Mitochondria: In Sickness and in Health
Open accessAbstract
Mitochondria perform diverse yet interconnected functions, producing ATP and many biosynthetic intermediates while also contributing to cellular stress responses such as autophagy and apoptosis. Mitochondria form a dynamic, interconnected network that is intimately integrated with other cellular compartments. In addition, mitochondrial functions extend beyond the boundaries of the cell and influence an organism's physiology by regulating communication between cells and tissues. It is therefore not surprising that mitochondrial dysfunction has emerged as a key factor in a myriad of diseases, including neurodegenerative and metabolic disorders. We provide a current view of how mitochondrial functions impinge on health and disease.
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
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?
Detection of mitochondrial motives by innate and adaptive immunity might elicit potent pro-inflammatory responses.
“Given the bacterial features of mitochondria, the detection of mitochondrial motives by cells of the innate and adaptive immunity might elicit potent pro-inflammatory responses147,276,277.”
From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [277]
The Introduction describes mitochondria’s bacterial ancestry, and “Mitochondrial Defects Cause Diverse and Complex Human Diseases” says that the innate immune system recognizes and targets mouse cells with allogenic mtDNA. Our copy does not say that adaptive immunity detects mitochondrial motifs or that such detection elicits potent pro-inflammatory responses. (LLM, conf=0.82)
Experimental — accuracy not yet measuredMitochondria are the primary producers of intracellular reactive oxygen species and are susceptible to oxidative stress caused by toxic metabolites such as β-amyloid.
“Mitochondria not only generate ATP but also act as the primary producers of intracellular reactive oxygen species (ROS) and are susceptible to oxidative stress caused by various toxic metabolites, such as β‐amyloid (Aβ) [3, 4].”
From Aerobic exercise improves astrocyte mitochondrial quality and transfer to neurons in a mouse model of Alzheimer's disease (2025) · cites this paper as [3]
The section “Mitochondria Are Metabolic Signaling Centers” states that mitochondrial complexes I and III generate ROS, and the paper also describes mitochondrial ATP production. It does not establish that mitochondria are the primary intracellular ROS producers or say that β-amyloid causes oxidative stress in mitochondria; searches for amyloid and Alzheimer-related oxidative stress did not find that link. Page numbers are unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredMOMP eventually leads to the dissipation of the mitochondrial transmembrane potential (Δψm)-mostly as a consequence of the respiratory impairment imposed by the loss of CYCS-and hence to the cessation of Δψm-dependent mitochondrial functions (including ATP synthesis and some forms of protein import).
“Of note, MOMP eventually leads to the dissipation of the mitochondrial transmembrane potential (Δψm)—mostly as a consequence of the respiratory impairment imposed by the loss of CYCS—and hence to the cessation of Δψm-dependent mitochondrial functions (including ATP synthesis and some forms of protein import) [200–203].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [200]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
1 retracted
Wenz, T., Diaz, F., Spiegelman, B. M., & Moraes, C. T. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.006 · Cited by 297 · see citing works
RetractedUnderstanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works
How mitochondria produce reactive oxygen species
Murphy, M. P. (2009) · Biochemical Journal · doi:10.1042/bj20081386 · Cited by 8,207 · see citing works
<i>IDH1</i> and <i>IDH2</i> Mutations in Gliomas
Yan, H., Parsons, D. W., Jin, G., McLendon, R., Rasheed, B. A., Yuan, W., Kos, I., Batinic-Haberle, I., Jones, S., Riggins, G. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808710 · Cited by 5,847 · see citing works
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227 · see citing works
Chronic Parkinsonism in Humans Due to a Product of Meperidine-Analog Synthesis
Langston, J. W., Ballard, P., Tetrud, J. W., & Irwin, I. (1983) · Science · doi:10.1126/science.6823561 · Cited by 4,914 · see citing works
A PGC1-α-dependent myokine that drives brown-fat-like development of white fat and thermogenesis
Boström, P., Wu, J., Jedrychowski, M. P., Korde, A., Ye, L., Lo, J. C., Rasbach, K. A., Boström, E. A., Choi, J. H., Long, J. Z., et al. (2012) · Nature · doi:10.1038/nature10777 · Cited by 4,810 · see citing works
Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
MITCHELL, P. (1961) · Nature · doi:10.1038/191144a0 · Cited by 4,704 · see citing works
Wu, Z., Puigserver, P., Andersson, U., Zhang, C., Adelmant, G., Mootha, V., Troy, A., Cinti, S., Lowell, B., Scarpulla, R. C., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80611-x · Cited by 4,139 · see citing works
Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
Narendra, D., Tanaka, A., Suen, D.-F., & Youle, R. J. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200809125 · Cited by 4,026 · see citing works
A Cold-Inducible Coactivator of Nuclear Receptors Linked to Adaptive Thermogenesis
Puigserver, P., Wu, Z., Park, C. W., Graves, R., Wright, M., & Spiegelman, B. M. (1998) · Cell · doi:10.1016/s0092-8674(00)81410-5 · Cited by 3,864 · see citing works
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in <i>PINK1</i>
Valente, E. M., Abou-Sleiman, P. M., Caputo, V., Muqit, M. M. K., Harvey, K., Gispert, S., Ali, Z., Del Turco, D., Bentivoglio, A. R., Healy, D. G., et al. (2004) · Science · doi:10.1126/science.1096284 · Cited by 3,481 · see citing works
Cold-Activated Brown Adipose Tissue in Healthy Men
van Marken Lichtenbelt, W. D., Vanhommerig, J. W., Smulders, N. M., Drossaerts, J. M. A. F. L., Kemerink, G. J., Bouvy, N. D., Schrauwen, P., & Teule, G. J. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808718 · Cited by 3,452 · see citing works
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300 · see citing works
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H., Wikstrom, J. D., Walzer, G., Stiles, L., Haigh, S. E., Katz, S., Las, G., et al. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601963 · Cited by 3,082 · see citing works
Functional Brown Adipose Tissue in Healthy Adults
Virtanen, K. A., Lidell, M. E., Orava, J., Heglind, M., Westergren, R., Niemi, T., Taittonen, M., Laine, J., Savisto, N.-J., Enerbäck, S., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808949 · Cited by 3,058 · see citing works
PINK1 Is Selectively Stabilized on Impaired Mitochondria to Activate Parkin
Narendra, D. P., Jin, S. M., Tanaka, A., Suen, D.-F., Gautier, C. A., Shen, J., Cookson, M. R., & Youle, R. J. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000298 · Cited by 2,944 · see citing works
The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
Mihaylova, M. M., & Shaw, R. J. (2011) · Nature Cell Biology · doi:10.1038/ncb2329 · Cited by 2,923 · see citing works
Premature ageing in mice expressing defective mitochondrial DNA polymerase
Trifunovic, A., Wredenberg, A., Falkenberg, M., Spelbrink, J. N., Rovio, A. T., Bruder, C. E., Bohlooly-Y, M., Gidlöf, S., Oldfors, A., Wibom, R., et al. (2004) · Nature · doi:10.1038/nature02517 · Cited by 2,734 · see citing works
Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
Tabas, I. A., & Ron, D. (2011) · Nature Cell Biology · doi:10.1038/ncb0311-184 · Cited by 2,603 · see citing works
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 · see citing works
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Jäger, S., Handschin, C., St.-Pierre, J., & Spiegelman, B. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705070104 · Cited by 2,491 · see citing works
Mitochondrial DNA mutation associated with Leber’s hereditary optic neuropathy
Wallace, D. C., Singh, G., Lott, M. T., Hodge, J. A., Schurr, T. G., Lezza, A. M. S., Elsas, L. J., & Nikoskelainen, E. K. (1988) · Science · doi:10.1126/science.3201231 · Cited by 2,440 · see citing works
Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
Kujoth, G. C., Hiona, A., Pugh, T. D., Someya, S., Panzer, K., Wohlgemuth, S. E., Hofer, T., Seo, A. Y., Sullivan, R., Jobling, W. A., et al. (2005) · Science · doi:10.1126/science.1112125 · Cited by 2,165 · see citing works
FGF-21 as a novel metabolic regulator
Kharitonenkov, A., Shiyanova, T. L., Koester, A., Ford, A. M., Micanovic, R., Galbreath, E. J., Sandusky, G. E., Hammond, L. J., Moyers, J. S., Owens, R. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23606 · Cited by 2,125 · see citing works
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072 · see citing works
Self-citationA Mitochondrial Protein Compendium Elucidates Complex I Disease Biology
Pagliarini, D. J., Calvo, S. E., Chang, B., Sheth, S. A., Vafai, S. B., Ong, S.-E., Walford, G. A., Sugiana, C., Boneh, A., Chen, W. K., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.016 · Cited by 1,994 · see citing works
IDH mutation impairs histone demethylation and results in a block to cell differentiation
Lu, C., Ward, P. S., Kapoor, G. S., Rohle, D., Turcan, S., Abdel-Wahab, O., Edwards, C. R., Khanin, R., Figueroa, M. E., Melnick, A., et al. (2012) · Nature · doi:10.1038/nature10860 · Cited by 1,985 · see citing works
IDH1 mutation is sufficient to establish the glioma hypermethylator phenotype
Turcan, S., Rohle, D., Goenka, A., Walsh, L. A., Fang, F., Yilmaz, E., Campos, C., Fabius, A. W. M., Lu, C., Ward, P. S., et al. (2012) · Nature · doi:10.1038/nature10866 · Cited by 1,974 · see citing works
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969 · see citing works
Integrative genomics identifies MCU as an essential component of the mitochondrial calcium uniporter
Baughman, J. M., Perocchi, F., Girgis, H. S., Plovanich, M. E., Belcher-Timme, C. A., Sancak, Y., Bao, X., Strittmatter, L., Goldberger, O., Bogorad, R., et al. (2011) · Nature · doi:10.1038/nature10234 · Cited by 1,926 · see citing works
Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies
Holt, I. J., Harding, A. E., & MORGAN-HUGHES, J. A. (1988) · Nature · doi:10.1038/331717a0 · Cited by 1,845 · see citing works
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., & Guo, M. (2006) · Nature · doi:10.1038/nature04779 · Cited by 1,788 · see citing works
The Role of Dynamin-Related Protein 1, a Mediator of Mitochondrial Fission, in Apoptosis
Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W., Robert, E. G., Catez, F., Smith, C. L., & Youle, R. J. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00055-7 · Cited by 1,755 · see citing works
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 · see citing works
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
Park, J., Lee, S. B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.-M., et al. (2006) · Nature · doi:10.1038/nature04788 · Cited by 1,705 · see citing works
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 · see citing works
Mutations in <i>SDHD</i> , a Mitochondrial Complex II Gene, in Hereditary Paraganglioma
Baysal, B. E., Ferrell, R. E., Willett-Brozick, J. E., Lawrence, E. C., Myssiorek, D., Bosch, A., Mey, A. V. D., Taschner, P. E. M., Rubinstein, W. S., Myers, E. N., et al. (2000) · Science · doi:10.1126/science.287.5454.848 · Cited by 1,638 · see citing works
The Multiple Leiomyoma Consortium (2002) · Nature Genetics · doi:10.1038/ng849 · Cited by 1,635 · see citing works
PINK1-dependent recruitment of Parkin to mitochondria in mitophagy
Vives-Bauza, C., Zhou, C., Huang, Y., Cui, M., de Vries, R. L. A., Kim, J., May, J., Tocilescu, M. A., Liu, W., Ko, H. S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911187107 · Cited by 1,616 · see citing works
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 · see citing works
Bender, A., Krishnan, K. J., Morris, C. M., Taylor, G. A., Reeve, A. K., Perry, R. H., Jaros, E., Hersheson, J. S., Betts, J., Klopstock, T., et al. (2006) · Nature Genetics · doi:10.1038/ng1769 · Cited by 1,570 · see citing works
The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
Li, Z., Okamoto, K.-I., Hayashi, Y., & Sheng, M. (2004) · Cell · doi:10.1016/j.cell.2004.11.003 · Cited by 1,498 · see citing works
Translocation of Proteins into Mitochondria
Neupert, W., & Herrmann, J. M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.163409 · Cited by 1,486 · see citing works
Delettre, C., Lenaers, G., Griffoin, J.-M., Gigarel, N., Lorenzo, C., Belenguer, P., Pelloquin, L., Grosgeorge, J., Turc-Carel, C., Perret, E., et al. (2000) · Nature Genetics · doi:10.1038/79936 · Cited by 1,446 · see citing works
Chipuk, J. E., Moldoveanu, T., Llambi, F., Parsons, M. J., & Green, D. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.025 · Cited by 1,432 · see citing works
A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
Stefani, D. D., Raffaello, A., Teardo, E., Szabò, I., & Rizzuto, R. (2011) · Nature · doi:10.1038/nature10230 · Cited by 1,431 · see citing works
Chronic parkinsonism secondary to intravenous injection of meperidine analogues
Davis, G. C., Williams, A. C., Markey, S. P., Ebert, M. H., Caine, E. D., Reichert, C. M., & Kopin, I. J. (1979) · Psychiatry Research · doi:10.1016/0165-1781(79)90006-4 · Cited by 1,377 · see citing works
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 · cited 9× · see citing works
“In this context, it is possible that the mitochondrial motility defects associated with absent or altered MFN1 and MFN2 proteins result from the targeted degradation of Miro (Baloh et al., 2007; Chen et al., 2005).”
BackgroundInfluentialProteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
Tanaka, A., Cleland, M. M., Xu, S., Narendra, D. P., Suen, D.-F., Karbowski, M., & Youle, R. J. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201007013 · Cited by 1,369 · see citing works
Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics
Martinou, J., & Youle, R. J. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.06.017 · Cited by 1,366 · see citing works
Alexander, C., Votruba, M., Pesch, U. E. A., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., et al. (2000) · Nature Genetics · doi:10.1038/79944 · Cited by 1,330 · see citing works
The energetics of genome complexity.
Lane, N., & Martin, W. (2010) · Nature · doi:10.1038/nature09486 · Cited by 1,289 · see citing works
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 · see citing works
Corton, J. M., Gillespie, J. G., Hawley, S. A., & Hardie, D. G. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.tb20498.x · Cited by 1,232 · see citing works
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
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 · see citing works
Mitochondrial pathology and apoptotic muscle degeneration in <i>Drosophila parkin</i> mutants
Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0737556100 · Cited by 1,203 · see citing works
Microdomains of Intracellular Ca2+: Molecular Determinants and Functional Consequences
Rizzuto, R., & Pozzan, T. (2005) · Physiological Reviews · doi:10.1152/physrev.00004.2005 · Cited by 1,201 · see citing works
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200 · see citing works
Self-citationThe axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,198 · see citing works
Essential role for Nix in autophagic maturation of erythroid cells
Sandoval, H., Thiagarajan, P., Dasgupta, S. K., Schumacher, A., Prchal, J. T., Chen, M., & Wang, J. (2008) · Nature · doi:10.1038/nature07006 · Cited by 1,185 · see citing works
Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells
Ito, K., Hirao, A., Arai, F., Matsuoka, S., Takubo, K., Hamaguchi, I., Nomiyama, K., Hosokawa, K., Sakurada, K., Nakagata, N., et al. (2004) · Nature · doi:10.1038/nature02989 · Cited by 1,175 · cited 1× · see citing works
“Observations from premature aging mouse models suggest that hematopoietic progenitors are especially sensitive to ROS and/or redox state changes that promote proliferation and prevent quiescence (Ito et al., 2004; Narasimhaiah et al., 2005).”
BackgroundOlichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., & Lenaers, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200677200 · Cited by 1,168 · see citing works
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 1,161 · see citing works
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 1,144 · see citing works
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 · see citing works
The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity
Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · see citing works
HIF-independent regulation of VEGF and angiogenesis by the transcriptional coactivator PGC-1α
Arany, Z., Foo, S.-Y., Ma, Y., Ruas, J. L., Bommi-Reddy, A., Girnun, G., Cooper, M., Laznik, D., Chinsomboon, J., Rangwala, S. M., et al. (2008) · Nature · doi:10.1038/nature06613 · Cited by 1,054 · see citing works
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 · see citing works
Complex iii releases superoxide to both sides of the inner mitochondrial membrane
Muller, F. L., Liu, Y., & Van Remmen, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407715200 · Cited by 1,036 · see citing works
A mitochondrial specific stress response in mammalian cells
Zhao, Q., Wang, J., Levichkin, I. V., Stasinopoulos, S., Ryan, M. T., & Hoogenraad, N. J. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf445 · Cited by 1,026 · see citing works
Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
Hamanaka, R. B., & Chandel, N. S. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.002 · Cited by 1,011 · see citing works
A new mitochondrial disease associated with mitochondrial DNA heteroplasmy.
Holt, I. J., Harding, A. E., Petty, R., & MORGAN-HUGHES, J. A. (1990) · PubMed · Cited by 996 · see citing works
Broad activation of the ubiquitin–proteasome system by Parkin is critical for mitophagy
Chan, N. C., Salazar, A. M., Pham, A. H., Sweredoski, M. J., Kolawa, N. J., Graham, R. L. J., Hess, S., & Chan, D. C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr048 · Cited by 993 · see citing works
Inhibiting Mitochondrial Fission Protects the Heart Against Ischemia/Reperfusion Injury
Ong, S.-B., Subrayan, S., Lim, S. Y., Yellon, D. M., Davidson, S. M., & Hausenloy, D. J. (2010) · Circulation · doi:10.1161/circulationaha.109.906610 · Cited by 986 · see citing works
NIX is required for programmed mitochondrial clearance during reticulocyte maturation
Schweers, R. L., Zhang, J., Randall, M. S., Loyd, M. R., Li, W., Dorsey, F. C., Kundu, M., Opferman, J. T., Cleveland, J. L., Miller, J. L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708818104 · Cited by 939 · see citing works
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 · see citing works
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works
Gegg, M. E., Cooper, J. M., Chau, K.-Y., Rojo, M., Schapira, A. H. V., & Taanman, J.-W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq419 · Cited by 910 · see citing works
Stoichiometric coupling of brain glucose metabolism and glutamatergic neuronal activity.
Sibson, N. R., Dhankhar, A., Mason, G. F., Rothman, D. L., Behar, K. L., & Shulman, R. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.316 · Cited by 897 · see citing works
The proteome of Saccharomyces cerevisiae mitochondria
Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R. P., Meyer, H. E., Schönfisch, B., Perschil, I., Chacińska, A., Guiard, B., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135385100 · Cited by 895 · see citing works
Mootha, V. K., Bunkenborg, J., Olsen, J. V., Hjerrild, M., Wisniewski, J. R., Stahl, E., Bolouri, M. S., Ray, H. N., Sihag, S., Kamal, M., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00926-7 · Cited by 889 · see citing works
The PINK1/Parkin pathway regulates mitochondrial morphology
Poole, A. C., Thomas, R. E., Andrews, L. A., McBride, H. M., Whitworth, A. J., & Pallanck, L. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709336105 · Cited by 885 · see citing works
Kraytsberg, Y., Kudryavtseva, E., McKee, A. C., Geula, C., Kowall, N. W., & Khrapko, K. (2006) · Nature Genetics · doi:10.1038/ng1778 · Cited by 884 · see citing works
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871 · see citing works
Identification of a novel FGF, FGF-21, preferentially expressed in the liver
Nishimura, T., Nakatake, Y., Konishi, M., & Itoh, N. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00067-1 · Cited by 847 · see citing works
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 · see citing works
Van Goethem, G., Dermaut, B., Löfgren, A., Martin, J.-J., & Van Broeckhoven, C. (2001) · Nature Genetics · doi:10.1038/90034 · Cited by 841 · see citing works
Verstreken, P., Ly, C. V., Venken, K. J. T., Koh, T.-W., Zhou, Y., & Bellen, H. J. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.018 · Cited by 841 · see citing works
The ATP synthase is involved in generating mitochondrial cristae morphology
Paumard, P., Vaillier, J., Coulary, B., Schaëffer, J., Soubannier, V., Mueller, D. M., Brèthes, D., di Rago, J., & Velours, J. (2002) · The EMBO Journal · doi:10.1093/emboj/21.3.221 · Cited by 809 · see citing works
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 · see citing works
Self-citationMAM: more than just a housekeeper
Hayashi, T., Rizzuto, R., Hajnoczky, G., & Su, T.-P. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.12.002 · Cited by 787 · see citing works
The axonal transport of mitochondria
Hollenbeck, P. J., & Saxton, W. M. (2005) · Journal of Cell Science · doi:10.1242/jcs.02745 · Cited by 771 · see citing works
SLP‐2 is required for stress‐induced mitochondrial hyperfusion
Tondera, D., Grandemange, S., Jourdain, A. A., Karbowski, M., Mattenberger, Y., Herzig, S., Cruz, S. D., Clerc, P., Lauria, I., Merkwirth, C., et al. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.89 · Cited by 767 · see citing works
A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes
Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755 · see citing works
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749 · see citing works
Regulation of apoptosis by endoplasmic reticulum pathways
Breckenridge, D. G., Germain, M., Mathai, J. P., Nguyen, M., & Shore, G. C. (2003) · Oncogene · doi:10.1038/sj.onc.1207108 · Cited by 742 · see citing works
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W. G., D'adamio, L., et al. (2006) · Cell · doi:10.1016/j.cell.2006.06.021 · Cited by 735 · see citing works
<i>Drosophila</i> Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin
Ziviani, E., Tao, R. N., & Whitworth, A. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913485107 · Cited by 735 · see citing works
Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
Brooks, C., Wei, Q., Cho, S.-G., & Dong, Z. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37829 · Cited by 735 · see citing works
Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation
Koivunen, P., Lee, S., Duncan, C. G., Lopez, G., Lu, G., Ramkissoon, S., Losman, J. A., Joensuu, P., Bergmann, U., Gross, S., et al. (2012) · Nature · doi:10.1038/nature10898 · Cited by 727 · see citing works
Mitochondrial protein import: from proteomics to functional mechanisms
Schmidt, O., Pfanner, N., & Meisinger, C. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2959 · Cited by 717 · see citing works
Deng, H., Dodson, M. W., Huang, H., & Guo, M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803998105 · Cited by 683 · see citing works
Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses
MacAskill, A. F., Rinholm, J. E., Twelvetrees, A. E., Arancibia‐Cárcamo, I. L., Muir, J., Fransson, Å., Aspenström, P., Attwell, D., & Kittler, J. T. (2009) · Neuron · doi:10.1016/j.neuron.2009.01.030 · Cited by 677 · see citing works
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 · see citing works
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 · see citing works
Glater, E. E., Megeath, L. J., Stowers, R. S., & Schwarz, T. L. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200601067 · Cited by 667 · see citing works
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 · see citing works
Yoneda, T., Benedetti, C., Urano, F., Clark, S. G., Harding, H. P., & Ron, D. (2004) · Journal of Cell Science · doi:10.1242/jcs.01275 · Cited by 636 · see citing works
Role of Bax and Bak in mitochondrial morphogenesis
Karbowski, M., Norris, K. L., Cleland, M. M., Jeong, S.-Y., & Youle, R. J. (2006) · Nature · doi:10.1038/nature05111 · Cited by 625 · see citing works
Dnm1 forms spirals that are structurally tailored to fit mitochondria
Ingerman, E., Perkins, E. M., Marino, M., Mears, J. A., McCaffery, J. M., Hinshaw, J. E., & Nunnari, J. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200506078 · Cited by 621 · see citing works
Self-citationYoshii, S. R., Kishi, C., Ishihara, N., & Mizushima, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209338 · Cited by 612 · see citing works
Kang, J.-S., Tian, J.-H., Pan, P.-Y., Zald, P., Li, C., Deng, C., & Sheng, Z.-H. (2008) · Cell · doi:10.1016/j.cell.2007.11.024 · Cited by 598 · see citing works
Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 595 · see citing works
ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans
Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., & Ron, D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.016 · Cited by 595 · see citing works
Cargo-Selected Transport from the Mitochondria to Peroxisomes Is Mediated by Vesicular Carriers
Neuspiel, M., Schauss, A. C., Braschi, E., Zunino, R., Rippstein, P. U., Rachubinski, R. A., Andrade-Navarro, M. A., & McBride, H. M. (2008) · Current Biology · doi:10.1016/j.cub.2007.12.038 · Cited by 592 · see citing works
Making heads or tails of phospholipids in mitochondria
Osman, C., Voelker, D. R., & Langer, T. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201006159 · Cited by 580 · see citing works
Mitochondrial Fusion in Yeast Requires the Transmembrane GTPase Fzo1p
Hermann, G. J., Thatcher, J., Mills, J. P., Hales, K. G., Fuller, M., Nunnari, J., & Shaw, J. (1998) · Journal of Cell Biology · doi:10.1083/jcb.143.2.359 · Cited by 572 · see citing works
Self-citationRegulation of OPA1 processing and mitochondrial fusion by m -AAA protease isoenzymes and OMA1
Ehses, S., Lauria, I., Mancuso, G., Bernacchia, A., Geimer, S., Tondera, D., Martinou, J., Westermann, B., Rugarli, E. I., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906084 · Cited by 570 · see citing works
Mitochondria: The Next (Neurode)Generation
Schon, E. A., & Przedborski, S. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.003 · Cited by 568 · see citing works
Song, W., Chen, J., Petrilli, A. M., Liot, G., Klinglmayr, E., Zhou, Y., Poquiz, P., Tjong, J., Pouladi, M. A., Hayden, M. R., et al. (2011) · Nature Medicine · doi:10.1038/nm.2313 · Cited by 556 · see citing works
Luoma, P., Melberg, A., Rinne, J. O., Kaukonen, J. A., Nupponen, N. N., Chalmers, R. M., Oldfors, A., Rautakorpi, I., Peltonen, L., Majamaa, K., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16983-3 · Cited by 548 · see citing works
Self-citationBidirectional Ca <sup>2+</sup> -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 · see citing works
Strong Purifying Selection in Transmission of Mammalian Mitochondrial DNA
Stewart, J. B., Freyer, C., Elson, J. L., Wredenberg, A., Cansu, Z., Trifunović, A., & Larsson, N. (2008) · PLoS Biology · doi:10.1371/journal.pbio.0060010 · Cited by 525 · see citing works
Fis1 and Bap31 bridge the mitochondria–ER interface to establish a platform for apoptosis induction
Iwasawa, R., Mahul‐Mellier, A., Datler, C., Pazarentzos, E., & Grimm, S. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.346 · Cited by 520 · see citing works
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 519 · see citing works
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 · see citing works
Nunnari, J. M., Marshall, W. F., Straight, A. F., Murray, A., Sedat, J. W., & Walter, P. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.7.1233 · Cited by 514 · see citing works
Self-citationPostfertilization Autophagy of Sperm Organelles Prevents Paternal Mitochondrial DNA Transmission
Rawi, S. A., Louvet‐Vallée, S., Djeddi, A., Sachse, M., Culetto, E., Hajjar, C., Boyd, L., Legouis, R., & Galy, V. (2011) · Science · doi:10.1126/science.1211878 · Cited by 505 · see citing works
Depletion of muscle mitochondrial DNA in AIDS patients with zidovudine-induced myopathy
Arnaudo, E., Shanske, S., DiMauro, S., Schon, E. A., Moraes, C. T., Schon, E. A., & Dalakas, M. C. (1991) · The Lancet · doi:10.1016/0140-6736(91)91294-5 · Cited by 504 · see citing works
The mitochondrial UPR – protecting organelle protein homeostasis
Haynes, C. M., & Ron, D. (2010) · Journal of Cell Science · doi:10.1242/jcs.075119 · Cited by 490 · see citing works
Tatuch, Y., Christodoulou, J., Feigenbaum, A., Clarke, J. T. R., Wherret, J., Smith, C., Rudd, N., Petrova-Benedict, R., & Robinson, B. H. (1992) · PubMed · Cited by 483 · see citing works
The mitochondrial contact site complex, a determinant of mitochondrial architecture
Harner, M. E., Körner, C., Walther, D. M., Mokranjac, D., Kaesmacher, J., Welsch, U., Griffith, J. M., Mann, M., Reggiori, F., & Neupert, W. (2011) · EMBO Journal · doi:10.1038/emboj.2011.379 · Cited by 478 · see citing works
Bax and Bak Coalesce into Novel Mitochondria-Associated Clusters during Apoptosis
Nechushtan, A., Smith, C. L., Lamensdorf, I., Yoon, S., & Youle, R. J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.6.1265 · Cited by 477 · see citing works
Molecular Diagnosis of Infantile Mitochondrial Disease with Targeted Next-Generation Sequencing
Calvo, S. E., Compton, A. G., Hershman, S. G., Lim, S. C., Lieber, D. S., Tucker, E. J., Laskowski, A., Garone, C., Liu, S., Jaffe, D. B., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003310 · Cited by 476 · see citing works
Hoppins, S. C., Collins, S. R., Cassidy-Stone, A., Hummel, E., DeVay, R. M., Lackner, L. L., Westermann, B., Schuldiner, M., Weissman, J. S., & Nunnari, J. M. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201107053 · Cited by 473 · see citing works
Self-citationBaloh, R., Schmidt, R., Pestronk, A., & Milbrandt, J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4798-06.2007 · Cited by 471 · see citing works
Degradation of Paternal Mitochondria by Fertilization-Triggered Autophagy in C. elegans Embryos
Sato, M., & Sato, K. (2011) · Science · doi:10.1126/science.1210333 · Cited by 469 · see citing works
A mouse model of mitochondrial disease reveals germline selection against severe mtDNA mutations
Fan, W., Waymire, K. G., Narula, N., Li, P., Rocher, C., Coskun, P. E., Vannan, M. A., Narula, J., MacGregor, G. R., & Wallace, D. C. (2008) · Science · doi:10.1126/science.1147786 · Cited by 466 · see citing works
Scheper, G. C., van der Klok, T., van Andel, R. J., van Berkel, C. G. M., Sissler, M., Smet, J., Muravina, T. I., Sv, S., Uziel, G., Bugiani, M., et al. (2007) · Nature Genetics · doi:10.1038/ng2013 · Cited by 453 · see citing works
The Mitochondrial Fusion-Promoting Factor Mitofusin Is a Substrate of the PINK1/Parkin Pathway
Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., & Pallanck, L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010054 · Cited by 440 · see citing works
Hunger States Switch a Flip-Flop Memory Circuit via a Synaptic AMPK-Dependent Positive Feedback Loop
Yang, Y., Atasoy, D., Su, H. H., & Sternson, S. M. (2011) · Cell · doi:10.1016/j.cell.2011.07.039 · Cited by 439 · see citing works
Suomalainen, A., Elo, J. M., Pietiläinen, K. H., Hakonen, A. H., Sevastianova, K., Korpela, M., Isohanni, P., Marjavaara, S. K., Tyni, T., Kiuru-Enari, S., et al. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70155-7 · Cited by 427 · see citing works
Self-citationMembrane Remodeling Induced by the Dynamin-Related Protein Drp1 Stimulates Bax Oligomerization
Montessuit, S., Somasekharan, S. P., Terrones, O., Lucken‐Ardjomande, S., Herzig, S., Schwarzenbacher, R., Manstein, D. J., Bossy‐Wetzel, E., Basáñez, G., Meda, P., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.017 · Cited by 422 · see citing works
Loss of Parkin or PINK1 Function Increases Drp1-dependent Mitochondrial Fragmentation*
Lutz, A., Exner, N., Fett, M. E., Schlehe, J. S., Kloos, K., Lämmermann, K., Brunner, B., Kurz-Drexler, A., Vogel, F., Reichert, A., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035774 · Cited by 421 · see citing works
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 · see citing works
AMP-activated protein kinase: nature's energy sensor
Carling, D., Mayer, F. V., Sanders, M. J., & Gamblin, S. J. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.610 · Cited by 416 · see citing works
Parone, P. A., Da Cruz, S., Tondera, D., Mattenberger, Y., James, D. I., Maechler, P., Barja, F., & Martinou, J.-C. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003257 · Cited by 415 · see citing works
Dual Role of Mitofilin in Mitochondrial Membrane Organization and Protein Biogenesis
von der Malsburg, K., Müller, J. M., Bohnert, M., Oeljeklaus, S., Kwiatkowska, P., Becker, T., Łoniewska-Lwowska, A., Wiese, S., Rao, S., Milenkovic, D., et al. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.08.026 · Cited by 412 · see citing works
PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
Kim, Y. S., Park, J., Kim, S., Song, S., Kwon, S., Lee, S., Kitada, T., Kim, J., & Chung, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.104 · Cited by 389 · see citing works
Shirendeb, U. P., Calkins, M. J., Mańczak, M., Anekonda, V., Dufour, B. D., McBride, J. L., Mao, P., & Reddy, P. H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr475 · Cited by 383 · see citing works
Benedetti, C., Haynes, C. M., Yang, Y., Harding, H. P., & Ron, D. (2006) · Genetics · doi:10.1534/genetics.106.061580 · Cited by 382 · see citing works
Fibroblast Growth Factor 21-Deficient Mice Demonstrate Impaired Adaptation to Ketosis
Badman, M. K., Koester, A., Flier, J. S., Kharitonenkov, A., & Maratos-Flier, E. (2009) · Endocrinology · doi:10.1210/en.2009-0532 · Cited by 362 · see citing works
Hotta, Y., Nakamura, H., Konishi, M., Murata, Y., Takagi, H., Matsumura, S., Inoue, K., Fushiki, T., & Itoh, N. (2009) · Endocrinology · doi:10.1210/en.2009-0119 · Cited by 352 · see citing works
MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
Braschi, E., Zunino, R., & McBride, H. M. (2009) · EMBO Reports · doi:10.1038/embor.2009.86 · Cited by 350 · see citing works
Tyynismaa, H., Mjosund, K. P., Wanrooij, S., Lappalainen, I., Ylikallio, E., Jalanko, A., Spelbrink, J. N., Paetau, A., & Suomalainen, A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505551102 · Cited by 342 · see citing works
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 · see citing works
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Jagasia, R., Grote, P., Westermann, B., & Conradt, B. (2005) · Nature · doi:10.1038/nature03316 · Cited by 319 · see citing works
Claypool, S. M., Oktay, Y., Boontheung, P., Loo, J. A., & Koehler, C. M. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200801152 · Cited by 318 · see citing works
Hakonen, A. H., Heiskanen, S., Juvonen, V., Lappalainen, I., Luoma, P. T., Rantamäki, M., Goethem, G. V., Löfgren, A., Hackman, P., Paetau, A. E., et al. (2005) · The American Journal of Human Genetics · doi:10.1086/444548 · Cited by 309 · see citing works
Self-citationA Stress-Responsive System for Mitochondrial Protein Degradation
Heo, J.-M., Livnat-Levanon, N., Taylor, E. B., Jones, K. T., Dephoure, N., Ring, J., Xie, J., Brodsky, J. L., Madeo, F., Gygi, S. P., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.021 · Cited by 304 · see citing works
Mitochondrial myopathy induces a starvation-like response
Tyynismaa, H., Carroll, C. J., Raimundo, N., Ahola-Erkkilä, S., Wenz, T., Ruhanen, H., Guse, K., Hemminki, A., Peltola-Mjøsund, K. E., Tulkki, V., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq310 · Cited by 300 · see citing works
Self-citationMitochondrial 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 299 · see citing works
Pietiläinen, K. H., Naukkarinen, J., Rissanen, A., Saharinen, J., Ellonen, P., Keränen, H., Suomalainen, A., Götz, A., Suortti, T., Yki‐Järvinen, H., et al. (2008) · PLoS Medicine · doi:10.1371/journal.pmed.0050051 · Cited by 299 · see citing works
Self-citationSterky, F. H., Lee, S., Wibom, R., Olson, L., & Larsson, N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103295108 · Cited by 296 · see citing works
In Vivo Correction of COX Deficiency by Activation of the AMPK/PGC-1α Axis
Viscomi, C. F., Bottani, E., Civiletto, G., Cerutti, R., Moggio, M. G., Fagiolari, G., Schon, E. A., Lamperti, C., & Zeviani, M. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.04.011 · Cited by 291 · see citing works
Costa, V., Giacomello, M., Hudec, R., Lopreiato, R., Ermak, G., Lim, D., Malorni, W., Davies, K. J. A., Carafoli, E., & Scorrano, L. (2010) · EMBO Molecular Medicine · doi:10.1002/emmm.201000102 · Cited by 285 · see citing works
Mammalian Dynamin-like Protein DLP1 Tubulates Membranes
Yoon, Y., Pitts, K. R., & McNiven, M. A. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.9.2894 · Cited by 285 · see citing works
Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
DeVay, R. M., Domínguez‐Ramírez, L., Lackner, L. L., Hoppins, S. C., Stahlberg, H., & Nunnari, J. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200906098 · Cited by 276 · see citing works
Self-citationJin, H., May, M. M., Tranebjærg, L., et al. (1996) · Nature Genetics · doi:10.1038/ng1096-177 · Cited by 271 · see citing works
Plasticity of skeletal muscle mitochondria: structure and function.
HOPPELER, H., & FL??CK, M. (2003) · Medicine & Science in Sports & Exercise · doi:10.1097/00005768-200301000-00016 · Cited by 267 · see citing works
Characterization of PINK1 processing, stability, and subcellular localization
Lin, W., & Kang, U. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05398.x · Cited by 261 · see citing works
Götz, A., Tyynismaa, H., Euro, L., Ellonen, P., Hyötyläinen, T., Ojala, T. H., Hämäläinen, R. H., Tommiska, J., Raivio, T., Orešič, M., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.04.006 · Cited by 257 · see citing works
Self-citationPierce, S. B., Chisholm, K. M., Lynch, E. D., Lee, M. K., Walsh, T., Opitz, J. M., Li, W., Klevit, R. E., & King, M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103471108 · Cited by 255 · see citing works
Brown, T., Tkachuk, A. N., Shtengel, G., Kopek, B. G., Bogenhagen, D., Hess, H., & Clayton, D. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05694-11 · Cited by 254 · see citing works
Norddahl, G. L., Pronk, C. J., Wahlestedt, M., Sten, G., Nygren, J. M., Ugale, A., Sigvardsson, M., & Bryder, D. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.03.009 · Cited by 249 · see citing works
The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes
Hoppins, S. C., Edlich, F., Harwig, M. C., Banerjee, S., McCaffery, J. M., Youle, R. J., & Nunnari, J. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.11.030 · Cited by 243 · see citing works
Self-citationThe AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover
Xu, S., Peng, G., Wang, Y., Fang, S., & Karbowski, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-09-0748 · Cited by 243 · see citing works
Vyas, I. L., Heikkila, R. E., & Nicklas, W. J. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb01768.x · Cited by 242 · see citing works
A Molecular basis for human hypersensitivity of aminoglyscoside antibiotics
Hutchin, T. P., Haworth, L., Higashi, K., et al. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.18.4174 · Cited by 241 · see citing works
Ahlqvist, K. J., Hämäläinen, R. H., Yatsuga, S., Uutela, M., Terzioglu, M., Götz, A., Forsström, S., Salvén, P., Angers‐Loustau, A., Kopra, O., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2011.11.012 · Cited by 240 · see citing works
Self-citationDavey, K., Parboosingh, J. S., McLeod, D. R., Chan, A., Casey, R., Ferreira, P., Snyder, F. F., Bridge, P. J., & Bernier, F. P. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2005.036657 · Cited by 239 · see citing works
Decrease of 3243 A–>G mtDNA mutation from blood in MELAS syndrome: a longitudinal study
Rahman, S., Poulton, J., Marchington, D., & Suomalainen, A. (2001) · The American Journal of Human Genetics · doi:10.1086/316930 · Cited by 237 · see citing works
Tiranti, V., Savoia, A., Forti, F., d'Apolito, M., Centra, M., Rocchi, M., & Zeviani, M. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.4.615 · Cited by 230 · see citing works
Rotation and structure of FoF1-ATP synthase
Okuno, D., Iino, R., & Noji, H. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr049 · Cited by 220 · see citing works
Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells
Kim, K., Stevens, M. V., Akter, M. H., Rusk, S. E., Huang, R. J., Cohen, A., Noguchi, A. C., Springer, D., Bocharov, A. V., Eggerman, T. L., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44736 · Cited by 210 · see citing works
Tissue heterogeneity of the mammalian mitochondrial proteome
Johnson, D., Harris, R. A., French, S. A., Blair, P. V., You, J., Bemis, K. G., Wang, M., & Balaban, R. S. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00108.2006 · Cited by 209 · see citing works
Cui, M., Tang, X., Christian, W. V., Yoon, Y., & Tieu, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.066662 · Cited by 205 · see citing works
Dickey, A. S., & Strack, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3159-11.2011 · Cited by 197 · see citing works
Jeninga, E. H., Schoonjans, K., & Auwerx, J. H. (2010) · Oncogene · doi:10.1038/onc.2010.206 · Cited by 191 · see citing works
Ketogenic diet slows down mitochondrial myopathy progression in mice
Ahola, S., Carroll, C. J., Mjøsund, K., Tulkki, V., Mattila, I. M., Seppänen‐Laakso, T., Orešič, M., Tyynismaa, H., & Suomalainen, A. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq076 · Cited by 191 · see citing works
Self-citationAMP-activated protein kinase: Also regulated by ADP?
Hardie, D. G., Carling, D., & Gamblin, S. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.06.004 · Cited by 187 · see citing works
Mechanisms of mitochondrial diseases
Ylikallio, E., & Suomalainen, A. (2011) · Annals of Medicine · doi:10.3109/07853890.2011.598547 · Cited by 185 · see citing works
Self-citationKuramoto, N., Wilkins, M. E., Fairfax, B. P., Revilla-Sanchez, R., Terunuma, M., Tamaki, K., Takarada‐Iemata, M., Warren, N. A., Couve, A., Calver, A. R., et al. (2007) · Neuron · doi:10.1016/j.neuron.2006.12.015 · Cited by 184 · see citing works
Wurm, C. A., Neumann, D., Lauterbach, M. A., Harke, B., Egner, A., Hell, S. W., & Jakobs, S. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1107553108 · Cited by 173 · see citing works
Effects of OPA1 mutations on mitochondrial morphology and apoptosis: Relevance to ADOA pathogenesis
Olichon, A., Landes, T., Pelloquin, L., Emorine, L. J., Mils, V., Guichet, A., Delettre, C., Hamel, C., Amati‐Bonneau, P., Bonneau, D., et al. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20950 · Cited by 163 · see citing works
Mayr, J. A., Zimmermann, F., Fauth, C., et al. (2011) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2011.11.011 · Cited by 142 · see citing works
A Mutation in the Mitochondrial Fission Gene Dnm1l Leads to Cardiomyopathy
Ashrafian, H., Docherty, L., Leo, V., Towlson, C., Neilan, M., Steeples, V., Lygate, C. A., Hough, T., Townsend, S., Williams, D. J., et al. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001000 · Cited by 140 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680 · see citing works
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works
Mitochondrial form and function
Friedman, J. R., & Nunnari, J. (2014) · Nature · doi:10.1038/nature12985 · Cited by 1,803 · see citing works
Self-citationEndoplasmic reticulum-mitochondria contacts: Function of the junction
Rowland, A. A., & Voeltz, G. K. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3440 · Cited by 1,018 · see citing works
α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
Wong, Y. C., & Krainc, D. (2017) · Nature Medicine · doi:10.1038/nm.4269 · Cited by 897 · see citing works
Quirós, P. M., Prado, M. A., Zamboni, N., D’Amico, D., Williams, R. W., Finley, D., Gygi, S. P., & Auwerx, J. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201702058 · Cited by 832 · see citing works
The <i>i</i> -AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Anand, R., Wai, T., Baker, M. J., Kladt, N., Schauss, A. C., Rugarli, E., & Langer, T. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201308006 · Cited by 812 · see citing works
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817 · see citing works
Mitonuclear communication in homeostasis and stress
Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works
Mitochondria: master regulators of danger signalling
Galluzzi, L., Kepp, O., & Kroemer, G. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3479 · Cited by 733 · see citing works
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 · see citing works
Self-citationRoca, F. J., & Ramakrishnan, L. (2013) · Cell · doi:10.1016/j.cell.2013.03.022 · Cited by 592 · see citing works
Crosstalk between metabolism and circadian clocks
Reinke, H., & Asher, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0096-9 · Cited by 598 · see citing works
Mitochondria as signaling organelles
Chandel, N. S. (2014) · BMC Biology · doi:10.1186/1741-7007-12-34 · Cited by 576 · see citing works
Mitochondrial fission facilitates the selective mitophagy of protein aggregates
Burman, J. L., Pickles, S., Wang, C., Sekine, S., Vargas, J. N. S., Zhang, Z., Youle, A. M., Nezich, C. L., Wu, X., Hammer, J. A., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201612106 · Cited by 479 · see citing works
Chronic inflammation and the hallmarks of aging
Baechle, J. J., Chen, N., Makhijani, P., Winer, S., Furman, D., & Winer, D. A. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101755 · Cited by 471 · see citing works
Parkin‐independent mitophagy requires Drp1 and maintains the integrity of mammalian heart and brain
Kageyama, Y., Hoshijima, M., Seo, K., Bedja, D., Sysa‐Shah, P., Andrabi, S. A., Chen, W., Höke, A., Dawson, V. L., Dawson, T. M., et al. (2014) · The EMBO Journal · doi:10.15252/embj.201488658 · Cited by 420 · see citing works
Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3
Khan, N. A., Auranen, M., Paetau, I., Pirinen, E., Euro, L., Forsström, S., Pasila, L., Velagapudi, V., Carroll, C. J., Auwerx, J., et al. (2014) · EMBO Molecular Medicine · doi:10.1002/emmm.201403943 · Cited by 385 · see citing works
Self-citationPharmacological approaches to restore mitochondrial function
Andreux, P. A., Houtkooper, R. H., & Auwerx, J. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4023 · Cited by 383 · see citing works
Impaired Mitochondrial Biogenesis in Adipose Tissue in Acquired Obesity
Heinonen, S., Buzkova, J., Muniandy, M., Kaksonen, R., Ollikainen, M., Ismail, K., Hakkarainen, A., Lundbom, J., Lundbom, N., Vuolteenaho, K., et al. (2015) · Diabetes · doi:10.2337/db14-1937 · Cited by 362 · see citing works
Self-citationChakrabarti, R., Ji, W.-K., Stan, R. V., de Juan Sanz, J., Ryan, T. A., & Higgs, H. N. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709111 · Cited by 349 · see citing works
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351 · see citing works
“, Parkinson’s and Alzheimer’s disease) disorders [13].”
BackgroundGrowth differentiation factor 15 is a myomitokine governing systemic energy homeostasis
Chung, H. K., Ryu, D., Kim, K. S., Chang, J. Y., Kim, Y. K., Yi, H.-S., Kang, S. G., Choi, M. J., Lee, S. E., Jung, S.-B., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201607110 · Cited by 357 · see citing works
Jovaisaite, V., Mouchiroud, L., & Auwerx, J. (2014) · Journal of Experimental Biology · doi:10.1242/jeb.090738 · Cited by 335 · see citing works
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337 · see citing works
Mitochondrial dysfunction and cell senescence: deciphering a complex relationship
Chapman, J., Fielder, E., & Passos, J. F. (2019) · FEBS Letters · doi:10.1002/1873-3468.13498 · Cited by 325 · see citing works
Metabolic regulation of <scp>NLRP</scp> 3
Hughes, M. M., & O'Neill, L. A. J. (2018) · Immunological Reviews · doi:10.1111/imr.12608 · Cited by 311 · see citing works
Skeletal muscle insulin resistance: role of mitochondria and other ROS sources
Di Meo, S., Iossa, S., & Venditti, P. (2017) · Journal of Endocrinology · doi:10.1530/joe-16-0598 · Cited by 282 · see citing works
Humanin: a harbinger of mitochondrial-derived peptides
Lee, C., Yen, K., & Cohen, P. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.01.005 · Cited by 284 · see citing works
Forsström, S., Jackson, C. B., Carroll, C. J., Kuronen, M., Pirinen, E., Pradhan, S., Marmyleva, A., Auranen, M., Kleine, I.-M., Khan, N. A., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.08.019 · Cited by 252 · see citing works
Self-citationA neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1
Hertz, N. T., Berthet, A., Sos, M. L., Thorn, K. S., Burlingame, A. L., Nakamura, K., & Shokat, K. M. (2013) · Cell · doi:10.1016/j.cell.2013.07.030 · Cited by 275 · see citing works
Ribas, V., Drew, B. G., Zhou, Z., Phun, J., Kalajian, N. Y., Soleymani, T., Daraei, P., Widjaja, K., Wanagat, J., de Aguiar Vallim, T. Q., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad3815 · Cited by 259 · see citing works
Neufeld-Cohen, A., Robles, M. S., Aviram, R., Manella, G., Adamovich, Y., Ladeuix, B., Nir, D., Rousso-Noori, L., Kuperman, Y., Golik, M., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519650113 · Cited by 262 · see citing works
Gioscia‐Ryan, R. A., LaRocca, T. J., Sindler, A. L., Zigler, M. C., Murphy, M. P., & Seals, D. R. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2013.268680 · Cited by 263 · see citing works
The hallmarks of fibroblast ageing
Tigges, J., Krutmann, J., Fritsche, E., Haendeler, J., Schaal, H., Fischer, J. W., Kalfalah, F., Reinke, H., Reifenberger, G., Stühler, K., et al. (2014) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2014.03.004 · Cited by 250 · see citing works
Dela Cruz, C. S., & Kang, M.-J. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.12.001 · Cited by 255 · see citing works
Training-Induced Changes in Mitochondrial Content and Respiratory Function in Human Skeletal Muscle
Granata, C., Jamnick, N. A., & Bishop, D. J. (2018) · Sports Medicine · doi:10.1007/s40279-018-0936-y · Cited by 247 · see citing works
Fumarate is a terminal electron acceptor in the mammalian electron transport chain
Spinelli, J. B., Rosen, P. C., Sprenger, H.-G., Puszynska, A. M., Mann, J. L., Roessler, J. M., Cangelosi, A. L., Henne, A., Condon, K. J., Zhang, T., et al. (2021) · Science · doi:10.1126/science.abi7495 · Cited by 221 · see citing works
Altered mitochondrial function in insulin-deficient and insulin-resistant states
Ruegsegger, G. N., Creo, A. L., Cortes, T. M., Dasari, S., & Nair, K. S. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120843 · Cited by 202 · see citing works
Quantitative 3D Mapping of the Human Skeletal Muscle Mitochondrial Network
Vincent, A. E., White, K., Davey, T., Philips, J., Ogden, R. T., Lawless, C., Warren, C., Hall, M. G., Ng, Y. S., Falkous, G., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.010 · Cited by 195 · see citing works
Karunakaran, D., Thrush, A. B., Nguyen, M.-A., Richards, L., Geoffrion, M., Singaravelu, R., Ramphos, E., Shangari, P., Ouimet, M., Pezacki, J. P., et al. (2015) · Circulation Research · doi:10.1161/circresaha.117.305624 · Cited by 188 · see citing works
Bishop, D. J., Botella, J., Genders, A. J., Lee, M. J.-C., Saner, N. J., Kuang, J., Yan, X., & Granata, C. (2019) · Physiology · doi:10.1152/physiol.00038.2018 · Cited by 180 · see citing works
Milenkovic, D., Matic, S., Kuhl, I., Ruzzenente, B., Freyer, C., Jemt, E., Park, C. B., Falkenberg, M., & Larsson, N.-G. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt051 · Cited by 173 · see citing works
Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1
Bustillo-Zabalbeitia, I., Montessuit, S., Raemy, E., Basañez, G., Terrones, O., & Martinou, J.-C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102738 · Cited by 162 · see citing works
The Ubiquitin-Proteasome System Regulates Mitochondrial Intermembrane Space Proteins
Bragoszewski, P., Gornicka, A., Sztolsztener, M. E., & Chacinska, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01579-12 · Cited by 149 · see citing works
Kim, J., Fiesel, F. C., Belmonte, K. C., Hudec, R., Wang, W.-X., Kim, C., Nelson, P. T., Springer, W., & Kim, J. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0121-4 · Cited by 163 · see citing works
“Discussion Mitochondria play critical roles in a variety of cellular functions, such as energy production, calcium homeostasis, and apoptosis [44].”
BackgroundMitochondria: Are they causal players in cellular senescence?
Correia-Melo, C., & Passos, J. F. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.017 · Cited by 160 · see citing works
Mitochondrial DNA as an inflammatory mediator in cardiovascular diseases
Nakayama, H., & Otsu, K. (2018) · Biochemical Journal · doi:10.1042/bcj20170714 · Cited by 160 · see citing works
Picca, A., Lezza, A. M. S., Leeuwenburgh, C., Pesce, V., Calvani, R., Bossola, M., Manes-Gravina, E., Landi, F., Bernabei, R., & Marzetti, E. (2018) · Rejuvenation Research · doi:10.1089/rej.2017.1989 · Cited by 144 · see citing works
The mitochondrial unfolded protein response–synchronizing genomes
Jovaisaite, V., & Auwerx, J. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.003 · Cited by 131 · see citing works
Mitochondrial DNA damage and atherosclerosis
Yu, E. P. K., & Bennett, M. R. (2014) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2014.06.008 · Cited by 124 · see citing works
“We increasingly recognise that mtDNA defects not only impact upon mitochondrial and cellular function but whole organism metabolism [58] .”
BackgroundHartmann, B., Wai, T., Hu, H., MacVicar, T., Musante, L., Fischer-Zirnsak, B., Stenzel, W., Gräf, R., van den Heuvel, L., Ropers, H.-H., et al. (2016) · eLife · doi:10.7554/elife.16078 · Cited by 124 · see citing works
Mitophagy and cGAS–STING crosstalk in neuroinflammation
Zhou, X., Wang, J., Yu, L., Qiao, G., Qin, D., Yuen-Kwan Law, B., Ren, F., Wu, J., & Wu, A. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.05.012 · Cited by 131 · see citing works
Luna-Marco, C., Iannantuoni, F., Hermo-Argibay, A., Devos, D., Salazar, J. D., Víctor, V. M., & Rovira-Llopis, S. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.01.015 · Cited by 114 · see citing works
Blank, M. F., & Grummt, I. (2017) · Transcription · doi:10.1080/21541264.2016.1276658 · Cited by 111 · see citing works
Structural basis of mitochondrial transcription
Hillen, H. S., Temiakov, D., & Cramer, P. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0122-9 · Cited by 111 · see citing works
Mitochondrial calcium cycling in neuronal function and neurodegeneration
Walters, G. C., & Usachev, Y. M. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1094356 · Cited by 105 · see citing works
Granata, C., Caruana, N. J., Botella, J., Jamnick, N. A., Huynh, K., Kuang, J., Janssen, H. A., Reljic, B., Mellett, N. A., Laskowski, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27153-3 · Cited by 93 · see citing works
The role of mitochondria in rheumatic diseases
Becker, Y. L. C., Duvvuri, B., Fortin, P. R., Lood, C., & Boilard, E. (2022) · Nature Reviews Rheumatology · doi:10.1038/s41584-022-00834-z · Cited by 81 · see citing works
Little, A. C., Kovalenko, I., Goo, L. E., Hong, H. S., Kerk, S. A., Yates, J. A., Purohit, V., Lombard, D. B., Merajver, S. D., & Lyssiotis, C. A. (2020) · Communications Biology · doi:10.1038/s42003-020-0988-z · Cited by 88 · see citing works
Li, W., Ali, T., Zheng, C., He, K., Liu, Z., Shah, F. A., Li, N., Yu, Z.-J., & Li, S. (2022) · Molecular Psychiatry · doi:10.1038/s41380-021-01327-3 · Cited by 80 · see citing works
Cwerman-Thibault, H., Augustin, S., Lechauve, C., Ayache, J., Ellouze, S., Sahel, J.-A., & Corral-Debrinski, M. (2015) · Molecular Therapy - Methods & Clinical Development · doi:10.1038/mtm.2015.3 · Cited by 86 · see citing works
Calcium, Bioenergetics, and Parkinson’s Disease
Zampese, E., & Surmeier, D. J. (2020) · Cells · doi:10.3390/cells9092045 · Cited by 79 · see citing works
Orr, A. L., Ashok, D., Sarantos, M. R., Shi, T., Hughes, R. E., & Brand, M. D. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.170 · Cited by 80 · see citing works
Kravic, B., Harbauer, A. B., Romanello, V., Simeone, L., Vögtle, F.-N., Kaiser, T., Straubinger, M., Huraskin, D., Böttcher, M., Cerqua, C., et al. (2018) · Autophagy · doi:10.1080/15548627.2017.1403716 · Cited by 75 · see citing works
Polg2 is essential for mammalian embryogenesis and is required for mtDNA maintenance
Humble, M. M., Young, M. J., Foley, J. F., Pandiri, A. R., Travlos, G. S., & Copeland, W. C. (2013) · Human Molecular Genetics · doi:10.1093/hmg/dds506 · Cited by 78 · see citing works
Muscle mitochondrial stress adaptation operates independently of endogenous FGF21 action
Ost, M., Coleman, V., Voigt, A., van Schothorst, E. M., Keipert, S., van der Stelt, I., Ringel, S., Graja, A., Ambrosi, T., Kipp, A. P., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2015.11.002 · Cited by 75 · see citing works
Environmental exposure and mitochondrial epigenetics: study design and analytical challenges
Byun, H.-M., & Baccarelli, A. A. (2014) · Human Genetics · doi:10.1007/s00439-013-1417-x · Cited by 68 · see citing works
Mitochondria-Derived Peptide MOTS-c: Effects and Mechanisms Related to Stress, Metabolism and Aging
Wan, W., Zhang, L., Lin, Y., Rao, X., Wang, X., Hua, F., & Ying, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-03885-2 · Cited by 70 · see citing works
Mitochondrial health, the epigenome and healthspan
Aon, M. A., Cortassa, S., Juhaszova, M., & Sollott, S. J. (2016) · Clinical Science · doi:10.1042/cs20160002 · Cited by 66 · see citing works
Are mitochondria the Achilles’ heel of the Kingdom Fungi?
Chatre, L., & Ricchetti, M. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2014.05.001 · Cited by 66 · see citing works
Amino acid starvation has opposite effects on mitochondrial and cytosolic protein synthesis
Johnson, M. A., Vidoni, S., Durigon, R., Pearce, S. F., Rorbach, J., He, J., Brea-Calvo, G., Minczuk, M., Reyes, A., Holt, I. J., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093597 · Cited by 63 · see citing works
A novel lysosome‐to‐mitochondria signaling pathway disrupted by amyloid‐β oligomers
Norambuena, A., Wallrabe, H., Cao, R., Wang, D. B., Silva, A., Svindrych, Z., Periasamy, A., Hu, S., Tanzi, R. E., Kim, D. Y., et al. (2018) · The EMBO Journal · doi:10.15252/embj.2018100241 · Cited by 61 · see citing works
The C8ORF38 homologue Sicily is a cytosolic chaperone for a mitochondrial complex I subunit
Zhang, K., Li, Z., Jaiswal, M., Bayat, V., Xiong, B., Sandoval, H., Charng, W.-L., David, G., Haueter, C., Yamamoto, S., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201208033 · Cited by 58 · see citing works
El‐Khoury, R., Kemppainen, K. K., Dufour, E., Szibor, M., Jacobs, H. T., & Rustin, P. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12570 · Cited by 56 · see citing works
Qin, X., Wang, R., Xu, H., Tu, L., Chen, H., Li, H., Liu, N., Wang, J., Li, S., Yin, F., et al. (2022) · Autophagy · doi:10.1080/15548627.2021.2022360 · Cited by 55 · see citing works
Tian, S., Chen, X., Wu, W., Lin, H., Qing, X., Liu, S., Wang, B., Xiao, Y., Shao, Z., & Peng, Y. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01168-4 · Cited by 53 · see citing works
The systems biology of mitochondrial fission and fusion and implications for disease and aging
Chauhan, A., Vera, J., & Wolkenhauer, O. (2014) · Biogerontology · doi:10.1007/s10522-013-9474-z · Cited by 52 · see citing works
Biomedical Implants with Charge‐Transfer Monitoring and Regulating Abilities
Wang, D., Tan, J., Zhu, H., Mei, Y., & Liu, X. (2021) · Advanced Science · doi:10.1002/advs.202004393 · Cited by 49 · see citing works
Sevini, F., Giuliani, C., Vianello, D., Giampieri, E., Santoro, A., Biondi, F., Garagnani, P., Passarino, G., Luiselli, D., Capri, M., et al. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.022 · Cited by 46 · see citing works
Frijhoff, J., Dagnell, M., Augsten, M., Beltrami, E., Giorgio, M., & Östman, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.12.022 · Cited by 43 · see citing works
Pareek, G., Thomas, R. E., & Pallanck, L. J. (2018) · Cell Death & Disease · doi:10.1038/s41419-018-0365-8 · Cited by 42 · see citing works
Regulation of mitochondrial function by forkhead transcription factors
Jerome, M. S., Kuthethur, R., Kabekkodu, S. P., & Chakrabarty, S. (2022) · Biochimie · doi:10.1016/j.biochi.2022.03.013 · Cited by 33 · see citing works
Myostatin: a potential therapeutic target for metabolic syndrome
Yang, M., Liu, C., Jiang, N., Liu, Y., Luo, S., Li, C., Zhao, H., Han, Y., Chen, W., Li, L., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1181913 · Cited by 33 · see citing works
Cai, J., Chen, Y., She, Y., He, X., Feng, H., Sun, H., Yin, M., Gao, J., Sheng, C., Li, Q., et al. (2025) · Brain Pathology · doi:10.1111/bpa.13316 · Cited by 30 · see citing works
The anti-viral dynamin family member MxB participates in mitochondrial integrity
Cao, H., Krueger, E. W., Chen, J., Drizyte-Miller, K., Schulz, M. E., & McNiven, M. A. (2020) · Nature Communications · doi:10.1038/s41467-020-14727-w · Cited by 25 · see citing works
Mdivi-1 and mitochondrial fission: recent insights from fungal pathogens
Koch, B., & Traven, A. (2019) · Current Genetics · doi:10.1007/s00294-019-00942-6 · Cited by 26 · see citing works
Brain mapping: the (un)folding of striate cortex
Schira, M. M., Tyler, C. W., & Rosa, M. G. P. (2012) · Current Biology · doi:10.1016/j.cub.2012.11.003 · Cited by 22 · see citing works
The manifold role of the mitochondria in skeletal muscle insulin resistance
Cade, W. T. (2018) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0000000000000480 · Cited by 21 · see citing works
Wakita, M., Ito, K., Fujii, K., Sakamoto, D., Mikawa, T., Sugawara, S., Zhou, X., Park, J. H., Miyagawa, H., Motooka, D., et al. (2026) · Nature Aging · doi:10.1038/s43587-025-01057-z · Cited by 9 · see citing works
- Authors
- Nunnari, J., & Suomalainen, A.
- Affiliations
- University of California, Davis (US)
- University of Helsinki (FI)
- Corresponding author
- Nunnari, Jodi
- Suomalainen, Anu
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 148
- Issue
- 6
- Pages
- 1145-1159
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5381524
- OpenAlex
- W2131415852
- Cited by
- 3,479
- References
- 243
- Citations by year
- 2026: 290 · 2025: 372 · 2024: 418 · 2023: 313 · 2022: 316 · 2021: 292 · 2020: 277 · 2019: 213 · 2018: 193 · 2017: 182 · 2016: 163 · 2015: 150 · 2014: 147 · 2013: 108 · 2012: 43
- FWCI
- 12.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Jane ja Aatos Erkon Säätiö
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062942, R01GM097432)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- mitochondria, mitochondrial dysfunction, ATP production, biosynthetic intermediates, autophagy, apoptosis, mitochondrial dynamics, intercellular communication, neurodegenerative diseases, metabolic disorders
- MeSH terms
- Animals, Autophagy, Humans, Mitochondria, Apoptosis, Neurodegenerative Diseases, Mitochondrial Diseases
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