The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Roles of mitochondria in human disease
Abstract
The chapters throughout this volume illustrate the many contributions of mitochondria to the maintenance of normal cell and tissue function, experienced as the health of the individual. Mitochondria are essential for maintaining aspects of physiology as fundamental as cellular energy balance, the modulation of calcium signalling, in defining cellular redox balance, and they house significant biosynthetic pathways. Mitochondrial numbers and volume within cells are regulated and have an impact on their functional roles, while, especially in the CNS (central nervous system), mitochondrial trafficking is critical to ensure the cellular distribution and strategic localization of mitochondria, presumably driven by local energy demand. Maintenance of a healthy mitochondrial population involves a complex system of quality control, involving degrading misfolded proteins, while damaged mitochondria are renewed by fusion or removed by autophagy. It seems evident that mechanisms that impair any of these processes will impair mitochondrial function and cell signalling pathways, leading to disordered cell function which manifests as disease. As gatekeepers of cell life and cell death, mitochondria regulate both apoptotic and necrotic cell death, and so at its most extreme, disturbances involving these pathways may trigger untimely cell death. Conversely, the lack of appropriate cell death can lead to inappropriate tissue growth and development of tumours, which are also characterized by altered mitochondrial metabolism. The centrality of mitochondrial dysfunction to a surprisingly wide range of major human diseases is slowly becoming recognized, bringing with it the prospect of novel therapeutic approaches to treat a multitude of unpleasant and pervasive diseases.
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Citations
Cites
The Biology of Cancer: Metabolic Reprogramming Fuels Cell Growth and Proliferation
DeBerardinis, R. J., Lum, J. J., Hatzivassiliou, G., & Thompson, C. B. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.002 · Cited by 4,088
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
Tumor cell metabolism: cancer's Achilles' heel
Kroemer, G., & Pouyssegur, J. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.05.005 · Cited by 2,337
Baines, C. P., Kaiser, R. A., Purcell, N. H., Blair, N. S., Osinska, H., Hambleton, M. A., Brunskill, E. W., Sayen, M. R., Gottlieb, R. A., Dorn, G. W., et al. (2005) · Nature · doi:10.1038/nature03434 · Cited by 2,280
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
Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
Scherz‐Shouval, R., Shvets, E., Fass, E., Shorer, H., Gil, L., & Elazar, Z. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601623 · Cited by 2,101
Lees, A. J., Hardy, J., & Revesz, T. (2009) · The Lancet · doi:10.1016/s0140-6736(09)60492-x · Cited by 1,956
The p66shc adaptor protein controls oxidative stress response and life span in mammals
Migliaccio, E., Giorgio, M., Mele, S., Pelicci, G., Reboldi, P., Pandolfi, P. P., Lanfrancone, L., & Pelicci, P. G. (1999) · Nature · doi:10.1038/46311 · Cited by 1,712
Transcriptional paradigms in mammalian mitochondrial biogenesis and function
Scarpulla, R. C. (2008) · Physiological Reviews · doi:10.1152/physrev.00025.2007 · Cited by 1,666
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
ROS-Generating Mitochondrial DNA Mutations Can Regulate Tumor Cell Metastasis
Ishikawa, K., Takenaga, K., Akimoto, M., Koshikawa, N., Yamaguchi, A., Imanishi, H., Nakada, K., Honma, Y., & Hayashi, J.-I. (2008) · Science · doi:10.1126/science.1156906 · Cited by 1,444
Functions and dysfunctions of mitochondrial dynamics
Detmer, S. A., & Chan, D. C. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2275 · Cited by 1,369
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270 · cited 1×
“These include structural proteins and large mechanochemical enzymes (GTPases) that control mitochondrial fi ssion and fusion [16,17], chaperones responsible for correct folding of soluble and membrane proteins, and proteases clearing non-functional, damaged proteins, all involved in various ways in maintaining the int…”
BackgroundReactive oxygen species in cancer cells: Live by the sword, die by the sword
Schumacker, P. T. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.08.015 · Cited by 1,242
Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes
Muoio, D. M., & Newgard, C. B. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2327 · Cited by 1,177
Cytoplasmic functions of the tumour suppressor p53
Green, D. R., & Kroemer, G. (2009) · Nature · doi:10.1038/nature07986 · Cited by 1,106
Glucolipotoxicity: fuel excess and β-cell dysfunction
Poitout, V., & Robertson, R. P. (2008) · Endocrine Reviews · doi:10.1210/er.2007-0023 · Cited by 1,092
The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
Kokoszka, J. E., Waymire, K. G., Levy, S. E., Sligh, J. E., Cai, J., Jones, D. P., MacGregor, G. R., & Wallace, D. C. (2004) · Nature · doi:10.1038/nature02229 · Cited by 1,086
Tumor suppressors and cell metabolism: a recipe for cancer growth
Jones, R. G., & Thompson, C. B. (2009) · Genes & Development · doi:10.1101/gad.1756509 · Cited by 1,085
ROS, mitochondria and the regulation of autophagy
Scherz-Shouval, R., & Elazar, Z. (2007) · Trends in Cell Biology · doi:10.1016/j.tcb.2007.07.009 · Cited by 954
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
Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D
Basso, E., Fante, L., Fowlkes, J., Petronilli, V., Forte, M. A., & Bernardi, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500089200 · Cited by 808 · cited 1×
“The roles of ANT and VDAC have been thrown into question by the failure of knockout experiments to prevent mPTP opening [81,82], whereas the role of CypD has been convincingly confi rmed using the same approach [83–85].”
ResultDevi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792
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
Gandhi, S., Wood-Kaczmar, A., Yao, Z., Plun-Favreau, H., Deas, E., Klupsch, K., Downward, J., Latchman, D. S., Tabrizi, S. J., Wood, N. W., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.013 · Cited by 682
Self-citationPINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1
Pridgeon, J. W., Olzmann, J. A., Chin, L.-S., & Li, L. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050172 · Cited by 596
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
Bota, D. A., & Davies, K. J. A. (2002) · Nature Cell Biology · doi:10.1038/ncb836 · Cited by 557
Regulation of tumor pH and the role of carbonic anhydrase 9
Swietach, P., Vaughan-Jones, R. D., & Harris, A. L. (2007) · Cancer and Metastasis Reviews · doi:10.1007/s10555-007-9064-0 · Cited by 539
PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons
Wood-Kaczmar, A., Gandhi, S., Yao, Z., Abramov, A. S. Y., Miljan, E. A., Keen, G., Stanyer, L., Hargreaves, I., Klupsch, K., Deas, E., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002455 · Cited by 316
Self-citationTal, R., Winter, G., Ecker, N., Klionsky, D. J., & Abeliovich, H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m605940200 · Cited by 268
Nitric Oxide, Cytochrome C Oxidase, and the Cellular Response to Hypoxia
Taylor, C. T., & Moncada, S. (2010) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.108.181628 · Cited by 220
Nagai, Y., Yonemitsu, S., Erion, D. M., Iwasaki, T., Stark, R., Weismann, D., Dong, J., Zhang, D., Jurczak, M. J., Löffler, M. G., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.011 · Cited by 203
Mitochondrial dysfunction in Parkinson's disease
Schapira, A. H. V. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402160 · Cited by 175
In beta-cells, mitochondria integrate and generate metabolic signals controlling insulin secretion
Maechler, P., Carobbio, S., & Rubi, B. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.12.006 · Cited by 140
Cited by
Mikkelsen, K., Stojanovska, L., Polenakovic, M., Bosevski, M., & Apostolopoulos, V. (2017) · Maturitas · doi:10.1016/j.maturitas.2017.09.003 · Cited by 1,072
Smith, R. A. J., Hartley, R. C., Cochemé, H. M., & Murphy, M. P. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.03.010 · Cited by 499
Schapira, A. H. (2012) · The Lancet · doi:10.1016/s0140-6736(11)61305-6 · Cited by 494
Raffaello, A., De Stefani, D., Sabbadin, D., Teardo, E., Merli, G., Picard, A., Checchetto, V., Moro, S., Szabò, I., & Rizzuto, R. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.157 · Cited by 490
Mitochondria: A central target for sex differences in pathologies
Ventura-Clapier, R., Moulin, M., Piquereau, J., Lemaire, C., Mericskay, M., Veksler, V., & Garnier, A. (2017) · Clinical Science · doi:10.1042/cs20160485 · Cited by 371
Metadata
- Authors
- Duchen, M. R., & Szabadkai, G.
- Venue
- Essays in Biochemistry
- Publisher
- Portland Press Ltd.
- Published
- 2010-06-14
- Volume
- 47
- Pages
- 115-137
- ISSN
- 0071-1365 (ISSN-L)
- 1744-1358
- OpenAlex
- W2057691269
- Cited by
- 168
- References
- 34
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- closed
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