The DOI matches its Crossref record; 74 of the 75 references it cites were found in a registry or an index.
Expression and Function of Myostatin in Obesity, Diabetes, and Exercise Adaptation
Open accessAbstract
Myostatin is a member of the transforming growth factor-β/bone morphogenetic protein (TGF-β/BMP) superfamily of secreted factors that functions as a potent inhibitor of skeletal muscle growth. Moreover, considerable evidence has accumulated that myostatin also regulates metabolism and that its inhibition can significantly attenuate the progression of obesity and diabetes. Although at least part of these effects on metabolism can be attributable to myostatin's influence over skeletal muscle growth and therefore on the total volume of metabolically active lean body mass, there is mounting evidence that myostatin affects the growth and metabolic state of other tissues, including the adipose and the liver. In addition, recent work has explored the role of myostatin in substrate mobilization, uptake, and/or utilization of muscle independent of its effects on body composition. Finally, the effects of both endurance and resistance exercise on myostatin expression, as well as the potential role of myostatin in the beneficial metabolic adaptations occurring in response to exercise, have also begun to be delineated in greater detail. The purpose of this review was to summarize the work to date on the expression and function of myostatin in obesity, diabetes, and exercise adaptation.
Overview
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
Verification
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?
The cited source doesn’t support the claim as written.
In the citing paper
“On the contrary, inhibition of myostatin upregulates oxidative metabolism in SkM [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
Checked by a reasoning model — may be wrong.
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
“Myostatin was the first identified muscle-secreted factor and is known to promote SkM atrophy [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
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
“It is the only myokine known to be downregulated by acute and chronic endurance- and resistance-type exercise in both rodents and humans [115].”
From The Role of Exercise in the Interplay between Myokines, Hepatokines, Osteokines, Adipokines, and Modulation of Inflammation for Energy Substrate Redistribution and Fat Mass Loss: A Review (2020) · cites this paper as [115]
Experimental — accuracy not yet measuredIn the citing paper
“Myostatin expression increases in skeletal muscle due to obesity and IR. Thus, it could favor the loss of skeletal muscle in SO [14, 61, 62].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [61]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Regulation of skeletal muscle mass in mice by a new TGF-p superfamily member
McPherron, A. C., Lawler, A. M., & Lee, S.-J. (1997) · Nature · doi:10.1038/387083a0 · Cited by 4,013
Self-citationDouble muscling in cattle due to mutations in the myostatin gene
McPherron, A. C., & Lee, S.-J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12457 · Cited by 2,039
Self-citationA deletion in the bovine myostatin gene causes the double–muscled phenotype in cattle
Grobet, L., Royo Martin, L. J., Poncelet, D., Pirottin, D., Brouwers, B., Riquet, J., Schoeberlein, A., Dunner, S., Ménissier, F., Massabanda, J., et al. (1997) · Nature Genetics · doi:10.1038/ng0997-71 · Cited by 1,556
Myostatin Mutation Associated with Gross Muscle Hypertrophy in a Child
Schuelke, M., Wagner, K. R., Stolz, L. E., Hübner, C., Riebel, T., Kömen, W., Braun, T., Tobin, J. F., & Lee, S.-J. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa040933 · Cited by 1,399
Mutations in myostatin ( GDF8 ) in Double-Muscled Belgian Blue and Piedmontese Cattle
Kambadur, R., Sharma, M., Smith, T. P. L., & Bass, J. J. (1997) · Genome Research · doi:10.1101/gr.7.9.910 · Cited by 1,204
Myostatin, a Negative Regulator of Muscle Growth, Functions by Inhibiting Myoblast Proliferation
Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J., & Kambadur, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004356200 · Cited by 1,014
Myostatin Inhibits Myoblast Differentiation by Down-regulating MyoD Expression
Langley, B. C., Thomas, M., Bishop, A., Sharma, M., Gilmour, S., & Kambadur, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204291200 · Cited by 910
Induction of Cachexia in Mice by Systemically Administered Myostatin
Zimmers, T. A., Davies, M. V., Koniaris, L. G., Haynes, P. A., Esquela‐Kerscher, A., Tomkinson, K. N., McPherron, A. C., Wolfman, N. M., & Lee, S. (2002) · Science · doi:10.1126/science.1069525 · Cited by 908
Self-citationMosher, D. S., Quignon, P., Bustamante, C. D., Sutter, N. B., Mellersh, C. S., Parker, H. G., & Ostrander, E. A. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030079 · Cited by 826
Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
Trendelenburg, A. U., Meyer, A., Rohner, D., Boyle, J., Hatakeyama, S., & Glass, D. J. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00105.2009 · Cited by 792
Flagged first, then by citations
1 of the 75 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 101–200 of 206
Diabetes Mellitus Should Be Considered While Analysing Sarcopenia-Related Biomarkers
Rentflejsz, J., & Wojszel, Z. B. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13041107 · Cited by 18
Grade, C. V. C., Mantovani, C. S., Fontoura, M. A., Yusuf, F., Brand‐Saberi, B., & Alvares, L. E. (2017) · Molecular Biology Reports · doi:10.1007/s11033-017-4126-z · Cited by 17
Kazemi, F. (2019) · Cytokine · doi:10.1016/j.cyto.2019.04.012 · Cited by 17
Spirulina supplementation during gradual weight loss in competitive wrestlers
Bagheri, R., Negaresh, R., Motevalli, M. S., Wong, A., Ashtary‐Larky, D., Kargarfard, M., & Rashidlamir, A. (2021) · British Journal Of Nutrition · doi:10.1017/s000711452100091x · Cited by 17
Bijeh, N., Ahmadi, M. M., Moghadam, B. H., Eskandari, M., & Golestani, F. (2022) · Biological Research For Nursing · doi:10.1177/10998004211073123 · Cited by 15
Bian, X., Wang, Q., Wang, Y., & Lou, S. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1305208 · Cited by 15
Szulc, P., Hofbauer, L. C., Rauner, M., Goettsch, C., Chapurlat, R. D., & Schoppet, M. (2012) · European Journal of Endocrinology · doi:10.1530/eje-12-0512 · Cited by 15
Bagheri, R., Ashtary‐Larky, D., Elliott, B., Willoughby, D. S., Kargarfard, M., Alipour, M., Lamuchi-Deli, N., Kooti, W., Asbaghi, O., & Wong, A. (2021) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2021.1874020 · Cited by 14
Impact of diets rich in olive oil, palm oil or lard on myokine expression in rats
Gauze-Gnagne, C., Raynaud, F., Djohan, Y. F., Lauret, C., Feillet‐Coudray, C., Coudray, C., Monde, A., Koffi, G., Morena-Carrere, M., Camara-Cissé, M., et al. (2020) · Food & Function · doi:10.1039/d0fo01269f · Cited by 13
Effects triggered in the periphery by acupuncture
Lund, I., & Lundeberg, T. (2015) · Acupuncture and Related Therapies · doi:10.1016/j.arthe.2015.08.002 · Cited by 13
Impaired Musculoskeletal Response to Age and Exercise in PPARβ−/− Diabetic Mice
Fu, H., Desvergne, B., Ferrari, S., & Bonnet, N. (2014) · Endocrinology · doi:10.1210/en.2014-1585 · Cited by 13
Hosseini, S. R. A., Moienneia, N., & Rad, M. M. (2017) · Obesity Medicine · doi:10.1016/j.obmed.2017.01.004 · Cited by 14
Hekmatikar, A. H. A., Nelson, A. R., & Petersen, A. C. (2023) · BMC Cancer · doi:10.1186/s12885-023-11391-3 · Cited by 13
Lee, Y., Lee, S. R., Baek, H. J., Kwon, J. E., Baek, N., Kang, T. H., Kim, H., & Kang, S. C. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052982 · Cited by 13
Jin, Y., Wan, K., Liu, C., Cheng, W., & Wang, R. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1401342 · Cited by 12
Takao, N., Kurose, S., Miyauchi, T., Onishi, K., Tamanoi, A., Tsuyuguchi, R., Fujii, A., Yoshiuchi, S., Takahashi, K., Tsutsumi, H., et al. (2021) · BMC Endocrine Disorders · doi:10.1186/s12902-021-00808-4 · Cited by 13
Skeletal muscle disorders as risk factors for type 2 diabetes
Tammineni, E. R., Manno, C. D., Oza, G., & Figueroa, L. (2025) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2025.112466 · Cited by 12
Lee, K., Vakili, S., Burden, H. J., Adams, S. E., Smith, G. C., Kulatea, B., Wright‐McNaughton, M., Sword, D., Watene-O’Sullivan, C., Atiola, R. D., et al. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101464 · Cited by 11
Possible Mechanisms Linking Obesity, Steroidogenesis, and Skeletal Muscle Dysfunction
Sheptulina, A. F., Antyukh, K. Y., Kiselev, A. R., Mitkovskaya, N. P., & Drapkina, O. M. (2023) · Life · doi:10.3390/life13061415 · Cited by 11
Genetic variation in human muscle strength—opportunities for therapeutic interventions?
Thomis, M. A., & Aerssens, J. (2012) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2012.03.003 · Cited by 11
Tammam, A. A.-E., Rizg, W. Y., Boushra, A. F., Alhelf, M., Alissa, M., Soliman, G. F., Ouais, G. N., Hosny, K. M., Alkhalidi, H. M., & Elebiary, A. M. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1228525 · Cited by 10
Ali, S. M., Ahmad, K., Shaikh, S., Chun, H. J., Choi, I., & Lee, E. J. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2223652 · Cited by 11
Schalt, A., Johannsen, M., Kim, J., Chen, R., Murphy, C. J., Coker, M. S., Gunga, H., Coker, R. H., & Steinach, M. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01761 · Cited by 10
Liu, S., Han, W., Jiang, S., Zhao, C., & Wu, C. (2015) · Gene · doi:10.1016/j.gene.2015.11.016 · Cited by 10
Juzentaihoto Suppresses Muscle Atrophy in KKAy Mice
Ishida, T., Jobu, K., Morisawa, S., Kawada, K., Yoshioka, S., & Miyamura, M. (2022) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b22-00039 · Cited by 9
Halmos, T., & Suba, I. (2014) · Orvosi Hetilap · doi:10.1556/oh.2014.29959 · Cited by 9
Mińko, A., Turoń-Skrzypińska, A., Rył, A., Mańkowska, K., Cymbaluk‐Płoska, A., & Rotter, I. (2024) · Biomedicines · doi:10.3390/biomedicines12040836 · Cited by 8
Myostatin in Obesity: A Molecular Link Between Metabolic Dysfunction and Musculotendinous Remodeling
Cesanelli, L., Minderis, P., Fokin, A., Ratkevičius, A., Satkunskienė, D., & Degens, H. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020967 · Cited by 7
Casamitjana, L., Blanco‐Hinojo, L., Giménez‐Palop, O., Pujol, J., Martínez‐Vilavella, G., Esteba‐Castillo, S., Pareja, R., Freijo, V., Vigil, L., Deus, J., et al. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11071831 · Cited by 7
Elashry, M. I., Eldaey, A., Glenske, K., Matsakas, A., Wenisch, S., Arnhold, S., & Patel, K. (2019) · Journal of Anatomy · doi:10.1111/joa.13025 · Cited by 7
Maladaptive Immune Activation in Age-Related Decline of Muscle Function
Montano, M. A., & Correa‐de‐Araujo, R. (2023) · The Journals of Gerontology Series A · doi:10.1093/gerona/glad036 · Cited by 7
Bivona, J. J., & Poynter, M. E. (2021) · PLoS ONE · doi:10.1371/journal.pone.0261618 · Cited by 7
Carraro, U. (2018) · European Journal of Translational Myology · doi:10.4081/ejtm.2018.7366 · Cited by 8
Novel insights regarding mechanisms for treatment of sarcopenia
Kraemer, R. R., & Castracane, V. D. (2014) · Metabolism · doi:10.1016/j.metabol.2014.11.002 · Cited by 7
Long non-coding RNA MALAT1: A crucial factor in fibrotic diseases
Ran, L., Pan, W., Feng, J., & Tang, L. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102630 · Cited by 8
Skeletal Muscle as Endocrine Organ
Ma, M., Zhang, Z., Hai, B., & Zhang, Y. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-88361-3_22 · Cited by 9
Cytokines in Skeletal Muscle Growth and Decay
Orzechowski, A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_5 · Cited by 7
Insight on sarcopenic obesity and epicatechin as a promising treatment option
Sabarathinam, S., Dhanasekaran, D., & Ganamurali, N. (2023) · Diabetes & Metabolic Syndrome Clinical Research & Reviews · doi:10.1016/j.dsx.2023.102856 · Cited by 6
Curiel-Cervantes, V., Solís‐S, J. C., Camacho-Barrón, M., Aguilar-Galarza, A., Valencia, M. E., & Anaya‐Loyola, M. A. (2022) · Growth Factors · doi:10.1080/08977194.2022.2049262 · Cited by 5
Tsutsui, Y., Itoh, S., Toshima, T., Yoshio, S., Yoshiya, S., Izumi, T., Iseda, N., Toshida, K., Nakayama, Y., Ishikawa, T., et al. (2024) · Hepatology Research · doi:10.1111/hepr.14027 · Cited by 5
Liu, R., Xi, Y., Duan, X., Zhao, Y., & Tian, Z. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123628 · Cited by 4
Larrad-Sáinz, A., Núñez, M. G., Barabash, A., Prados, I. G., Valerio, J., Gil, J. L. E., Crespo, M. E. O., de la Muela, M. H., Madrid, B. B., Serrano‐García, I., et al. (2025) · Nutrients · doi:10.3390/nu17152487 · Cited by 4
Lee, H., & Lim, Y. (2025) · Nutrients · doi:10.3390/nu17223615 · Cited by 5
Serum Myostatin among Excessive Drinkers
Martín‐González, C., Pérez‐Hernández, O., Rodríguez, A. G., Abreu-González, P., Toledo, P. O., Fernández-Rodríguez, C. M., Alvisa-Negrín, J. C., Martı́nez-Riera, A., & González‐Reimers, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032981 · Cited by 4
Can Exercise-Mediated Adipose Browning Provide an Alternative Explanation for the Obesity Paradox?
Zhao, J., Li, X., Liang, C., & Yan, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26051790 · Cited by 5
Shiomitsu, S., Hansen, C. M., Lenfest, M. I., Frye, C. W., & Wakshlag, J. J. (2022) · Journal of the American Veterinary Medical Association · doi:10.2460/javma.22.07.0323 · Cited by 5
Diabetes and Physical Activity
Banu, J. (2016) · Journal of Endocrinology and Diabetes · doi:10.15226/2374-6890/3/1/00140 · Cited by 4
Gender Features of Radical Oxidation of Lipids in Menopausal Women and Men in Andropause
Колесникова, Л. И., Михайловна, М. И., Semenova, N. V., Osipova, E. V., & Darenskaya, M. A. (2016) · Annals of the Russian academy of medical sciences · doi:10.15690/vramn629 · Cited by 4
Transcript characteristic of myostatin in sheep fibroblasts
Lü, J., Ren, H., Sheng, X., Zhang, X., Li, S., Zhao, F., Zhou, X., Zhang, L., Wei, C., Ding, J., et al. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24140 · Cited by 3
Recent Studies on Natural Products that Improve Myogenesis
채종범, & 남주옥 (2020) · JoLS Journal of Life Sciences · doi:10.5352/jls.2020.30.2.202 · Cited by 3
Marine Phytoplankton Improves Exercise Recovery in Humans and Activates Repair Mechanisms in Rats
Sharp, M. H., Şahin, K., Stefan, M., Gheith, R. H., Reber, D. D., Ottinger, C., Orhan, C., Tuzcu, M., Şahin, N., Lowery, R. P., et al. (2020) · International Journal of Sports Medicine · doi:10.1055/a-1320-1061 · Cited by 3
Studying Myostatin as a Diagnostic Indicator in Sera of Iraqi Women with Metabolic Syndrome
Assaf, R. H., & Farhan, L. O. (2023) · Baghdad Science Journal · doi:10.21123/bsj.2023.8180 · Cited by 3
zadeh, M. H., Fatemi, S. F., Rezvani, R., Farsani, G. M., Pazouki, A., & Zamaninour, N. (2024) · Obesity Surgery · doi:10.1007/s11695-024-07465-1 · Cited by 3
Investigation of snails transmitting parasitic diseases in Yunnan Province.
Yuan-xiao, C., Zhang, W., Ming, T., Chen, Y., WenLin, W., & Naiguang, Z. (2009) · Journal of Pathogen Biology · Cited by 3
Reinhardt, J., Dankbar, B., Geers, F., Werbenko, E., Geyer, C., Bleckmann, A., Menck, K., Grözinger, A., Hartmann, W., Tio, J., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03622-7 · Cited by 2
Bondi, D., Bevere, M., Piccirillo, R., Sorci, G., Felice, V. D., Cecconi, A. D. R., Damico, D. C. S., Pietrangelo, T., & Fulle, S. (2023) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2023.107705 · Cited by 2
Masik, N. P., & Kalandey, K. Y. (2019) · PAIN JOINTS SPINE · doi:10.22141/2224-1507.9.2.2019.172123 · Cited by 2
МЕТААНАЛИЗ АССОЦИАЦИИ ПОЛИМОРФИЗМА ГЕНА MSTN RS1805086 С СИЛОВЫМИ ПОКАЗАТЕЛЯМИ СПОРТСМЕНОВ
Aksenov, M. O. (2021) · Siberian Journal of Life Sciences and Agriculture · doi:10.12731/2658-6649-2021-13-2-303-335 · Cited by 2
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-031-40116-9_56 · Cited by 2
Genes in Skeletal Muscle Remodeling and Impact of Feeding
Chen, Y.-W., Barberio, M. D., & Hubal, M. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802167-5.00023-2 · Cited by 1
Sporda Dayanıklılık ve Aerobik Dayanıklılık Testleri
Atasever, G., & Kıyıcı, F. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2773 · Cited by 1
Egzersizde Protein Sentezi ve Etkileyen Faktörler
Akkuş, E. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2771 · Cited by 1
Apelin and Myostatin Levels in Adolescents With Type‐1‐Diabetes
Cohen, M., Weiss, L., Weiss, R., Shehadeh, N., & Khamaisi, M. (2025) · Pediatric Diabetes · doi:10.1155/pedi/1578938 · Cited by 1
Maternal Health and Safety Outcomes of Prenatal Myostatin Inhibition in Osteogenesis Imperfecta Mice
Crawford, T. K., Lafaver, B. N., Oestreich, A. K., Davis, B. R., Cooper, C. S., Chapman, I. M., Luhmann, M. K., Opoku, R., Schulte, A. K., Mastaitis, J. W., et al. (2025) · Endocrinology · doi:10.1210/endocr/bqaf080 · Cited by 1
Kim, M. Y., Harriot, A. D., & Kim, D. (2026) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2026.115896 · Cited by 1
Pollock, N. K. (2012) · IBMS BoneKEy · doi:10.1038/bonekey.2012.25 · Cited by 1
Intermittent breaking of isolation may ameliorate decrease in physical activity caused by isolation
Uchida, A., Nakagawa, K., Yoshimi, K., Nagasawa, Y., Yamaguchi, K., Uesaka, N., & Tohara, H. (2024) · PLoS ONE · doi:10.1371/journal.pone.0314262 · Cited by 1
Choi, A. R., & Kim, K. S. (2025) · Journal of Korean Diabetes · doi:10.4093/jkd.2025.26.2.75 · Cited by 1
Krentz, A. J., & Bédossa, P. (2019) · Springer eBooks · doi:10.1007/978-3-030-11748-1_10 · Cited by 1
Management of Sarcopenic Obesity for Older Adults with Lower-Extremity Osteoarthritis
Liou, T., Liao, C., & Huang, S. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.93487 · Cited by 1
Background and Management of Muscular Atrophy
Cseri, J. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.90959 · Cited by 1
Pashkovа, O. Y., Chudova, N. I., & Litvinenko, O. S. (2021) · Ukrainian Journal of Pediatric Endocrinology · doi:10.30978/ujpe2021-2-19 · Cited by 1
Miedany, Y. M. E. (2022) · Springer eBooks · doi:10.1007/978-3-030-87950-1_3 · Cited by 1
Zarfeshani, A. (2016) · Journal of Obesity and Bariatrics · doi:10.13188/2377-9284.1000018 · Cited by 1
Daryanoosh, F., Moghadam, M. S., Pahlavani, H. A., Bahmanbeglou, N. A., & Mirzaei, S. (2022) · Research Square · doi:10.21203/rs.3.rs-2105962/v1 · Cited by 1
Skjølsvik, A. M. (2012) · NORA - Norwegian Open Research Archives
Interplay of Nutrients and Muscle Myokines on the Preventive Health for Obesity Disorders
Venkata, R. K. (2019) · Interventions in Obesity & Diabetes · doi:10.31031/iod.2019.03.000558
Qomi, M. H., Arshadi, S., Banaeifar, A., & Kazemzadeh, Y. (2019) · Nutrition and Food Sciences Research · doi:10.29252/nfsr.6.4.9
Myostatin and plasticity of skeletal muscle tissue
Pagliara, V., Nasso, R., Ascione, A., Masullo, M., & Arcone, R. (2019) · Summer Conferences of Sports Science · doi:10.14198/jhse.2019.14.proc5.12
Townsend, L. K., McKie, G. L., Shamshoum, H., & Wright, D. C. (2020) · Routledge eBooks · doi:10.4324/9781003123835-3
Zhang, Y., Zheng, Y., Wu, L., Li, Z., Xiao, N., Li, H., An, L., Shi, D., Liu, Q., & Cui, K. (2020) · Research Square · doi:10.21203/rs.3.rs-125471/v1
Kutty, P. K., & Kutty, M. K. (2021) · Springer eBooks · doi:10.1007/978-981-33-6408-0_1
Ibrahim, M. A., Mustafa, A. I., Elhalim, W. A. A., & Gendia, S. H. (2020) · Benha Journal of Applied Sciences · doi:10.21608/bjas.2020.137121
Cordingley, D. M., & Cornish, S. M. (2022) · OBM Geriatrics · doi:10.21926/obm.geriatr.2204206
Rahmanian, N., Hekmat, A., & Hajebrahimi, Z. (2022) · علوم و فناوری فضایی · doi:10.30699/jsst.2021.1346
Obesity, Myokines, and Metabolic Health
Malandrino, N., & Ahima, R. S. (2023) · Springer eBooks · doi:10.1007/978-3-319-12125-3_56-1
Muskulatur: „peripheres mechanisch- und Signalstoff-gestütztes Zentrum der Gesundheit“
Laube, W. (2023) · Springer eBooks · doi:10.1007/978-3-662-67753-7_8
Dragan, F. G., Gonçalves, L. M. F., & de Almeida‐Val, V. M. F. (2024) · International Journal of Fisheries and Aquatic Studies · doi:10.22271/fish.2024.v12.i1a.2886
Mogharnasi, M., Ilbeigi, S., Mehr, P. A., & rezaee, S. (2024) · Research Square · doi:10.21203/rs.3.rs-4107723/v1
Sportif Performans Açısından İzokinetik Kuvvet Değerlendirme ve Yorumlama
Yılmaz, H. H., & Daşkesen, S. S. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2774
Spor Mimarisi ve Dijital Teknolojilerin Kesişimi
Dertli, M. E., & Dertli, Ş. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2775
Er, F. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2770
Video Analiz Yönteminin Performans ve Teknik Gelişimine Katkısı (Alp Disiplini Örneği)
Aktaş, B. S. (2024) · Özgür Yayınları eBooks · doi:10.58830/ozgur.pub640.c2793
He, H.-X., Zhu, K.-C., Liu, B.-S., Guo, H., Zhang, N., Xian, L., Zhu, T., Zhang, D., & Yang, M. (2025) · Fish Physiology and Biochemistry · doi:10.1007/s10695-025-01606-8
Role of ACTN3 R577X Polymorphism in Mitochondrial Myokines After Endurance Exercise
Manoel, L. A. D. S., de Fontes-Junior, A. A., Sierra, A., de Menezes, D. C., Zocoler, C. A. S., Lima, G., Barbeiro, H. V., de Souza, H. P., Pesquero, J., & Cury‐Boaventura, M. F. (2026) · Clinical bioenergetics · doi:10.3390/clinbioenerg2010002
Reduced masticatory stimuli modulate myokine secretion in the masseter muscle in mice
Kawasaki, M., Kato, C., Tanigawa, M., Misawa, E., Nakamura, K., Inaba, H., Abe, Y., Kokai, S., & ONO, T. (2026) · PLoS ONE · doi:10.1371/journal.pone.0341417
Radfar, B., Bagheri, R., Ghobadi, H., Hematabadi, A., Askari, B., Rashidlamir, A., & Dutheil, F. (2026) · Nutrients · doi:10.3390/nu18040611
Metadata
- Authors
- ALLEN, D. L., HITTEL, D. S., & MCPHERRON, A. C.
- Affiliations
- University of Colorado Boulder (US)
- University of Calgary (CA)
- National Institutes of Health (US)
- Venue
- Medicine & Science in Sports & Exercise
- Published
- 2011-10
- Volume
- 43
- Issue
- 10
- Pages
- 1828-1835
- ISSN
- 0195-9131 (ISSN-L)
- PMC
- PMC3192366
- OpenAlex
- W2008438711
- Cited by
- 207
- References
- 75
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 19 · 2023: 17 · 2022: 24 · 2021: 16 · 2020: 13 · 2019: 14 · 2018: 12 · 2017: 13 · 2016: 7 · 2015: 11 · 2014: 17 · 2013: 9 · 2012: 9
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Medicine & Science in Sports & Exercise (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (ZIADK056020, ZIADK075048)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- myostatin, obesity, diabetes mellitus, exercise adaptation, skeletal muscle growth, adipose tissue, liver, substrate mobilization, lean body mass, endurance exercise, resistance training, metabolic adaptation
- MeSH terms
- Adaptation, Physiological, Adipose Tissue, Animals, Diabetes Mellitus, Type 2, Female, Humans, Liver, Male, Obesity, Exercise, Muscle, Skeletal, Mice, Rats, Myostatin
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
