The DOI matches its Crossref record; 123 of the 123 references it cites were found in a registry or an index.
Mitochondria: More Than Just a Powerhouse
Open accessAbstract
Pioneering biochemical studies have long forged the concept that the mitochondria are the 'energy powerhouse of the cell'. These studies, combined with the unique evolutionary origin of the mitochondria, led the way to decades of research focusing on the organelle as an essential, yet independent, functional component of the cell. Recently, however, our conceptual view of this isolated organelle has been profoundly altered with the discovery that mitochondria function within an integrated reticulum that is continually remodeled by both fusion and fission events. The identification of a number of proteins that regulate these activities is beginning to provide mechanistic details of mitochondrial membrane remodeling. However, the broader question remains regarding the underlying purpose of mitochondrial dynamics and the translation of these morphological transitions into altered functional output. One hypothesis has been that mitochondrial respiration and metabolism may be spatially and temporally regulated by the architecture and positioning of the organelle. Recent evidence supports and expands this idea by demonstrating that mitochondria are an integral part of multiple cell signaling cascades. Interestingly, proteins such as GTPases, kinases and phosphatases are involved in bi-directional communication between the mitochondrial reticulum and the rest of the cell. These proteins link mitochondrial function and dynamics to the regulation of metabolism, cell-cycle control, development, antiviral responses and cell death. In this review we will highlight the emerging evidence that provides molecular definition to mitochondria as a central platform in the execution of diverse cellular events.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Normally, mitochondria use electrons from different carbon sources to generate a proton gradient across the inner mitochondrial membrane. The energy of this gradient is used to generate ATP (9, 30).”
From Mitochondrial Dysfunction Contributes to Oncogene-Induced Senescence (2009) · cites this paper as [30]
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Hereditary Early-Onset Parkinson's Disease Caused by Mutations in PINK1
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
Rab proteins as membrane organizers
Zerial, M., & McBride, H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052055 · Cited by 3,381
Self-citationSeth, R. B., Sun, L., Ea, C.-K., & Chen, Z. J. (2005) · Cell · doi:10.1016/j.cell.2005.08.012 · Cited by 3,329
Critical nodes in signalling pathways: insights into insulin action
Taniguchi, C. M., Emanuelli, B., & Kahn, C. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1837 · Cited by 2,760
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
IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction
Kawai, T., Takahashi, K., Sato, S., Coban, C., Kumar, H., Kato, H., Ishii, K. J., Takeuchi, O., & Akira, S. (2005) · Nature Immunology · doi:10.1038/ni1243 · Cited by 2,562
Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
Meylan, E., Curran, J., Hofmann, K., Moradpour, D., Binder, M., Bartenschlager, R., & Tschopp, J. (2005) · Nature · doi:10.1038/nature04193 · Cited by 2,401
The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
Dynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Flagged first, then by citations
Cited by
Sorted by citations
Recent Strategies to Develop Innovative Photosensitizers for Enhanced Photodynamic Therapy
Pham, T. C., Nguyen, V.-N., Choi, Y., Lee, S., & Yoon, J. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00381 · Cited by 1,813
Mitochondrial dynamics: overview of molecular mechanisms
Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397
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
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
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
Mitochondrial Dynamics in Mammalian Health and Disease
Liesa, M., Palacín, M., & Zorzano, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00030.2008 · Cited by 953
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
Self-citationCross talk between mitochondria and NADPH oxidases
Dikalov, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.06.033 · Cited by 783
The role of mitochondria in apoptosis
Jeong, S., & Seol, D. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.1.011 · Cited by 776
Bioenergetic role of mitochondrial fusion and fission
Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687
Surface chemistry and aspect ratio mediated cellular uptake of Au nanorods
Qiu, Y., Liu, Y., Wang, L., Xu, L., Bai, R., Ji, Y., Wu, X., Zhao, Y., Li, Y., & Chen, C. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.06.051 · Cited by 691
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
Lopresti, A. L., Hood, S. D., & Drummond, P. D. (2013) · Journal of Affective Disorders · doi:10.1016/j.jad.2013.01.014 · Cited by 724
Mitochondrial signal transduction
Picard, M. A., & Shirihai, O. S. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.10.008 · Cited by 688
“As echoed by others, 44,45 the ‘‘powerhouse’’ analogy promotes an overly simplistic picture of this beautifully complex organ-elle.”
BackgroundThe role of mitochondrial dysfunction in sepsis-induced multi-organ failure
Singer, M. (2013) · Virulence · doi:10.4161/viru.26907 · Cited by 638
Mitochondria in health, disease, and aging
Harrington, J. S., Ryter, S. W., Plataki, M. E., Price, D. R., & Choi, A. M. K. (2023) · Physiological Reviews · doi:10.1152/physrev.00058.2021 · Cited by 641
Burgos‐Morón, E., Abad‐Jiménez, Z., Marañón, A., Iannantuoni, F., Escribano‐López, I., López‐Domènech, S., Salom, C., Jover, A., Llabata, V. M., Torres, I. R., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8091385 · Cited by 612
“In fact, mitochondria are the main source of reactive oxygen species (ROS) and participate in redox homeostasis and other functions, such as apoptosis and Ca2+ metabolism [3,4] and ATP (adenosine triphosphate) production or heat generation.”
BackgroundMitochondrial-nuclear communications
Ryan, M. T., & Hoogenraad, N. J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052305.091720 · Cited by 575
Merkwirth, C., Dargazanli, S., Tatsuta, T., Geimer, S., Löwer, B., Wunderlich, F. T., von Kleist-Retzow, J., Waisman, A., Westermann, B., & Langer, T. (2008) · Genes & Development · doi:10.1101/gad.460708 · Cited by 535
Quality control of mitochondria: protection against neurodegeneration and ageing
Tatsuta, T., & Langer, T. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601972 · Cited by 525
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 537
Self-citationNew insights into the function and regulation of mitochondrial fission
Otera, H., Ishihara, N., & Mihara, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.002 · Cited by 501
The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
Karbowski, M., Neutzner, A., & Youle, R. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200611064 · Cited by 485
Stowe, D. F., & Camara, A. K. S. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2331 · Cited by 471
Comprehensive molecular characterization of mitochondrial genomes in human cancers
Yuan, Y., Ju, Y. S., Kim, Y.-W., Li, J., Wang, Y., Yoon, S.-S., Yang, J. Y. H., Martincorena, I., Creighton, C. J., Weinstein, J. N., et al. (2020) · Nature Genetics · doi:10.1038/s41588-019-0557-x · Cited by 485
“This may be interlinked with the general inadequacy of mitochondrial quality control and resultant increase in the steady state mtDNA copy number, as seen in renal oncocytoma 37 .”
The Role of Autophagy in Parkinson's DiseasePreprint
Lynch-Day, M. A., Mao, K., Wang, K., Zhao, M., & Klionsky, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a009357 · Cited by 477
Dong, S., Liang, S., Cheng, Z., Zhang, X., Luo, L., Li, L., Zhang, W., Li, S., Xu, Q., Zhong, M., et al. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02229-6 · Cited by 466
“from OXPHOS to alternative pathways Mitochondria are the center of cellular energy metabolism [23].”
BackgroundWang, K., Long, B., Zhou, L., Liu, F., Zhou, Q., Liu, C.-Y., Fan, Y.-Y., & Li, P. (2014) · Nature Communications · doi:10.1038/ncomms4596 · Cited by 456
Kanda, A., Chen, W., Othman, M., Branham, K. E. H., Brooks, M., Khanna, R., He, S., Lyons, R., Abecasis, G. R., & Swaroop, A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703933104 · Cited by 441
Wang, Y., Nartiss, Y., Steipe, B., McQuibban, G. A., & Kim, P. K. (2012) · Autophagy · doi:10.4161/auto.21211 · Cited by 438
Mitochondria: from cell death executioners to regulators of cell differentiation
Kasahara, A., & Scorrano, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.08.005 · Cited by 433
Wu, S., Zhou, F., Zhang, Z., & Xing, D. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08010.x · Cited by 423
Tian, J., Ban, X., Zeng, H. M., He, J., Chen, Y., & Wang, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030147 · Cited by 425
Mitochondrial Dysfunction Contributes to Oncogene-Induced Senescence
Moiseeva, O., Bourdeau, V., Roux, A., Deschênes-Simard, X., & Ferbeyre, G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01868-08 · Cited by 408
Calcium signaling around Mitochondria Associated Membranes (MAMs)
Patergnani, S., Suski, J. M., Agnoletto, C., Bononi, A., Bonora, M., Marchi, E. D., Giorgi, C., Marchi, S., Missiroli, S., Poletti, F., et al. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-19 · Cited by 422
Mitochondria removal by autophagy
Wang, K., & Klionsky, D. J. (2011) · Autophagy · doi:10.4161/auto.7.3.14502 · Cited by 380
Merkwirth, C., & Langer, T. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.05.013 · Cited by 413
Mitochondrial dynamics: regulatory mechanisms and emerging role in renal pathophysiology
Zhan, M., Brooks, C. R., Liu, F., Sun, L., & Dong, Z. (2013) · Kidney International · doi:10.1038/ki.2012.441 · Cited by 401
Effects of ionizing radiation on mitochondria
Kam, W. W.-Y., & Banati, R. B. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.024 · Cited by 386
Jin, H., Kanthasamy, A., Ghosh, A., Anantharam, V., Kalyanaraman, B., & Kanthasamy, A. G. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.007 · Cited by 373
Li, J., Donath, S., Li, Y., Qin, D., Prabhakar, B. S., & Li, P. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000795 · Cited by 363
Moore, A. S., & Holzbaur, E. L. F. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1523810113 · Cited by 362
“M form interconnected networks that continuously remodel in response to shifting cellular needs (1).”
BackgroundMitochondria: The calcium connection
Contreras, L., Drago, I., Zampese, E., & Pozzan, T. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.05.005 · Cited by 363
Spinocerebellar ataxia: an update
Sullivan, R., Yau, W. Y., O’Connor, E., & Houlden, H. (2018) · Journal of Neurology · doi:10.1007/s00415-018-9076-4 · Cited by 368
Mitochondria and Mood: Mitochondrial Dysfunction as a Key Player in the Manifestation of Depression
Allen, J., Romay-Tallón, R., Brymer, K. J., Caruncho, H. J., & Kalynchuk, L. E. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00386 · Cited by 362
“In addition, mitochondria also play a prominent role in the regulation of apoptotic cell death (for examples, see Davidson and Hardison, 1984; Herrmann and Neupert, 2000; Calabrese et al., 2001; Chan, 2006; Chipuk et al., 2006; Fattal et al., 2006; McBride et al., 2006; Youle and van der Bliek, 2012; Tobe, 2013; Bansa…”
BackgroundMitochondrial ‘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
Fisicaro, P., Barili, V., Montanini, B., Acerbi, G., Ferracin, M., Guerrieri, F., Salerno, D., Boni, C., Massari, M., Cavallo, M. C., et al. (2017) · Nature Medicine · doi:10.1038/nm.4275 · Cited by 356
Wang, X., Su, B., Fujioka, H., & Zhu, X. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071208 · Cited by 341
Membrane curvature in cell biology: An integration of molecular mechanisms
Jarsch, I. K., Daste, F., & Gallop, J. L. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201604003 · Cited by 339
“The major function of mitochondria is to provide energy to cells through oxidative phosphorylation (McBride et al., 2006).”
BackgroundMandal, S., Lindgren, A., Srivastava, A., Clark, A. T., & Banerjee, U. K. (2010) · Stem Cells · doi:10.1002/stem.590 · Cited by 328
Mitochondrial Structure and Function Are Disrupted by Standard Isolation Methods
Picard, M. A., Taivassalo, T., Ritchie, D., Wright, K. J., Thomas, M. M., Romestaing, C., & Hepple, R. T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018317 · Cited by 336
Cell-type-specific profiling of brain mitochondria reveals functional and molecular diversity
Fecher, C., Trovò, L., Müller, S. A., Snaidero, N., Wettmarshausen, J., Heink, S., Ortiz, O., Wagner, I., Kühn, R., Hartmann, J., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0479-z · Cited by 330
Resveratrol nanoformulations: Challenges and opportunities
Summerlin, N., Soo, E., Thakur, S. S., Qu, Z., Jambhrunkar, S., & Popat, A. (2015) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2015.01.003 · Cited by 319
Mitochondrial dynamics regulate the RIG-I-like receptor antiviral pathway
Castanier, C., Garcin, D., Vazquez, A., & Arnoult, D. (2010) · The EMBO Reports · doi:10.1038/embor.2009.258 · Cited by 316
Vps35 Mediates Vesicle Transport between the Mitochondria and Peroxisomes
Braschi, E., Goyon, V., Zunino, R., Mohanty, A., Xu, L., & McBride, H. M. (2010) · Current Biology · doi:10.1016/j.cub.2010.05.066 · Cited by 308
Self-citationIncreasing role of the cancer chemotherapeutic doxorubicin in cellular metabolism
Meredith, A., & Dass, C. (2016) · The Journal of pharmacy and pharmacology · doi:10.1111/jphp.12539 · Cited by 283
Bullón, P., Newman, H. N., & Battino, M. A. (2013) · Periodontology 2000 · doi:10.1111/j.1600-0757.2012.00455.x · Cited by 309
Besserer, A., Bécard, G., Jauneau, A., Roux, C. P., & Séjalon‐Delmas, N. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.121400 · Cited by 316
Osman, C., Haag, M., Potting, C., Rodenfels, J., Dip, P. V., Wieland, F., Brügger, B., Westermann, B., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810189 · Cited by 301
Jiang, L., Li, L., He, X., Yi, Q., He, B., Cao, J., Pan, W., & Gu, Z. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.02.004 · Cited by 297
Zhu, J., Wang, K. Z. Q., & Chu, C. T. (2013) · Autophagy · doi:10.4161/auto.24135 · Cited by 303
Fluorescent probes for the selective detection of chemical species inside mitochondria
Xu, Z., & Xu, L. S. (2015) · Chemical Communications · doi:10.1039/c5cc09248e · Cited by 291
Crosstalk between mitochondrial biogenesis and mitophagy to maintain mitochondrial homeostasis
Liu, L., Li, Y., Chen, G., & Chen, Q. (2023) · Journal of Biomedical Science · doi:10.1186/s12929-023-00975-7 · Cited by 322
Sirtuins and Type 2 Diabetes: Role in Inflammation, Oxidative Stress, and Mitochondrial Function
Kitada, M., Ogura, Y., Monno, I., & Koya, D. (2019) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00187 · Cited by 298
Liu, J., Chen, Y., Li, G., Zhang, P., Jin, C., Zeng, L., Ji, L., & Chao, H. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.04.002 · Cited by 281
The role of abnormal mitochondrial dynamics in the pathogenesis of Alzheimer’s disease
Wang, X., Su, B., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05867.x · Cited by 284
Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease
Dodson, M. W., & Guo, M. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.04.010 · Cited by 281
Lee, J. H., Park, A., Oh, K., Lee, S. C., Kim, W. K., & Bae, K. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194924 · Cited by 280
Recent advances in our understanding of neurodegeneration
Jellinger, K. A. (2009) · Journal of Neural Transmission · doi:10.1007/s00702-009-0240-y · Cited by 274
Plant Mitochondrial Recombination Surveillance Requires Unusual RecA and MutS Homologs
Shedge, V., Arrieta-Montiel, M. P., Christensen, A. C., & Mackenzie, S. A. (2007) · The Plant Cell · doi:10.1105/tpc.106.048355 · Cited by 272
Genetic aspects of mitochondrial genome evolution
Bernt, M., Braband, A., Schierwater, B., & Stadler, P. F. (2012) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2012.10.020 · Cited by 270
Abnormalities in Mitochondrial Structure in Cells from Patients with Bipolar Disorder
Cataldo, A. M., McPhie, D. L., Lange, N. T., Punzell, S., Elmiligy, S., Ye, N., Froimowitz, M. P., Hassinger, L. C., Menesale, E. B., Sargent, L. W., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.081068 · Cited by 279
Cyclin B1/CDK1-regulated mitochondrial bioenergetics in cell cycle progression and tumor resistance
Xie, B., Wang, S., Jiang, N., & Li, J. J. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.11.019 · Cited by 268
“OXPHOS supplies more than 90% of cellular ATP required for eukaryotic cells [87], and it is irrefutably critical for the progression of cell cycle as the level of ATP determines whether cells are ready for division [88].”
BackgroundThe SUMO protease SENP5 is required to maintain mitochondrial morphology and function
Zunino, R., Schauss, A. C., Rippstein, P. U., Andrade-Navarro, M. A., & McBride, H. M. (2007) · Journal of Cell Science · doi:10.1242/jcs.03418 · Cited by 262
Self-citationFatty acid oxidation is required for the respiration and proliferation of malignant glioma cells
Lin, H., Patel, S., Affleck, V., Wilson, I., Turnbull, D. M., Joshi, A. R., Maxwell, R. J., & Stoll, E. A. (2016) · Neuro-Oncology · doi:10.1093/neuonc/now128 · Cited by 258
Jiang, N., Fan, J., Xu, F., Peng, X., Mu, H., Wang, J., & Xiong, X. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201410645 · Cited by 259
Molecular mechanisms and physiologic functions of mitochondrial dynamics
Otera, H., & Mihara, K. (2011) · The Journal of Biochemistry · doi:10.1093/jb/mvr002 · Cited by 265
Protein Degradation within Mitochondria: Versatile Activities of AAA Proteases and Other Peptidases
Koppen, M., & Langer, T. (2007) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230701380452 · Cited by 252
Impairing the Mitochondrial Fission and Fusion Balance: A New Mechanism of Neurodegeneration
Knott, A. B., & Bossy‐Wetzel, E. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1427.030 · Cited by 263
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250
Mitochondrial protein acetylation regulates metabolism
Anderson, K. A., & Hirschey, M. D. (2012) · Essays in Biochemistry · doi:10.1042/bse0520023 · Cited by 249
Calcium Transport and Signaling in Mitochondria
Bravo, R., Parra, V., López‐Crisosto, C., Díaz, P., Quest, A. F. G., & Lavandero, S. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160013 · Cited by 304
“Moreover, the IMM possesses invaginations, the so-called mitochondrial cristae, which contain the electron transport chain (ETC) complexes (34,57,59).”
Regulation of mitochondrial morphology and function by stearoylation of TFR1
Senyilmaz, D., Virtue, S., Xu, X., Tan, C. Y., Griffin, J. L., Miller, A. K., Vidal‐Puig, A., & Teleman, A. A. (2015) · Nature · doi:10.1038/nature14601 · Cited by 253
Yoshizumi, T., Ichinohe, T., Sasaki, O., Otera, H., Kawabata, S.-I., Mihara, K., & Koshiba, T. (2014) · Nature Communications · doi:10.1038/ncomms5713 · Cited by 257
Mitochondrial Respiration Regulates Adipogenic Differentiation of Human Mesenchymal Stem Cells
Zhang, Y., Marsboom, G., Tóth, P. T., & Rehman, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077077 · Cited by 250
Mitochondrial dysfunction in neurodegenerative diseases and cancer
de Moura, M. B., Santana‐Santos, L., & Houten, B. V. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20575 · Cited by 247
Kuznetsov, A. V., & Margreiter, R. (2009) · International Journal of Molecular Sciences · doi:10.3390/ijms10041911 · Cited by 251
Wang, F., Zhang, Y., Liu, Z., Du, Z., Zhang, L., Ren, J., & Qu, X. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201901760 · Cited by 242
Bioenergetics of the failing heart
Ventura‐Clapier, R., Garnier, A., Veksler, V., & Joubert, F. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2010.09.006 · Cited by 254
Liu, Y., Zhou, J., Wang, L., Hu, X., Liu, X., Liu, M., Cao, Z. C., Shangguan, D., & Tan, W. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b04048 · Cited by 237
PARP-1 involvement in neurodegeneration: A focus on Alzheimer’s and Parkinson’s diseases
Martire, S., Mosca, L., & D’Erme, M. (2015) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2015.04.001 · Cited by 228
Lavrov, D. V., & Pett, W. (2016) · Genome Biology and Evolution · doi:10.1093/gbe/evw195 · Cited by 234
“…oxidative phosphorylation, mitochondria perform a variety of additional cellular functions, such as biosynthesis of amino acids and steroids, b-oxidation of fatty acids, FeS metabolism, and initiation of apoptosis (Mcbride et al. 2006; Pagliarini and Rutter 2013; Chandel 2014; Birsoy et al. 2015).”
BackgroundmiR-484 regulates mitochondrial network through targeting Fis1
Wang, K., Long, B., Jiao, J.-Q., Wang, J., Liu, J., Li, Q., & Li, P. (2012) · Nature Communications · doi:10.1038/ncomms1770 · Cited by 230
Morciano, G., Giorgi, C., Bonora, M., Punzetti, S., Pavasini, R., Wieckowski, M. R., Campo, G. C., & Pinton, P. (2014) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2014.08.015 · Cited by 232
Ban-Ishihara, R., Ishihara, T., Sasaki, N., Mihara, K., & Ishihara, N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301951110 · Cited by 231
Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer’s disease
Atamna, H., & Frey, W. H. (2007) · Mitochondrion · doi:10.1016/j.mito.2007.06.001 · Cited by 278
Mitochondrial dysfunction in fatty acid oxidation disorders: insights from human and animal studies
Wajner, M., & Amaral, A. U. (2015) · Bioscience Reports · doi:10.1042/bsr20150240 · Cited by 230
VDAC1 at the Intersection of Cell Metabolism, Apoptosis, and Diseases
Shoshan‐Barmatz, V., Shteinfer‐Kuzmine, A., & Verma, A. (2020) · Biomolecules · doi:10.3390/biom10111485 · Cited by 246
Grasso, D., Zampieri, L. X., Capelôa, T., de Velde, J. A. V., & Sonveaux, P. (2020) · Cell Stress · doi:10.15698/cst2020.06.221 · Cited by 239
“pact that these organelles have in multiple vital processes in eukaryotic cells [28].”
BackgroundDoblado, L., Lueck, C., Rey, C., Samhan-Arias, A. K., Priéto, I., Stacchiotti, A., & Monsalve, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22083903 · Cited by 238
Metadata
- Authors
- McBride, H. M., Neuspiel, M., & Wasiak, S.
- Affiliations
- Ottawa Heart Institute (CA)
- Corresponding author
- McBride, Heidi M.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2006-07
- Volume
- 16
- Issue
- 14
- Pages
- R551-R560
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2084034472
- Cited by
- 1,985
- References
- 123
- Citations by year
- 2026: 48 · 2025: 95 · 2024: 129 · 2023: 126 · 2022: 127 · 2021: 132 · 2020: 130 · 2019: 102 · 2018: 97 · 2017: 125 · 2016: 126 · 2015: 115 · 2014: 100 · 2013: 116 · 2012: 92
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2573 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- mitochondria, mitochondrial dynamics, mitochondrial fusion, mitochondrial fission, mitochondrial reticulum, mitochondrial membrane remodeling, mitochondrial respiration, mitochondrial metabolism, signal transduction, GTPase, kinases, phosphatase, cell death, cell cycle regulation, antiviral response, organelle positioning
- MeSH terms
- Cell Division, Mitochondria, Models, Biological, Neurons, Phosphoric Monoester Hydrolases, Protein Kinases, Signal Transduction, Tumor Suppressor Protein p53, NF-kappa B, Apoptosis, ras Proteins, Mitochondrial Proteins, Mitochondrial Membranes
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