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Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3
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Nutrient availability is the major regulator of life and reproduction, and a complex cellular signaling network has evolved to adapt organisms to fasting. These sensor pathways monitor cellular energy metabolism, especially mitochondrial ATP production and NAD + /NADH ratio, as major signals for nutritional state. We hypothesized that these signals would be modified by mitochondrial respiratory chain disease, because of inefficient NADH utilization and ATP production. Oral administration of nicotinamide riboside (NR), a vitamin B3 and NAD + precursor, was previously shown to boost NAD + levels in mice and to induce mitochondrial biogenesis. Here, we treated mitochondrial myopathy mice with NR. This vitamin effectively delayed early‐ and late‐stage disease progression, by robustly inducing mitochondrial biogenesis in skeletal muscle and brown adipose tissue, preventing mitochondrial ultrastructure abnormalities and mtDNA deletion formation. NR further stimulated mitochondrial unfolded protein response, suggesting its protective role in mitochondrial disease. These results indicate that NR and strategies boosting NAD + levels are a promising treatment strategy for mitochondrial myopathy.
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“new therapeutic strategies have emerged to restore NAD+ levels in muscle by administration of dietary NAD+ precursors such as NR or NMN46,53,54”
From Mitochondrial oxidative capacity and NAD+ biosynthesis are reduced in human sarcopenia across ethnicities (2019) · cites this paper as [54]
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“the conversion of these precursors to NAD+ bypasses the rate limited enzyme NAMPT”
From Mitochondrial oxidative capacity and NAD+ biosynthesis are reduced in human sarcopenia across ethnicities (2019) · cites this paper as [54]
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1 retracted
Wenz, T., Diaz, F., Spiegelman, B. M., & Moraes, C. T. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.006 · Cited by 297
RetractedTranscriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Self-citationAMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
Cantó, C., Gerhart-Hines, Z., Feige, J. N., Lagouge, M., Noriega, L., Milne, J. C., Elliott, P. J., Puigserver, P., & Auwerx, J. (2009) · Nature · doi:10.1038/nature07813 · Cited by 3,300
Self-citationStress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
Brunet, A., Sweeney, L. B., Sturgill, J. F., Chua, K. F., Greer, P. L., Lin, Y., Tran, H., Ross, S. E., Mostoslavsky, R., Cohen, H. Y., et al. (2004) · Science · doi:10.1126/science.1094637 · Cited by 3,239
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
Rodgers, J. T., Lerin, C., Haas, W., Gygi, S. P., Spiegelman, B. M., & Puigserver, P. (2005) · Nature · doi:10.1038/nature03354 · Cited by 3,160
FGF-21 as a novel metabolic regulator
Kharitonenkov, A., Shiyanova, T. L., Koester, A., Ford, A. M., Micanovic, R., Galbreath, E. J., Sandusky, G. E., Hammond, L. J., Moyers, J. S., Owens, R. A., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23606 · Cited by 2,125
Gomes, A. P., Price, N. L., Ling, A. J. Y., Moslehi, J. J., Montgomery, M. K., Rajman, L., White, J. P., Teodoro, J. S., Wrann, C. D., Hubbard, B. P., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.037 · Cited by 1,482
Cantó, C., Houtkooper, R. H., Pirinen, E., Youn, D. Y., Oosterveer, M. H., Cen, Y., Fernandez-Marcos, P. J., Yamamoto, H., Andreux, P. A., Cettour-Rose, P., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.022 · Cited by 1,238
Self-citationMouchiroud, L., Houtkooper, R. H., Moullan, N., Katsyuba, E., Ryu, D., Cantó, C., Mottis, A., Jo, Y.-S., Viswanathan, M., Schoonjans, K., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.016 · Cited by 1,210
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Pickles, S., Vigié, P., & Youle, R. J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.004 · Cited by 2,081
Sarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797
Cantó, C., Menzies, K. J., & Auwerx, J. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.05.023 · Cited by 1,648
Self-citationGorman, G. S., Chinnery, P. F., DiMauro, S., Hirano, M., Koga, Y., McFarland, R., Suomalainen, A., Thorburn, D. R., Zeviani, M., & Turnbull, D. M. (2016) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2016.80 · Cited by 1,650
Self-citationNAD + in aging, metabolism, and neurodegeneration
Verdin, E. (2015) · Science · doi:10.1126/science.aac4854 · Cited by 1,319
NAD+ Intermediates: The Biology and Therapeutic Potential of NMN and NR
Yoshino, J., Baur, J. A., & Imai, S.-I. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.11.002 · Cited by 1,061
Mills, K. F., Yoshida, S., Stein, L. R., Grozio, A., Kubota, S., Sasaki, Y., Redpath, P., Migaud, M. E., Apte, R. S., Uchida, K., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.09.013 · Cited by 930
Metabolic control of autophagy
Galluzzi, L., Pietrocola, F., Levine, B., & Kroemer, G. (2014) · Cell · doi:10.1016/j.cell.2014.11.006 · Cited by 855
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Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834
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Quirós, P. M., Mottis, A., & Auwerx, J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.23 · Cited by 787
Self-citationThe mitochondrial UPR: mechanisms, physiological functions and implications in ageing
Shpilka, T., & Haynes, C. M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.110 · Cited by 742
NAD+ homeostasis in health and disease
Katsyuba, E., Romani, M., Hofer, D., & Auwerx, J. (2020) · Nature Metabolism · doi:10.1038/s42255-019-0161-5 · Cited by 627
Self-citationMitochondrial diseases: the contribution of organelle stress responses to pathology
Suomalainen, A., & Battersby, B. J. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.66 · Cited by 505
Self-citationNAD + metabolism: Bioenergetics, signaling and manipulation for therapy
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Leigh syndrome: One disorder, more than 75 monogenic causes
Lake, N. J., Compton, A. G., Rahman, S., & Thorburn, D. R. (2015) · Annals of Neurology · doi:10.1002/ana.24551 · Cited by 499
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Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 517
Mitochondrial Diseases: Hope for the Future
Russell, O. M., Gorman, G. S., Lightowlers, R. N., & Turnbull, D. M. (2020) · Cell · doi:10.1016/j.cell.2020.02.051 · Cited by 480
mTORC1 Regulates Mitochondrial Integrated Stress Response and Mitochondrial Myopathy Progression
Khan, N. A., Nikkanen, J., Yatsuga, S., Jackson, C. B., Wang, L., Pradhan, S., Kivelä, R., Pessia, A., Velagapudi, V., & Suomalainen, A. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.07.007 · Cited by 394
Self-citationGariani, K., Menzies, K. J., Ryu, D., Wegner, C. J., Wang, X., Ropelle, E. R., Moullan, N., Zhang, H., Perino, A., Lemos, V., et al. (2016) · Hepatology · doi:10.1002/hep.28245 · Cited by 368
Self-citationLoss of NAD Homeostasis Leads to Progressive and Reversible Degeneration of Skeletal Muscle
Frederick, D. W., Loro, E., Liu, L., Davila, A., Chellappa, K., Silverman, I. M., Quinn, W. J., Gosai, S. J., Tichy, E. D., Davis, J. G., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.005 · Cited by 367
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Diguet, N., Trammell, S. A. J., Tannous, C., Deloux, R., Piquereau, J., Mougenot, N., Gouge, A., Gressette, M., Manoury, B., Blanc, J., et al. (2018) · Circulation · doi:10.1161/circulationaha.116.026099 · Cited by 358
Migliavacca, E., Tay, S. K. H., Patel, H. P., Sonntag, T., Civiletto, G., McFarlane, C., Forrester, T., Barton, S. J., Leow, M. K., Antoun, E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13694-1 · Cited by 365
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Mitchell, S. J., Bernier, M., Aon, M. A., Cortassa, S., Kim, E. Y., Fang, E. F., Palacios, H. H., Ali, A., Navas-Enamorado, I., Di Francesco, A., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.001 · Cited by 338
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 353
Repairing mitochondrial dysfunction in disease
Sorrentino, V., Menzies, K. J., & Auwerx, J. (2018) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-104908 · Cited by 337
Protein acetylation in metabolism – metabolites and cofactors
Menzies, K. J., Zhang, H., Katsyuba, E., & Auwerx, J. (2016) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.181 · Cited by 331
Self-citationThe pharmacological regulation of cellular mitophagy
Georgakopoulos, N., Wells, G., & Campanella, M. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2287 · Cited by 330
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Self-citationMitochondrial medicine in the omics era
Rahman, J., & Rahman, S. (2018) · The Lancet · doi:10.1016/s0140-6736(18)30727-x · Cited by 295
Castro-Portuguez, R., & Sutphin, G. L. (2020) · Experimental Gerontology · doi:10.1016/j.exger.2020.110841 · Cited by 296
Pirinen, E., Auranen, M., Khan, N. A., Brilhante, V., Urho, N., Pessia, A., Hakkarainen, A., Kuula, J., Heinonen, U., Schmidt, M. S., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.04.008 · Cited by 286
Self-citationLethal Cardiomyopathy in Mice Lacking Transferrin Receptor in the Heart
Xu, W., Barrientos, T., Mao, L., Rockman, H. A., Sauve, A. A., & Andrews, N. C. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.023 · Cited by 280
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Self-citationVannini, N., Campos, V., Girotra, M., Trachsel, V., Rojas-Sutterlin, S., Tratwal, J., Ragusa, S., Stefanidis, E., Ryu, D., Rainer, P. Y., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2019.02.012 · Cited by 218
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Berthiaume, J. M., Kurdys, J., Muntean, D. M., & Rosca, M. G. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7415 · Cited by 169
Remie, C. M., Roumans, K. H., Moonen, M. P., Connell, N. J., Havekes, B., Mevenkamp, J., Lindeboom, L., de Wit, V. H., van de Weijer, T., Aarts, S. A., et al. (2020) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/nqaa072 · Cited by 160
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Zeng, X., Yang, J., Hu, O., Huang, J., Li, R., Chen, M., Zhang, Y., Zhou, X., Zhu, J., Zhang, Q., et al. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7172 · Cited by 163
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Hood, D. A., Tryon, L. D., Carter, H. N., Kim, Y., & Chen, C. C. W. (2016) · Biochemical Journal · doi:10.1042/bcj20160009 · Cited by 159
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Morris, G., Walder, K., McGee, S. L., Dean, O. M., Tye, S. J., Maes, M., & Berk, M. (2017) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2017.01.014 · Cited by 162
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Mori, V., Amici, A., Mazzola, F., Stefano, M. D., Conforti, L., Magni, G., Ruggieri, S., Raffaelli, N., & Orsomando, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113939 · Cited by 158
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Liu, S., Fu, S., Wang, G., Cao, Y., Li, L., Li, X., Yang, J. J., Li, N., Shan, Y., Cao, Y., et al. (2021) · Cell Metabolism · doi:10.1016/j.cmet.2021.06.013 · Cited by 159
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Jovaisaite, V., & Auwerx, J. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2014.12.003 · Cited by 131
Self-citationGiordano, L., Deceglie, S., D’Adamo, P., Valentino, M. L., Morgia, C. L., Fracasso, F., Roberti, M., Cappellari, M., Petrosillo, G., Ciaravolo, S., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.364 · Cited by 135
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Carelli, V., & Chan, D. C. (2014) · Neuron · doi:10.1016/j.neuron.2014.11.022 · Cited by 134
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Viscomi, C. F., Bottani, E., & Zeviani, M. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.03.001 · Cited by 109
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Self-citationOkabe, K., Yaku, K., Uchida, Y., Fukamizu, Y., Sato, T., Sakurai, T., Tobe, K., & Nakagawa, T. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.868640 · Cited by 105
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Cagin, U., & Enrı́quez, J. A. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.01.026 · Cited by 107
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Elhassan, Y., Philp, A., & Lavery, G. G. (2017) · Journal of the Endocrine Society · doi:10.1210/js.2017-00092 · Cited by 93
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Koopman, W. J. H., Beyrath, J., Fung, C., Koene, S., Rodenburg, R. J., Willems, P. H. G. M., & Smeitink, J. A. M. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201506131 · Cited by 90
Frederick, D. W., Davis, J. G., Dávila, A., Agarwal, B., Michán, S., Puchowicz, M. A., Nakamaru‐Ogiso, E., & Baur, J. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.579565 · Cited by 91
Szeto, H. H., & Liu, S. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.10.013 · Cited by 89
Upregulation of GPR109A in Parkinson’s Disease
Wakade, C. G., Chong, R. K. Y., Bradley, E., Thomas, B., & Morgan, J. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109818 · Cited by 91
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Kulikova, V., Shabalin, K., Nerinovski, K., Dölle, C., Niere, M., Yakimov, A., Redpath, P., Khodorkovskiy, M., Migaud, M. E., Ziegler, M., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664458 · Cited by 84
Gut, P., Matilainen, S., Meyer, J. G., Pällijeff, P., Richard, J., Carroll, C. J., Euro, L., Jackson, C. B., Isohanni, P., Minassian, B. A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19743-4 · Cited by 83
Self-citationLi, J., Wang, P., Long, N., Zhuang, J., Springer, D., Zou, J., Lin, Y., Bleck, C. K. E., Park, J., Kang, J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904979116 · Cited by 82
Bottani, E., Lamperti, C., Prigione, A., Tiranti, V., Persico, N., & Brunetti, D. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12111083 · Cited by 89
Poljšak, B., & Milisav, I. (2016) · Rejuvenation Research · doi:10.1089/rej.2015.1767 · Cited by 88
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Natarajan, V., Chawla, R., Mah, T. K. L., Vivekanandan, R., Tan, S., Sato, P. Y., & Mallilankaraman, K. B. (2020) · PROTEOMICS · doi:10.1002/pmic.201800404 · Cited by 83
Hamity, M. V., White, S. R., Walder, R. Y., Schmidt, M. S., Brenner, C., & Hammond, D. L. (2017) · Pain · doi:10.1097/j.pain.0000000000000862 · Cited by 79
Muscle mitochondrial stress adaptation operates independently of endogenous FGF21 action
Ost, M., Coleman, V., Voigt, A., van Schothorst, E. M., Keipert, S., van der Stelt, I., Ringel, S., Graja, A., Ambrosi, T., Kipp, A. P., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2015.11.002 · Cited by 75
BST1 regulates nicotinamide riboside metabolism via its glycohydrolase and base-exchange activities
Yaku, K., Palikhe, S., Izumi, H., Yoshida, T., Hikosaka, K., Hayat, F., Karim, M., Iqbal, T., Nitta, Y., Sato, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27080-3 · Cited by 76
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Buzková, J., Nikkanen, J., Ahola, S., Hakonen, A. H., Sevastianova, K., Hovinen, T., Yki‐Järvinen, H., Pietiläinen, K. H., Lönnqvist, T. R. I., Velagapudi, V., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201809091 · Cited by 72
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Self-citationRuggieri, S., Orsomando, G., Sorci, L., & Raffaelli, N. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.02.021 · Cited by 71
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Wodrich, A. P. K., Scott, A. W., Shukla, A. K., Harris, B. T., & Giniger, E. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.831116 · Cited by 73
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Metadata
- Authors
- Khan, N. A., Auranen, M., Paetau, I., Pirinen, E., Euro, L., Forsström, S., Pasila, L., Velagapudi, V., Carroll, C. J., Auwerx, J., & Suomalainen, A.
- Affiliations
- University of Helsinki (FI)
- University of Eastern Finland (FI)
- Institute for Molecular Medicine Finland (FI)
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Suomalainen, Anu
- ORCID
- Venue
- EMBO Molecular Medicine
- Published
- 2014-04-07
- Volume
- 6
- Issue
- 6
- Pages
- 721-731
- ISSN
- 1757-4676 (ISSN-L)
- 1757-4684
- PMC
- PMC4203351
- OpenAlex
- W2132438126
- Cited by
- 385
- References
- 34
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 19 · 2023: 32 · 2022: 29 · 2021: 36 · 2020: 45 · 2019: 37 · 2018: 39 · 2017: 31 · 2016: 30 · 2015: 34 · 2014: 12
- FWCI
- 18.17
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- EMBO Molecular Medicine (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- St George's Online Research Archive (St George's University of London) (acceptedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Työväentutkimus Vuosikirja (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- European Research Council
- Saastamoinen Foundation
- Finnish Cultural Foundation
- Finnish Diabetes Foundation
- Finnish Academy
- Jane and Aatos Erkko Foundation
- Sigrid Jusélius Foundation
- Academy of Finland, and University of Helsinki
- Ecole Polytechnique Fédérale de Lausanne
- ERC
- NIH (R01HL106511‐01A, R01AG043930)
- Velux Stiftung
- Swiss National Science Foundation
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- nicotinamide riboside, mitochondrial myopathy, NAD+ precursors, NAD+/NADH ratio, mitochondrial biogenesis, mitochondrial unfolded protein response, mitochondrial DNA deletions, skeletal muscle, brown adipose tissue, mitochondrial ATP production, disease progression
- MeSH terms
- Forkhead Box Protein O1, Animals, Adipose Tissue, Brown, Energy Metabolism, Liver, Male, Mice, Inbred C57BL, Mitochondria, NAD, Niacinamide, Pyridinium Compounds, Vitamin B Complex, Mitochondrial Myopathies, Muscle, Skeletal, Lipid Metabolism, Mice, Forkhead Transcription Factors, Sirtuin 1, Unfolded Protein Response
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