer Letters · doi:10.1016/j.canlet.2026.218309 · Cited by 2
Time-resolved tmFRET reveals GTP-coupled conformational changes in Mfn1
Hurwitz, S. M., Zagotta, W. N., Gordon, S. E., & Hoppins, S. C. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202511077 · Cited by 2
Disease-causing MFN2 mutants impair mitochondrial fission dynamics by distinct DRP1 dysregulation
Lagos, D., Santiago, P., Pérez-Bravo, N., Cartes-Saavedra, B., Vial-Brizzi, J., Troncoso-Chandía, D., Podmanicky, O., Horváth, R., & Eisner, V. (2026) · Cell Death and Disease · doi:10.1038/s41419-026-08838-3 · Cited by 2
Cool views of membrane remodeling
Kehr, A. D., & Hinshaw, J. E. (2018) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2018.02.004 · Cited by 2
Nucleotide-Dependent Dimerization and Conformational Switching of Atlastin
O’Donnell, J. P., Kelly, C. M., & Sondermann, H. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0676-6_8 · Cited by 2
Determination of Mitochondrial Morphology in Live Cells Using Confocal Microscopy
Lin, M., Wang, J., Xian, Z., Zeng, C., & Xu, J. (2025) · Journal of Visualized Experiments · doi:10.3791/68167 · Cited by 1
Liu, H., Li, Y., Qiu, J., Zhang, J., Lai, H., & Zhang, X. (2025) · Canadian Journal of Urology · doi:10.32604/cju.2025.066523 · Cited by 1
Self-citationSENP1: A perspective from immune cells to disease (Review)
Feng, X., Wu, G., & Zeng, Q. (2025) · Oncology Reports · doi:10.3892/or.2025.8947 · Cited by 1
Zhang, H., Li, J., Wang, Y., Li, Q., Song, L., & Li, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147738 · Cited by 1
Zeng, X., Zhou, X., Jiang, W., Wu, P., Zhang, H., Ma, Y.-B., Liu, Y., Jin, X., Ren, H., Zhang, L., et al. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c12483 · Cited by 1
Neuronal mitochondrial dynamics: roles in brain disorders and therapeutic potential
Zhang, X., Du, J., Wang, S.-Z., Mo, X., & Zhang, X. (2026) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01746-w · Cited by 3
Mitochondrial dynamics and cancer: mechanisms and targeted therapy
Wang, A., Ye, X., Zhao, Y., & Zhang, C. (2026) · Cell Biology and Toxicology · doi:10.1007/s10565-026-10174-3 · Cited by 1
An, W., Reyes, C., Espinosa‐Díez, C., Patel, P., Guimaraes, D., Villareal, F., Jessup, M., Croix, C. S., Gomez, D. A., Rao, K., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104169 · Cited by 1
Chen, R., Huang, J., Wang, Y., Yao, S., Wu, F., Liu, J., Song, C., Lin, L., Lin, X., Deng, Y. F., et al. (2026) · Advanced Science · doi:10.1002/advs.76243 · Cited by 1
Mitochondrial Dysfunction Signature in Diabetic Vascular Endothelium
Popov, L. (2018) · Journal of Clinical & Experimental Pathology · doi:10.4172/2161-0681.1000334 · Cited by 1
Ford, M. G. J., & Ramachandran, R. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2209-4_18 · Cited by 1
Fusion activators enhance mitochondrial function
Rosencrans, W. M., & Chan, D. C. (2023) · Mitochondrial Communications · doi:10.1016/j.mitoco.2023.03.001 · Cited by 1
Self-citationMembrane remodeling by the Bacterial Dynamin-like Protein (BDLP) from Nostoc punctiformePreprint
Singh, K., & Pucadyil, T. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.27.656310 · Cited by 1
Versini, R., Baaden, M., Bonvin, A. M. J. J., Fuchs, P., & Taly, A. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.10.717648 · Cited by 1
Sinha, S., & Aradhyam, G. K. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/495721
Bernez, S. (2021)
Caracterização funcional e da dinâmica espacial da miosina-Va no processo de fissão mitocondrial
Araujo, J. S. (2021) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2021.tde-11062021-090108
Impaired mitochondrial dynamics in disease
Bagshaw, O. R. M., Balardo, C. J., Bland, N. A., Pardiwalla, N., Samuel, I. A. J., Zoso, S. L. S., & Stuart, J. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85666-9.00011-5
Yan, L., Peng, X., Li, T., Liu, L., & Yang, G. (2020) · doi:10.21203/rs.2.23868/v1
Identification of Mfn2-S249 as a Phosphoregulatory Switch of Mitochondrial Fusion DynamicsPreprint
Kumar, S., Ramonett, A., Ahmed, T., Kwak, E., Flores, P. C., Ortiz, H. R., Langlais, P. R., Mythreye, K., & Lee, N. Y. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.11.475884
Mechanisms of regulation of mitochondria-endoplasmic reticulum contact sites
Couto, R. (2019) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-7742
Mao, X., Liu, X., Fu, P., & Xiang, C. (2020) · doi:10.21203/rs.3.rs-31482/v1
Gomes, G. B. (2020) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/d.42.2020.tde-13012022-181211
Plasticidade mitocondrial na doença de Chagas
Ribeiro, M. A. C. (2022) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.42.2022.tde-21082023-154733
VARUK, O. O., Ruiz, A., Orengo, C., Cozzolino, A., de Boissier, P., Aouane, A., & Rival, T. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.14.642792
Structural and functional characterization of the brain-specific dynamin superfamily member RNF112
Zhong, Y.-T., Huang, L., Li, K., Yang, B., Ye, X., Zhong, H.-R., Yu, B., Ma, M., Yuan, Y., Yang, M., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419449122
Self-citationYu, R., Liu, T., Jin, S.-B., Ankarcrona, M., Lendahl, U., Nistér, M., & Zhao, J. (2021) · Figshare · doi:10.6084/m9.figshare.16851238
Metadata
- Authors
- Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., & Gao, S.
- Affiliations
- Sun Yat-sen University (CN)
- California Institute of Technology (US)
- Corresponding author
- Gao, Song
- Venue
- Nature
- Published
- 2017-01-23
- Volume
- 542
- Issue
- 7641
- Pages
- 372-376
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC5319402
- OpenAlex
- W2581248702
- Cited by
- 326
- References
- 53
- Citations by year
- 2026: 28 · 2025: 37 · 2024: 22 · 2023: 40 · 2022: 44 · 2021: 35 · 2020: 35 · 2019: 34 · 2018: 35 · 2017: 16
- FWCI
- 13.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM119388, R01GM083121, R01GM110039)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- mitofusin 1, mitochondrial fusion, GTP hydrolysis, conformational change, dynamin-related GTPase, mitochondrial outer membrane, helical domain, mitochondrial elongation, mitochondrial tethering, neuromuscular disorders, crystal structure
- MeSH terms
- Protein Domains, Amino Acid Sequence, Guanosine Triphosphate, Humans, Hydrolysis, Membrane Fusion, Membrane Potentials, Mitochondria, Models, Molecular, Tryptophan, Crystallography, X-Ray, GTP Phosphohydrolases, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Biocatalysis, Protein Multimerization, Mitochondrial Dynamics
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
