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The Mitochondrial-Derived Peptide MOTS-c Promotes Metabolic Homeostasis and Reduces Obesity and Insulin Resistance
Open accessAbstract
Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA. Here we report a sORF within the mitochondrial 12S rRNA encoding a 16-amino-acid peptide named MOTS-c (mitochondrial open reading frame of the 12S rRNA-c) that regulates insulin sensitivity and metabolic homeostasis. Its primary target organ appears to be the skeletal muscle, and its cellular actions inhibit the folate cycle and its tethered de novo purine biosynthesis, leading to AMPK activation. MOTS-c treatment in mice prevented age-dependent and high-fat-diet-induced insulin resistance, as well as diet-induced obesity. These results suggest that mitochondria may actively regulate metabolic homeostasis at the cellular and organismal level via peptides encoded within their genome.
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“whilst recent studies have demonstrated that MOTS-c may also exert protective effects against diet-induced obesity and insulin resistance by altering skeletal muscle gene expression related to metabolism and inflammation”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [117]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Mitochondrial-derived peptides such as MOTS-c may further promote fatigue resistance and enhance muscle strength by activating key metabolic pathways and supporting mitochondrial health”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [117]
Experimental — accuracy not yet measuredIn the citing paper
“The mitochondrial open reading frame of the 12S rRNA-c (MOTS-c) is a bioactive mitochondrial-derived peptide shown to activate the AMPK pathway and modulate metabolic homeostasis [193].”
From AMPK, Mitochondrial Function, and Cardiovascular Disease (2020) · cites this paper as [193]
In the citing paper
“Interestingly, treatment with MOTS-C in mice prevent agedependent and high-fat diet induced insulin resistance and obesity indicating an important role of mitochondria in the control of fat metabolism probably producing prolongevity effects (Fuku et al., 2015; Lee et al., 2015).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2015
In the citing paper
“treatment with MOTS-C in mice prevent agedependent and high-fat diet induced insulin resistance and obesity indicating an important role of mitochondria in the control of fat metabolism probably producing prolongevity effects (Fuku et al., 2015; Lee et al., 2015).”
From Mitochondrial Activity and Dynamics Changes Regarding Metabolism in Ageing and Obesity (2017) · cites this paper as Lee et al., 2015
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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
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
Physiological Roles of Mitochondrial Reactive Oxygen Species
Sena, L. A., & Chandel, N. S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.025 · Cited by 2,632
Not So Different After All: A Comparison of Methods for Detecting Amino Acid Sites Under Selection
Pond, S. L. K., & Frost, S. D. W. (2005) · Molecular Biology and Evolution · doi:10.1093/molbev/msi105 · Cited by 2,320
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
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
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
Pearson, K. J., Baur, J. A., Lewis, K. N., Peshkin, L., Price, N. L., Labinskyy, N., Swindell, W. R., Kamara, D., Minor, R. K., Perez, E., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.06.011 · Cited by 1,162
Analysis of Microarray Data Using Z Score Transformation
Cheadle, C., Vawter, M. P., Freed, W. J., & Becker, K. G. (2003) · Journal of Molecular Diagnostics · doi:10.1016/s1525-1578(10)60455-2 · Cited by 1,150
Metabolism of Inflammation Limited by AMPK and Pseudo-Starvation
O'Neill, L. A. J., & Hardie, D. G. (2013) · Nature · doi:10.1038/nature11862 · Cited by 1,133
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Items 101–200 of 723
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Yang, Y., Gao, H., Zhou, H., Liu, Q., Qi, Z., Zhang, Y., & Zhang, J. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109075 · Cited by 74
Mitochondrial-derived peptides in aging and age-related diseases
Kim, S., Miller, B., Kumagai, H., Silverstein, A. R., Flores, M., & Yen, K. (2020) · GeroScience · doi:10.1007/s11357-020-00262-5 · Cited by 74
Self-citationPlacental mitochondrial dysfunction with metabolic diseases: Therapeutic approaches
Hebert, J. F., & Myatt, L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165967 · Cited by 73
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
Zhao, Y., Zhu, S., Wang, H., Wang, L., Du, T., Ye, Z., Zhai, D., Zhu, Z. G., Tian, X., Lu, Z., et al. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104381 · Cited by 71
Lopes, C., Mota, S., Deus, C., Tavares, H., & Beatriz, M. (2022) · Cells · doi:10.3390/cells11152364 · Cited by 77
Mitochondria-Derived Peptide MOTS-c: Effects and Mechanisms Related to Stress, Metabolism and Aging
Wan, W., Zhang, L., Lin, Y., Rao, X., Wang, X., Hua, F., & Ying, J. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-03885-2 · Cited by 70
Mitochondrial pathways in human health and aging
Bornstein, R., González, B., & Johnson, S. C. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.07.007 · Cited by 71
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Ferreira, T., & Rodrı́guez, S. (2024) · Genes · doi:10.3390/genes15050617 · Cited by 70
Microproteins: Overlooked regulators of physiology and disease
Hassel, K. R., Brito‐Estrada, O., & Makarewich, C. A. (2023) · iScience · doi:10.1016/j.isci.2023.106781 · Cited by 74
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Kumagai, H., Coelho, A. R., Wan, J., Mehta, H. H., Yen, K., Huang, A., Zempo, H., Fuku, N., Maeda, S., Oliveira, P. J., et al. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00275.2020 · Cited by 68
Self-citationYin, Y., Pan, Y., He, J., Zhong, H., Wu, Y., Ji, C., Liu, L., & Cui, X. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105987 · Cited by 66
Mitochondrial proteome research: the road ahead
Baker, Z. N., Forny, P., & Pagliarini, D. J. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00650-7 · Cited by 67
Kim, S., Miller, B., Mehta, H. H., Xiao, J., Wan, J., Arpawong, T. E., Yen, K., & Cohen, P. (2019) · Physiological Reports · doi:10.14814/phy2.14171 · Cited by 66
Self-citationAnsari, M. A., Chauhan, W., Shoaib, S., Alyahya, S. A., Ali, M., Ashraf, H., Alomary, M. N., & Al-Suhaimi, E. A. (2023) · International Journal of Obesity · doi:10.1038/s41366-023-01369-3 · Cited by 66
Gidlund, E., von Walden, F., Venojärvi, M., Risérus, U., Heinonen, O. J., Norrbom, J., & Sundberg, C. J. (2016) · Physiological Reports · doi:10.14814/phy2.13063 · Cited by 64
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Chu, Q., Rathore, A., Diedrich, J. K., Donaldson, C. J., Yates, J. R., & Saghatelian, A. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00265 · Cited by 66
Lu, H., Tang, S., Xue, C., Liu, Y., Wang, J., Zhang, W., Luo, W., & Chen, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102456 · Cited by 63
Wang, J., Suo, Y., Zhang, J., Zou, Q., Tan, X., Yuan, T., Liu, Z., & Liu, X. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.03.008 · Cited by 62
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Oliveira, G. L., Coelho, A. R., Marques, R., & Oliveira, P. J. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.166016 · Cited by 65
Mitochondrial-encoded MOTS-c prevents pancreatic islet destruction in autoimmune diabetes
Kong, B. S., Min, S. H., Lee, C. D., & Cho, Y. M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109447 · Cited by 69
Self-citationHu, Z., Yang, L., Zhang, M., Tang, H., Huang, Y., Su, Y., Ding, Y., Li, C. V., Wang, M., Zhou, Y., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.04.012 · Cited by 62
Plasma Mots-C Levels are Associated with Insulin Sensitivity in Lean but Not in Obese Individuals
Cataldo, L. R., Fernández‐Verdejo, R., Santos, J. L., & Galgani, J. E. (2018) · Journal of Investigative Medicine · doi:10.1136/jim-2017-000681 · Cited by 62
A short ORF-encoded transcriptional regulator
Koh, M., Ahmad, I., Ko, Y., Zhang, Y., Martinez, T. F., Diedrich, J. K., Chu, Q., Moresco, J. J., Erb, M. A., Saghatelian, A., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2021943118 · Cited by 62
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
Cnm1 mediates nucleus–mitochondria contact site formation in response to phospholipid levels
Eisenberg‐Bord, M., Zung, N., Collado, J., Drwesh, L., Fenech, E. J., Fadel, A., Dezorella, N., Bykov, Y. S., Rapaport, D., Fernández‐Busnadiego, R., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104100 · Cited by 60
Extending human healthspan and longevity: a symposium report
DeVito, L. M., Barzilai, N., Cuervo, A. M., Niedernhofer, L. J., Milman, S., Levine, M. E., Promislow, D., Ferrucci, L., Kuchel, G. A., Mannick, J. B., et al. (2021) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14681 · Cited by 58
Self-citationCancer-related micropeptides encoded by ncRNAs: Promising drug targets and prognostic biomarkers
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de Araujo, C. B., Heimann, A. S., Remer, R. A., Russo, L. C., Colquhoun, A., Forti, F. L., & Ferro, E. S. (2019) · Biomolecules · doi:10.3390/biom9040150 · Cited by 59
Woodhead, J. S. T., D’Souza, R. F., Hedges, C. P., Wan, J., Berridge, M. V., Cameron-Smith, D., Cohen, P., Hickey, A. J. R., Mitchell, C. J., & Merry, T. L. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00032.2020 · Cited by 57
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Thevis, M., Walpurgis, K., & Thomas, A. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04639 · Cited by 60
Guo, Q., Chang, B., Yu, Q., Xu, S.-T., Yi, X., & Cao, S. (2020) · Diabetologia · doi:10.1007/s00125-020-05269-3 · Cited by 57
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Alexeyev, M. F. (2016) · Frontiers in bioscience · doi:10.2741/4520 · Cited by 56
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Okada, A. K., Teranishi, K., Lobo, F., Isas, J. M., Xiao, J., Yen, K., Cohen, P., & Langen, R. (2017) · Scientific Reports · doi:10.1038/s41598-017-08372-5 · Cited by 56
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Wang, X., Weidling, I. W., Koppel, S. J., Menta, B. W., Ortiz, J. P., Kalani, A., Wilkins, H., & Swerdlow, R. H. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.09.006 · Cited by 56
D’Souza, R. F., Woodhead, J. S. T., Hedges, C. P., Zeng, N., Wan, J., Kumagai, H., Lee, C., Cohen, P., Cameron-Smith, D., Mitchell, C. J., et al. (2020) · Aging · doi:10.18632/aging.102944 · Cited by 55
Self-citationDecoding the Rosetta stone of mitonuclear communication
English, J., Son, J. M., Cardamone, M. D., Lee, C., & Perissi, V. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.105161 · Cited by 55
Self-citationSocialized mitochondria: mitonuclear crosstalk in stress
Kim, K. H., & Lee, C. B. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01211-4 · Cited by 62
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Li, S., & Laher, I. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.08.014 · Cited by 54
Guo, D., Liu, W., Zhang, X., Zhao, M., Zhu, B., Hou, T., & He, H. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900525 · Cited by 54
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Zempo, H., Kim, S., Fuku, N., Nishida, Y., Higaki, Y., Wan, J., Yen, K., Miller, B., Vicinanza, R., Miyamoto‐Mikami, E., et al. (2021) · Aging · doi:10.18632/aging.202529 · Cited by 55
Self-citationMitochondrial DNA variation in Alzheimer’s disease reveals a unique microprotein called SHMOOSE
Miller, B., Kim, S., Mehta, H. H., Cao, K., Kumagai, H., Thumaty, N., Leelaprachakul, N., Braniff, R. G., Jiao, H., Vaughan, J. M., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01769-3 · Cited by 55
Self-citationMin, K., Davila, S., Zealy, R. W., Lloyd, L. T., Lee, I. Y., Lee, R., Roh, K.-H., Jung, A., Jemielity, J., Choi, E., et al. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.05.002 · Cited by 58
Mitonuclear genomics and aging
Reynolds, J. C., Bwiza, C. P., & Lee, C. D. (2020) · Human Genetics · doi:10.1007/s00439-020-02119-5 · Cited by 56
Self-citationWei, M., Gan, L., Liu, Z., Liu, L., Chang, J.-R., Yin, D.-C., Cao, H.-L., Su, X.-L., & Smith, W. W. (2020) · Cardiorenal Medicine · doi:10.1159/000503224 · Cited by 52
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Yong, C. Q. Y., & Tang, B. L. (2018) · Cells · doi:10.3390/cells7080105 · Cited by 51
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Dal, F., & Ahbab, M. A. (2024) · Cambridge Prisms Plastics · doi:10.1017/plc.2024.6 · Cited by 56
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Chen, Y., Ho, L., & Tergaonkar, V. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.10.038 · Cited by 50
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Meng, K., Lu, S., Li, Y., Hu, L., Zhang, J., Cao, Y., Wang, Y., Zhang, C. Z., & He, Q. (2023) · EMBO Reports · doi:10.15252/embr.202256282 · Cited by 49
Singh, B., Modica-Napolitano, J. S., & Singh, K. K. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.05.004 · Cited by 49
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Xiao, M.-H., Lin, Y.-F., Xie, P.-P., Chen, H.-X., Deng, J., Zhang, W., Zhao, N., Xie, C., Meng, Y., Liu, X., et al. (2021) · Molecular Therapy · doi:10.1016/j.ymthe.2021.08.032 · Cited by 47
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Rochette, L., Méloux, A., Zeller, M., Cottin, Y., & Vergely, C. (2020) · Archives of cardiovascular diseases · doi:10.1016/j.acvd.2020.03.020 · Cited by 46
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Yin, X., Jing, Y., & Xu, H. (2019) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1571919 · Cited by 46
Mehta, H. H., Xiao, J., Ramírez, R., Miller, B., Kim, S., Cohen, P., & Yen, K. (2019) · Metabolomics · doi:10.1007/s11306-019-1549-7 · Cited by 46
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Yin, X., Quan, C., Yuanyuan, J., & Xu, H. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2019.106174 · Cited by 46
Yin, X., Jing, Y., Chen, Q., Abbas, A. B., Hu, J., & Xu, H. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.172909 · Cited by 46
Dabravolski, S. A., Nikiforov, N. G., Starodubova, A. V., Попкова, Т. В., & Orekhov, A. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168770 · Cited by 46
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Chekulaeva, M., & Rajewsky, N. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032680 · Cited by 46
Mitochondrial retrograde signaling in the nervous system
Hunt, R. J., & Bateman, J. M. (2017) · FEBS Letters · doi:10.1002/1873-3468.12890 · Cited by 45
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Friesen, M., Warren, C. R., Yu, H., Toyohara, T., Ding, Q., Florido, M. H. C., Sayre, C., Pope, B. D., Goff, L. A., Rinn, J. L., et al. (2020) · Stem Cell Reports · doi:10.1016/j.stemcr.2020.03.002 · Cited by 45
Goetzl, E. J., Srihari, V. H., Gülöksüz, S., Ferrara, M., Tek, C., & Heninger, G. R. (2021) · The FASEB Journal · doi:10.1096/fj.202002519r · Cited by 45
Paharkova, V., Alvarez, G., Nakamura, H. K., Cohen, P., & Lee, K. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.06.015 · Cited by 45
Self-citationTero-Vescan, A., Degens, H., Matsakas, A., Ștefănescu, R., Ősz, B. E., & Slevin, M. (2025) · Pharmaceuticals · doi:10.3390/ph18081222 · Cited by 44
“…regulators of mitochondrial function and stress resistance [116], whilst recent studies have demonstrated that MOTS-c may also exert protective effects against diet-induced obesity and insulin resistance by altering skeletal muscle gene expression related to metabolism and inflammation [117].”
He, J., Jin, Y., He, C., Li, Z., Yu, W., Zhou, J., Luo, R., Chen, Q., Wu, Y., Wang, S., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1338804 · Cited by 44
Zhao, X., Zhang, J., Li, C., Kuang, W., Deng, J., Tan, X., Li, C., & Li, S. (2024) · Mitochondrion · doi:10.1016/j.mito.2024.101975 · Cited by 47
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Li, Q., Lu, H., Hu, G., Ye, Z., Zhai, D., Zhao, Y., Wang, L., An, X., & Lu, Z. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.03.194 · Cited by 43
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Metadata
- Authors
- 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., & Cohen, P.
- Affiliations
- University of Southern California (US)
- University of California, Los Angeles (US)
- Corresponding author
- Lee, Changhan
- Cohen, Pinchas
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-03
- Volume
- 21
- Issue
- 3
- Pages
- 443-454
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4350682
- OpenAlex
- W2160343816
- Cited by
- 715
- References
- 62
- Citations by year
- 2026: 61 · 2025: 77 · 2024: 104 · 2023: 97 · 2022: 59 · 2021: 67 · 2020: 68 · 2019: 55 · 2018: 45 · 2017: 27 · 2016: 40 · 2015: 15
- FWCI
- 18.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (UL1TR000130, 7r01ag034430-05)
- National Institute on Aging (1R01AG 034430, # R01AG034430)
- National Institute of General Medical Sciences (R01GM090311)
- National Institute of Diabetes and Digestive and Kidney Diseases (NIH DK063491, P30DK063491)
- National Institute of Environmental Health Sciences (R01ES020812)
- National Center for Advancing Translational Sciences
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- MOTS-c, mitochondrial peptides, 12S rRNA, small open reading frames, mitochondrial DNA, metabolic homeostasis, insulin resistance, obesity, AMPK activation, folate cycle, de novo purine synthesis, skeletal muscle, mitochondrial signaling
- MeSH terms
- Animals, Cell Line, DNA, Mitochondrial, HeLa Cells, Homeostasis, Humans, Insulin, Insulin Resistance, Male, Mice, Inbred C57BL, Mice, Inbred ICR, Mitochondria, Obesity, Peptides, Signal Transduction, Muscle, Skeletal, Cell Line, Tumor, Mice, AMP-Activated Protein Kinases, HEK293 Cells, Diet, High-Fat
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