MOTS-c: a novel mitochondrial-derived peptide regulating muscle and fat metabolism
Open accessAbstract
Mitochondria are ancient organelles that are thought to have emerged from once free-living α-proto-bacteria. As such, they still possess several bacterial-like qualities, including a semi-autonomous genetic system, complete with an independent genome and a unique genetic code. The bacterial-like circular mitochondrial DNA (mtDNA) has been described to encode 37 genes, including 22 tRNAs, 2 rRNAs, and 13 mRNAs. Two additional peptides reported to originate from the mtDNA, namely humanin (Hashimoto et al., 2001; Ikone et al., 2003; Guo et al., 2003) [1-3] and MOTS-c (mitochondrial ORF of the twelve S c) (Lee et al., 2015) [4], indicate a larger mitochondrial genetic repertoire (Shokolenko and Alexeyev, 2015) [5]. These mitochondrial-derived peptides (MDPs) have profound and distinct biological activities and provide a paradigm-shifting concept of active mitochondrial-encoded signals that act at the cellular and organismal level (i.e. mitochondrial hormone) (da Cunha et al., 2015; Quiros et al., 2016) [6,7]. Considering that mitochondria are the single most important metabolic organelle, it is not surprising that these MDPs have metabolic actions. MOTS-c has been shown to target the skeletal muscle and enhance glucose metabolism. As such, MOTS-c has implications in the regulation of obesity, diabetes, exercise, and longevity, representing an entirely novel mitochondrial signaling mechanism to regulate metabolism within and between cells.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
MOTS-C appears mainly in skeletal muscle.
“The short open reading frame found within the mitochondrial 12S rRNA known as MOTS-C (mitochondrial open reading frame of the 12S rRNA-c) appears mainly in skeletal muscle and activate AMPK (Lee et al., 2016).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2016
MOTS-C activates AMPK.
“The short open reading frame found within the mitochondrial 12S rRNA known as MOTS-C (mitochondrial open reading frame of the 12S rRNA-c) appears mainly in skeletal muscle and activate AMPK (Lee et al., 2016).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2016
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works
López-Otín, C., Blasco, M. A., Partridge, L., Serrano, M., & Kroemer, G. (2013) · Cell · doi:10.1016/j.cell.2013.05.039 · Cited by 14,982 · see citing works
AMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602 · see citing works
Rapid evolution of animal mitochondrial DNA
Brown, W. M., George, M., & Wilson, A. C. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.4.1967 · Cited by 3,439 · see citing works
Serine, glycine and one-carbon units: cancer metabolism in full circle
Locasale, J. W. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3557 · Cited by 1,725 · see citing works
AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function
Hardie, D. G. (2011) · Genes & Development · doi:10.1101/gad.17420111 · Cited by 1,638 · see citing works
The mitochondrial genome: structure, transcription, translation and replication
Taanman, J.-W. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(98)00161-3 · Cited by 1,635 · see citing works
Price, N. L., Gomes, A. P., Ling, A. J. Y., Duarte, F. V., Martin-Montalvo, A., North, B. J., Agarwal, B., Ye, L., Ramadori, G., Teodoro, J. S., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.003 · Cited by 1,602 · see citing works
NAD+ and sirtuins in aging and disease
Imai, S.-I., & Guarente, L. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.04.002 · Cited by 1,481 · see citing works
Metformin improves healthspan and lifespan in mice
Martin-Montalvo, A., Mercken, E. M., Mitchell, S. J., Palacios, H. H., Mote, P. L., Scheibye-Knudsen, M., Gomes, A. P., Ward, T. M., Minor, R. K., Blouin, M.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3192 · Cited by 1,445 · see citing works
NAD <sup>+</sup> in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319 · see citing works
AMPK and PPARδ Agonists Are Exercise Mimetics
Narkar, V. A., Downes, M., Yu, R. T., Embler, E., Wang, Y.-X., Banayo, E., Mihaylova, M. M., Nelson, M. C., Zou, Y., Juguilon, H., et al. (2008) · Cell · doi:10.1016/j.cell.2008.06.051 · Cited by 1,222 · see citing works
The role of mitochondria in aging
Bratic, A., & Larsson, N.-G. (2013) · Journal of Clinical Investigation · doi:10.1172/jci64125 · Cited by 1,087 · see citing works
The Cell Non-Autonomous Nature of Electron Transport Chain-Mediated Longevity
Durieux, J., Wolff, S., & Dillin, A. (2011) · Cell · doi:10.1016/j.cell.2010.12.016 · Cited by 1,059 · cited 1× · see citing works
“For instance, an interesting study in Caenorhabditis elegans showed that an imbalance between mitochondrial- and nuclear-encoded proteins in neurons activates the mitochondrial unfolded protein response (UPRmt) in intestinal cells, through an unidentified mi-tokine [18,19].”
BackgroundMerrill, G. F., Kurth, E. J., Hardie, D. G., & Winder, W. W. (1997) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1997.273.6.e1107 · Cited by 1,048 · 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
Folate and DNA Methylation: A Review of Molecular Mechanisms and the Evidence for Folate's Role
Crider, K. S., Yang, T. P., Berry, R. J., & Bailey, L. B. (2012) · Advances in Nutrition · doi:10.3945/an.111.000992 · Cited by 1,022 · see citing works
Metformin retards aging in C. elegans by altering microbial folate and methionine metabolism
Cabreiro, F., Au, C., Leung, K.-Y., Vergara-Irigaray, N., Cochemé, H. M., Noori, T., Weinkove, D., Schuster, E., Greene, N. D. E., & Gems, D. (2013) · Cell · doi:10.1016/j.cell.2013.02.035 · Cited by 967 · see citing works
Eukaryotic evolution, changes and challenges
Embley, T. M., & Martin, W. (2006) · Nature · doi:10.1038/nature04546 · Cited by 867 · see citing works
Mitonuclear communication in homeostasis and stress
Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787 · see citing works
Miller, R. A., Buehner, G., Chang, Y., Harper, J. M., Sigler, R. E., & Smith‐Wheelock, M. (2005) · Aging Cell · doi:10.1111/j.1474-9726.2005.00152.x · Cited by 734 · see citing works
Lee, C., Zeng, J., Drew, B. G., Sallam, T., Martin-Montalvo, A., Wan, J., Kim, S.-J., Mehta, H., Hevener, A. L., de Cabo, R., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.009 · Cited by 715 · see citing works
Self-citationBrown and beige fat in humans: thermogenic adipocytes that control energy and glucose homeostasis
Sidossis, L. S., & Kajimura, S. (2015) · Journal of Clinical Investigation · doi:10.1172/jci78362 · Cited by 710 · see citing works
Yun, J., & Finkel, T. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.01.011 · Cited by 626 · see citing works
INTRAMITOCHONDRIAL FIBERS WITH DNA CHARACTERISTICS
Nass, M. M. K., & Nass, S. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.19.3.593 · Cited by 625 · see citing works
Hashimoto, Y., Niikura, T., Tajima, H., Yasukawa, T., Sudo, H., Ito, Y., Kita, Y. A., Kawasumi, M., Kouyama, K., Doyu, M., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101133498 · Cited by 624 · see citing works
Humanin peptide suppresses apoptosis by interfering with Bax activation
Guo, B., Zhai, D., Cabezas, E., Welsh, K., Nouraini, S., Satterthwait, A. C., & Reed, J. C. (2003) · Nature · doi:10.1038/nature01627 · Cited by 619 · see citing works
Low methionine ingestion by rats extends life span.
Orentreich, N., Matias, J. R., Felice, A. D., & Zimmerman, J. (1993) · Journal of NutriLife · doi:10.1093/jn/123.2.269 · Cited by 608 · see citing works
Detection and Quantitation of Circulating Human Irisin by Tandem Mass Spectrometry
Jedrychowski, M. P., Wrann, C. D., Paulo, J. A., Gerber, K. K., Szpyt, J., Robinson, M. M., Nair, K. S., Gygi, S. P., & Spiegelman, B. M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.08.001 · Cited by 569 · see citing works
Evolution of Mitochondria as Signaling Organelles
Chandel, N. S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.013 · Cited by 555 · see citing works
Emerging evidence for functional peptides encoded by short open reading frames
Andrews, S. J., & Rothnagel, J. A. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3520 · Cited by 547 · see citing works
AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
McGee, S. L., van Denderen, B. J. W., Howlett, K. F., Mollica, J., Schertzer, J. D., Kemp, B. E., & Hargreaves, M. (2008) · Diabetes · doi:10.2337/db07-0843 · Cited by 455 · see citing works
Metabolic flux and the regulation of mammalian cell growth
Locasale, J. W., & Cantley, L. C. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.014 · Cited by 449 · see citing works
Methionine restriction increases blood glutathione and longevity in F344 rats
Richie, J. P., Leutzinger, Y., Parthasarathy, S., Maixoy, V., Orentreich, N., & Zimmerman, J. A. (1994) · The FASEB Journal · doi:10.1096/fasebj.8.15.8001743 · Cited by 363 · see citing works
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
Endosymbiotic origin and differential loss of eukaryotic genes
Ku, C., Sathi, S. N., Roettger, M., Sousa, F. L., Lockhart, P. J., Bryant, D., Hazkani‐Covo, E., McInerney, J. O., Landan, G., & Martin, W. F. (2015) · Nature · doi:10.1038/nature14963 · Cited by 353 · see citing works
The molecular determinants of de novo nucleotide biosynthesis in cancer cells
Tong, X., Zhao, F., & Thompson, C. B. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.01.002 · Cited by 351 · see citing works
Fujii, N., Hayashi, T., Hirshman, M. F., Smith, J. T., Habinowski, S. A., Kaijser, L., Mu, J., Ljungqvist, O., Birnbaum, M. J., Witters, L. A., et al. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3073 · Cited by 351 · see citing works
INTRAMITOCHONDRIAL FIBERS WITH DNA CHARACTERISTICS
Nass, S., & Nass, M. M. K. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.19.3.613 · Cited by 332 · see citing works
Extensive translation of small Open Reading Frames revealed by Poly-Ribo-Seq
Aspden, J. L., Eyre‐Walker, Y. C., Phillips, R. J., Amin, U., Mumtaz, M. A., Brocard, M., & Couso, J. P. (2014) · eLife · doi:10.7554/elife.03528 · Cited by 331 · see citing works
Cloonan, S. M., & Choi, A. M. K. (2016) · Journal of Clinical Investigation · doi:10.1172/jci81113 · Cited by 322 · cited 1× · see citing works
“MOTS-c is also implicated in lung [66] and heart disease [67].”
BackgroundCobb, L. J., Lee, C. D., Xiao, J., Yen, K., Wong, R. G., Nakamura, H. K., Mehta, H. H., Gao, Q., Ashur, C., Huffman, D. M., et al. (2016) · Aging · doi:10.18632/aging.100943 · Cited by 288 · see citing works
Self-citationDiscovery and characterization of smORF-encoded bioactive polypeptides
Saghatelian, A., & Couso, J. P. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1964 · Cited by 286 · see citing works
Humanin: a harbinger of mitochondrial-derived peptides
Lee, C., Yen, K., & Cohen, P. (2013) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2013.01.005 · Cited by 284 · see citing works
Self-citationIkonen, M., Liu, B., Hashimoto, Y., Ma, L., Lee, K., Niikura, T., Nishimoto, I., & Cohen, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135111100 · Cited by 279 · see citing works
Self-citationZimmerman, J. A. (2003) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00149-3 · Cited by 279 · see citing works
Lee, B. C., Kaya, A., Ma, S., Kim, G., Gerashchenko, M. V., Yim, S. H., Hu, Z., Harshman, L. G., & Gladyshev, V. N. (2014) · Nature Communications · doi:10.1038/ncomms4592 · Cited by 270 · see citing works
Humanin: A Novel Central Regulator of Peripheral Insulin Action
Muzumdar, R. H., Huffman, D. M., Atzmon, G., Buettner, C., Cobb, L. J., Fishman, S., Budagov, T., Cui, L., Einstein, F. H., Poduval, A., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006334 · Cited by 248 · see citing works
Self-citationContinued Colonization of the Human Genome by Mitochondrial DNA
Ricchetti, M., Tekaia, F., & Dujon, B. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020273 · Cited by 227 · see citing works
Species identification through mitochondrial rRNA genetic analysis
Yang, L., Tan, Z., Wang, D., Xue, L., Guan, M., Huang, T., & Li, R. (2014) · Scientific Reports · doi:10.1038/srep04089 · Cited by 224 · see citing works
Lifespan Extension by Methionine Restriction Requires Autophagy-Dependent Vacuolar Acidification
Ruckenstuhl, C., Netzberger, C., Entfellner, I., Carmona‐Gutiérrez, D., Kickenweiz, T., Stekovic, S., Gleixner, C., Schmid, C., Klug, L., Sorgo, A. G., et al. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004347 · Cited by 223 · see citing works
Hashimoto, Y., Ito, Y., Niikura, T., Shao, Z., Hata, M., Oyama, F., & Nishimoto, I. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4765 · Cited by 223 · see citing works
Hyperinsulinemic–Euglycemic Clamp to Assess Insulin Sensitivity In Vivo
Kim, J. K. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-448-3_15 · Cited by 215 · see citing works
The emerging role of the mitochondrial-derived peptide humanin in stress resistance
Yen, K., Lee, C. D., Mehta, H. H., & Cohen, P. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0203 · Cited by 208 · see citing works
Self-citationThe coordination of nuclear and mitochondrial communication during aging and calorie restriction
Finley, L. W. S., & Haigis, M. C. (2009) · Ageing Research Reviews · doi:10.1016/j.arr.2009.03.003 · Cited by 207 · see citing works
Musclin is an activity-stimulated myokine that enhances physical endurance
Subbotina, E., Sierra, A., Zhu, Z., Gao, Z., Koganti, S. R. K., Reyes, S., Stepniak, E., Walsh, S. A., Acevedo, M. R., Perez-Terzic, C. M., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1514250112 · Cited by 198 · see citing works
Structural basis of AMPK regulation by adenine nucleotides and glycogen
Li, X., Wang, L., Zhou, X. E., Ke, J., de Waal, P. W., Gu, X., Tan, M. H. E., Wang, D., Wu, D., Xu, H. E., et al. (2014) · Cell Research · doi:10.1038/cr.2014.150 · Cited by 197 · see citing works
Bachar, A., Scheffer, L., Schroeder, A. S., Nakamura, H. K., Cobb, L. J., Oh, Y. K., Lerman, L. O., Pagano, R. E., Cohen, P., & Lerman, A. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq191 · Cited by 182 · see citing works
Self-citationMitohormesis in exercise training
Merry, T. L., & Ristow, M. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.11.032 · Cited by 176 · see citing works
Hill, G. E. (2015) · Molecular Biology and Evolution · doi:10.1093/molbev/msv104 · Cited by 174 · see citing works
Mitochondrial Retrograde Signaling: Triggers, Pathways, and Outcomes
da Cunha, F. M., Torelli, N. Q., & Kowaltowski, A. J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/482582 · Cited by 168 · see citing works
Acute Humanin Therapy Attenuates Myocardial Ischemia and Reperfusion Injury in Mice
Muzumdar, R. H., Huffman, D. M., Calvert, J. W., Jha, S. K., Weinberg, Y., Cui, L., Nemkal, A., Atzmon, G., Klein, L., Gundewar, S., et al. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.205997 · Cited by 162 · see citing works
Improved Identification and Analysis of Small Open Reading Frame Encoded Polypeptides
Ma, J., Diedrich, J. K., Jungreis, I., Donaldson, C. J., Vaughan, J. M., Kellis, M., Yates, J. R., & Saghatelian, A. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00191 · Cited by 145 · see citing works
The Crabtree effect: a review.
Ibsen, K. H. (1961) · PubMed · Cited by 144 · see citing works
Establishment of Human Cell Lines Lacking Mitochondrial DNA
Hashiguchi, K., & Zhang-Akiyama, Q.-M. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-521-3_23 · Cited by 141 · see citing works
Mutation hot spots in mammalian mitochondrial DNAPreprint
Galtier, N., Enard, D., Radondy, Y., Bazin, É., & Belkhir, K. (2005) · Genome Research · doi:10.1101/gr.4305906 · Cited by 139 · 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
Maeda, S., McCandliss, R., Gross, M. S., et al. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7010 · Cited by 125 · see citing works
Systemic Nutrient and Stress Signaling via Myokines and Myometabolites
Rai, M., & Demontis, F. (2016) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021115-105305 · Cited by 123 · see citing works
Corominas-Faja, B., Quirantes‐Piné, R., Oliveras‐Ferraros, C., Vázquez‐Martín, A., Cufí, S., Martı́n-Castillo, B., Micol, V., Joven, J., Segura‐Carretero, A., & Menéndez, J. A. (2012) · Aging · doi:10.18632/aging.100472 · Cited by 121 · see citing works
A Mitochondrial Ribosomal and RNA Decay Pathway Blocks Cell Proliferation
Richter, U., Lahtinen, T., Marttinen, P., Myöhänen, M., Greco, D., Cannino, G., Jacobs, H. T., Lietzén, N., Nyman, T. A., & Battersby, B. J. (2013) · Current Biology · doi:10.1016/j.cub.2013.02.019 · Cited by 119 · see citing works
Fetterman, J. L., Zelickson, B. R., Johnson, L. W., Moellering, D. R., Westbrook, D. G., Pompilius, M., Sammy, M. J., Johnson, M. S., Dunham‐Snary, K. J., Cao, X., et al. (2013) · Biochemical Journal · doi:10.1042/bj20130029 · Cited by 100 · see citing works
The mitochondrial‐derived peptide <scp>MOTS</scp> ‐c: a player in exceptional longevity?
Fuku, N., Pareja‐Galeano, H., Zempo, H., Alis, R., Arai, Y., Lucia, A., & Hirose, N. (2015) · Aging Cell · doi:10.1111/acel.12389 · Cited by 98 · see citing works
Mitochondrial DNA: A disposable genome?
Shokolenko, I. N., & ALEXEYEV, M. F. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.05.016 · Cited by 83 · see citing works
<scp>IGF</scp>‐I regulates the age‐dependent signaling peptide humanin
Lee, C., Wan, J., Miyazaki, B., Fang, Y., Guevara‐Aguirre, J., Yen, K., Longo, V., Bartke, A., & Cohen, P. (2014) · Aging Cell · doi:10.1111/acel.12243 · Cited by 80 · see citing works
Self-citationEnrichment of longevity phenotype in mtDNA haplogroups D4b2b, D4a, and D5 in the Japanese population
Alexe, G., Fuku, N., Bilal, E., Ueno, H., Nishigaki, Y., Fujita, Y., Ito, M., Arai, Y., Hirose, N., Bhanot, G., et al. (2007) · Human Genetics · doi:10.1007/s00439-007-0330-6 · Cited by 76 · see citing works
Caloric restriction and exercise “mimetics”: ready for prime time
Handschin, C. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2015.11.009 · Cited by 72 · see citing works
Mitochondrial Stress Signals Revise an Old Aging Theory
Woo, D. K., & Shadel, G. S. (2011) · Cell · doi:10.1016/j.cell.2010.12.023 · Cited by 60 · see citing works
Mitochondrial signaling in the vascular endothelium: beyond reactive oxygen species
Kadlec, A. O., Beyer, A., Ait‐Aissa, K., & Gutterman, D. D. (2016) · Basic Research in Cardiology · doi:10.1007/s00395-016-0546-5 · Cited by 59 · see citing works
A Mitochondrially Encoded Hormone Ameliorates Obesity and Insulin Resistance
Zarse, K., & Ristow, M. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.02.013 · Cited by 56 · see citing works
The biochemistry and cell biology of aging: metabolic regulation through mitochondrial signaling
Long, Y. C., Tan, T. M. C., Inoue, T., & Tang, B. L. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00665.2013 · Cited by 55 · see citing works
Exercise Pills: At the Starting Line
Li, S., & Laher, I. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.014 · Cited by 54 · see citing works
Mitochondrial–nuclear genome interactions in non-alcoholic fatty liver disease in mice
Betancourt, A. M., King, A. L., Fetterman, J. L., Millender-Swain, T., Finley, R. D., Oliva, C. R., Crowe, D. R., Ballinger, S. W., & Bailey, S. M. (2014) · Biochemical Journal · doi:10.1042/bj20131433 · Cited by 51 · see citing works
Thevis, M., & Schänzer, W. (2016) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.7470 · Cited by 43 · see citing works
Lane, N. J. (2011) · Science · doi:10.1126/science.1214012 · Cited by 41 · see citing works
Pesole, G., Allen, J. F., Lane, N. J., et al. (2012) · EMBO Reports · doi:10.1038/embor.2012.57 · Cited by 40 · see citing works
Mitochondrial-nuclear DNA mismatch matters
Dunham‐Snary, K. J., & Ballinger, S. W. (2015) · Science · doi:10.1126/science.aac5271 · Cited by 38 · see citing works
Hall, S. S. (2015) · Science · doi:10.1126/science.349.6254.1274 · Cited by 37 · see citing works
Effect of mitochondrial stress on systemic metabolism
Lee, M. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12822 · Cited by 32 · see citing works
Horan, M. P., Gemmell, N. J., & Wolff, J. N. (2013) · European Journal of Human Genetics · doi:10.1038/ejhg.2013.75 · Cited by 26 · see citing works
Tsuzuki, T., Nomiyama, H., Setoyama, C., Maeda, S., 島田, 和., & Pestka, S. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)90833-1 · Cited by 25 · see citing works
Lee, D. E., Brown, J. L., Rosa, M. E., Brown, L. A., Perry, R. A., Washington, T. A., & Greene, N. P. (2016) · Acta Physiologica · doi:10.1111/apha.12687 · Cited by 24 · see citing works
The hidden risks for ‘three-person’ babies
Hamilton, G. (2015) · Nature · doi:10.1038/525444a · Cited by 23 · see citing works
The role of mitochondrial derived peptides (MDPs) in metabolism
Alis, R., Lucía, A., Blesa, J. R., & Sanchis‐Gomar, F. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25023 · Cited by 22 · see citing works
AICAR inhibits oxygen consumption by intact skeletal muscle cells in culture
Spangenburg, E. E., Jackson, K. C., & Schuh, R. A. (2013) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-013-0269-0 · Cited by 10 · see citing works
Hunter, P. (2016) · EMBO Reports · doi:10.15252/embr.201541835 · Cited by 9 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [83]Li S Laher I Exercise pills: at the starting line Trends PharmacolSci 2015 26439443
- [89]Fuku N The mitochondrial-derived peptide MOTS-c: a player in exceptional longevity? Aging Cell 2015 PMC4693465 26289118
Cited by
Sorted by citations
Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity
López-Lluch, G. (2017) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2016.12.005 · Cited by 103 · see citing works
“The short open reading frame found within the mitochondrial 12S rRNA known as MOTS-C (mitochondrial open reading frame of the 12S rRNA-c) appears mainly in skeletal muscle and activate AMPK (Lee et al., 2016).”
BackgroundThe Oxygen Paradox, the French Paradox, and age-related diseases
Davies, J. M. S., Cillard, J., Friguet, B., Cadenas, E., Cadet, J., Cayce, R., Fishmann, A., Liao, D., Bulteau, A.-L., Derbré, F., et al. (2017) · GeroScience · doi:10.1007/s11357-017-0002-y · Cited by 82 · see citing works
“…encoded within the mtDNA, has been shown to normalize mitochondrial function and to prevent metabolic deterioration, vascular disease, diabetes, and neurodegeneration, namely the mitochondrial-derived peptides, humanin (Yen et al. 2013), MOTS-c (Lee et al. 2016a), and SHLPs (Cobb et al. 2016).”
BackgroundSelf-citationSystemic Regulators of Skeletal Muscle Regeneration in Obesity
Sinha, I., Sakthivel, D., & Varon, D. E. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00029 · Cited by 39 · see citing works
- Authors
- Lee, C., Kim, K. H., & Cohen, P.
- Affiliations
- University of Southern California (US)
- Corresponding author
- Cohen, Pinchas
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2016-11
- Volume
- 100
- Pages
- 182-187
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC5116416
- OpenAlex
- W2396381638
- Cited by
- 178
- References
- 96
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 19 · 2023: 18 · 2022: 20 · 2021: 17 · 2020: 27 · 2019: 16 · 2018: 19 · 2017: 9 · 2016: 6
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Health (1R01GM090311, 1R01ES020812, 1P01AG034906)
- Ellison Medical Foundation
- Zumberge award
- SC-CTSI
- Hanson Thorell Family Research Award
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- MOTS-c, mitochondrial peptides, mitochondrial DNA, humanin, muscle metabolism, fat metabolism, glucose metabolism, obesity, diabetes mellitus, physical activity, longevity, mitochondrial signaling
- MeSH terms
- Adipose Tissue, Animals, DNA, Mitochondrial, Glucose, Humans, Mitochondria, Signal Transduction, Muscle, Skeletal, Mitochondrial Proteins, Intracellular Signaling Peptides and Proteins, Genes, Mitochondrial, Lipid Metabolism, Mice
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
