Mitochondrial dynamics in adaptive and maladaptive cellular stress responses

Mitochondrial Fission, Fusion, and Stress

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Mechanisms of mitophagy

Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273

Fission and selective fusion govern mitochondrial segregation and elimination by autophagy

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

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Cellular mechanisms and physiological consequences of redox-dependent signalling

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Mitochondria as sensors and regulators of calcium signalling

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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

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

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Mitochondrial Dynamics Controls T Cell Fate through Metabolic Programming

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Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy

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Structural and functional features and significance of the physical linkage between ER and mitochondria

Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377

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

Mitochondrial Dynamics in the Regulation of Nutrient Utilization and Energy Expenditure

Liesa, M., & Shirihai, O. S. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.03.002 · Cited by 1,341

OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28

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PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria

Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323

Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology

Yu, T., Robotham, J. L., & Yoon, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511154103 · Cited by 1,246

Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations

Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211

PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility

Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,198

Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria

Cereghetti, G. M., Stangherlin, A., de Brito, O. M., Chang, C. R., Blackstone, C., Bernardi, P., & Scorrano, L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808249105 · Cited by 1,129

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

AMP-activated protein kinase mediates mitochondrial fission in response to energy stress

Toyama, E. Q., Herzig, S., Courchet, J., Lewis, T. L., Losón, O. C., Hellberg, K., Young, N. P., Chen, H., Polleux, F., Chan, D. C., et al. (2016) · Science · doi:10.1126/science.aab4138 · Cited by 1,085

Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice

Ishihara, N., Nomura, M., Jofuku, A., Kato, H., Suzuki, S. O., Masuda, K., Otera, H., Nakanishi, Y., Nonaka, I., Goto, Y.-I., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1907 · Cited by 1,066

Fatty Acid Trafficking in Starved Cells: Regulation by Lipid Droplet Lipolysis, Autophagy, and Mitochondrial Fusion Dynamics

Rambold, A. S., Cohen, S., & Lippincott-Schwartz, J. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.029 · Cited by 1,038

ULTRASTRUCTURAL BASES FOR METABOLICALLY LINKED MECHANICAL ACTIVITY IN MITOCHONDRIA

Hackenbrock, C. R. (1966) · The Journal of Cell Biology · doi:10.1083/jcb.30.2.269 · Cited by 983

Mitochondrial fusion protects against neurodegeneration in the cerebellum

Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924

Supercomplex assembly determines electron flux in the mitochondrial electron transport chain

Lapuente-Brun, E., Moreno-Loshuertos, R., Acín-Pérez, R., Latorre-Pellicer, A., Colás, C., Balsa, E., Perales-Clemente, E., Quirós, P. M., Calvo, E., Rodríguez-Hernández, M. A., et al. (2013) · Science · doi:10.1126/science.1230381 · Cited by 830

Mitochondrial threshold effects

Rossignol, R., Faustin, B., Rocher, C., Malgat, M., Mazat, J., & Letellier, T. (2003) · Biochemical Journal · doi:10.1042/bj20021594 · Cited by 816

Intracellular Ca2+ Sensing: Its Role in Calcium Homeostasis and Signaling

Bagur, R., & Hajnóczky, G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.028 · Cited by 815

SLP‐2 is required for stress‐induced mitochondrial hyperfusion

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Chronic enrichment of hepatic endoplasmic reticulum–mitochondria contact leads to mitochondrial dysfunction in obesity

Arruda, A. P., Pers, B. M., Parlakgül, G., Güney, E., Inouye, K., & Hotamışlıgil, G. S. (2014) · Nature Medicine · doi:10.1038/nm.3735 · Cited by 741

Dimer ribbons of ATP synthase shape the inner mitochondrial membrane

Strauss, M., Hofhaus, G., Schröder, R. R., & Kühlbrandt, W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.35 · Cited by 677

ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells

Lewis, S. C., Uchiyama, L. F., & Nunnari, J. (2016) · Science · doi:10.1126/science.aaf5549 · Cited by 673

The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice

Wakabayashi, J., Zhang, Z., Wakabayashi, N., Tamura, Y., Fukaya, M., Kensler, T. W., Iijima, M., & Sesaki, H. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903065 · Cited by 667

Mitofusin 2 Is Necessary for Transport of Axonal Mitochondria and Interacts with the Miro/Milton Complex

Misko, A. L., Jiang, S., Wegorzewska, I., Milbrandt, J., & Baloh, R. H. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.6248-09.2010 · Cited by 653

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

Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion

Song, Z., Ghochani, M., McCaffery, J. M., Frey, T. G., & Chan, D. C. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0252 · Cited by 623

Mitochondria as a Target of Environmental Toxicants

Meyer, J. N., Leung, M. C. K., Rooney, J. P., Sendoel, A., Hengartner, M. O., Kisby, G. E., & Bess, A. S. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft102 · Cited by 587

An energetic view of stress: Focus on mitochondria

Picard, M. A., McEwen, B. S., Epel, E. S., & Sandi, C. (2018) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2018.01.001 · Cited by 584

The role of mitochondria in amyotrophic lateral sclerosis

Smith, E. F., Shaw, P. J., & Vos, K. J. D. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.052 · Cited by 579

Age-Associated Loss of OPA1 in Muscle Impacts Muscle Mass, Metabolic Homeostasis, Systemic Inflammation, and Epithelial Senescence

Tezze, C., Romanello, V., Desbats, M. A., Fadini, G. P., Albiero, M., Favaro, G., Ciciliot, S., Soriano, M. E., Morbidoni, V., Cerqua, C., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.021 · Cited by 568

Mitochondria: The Next (Neurode)Generation

Schon, E. A., & Przedborski, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.003 · Cited by 568

Bidirectional Ca 2+ -dependent control of mitochondrial dynamics by the Miro GTPase

Saotome, M., Safiulina, D., Szabadkai, G., Das, S., Fransson, Å., Aspenstrom, P., Rizzuto, R., & Hajnóczky, G. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808953105 · Cited by 538

Mitochondrial Trafficking in Neurons

Schwarz, T. L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011304 · Cited by 525

OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes

Amati-Bonneau, P., Valentino, M. L., Reynier, P., Gallardo, M. E., Bornstein, B., Boissiere, A., Campos, Y., Rivera, H., de la Aleja, J. G., Carroccia, R., et al. (2008) · Brain · doi:10.1093/brain/awm298 · Cited by 520

Mitofusin 2 in POMC neurons connects ER stress with leptin resistance and energy imbalance

Schneeberger, M., Dietrich, M. O., Sebastián, D., Imbernón, M., Castaño, C., Garcia, A., Esteban, Y., Gonzalez-Franquesa, A., Rodríguez, I. C., Bortolozzi, A., et al. (2013) · Cell · doi:10.1016/j.cell.2013.09.003 · Cited by 519

Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells

Head, B., Griparic, L., Amiri, M., Gandre-Babbe, S., & van der Bliek, A. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200906083 · Cited by 515

Mitochondrial Fusion is Essential for Organelle Function and Cardiac Homeostasis

Chen, Y., Liu, Y., & Dorn, G. W. (2011) · Circulation Research · doi:10.1161/circresaha.111.258723 · Cited by 515

Multiple dynamin family members collaborate to drive mitochondrial division

Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512

Mitochondrial diseases: the contribution of organelle stress responses to pathology

Suomalainen, A., & Battersby, B. J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.66 · Cited by 505

Mitofusins, from Mitochondria to Metabolism

Schrepfer, E., & Scorrano, L. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.022 · Cited by 504

The mitochondrial contact site complex, a determinant of mitochondrial architecture

Harner, M. E., Körner, C., Walther, D. M., Mokranjac, D., Kaesmacher, J., WELSCH, U. N., Griffith, J. M., Mann, M., Reggiori, F., & Neupert, W. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.379 · Cited by 497

Modulation of the endoplasmic reticulum–mitochondria interface in Alzheimer’s disease and related models

Hedskog, L., Pinho, C. M., Filadi, R., Rönnbäck, A., Hertwig, L., Wiehager, B., Larssen, P., Gellhaar, S., Sandebring, A., Westerlund, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300677110 · Cited by 478

Control of mitochondrial motility and distribution by the calcium signal

Yi, M., Weaver, D., & Hajnóczky, G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200406038 · Cited by 476

Proteolytic Cleavage of Opa1 Stimulates Mitochondrial Inner Membrane Fusion and Couples Fusion to Oxidative Phosphorylation

Mishra, P., Carelli, V., Manfredi, G., & Chan, D. C. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.03.011 · Cited by 473

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

Structure and dynamics of the mitochondrial inner membrane cristae

Mannella, C. A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.006 · Cited by 455

Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice

Gong, G., Song, M., Csordás, G., Kelly, D. P., Matkovich, S. J., & Dorn, G. W. (2015) · Science · doi:10.1126/science.aad2459 · Cited by 451

Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function

Davies, V. J., Hollins, A. J., Piechota, M. J., Yip, W., Davies, J. R., White, K. E., Nicols, P. P., Boulton, M. E., & Votruba, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm079 · Cited by 449

SIRT3 Deacetylates and Activates OPA1 To Regulate Mitochondrial Dynamics during Stress

Samant, S. A., Zhang, H. J., Hong, Z., Pillai, V. B., Sundaresan, N. R., Wolfgeher, D., Archer, S. L., Chan, D. C., & Gupta, M. P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01483-13 · Cited by 446

Sphingolipid Metabolism Cooperates with BAK and BAX to Promote the Mitochondrial Pathway of Apoptosis

Chipuk, J. E., McStay, G. P., Bharti, A., Kuwana, T., Clarke, C. J., Siskind, L. J., Obeid, L. M., & Green, D. R. (2012) · Cell · doi:10.1016/j.cell.2012.01.038 · Cited by 436

Mitochondrial trafficking and anchoring in neurons: New insight and implications

Sheng, Z. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201312123 · Cited by 429

Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance

Hudson, G., Amati-Bonneau, P., Blakely, E. L., Stewart, J. D., He, L., Schaefer, A. M., Griffiths, P. G., Ahlqvist, K., Suomalainen, A., Reynier, P., et al. (2008) · Brain · doi:10.1093/brain/awm272 · Cited by 428

Mitochondrial oxidative stress causes mitochondrial fragmentation via differential modulation of mitochondrial fission–fusion proteins

Wu, S., Zhou, F., Zhang, Z., & Xing, D. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08010.x · Cited by 423

Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria

Ono, T., Isobe, K., Nakada, K., & Hayashi, J.-I. (2001) · Nature Genetics · doi:10.1038/90116 · Cited by 420

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

OPA1‐dependent cristae modulation is essential for cellular adaptation to metabolic demand

Patten, D. A., Wong, J., Khacho, M., Soubannier, V., Mailloux, R. J., Pilon‐Larose, K., MacLaurin, J. G., Park, D. S., McBride, H. M., Trinkle‐Mulcahy, L., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488349 · Cited by 411

Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin

Ban, T., Ishihara, T., Kohno, H., Saita, S., Ichimura, A., Maenaka, K., Oka, T., Mihara, K., & Ishihara, N. (2017) · Nature Cell Biology · doi:10.1038/ncb3560 · Cited by 410

Bridging the gap: Membrane contact sites in signaling, metabolism, and organelle dynamics

Prinz, W. A. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201401126 · Cited by 409

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

Perinuclear Mitochondrial Clustering Creates an Oxidant-Rich Nuclear Domain Required for Hypoxia-Induced Transcription

Al‐Mehdi, A., Pastukh, V. M., Swiger, B. M., Reed, D., Patel, M., Bardwell, G. C., Pastukh, V. V., ALEXEYEV, M. F., & Gillespie, M. N. (2012) · Science Signaling · doi:10.1126/scisignal.2002712 · Cited by 396

Mitochondrial Networking Protects β-Cells From Nutrient-Induced Apoptosis

Molina, A. J. A., Wikstrom, J. D., Stiles, L., Las, G., Mohamed, H., Elorza, A., Walzer, G., Twig, G., Katz, S., Corkey, B. E., et al. (2009) · Diabetes · doi:10.2337/db07-1781 · Cited by 381

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

Gene–environment interactions in Leber hereditary optic neuropathy

Kirkman, M. A., Yu‐Wai‐Man, P., Korsten, A., Leonhardt, M., Dimitriadis, K., de Coo, I. F. M., Klopstock, T., & Chinnery, P. F. (2009) · Brain · doi:10.1093/brain/awp158 · Cited by 358

Mitochondrial Fusion Directs Cardiomyocyte Differentiation via Calcineurin and Notch Signaling

Kasahara, A., Cipolat, S., Chen, Y., Dorn, G. W., & Scorrano, L. (2013) · Science · doi:10.1126/science.1241359 · Cited by 354

Mitofusin 2-Containing Mitochondrial-Reticular Microdomains Direct Rapid Cardiomyocyte Bioenergetic Responses Via Interorganelle Ca 2+ Crosstalk

Chen, Y., Csordás, G., Jowdy, C. C., Schneider, T. G., Csordás, N., Wang, W., Liu, Y., Kohlhaas, M., Meiser, M., Bergem, S., et al. (2012) · Circulation Research · doi:10.1161/circresaha.112.266585 · Cited by 353

Actin filaments target the oligomeric maturation of the dynamin GTPase Drp1 to mitochondrial fission sites

Ji, W.-K., Hatch, A. L., Merrill, R. A., Strack, S., & Higgs, H. N. (2015) · eLife · doi:10.7554/elife.11553 · Cited by 347

Miro proteins coordinate microtubule‐ and actin‐dependent mitochondrial transport and distribution

López‐Doménech, G., Covill‐Cooke, C., Ivankovic, D., Halff, E. F., Sheehan, D. F., Norkett, R., Birsa, N., & Kittler, J. T. (2018) · The EMBO Journal · doi:10.15252/embj.201696380 · Cited by 345

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

Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission

Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336

Why do BCL-2 inhibitors work and where should we use them in the clinic?

Montero, J., & Letai, A. (2017) · Cell Death and Differentiation · doi:10.1038/cdd.2017.183 · Cited by 335

Facilitation of axon regeneration by enhancing mitochondrial transport and rescuing energy deficits

Zhou, B., Yu, P., Lin, M.-Y., Sun, T., Chen, Y., & Sheng, Z. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201605101 · Cited by 328

Orchestration of lymphocyte chemotaxis by mitochondrial dynamics

Campello, S., Lacalle, R. A., Bettella, M., Mañes, S., Scorrano, L., & Viola, A. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061877 · Cited by 325

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

Bax and Bak Promote Apoptosis by Modulating Endoplasmic Reticular and Mitochondrial Ca2+ Stores

Nutt, L. K., Pataer, A., Pahler, J., Fang, B., Roth, J. A., McConkey, D. J., & Swisher, S. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106817200 · Cited by 320

Abrogating Mitochondrial Dynamics in Mouse Hearts Accelerates Mitochondrial Senescence

Song, M., Franco, A., Fleischer, J. A., Zhang, L., & Dorn, G. W. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.09.023 · Cited by 309

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

Häcki, J., Egger, L., Monney, L., Conus, S., Rossé, T., Fellay, I., & Borner, C. (2000) · Oncogene · doi:10.1038/sj.onc.1203592 · Cited by 303

MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture

Friedman, J. R., Mourier, A., Yamada, J., McCaffery, J. M., & Nunnari, J. (2015) · eLife · doi:10.7554/elife.07739 · Cited by 291

Opa1-Mediated Cristae Opening Is Bax/Bak and BH3 Dependent, Required for Apoptosis, and Independent of Bak Oligomerization

Yamaguchi, R., Lartigue, L., Perkins, G. A., Scott, R. T., Dixit, A., Kushnareva, Y., Kuwana, T., Ellisman, M. H., & Newmeyer, D. D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.010 · Cited by 290

Altered fusion dynamics underlie unique morphological changes in mitochondria during hypoxia–reoxygenation stress

Liu, X., & Hajnóczky, G. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.13 · Cited by 287

Glucose Regulates Mitochondrial Motility via Milton Modification by O-GlcNAc Transferase

Pekkurnaz, G., Trinidad, J. C., Wang, X., Kong, D., & Schwarz, T. L. (2014) · Cell · doi:10.1016/j.cell.2014.06.007 · Cited by 283

A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery.

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A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy

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