Control of mitochondrial morphology by a human mitofusin

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669

Predicting coiled coils from protein sequences.

Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392

PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization

Nakai, K., & Horton, P. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01336-x · Cited by 2,181

Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice

Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594

The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast

Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795

Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms.

Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758

A Human Dynamin-related Protein Controls the Distribution of Mitochondria

Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

Wolf, E., Kim, P. S., & Berger, B. (1997) · Protein Science · doi:10.1002/pro.5560060606 · Cited by 720

C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane

Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670

Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development

Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601

Calcium, ATP, and ROS: a mitochondrial love-hate triangle

Brookes, P. S., Yoon, Y., Robotham, J. L., Anders, M. W., & Sheu, S.-S. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00139.2004 · Cited by 2,575

Mitochondrial fusion and fission in cell life and death

Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002

During autophagy mitochondria elongate, are spared from degradation and sustain cell viability

Gomes, L. C., Benedetto, G. D., & Scorrano, L. (2011) · Nature Cell Biology · doi:10.1038/ncb2220 · Cited by 1,735

OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion

Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T., Bartoli, D., Polishuck, R. S., Danial, N. N., De Strooper, B., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.025 · Cited by 1,673

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550

Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A

Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., et al. (2004) · Nature Genetics · doi:10.1038/ng1341 · Cited by 1,572

Mitochondrial dynamics: overview of molecular mechanisms

Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397

Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction

Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376

The dynamin superfamily: universal membrane tubulation and fission molecules?

Praefcke, G. J. K., & McMahon, H. T. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1313 · Cited by 1,370

OPA1 requires mitofusin 1 to promote mitochondrial fusion

Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300

Mitochondrial dynamics and apoptosis

Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270

Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency

Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265

Fusion and fission: interlinked processes critical for mitochondrial health

Chan, D. C. (2012) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132529 · Cited by 1,196

Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation

Rambold, A. S., Kostelecky, B., Elia, N., & Lippincott‐Schwartz, J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107402108 · Cited by 1,188

Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells

Otera, H., Wang, C., Cleland, M. M., Setoguchi, K., Yokota, S., Youle, R. J., & Mihara, K. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007152 · Cited by 1,110

Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis

Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042

Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications

Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034

Mitochondrial Fusion and Fission in Mammals

Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972

Mitochondrial Dynamics in Mammalian Health and Disease

Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953

Structural Basis of Mitochondrial Tethering by Mitofusin Complexes

Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., & Chan, D. C. (2004) · Science · doi:10.1126/science.1099793 · Cited by 910

Mechanisms of Mitochondrial Fission and FusionPreprint

van der Bliek, A. M., Shen, Q., & Kawajiri, S. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011072 · Cited by 903

Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis

Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846

Mitochondrial dysfunction as a cause of optic neuropathies

Carelli, V., Ross‐Cisneros, F. N., & Sadun, A. A. (2004) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2003.10.003 · Cited by 852

Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism

Bach, D., Pich, S., Soriano, F. X., Vega, N., Baumgartner, B., Oriola, J., Daugaard, J. R., Lloberas, J., Camps, M., Zierath, J. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212754200 · Cited by 832

The Mitochondrial Protein hFis1 Regulates Mitochondrial Fission in Mammalian Cells through an Interaction with the Dynamin-Like Protein DLP1

Yoon, Y., Krueger, E. W., Oswald, B. J., & McNiven, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5409-5420.2003 · Cited by 820

Mito-Morphosis: Mitochondrial Fusion, Fission, and Cristae Remodeling as Key Mediators of Cellular Function

Pernas, L. F., & Scorrano, L. (2015) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105011 · Cited by 845

The Machines that Divide and Fuse Mitochondria

Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790

Mitochondrial fission in apoptosis

Youle, R. J., & Karbowski, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1697 · Cited by 773

The Novel Tail-anchored Membrane Protein Mff Controls Mitochondrial and Peroxisomal Fission in Mammalian Cells

Gandre-Babbe, S., & van der Bliek, A. M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1287 · Cited by 769

Dynamics of mitochondrial morphology in healthy cells and during apoptosis

Karbowski, M., & Youle, R. J. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401260 · Cited by 780

The Molecular Bases of Training Adaptation

Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756

Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes

Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737

Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity

Ishihara, N., Eura, Y., & Mihara, K. (2004) · Journal of Cell Science · doi:10.1242/jcs.01565 · Cited by 731

Mechanisms of membrane fusion: disparate players and common principles

Martens, S., & McMahon, H. T. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2417 · Cited by 733

Bioenergetic role of mitochondrial fusion and fission

Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687

Mitochondrial Fusion in Human Cells Is Efficient, Requires the Inner Membrane Potential, and Is Mediated by Mitofusins

Legros, F., Lombès, A., Frachon, P., & Rojo, M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-06-0330 · Cited by 676

Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions

Csordás, G., Weaver, D., & Hajnóczky, G. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.02.009 · Cited by 625

Mitofusin 2 ablation increases endoplasmic reticulum–mitochondria coupling

Filadi, R., Greotti, E., Turacchio, G., Luini, A., Pozzan, T., & Pizzo, P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504880112 · Cited by 593

Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo

Rojo, M., Legros, F., Chateau, D., & Lombès, A. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.8.1663 · Cited by 555

Emerging functions of mammalian mitochondrial fusion and fission

Chen, H., & Chan, D. C. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi270 · Cited by 538

Phosphatidylethanolamine Metabolism in Health and Disease

Calzada, E., Onguka, O., & Claypool, S. M. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.10.001 · Cited by 558

The role of mitochondrial dysfunction in cardiovascular disease: a brief review

Chistiakov, D. A., Shkurat, T. P., Melnichenko, A. А., Grechko, A. V., & Orekhov, A. N. (2017) · Annals of Medicine · doi:10.1080/07853890.2017.1417631 · Cited by 511

New insights into the function and regulation of mitochondrial fission

Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 501

The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division

Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 485

Mitochondrial fission mediates high glucose-induced cell death through elevated production of reactive oxygen species

Yu, T., Sheu, S.-S., Robotham, J. L., & Yoon, Y. (2008) · Cardiovascular Research · doi:10.1093/cvr/cvn104 · Cited by 462

The Charcot-Marie-Tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system

Pich, S., Bach, D., Briones, P., Liesa, M., Camps, M., Testar, X., Palacín, M., & Zorzano, A. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi149 · Cited by 455

Altered Axonal Mitochondrial Transport in the Pathogenesis of Charcot-Marie-Tooth Disease from Mitofusin 2 Mutations

Baloh, R. H., Schmidt, R. E., Pestronk, A., & Milbrandt, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4798-06.2007 · Cited by 450

Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells

Santel, A., Frank, S., Gaume, B. R., Herrler, M., Youle, R. J., & Fuller, M. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00479 · Cited by 445

Mfn2 modulates the UPR and mitochondrial function via repression of PERK

Muñoz, J. P., Ivanova, S., Sánchez‐Wandelmer, J., Martínez‐Cristóbal, P., Noguera, E., Sancho, A., Díaz‐Ramos, A., Hernández‐Alvarez, M. I., Sebastián, D., Mauvezin, C., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.168 · Cited by 451

Diverse roles of mitochondria in ischemic stroke

Yang, J., Mukda, S., & Chen, S. (2018) · Redox Biology · doi:10.1016/j.redox.2018.03.002 · Cited by 459

The human dynamin‐related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter‐membrane space

Olichon, A., Emorine, L. J., Descoins, E., Pelloquin, L., Brichese, L., Gas, N., Guillou, E., Delettre, C., Valette, A., Hamel, C., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02985-x · Cited by 430

Mitochondrial fission in apoptosis, neurodegeneration and aging

Bossy‐Wetzel, E., Barsoum, M. J., Godzik, A., Schwarzenbacher, R., & Lipton, S. A. (2003) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2003.10.015 · Cited by 438

OPA1 processing in cell death and disease – the long and short of it

MacVicar, T., & Langer, T. (2016) · Journal of Cell Science · doi:10.1242/jcs.159186 · Cited by 435

MARCH‐V is a novel mitofusin 2‐ and Drp1‐binding protein able to change mitochondrial morphology

Nakamura, N., Kimura, Y. N., Tokuda, M., Honda, S., & Hirose, S. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400790 · Cited by 419

Molecular mechanisms of mitochondrial dynamics

Tábara, L. C., Segawa, M., & Prudent, J. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00785-1 · Cited by 445

Free Radicals in Cross Talk Between Autophagy and Apoptosis

Kaminskyy, V. O., & Zhivotovsky, B. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5746 · Cited by 421

Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network

Niemann, A., Rüegg, M., Padula, V. L., Schenone, A. E., & Suter, U. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507087 · Cited by 402

Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology

Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 401

Mitochondrial Fusion: The Machineries In and Out

Gao, S., & Hu, J. (2020) · Trends in Cell Biology · doi:10.1016/j.tcb.2020.09.008 · Cited by 396

Atypical Rho GTPases Have Roles in Mitochondrial Homeostasis and Apoptosis

Fransson, Å., Ruusala, A., & Aspenström, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208609200 · Cited by 396

Mitochondrial dynamics and division in budding yeast

Shaw, J. M., & Nunnari, J. (2002) · Trends in Cell Biology · doi:10.1016/s0962-8924(01)02246-2 · Cited by 375

Composition and dynamics of human mitochondrial nucleoids.

Garrido, N., Griparić, L., Jokitalo, E., Wartiovaara, J., van der Bliek, A. M., & Spelbrink, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0399 · Cited by 390

Dysregulation of HSG triggers vascular proliferative disorders

Chen, K.-H., Guo, X., Ma, D., Guo, Y., Li, Q., Yang, D., Li, P., Qiu, X., Wen, S., Xiao, R.-P., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1161 · Cited by 370

Expression of Mfn2, the Charcot-Marie-Tooth Neuropathy Type 2A Gene, in Human Skeletal Muscle

Bach, D., Naon, D., Pich, S., Soriano, F. X., Vega, N., Rieusset, J., Laville, M., Guillet, C., Boirie, Y., Wallberg-Henriksson, H., et al. (2005) · Diabetes · doi:10.2337/diabetes.54.9.2685 · Cited by 369

Mitochondrial metabolism, redox signaling, and fusion: a mitochondria-ROS-HIF-1α-Kv1.5 O2-sensing pathway at the intersection of pulmonary hypertension and cancer

Archer, S. L., Gomberg‐Maitland, M., Maitland, M. L., Rich, S., Garcia, J. G. N., & Weir, Ε. K. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01324.2007 · Cited by 372

FUNDC1 regulates mitochondrial dynamics at the ER–mitochondrial contact site under hypoxic conditions

Wu, W., Lin, C., Wu, K., Jiang, L., Wang, X., Li, W., Zhuang, H., Zhang, X., Chen, H. H., Li, S., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593102 · Cited by 370

Mitofusin-2 Maintains Mitochondrial Structure and Contributes to Stress-Induced Permeability Transition in Cardiac Myocytes

Papanicolaou, K. N., Khairallah, R. J., Ngoh, G. A., Chikando, A. C., Luptak, I., O’Shea, K. M., Riley, D. D., Lugus, J. J., Colucci, W. S., Lederer, W. J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00911-10 · Cited by 371

Mitofusin 2: from functions to disease

Filadi, R., Pendin, D., & Pizzo, P. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0023-6 · Cited by 373

Determinants and outcomes of mitochondrial dynamics

Quintana–Cabrera, R., & Scorrano, L. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.012 · Cited by 362

Mitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury

Anzell, A. R., Maizy, R., Przyklenk, K., & Sanderson, T. H. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0503-9 · Cited by 359

Mitochondrial ‘kiss‐and‐run’: interplay between mitochondrial motility and fusion–fission dynamics

Liu, X., Weaver, D., Shirihai, O. S., & Hajnóczky, G. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.255 · Cited by 360

Regulation and Function of Mitochondria–Lysosome Membrane Contact Sites in Cellular Homeostasis

Wong, Y. C., Kim, S., Peng, W., & Krainc, D. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.004 · Cited by 355

Complementation between mouse Mfn1 and Mfn2 protects mitochondrial fusion defects caused by CMT2A disease mutations

Detmer, S. A., & Chan, D. C. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611080 · Cited by 343

Evidence for a Mitochondrial Regulatory Pathway Defined by Peroxisome Proliferator–Activated Receptor-γ Coactivator-1α, Estrogen-Related Receptor-α, and Mitofusin 2

Soriano, F. X., Liesa, M., Bach, D., Chan, D. C., Palacín, M., & Zorzano, A. (2006) · Diabetes · doi:10.2337/db05-0509 · Cited by 343

Fzo1, a Protein Involved in Mitochondrial Fusion, Inhibits Apoptosis

Sugioka, R., Shimizu, S., & Tsujimoto, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408910200 · Cited by 341

The functional organization of mitochondrial genomes in human cells

Iborra, F. J., Kimurâ, H., & Cook, P. R. (2004) · BMC Biology · doi:10.1186/1741-7007-2-9 · Cited by 339

Mitochondrial fission and fusion: A dynamic role in aging and potential target for age-related disease

Liu, Y. J., McIntyre, R. L., Janssens, G. E., & Houtkooper, R. H. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111212 · Cited by 347

Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology

Stojanovski, D., Koutsopoulos, O. S., Okamoto, K., & Ryan, M. T. (2004) · Journal of Cell Science · doi:10.1242/jcs.01058 · Cited by 332

MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

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., et al. (2017) · Nature · doi:10.1038/nature21077 · Cited by 326

Glutamate Decreases Mitochondrial Size and Movement in Primary Forebrain Neurons

Rintoul, G. L., Filiano, A. J., Brocard, J. B., Kress, G. J., & Reynolds, I. J. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-21-07881.2003 · Cited by 326

Mitochondrial morphology and cardiovascular disease

Ong, S., & Hausenloy, D. J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq237 · Cited by 331

Determinants and Functions of Mitochondrial Behavior

Labbè, K., Murley, A., & Nunnari, J. M. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155756 · Cited by 324

The Metabolic Theory of Pulmonary Arterial Hypertension

Paulin, R., & Michelakis, E. D. (2014) · Circulation Research · doi:10.1161/circresaha.115.301130 · Cited by 328

Mitochondrial dynamics in health and disease

Yapa, N. M. B., Lisnyak, V., Reljić, B., & Ryan, M. T. (2021) · FEBS Letters · doi:10.1002/1873-3468.14077 · Cited by 323

Activated Mitofusin 2 Signals Mitochondrial Fusion, Interferes with Bax Activation, and Reduces Susceptibility to Radical Induced Depolarization

Neuspiel, M., Zunino, R., Gangaraju, S., Rippstein, P. U., & McBride, H. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501599200 · Cited by 308

Mitochondrial dynamics controlled by mitofusins regulate Agrp neuronal activity and diet-induced obesity

Dietrich, M. O., Liu, Z.-W., & Horvath, T. L. (2013) · Cell · doi:10.1016/j.cell.2013.09.004 · Cited by 306

Animal mitochondrial DNA recombination revisited

Rokas, A., Ladoukakis, E. D., & Zouros, E. (2003) · Trends in Ecology & Evolution · doi:10.1016/s0169-5347(03)00125-3 · Cited by 304

The function of the respiratory supercomplexes: The plasticity model

Acín‐Pérez, R., & Enrı́quez, J. A. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.12.009 · Cited by 319

The Mechanobiology of Aging

Phillip, J. M., Aifuwa, I., Walston, J. D., & Wirtz, D. (2015) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071114-040829 · Cited by 304

Mitochondrial fission and fusion

Scott, I., & Youle, R. J. (2010) · Essays in Biochemistry · doi:10.1042/bse0470085 · Cited by 306

Mitochondrial dynamics in cell death and neurodegeneration

Cho, D., Nakamura, T., & Lipton, S. A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0435-2 · Cited by 306

Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence

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