SIRT1 signaling as potential modulator of skeletal muscle diseases
Abstract
Skeletal muscle diseases heavily impair the strength and the movement of patients. Muscles loose their adaptive capacity, undergoing atrophy or wasting, due to a number of pathological insults. Metabolic changes, such as those occurring during aging, contribute to the progressive reduction of myofiber size and decline of skeletal muscle performance that is typically observed in the elderly. The nicotinamide adenine dinucleotide (NAD)-dependent deacetylase SIRT1 has been involved in the protection against metabolic disorders, against cancers and in the enhancement of life span. Here we discuss the current evidence placing SIRT1 at the crossroad between energy homeostasis, fiber strength, and regeneration from damage in the skeletal muscle. Furthermore, we underline how cell type specific targeting of SIRT1 could be beneficial in the treatment of skeletal muscle diseases.
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Activation of SIRT1 may help improve skeletal muscle disease.
“activation of SIRT1 may help improve skeletal muscle disease.”
From GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway (2023) · cites this paper as [59]
Cites
Missing Pieces in the NF-κB Puzzle
Ghosh, S., & Karin, M. (2002) · Cell · doi:10.1016/s0092-8674(02)00703-1 · Cited by 3,638 · see citing works
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022 · see citing works
Modulation of NF‐κB‐dependent transcription and cell survival by the SIRT1 deacetylase
Yeung, F., Hoberg, J. E., Ramsey, C. S., Keller, M. D., Jones, D. R., Frye, R. A., & Mayo, M. W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600244 · Cited by 2,750 · see citing works
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
Emery, A. E. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07815-7 · Cited by 1,667 · see citing works
Metabolic control of muscle mitochondrial function and fatty acid oxidation through SIRT1/PGC‐1α
Gerhart‐Hines, Z., Rodgers, J. T., Bare, O., Lerin, C., Kim, S., Mostoslavsky, R., Alt, F. W., Wu, Z., & Puigserver, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601633 · Cited by 1,294 · see citing works
Sandri, M., Lin, J., Handschin, C., Yang, W., Arany, Z. P., Lecker, S. H., Goldberg, A. L., & Spiegelman, B. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607795103 · Cited by 974 · see citing works
Cantó, C., Jiang, L. Q., Deshmukh, A. S., Mataki, C., Coste, A., Lagouge, M., Zierath, J. R., & Auwerx, J. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.02.006 · Cited by 921 · see citing works
Aberrant repair and fibrosis development in skeletal muscle
Mann, C. J., Perdiguero, E., Kharraz, Y., Aguilar, S., Pessina, P., Serrano, A. L., & Muñoz-Cánoves, P. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-21 · Cited by 853 · cited 1× · see citing works
“Moreover, the final outcome of most SMDs is the fibroadipogenic degeneration, which can be also observed in aged muscles [2].”
BackgroundFulco, M., Cen, Y., Zhao, P., Hoffman, E. P., McBurney, M. W., Sauve, A. A., & Sartorelli, V. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.02.004 · Cited by 821 · see citing works
Sir2 Regulates Skeletal Muscle Differentiation as a Potential Sensor of the Redox State
Fulco, M., Schiltz, R. L., Iezzi, S., King, M. T., Zhao, P., Kashiwaya, Y., Hoffman, E. P., Veech, R. L., & Sartorelli, V. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00226-0 · Cited by 590 · see citing works
Villalta, S. A., Nguyen, H. X., Deng, B., Gotoh, T., & Tidball, J. G. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn376 · Cited by 512 · see citing works
Guarente, L. (2011) · New England Journal of Medicine · doi:10.1056/nejmra1100831 · Cited by 510 · see citing works
Regulation of Hypoxia-Inducible Factor 2α Signaling by the Stress-Responsive Deacetylase Sirtuin 1
Dioum, E. M., Chen, R., Alexander, M. S., Zhang, Q., Hogg, R. T., Gerard, R. D., & Garcia, J. A. (2009) · Science · doi:10.1126/science.1169956 · Cited by 470 · see citing works
Acharyya, S., Villalta, S. A., Bakkar, N., Bupha‐Intr, T., Janssen, P. M. L., Carathers, M., Li, Z.-W., Beg, A. A., Ghosh, S., Sahenk, Z., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30556 · Cited by 436 · see citing works
SIRT1 inhibits inflammatory pathways in macrophages and modulates insulin sensitivity
Yoshizaki, T., Schenk, S., Imamura, T., Babendure, J. L., Sonoda, N., Bae, E. J., Oh, D. Y., Lu, M. M., Milne, J. C., Westphal, C. H., et al. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00417.2009 · Cited by 420 · see citing works
Yang, Z., Kahn, B. B., Shi, H., & Xue, B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.123620 · Cited by 413 · see citing works
Sundaresan, N. R., Pillai, V. B., Wolfgeher, D., Samant, S. A., Vasudevan, P., Parekh, V., Raghuraman, H., Cunningham, J. M., Gupta, M., & Gupta, M. P. (2011) · Science Signaling · doi:10.1126/scisignal.2001465 · Cited by 345 · see citing works
The emerging biology of satellite cells and their therapeutic potential
Kuang, S., & Rudnicki, M. A. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.004 · Cited by 339 · see citing works
Myeloid Deletion of SIRT1 Induces Inflammatory Signaling in Response to Environmental Stress
Schug, T. T., Xu, Q., Gao, H., Peres-da-Silva, A., Draper, D. W., Fessler, M. B., Purushotham, A., & Li, X. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00657-10 · Cited by 324 · see citing works
Mourkioti, F., Kratsios, P., Luedde, T., Song, Y.-H., Delafontaine, P., Adami, R., Parente, V., Bottinelli, R., Pasparakis, M., & Rosenthal, N. A. (2006) · Journal of Clinical Investigation · doi:10.1172/jci28721 · Cited by 315 · see citing works
TNF-α regulates myogenesis and muscle regeneration by activating p38 MAPK
Chen, S., Jin, B., & Li, Y.-P. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00486.2006 · Cited by 301 · see citing works
SirT1 Regulates Adipose Tissue Inflammation
Gillum, M. P., Kotas, M. E., Erion, D. M., Kursawe, R., Chatterjee, P., Nead, K. T., Muise, E. S., Hsiao, J. J., Frederick, D. W., Yonemitsu, S., et al. (2011) · Diabetes · doi:10.2337/db11-0616 · Cited by 294 · see citing works
Macrophage skewing by Phd2 haplodeficiency prevents ischaemia by inducing arteriogenesis
Takeda, Y., Costa, S., Delamarre, E., Roncal, C., de Oliveira, R. L., Squadrito, M. L., Finisguerra, V., Deschoemaeker, S., Bruyére, F., Wenes, M., et al. (2011) · Nature · doi:10.1038/nature10507 · Cited by 287 · see citing works
The Sirtuin family: therapeutic targets to treat diseases of aging
Milne, J. C., & Denu, J. M. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.01.019 · Cited by 271 · see citing works
Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
Hunter, R. B., & Kandarian, S. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21696 · Cited by 249 · see citing works
Amat, R., Planavila, A., Chen, S. L., Iglesias, R., Giralt, M., & Villarroya, F. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022749 · Cited by 218 · see citing works
Self-citationPhilp, A., Chen, A., Lan, D., Meyer, G. A., Murphy, A. N., Knapp, A. E., Olfert, I. M., McCurdy, C. E., Marcotte, G. R., Hogan, M. C., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.261685 · Cited by 184 · see citing works
Kryger, A. I., & Andersen, J. L. (2007) · Scandinavian Journal of Medicine & Science in Sports · doi:10.1111/j.1600-0838.2006.00575.x · Cited by 175 · see citing works
Hori, Y. S., Kuno, A., Hosoda, R., Tanno, M., Miura, T., Shimamoto, K., & Horio, Y. (2011) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.111.183210 · Cited by 165 · see citing works
Villalta, S. A., Deng, B., Rinaldi, C., Wehling-Henricks, M., & Tidball, J. G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101267 · Cited by 158 · see citing works
Regulation of muscle atrophy in aging and disease
Vinciguerra, M., Musaro, A., & Rosenthal, N. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_15 · Cited by 149 · see citing works
Self-citationPGC-1α regulates a HIF2α-dependent switch in skeletal muscle fiber types
Rasbach, K. A., Gupta, R. K., Ruas, J. L., Wu, J., Naseri, E., Estall, J. L., & Spiegelman, B. M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016089107 · Cited by 142 · see citing works
NF-κB Signaling in the Aging Process
Salminen, A., & Kaarniranta, K. (2009) · Journal of Clinical Immunology · doi:10.1007/s10875-009-9296-6 · Cited by 123 · see citing works
mIGF‐1/JNK1/SirT1 signaling confers protection against oxidative stress in the heart
Vinciguerra, M., Santini, M. P., Martínez, C., Pazienza, V., Claycomb, W. C., Giuliani, A., & Rosenthal, N. A. (2011) · Aging Cell · doi:10.1111/j.1474-9726.2011.00766.x · Cited by 122 · see citing works
Self-citationNF-κB Signaling in Skeletal Muscle Health and Disease
Peterson, J. M., Bakkar, N., & D, D. C. G. (2011) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-385940-2.00004-8 · Cited by 118 · see citing works
Sirt1 increases skeletal muscle precursor cell proliferation
Rathbone, C. R., Booth, F. W., & Lees, S. J. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.08.003 · Cited by 117 · see citing works
Vinciguerra, M., Santini, M. P., Claycomb, W. C., Ladurner, A. G., & Rosenthal, N. A. (2009) · Aging · doi:10.18632/aging.100107 · Cited by 110 · see citing works
Self-citationThe physiological roles of Sirt1 in skeletal muscle
Pardo, P. S., & Boriek, A. M. (2011) · Aging · doi:10.18632/aging.100312 · Cited by 99 · see citing works
Li, P., Zhao, Y., Wu, X., Xia, M., Fang, M., Iwasaki, Y., Sha, J., Chen, Q., Xu, Y., & Shen, A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr984 · Cited by 91 · see citing works
Machida, S., & Booth, F. W. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.08.009 · Cited by 87 · see citing works
Zorzano, A., Hernández‐Álvarez, M. I., Palacı́n, M., & Mingrone, G. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.02.017 · Cited by 66 · see citing works
SirT1 in muscle physiology and disease: lessons from mouse models
Vinciguerra, M., Fulco, M., Ladurner, A. G., Sartorelli, V., & Rosenthal, N. A. (2010) · Disease Models & Mechanisms · doi:10.1242/dmm.004655 · Cited by 66 · see citing works
Self-citationRyan, M. J., Dudash, H. J., Docherty, M., Geronilla, K. B., Baker, B. A., Haff, G. G., Cutlip, R. G., & Alway, S. E. (2008) · The Journals of Gerontology Series A · doi:10.1093/gerona/63.10.1015 · Cited by 60 · see citing works
Acute exercise reverses aged-induced impairments in insulin signaling in rodent skeletal muscle
Pauli, J. R., Ropelle, E. R., Cintra, D. E., de Souza, C. T., da Silva, A. S. R., Moraes, J. C., Prada, P. O., Leme, J. A. C. D. A., Luciano, E., Velloso, L. A., et al. (2010) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2010.03.004 · Cited by 60 · see citing works
Tang, Y. M., Reay, D. P., Salay, M., Mi, M. Y., Clemens, P. R., D, D. C. G., Robbins, P. D., Huard, J., & Wang, B. (2010) · Gene Therapy · doi:10.1038/gt.2010.110 · Cited by 53 · see citing works
Bhatnagar, S., Kumar, A., Makonchuk, D. Y., Li, H., & Kumar, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.064063 · Cited by 41 · see citing works
Genetic Defects in Muscular Dystrophy
Chandrasekharan, K., & Martin, P. T. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)79017-0 · Cited by 23 · see citing works
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Wang, Y., & Pessin, J. E. (2013) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/mco.0b013e328360272d · Cited by 416 · see citing works
Stenvinkel, P., Carrero, J. J., von Walden, F., Ikizler, T. A., & Nader, G. A. (2015) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfv122 · Cited by 186 · see citing works
Angulo, J., Assar, M. E., & Rodríguez‐Mañas, L. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.06.001 · Cited by 185 · see citing works
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Kim, H.-D., Hesterman, J., Call, T., Magazu, S., Keeley, E., Armenta, K., Kronman, H., Neve, R. L., Nestler, E. J., & Ferguson, D. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0212-16.2016 · Cited by 158 · see citing works
Santa, F. D., Vitiello, L., Torcinaro, A., & Ferraro, E. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7420 · Cited by 154 · see citing works
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Liu, N., Garry, G. A., Li, S., Bezprozvannaya, S., Sanchez‐Ortiz, E., Chen, B., Shelton, J. M., Jaichander, P., Bassel‐Duby, R., & Olson, E. N. (2017) · Nature Cell Biology · doi:10.1038/ncb3477 · Cited by 144 · see citing works
Role and possible mechanisms of Sirt1 in depression
Lu, G., Li, J., Zhang, H., Zhao, X., Yan, L.-J., & Yang, X. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8596903 · Cited by 106 · see citing works
Guo, A., Li, K., Tian, H., Fan, Z., Chen, Q., Yang, Y., Yu, J., Wu, Y., & Xiao, Q. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16448 · Cited by 112 · see citing works
GLP-1RA Liraglutide and Semaglutide Improves Obesity-Induced Muscle Atrophy via SIRT1 Pathway
Xiang, J., Qin, L., Zhong, J., Xia, N., & Liang, Y. (2023) · Diabetes, Metabolic Syndrome and Obesity · doi:10.2147/dmso.s425642 · Cited by 100 · see citing works
Chen, W.-K., Tsai, Y., Shibu, M. A., Shen, C.-Y., Chang-Lee, S. N., Chen, R., Yao, C., Ban, B., Kuo, W., & Huang, C. (2018) · Aging · doi:10.18632/aging.101714 · Cited by 86 · see citing works
Mohamed, J. S., Wilson, J. C., Myers, M. J., Sisson, K. J., & Alway, S. E. (2014) · Aging · doi:10.18632/aging.100696 · Cited by 81 · see citing works
Bosutti, A., & Degens, H. (2015) · Scientific Reports · doi:10.1038/srep08093 · Cited by 81 · see citing works
An extensive review regarding the adipokines in the pathogenesis and progression of osteoarthritis.
Tu, C., He, J.-Y., Wu, B., Wang, W.-C., & Li, Z.-H. (2019) · Cytokine · doi:10.1016/j.cyto.2018.06.019 · Cited by 71 · see citing works
Effects of Ginsenoside Rg3 on fatigue resistance and SIRT1 in aged rats.
Yang, Q.-Y., Lai, X., Ouyang, J., & Yang, J.-D. (2018) · Toxicology · doi:10.1016/j.tox.2018.08.010 · Cited by 68 · see citing works
Shiota, A., Shimabukuro, M., Fukuda, D., Soeki, T., Sato, H., Uematsu, E., Hirata, Y., Kurobe, H., Maeda, N., Sakaue, H., et al. (2012) · Cardiovascular Diabetology · doi:10.1186/1475-2840-11-139 · Cited by 64 · see citing works
Szekeres, Z., Nagy, A., Jahner, K., & Szabados, E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158214 · Cited by 66 · see citing works
COPD elicits remodeling of the diaphragm and vastus lateralis muscles in humans
Levine, S., Bashir, M. H., Clanton, T. L., Powers, S. K., & Singhal, S. K. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01121.2012 · Cited by 61 · see citing works
Control of MicroRNA Expression as a New Way for Resveratrol To Deliver Its Beneficial Effects
Lançon, A., Kaminski, J., Tili, E., Michaille, J., & Latruffe, N. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301479v · Cited by 58 · see citing works
Abu Bakar, M. H., Shariff, K. A., Tan, J. S., & Lee, L. K. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173371 · Cited by 51 · see citing works
Assar, M. E., Rodríguez-Sánchez, I., Álvarez‐Bustos, A., & Rodríguez‐Mañas, L. (2024) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2024.101271 · Cited by 50 · see citing works
Agerholm, M., Dall, M., Jensen, B. A. H., Prats, C., Madsen, S., Basse, A. L., Graae, A.-S., Risis, S., Goldenbaum, J., Quistorff, B., et al. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00213.2017 · Cited by 43 · see citing works
Xu, C., Bai, B., Fan, P., Cai, Y., Huang, B., Law, I. K. M., Liu, L., Xu, A., Tung, C., Li, X., et al. (2013) · Europe PMC (PubMed Central) · Cited by 42 · see citing works
Regulation of stem cell aging by SIRT1 – Linking metabolic signaling to epigenetic modifications
An, Y., & Dang, W. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.03.031 · Cited by 32 · see citing works
Trolese, M. C., Scarpa, C., Melfi, V., Fabbrizio, P., Sironi, F. M., Rossi, M., Bendotti, C., & Nardo, G. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.04.018 · Cited by 29 · see citing works
SIRT1: A Novel Target for the Treatment of Muscular Dystrophies
Kuno, A., & Horio, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/6714686 · Cited by 29 · see citing works
Shibu, M. A., Wang, T., Wang, M.-F., & Lin, W. (2020) · Aging · doi:10.18632/aging.103081 · Cited by 28 · see citing works
Cardioprotective mIGF-1/SIRT1 signaling induces hypertension, leukocytosis and fear response in mice
Bolasco, G., Calogero, R., Carrara, M., Banchaabouchi, M. A., Bilbao, D., Mazzoccoli, G., & Vinciguerra, M. (2012) · Aging · doi:10.18632/aging.100464 · Cited by 26 · see citing works
Self-citationKim, H., Wei, J., Call, T., Ma, X., Quintus, N. T., Summers, A. J., Carotenuto, S., Johnson, R., Nguyen, A., Cui, Y., et al. (2024) · Biological Psychiatry · doi:10.1016/j.biopsych.2024.03.017 · Cited by 21 · see citing works
Imbriano, C., Moresi, V., Belluti, S., Renzini, A., Cavioli, G., Maretti, E., & Molinari, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015161 · Cited by 20 · see citing works
Ramsay, T. G., Stoll, M. J., Shannon, A. E., & Blomberg, L. A. (2018) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-018-0251-3 · Cited by 18 · see citing works
You, B., Dun, Y., Fu, S., Qi, D., Zhang, W., Liu, Y., Qiu, L., Xie, M., & Liu, S. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.646489 · Cited by 17 · see citing works
Fröhlich, J., Raffaele, M., Skálová, H., Leire, E., Pata, I., Pata, P., Gorbunova, V. A., & Vinciguerra, M. (2022) · GeroScience · doi:10.1007/s11357-022-00713-1 · Cited by 16 · see citing works
Self-citationJuzentaihoto Suppresses Muscle Atrophy and Decreased Motor Function in SAMP8 Mice
Morita, Y., Ishida, T., Morisawa, S., Jobu, K., Ou, Y., Fujita, H. M., Hanazaki, K., & Miyamura, M. (2020) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b20-00555 · Cited by 15 · see citing works
Epigenetics of Skeletal Muscle Atrophy
Du, J., Wu, Q., & Bae, E. J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158362 · Cited by 15 · see citing works
The TRPA1 channel is a cardiac target of mIGF-1/SIRT1 signaling
Pazienza, V., Pomara, C., Cappello, F., Calogero, R., Carrara, M., Mazzoccoli, G., & Vinciguerra, M. (2014) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00150.2014 · Cited by 15 · see citing works
Self-citationSIRT1 Synchs Satellite Cell Metabolism with Stem Cell Fate
Díaz‐Ruiz, A., González‐Freire, M., Ferrucci, L., Bernier, M., & de Cabo, R. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.01.006 · Cited by 14 · see citing works
Chen, Q., Huang, W., Çapanoğlu, E., Amrouche, A. T., & Lu, B. (2023) · Food Frontiers · doi:10.1002/fft2.261 · Cited by 12 · see citing works
AUF1 gene transfer increases exercise performance and improves skeletal muscle deficit in adult mice
Abbadi, D., Andrews, J. J., Katsara, O., & Schneider, R. J. (2021) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2021.07.005 · Cited by 11 · see citing works
Xia, H., Zhang, B., Yang, D., Zhu, C., Zhang, J., Chen, H., Ma, H., Hu, S., Xu, C., Shi, C., et al. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.624303 · Cited by 9 · see citing works
Smimmo, M., Casale, V., D'Andrea, D., Bello, I., Iaccarino, N., Romano, F., Brancaleone, V., Panza, E., Bianca, R. D. D. V., Katsouda, A., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103645 · Cited by 8 · see citing works
Wu, Z., Li, W., Yang, Y., Zheng, Y., Zhou, M., Li, Y., Li, H. Z., Wu, H., & Du, L. (2023) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202300033 · Cited by 8 · see citing works
Zhang, W., Fu, C., Dong, Y., Yuan, Y., Zhang, W., Gu, D., Wu, Y., Zhang, D., Wang, L., & Cheng, X. (2024) · Quantitative Imaging in Medicine and Surgery · doi:10.21037/qims-24-127 · Cited by 6 · see citing works
NeuroHeal Improves Muscle Regeneration after Injury
Marmolejo-Martínez-Artesero, S., Romeo-Guitart, D., Venegas, V., Marotta, M., & Casas, C. (2020) · Cells · doi:10.3390/cells10010022 · Cited by 5 · see citing works
Kujawowicz, K., Mirończuk-Chodakowska, I., Cyuńczyk, M., & Witkowska, A. M. (2025) · Nutrients · doi:10.3390/nu17040726 · Cited by 5 · see citing works
Tanaka, K., Kawakami, S., Mori, S., Yamaguchi, T., Saito, E., Setoguchi, Y., Matsui, Y., Nishimura, E., Ebihara, S., & Kawama, T. (2024) · Life · doi:10.3390/life14050589 · Cited by 8 · see citing works
Fröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Clinical Epigenetics · doi:10.1186/s13148-024-01710-1 · Cited by 6 · see citing works
Self-citationMolecular Regulation and Rejuvenation of Muscle Stem (Satellite) Cell Aging
Meiliana, A., Dewi, N. M., & Wijaya, A. (2015) · The Indonesian Biomedical Journal · doi:10.18585/inabj.v7i2.73 · Cited by 4 · see citing works
Yoon, S., Beermann, M. L., Yu, B., Shao, D., Bachschmid, M. M., & Miller, J. B. (2017) · Journal of Neuromuscular Diseases · doi:10.3233/jnd-170262 · Cited by 4 · see citing works
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Ou, Y., Jobu, K., Ishida, T., Morisawa, S., Fujita, H. M., Kawada, K., Yoshioka, S., & Miyamura, M. (2022) · Journal of Natural Medicines · doi:10.1007/s11418-021-01590-2 · Cited by 4 · see citing works
Shykholeslami, Z., Abdi, A., Barari, A., & Hosseini, S. A. (2019) · Jorjani Biomedicine Journal · doi:10.29252/jorjanibiomedj.7.4.57 · Cited by 3 · see citing works
Sánchez-Nuño, S., Santocildes, G., Rebull, J., Bardallo, R. G., Farrés, M. G., Viscor, G., Carbonell, T., & Torrella, J. R. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.09.032 · Cited by 2 · see citing works
Falvino, A., Bonanni, R., Gasperini, B., Cariati, I., Chiavoghilefu, A., Smakaj, A., Visconti, V. V., Botta, A., Iundusi, R., Gasbarra, E., et al. (2025) · Biomedicines · doi:10.3390/biomedicines13061350 · Cited by 2 · see citing works
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(2015) · Clinical and Experimental Pharmacology · doi:10.4172/2161-1459.1000177 · Cited by 1 · see citing works
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Bennett, B. T. (2013) · doi:10.33915/etd.4952
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Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752201
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kučera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752195
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kučera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752216
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752222
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752213
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kučera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752210
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752198
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752204
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752225
Self-citationFröhlich, J., Liorni, N., Mangoni, M., Lochmanová, G., Pírek, P., Kaštánková, N., Pata, P., Kucera, J., Chaldakov, G. N., Tonchev, A. B., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26752219
Self-citation
- Authors
- Tonkin, J., Villarroya, F., Puri, P. L., & Vinciguerra, M.
- Affiliations
- European Molecular Biology Laboratory (IT)
- Centro de Investigación Biomédica en Red (ES)
- Foundation for Liver Research (GB)
- Corresponding author
- Vinciguerra, Manlio
- Venue
- Current Opinion in Pharmacology
- Publisher
- Elsevier BV
- Published
- 2012-06
- Volume
- 12
- Issue
- 3
- Pages
- 372-376
- ISSN
- 1471-4892 (ISSN-L)
- OpenAlex
- W1991156731
- Cited by
- 60
- References
- 48
- Citations by year
- 2025: 3 · 2024: 13 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 4 · 2019: 1 · 2018: 6 · 2017: 4 · 2016: 3 · 2015: 5 · 2014: 2 · 2013: 3 · 2012: 5
- FWCI
- 0.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Nottingham Trent University's Institutional Repository (Nottingham Trent Repository) (submittedVersion)
- Funders
- Foundation for Liver Research (London, UK)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Keywords
- SIRT1, skeletal muscle disorders, muscle atrophy, NAD+-dependent deacetylase, energy homeostasis, muscle regeneration, aging, sarcopenia, cell type-specific targeting
- MeSH terms
- Aging, Animals, Humans, Macrophages, Muscular Diseases, Regeneration, Signal Transduction, Disease Progression, Muscle, Skeletal, Satellite Cells, Skeletal Muscle, Cell Proliferation, Sirtuin 1
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