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Global Phosphoproteomic Analysis of Human Skeletal Muscle Reveals a Network of Exercise-Regulated Kinases and AMPK Substrates
Open accessAbstract
Exercise is essential in regulating energy metabolism and whole-body insulin sensitivity. To explore the exercise signaling network, we undertook a global analysis of protein phosphorylation in human skeletal muscle biopsies from untrained healthy males before and after a single high-intensity exercise bout, revealing 1,004 unique exercise-regulated phosphosites on 562 proteins. These included substrates of known exercise-regulated kinases (AMPK, PKA, CaMK, MAPK, mTOR), yet the majority of kinases and substrate phosphosites have not previously been implicated in exercise signaling. Given the importance of AMPK in exercise-regulated metabolism, we performed a targeted in vitro AMPK screen and employed machine learning to predict exercise-regulated AMPK substrates. We validated eight predicted AMPK substrates, including AKAP1, using targeted phosphoproteomics. Functional characterization revealed an undescribed role for AMPK-dependent phosphorylation of AKAP1 in mitochondrial respiration. These data expose the unexplored complexity of acute exercise signaling and provide insights into the role of AMPK in mitochondrial biochemistry.
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“Moreover, the phosphorylation of human BAG3 on Thr285 and Ser 289 decreases in response to endurance exercise (61).”
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Smyth, G. K. (2004) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1027 · Cited by 11,829
Role of AMP-Activated Protein Kinase in Mechanism of Metformin Action
Zhou, G., Myers, R., Li, Y., Chen, Y., Shen, X., Fenyk-Melody, J., Wu, M., Ventre, J., Doebber, T., Fujii, N., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13505 · Cited by 5,652
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
Gillet, L. C., Navarro, P., Tate, S., Röst, H., Selevsek, N., Reiter, L., Bonner, R., & Aebersold, R. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o111.016717 · Cited by 2,877
Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation
Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B. W., Latham, V. M., & Sullivan, M. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr1122 · Cited by 1,636
Antioxidants prevent health-promoting effects of physical exercise in humans
Ristow, M., Zarse, K., Oberbach, A., Klöting, N., Birringer, M., Kiehntopf, M., Stumvoll, M., Kahn, C. R., & Blüher, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903485106 · Cited by 1,582
Cited by
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Items 201–300 of 426
Molecular Transducers of Physical Activity Consortium (MoTrPAC): human studies design and protocol
MoTrPAC Study Group, Jakicic, J. M., Kohrt, W. M., Houmard, J. A., Miller, M. E., Radom‐Aizik, S., Rasmussen, B. B., Ravussin, É., Serra, M. C., Stowe, C. L., et al. (2024) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00102.2024 · Cited by 26
Strang, J. E., Astridge, D. D., Nguyen, V., & Reigan, P. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02354 · Cited by 27
Hesketh, S. J., Sutherland, H., Lisboa, P. J. G., Jarvis, J. C., & Burniston, J. G. (2020) · The FASEB Journal · doi:10.1096/fj.202000668rr · Cited by 21
Exercise and health: historical perspectives and new insights
Hargreaves, M. (2021) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00242.2021 · Cited by 26
Rinschen, M. M., Harder, J. L., Carter-Timofte, M. E., Rodriguez, L. Z., Mirabelli, C., Demir, F., Kurmasheva, N., Ramakrishnan, S. K., Kunke, M., Tan, Y., et al. (2022) · Science Signaling · doi:10.1126/scisignal.abo7940 · Cited by 24
Hwang, P. S., & Willoughby, D. S. (2018) · Journal of the American College of Nutrition · doi:10.1080/07315724.2018.1461146 · Cited by 22
Dowling, P., Swandulla, D., & Ohlendieck, K. (2023) · Cells · doi:10.3390/cells12212560 · Cited by 22
McConell, G. K. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00511.2019 · Cited by 24
Hoshino, D., Kawata, K., Kunida, K., Hatano, A., Yugi, K., Wada, T., Fujii, M., Sano, T., Ito, Y., Furuichi, Y., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101558 · Cited by 23
Masson, S. W. C., Woodhead, J. S. T., D’Souza, R. F., Broome, S. C., MacRae, C. L., Cho, H. C., Atiola, R. D., Futi, T., Dent, J. R., Shepherd, P. R., et al. (2021) · The Journal of Physiology · doi:10.1113/jp281352 · Cited by 21
Lin, K., Wilson, G. M., Blanco, R., Steinert, N. D., Zhu, W. G., Coon, J. J., & Hornberger, T. A. (2021) · The Journal of Physiology · doi:10.1113/jp281071 · Cited by 20
Verbrugge, S. A. J., Alhusen, J. A., Kempin, S., Pillon, N. J., Rozman, J., Wackerhage, H., & Kleinert, M. (2022) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30179 · Cited by 21
Self-citationA primer on global molecular responses to exercise in skeletal muscle: Omics in focus
Murach, K. A., & Bagley, J. R. (2025) · Journal of sport and health science/Journal of Sport and Health Science · doi:10.1016/j.jshs.2025.101029 · Cited by 22
Improving Phosphoproteomics Profiling Using Data-Independent Mass Spectrometry
Srinivasan, A., Sing, J., Gingras, A., & Röst, H. L. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00172 · Cited by 22
Zhao, J., Yang, Q., Zhang, L., Liang, X., Sun, X., Wang, B., Chen, Y., Zhu, M. J., & Du, . (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.149 · Cited by 21
AMPK Interactome Reveals New Function in Non-homologous End Joining DNA Repair
Chen, Z., Wang, C., Jain, A., Srivastava, M., Tang, M., Zhang, H., Feng, X., Nie, L., Su, D., Xiong, Y., et al. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001794 · Cited by 23
Exercise—A Panacea of Metabolic Dysregulation in Cancer: Physiological and Molecular Insights
Raun, S. H., Buch‐Larsen, K., Schwarz, P., & Sylow, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073469 · Cited by 20
Alack, K., Weiß, A., Krüger, K., Höret, M., SCHERMULY, R. T., Frech, T., Eggert, M., & Mooren, F. (2020) · Scientific Reports · doi:10.1038/s41598-020-57676-6 · Cited by 21
Temporal dynamics of the multi-omic response to endurance exercise training across tissuesPreprint
MoTrPAC Study Group, Amar, D., Gay, N. R., Beltran, P. M. J., Adkins, J., Armenteros, J. J. A., Ashley, E. A., Ávila-Pacheco, J., Bae, D., Bararpour, N., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.21.508770 · Cited by 19
Malik, Z. A., Davies, K. A. B., Hall, E. C. R., Barrett, J., Pullinger, S. A., Erskine, R. M., Shepherd, S. O., Iqbal, Z., Edwards, B., & Burniston, J. G. (2020) · Proteomes · doi:10.3390/proteomes8030022 · Cited by 18
Protocol for the processing and downstream analysis of phosphoproteomic data with PhosR
Kim, H. J., Kim, T.-Y., Xiao, D., & Yang, P. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100585 · Cited by 19
Self-citationTransient changes to metabolic homeostasis initiate mitochondrial adaptation to endurance exercise
Dent, J. R., Stocks, B., Campelj, D. G., & Philp, A. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.03.022 · Cited by 19
Morrison, K. R., Wang, T., Chan, K. Y., Trotter, E. W., Gillespie, A., Michael, M., Oakhill, J. S., Hagan, I., & Petersen, J. (2023) · Open Biology · doi:10.1098/rsob.230021 · Cited by 17
Henríquez‐Olguín, C., Meneses‐Valdés, R., Kritsiligkou, P., & Fuentes-Lemus, E. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.10.404 · Cited by 19
Exercise Improves Heart Function after Myocardial Infarction: The Merits of AMPK
Zhang, X., Zhao, Y., Guo, D., Luo, M., Zhang, Q., Zhang, L., & Zhang, D. (2024) · Cardiovascular Drugs and Therapy · doi:10.1007/s10557-024-07564-2 · Cited by 20
Akberdin, I. R., Kiselev, I. N., Pintus, S. S., Sharipov, R., Vertyshev, A. Y., Виноградова, О. Л., Popov, D. V., & Kolpakov, F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910353 · Cited by 19
Proteomic study of skeletal muscle in obesity and type 2 diabetes: progress and potential
Kruse, R., & Højlund, K. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2018.1528147 · Cited by 20
Pauper, M., Hentschel, A., Tiburcy, M., Beltrán, S., Ruck, T., Schara, U., & Roos, A. (2025) · Biomolecules · doi:10.3390/biom15010130 · Cited by 18
Chaanine, A. H., Higgins, L., Markowski, T. W., Harman, J. C., Kachman, M. T., Burant, C., Navar, L. G., Busija, D. W., & Delafontaine, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010235 · Cited by 16
Zuo, C., Ma, X., Ye, C., Zheng, Z., & Bo, S. (2023) · Environmental Health and Preventive Medicine · doi:10.1265/ehpm.23-00146 · Cited by 17
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Boengler, K., Eickelmann, C., & Kleinbongard, P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084491 · Cited by 17
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Kruse, R., Sahebekhtiari, N., & Højlund, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155374 · Cited by 19
Regulation of nutrient uptake by AMP-activated protein kinase
Alghamdi, F. B., Alshuweishi, Y., & Salt, I. P. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109807 · Cited by 18
He, L., She, X., Guo, L., Gao, M., Wang, S., Lu, Z., Guo, H.-T., Li, R., Nie, Y., Xing, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58790-7 · Cited by 16
Exercise-responsive phosphoproteins in the heart
Guo, H., Isserlin, R., Emili, A., & Burniston, J. G. (2017) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2017.08.001 · Cited by 16
Ottensmeyer, J., Esch, A., Baeta, H., Sieger, S., Gupta, Y., Rathmann, M. F., Jeschke, A., Jacko, D., Schaaf, K., Schiffer, T., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.07.088 · Cited by 18
Pantothenate kinase 4 controls skeletal muscle substrate metabolism
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Self-citationPataky, M. W., Heppelmann, C. J. H., Sevits, K. J., Asokan, A. K., Kumar, A. P., Klaus, K. A., Dasari, S., Kunz, H., Strub, M. D., Robinson, M. M., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60049-0 · Cited by 19
The effect of SiNPs on DNA methylation of genome in mouse spermatocytes
Sang, Y., Liu, J., Li, X., Zhou, G., Zhang, Y., Gao, L., Zhao, Y., & Zhou, X. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-13459-8 · Cited by 16
Mejia, G. L., Asiedu, M. N., Hitoshi, Y., Dussor, G. O., & Price, T. J. (2016) · PAIN Reports · doi:10.1097/pr9.0000000000000562 · Cited by 14
Drosophilaas a Model System to Study Nonautonomous Mechanisms Affecting Tumour Growth and Cell Death
Parvy, J.-P., Hodgson, J. A., & Cordero, J. B. (2018) · BioMed Research International · doi:10.1155/2018/7152962 · Cited by 17
Knudsen, J. R., Henríquez‐Olguín, C., Li, Z., & Jensen, T. E. (2019) · Experimental Physiology · doi:10.1113/ep087545 · Cited by 16
Self-citationSmall, L., Brandon, A. E., Parker, B. L., Deshpande, V., Samsudeen, A., Kowalski, G. M., Reznick, J., Wilks, D. L., Preston, E., Bruce, C. R., et al. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.04.006 · Cited by 15
Self-citationSpengler, K., Zibrova, D., Woods, A., Langendorf, C. G., Scott, J. W., Carling, D., & Heller, R. (2020) · Biochemical Journal · doi:10.1042/bcj20200555 · Cited by 15
Onslev, J., Jensen, J., Bangsbo, J., Wojtaszewski, J. F. P., & Hostrup, M. (2018) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-01349 · Cited by 15
Self-citationElongated mitochondrial constrictions and fission in muscle fatigue
Lavorato, M., Loro, E., Debattisti, V., Khurana, T. S., & Franzini‐Armstrong, C. (2018) · Journal of Cell Science · doi:10.1242/jcs.221028 · Cited by 15
Brescia, M., Chao, Y., Koschinski, A., Tomek, J., & Zaccolo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197056 · Cited by 15
Effects of extracellular orotic acid on acute contraction-induced adaptation patterns in C2C12 cells
Beiter, T., Hudemann, J., Burgstahler, C., Niess, A. M., & Munz, B. (2018) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-018-3330-z · Cited by 14
Sabaratnam, R., Pedersen, A. J. T., Eskildsen, T. V., Kristensen, J. M., Wojtaszewski, J. F. P., & Højlund, K. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-02679 · Cited by 15
Self-citationFilamin C dimerisation is regulated by HSPB7
Wang, Z., Cao, G., Collier, M. P., Qiu, X., Broadway‐Stringer, S., Šaman, D., Ng, J. Z. Y., Sen, N., Azad, A. J., Hooper, C. L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58889-x · Cited by 14
Juginović, A., Kekić, A., Aranza, I., Biloš, V., & Armanda, M. (2025) · Life · doi:10.3390/life15071023 · Cited by 14
Association of physical activity and trajectories of physical activity with cardiovascular disease
Chrysant, S. G., & Chrysant, G. S. (2023) · Expert Review of Cardiovascular Therapy · doi:10.1080/14779072.2023.2174102 · Cited by 13
The genetic and dietary landscape of the muscle insulin signalling network
van Gerwen, J., Masson, S. W. C., Cutler, H. B., Díaz‐Vegas, A., Potter, M., Stöckli, J., Madsen, S., Nelson, M. E., Humphrey, S. J., & James, D. E. (2023) · eLife · doi:10.7554/elife.89212 · Cited by 17
Self-citationAMPK regulates the maintenance and remodelling of the neuromuscular junction
Ng, S. Y., Mikhail, A. I., Mattina, S. R., Mohammed, S. A., Khan, S., Desjardins, E. M., Lim, C., Phillips, S. M., Steinberg, G. R., & Ljubicic, V. (2024) · Molecular Metabolism · doi:10.1016/j.molmet.2024.102066 · Cited by 13
Hoffman, N. J., Whitfield, J., Xiao, D., Radford, B. E., Suni, V., Blazev, R., Yang, P., Parker, B. L., & Hawley, J. A. (2025) · Sports Medicine · doi:10.1007/s40279-025-02217-2 · Cited by 13
Self-citationHe, Y., Qiu, R., Wu, B., Gui, W., Lin, X., Li, H., & Zheng, F. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00495.2020 · Cited by 14
Vepkhvadze, T. F., Vorotnikov, A. V., & Popov, D. V. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921050084 · Cited by 12
Teich, T., & Riddell, M. C. (2016) · Endocrinology · doi:10.1210/en.2016-1453 · Cited by 16
Qi, Y. A., Zhang, X., Seyoum, B., Msallaty, Z., Mallisho, A., Caruso, M. A., Damacharla, D., Ma, D., Al-Janabi, W., Tagett, R., et al. (2019) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgz115 · Cited by 12
Li, S., Dong, S., Xu, Q., Shi, B., Li, L., Zhang, W., Zhu, J., Cheng, Y., Zhang, G., & Zhong, M. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.837798 · Cited by 13
Skeletal muscle proteomics: considerations and opportunities
Wong, J. P. H., Ng, Y., Larsen, J. K., Blazev, R., Deshmukh, A. S., & Parker, B. L. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00073-2 · Cited by 18
Self-citationCellular Feimin enhances exercise performance by suppressing muscle thermogenesis
Peng, Y. C., Jia, L., Xiao, H., Shi, X., Fang, X., Qiu, Y., Gan, Z., & Wang, Y. (2025) · Nature Metabolism · doi:10.1038/s42255-024-01176-8 · Cited by 12
The Role of Myokines in Liver Diseases
Nishikawa, H., Kim, S. K., & Asai, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031043 · Cited by 12
Multifaceted role of SMCR8 as autophagy regulator
Jung, J., & Behrends, C. (2017) · Small GTPases · doi:10.1080/21541248.2017.1346553 · Cited by 13
Xu, N., Meng, H., Liu, T., Feng, Y., Qi, Y., Zhang, D.-H., & Wang, H. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.122 · Cited by 12
Zhang, S., Wang, C., Qin, S., Chen, C., Bao, Y., Zhang, Y., Xu, L., Liu, Q., Zhao, Y., Li, K., et al. (2024) · Genome Research · doi:10.1101/gr.278344.123 · Cited by 13
Di, Y., Li, W., Šalovská, B., Ba, Q., Hu, Z., Wang, S., & Liu, Y. (2023) · Biophysics Reports · doi:10.52601/bpr.2023.230007 · Cited by 11
Research trends and hotspots of exercise for people with sarcopenic: A bibliometric analysis
Zang, W., Chen, H., Yan, J. H., Li, D., Xiao, N., Zheng, X., & Zhang, Z. (2023) · Medicine · doi:10.1097/md.0000000000035148 · Cited by 12
Kjærgaard, J., Lindqvist, C. B., Quesada, J. P., Jessen, S., Schlabs, F., Ehrlich, A. M., Yonamine, C. Y., García-Ureña, M., Schmalbruch, J. H., Small, L., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102163 · Cited by 11
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112933 · Cited by 12
Autophagy and Exercise: Current Insights and Future Research Directions
Botella, J., Shaw, C. S., & Bishop, D. J. (2023) · International Journal of Sports Medicine · doi:10.1055/a-2153-9258 · Cited by 12
Glyoxalase I is a novel target for the prevention of metabolic derangement
Miranda, E. R., & Haus, J. M. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108524 · Cited by 11
Molecular Mechanisms Mediating Adaptation to Exercise
Gholamnezhad, Z., Mégarbane, B., & Rezaee, R. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1792-1_3 · Cited by 12
Molecular studies of exercise, skeletal muscle, and ageing
Timmons, J. A., & Gallagher, I. J. (2016) · F1000Research · doi:10.12688/f1000research.8255.1 · Cited by 11
Exercise, Epigenetics, and Body Composition: Molecular Connections
Williams, A., Wadsworth, D. D., & Geetha, T. (2025) · Cells · doi:10.3390/cells14191553 · Cited by 13
Molina‐López, J., Quispe-Ricalde, M. A., Hernández, B. V., Planells, A., Otero, R., & Planells, E. (2020) · PLoS ONE · doi:10.1371/journal.pone.0232237 · Cited by 10
Nrf2 modulates the benefits of evening exercise in type 2 diabetes
Fasipe, B., & Laher, I. (2023) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2023.09.001 · Cited by 11
Single-Cell Transcriptomics Identifies Pituitary Gland Changes in Diet-Induced Obesity in Male Mice
Ruggiero-Ruff, R. E., Le, B. H., Villa, P. A., Lainez, N. M., Athul, S. W., Das, P., Ellsworth, B. S., & Coss, D. (2023) · Endocrinology · doi:10.1210/endocr/bqad196 · Cited by 8
Gross, S. M., & Lehman, S. L. (2016) · Physiological Genomics · doi:10.1152/physiolgenomics.00112.2015 · Cited by 10
Alterations of Lysine Acetylation Profile in Murine Skeletal Muscles Upon Exercise
Liang, D., Chen, C., Huang, S. M., Liu, S., Fu, L., & Niu, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.859313 · Cited by 10
Akberdin, I. R., Kiselev, I. N., Pintus, S. S., Sharipov, R. N., Vertyshev, A. Y., Vinogradova, O. L., Popov, D. V., & Kolpakov, F. A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.31.446385 · Cited by 9
The mitochondrial multi-omic response to exercise training across tissuesPreprint
Amar, D., Gay, N. R., Jimenez‐Morales, D., Beltran, P. M. J., Ramaker, M. E., Raja, A. N., Zhao, B., Sun, Y., Marwaha, S., Gaul, D. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.13.523698 · Cited by 10
Metabolic Flexibility and Mechanical Efficiency in Women Over-60
Blasco-Lafarga, C., Monferrer-Marín, J., Roldán, A., Monteagudo, P., & Chulvi‐Medrano, I. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.869534 · Cited by 9
Achter, J. S., Torres-Vega, E., Sorrentino, A., Kahnert, K., Galsgaard, K. D., Hernández-Varas, P., Wierer, M., Holst, J. J., Wojtaszewski, J. F. P., Mills, R. W., et al. (2024) · Cardiovascular Diabetology · doi:10.1186/s12933-024-02338-4 · Cited by 9
Self-citationZhang, X., Liao, S., Huang, L., & Wang, J. (2024) · Advanced Biology · doi:10.1002/adbi.202400235 · Cited by 11
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Møller, L. L. V., Raun, S. H., Fritzen, A. M., & Sylow, L. (2022) · Journal of Biological Methods · doi:10.14440/jbm.2022.385 · Cited by 9
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Metadata
- Authors
- Hoffman, N. J., Parker, B. L., Chaudhuri, R., Fisher-Wellman, K. H., Kleinert, M., Humphrey, S. J., Yang, P., Holliday, M., Trefely, S., Fazakerley, D. J., Stöckli, J., Burchfield, J. G., Jensen, T. E., Jothi, R., Kiens, B., Wojtaszewski, J. F. P., Richter, E. A., & James, D. E.
- Affiliations
- The University of Sydney (AU)
- University of Copenhagen (DK)
- Garvan Institute of Medical Research (AU)
- National Institutes of Health (US)
- Corresponding author
- James, David E.
- ORCID
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 22
- Issue
- 5
- Pages
- 922-935
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4635038
- OpenAlex
- W1839260472
- Cited by
- 426
- References
- 50
- Citations by year
- 2026: 27 · 2025: 38 · 2024: 45 · 2023: 37 · 2022: 47 · 2021: 46 · 2020: 45 · 2019: 50 · 2018: 32 · 2017: 30 · 2016: 25 · 2015: 4
- FWCI
- 13.18
- Type
- journal article
- Language
- en
- Update notices
- erratum (2015-11-03)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- PubMed Central (acceptedVersion)
- Research Bank (Australian Catholic University) (submittedVersion)
- Funders
- Novo Nordisk Fonden (NNF15OC0015182, NNF14OC0012009, NNF14OC0012319)
- National Institutes of Health
- National Institute of Environmental Health Sciences (ZIAES102625)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
- Keywords
- skeletal muscle, protein phosphorylation, AKAP1, mitochondrial respiration, high-intensity exercise, phosphosites, kinase substrates, energy metabolism, insulin sensitivity, phosphoproteomics
- MeSH terms
- Machine Learning, Adult, Energy Metabolism, Humans, Male, Mitochondria, Phosphoproteins, Phosphorylation, Physical Conditioning, Animal, Substrate Specificity, Signal Transduction, Exercise, Muscle, Skeletal, A Kinase Anchor Proteins, AMP-Activated Protein Kinases
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