The DOI matches its Crossref record; 49 of the 50 references it cites were found in a registry or an index.
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.
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 check wasn’t confident either way, so it gives no verdict — never disputed.
In the citing paper
“Moreover, the phosphorylation of human BAG3 on Thr285 and Ser 289 decreases in response to endurance exercise (61).”
From The Hippo signal transduction network for exercise physiologists (2016) · cites this paper as [61]
Experimental — accuracy not yet measured
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
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
Sorted by citations
Items 301–400 of 426
Feng, H., Tian, C., Jiang, W., Sun, Z., Li, Y., Han, B., Chen, L., Wang, D., Xiang, H., Zhu, J., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.140240 · Cited by 8
The role of physical activity and epigenetic changes in colorectal cancer prevention
Sun, Y., Keat, O. B., & Rajabi, S. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03872-1 · Cited by 7
Chuang, S.-J., Johanns, M., Ruys, S. P. D., Steinberg, G. R., Kemp, B. E., Viollet, B., & Rider, M. H. (2021) · Biochemical Journal · doi:10.1042/bcj20210411 · Cited by 8
Activation of the 26S Proteasome to Reduce Proteotoxic Stress and Improve the Efficacy of PROTACs
Sedláček, J. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.4c00408 · Cited by 6
Liu, Z., Yang, Y., Song, L., Ruan, X., Li, X., He, Y., Zou, Y., Ding, S., & Sun, Y. (2025) · Journal of Innate Immunity · doi:10.1159/000548603 · Cited by 6
Ramos‐Jiménez, A., Rubio-Valles, M., Arvizuo, J. G., Juárez-Oropeza, M. A., Ramos-Hernández, J. A., Chávez-Guevara, I. A., González-Rodríguez, E., Moreno-Brito, V., & Torres, R. P. H. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27083475 · Cited by 6
Lee, T. J., Sasaki, Y., Ruzycki, P. A., Ban, N., Lin, J. B., Wu, H.-T., Santeford, A. C., & Apte, R. S. (2024) · JCI Insight · doi:10.1172/jci.insight.173707 · Cited by 6
Hawley, J. A., & Krook, A. (2015) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2015.201 · Cited by 6
Czarna, M., Heidorn, H., Fernando, S., Sanislav, O., Jarmuszkiewicz, W., Mutzel, R., & Fisher, P. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111675 · Cited by 7
Welch, N., Singh, S. S., Musich, R. J., Mansuri, M. S., Bellar, A., Mishra, S., Chelluboyina, A. K., Sekar, J., Attaway, A. H., Li, L., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105325 · Cited by 6
Zhang, K., Xie, N., Ye, H., Miao, J., Xia, B., Yu, Y., Peng, H., Xu, S. B., Wu, T., Tao, C., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108590 · Cited by 6
Cross-Species PTM Mapping from Phosphoproteomic Data
Chaudhuri, R., & Yang, J. Y. H. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-6783-4_22 · Cited by 6
Self-citationDetecting Modifications in Proteomics Experiments with Param-Medic
May, D., Tamura, K., & Noble, W. S. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00954 · Cited by 6
Physiological State Dictates the Proteasomal-Mediated Purging of Misfolded Protein Fragments
Eldeeb, M. A., Ragheb, M. A., Esmaili, M., & Hussein, F. (2019) · Protein and Peptide Letters · doi:10.2174/0929866526666191026111951 · Cited by 6
CDK4, a new metabolic sensor that antagonizes AMPK
Fajas, L., & López‐Mejía, I. C. (2017) · Molecular & Cellular Oncology · doi:10.1080/23723556.2017.1409862 · Cited by 7
Regulation of Kir2.1 Function Under Shear Stress and Cholesterol Loading
Le, N., & Abe, J. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.118.008749 · Cited by 6
Exerkines: Benign adaptation for exercise and benefits for non-alcoholic fatty liver disease
Chen, Y., Zhang, Y., Jin, X., Hong, S., & Tian, H. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150305 · Cited by 5
Zhang, C., Gao, S., Han, W., Wu, J., Huang, Z., Zhang, X., Wu, Y., Li, S., Shi, M., Gao, B., et al. (2025) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2025.08.005 · Cited by 5
Exercise Modulates Exocytosis: Chemical Insights from the Intracellular Vesicle Perspective
Liu, R., He, X., Liu, J., Sun, Z., Yu, P., Hou, L., & Mao, L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202511277 · Cited by 6
Li, J., Madsen, A. B., Knudsen, J. R., Henríquez‐Olguín, C., Persson, K. W., Li, Z., Raun, S. H., Li, T., Kiens, B., Wojtaszewski, J. F. P., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202402064r · Cited by 6
Self-citationSILAC kinase screen identifies potential MASTL substrates
Marzec, K. A., Rogers, S., McCloy, R. A., Parker, B. L., James, D. E., Watkins, D. N., & Burgess, A. (2022) · Scientific Reports · doi:10.1038/s41598-022-14933-0 · Cited by 6
Self-citationCandra, A., Fahrimal, Y., Yusni, Y., Azwar, A., & Santi, T. D. (2024) · Narra J · doi:10.52225/narra.v4i1.321 · Cited by 5
Kokot, T., Zimmermann, J. P., Schwäble, A. N., Reimann, L., Herr, A., Höfflin, N., Köhn, M., & Warscheid, B. (2024) · Scientific Reports · doi:10.1038/s41598-024-78953-8 · Cited by 5
Biased Duplications and Loss of Members in Tdrd Family in Teleost Fish
Chen, F., Luo, M., Lai, F., Yu, C., Cheng, H., & Zhou, R. (2017) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.22757 · Cited by 5
Nagy, T., Kátai, E., Fisi, V., Takács, T. T., Stréda, A., Wittmann, I., & Miseta, A. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00970 · Cited by 5
Raun, S. H., Pham, T. C. P., Viggars, M. R., Ato, S., Takagaki, Y., Yan, Z., Bock, K. D., Hornberger, T. A., Richter, E. A., Auwerx, J. H., et al. (2026) · Cell Metabolism · doi:10.1016/j.cmet.2026.03.005 · Cited by 5
Self-citationLuk, H., Levitt, D. E., Appell, C. R., & Jiwan, N. C. (2025) · Physiological Reports · doi:10.14814/phy2.70291 · Cited by 4
Systems modeling and uncertainty quantification of AMP-activated protein kinase signaling
Linden-Santangeli, N. J., Zhang, J., Krämer, B., & Rangamani, P. (2025) · npj Systems Biology and Applications · doi:10.1038/s41540-025-00588-w · Cited by 4
Links between Exercise Capacity, Exercise Training, and Metabolism
Spagnolo, A., Klug, S., Schenkl, C., & Schwarzer, M. (2023) · Comprehensive physiology · doi:10.1002/j.2040-4603.2023.tb00283.x · Cited by 4
The exercise pill: should we replace exercise with pharmaceutical means?
Loland, S. (2017) · Sport Ethics and Philosophy · doi:10.1080/17511321.2016.1272132 · Cited by 4
Enzymatic Phosphorylation of Oxidized Tyrosine Residues
Heininen, J., Erbacher, C., Kotiaho, T., Kostiainen, R. K., & Teppo, J. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00061 · Cited by 4
Antoni, C., Boqué, N., Nuria, C., Herrero, P., Jordi, M.-P., Arola, L., & Puiggròs, F. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816193-7.00019-1 · Cited by 4
Kido, K., Hingst, J. R., Onslev, J., Sjøberg, K. A., Birk, J. B., Eskesen, N. O., Zhou, T., Kawanaka, K., Havelund, J. F., Færgeman, N. J., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci183567 · Cited by 4
Self-citationExtracellular mitochondria: a potential player involved in exercise health benefits
Pedrosa, M. B., Santos, L. L., Ferreira, R. M. S., & Magalhães, J. S. (2025) · Biochimie · doi:10.1016/j.biochi.2025.12.011 · Cited by 4
Role of mitochondrial dysfunction in muscle wasting in cancer cachexia: a narrative review
Su, X., Wang, S., Qu, Y., Wang, Y., Tian, Z., Chao, X., Li, Z., & Ma, D. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-07906-8 · Cited by 7
Hidouri, S., Driss, T., Tagougui, S., Kammoun, N., Chtourou, H., & Hammouda, O. (2024) · Sensors · doi:10.3390/s24030909 · Cited by 5
Identification of phosphatases that dephosphorylate the co-chaperone BAG3
Kokot, T., Zimmermann, J. P., Chand, Y., Krier, F., Reimann, L., Scheinost, L., Höfflin, N., Esch, A., Höhfeld, J., Warscheid, B., et al. (2024) · Life Science Alliance · doi:10.26508/lsa.202402734 · Cited by 3
Fernandez-Vivero, D., Terrados, N., Pinto-Hernández, P., Noguero‐Lopez, C., Fernández‐Garcia, B., Whitham, M., Iglesias‐Gutiérrez, E., & Fernández‐Sanjurjo, M. (2025) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.70092 · Cited by 3
Scheffler, T. L., & Gerrard, D. E. (2016) · Journal of Animal Science · doi:10.2527/jas.2015-0055 · Cited by 3
Gouvêa, A. L., da Silva, M. G., Braga, B. C., Martinez, C. G., Lauthartte, L. C., Bastos, W. R., & Kurtenbach, E. (2021) · JCSM Clinical Reports · doi:10.1002/crt2.34 · Cited by 3
Kulkarni, P. P. (2022) · Chronicle of Diabetes Research and Practice · doi:10.4103/cdrp.cdrp_5_21 · Cited by 3
Active regulation mechanisms of LLPS and MLOs biogenesis
Fernández-Álvarez, A. J., Thomas, M. G., Giudice, J., & Boccaccio, G. L. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00005-1 · Cited by 3
Fast and slow skeletal myosin binding protein-C and aging
Perazza, L. R., Wei, G., & Thompson, L. V. (2022) · GeroScience · doi:10.1007/s11357-022-00689-y · Cited by 3
Solem, K., Clauss, M., & Jensen, J. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1620943 · Cited by 5
Ampk alpha2 T172 activation dictates exercise performance and energy transduction in skeletal muscle
Montalvo, R. N., Li, X., Many, G. M., Sagendorf, T. J., Yu, Q., Shen, W., Wase, N. V., Burgardt, A. R., Zhang, T., Gritsenko, M., et al. (2026) · Science Advances · doi:10.1126/sciadv.aeb3338 · Cited by 5
Metformin suppresses β-cell apoptosis under ER stress by inhibiting protein translation
Inoue, R., Tajima, K., Okuyama, T., Sakai, C., Kanno, T., Zou, M., Kyohara, M., Matsunaga, K., Tsuno, T., Luo, J., et al. (2026) · Metabolism · doi:10.1016/j.metabol.2026.156607 · Cited by 2
AMPK: a master regulator of mitochondrial quality and quantity
Shaw, R. J., Ganley, I. G., Prudent, J., & Hardie, D. G. (2026) · Trends in Cell Biology · doi:10.1016/j.tcb.2026.04.008 · Cited by 2
Effect of an endothelial regulatory module on plasma proteomics in exercising horses
Roudbar, M. A., Rosengren, M., Mousavi, S. F., Fegraeus, K., Naboulsi, R., Meadows, J. R. S., & Lindgren, G. (2024) · Comparative Biochemistry and Physiology Part D Genomics and Proteomics · doi:10.1016/j.cbd.2024.101265 · Cited by 2
Takahashi, Y., Matsumoto, T., Wang, W., Inaba, T., Terada, S., & Hatta, H. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00311.2025 · Cited by 3
Stead, C. A., Thomas, A. C. Q., Nishimura, Y., Abbasi, M., Barrett, J., & Burniston, J. G. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-88361-3_7 · Cited by 2
Solfest, J. S., Nie, Y., Weiss, J. A., Garner, R. T., Kuang, S., Stout, J., & Gavin, T. P. (2019) · Sport Sciences for Health · doi:10.1007/s11332-019-00547-z · Cited by 2
Skeletal muscle glycogen synthesis – it turns out we still know very little
Mackenzie, R. (2020) · The Journal of Physiology · doi:10.1113/jp280759 · Cited by 2
How mass spectrometry can be exploited to study AMPK
Rider, M. H., Vertommen, D., & Johanns, M. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240009 · Cited by 2
dos Santos, J. A. R. (2021) · Retos · doi:10.47197/retos.v42i0.87563 · Cited by 2
Kuhnen, G., Russomanno, T. G., Murgia, M., Pillon, N. J., Schönfelder, M., & Wackerhage, H. (2022) · Research Square · doi:10.21203/rs.3.rs-1519277/v1 · Cited by 2
The genetic and dietary landscape of the muscle insulin signalling networkPreprint
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) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.21.546001 · Cited by 2
Self-citationHan, B., Li, G. X., Liew, W. L., Chan, E., Huang, S., Khoo, C. M., Leow, M. K., Lee, Y. S., Zhao, T., Wang, L. C., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.30.547176 · Cited by 2
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. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.05.574393 · Cited by 2
Jayavelu, A. K., Liu, J. J., Schriever, S. C., Pfluger, P. T., Schwarzer, C., Krahmer, N., & Mann, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.29.620939 · Cited by 1
Exercise Mimetics: Fact Or Fantasy?
Lakshmi, G., & Sridhar, G. R. (2021) · Adipobiology · doi:10.14748/adipo.v11.8559 · Cited by 1
Ahmadi, A., Kashef, M., Rajabi, H., & Salehpour, M. (2023) · Archives of Sports Medicine and Physiotherapy · doi:10.17352/asmp.000018 · Cited by 1
Exercise Modulates Exocytosis: Chemical Insights from the Intracellular Vesicle Perspective
Liu, R., He, X., Liu, J., Sun, Z., Yu, P., Hou, L., & Mao, L. (2025) · Angewandte Chemie · doi:10.1002/ange.202511277 · Cited by 1
Takahashi, K., Mukai, K., Takahashi, Y., Ebisuda, Y., Sugiyama, F., Hatta, H., & Kitaoka, Y. (2025) · Journal of Experimental Biology · doi:10.1242/jeb.250956 · Cited by 1
Bridging the gap: multi-omic insights into exercise responses in postmenopausal women
Aiyanna, R. K., Wang, S., Grolaux, R., Reisman, E. G., Jones, B., & Eynon, N. (2026) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00172.2026 · Cited by 1
The Role of Omics Approaches in Muscle Research
Schiaffino, S., Reggiani, C., & Murgia, M. (2019) · Springer eBooks · doi:10.1007/978-1-4939-9802-9_1 · Cited by 1
Skeletal Muscle Protein Metabolism During Exercise
Joanisse, S., McKendry, J., Nunes, E. A., Thomas, A. C. Q., & Phillips, S. M. (2022) · Physiology in health and disease · doi:10.1007/978-3-030-94305-9_9 · Cited by 2
Overview of Exercise Metabolism
Hargreaves, M. (2022) · Physiology in health and disease · doi:10.1007/978-3-030-94305-9_2 · Cited by 1
Brenmoehl, J., Meyer, Z., Walz, C., Ohde, D., & Hoeflich, A. (2024) · Cells · doi:10.3390/cells13242123 · Cited by 1
SARIALİOĞLU, N. (2025) · Turkish Journal of Kinesiology · doi:10.31459/turkjkin.1666684 · Cited by 1
Role of the Glucocorticoid Receptor in Systemic Energy Metabolism
Tanaka, H., Yoshikawa, N., Yamazaki, H., Uehara, M., & Oda, A. (2018) · Nihon Naika Gakkai Zasshi · doi:10.2169/naika.107.1373 · Cited by 1
Mass spectrometry for human kinome analysis
Miao, W., & Wang, Y. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821433-6.00001-5 · Cited by 1
Liu, Z., Yang, Y., Song, L., Ruan, X., He, Y., Zou, Y., Ding, S., & Sun, Y. (2024) · Research Square · doi:10.21203/rs.3.rs-3965620/v1 · Cited by 1
Exercise modulation of the alternative splicing landscape in human tissuesPreprint
Zhang, Z., Nudelman, G., Pinças, H., Iyer, G. R., Smith, G. R., Keshishian, H., Jin, C. A., Trappe, S. W., Katz, D. H., Burant, C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.03.704460 · Cited by 1
Mitogen-Activated Protein Kinase-Dependent Fiber-Type Regulation in Skeletal MusclePreprint
Boyer, J. G., Song, T., Lee, D., Fu, X., Sadayappan, S., & Molkentin, J. D. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/361600
Dechandt, C. R. P. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.17.2018.tde-13092018-104230
Invited talk: Mapping complex molecular networks underlying exercise using global phosphoproteomics
Hoffman, N. J., Parker, B. L., Chaudhuri, R., & James, D. E. (2019) · Obesity Research & Clinical Practice · doi:10.1016/j.orcp.2016.10.071
Self-citationRodríguez-Silva, M., Ashourian, K., Smith, A. D., & Chambers, J. W. (2019) · Neuromethods · doi:10.1007/978-1-4939-9228-7_6
From brain to muscle and back : novel approaches to harness the benefits of exercise
Kelahmetoglu, Y. (2020) · Figshare
Combat COVID-19 with Exercise and Vitamin D Supplementation
Mishra, A. K., & Murrell, W. (2021) · Biologic Orthopedics Journal · doi:10.22374/boj.v3i1.15
Vepkhvadze, T. F., Vorotnikov, A. V., & Popov, D. V. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521050080
Liang, D., Chen, C., Huang, S. M., Liu, S., Fu, L., & Niu, Y. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3974358
In Cellulo Kinase Screen Identifies Potential MASTL SubstratesPreprint
Marzec, K. A., Rogers, S., McCloy, R. A., Parker, B. L., James, D. E., Watkins, D. N., & Burgess, A. (2022) · Research Square · doi:10.21203/rs.3.rs-1503557/v1
Self-citationPhillips, S. M. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727649711.793571158
Exercise preserves fitness capacity during aging through AMPK and mitochondrial dynamicsPreprint
Campos, J. C., Bozi, L. H. M., Traa, A., van der Bliek, A. M., Raamsdonk, J. M. V., Blackwell, T. K., & Ferreira, J. C. B. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.20.496837
Exercise: Thermodynamic and Bioenergetic Principles
Halling, J. F., Gudiksen, A., Pilegaard, H., & Neufer, P. D. (2022) · Physiology in health and disease · doi:10.1007/978-3-030-94305-9_3 · Cited by 2
Pantothenate Kinase 4 controls efficient skeletal muscle energy substrate metabolism via acetyl-CoAPreprint
Miranda‐Cervantes, A., Fritzen, A. M., Raun, S. H., Hodek, O., Møller, L. L. V., Johann, K., Deisen, L., Gregorevic, P., Gudiksen, A., Artati, A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.14.551603
Self-citationRaun, S. H. (2024) · Nature Reviews Endocrinology · doi:10.1038/s41574-023-00944-y
The genetic and dietary landscape of the muscle insulin signalling networkPreprint
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. (2024) · eLife · doi:10.7554/elife.89212.2
Self-citationXu, M., Liu, Y.-Y., Liu, C.-Y., Xue, Z., Chen, J.-B., Liu, Y.-F., & Chen, J.-X. (2024) · Pharmacological Research - Modern Chinese Medicine · doi:10.1016/j.prmcm.2024.100398
Muscle Biopsy Sample Preparation and Proteomics Analysis Based on UHPLC-MS/MS
Du, J., Hou, J., Yun, H., & Song, Y. (2024) · BIO-PROTOCOL · doi:10.21769/bioprotoc.5137
Lee, C.-M. J., Nguyen, J., Pope, B., Imami, A. S., Ryan, V. W. G., Sahay, S., Mathis, V., Pulvender, P., Eby, H., Arvay, T. O., et al. (2025) · PLoS ONE · doi:10.1371/journal.pone.0321596
McColl, T. J., Zhang, R., Dugourd, A. J. F., Sáez-Rodríguez, J., & Clarke, D. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.11.681841
Schlabs, F. L., Larsen, J. K., Kruse, R., Deshmukh, A. S., & See, P. D. F. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5847954
Achter, J. S., Vega, E. T., 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) · Figshare · doi:10.6084/m9.figshare.26751152
Self-citationAchter, J. S., Vega, E. T., 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) · Figshare · doi:10.6084/m9.figshare.26751137
Self-citationAchter, J. S., Vega, E. T., 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) · Figshare · doi:10.6084/m9.figshare.26751140
Self-citationAchter, J. S., Vega, E. T., 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) · Figshare · doi:10.6084/m9.figshare.26751158
Self-citationLi, Z., Peng, L., Sun, L., & Si, J. (2023) · Figshare · doi:10.6084/m9.figshare.26612288
Trewin, A. J., Silver, J. L., Dillon, H. T., Gatta, P. A. D., Parker, L., Hiam, D., Lee, Y. P., Richardson, M. F., (13072152), G. W., & Lamon, S. (2022) · Figshare · doi:10.6084/m9.figshare.20336770
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
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