Mammalian Mitochondria and Aging: An Update

Kauppila, Timo E.S.; Kauppila, Johanna H.K.; Larsson, Nils-Göran

doi:10.1016/j.cmet.2016.09.017

Cited by 578Mitochondrial Function and PathologyGenetics, Aging, and Longevity in Model OrganismsAutophagy in Disease and Therapy

Mammalian Mitochondria and Aging: An Update

Open access

Kauppila, Timo E.S., Kauppila, Johanna H.K., Larsson, Nils-Göran·2017·Cell Metabolism

DOI 10.1016/j.cmet.2016.09.017

Open this paper in CoChat — free account Open PDF

Abstract

Mitochondria were first postulated to contribute to aging more than 40 years ago. During the following decades, multiple lines of evidence in model organisms and humans showed that impaired mitochondrial function can contribute to age-associated disease phenotypes and aging. However, in contrast to the original theory favoring oxidative damage as a cause for mtDNA mutations, there are now strong data arguing that most mammalian mtDNA mutations originate as replication errors made by the mtDNA polymerase. Currently, a substantial amount of mitochondrial research is focused on finding ways to either remove or counteract the effects of mtDNA mutations with the hope of extending the human health- and lifespan. This review summarizes the current knowledge regarding the formation of mtDNA mutations and their impact on mitochondrial function. We also critically discuss proposed pathways interlinked with mammalian mtDNA mutations and suggest future research strategies to elucidate the role of mtDNA mutations in aging.

Integrity signals

Registry

Crossref · 10.1016/j.cmet.2016.09.017

Cites

221 of 221 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Findings in multiple species question the role of oxidative stress on mtDNA mutagenesis.
“Research findings in multiple species question the role of oxidative stress on mtDNA mutagenesis60.”
From Mitochondrial and metabolic dysfunction in ageing and age-related diseases (2022) · cites this paper as [60]
Mitochondrial dysfunction is a major contributor to aging and aging-driven degenerative diseases such as diabetes, heart diseases, cancer, Alzheimer's disease and Parkinson's disease.
“It is now recognized that mitochondrial dysfunction is a major contributor to aging and aging-driven degenerative disease, such as diabetes, heart diseases, cancer, Alzheimer’s disease and Parkinson’s disease [35,36,37,38,39,40].”
From The mitochondrial permeability transition: Nexus of aging, disease and longevity (2021) · cites this paper as [37]

Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567 · see citing works
Instability and decay of the primary structure of DNA
Lindahl, T. (1993) · Nature · doi:10.1038/362709a0 · Cited by 5,679 · see citing works
Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
Duve, C. D., Pressman, B. C., Gianetto, R., Wattiaux, R., & Appelmans, F. (1955) · Biochemical Journal · doi:10.1042/bj0600604 · Cited by 4,176 · see citing works
Mechanisms of mitophagy
Youle, R. J., & Narendra, D. P. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3028 · Cited by 3,273 · see citing works
The Loss of Skeletal Muscle Strength, Mass, and Quality in Older Adults: The Health, Aging and Body Composition Study
Goodpaster, B. H., Park, S. W., Harris, T. B., Kritchevsky, S. B., Nevitt, M., Schwartz, A. V., Simonsick, E. M., Tylavsky, F. A., Visser, M., Newman, A. B., et al. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.10.1059 · Cited by 3,083 · cited 1× · see citing works
“For instance, loss of muscle strength, one important sign of human aging, can be detected already in the early thirties and is caused more by the loss of muscle quality than quantity (Goodpaster et al., 2006).”
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
Self-citation
Transcriptional co-activator PGC-1α drives the formation of slow-twitch muscle fibres
Lin, J., Wu, H., Tarr, P. T., Zhang, C.-Y., Wu, Z., Boss, O., Michael, L. F., Puigserver, P., Isotani, E., Olson, E. N., et al. (2002) · Nature · doi:10.1038/nature00904 · Cited by 2,546 · 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
Autophagy and Aging
Rubinsztein, D. C., Mariño, G., & Kroemer, G. (2011) · Cell · doi:10.1016/j.cell.2011.07.030 · Cited by 2,107 · see citing works
Oxidative damage and mitochondrial decay in aging.
Shigenaga, M. K., Hagen, T. M., & Ames, B. N. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10771 · Cited by 2,055 · see citing works
The Biologic Clock: The Mitochondria?
Harman, D. (1972) · Journal of the American Geriatrics Society · doi:10.1111/j.1532-5415.1972.tb00787.x · Cited by 1,991 · see citing works
Extension of murine life span by overexpression of catalase targeted to mitochondria
Schriner, S. E., Linford, N. J., Martin, G. M., Treuting, P., Ogburn, C. E., Emond, M., Coskun, P. E., Ladiges, W., Wolf, N., Van Remmen, H., et al. (2005) · Science · doi:10.1126/science.1106653 · Cited by 1,724 · see citing works
High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease
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
DNA damage by oxygen‐derived species Its mechanism and measurement in mammalian systems
Halliwell, B. B., & Aruoma, O. I. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80347-6 · Cited by 1,526 · see citing works
The mitochondrial basis of aging
Sun, N., Youle, R. J., & Finkel, T. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.028 · Cited by 1,441 · see citing works
Selective Mitochondrial Autophagy, or Mitophagy, as a Targeted Defense Against Oxidative Stress, Mitochondrial Dysfunction, and Aging
Lemasters, J. J. (2005) · Rejuvenation Research · doi:10.1089/rej.2005.8.3 · Cited by 1,342 · see citing works
Peroxisome proliferator–activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis
Lehman, J. J., Barger, P. M., Kovacs, A., Saffitz, J. E., Medeiros, D. M., & Kelly, D. P. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10268 · Cited by 1,285 · see citing works
Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
Chen, H., Vermulst, M., Wang, Y. E., Chomyn, A., Prolla, T. A., McCaffery, J. M., & Chan, D. C. (2010) · Cell · doi:10.1016/j.cell.2010.02.026 · Cited by 1,211 · see citing works
Defects in Adaptive Energy Metabolism with CNS-Linked Hyperactivity in PGC-1α Null Mice
Lin, J., Wu, P.-H., Tarr, P. T., Lindenberg, K. S., St-Pierre, J., Zhang, C.-Y., Mootha, V. K., Jäger, S., Vianna, C. R., Reznick, R. M., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.013 · Cited by 1,162 · see citing works
Sirt3 mediates reduction of oxidative damage and prevention of age-related hearing loss under caloric restriction
Someya, S., Yu, W., Hallows, W. C., Xu, J., Vann, J. M., Leeuwenburgh, C., Tanokura, M., Denu, J. M., & Prolla, T. A. (2010) · Cell · doi:10.1016/j.cell.2010.10.002 · Cited by 1,150 · see citing works
Historical landmarks of autophagy research
Ohsumi, Y. (2013) · Cell Research · doi:10.1038/cr.2013.169 · Cited by 1,093 · see citing works
The sirtuin SIRT6 regulates lifespan in male mice
Kanfi, Y., Naiman, S., Amir, G., Peshti, V., Zinman, G., Nahum, L., Bar-Joseph, Z., & Cohen, H. Y. (2012) · Nature · doi:10.1038/nature10815 · Cited by 1,059 · see citing works
Protein oxidation and aging
Stadtman, E. R. (2006) · Free Radical Research · doi:10.1080/10715760600918142 · Cited by 1,056 · see citing works
The dynamics of mitochondrial DNA heteroplasmy: implications for human health and disease
Stewart, J. B., & Chinnery, P. F. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3966 · Cited by 1,041 · see citing works
Mitochondrial Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960 · see citing works
PGC-1α Deficiency Causes Multi-System Energy Metabolic Derangements: Muscle Dysfunction, Abnormal Weight Control and Hepatic Steatosis
Leone, T. C., Lehman, J. J., Finck, B. N., Schaeffer, P. J., Wende, A. R., Boudina, S., Courtois, M., Wozniak, D. F., Sambandam, N., Bernal-Mizrachi, C., et al. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030101 · Cited by 951 · see citing works
Antioxidant supplements for prevention of mortality in healthy participants and patients with various diseases
Bjelakovic, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. (2012) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd007176.pub2 · Cited by 924 · see citing works
Prevalence of nuclear and mitochondrial DNA mutations related to adult mitochondrial disease
Gorman, G., Schaefer, A., Ng, Y., Gomez, N., Blakely, E., Alston, C., Feeney, C., Horvath, R., Yu-Wai-Man, P., Chinnery, P., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24362 · Cited by 921 · see citing works
Mitochondrial DNA deletions in human brain: regional variability and increase with advanced age
Corral-Debrinski, M., Horton, T., Lott, M. T., Shoffner, J. M., Flint Beal, M., & Wallace, D. C. (1992) · Nature Genetics · doi:10.1038/ng1292-324 · Cited by 890 · see citing works
Biologically relevant metal ion‐dependent hydroxyl radical generation An update
Halliwell, B. B., & Gutteridge, J. M. C. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80911-y · Cited by 884 · see citing works
Mitochondrial DNA deletions are abundant and cause functional impairment in aged human substantia nigra neurons
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
CYTOPLASMIC COMPONENTS IN HEPATIC CELL LYSOSOMES
Ashford, T. P., & Porter, K. R. (1962) · The Journal of Cell Biology · doi:10.1083/jcb.12.1.198 · Cited by 849 · see citing works
PARP-1 inhibition increases mitochondrial metabolism through SIRT1 activation
Bai, P., Cantó, C., Oudart, H., Brunyánszki, A., Cen, Y., Thomas, C., Yamamoto, H., Huber, A., Kiss, B., Houtkooper, R. H., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.03.004 · Cited by 837 · see citing works
Mitochondrial threshold effects
Rossignol, R., Faustin, B., Rocher, C., Malgat, M., Mazat, J., & Letellier, T. (2003) · Biochemical Journal · doi:10.1042/bj20021594 · Cited by 802 · see citing works
SIRT3 deficiency and mitochondrial protein hyperacetylation accelerate the development of the metabolic syndrome
Hirschey, M. D., Shimazu, T., Jing, E., Grueter, C. A., Collins, A. M., Aouizerat, B., Stančáková, A., Goetzman, E., Lam, M. M., Schwer, B., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.019 · Cited by 787 · see citing works
Detection of a specific mitochondrial DNA deletion in tissues of older humans
Cortopassi, G. A., & Arnheim, N. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.23.6927 · Cited by 785 · see citing works
Does oxidative damage to DNA increase with age?
Hamilton, M. L., Van Remmen, H., Drake, J. A., Yang, H., Guo, Z. M., Kewitt, K., Walter, C. A., & Richardson, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171202698 · Cited by 768 · see citing works
Oxidative damage to mitochondrial DNA shows marked age-dependent increases in human brain
Mecocci, P., MacGarvey, U., Kaufman, A. E., Koontz, D., Shoffner, J. M., Wallace, D. C., & Beal, M. F. (1993) · Annals of Neurology · doi:10.1002/ana.410340416 · Cited by 757 · cited 1× · see citing works
“Traditionally, PGC1a has been thought to mediate exercise and dietary restriction-induced mitochondrial biogenesis, but these assumptions have recently been questioned (Finley et al., 2012; Geng et al., 2010; Leick et al., 2008; Miller et al., 2012; Rowe et al., 2012).”
Senescence in natural populations of animals: Widespread evidence and its implications for bio-gerontology
Nussey, D. H., Froy, H., Lemaître, J., Gaillard, J., & Austad, S. N. (2012) · Ageing Research Reviews · doi:10.1016/j.arr.2012.07.004 · Cited by 687 · see citing works
Role of PINK1 Binding to the TOM Complex and Alternate Intracellular Membranes in Recruitment and Activation of the E3 Ligase Parkin
Lazarou, M., Jin, S. M., Kane, L. A., & Youle, R. J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2011.12.014 · Cited by 670 · see citing works
A pattern of accumulation of a somatic deletion of mitochondrial DNA in aging human tissues.
Cortopassi, G. A., Shibata, D. K., Soong, N.-W., & Arnheim, N. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7370 · Cited by 639 · see citing works
Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome
Hebert, A. S., Dittenhafer-Reed, K. E., Yu, W., Bailey, D. J., Selen, E. S., Boersma, M. D., Carson, J. J., Tonelli, M., Balloon, A. J., Higbee, A. J., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.024 · Cited by 636 · see citing works
The role of oxidative damage and stress in aging
Bokov, A. F., Chaudhuri, A. R., & Richardson, A. G. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.07.009 · Cited by 621 · see citing works
Sirt1 improves healthy ageing and protects from metabolic syndrome-associated cancer
Herranz, D., Muñoz-Martin, M., Cañamero, M., Mulero, F., Martinez-Pastor, B., Fernandez-Capetillo, O., & Serrano, M. (2010) · Nature Communications · doi:10.1038/ncomms1001 · Cited by 612 · see citing works
Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1α muscle-specific knock-out animals.
Handschin, C., Chin, S., Li, P., Liu, F., Maratos-Flier, E., LeBrasseur, N. K., Yan, Z., & Spiegelman, B. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704817200 · Cited by 611 · see citing works
Is the oxidative stress theory of aging dead?
Pérez, V. I., Bokov, A., Remmen, H. V., Mele, J., Ran, Q., Ikeno, Y., & Richardson, A. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.06.003 · Cited by 604 · see citing works
Somatic mtDNA mutations cause aging phenotypes without affecting reactive oxygen species production
Trifunovic, A., Hansson, A., Wredenberg, A., Rovio, A. T., Dufour, E., Khvorostov, I., Spelbrink, J. N., Wibom, R., Jacobs, H. T., & Larsson, N.-G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508886102 · Cited by 555 · see citing works
Self-citation
Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA
Kukat, C., Wurm, C., Spåhr, H., Falkenberg, M., Larsson, N., & Jakobs, S. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1109263108 · Cited by 551 · see citing works
Self-citation
Mitochondrial mutations may increase oxidative stress: Implications for carcinogenesis and aging?
Bandy, B., & Davison, A. J. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90152-9 · Cited by 550 · see citing works
Somatic Mitochondrial DNA Mutations in Mammalian Aging
Larsson, N. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-093701 · Cited by 543 · see citing works
Self-citation
Oxidative damage to mitochondrial DNA is inversely related to maximum life span in the heart and brain of mammals
Barja, G., & Herrero, A. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.2.312 · Cited by 540 · see citing works
Mitochondrial DNA mutations in human colonic crypt stem cells
Taylor, R. W., Barron, M. J., Borthwick, G. M., Gospel, A., Chinnery, P. F., Samuels, D. C., Taylor, G. A., Plusa, S. M., Needham, S. J., Greaves, L. C., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci19435 · Cited by 530 · see citing works
Overexpression of Catalase Targeted to Mitochondria Attenuates Murine Cardiac Aging
Dai, D., Santana, L. F., Vermulst, M., Tomazela, D. M., Emond, M. J., MacCoss, M. J., Gollahon, K. A., Martin, G. M., Loeb, L. A., Ladiges, W., et al. (2009) · Circulation · doi:10.1161/circulationaha.108.822403 · Cited by 497 · see citing works
MOLECULAR GENETIC ASPECTS OF HUMAN MITOCHONDRIAL DISORDERS
Larsson, N.-G., & Clayton, D. A. (1995) · Annual Review of Genetics · doi:10.1146/annurev.ge.29.120195.001055 · Cited by 493 · see citing works
Self-citation
Widespread and Enzyme-independent Nϵ-Acetylation and Nϵ-Succinylation of Proteins in the Chemical Conditions of the Mitochondrial Matrix*
Wagner, G. R., & Payne, R. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.486753 · Cited by 490 · see citing works
Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
Rosenquist, T. A., Zharkov, D. O., & Grollman, A. P. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7429 · Cited by 485 · see citing works
Origins and functional consequences of somatic mitochondrial DNA mutations in human cancer
Ju, Y. S., Alexandrov, L. B., Gerstung, M., Martin, S., Nik‐Zainal, S., Ramakrishna, M., Davies, H. R., Papaemmanuil, E., Gundem, G., Shlien, A., et al. (2014) · eLife · doi:10.7554/elife.02935 · Cited by 481 · see citing works
Establishing the background level of base oxidation in human lymphocyte DNA: results of an interlaboratory validation study
Gedik, C. M., & Collins, A. R. (2004) · The FASEB Journal · doi:10.1096/fj.04-1767fje · Cited by 449 · see citing works
Dependence of H2O2 formation by rat heart mitochondria on substrate availability and donor age
Hansford, R. G., Hogue, B. A., & Mildaziene, V. (1997) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1022420007908 · Cited by 447 · see citing works
SIRT3 Protein Deacetylates Isocitrate Dehydrogenase 2 (IDH2) and Regulates Mitochondrial Redox Status
Yu, W., Dittenhafer‐Reed, K. E., & Denu, J. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.355206 · Cited by 445 · see citing works
Mitochondrial DNA–Deletion Mutations Accumulate Intracellularly to Detrimental Levels in Aged Human Skeletal Muscle Fibers
Bua, E., Johnson, J., Herbst, A., Delong, B., McKenzie, D., Salamat, S., & Aiken, J. M. (2006) · The American Journal of Human Genetics · doi:10.1086/507132 · Cited by 442 · see citing works
Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications
Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 437 · see citing works
SIRT3 Reverses Aging-Associated Degeneration
Brown, K., Xie, S., Qiu, X., Mohrin, M., Shin, J., Liu, Y., Zhang, D., Scadden, D. T., & Chen, D. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.005 · Cited by 436 · see citing works
Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis.
Sakumi, K., Furuichi, M., Tsuzuki, T., Kakuma, T., KAWABATA, S., Maki, H., & Sekiguchi, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49494-5 · Cited by 435 · see citing works
Can autophagy promote longevity?
Madeo, F., Tavernarakis, N., & Kroemer, G. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-842 · Cited by 429 · see citing works
. HIV-1 infection is associated with an earlier occurrence of a phenotype related to frailty.
Desquilbet, L., Jacobson, L. P., Fried, L. P., Phair, J. P., Jamieson, B. D., Holloway, M., Margolick, J. B., & Study, F. T. M. A. C. (2007) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/62.11.1279 · Cited by 420 · see citing works
CELLULAR DIFFERENTIATION IN THE KIDNEYS OF NEWBORN MICE STUDIED WITH THE ELECTRON MICROSCOPE
Clark, S. L. (1957) · The Journal of Cell Biology · doi:10.1083/jcb.3.3.349 · Cited by 418 · see citing works
Architecture of mammalian respiratory complex I
Vinothkumar, K. R., Zhu, J., & Hirst, J. (2014) · Nature · doi:10.1038/nature13686 · Cited by 413 · see citing works
Minimizing the damage: repair pathways keep mitochondrial DNA intact
Kazak, L., Reyes, A., & Holt, I. J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3439 · Cited by 412 · see citing works
New insights into PGC ‐1 coactivators: redefining their role in the regulation of mitochondrial function and beyond
Villena, J. A. (2014) · FEBS Journal · doi:10.1111/febs.13175 · Cited by 404 · see citing works
Universal heteroplasmy of human mitochondrial DNA
Payne, B. A. I., Wilson, I., Yu‐Wai‐Man, P., Coxhead, J., Deehan, D. J., Horváth, R., Taylor, R. W., Samuels, D. C., Santibanez‐Koref, M., & Chinnery, P. F. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds435 · Cited by 396 · see citing works
Parkin and PINK1: much more than mitophagy
Scarffe, L. A., Stevens, D. A., Dawson, V. L., & Dawson, T. M. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.004 · Cited by 392 · see citing works
Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
Chae, H. Z., Kim, H. J., Kang, S. W., & Rhee, S. G. (1999) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(99)00037-6 · Cited by 390 · see citing works
Mitochondrial DNA deletion mutations colocalize with segmental electron transport system abnormalities, muscle fiber atrophy, fiber splitting, and oxidative damage in sarcopenia
WANAGAT, J., CAO, Z., PATHARE, P., & AIKEN, J. M. (2001) · The FASEB Journal · doi:10.1096/fj.00-0320com · Cited by 378 · see citing works
Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid
Kukat, C., Davies, K. M., Wurm, C. A., Spåhr, H., Bonekamp, N. A., Kühl, I., Joos, F., Polosa, P. L., Park, C. B., Posse, V., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1512131112 · Cited by 378 · see citing works
Self-citation
Succinate Dehydrogenase Is a Direct Target of Sirtuin 3 Deacetylase Activity
Finley, L. W. S., Haas, W., Desquiret‐Dumas, V., Wallace, D. C., Procaccio, V., Gygi, S. P., & Haigis, M. C. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023295 · Cited by 364 · see citing works
PINK1 Loss-of-Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling
Morais, V. A., Haddad, D., Craessaerts, K., Bock, P. D., Swerts, J., Vilain, S., Aerts, L., Overbergh, L., Grünewald, A., Seibler, P., et al. (2014) · Science · doi:10.1126/science.1249161 · Cited by 364 · see citing works
Ultra-sensitive sequencing reveals an age-related increase in somatic mitochondrial mutations that are inconsistent with oxidative damage
Kennedy, S. R., Salk, J. J., Schmitt, M. W., & Loeb, L. A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003794 · Cited by 363 · see citing works
NAD+-Dependent Activation of Sirt1 Corrects the Phenotype in a Mouse Model of Mitochondrial Disease
Cerutti, R., Pirinen, E., Lamperti, C., Marchet, S., Sauve, A. A., Li, W., Leoni, V., Schon, E. A., Dantzer, F., Auwerx, J., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.04.001 · Cited by 343 · cited 1× · see citing works
“As expected, the Parp1 / mice also show fiber type switching toward a more oxidative fiber type and increased mitochondrial biogenesis, which can rescue some of the biochemical phenotypes of the above-mentioned Sco2 knockout-knockin mouse (Bai et al., 2011; Cerutti et al., 2014).”
Mutations causing mitochondrial disease: What is new and what challenges remain?
Lightowlers, R. N., Taylor, R. W., & Turnbull, D. M. (2015) · Science · doi:10.1126/science.aac7516 · Cited by 341 · see citing works
Random intracellular drift explains the clonal expansion of mitochondrial DNA mutations with age
Elson, J. L., Samuels, D. C., Turnbull, D. M., & Chinnery, P. F. (2001) · The American Journal of Human Genetics · doi:10.1086/318801 · Cited by 340 · see citing works
Mitochondrial dysfunction in aging: Much progress but many unresolved questions
Payne, B. A. I., & Chinnery, P. F. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.022 · Cited by 335 · see citing works
Analyses of mitochondrial respiratory chain function and mitochondrial DNA deletion in human skeletal muscle: Effect of ageing
Cooper, J. A. D., Mann, V. M., & Schapira, A. H. V. (1992) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(92)90270-u · Cited by 335 · see citing works
ELECTRON MICROSCOPY OF LYSOSOME-RICH FRACTIONS FROM RAT LIVER
Novikoff, A. B., Beaufay, H., & Duve, C. D. (1956) · The Journal of Cell Biology · doi:10.1083/jcb.2.4.179 · Cited by 332 · see citing works
Distribution and threshold expression of the tRNA(Lys) mutation in skeletal muscle of patients with myoclonic epilepsy and ragged-red fibers (MERRF).
Boulet, L., Karpati, G., & Shoubridge, E. A. (1992) · Europe PMC (PubMed Central) · Cited by 331 · see citing works
Repair of 8-oxodeoxyguanosine lesions in mitochondrial dna depends on the oxoguanine dna glycosylase (OGG1) gene and 8-oxoguanine accumulates in the mitochondrial dna of OGG1-defective mice.
de Souza-Pinto, N. C., Eide, L., Hogue, B. A., Thybo, T., Stevnsner, T., Seeberg, E. C., Klungland, A., & Bohr, V. A. (2001) · PubMed · Cited by 328 · see citing works
Endogenous Parkin Preserves Dopaminergic Substantia Nigral Neurons following Mitochondrial DNA Mutagenic Stress
Pickrell, A. M., Huang, C.-H., Kennedy, S. R., Ordureau, A., Sideris, D. P., Hoekstra, J. G., Harper, J. W., & Youle, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.034 · Cited by 327 · see citing works
Transcriptional coactivators PGC-1α and PGC-lβ control overlapping programs required for perinatal maturation of the heart
Lai, L., Leone, T. C., Zechner, C., Schaeffer, P. J., Kelly, S. M., Flanagan, D. P., Medeiros, D. M., Kovacs, A., & Kelly, D. P. (2008) · Genes & Development · doi:10.1101/gad.1661708 · Cited by 326 · see citing works
Maternal inheritance of mitochondrial DNA by diverse mechanisms to eliminate paternal mitochondrial DNA
Sato, M., & Sato, K. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.010 · Cited by 325 · see citing works
Measurement of H2O2 within Living Drosophila during Aging Using a Ratiometric Mass Spectrometry Probe Targeted to the Mitochondrial Matrix
Cochemé, H. M., Quin, C., McQuaker, S. J., Cabreiro, F., Logan, A., Prime, T. A., Abakumova, I., Patel, J. V., Fearnley, I. M., James, A. M., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.003 · Cited by 313 · see citing works
Mouse L cell mitochondrial DNA molecules are selected randomly for replication throughout the cell cycle
Bogenhagen, D. F., & Clayton, D. A. (1977) · Cell · doi:10.1016/0092-8674(77)90286-0 · Cited by 312 · see citing works
Mechanisms and Dynamics of Protein Acetylation in Mitochondria
Baeza, J., Smallegan, M. J., & Denu, J. M. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.006 · Cited by 312 · see citing works
Antioxidant supplements for prevention of mortality in healthy participants and patients with various diseases
Bjelaković, G., Nikolova, D., Gluud, L. L., Simonetti, R. G., & Gluud, C. N. (2008) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd007176 · Cited by 307 · see citing works
Extensive pathogenicity of mitochondrial heteroplasmy in healthy human individuals
Ye, K., Lü, J., Ma, F., Keinan, A., & Gu, Z. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403521111 · Cited by 296 · see citing works
Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo
Sterky, 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
Self-citation
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
Cytochrome c oxidase deficient fibres in the limb muscle and diaphragm of man without muscular disease: An age-related alteration
Müller‐Höcker, J. (1990) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(90)90006-9 · Cited by 284 · see citing works
Role of mitochondrial DNA mutations in human aging: Implications for the central nervous system and muscle
Brierley, E. J., Johnson, M. A., Lightowlers, R. N., James, O., & Turnbull, D. M. (1998) · Annals of Neurology · doi:10.1002/ana.410430212 · Cited by 282 · see citing works
Efficient mitochondrial biogenesis drives incomplete penetrance in Leber’s hereditary optic neuropathy
Giordano, C., Iommarini, L., Giordano, L., Maresca, A., Pisano, A., Valentino, M. L., Caporali, L., Liguori, R., Deceglie, S., Roberti, M., et al. (2013) · Brain · doi:10.1093/brain/awt343 · Cited by 282 · see citing works
Ablation of PGC-1β Results in Defective Mitochondrial Activity, Thermogenesis, Hepatic Function, and Cardiac Performance
Lelliott, C. J., Medina-Gomez, G., Petrovic, N., Kis, A., Feldmann, H. M., Bjursell, M., Parker, N., Curtis, K., Campbell, M., Hu, P., et al. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040369 · Cited by 280 · cited 1× · see citing works
“Pgc1a and Pgc1b knockout mice are viable and show modest mitochondrial phenotypes (Lelliott et al., 2006; Sonoda et al., 2007; Vianna et al., 2006).”
Age-dependent cardiomyopathy in mitochondrial mutator mice is attenuated by overexpression of catalase targeted to mitochondria
Dai, D., Chen, T., Wanagat, J., Laflamme, M., Marcinek, D. J., Emond, M. J., Ngo, C. P., Prolla, T. A., & Rabinovitch, P. S. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00581.x · Cited by 280 · see citing works
Cytochrome-c-oxidase deficient cardiomyocytes in the human heart--an age-related phenomenon. A histochemical ultracytochemical study.
Müller‐Höcker, J. (1989) · PubMed Central · Cited by 280 · see citing works
Proteome-Wide Mapping of the Drosophila Acetylome Demonstrates a High Degree of Conservation of Lysine Acetylation
Weinert, B. T., Wagner, S., Horn, H., Henriksen, P., Liu, W. R., Olsen, J. V., Jensen, L. J., & Choudhary, C. (2011) · Science Signaling · doi:10.1126/scisignal.2001902 · Cited by 275 · see citing works
Total Skeletal Muscle PGC-1 Deficiency Uncouples Mitochondrial Derangements from Fiber Type Determination and Insulin Sensitivity
Zechner, C., Lai, L., Zechner, J. F., Geng, T., Yan, Z., Rumsey, J. W., Collia, D., Chen, Z., Wozniak, D. F., Leone, T. C., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.11.008 · Cited by 274 · cited 2× · see citing works
“…of Pgc1a in mice leads to muscle fiber type switching from fast-twitching glycolytic fibers to slow-twitching oxidative fibers (Lin et al., 2002), it is still unclear how important PGC1a is for muscle fiber type determination in wild-type mice (Handschin et al., 2007; Zechner et al., 2010).”
Germline mitochondrial DNA mutations aggravate ageing and can impair brain development
Ross, J. M., Stewart, J. B., Hagström, E., Brené, S., Mourier, A., Coppotelli, G., Freyer, C., Lagouge, M., Hoffer, B. J., Olson, L., et al. (2013) · Nature · doi:10.1038/nature12474 · Cited by 273 · see citing works
Self-citation
Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae
Weinert, B. T., Iešmantavičius, V., Moustafa, T., Scholz, C. W., Wagner, S., Magnes, C., Zechner, R., & Choudhary, C. (2014) · Molecular Systems Biology · doi:10.1002/msb.134766 · Cited by 272 · see citing works
Transgenic expression of green fluorescence protein can cause dilated cardiomyopathy
Huang, W., Aramburu, J. F., Douglas, P. S., & Izumo, S. (2000) · Nature Medicine · doi:10.1038/74914 · Cited by 271 · see citing works
The role of mitochondrial DNA mutations and free radicals in disease and ageing
Lagouge, M., & Larsson, N. (2013) · Journal of Internal Medicine · doi:10.1111/joim.12055 · Cited by 270 · see citing works
Self-citation
PGC-1β controls mitochondrial metabolism to modulate circadian activity, adaptive thermogenesis, and hepatic steatosis
Sonoda, J., Mehl, I. R., Chong, L.-W., Nofsinger, R. R., & Evans, R. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611623104 · Cited by 266 · see citing works
PGC-1α plays a functional role in exercise-induced mitochondrial biogenesis and angiogenesis but not fiber-type transformation in mouse skeletal muscle
Geng, T., Li, P., Okutsu, M., Yin, X., Kwek, J., Zhang, M., & Yan, Z. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00481.2009 · Cited by 263 · see citing works
Calorie restriction alters mitochondrial protein acetylation
Schwer, B., Eckersdorff, M., Li, Y., Silva, J. C., Fermin, D., Kurtev, M. V., Giallourakis, C., Comb, M. J., Alt, F. W., & Lombard, D. B. (2009) · Aging Cell · doi:10.1111/j.1474-9726.2009.00503.x · Cited by 259 · cited 2× · see citing works
“Second, the overall acetylation of mitochondrial proteins is known to change upon alterations in cellular metabolism; e.g., dietary restriction alters mitochondrial protein acetylation (Hebert et al., 2013; Schwer et al., 2009).”
Mitochondrial redox signalling at a glance
Collins, Y., Chouchani, E. T., James, A. M., Menger, K. E., Cochemé, H. M., & Murphy, M. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.098475 · Cited by 255 · see citing works
Superresolution Fluorescence Imaging of Mitochondrial Nucleoids Reveals Their Spatial Range, Limits, and Membrane Interaction
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
Accumulating Mitochondrial DNA Mutations Drive Premature Hematopoietic Aging Phenotypes Distinct from Physiological Stem Cell Aging
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
Ageing-associated 5 kb deletion in human liver mitochondrial DNA
Yen, T.-C., Su, J.-H., King, K.-L., & Wei, Y.-H. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91788-e · Cited by 248 · see citing works
Mechanisms of Field Cancerization in the Human Stomach: The Expansion and Spread of Mutated Gastric Stem Cells
McDonald, S. A. C., Greaves, L. C., Gutierrez–Gonzalez, L., Rodriguez–Justo, M., Deheragoda, M., Leedham, S. J., Taylor, R. W., Lee, C. Y., Preston, S. L., Lovell, M., et al. (2008) · Gastroenterology · doi:10.1053/j.gastro.2007.11.035 · Cited by 242 · see citing works
Accumulation of deletions in human mitochondrial DNA during normal aging: analysis by quantitative PCR
Simonetti, S., Chen, X., DiMauro, S., & Schon, E. A. (1992) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(92)90059-v · Cited by 241 · see citing works
Somatic Progenitor Cell Vulnerability to Mitochondrial DNA Mutagenesis Underlies Progeroid Phenotypes in Polg Mutator Mice
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-citation
PGC-1α is not mandatory for exercise- and training-induced adaptive gene responses in mouse skeletal muscle
Leick, L., Wojtaszewski, J. F. P., Johansen, S. T., Kiilerich, K., Comes, G., Hellsten, Y., Hidalgo, J., & Pilegaard, H. (2007) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00666.2007 · Cited by 236 · see citing works
Mitofusin 2 is required to maintain mitochondrial coenzyme Q levels
Mourier, A., Motori, E., Brandt, T., Lagouge, M., Atanassov, I., Galinier, A., Rappl, G., Brodesser, S., Hultenby, K. R., Dieterich, C., et al. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201411100 · Cited by 234 · see citing works
Self-citation
Mitochondrial aging is accelerated by anti-retroviral therapy through the clonal expansion of mtDNA mutations
Payne, B. A. I., Wilson, I., Hateley, C. A., Horváth, R., Santibanez‐Koref, M., Samuels, D. C., Price, D., & Chinnery, P. F. (2011) · Nature Genetics · doi:10.1038/ng.863 · Cited by 232 · see citing works
Risk of developing a mitochondrial DNA deletion disorder
Chinnery, P. F., DiMauro, S., Shanske, S., Schon, E. A., Zeviani, M., Mariotti, C., Carrara, F., Lombès, A., Laforêt, P., de Baulny, H. O., et al. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16851-7 · Cited by 232 · see citing works
Random Point Mutations with Major Effects on Protein-Coding Genes Are the Driving Force behind Premature Aging in mtDNA Mutator Mice
Edgar, D., Shabalina, I. G., Cámara, Y., Wredenberg, A., Calvaruso, M. A., Nijtmans, L. G. J., Nedergaard, J., Cannon, B., Larsson, N., & Trifunović, A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.010 · Cited by 230 · see citing works
Self-citation
Identification of a molecular component of the mitochondrial acetyltransferase programme: a novel role for GCN5L1
Scott, I., Webster, B. R., Li, J. H., & Sack, M. N. (2012) · Biochemical Journal · doi:10.1042/bj20120118 · Cited by 214 · see citing works
Multiple deletions of mitochondrial DNA are associated with the decline of motility and fertility of human spermatozoa
Kao, S. (1998) · Molecular Human Reproduction · doi:10.1093/molehr/4.7.657 · Cited by 211 · see citing works
Structural basis for the dual coding potential of 8‐oxoguanosine by a high‐fidelity DNA polymerase
Brieba, L. G., Eichman, B. F., Kokoska, R. J., Doublié, S., Kunkel, T. A., & Ellenberger, T. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600354 · Cited by 210 · see citing works
Ageing muscle: clonal expansions of mitochondrial DNA point mutations and deletions cause focal impairment of mitochondrial function
Fayet, G., Jansson, M., Sternberg, D., Moslemi, A.-R., Blondy, P., Lombès, A., Fardeau, M., & Oldfors, A. (2002) · Neuromuscular Disorders · doi:10.1016/s0960-8966(01)00332-7 · Cited by 206 · see citing works
Ultra-Deep Sequencing of Mouse Mitochondrial DNA: Mutational Patterns and Their Origins
Ameur, A., Stewart, J. B., Freyer, C., Hagström, E., Ingman, M., Larsson, N., & Gyllensten, U. B. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002028 · Cited by 202 · see citing works
Self-citation
Accumulation of mitochondrial DNA deletion mutations in aged muscle fibers: evidence for a causal role in muscle fiber loss
Herbst, A., Pak, J. W., McKenzie, D., Bua, E., Bassiouni, M., & Aiken, J. M. (2007) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/62.3.235 · Cited by 200 · see citing works
Repair of Formamidopyrimidines in DNA Involves Different Glycosylases
Hu, J., de Souza-Pinto, N. C., Haraguchi, K., Hogue, B. A., Jaruga, P., Greenberg, M. M., Dizdaroğlu, M., & Bohr, V. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508772200 · Cited by 197 · see citing works
Mitochondrial Deoxyribonucleic Acid 4977-bp Deletion is Associated with Diminished Fertility and Motility of Human Sperm1
Kao, S., Chao, H., & Wei, Y. (1995) · Biology of Reproduction · doi:10.1095/biolreprod52.4.729 · Cited by 197 · see citing works
Is there more to aging than mitochondrial DNA and reactive oxygen species?
ALEXEYEV, M. F. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07269.x · Cited by 194 · see citing works
DNA ligase III is critical for mtDNA integrity but not Xrcc1-mediated nuclear DNA repair
Gao, Y., Katyal, S., Lee, Y., Zhao, J., Rehg, J. E., Russell, H. R., & McKinnon, P. J. (2011) · Nature · doi:10.1038/nature09773 · Cited by 193 · see citing works
Intracellular Localization of 8-Oxo-dGTPase in Human Cells, with Special Reference to the Role of the Enzyme in Mitochondria
Kang, D., Nishida, J., Iyama, A., Nakabeppu, Y., Furuichi, M., Fujiwara, T., Sekiguchi, M., & Takeshige, K. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.24.14659 · Cited by 188 · see citing works
Two direct repeats cause most human mtDNA deletions
Samuels, D. C., Schon, E. A., & Chinnery, P. F. (2004) · Trends in Genetics · doi:10.1016/j.tig.2004.07.003 · Cited by 185 · see citing works
Mechanisms of formation and accumulation of mitochondrial DNA deletions in aging neurons
Fukui, H., & Moraes, C. T. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn437 · Cited by 185 · see citing works
Hypomorphic mutation of PGC-1β causes mitochondrial dysfunction and liver insulin resistance.
Vianna, C. R., Huntgeburth, M., Coppari, R., Choi, C. S., Lin, J., Krauss, S., Barbatelli, G., Tzameli, I., Kim, Y.-B., Cinti, S., et al. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.11.003 · Cited by 181 · see citing works
Functional Expression of hMYH, a Human Homolog of the Escherichia coli MutY Protein
Slupska, M. M., Luther, W. M., Chiang, J., Yang, H., & Miller, J. H. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.19.6210-6213.1999 · Cited by 174 · see citing works
SIRT3 Deacetylates ATP Synthase F <sub>1</sub> Complex Proteins in Response to Nutrient- and Exercise-Induced Stress
Vassilopoulos, A., Pennington, J. D., Andresson, T., Rees, D. M., Bosley, A. D., Fearnley, I. M., Ham, A., Flynn, C. R., Hill, S., Rose, K. L., et al. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5420 · Cited by 173 · see citing works
Oxidative stress is not a major contributor to somatic mitochondrial DNA mutations
Itsara, L. S., Kennedy, S. R., Fox, E. J., Yu, S., Hewitt, J. J., Sanchez-Contreras, M., Cardozo-Pelaez, F., & Pallanck, L. J. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1003974 · Cited by 173 · see citing works
Clonal expansion of early to mid-life mitochondrial DNA point mutations drives mitochondrial dysfunction during human ageing
Greaves, L. C., Nooteboom, M., Elson, J. L., Tuppen, H. A. L., Taylor, G. A., Commane, D. M., Arasaradnam, R. P., Khrapko, K., Taylor, R. W., Kirkwood, T. B. L., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004620 · Cited by 172 · see citing works
Homeostatic Responses Regulate Selfish Mitochondrial Genome Dynamics in C. elegans
Gitschlag, B. L., Kirby, C. S., Samuels, D. C., Gangula, R., Mallal, S. A., & Patel, M. R. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.06.008 · Cited by 171 · see citing works
Mitochondrial DNA deletion mutations are concomitant with ragged red regions of individual, aged muscle fibers: Analysis by laser-capture microdissection
Cao, Z. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.21.4502 · Cited by 170 · see citing works
Rapid directional shift of mitochondrial DNA heteroplasmy in animal tissues by a mitochondrially targeted restriction endonuclease
Bayona‐Bafaluy, M. P., Blits, B., Battersby, B. J., Shoubridge, E. A., & Moraes, C. T. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502896102 · Cited by 169 · see citing works
Parkin Mono-ubiquitinates Bcl-2 and Regulates Autophagy
Chen, D., Gao, F., Li, B., Wang, H., Xu, Y., Zhu, C., & Wang, G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101469 · Cited by 168 · see citing works
TheGpx1Gene Encodes Mitochondrial Glutathione Peroxidase in the Mouse Liver
Esworthy, R. S., Ho, Y., & Chu, F. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9901 · Cited by 165 · see citing works
Segregation and manifestations of the mtDNA tRNA(Lys) A-->G(8344) mutation of myoclonus epilepsy and ragged-red fibers (MERRF) syndrome.
Larsson, N., Tulinius, M., Holme, E., Oldfors, A., Andersen, O., Wahlström, J., & Aasly, J. O. (1992) · Europe PMC (PubMed Central) · Cited by 163 · see citing works
Self-citation
Mitochondrial DNA mutations in neurodegeneration
Keogh, M. J., & Chinnery, P. F. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.015 · Cited by 163 · see citing works
Mitochondrial protein acetylation is driven by acetyl-CoA from fatty acid oxidation
Pougovkina, O., Brinke, H. T., Ofman, R., van Cruchten, A. G., Kulik, W., Wanders, R. J. A., Houten, S. M., & de Boer, V. C. J. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu059 · Cited by 161 · see citing works
Locating the stem cell niche and tracing hepatocyte lineages in human liver #
Fellous, T. G., Islam, S., Tadrous, P. J., Elia, G., Kocher, H. M., Bhattacharya, S., Mears, L., Turnbull, D. M., Taylor, R. W., Greaves, L. C., et al. (2009) · Hepatology · doi:10.1002/hep.22791 · Cited by 157 · see citing works
Differential subcellular localization of human MutY homolog (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase
Takao, M., Zhang, Q.-M., Yonei, S., & Yasui, A. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.18.3638 · Cited by 157 · see citing works
Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells
Chattopadhyay, R. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl177 · Cited by 155 · see citing works
Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions
Weinert, B. T., Moustafa, T., Iešmantavičius, V., Zechner, R., & Choudhary, C. (2015) · The EMBO Journal · doi:10.15252/embj.201591271 · Cited by 150 · see citing works
The Dark Side of EGFP: Defective Polyubiquitination
Baens, M., Noels, H., Broeckx, V., Hagens, S., Fevery, S., Billiau, A. D., Vankelecom, H., & Marynen, P. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000054 · Cited by 149 · see citing works
Post-translational modifications in mitochondria: protein signaling in the powerhouse
Stram, A. R., & Payne, R. M. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2280-4 · Cited by 149 · see citing works
Origins of human mitochondrial point mutations as DNA polymerase γ-mediated errors
Zheng, W., Khrapko, K., Coller, H. A., Thilly, W. G., & Copeland, W. C. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.12.012 · Cited by 141 · see citing works
Dietary restriction.; mitochondrial function and aging: From yeast to humans
Ruetenik, A., & Barrientos, A. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.005 · Cited by 139 · see citing works
Autophagy and mitophagy participate in ocular lens organelle degradation
Costello, M. J., Brennan, L., Basu, S., Chauss, D., Mohamed, A., Gilliland, K. O., Johnsen, S., Menko, A. S., & Kantorow, M. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.08.017 · Cited by 138 · see citing works
A comprehensive assessment of mitochondrial protein synthesis and cellular proliferation with age and caloric restriction
Miller, B. F., Robinson, M. M., Bruss, M. D., Hellerstein, M. K., & Hamilton, K. L. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00769.x · Cited by 137 · see citing works
Effects of physical activity and age on mitochondrial function
Brierley, E. J., Johnson, M. A., James, O., & Turnbull, D. M. (1996) · QJM · doi:10.1093/qjmed/89.4.251 · Cited by 136 · see citing works
Peroxisome proliferator activator receptor gamma coactivator-1alpha (PGC-1α) improves motor performance and survival in a mouse model of amyotrophic lateral sclerosis
Zhao, W., Varghese, M., Yemul, S., Pan, Y., Cheng, A., Marano, P., Hassan, S., Vempati, P., Chen, F., Qian, X., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-51 · Cited by 134 · see citing works
Mitochondrial disease in adults: what's old and what's new?
Chinnery, P. F. (2015) · EMBO Molecular Medicine · doi:10.15252/emmm.201505079 · Cited by 133 · see citing works
Nature of Mitochondrial DNA Deletions in Substantia Nigra Neurons
Reeve, A. K., Krishnan, K. J., Elson, J. L., Morris, C. M., Bender, A., Lightowlers, R. N., & Turnbull, D. M. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2007.09.018 · Cited by 132 · see citing works
Transmission of mitochondrial mutations and action of purifying selection in Drosophila melanogaster
Ma, H., Xu, H., & O’Farrell, P. H. (2014) · Nature Genetics · doi:10.1038/ng.2919 · Cited by 130 · see citing works
mtDNA makes a U-turn for the mitochondrial nucleoid
Kukat, C., & Larsson, N. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.04.009 · Cited by 128 · see citing works
Self-citation
Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy
Fedorowicz, M. A., de Vries, R. L. A., Rüb, C., Becker, D., Huang, Y., Zhou, C., Wolken, D. M. A., Voos, W., Liu, Y., & Przedborski, S. (2013) · EMBO Reports · doi:10.1002/embr.201337294 · Cited by 127 · see citing works
PGC-1α is Dispensable for Exercise-Induced Mitochondrial Biogenesis in Skeletal Muscle
Rowe, G. C., El‐Khoury, R., Patten, I. S., Rustin, P., & Arany, Z. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041817 · Cited by 127 · see citing works
Simultaneous DNA and RNA Mapping of Somatic Mitochondrial Mutations across Diverse Human Cancers
Stewart, J. B., Alaei-Mahabadi, B., Sabarinathan, R., Samuelsson, T., Gorodkin, J., Gustafsson, C. M., & Larsson, E. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005333 · Cited by 126 · see citing works
Muscle-Specific SIRT1 Gain-of-Function Increases Slow-Twitch Fibers and Ameliorates Pathophysiology in a Mouse Model of Duchenne Muscular Dystrophy
Chalkiadaki, A., Igarashi, M., Nasamu, A. S., Knezevic, J., & Guarente, L. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004490 · Cited by 126 · see citing works
Sustained expression of PGC-1 in the rat nigrostriatal system selectively impairs dopaminergic function
Ciron, C., Lengacher, S., Dusonchet, J., Aebischer, P., & Schneider, B. L. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr618 · Cited by 126 · see citing works
Effect of bezafibrate treatment on late-onset mitochondrial myopathy in mice
Yatsuga, S., & Suomalainen, A. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr482 · Cited by 124 · see citing works
Coronary Aging in HIV‐Infected Patients
Guaraldi, G., Zona, S., Alexopoulos, N. A., Orlando, G., Carli, F., Ligabue, G., Fiocchi, F., Lattanzi, A., Rossi, R., Modena, M. G., et al. (2009) · Clinical Infectious Diseases · doi:10.1086/648080 · Cited by 123 · see citing works
The Naked Mole-Rat Response to Oxidative Stress: Just Deal with It
Lewis, K. N., Andziak, B., Yang, T., & Buffenstein, R. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4911 · Cited by 119 · see citing works
The human OPA1delTTAG mutation induces premature age-related systemic neurodegeneration in mouse
Sarzi, E., Angebault, C., Seveno, M., Guéguen, N., Chaix, B., Biélicki, G., Boddaert, N., Mausset-Bonnefont, A.-L., Cazevieille, C., Rigau, V., et al. (2012) · Brain · doi:10.1093/brain/aws303 · Cited by 119 · see citing works
Association of G-quadruplex forming sequences with human mtDNA deletion breakpoints
Dong, D.-W. W., Pereira, F., Barrett, S. P., Kolesar, J., Cao, K.-J., Damas, J., Yatsunyk, L., Johnson, F., & Kaufman, B. A. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-677 · Cited by 116 · see citing works
Loss of CLPP alleviates mitochondrial cardiomyopathy without affecting the mammalian UPRmt
Seiferling, D., Szczepanowska, K., Becker, C., Senft, K., Hermans, S., Maiti, P., König, T., Kukat, A., & Trifunović, A. (2016) · EMBO Reports · doi:10.15252/embr.201642077 · Cited by 116 · see citing works
Keeping mtDNA in Shape between Generations
Stewart, J. B., & Larsson, N. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004670 · Cited by 113 · see citing works
Self-citation
Mitochondrial sirtuins: Emerging roles in metabolic regulations, energy homeostasis and diseases
Parihar, P., Solanki, I., Mansuri, M. L., & Parihar, M. S. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.12.004 · Cited by 112 · see citing works
Erythroid dysplasia, megaloblastic anemia, and impaired lymphopoiesis arising from mitochondrial dysfunction
Chen, M. L., Logan, T. D., Hochberg, M. L., Shelat, S. G., Yu, X., Wilding, G. E., Tan, W., Kujoth, G. C., Prolla, T. A., Selak, M. A., et al. (2009) · Blood · doi:10.1182/blood-2008-08-169474 · Cited by 108 · see citing works
Emerging concepts in the therapy of mitochondrial disease
Viscomi, C. F., Bottani, E., & Zeviani, M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.001 · Cited by 107 · see citing works
Overexpression of peroxisome proliferator-activated receptor γ co-activator-1α leads to muscle atrophy with depletion of ATP.
Miura, S., Tomitsuka, E., Kamei, Y., Yamazaki, T., Kai, Y., Tamura, M., Kita, K., Nishino, I., & Ezaki, O. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.060034 · Cited by 107 · see citing works
The protonophore CCCP interferes with lysosomal degradation of autophagic cargo in yeast and mammalian cells
Padman, B. S., Bach, M., Lucarelli, G., Prescott, M., & Ramm, G. (2013) · Autophagy · doi:10.4161/auto.26557 · Cited by 106 · see citing works
Disconnecting Mitochondrial Content from Respiratory Chain Capacity in PGC-1-Deficient Skeletal Muscle
Rowe, G. C., Patten, I. S., Zsengellér, Z. K., El‐Khoury, R., Okutsu, M., Bampoh, S., Koulisis, N., Farrell, C., Hirshman, M. F., Yan, Z., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.023 · Cited by 104 · see citing works
Skeletal muscle transcriptional coactivator PGC-1α mediates mitochondrial, but not metabolic, changes during calorie restriction
Finley, L. W. S., Lee, J., Souza, A., Desquiret-Dumas, V., Bullock, K., Rowe, G. C., Procaccio, V., Clish, C. B., Arany, Z., & Haigis, M. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1115813109 · Cited by 102 · see citing works
Increased mitochondrial biogenesis in muscle improves aging phenotypes in the mtDNA mutator mouse
Dillon, L. M., Williams, S. L., Hida, A., Peacock, J. D., Prolla, T. A., Lincoln, J., & Moraes, C. T. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds049 · Cited by 98 · see citing works
Mitochondrial and sex steroid hormone crosstalk during aging
Velarde, M. C. (2014) · Longevity & Healthspan · doi:10.1186/2046-2395-3-2 · Cited by 96 · see citing works
In vivo levels of mitochondrial hydrogen peroxide increase with age in mt DNA mutator mice
Logan, A., Shabalina, I. G., Prime, T. A., Rogatti, S., Kalinovich, A., Hartley, R. C., Budd, R. C., Cannon, B., & Murphy, M. P. (2014) · Aging Cell · doi:10.1111/acel.12212 · Cited by 93 · see citing works
The DNA polymerase Y955C disease variant associated with PEO and parkinsonism mediates the incorporation and translesion synthesis opposite 7,8-dihydro-8-oxo-2'-deoxyguanosine
Graziewicz, M. A., Bienstock, R. J., & Copeland, W. C. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm227 · Cited by 93 · see citing works
No decline in skeletal muscle oxidative capacity with aging in long-term calorically restricted rats: Effects are independent of mitochondrial DNA integrity
Baker, D. J., Betik, A. C., Krause, D. J., & Hepple, R. T. (2006) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/61.7.675 · Cited by 89 · see citing works
Dopaminergic midbrain neurons are the prime target for mitochondrial DNA deletions
Bender, A., Schwarzkopf, R.-M., McMillan, A., Krishnan, K. J., Rieder, G., Neumann, M., Elstner, M., Turnbull, D. M., & Klopstock, T. (2008) · Journal of Neurology · doi:10.1007/s00415-008-0892-9 · Cited by 88 · see citing works
Mosaic deficiency in mitochondrial oxidative metabolism promotes cardiac arrhythmia during aging
Baris, O. R., Ederer, S., Neuhaus, J. F. G., von Kleist-Retzow, J.-C., Wunderlich, C. M., Pal, M., Wunderlich, F. T., Peeva, V., Zsurka, G., Kunz, W. S., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.04.005 · Cited by 87 · see citing works
Skeletal muscle mitochondrial H2O2 emission increases with immobilization and decreases after aerobic training in young and older men
Gram, M., Vigelsø, A., Yokota, T., Helge, J. W., Dela, F., & Hey‐Mogensen, M. (2015) · The Journal of Physiology · doi:10.1113/jp270211 · Cited by 86 · see citing works
The exonuclease activity of DNA polymerase γ is required for ligation during mitochondrial DNA replication
Macao, B., Uhler, J. P., Siibak, T., Zhu, X., Shi, Y.-H., Sheng, W., Olsson, M., Stewart, J., Gustafsson, C., & Falkenberg, M. (2015) · Nature Communications · doi:10.1038/ncomms8303 · Cited by 86 · see citing works
Somatic mitochondrial DNA mutations in cancer escape purifying selection and high pathogenicity mutations lead to the oncocytic phenotype: pathogenicity analysis of reported somatic mtDNA mutations in tumors
Pereira, L., Soares, P. A., Máximo, V., & Samuels, D. C. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-53 · Cited by 83 · see citing works
Accumulation of mitochondrial DNA deletions in human retina during aging.
Barreau, E., Brossas, J., Courtois, Y., & Tréton, J. (1996) · PubMed · Cited by 78 · see citing works
Linear mtDNA fragments and unusual mtDNA rearrangements associated with pathological deficiency of MGME1 exonuclease
Nicholls, T. J., Zsurka, G., Peeva, V., Schöler, S., Szczesny, R. J., Cysewski, D., Reyes, A., Kornblum, C., Sciacco, M., Moggio, M., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu336 · Cited by 78 · see citing works
Mitochondrial DNA deletions are associated with non-B DNA conformations
Damas, J., Carneiro, J., Gonçalves, J., Stewart, J. B., Samuels, D. C., Amorim, A., & Pereira, F. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks500 · Cited by 77 · see citing works
In vivo mutagenesis reveals that OriL is essential for mitochondrial DNA replication
Wanrooij, S., Fusté, J. M., Stewart, J. B., Wanrooij, P. H., Samuelsson, T., Larsson, N., Gustafsson, C. M., & Falkenberg, M. (2012) · EMBO Reports · doi:10.1038/embor.2012.161 · Cited by 75 · see citing works
Self-citation
Rapid Accumulation of Deleted Mitochondrial Deoxyribonucleic Acid in Postmenopausal Ovaries
Kitagawa, T., Suganuma, N., Nawa, A., et al. (1993) · Biology of Reproduction · doi:10.1095/biolreprod49.4.730 · Cited by 73 · see citing works
Comparison of Mitochondrial Mutation Spectra in Ageing Human Colonic Epithelium and Disease: Absence of Evidence for Purifying Selection in Somatic Mitochondrial DNA Point Mutations
Greaves, L. C., Elson, J. L., Nooteboom, M., Grady, J. P., Taylor, G. A., Taylor, R. W., Mathers, J. C., Kirkwood, T. B. L., & Turnbull, D. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003082 · Cited by 72 · see citing works

Flagged first, then by citations

Sorted by citations

Mitochondrial and metabolic dysfunction in ageing and age-related diseases
Amorim, J. A., Coppotelli, G., Rolo, A. P., Palmeira, C. M., Ross, J. M., & Sinclair, D. A. (2022) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00626-7 · Cited by 990 · see citing works
The central role of DNA damage in the ageing process
Schumacher, B., Pothof, J., Vijg, J., & Hoeijmakers, J. H. J. (2021) · Nature · doi:10.1038/s41586-021-03307-7 · Cited by 907 · see citing works
Sex differences in biological aging with a focus on human studies
Hägg, S., & Jylhävä, J. (2021) · eLife · doi:10.7554/elife.63425 · Cited by 442 · see citing works
Mitochondria: Central Organelles for Melatonin′s Antioxidant and Anti-Aging Actions
Reiter, R., Tan, D., Rosales-Corral, S., Galano, A., Zhou, X., & Xu, B. (2018) · Molecules · doi:10.3390/molecules23020509 · Cited by 393 · 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
“In mammals, these organelles play a central role in many metabolic processes including–among others–adenosine triphosphate (ATP) generation, β-oxidation of fatty acids, ketone body production, and iron-sulfur cluster synthesis [13,14].”
Background
The role of mitochondria in aging
Jang, J. Y., Blum, A., Liu, J., & Finkel, T. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120842 · Cited by 358 · see citing works
Telomere and its role in the aging pathways: telomere shortening, cell senescence and mitochondria dysfunction
Zhu, Y., Liu, X., Ding, X., Wang, F., & Geng, X. (2019) · Biogerontology · doi:10.1007/s10522-018-9769-1 · Cited by 255 · see citing works
Mitochondrial dysfunction and damage associated molecular patterns (DAMPs) in chronic inflammatory diseases
Dela Cruz, C. S., & Kang, M.-J. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.12.001 · Cited by 255 · see citing works
Calorie Restriction and Aging in Humans
Flanagan, E. W., Most, J., Mey, J. T., & Redman, L. M. (2020) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-122319-034601 · Cited by 239 · see citing works
MOTS-c Is an Exercise-Induced Mitochondrial-Encoded Regulator of Age-Dependent Physical Decline and Muscle Homeostasis
Reynolds, J. C., Lai, R. W., Woodhead, J. S. T., Joly, J. H., Mitchell, C. J., Cameron-Smith, D., Lu, R., Cohen, P., Graham, N. A., Benayoun, B. A., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20790-0 · Cited by 199 · see citing works
Artificial Mitochondria Transfer: Current Challenges, Advances, and Future Applications
Caicedo, A., Aponte, P. M., Cabrera, F., Hidalgo, C., & Khoury, M. (2017) · Stem Cells International · doi:10.1155/2017/7610414 · Cited by 150 · see citing works
Polyphenols as Caloric Restriction Mimetics Regulating Mitochondrial Biogenesis and Mitophagy
Davinelli, S., De Stefani, D., De Vivo, I., & Scapagnini, G. (2020) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2020.02.011 · Cited by 117 · see citing works
The mitochondrial permeability transition: Nexus of aging, disease and longevity
Rottenberg, H., & Hoek, J. B. (2021) · Cells · doi:10.3390/cells10010079 · Cited by 94 · see citing works
Impact of exercise training on muscle mitochondria modifications in older adults: a systematic review of randomized controlled trials
Lippi, L., de Sire, A., Mezian, K., Curci, C., Perrero, L., Turco, A., Andaloro, S., Ammendolia, A., Fusco, N., & Invernizzi, M. (2022) · Aging Clinical and Experimental Research · doi:10.1007/s40520-021-02073-w · Cited by 65 · see citing works
Voluntary exercise normalizes the proteomic landscape in muscle and brain and improves the phenotype of progeroid mice
Ross, J. M., Coppotelli, G., Branca, R. M., Kim, K. M., Lehtiö, J., Sinclair, D. A., & Olson, L. (2019) · Aging Cell · doi:10.1111/acel.13029 · Cited by 41 · see citing works
The Schizosaccharomyces pombe PPR protein Ppr10 associates with a novel protein Mpa1 and acts as a mitochondrial translational activator
Wang, Y., Yan, J., Zhang, Q., Ma, X., Zhang, J., Su, M., Wang, X., & Huang, Y. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx127 · Cited by 34 · see citing works

Mitochondrial genome and human mitochondrial diseases
Mazunin, I., Volodko, N. V., Starikovskaya, E. B., & Sukernik, R. I. (2010) · Molecular Biology · doi:10.1134/s0026893310050018 · Cited by 22 · see citing works
Mitochondrial DNA and OXPHOS Disorders
Zeviani, M., & Carelli, V. (2007) · Springer eBooks · doi:10.1007/0-387-26992-4_6
Mitochondrial diseases
Graff, C., Bui, T., & Larsson, N. (2002) · Best Practice & Research Clinical Obstetrics & Gynaecology · doi:10.1053/beog.2002.0315 · Cited by 17 · see citing works
Self-citation
Comprehensive Molecular Diagnosis of Mitochondrial Disorders: Qualitative and Quantitative Approach
Wong, L. C. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1293.024 · Cited by 19 · see citing works
Progress on the Physiological Function of Mitochondrial DNA and Its Specific Detection and Therapy
Zhang, C., Xue, Y., Wang, L., Wu, Q., Fang, B., Sheng, Y., Bai, H., Peng, B., Yang, N., & Li, L. (2021) · ChemBioChem · doi:10.1002/cbic.202100474 · Cited by 5 · see citing works

Authors: Kauppila, T. E. S., Kauppila, J. H. K., & Larsson, N.-G.
Affiliations: Max Planck Institute for Biology of Ageing (DE)
Karolinska Institutet (SE)
Corresponding author: Larsson, Nils-Göran
ORCID: Larsson, Nils-Göran
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2017-01
Volume: 25
Issue: 1
Pages: 57-71
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2016.09.017
OpenAlex: W2546215880
Cited by: 578
References: 221
Citations by year: 2026: 32 · 2025: 42 · 2024: 65 · 2023: 68 · 2022: 79 · 2021: 82 · 2020: 80 · 2019: 46 · 2018: 56 · 2017: 27 · 2016: 1
FWCI: 3.94
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 374 d)
Locations: Cell Metabolism (publishedVersion)
PubMed (publishedVersion)
Max Planck Digital Library (submittedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion)
Funders: Swedish Research Council (2015-00418)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords: mitochondrial aging, mitochondrial DNA mutations, mitochondrial dysfunction, replication errors, oxidative damage, age-related diseases, lifespan extension, healthspan, mitochondrial biogenesis
MeSH terms: Aging, Animals, Disease, DNA, Mitochondrial, Humans, Mammals, Mitochondria, Reactive Oxygen Species

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

Mammalian Mitochondria and Aging: An Update

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks