Cited by 152Muscle metabolism and nutritionMuscle Physiology and DisordersCardiovascular and exercise physiology

The DOI matches its Crossref record; 103 of the 103 references it cites were found in a registry or an index.

Assessing the role of muscle protein breakdown in response to nutrition and exercise in humans.

Open access

Tipton, Kevin D., Hamilton, D. Lee, Gallagher, Iain J.·2018·Sports Medicine

DOI 10.1007/s40279-017-0845-5PMC PMC5790854

Open this paper in CoChat — free account Open PDF

Abstract

Muscle protein breakdown (MPB) is an important metabolic component of muscle remodeling, adaptation to training, and increasing muscle mass. Degradation of muscle proteins occurs via the integration of three main systems-autophagy and the calpain and ubiquitin-proteasome systems. These systems do not operate independently, and the regulation is complex. Complete degradation of a protein requires some combination of the systems. Determination of MPB in humans is technically challenging, leading to a relative dearth of information. Available information on the dynamic response of MPB primarily comes from stable isotopic methods with expression and activity measures providing complementary information. It seems clear that resistance exercise increases MPB, but not as much as the increase in muscle protein synthesis. Both hyperaminoacidemia and hyperinsulinemia inhibit the post-exercise response of MPB. Available data do not allow a comprehensive examination of the mechanisms behind these responses. Practical nutrition recommendations for interventions to suppress MPB following exercise are often made. However, it is likely that some degree of increased MPB following exercise is an important component for optimal remodeling. At this time, it is not possible to determine the impact of nutrition on any individual muscle protein. Thus, until we can develop and employ better methods to elucidate the role of MPB following exercise and the response to nutrition, recommendations to optimize post exercise nutrition should focus on the response of muscle protein synthesis. The aim of this review is to provide a comprehensive examination of the state of knowledge, including methodological considerations, of the response of MPB to exercise and nutrition in humans.

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

Crossref · 10.1007/s40279-017-0845-5

Cites

103 of 103 references verified0 citation errors · 0 not checkable

Statistics

Fig. 1 Methods of assessing skeletal muscle protein breakdown (MPB). Skeletal muscle proteins are broken down by a combination of the three main protein breakdown systems. These breakdown systems do not work in isolation but rather work together to remodel skeletal muscle. (1) The calpain proteases disassemble myofibrils into smaller component parts, (2) the ubiquitin-proteasome system degrades these component into individual amino acids, and can label proteins (membrane receptors, channels and transporters) for destruction by the third system, (3) the autophagy-lysosome system, which predominantly breaks down membrane based proteins. Dynamic MPB measures use labelled amino-acid tracers (such as phenylalanine stable-isotopes) and provide a dynamic view of whole MPB. 3-Methylhistidine is a unique metabolite of myofibrillar protein breakdown and its appearance in blood and urine can be assumed to have come from the processes of myofibrillar protein breakdown. Skeletal muscle is the body’s largest depot of myofibrillar protein so changes in plasma/urinary/interstitial 3-methylhistidine are believed reflective of skeletal MPB. Other static markers of protein breakdown include the assessment of the messenger RNA (mRNA)/protein expression/activity/localization of components of the breakdown machinery. Markers are available to estimate changes in the activity of each of the three breakdown systems. L-Phe l-phenylalanine, AV arterio-venous, MuRF muscle ring finger protein, FKHR forkhead transcription factorCC BY · PubMed Central

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Gene Ontology: tool for the unification of biology
Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D., Butler, H., Cherry, J. M., Davis, A. P., Dolinski, K., Dwight, S. S., Eppig, J. T., et al. (2000) · Nature Genetics · doi:10.1038/75556 · Cited by 43,206
Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A., & Speleman, F. (2002) · Genome Biology · doi:10.1186/gb-2002-3-7-research0034 · Cited by 20,038
The MIQE guidelines: minimum information for publication of quantitative real-time PCR experiments
Bustin, S. A., Benes, V., Garson, J. A., Hellemans, J., Huggett, J., Kubista, M., Mueller, R., Nolan, T., Pfaffl, M. W., Shipley, G. L., et al. (2009) · Clinical Chemistry · doi:10.1373/clinchem.2008.112797 · Cited by 16,303 · cited 1×
“reporting of qRT-PCR studies were published [65].”
Sequencing technologies – the next generation
Metzker, M. L. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2626 · Cited by 7,066
Determination of stable housekeeping genes, differentially regulated target genes and sample integrity: BestKeeper – Excel-based tool using pair-wise correlations
Pfaffl, M. W., Tichopad, A., Prgomet, C., & Neuvians, T. P. (2004) · Biotechnology Letters · doi:10.1023/b:bile.0000019559.84305.47 · Cited by 5,065
Identification of ubiquitin ligases required for skeletal muscle atrophy.
Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521
Real-time RT-PCR normalisation; strategies and considerations
Huggett, J. F., Dheda, K. U. J., Bustin, S. A., & Zumla, A. I. (2005) · Genes and Immunity · doi:10.1038/sj.gene.6364190 · Cited by 1,858
Reactome: a database of reactions, pathways and biological processes
Croft, D., O'Kelly, G., Wu, G., Haw, R., Gillespie, M., Matthews, L., Caudy, M., Garapati, P., Gopinath, G., Jassal, B., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1018 · Cited by 1,751
The underappreciated role of muscle in health and disease
Wolfe, R. R. (2006) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/84.3.475 · Cited by 1,641
Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
Lecker, S. H., Jagoe, R. T., Gilbert, A., Gomes, M., Baracos, V., Bailey, J., Price, S. R., Mitch, W. E., & Goldberg, A. L. (2004) · The FASEB Journal · doi:10.1096/fj.03-0610com · Cited by 1,539

Show all 103 references

Sorted by citations

Skeletal muscle atrophy: From mechanisms to treatments
Yin, L., Li, N., Jia, W., Wang, N., Liang, M., Yang, X., & Du, G. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105807 · Cited by 423
Stimuli and sensors that initiate skeletal muscle hypertrophy following resistance exercise
Wackerhage, H., Schoenfeld, B. J., Hamilton, D. L., Lehti, M., & Hulmi, J. J. (2019) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00685.2018 · Cited by 357
Self-citation
Metabolite Concentration Changes in Humans After a Bout of Exercise: a Systematic Review of Exercise Metabolomics Studies
Schranner, D., Kastenmüller, G., Schönfelder, M., Römisch‐Margl, W., & Wackerhage, H. (2020) · Sports Medicine - Open · doi:10.1186/s40798-020-0238-4 · Cited by 263
Mechanisms of mechanical overload-induced skeletal muscle hypertrophy: current understanding and future directions
Roberts, M. D., McCarthy, J. J., Hornberger, T. A., Phillips, S. M., Mackey, A. L., Nader, G. A., Boppart, M. D., Kavazis, A. N., Reidy, P. T., Ogasawara, R., et al. (2023) · Physiological Reviews · doi:10.1152/physrev.00039.2022 · Cited by 214
Antioxidant and Adaptative Response Mediated by Nrf2 during Physical Exercise
Vargas-Mendoza, N., Morales‐González, Á., Madrigal‐Santillán, E., Madrigal‐Bujaidar, E., Álvarez‐González, I., García-Melo, L. F., Anguiano‐Robledo, L., Fregoso-Aguilar, T. A., & Morales‐González, J. A. (2019) · Antioxidants · doi:10.3390/antiox8060196 · Cited by 170
Impact of nutrition on skin wound healing and aesthetic outcomes: A comprehensive narrative review
Seth, I., Lim, B., Cevik, J., Gracias, D., Chua, M., Kenney, P. S., Rozen, W. M., & Cuomo, R. (2024) · JPRAS Open · doi:10.1016/j.jpra.2024.01.006 · Cited by 115
Potential Therapeutic Strategies for Skeletal Muscle Atrophy
Huang, L. T., Li, M., Deng, C., Qiu, J., Wang, K., Chang, M., Zhou, S., Gu, Y., Shen, Y., Wang, W., et al. (2022) · Antioxidants · doi:10.3390/antiox12010044 · Cited by 119
Physiological Differences Between Low Versus High Skeletal Muscle Hypertrophic Responders to Resistance Exercise Training: Current Perspectives and Future Research Directions
Roberts, M. D., Haun, C. T., Mobley, C. B., Mumford, P. W., Romero, M. A., Roberson, P. A., Vann, C. G., & McCarthy, J. J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00834 · Cited by 107
The effects of branched-chain amino acids on muscle protein synthesis, muscle protein breakdown and associated molecular signalling responses in humans: an update
Kaspy, M. S., Hannaian, S. J., Bell, Z. W., & Churchward‐Venne, T. A. (2023) · Nutrition Research Reviews · doi:10.1017/s0954422423000197 · Cited by 117
Mechanisms Linking the Gut-Muscle Axis With Muscle Protein Metabolism and Anabolic Resistance: Implications for Older Adults at Risk of Sarcopenia
Prokopidis, K., Chambers, E. S., Lochlainn, M. N., & Witard, O. C. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.770455 · Cited by 115
Age-related muscle anabolic resistance: inevitable or preventable?
Aragon, A. A., Tipton, K. D., & Schoenfeld, B. J. (2022) · Nutrition Reviews · doi:10.1093/nutrit/nuac062 · Cited by 102
Self-citation
Muscle Protein Synthesis and Whole-Body Protein Turnover Responses to Ingesting Essential Amino Acids, Intact Protein, and Protein-Containing Mixed Meals with Considerations for Energy Deficit
Gwin, J. A., Church, D. D., Wolfe, R. R., Ferrando, A. A., & Pasiakos, S. M. (2020) · Nutrients · doi:10.3390/nu12082457 · Cited by 93
The role of intermittent fasting and meal timing in weight management and metabolic health
Templeman, I., Gonzalez, J. T., Thompson, D., & Betts, J. A. (2019) · Proceedings of The Nutrition Society · doi:10.1017/s0029665119000636 · Cited by 95
Testosterone therapy induces molecular programming augmenting physiological adaptations to resistance exercise in older men
Gharahdaghi, N., Rudrappa, S. S., Brook, M. S., IDRIS, I. R., Crossland, H., Hamrock, C., Aziz, M. H. A., Kadi, F., Tarum, J., Greenhaff, P. L., et al. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12472 · Cited by 88
Isolated Leucine and Branched-Chain Amino Acid Supplementation for Enhancing Muscular Strength and Hypertrophy: A Narrative Review
Plotkin, D. L., Delcastillo, K., Van Every, D. W., Tipton, K. D., Aragon, A. A., & Schoenfeld, B. J. (2021) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.2020-0356 · Cited by 80
Self-citation
The effect of sleep restriction, with or without high‐intensity interval exercise, on myofibrillar protein synthesis in healthy young men
Saner, N. J., Lee, M. J. ‐., Pitchford, N. W., Kuang, J., Roach, G. D., Garnham, A., Stokes, T., Phillips, S. M., Bishop, D. J., & Bartlett, J. D. (2020) · The Journal of Physiology · doi:10.1113/jp278828 · Cited by 68
Lactobacillus plantarum HY7715 Ameliorates Sarcopenia by Improving Skeletal Muscle Mass and Function in Aged Balb/c Mice
Lee, K., Kim, J., Park, S.-D., Shim, J.-J., & Lee, J.-L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810023 · Cited by 76
Systemic muscle wasting and coordinated tumour response drive tumourigenesis
Newton, H., Wang, Y.-F., Camplese, L., Mokochinski, J. B., Kramer, H., Brown, A. E., Fets, L., & Hirabayashi, S. (2020) · Nature Communications · doi:10.1038/s41467-020-18502-9 · Cited by 64
Mechanisms Involved in Gut Microbiota Regulation of Skeletal Muscle
Li, G., Jin, B., & Fan, Z. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/2151191 · Cited by 72
Acute sprint exercise transcriptome in human skeletal muscle
Rundqvist, H., Montelius, A., Österlund, T., Norman, B., Esbjörnsson, M., & Jansson, E. (2019) · PLoS ONE · doi:10.1371/journal.pone.0223024 · Cited by 62
Revisiting the roles of protein synthesis during skeletal muscle hypertrophy induced by exercise
Figueiredo, V. C. (2019) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00162.2019 · Cited by 60
Making Sense of Muscle Protein Synthesis: A Focus on Muscle Growth During Resistance Training
Witard, O. C., Bannock, L. G., & Tipton, K. D. (2021) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.2021-0139 · Cited by 71
Self-citation
The Influence of Post-Exercise Cold-Water Immersion on Adaptive Responses to Exercise: A Review of the Literature
Broatch, J. R., Petersen, A. C., & Bishop, D. J. (2018) · Sports Medicine · doi:10.1007/s40279-018-0910-8 · Cited by 70
Exogenous insulin‐like growth factor 1 attenuates cisplatin‐induced muscle atrophy in mice
Sakai, H., Asami, M., Naito, H., Kitora, S., Suzuki, Y., Miyauchi, Y., Tachinooka, R., Yoshida, S., Kon, R., Ikarashi, N., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12760 · Cited by 58
Dietary Protein for Training Adaptation and Body Composition Manipulation in Track and Field Athletes
Witard, O. C., Garthe, I., & Phillips, S. M. (2018) · International Journal of Sport Nutrition and Exercise Metabolism · doi:10.1123/ijsnem.2018-0267 · Cited by 67
Resistance Exercise, Aging, Disuse, and Muscle Protein Metabolism
McKendry, J., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Comprehensive physiology · doi:10.1002/cphy.c200029 · Cited by 78
Loss of RNA-Binding Protein Sfpq Causes Long-Gene Transcriptopathy in Skeletal Muscle and Severe Muscle Mass Reduction with Metabolic Myopathy
Hosokawa, M., Takeuchi, A., Tanihata, J., Iida, K., Takeda, S., & Hagiwara, M. (2019) · iScience · doi:10.1016/j.isci.2019.02.023 · Cited by 54
Physiology of activins/follistatins: Associations with metabolic and anthropometric variables and response to exercise
Perakakis, N., Mougios, V., Fatouros, I., Siopi, A., Draganidis, D., Peradze, N., Ghaly, W., & Mantzoros, C. S. (2018) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2018-01056 · Cited by 52
Effect of Caloric Restriction on BMI, Gut Microbiota, and Blood Amino Acid Levels in Non-Obese Adults
Zou, H., Wang, D., Ren, H., Chen, P., Fang, C., Shi, Z., Zhang, P., Wang, J., Wang, J., Cai, K., et al. (2020) · Nutrients · doi:10.3390/nu12030631 · Cited by 51
The effects of whey, pea, and collagen protein supplementation beyond the recommended dietary allowance on integrated myofibrillar protein synthetic rates in older males: a randomized controlled trial
McKendry, J., Lowisz, C. V., Nanthakumar, A., Macdonald, M. L., Lim, C., Currier, B. S., & Phillips, S. M. (2024) · American Journal of Clinical Nutrition · doi:10.1016/j.ajcnut.2024.05.009 · Cited by 56
Exercise-specific adaptations in human skeletal muscle: Molecular mechanisms of making muscles fit and mighty
Thomas, A. C. Q., Stead, C. A., Burniston, J. G., & Phillips, S. M. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.08.010 · Cited by 57
Cellular and molecular pathways controlling muscle size in response to exercise
Attwaters, M., & Hughes, S. M. (2021) · FEBS Journal · doi:10.1111/febs.15820 · Cited by 47
The Effects of Dietary Protein Supplementation on Acute Changes in Muscle Protein Synthesis and Longer-Term Changes in Muscle Mass, Strength, and Aerobic Capacity in Response to Concurrent Resistance and Endurance Exercise in Healthy Adults: A Systematic Review
Hartono, F. A., Martin-Arrowsmith, P. W., Peeters, W., & Churchward‐Venne, T. A. (2022) · Sports Medicine · doi:10.1007/s40279-021-01620-9 · Cited by 50
Myogenic, genomic and non‐genomic influences of the vitamin D axis in skeletal muscle
Bollen, S. E., & Atherton, P. J. (2020) · Cell Biochemistry and Function · doi:10.1002/cbf.3595 · Cited by 43
A Muscle-Centric Perspective on Intermittent Fasting: A Suboptimal Dietary Strategy for Supporting Muscle Protein Remodeling and Muscle Mass?
Williamson, E., & Moore, D. R. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.640621 · Cited by 42
Effect of resistance training and fish protein intake on motor unit firing pattern and motor function of elderly
Watanabe, K., Holobar, A., Mita, Y., Kouzaki, M., Ogawa, M., Akima, H., & Moritani, T. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01733 · Cited by 37
Role of the gut–muscle axis in mitochondrial function of ageing muscle under different exercise modes
Xie, X., & Huang, C. X. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102316 · Cited by 38
What skeletal muscle has to say in amyotrophic lateral sclerosis: Implications for therapy
Manzano, R., Toivonen, J. M., Moreno‐Martínez, L., de la Torre, M., Moreno‐García, L., López‐Royo, T., Molina, N., Zaragoza, P., Calvo, A. C., & Osta, R. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15276 · Cited by 34
Understanding the effects of nutrition and post-exercise nutrition on skeletal muscle protein turnover: Insights from stable isotope studies
Joanisse, S., McKendry, J., Lim, C., Nunes, E. A., Stokes, T., Mcleod, J. C., & Phillips, S. M. (2021) · Clinical Nutrition Open Science · doi:10.1016/j.nutos.2021.01.005 · Cited by 41
Invited review: Muscle protein breakdown and its assessment in periparturient dairy cows
Sadri, H., Ghaffari, M. H., & Sauerwein, H. (2022) · Journal of Dairy Science · doi:10.3168/jds.2022-22068 · Cited by 43
Multi-omics reveals immune response and metabolic profiles during high-altitude mountaineering
Yin, J., Lv, J., Yang, S., Wang, Y., Huang, Z., Wang, X., Hou, G., Zhou, W., Liu, Y., Wang, W., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115134 · Cited by 36
Targeting the Gut Microbiota to Improve Dietary Protein Efficacy to Mitigate Sarcopenia
Castro, E. D. M., Murphy, C. H., & Roche, H. M. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.656730 · Cited by 31
Exercise and physical activity in cirrhosis: opportunities or perils
Bellar, A., Welch, N., & Dasarathy, S. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00798.2019 · Cited by 33
Critical variables regulating age-related anabolic responses to protein nutrition in skeletal muscle
Deane, C. S., Cox, J., & Atherton, P. J. (2024) · Frontiers in Nutrition · doi:10.3389/fnut.2024.1419229 · Cited by 36
Effects of High-Volume Versus High-Load Resistance Training on Skeletal Muscle Growth and Molecular Adaptations
Vann, C. G., Sexton, C. L., Osburn, S. C., Smith, M. A., Haun, C. T., Rumbley, M. N., Mumford, P. W., Ferguson, B. K., Montgomery, N. T., Fox, C. D., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.857555 · Cited by 30
Comparable Rates of Integrated Myofibrillar Protein Synthesis Between Endurance-Trained Master Athletes and Untrained Older Individuals
McKendry, J., Shad, B. J., Smeuninx, B., Oikawa, S. Y., Wallis, G. A., Greig, C. A., Phillips, S. M., & Breen, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.01084 · Cited by 27
Reducing NF-κB Signaling Nutritionally is Associated with Expedited Recovery of Skeletal Muscle Function After Damage
Jameson, T. S. O., Pavis, G. F., Dirks, M. L., Lee, B. P., Abdelrahman, D. R., Murton, A. J., Porter, C., Alamdari, N., Mikus, C. R., Wall, B. T., et al. (2021) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgab106 · Cited by 25
The Contribution of Tumor Derived Exosomes to Cancer Cachexia
Pitzer, C. R., Paez, H. G., & Alway, S. E. (2023) · Cells · doi:10.3390/cells12020292 · Cited by 25
Dietary protein recommendations to support healthy muscle ageing in the 21st century and beyond: considerations and future directions
Morgan, P. T., Witard, O. C., Højfeldt, G. W., Church, D. D., & Breen, L. (2023) · Proceedings of The Nutrition Society · doi:10.1017/s0029665123003750 · Cited by 29
FGF21 Induces Skeletal Muscle Atrophy and Increases Amino Acids in Female Mice: A Potential Role for Glucocorticoids
Larson, K. R., Jayakrishnan, D., Sauza, K. A. S., Goodson, M. L., CHAFFIN, A. T. B., Davidyan, A., Pathak, S. J., Fang, Y., Magaña, D. G., Miller, B. F., et al. (2024) · Endocrinology · doi:10.1210/endocr/bqae004 · Cited by 24
Too low protein and energy intake in nursing home residents
Borkent, J. W., Manders, M., Nijhof, A., Wijker, L., Feskens, E. J. M., Naumann, E., & de van der Schueren, M. A. E. (2023) · Nutrition · doi:10.1016/j.nut.2023.112005 · Cited by 24
Sarcopenia as the Mobility Phenotype of Aging: Clinical Implications
Ji, S., Jung, H., Baek, J. Y., Jang, I., & Lee, E. (2024) · Journal of Bone Metabolism · doi:10.11005/jbm.2024.31.1.1 · Cited by 23
A Well-Balanced Vegan Diet Does not Compromise Daily Mixed Muscle Protein Synthesis Rates when Compared with an Omnivorous Diet in Active Older Adults: A Randomized Controlled Cross-Over Trial
Domić, J., Pinckaers, P. J., Grootswagers, P., Siebelink, E., Gerdessen, J. C., van Loon, L. J. C., & de Groot, C. P. G. M. (2024) · Journal of Nutrition · doi:10.1016/j.tjnut.2024.12.019 · Cited by 26
Contribution of skeletal muscle to cancer immunotherapy: A focus on muscle function, inflammation, and microbiota
Deng, Y., Zhao, L., Huang, X., Zeng, Y., Xiong, Z., & Zuo, M. (2022) · Nutrition · doi:10.1016/j.nut.2022.111829 · Cited by 27
Distinct skeletal muscle molecular responses to pulmonary rehabilitation in chronic obstructive pulmonary disease: a cluster analysis
Kneppers, A. E. M., Haast, R. A. M., LANGEN, R. C. J., Verdijk, L. B., Leermakers, P. A., Gosker, H. R., van Loon, L. J. C., Lainščak, M., & Schols, A. M. W. J. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12370 · Cited by 23
The effect of exercise and physical activity on skeletal muscle epigenetics and metabolic adaptations
Mallett, G. S. (2025) · European Journal of Applied Physiology · doi:10.1007/s00421-025-05704-6 · Cited by 23
Ergo-Nutritional Intervention in Basketball: A Systematic Review
Escribano-Ott, I., Calleja-González, J., & Mielgo‐Ayuso, J. (2022) · Nutrients · doi:10.3390/nu14030638 · Cited by 22
Inhibiting 5‐lipoxygenase prevents skeletal muscle atrophy by targeting organogenesis signalling and insulin‐like growth factor‐1
Kim, H., Kim, S., Lee, S., Jung, D., & Williams, D. R. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13092 · Cited by 23
A 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
Pharmacological hypogonadism impairs molecular transducers of exercise‐induced muscle growth in humans
Gharahdaghi, N., Rudrappa, S. S., Brook, M. S., Farrash, W. F., IDRIS, I. R., Aziz, M. H. A., Kadi, F., Papaioannou, K., Phillips, B. E., Sian, T. S., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12843 · Cited by 22
Resistance exercise: a mighty tool that adapts, destroys, rebuilds and modulates the molecular and structural environment of skeletal muscle
Bersiner, K., Park, S., Schaaf, K., Yang, W., Theis, C., Jacko, D., & Gehlert, S. (2023) · Physical Activity and Nutrition · doi:10.20463/pan.2023.0021 · Cited by 20
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
Repeated and Interrupted Resistance Exercise Induces the Desensitization and Re-Sensitization of mTOR-Related Signaling in Human Skeletal Muscle Fibers
Jacko, D., Schaaf, K., Masur, L., Windoffer, H., Aussieker, T., Schiffer, T., Zacher, J., Bloch, W., & Gehlert, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105431 · Cited by 20
Recent advances in measuring and understanding the regulation of exercise-mediated protein degradation in skeletal muscle
Nishimura, Y., Musa, I., Holm, L., & Lai, Y. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00115.2021 · Cited by 20
Lean mass sparing in resistance-trained athletes during caloric restriction: the role of resistance training volume
Roth, C., Schoenfeld, B. J., & Behringer, M. (2022) · European Journal of Applied Physiology · doi:10.1007/s00421-022-04896-5 · Cited by 21
Assessing the whole-body protein synthetic response to feeding in vivo in human subjects
Trommelen, J., & van Loon, L. J. C. (2021) · Proceedings of The Nutrition Society · doi:10.1017/s0029665120008009 · Cited by 21
Sarcopenic metabolomic profile reflected a sarcopenic phenotype associated with amino acid and essential fatty acid changes
Opazo, R., Bárbara Angel, B., Márquez, C., Lera, L., dos Santos, G. R. C., Monnerat, G., & Cecilia Albala, B. (2021) · Metabolomics · doi:10.1007/s11306-021-01832-0 · Cited by 18
Nutrition strategies to counteract sarcopenia: a focus on protein, LC n -3 PUFA and precision nutrition
Murphy, C. H., McCarthy, S. N., & Roche, H. M. (2023) · Proceedings of The Nutrition Society · doi:10.1017/s0029665123003555 · Cited by 19
Mitigating skeletal muscle wasting in unloading and augmenting subsequent recovery
Michel, J. M., Hettinger, Z. R., Ambrosio, F., Egan, B., Roberts, M. D., Ferrando, A. A., Graham, Z., & Bamman, M. M. (2024) · The Journal of Physiology · doi:10.1113/jp284301 · Cited by 15
Positive Effects of Aerobic-Resistance Exercise and an Ad Libitum High-Protein, Low-Glycemic Index Diet on Irisin, Omentin, and Dyslipidemia in Men with Abdominal Obesity: A Randomized Controlled Trial
Suder, A., Makiel, K., Targosz, A., Kosowski, P., & Malina, R. M. (2024) · Nutrients · doi:10.3390/nu16203480 · Cited by 16
In vivo collagen and mixed muscle protein turnover in 2 meat-type broiler strains in relation to woody breast myopathy
Maharjan, P., Weil, J. T., Beitia, A., Suesuttajit, N., Hilton, K., Caldas, J. V., Umberson, C., Martinez, D. A., Owens, C. M., & Coon, C. N. (2020) · Poultry Science · doi:10.1016/j.psj.2020.06.059 · Cited by 15
Ergogenic Effects of Green Tea Combined with Isolated Soy Protein on Increasing Muscle Mass and Exercise Performance in Resistance-Trained Mice
Lee, M., Hsu, Y.-J., Yang, L.-H., Huang, C., & Ho, C.-S. (2021) · Nutrients · doi:10.3390/nu13124547 · Cited by 15
The Plateau in Muscle Growth with Resistance Training: An Exploration of Possible Mechanisms
Kataoka, R., Hammert, W. B., Yamada, Y., Song, J. S., Seffrin, A., Kang, A., Spitz, R. W., Wong, V. H. Y., & Loenneke, J. P. (2023) · Sports Medicine · doi:10.1007/s40279-023-01932-y · Cited by 17
Health and ergogenic potential of oral adenosine-5′-triphosphate (ATP) supplementation
Jäger, R., Purpura, M., Rathmacher, J. A., Fuller, J. C., Pitchford, L. M., Rossi, F. E., & Kerksick, C. M. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104357 · Cited by 14
Mimicking exercise in vitro: effects of myotube contractions and mechanical stretch on omics
Lautaoja-Kivipelto, J. H., Turner, D. C., Sharples, A. P., Kivelä, R., Pekkala, S., Hulmi, J. J., & Ylä‐Outinen, L. (2023) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00586.2022 · Cited by 15
A novel stable isotope tracer method to simultaneously quantify skeletal muscle protein synthesis and breakdown
Crossland, H., Smith, K., Atherton, P. J., & Wilkinson, D. J. (2020) · Metabolism Open · doi:10.1016/j.metop.2020.100022 · Cited by 14
Subpopulation-specific differences in skeletal muscle mitochondria in humans with obesity: insights from studies employing acute nutritional and exercise stimuli
Wahwah, N., Kras, K. A., Roust, L. R., & Katsanos, C. S. (2020) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00463.2019 · Cited by 14
Higher glucose availability augments the metabolic responses of the C2C12 myotubes to exercise-like electrical pulse stimulation
Lautaoja-Kivipelto, J. H., O’Connell, T. M., Mäntyselkä, S., Peräkylä, J., Kainulainen, H., Pekkala, S., Permi, P., & Hulmi, J. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00133.2021 · Cited by 12
(Dys)regulation of Protein Metabolism in Skeletal Muscle of Humans With Obesity
Freitas, E. D. S., & Katsanos, C. S. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.843087 · Cited by 12
Molecular Regulators of Muscle Mass and Mitochondrial Remodeling Are Not Influenced by Testosterone Administration in Young Women
Horwath, O., Moberg, M., Hirschberg, A. L., Ekblom, B. T., & Apró, W. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.874748 · Cited by 9
Meat nutritive value and human health
Pereira, P. M. D. C. C., & Vicente, F. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85879-3.00024-6 · Cited by 13
Menopause, Female Sex Hormones, Skeletal Muscle Mass and Muscle Protein Turnover in Humans
Menzies, C., Bowtell, R. W., Shur, N. F., & Brook, M. S. (2026) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.70232 · Cited by 18
Possibilities of using branched-chain amino acids for the treatment and prevention of sarcopenia in elderly and old patients (literature review)
Kurmaev, D. P., Bulgakova, S. V., Treneva, E. V., Сергеевна, Ч. И., Kosareva, O. V., Sharonova, L. A., & Dolgikh, Y. A. (2023) · Бюллетень Восточно-Сибирского научного центра Сибирского отделения Российской академии медицинских наук · doi:10.29413/abs.2023-8.3.11 · Cited by 10
Skeletal muscle myosin heavy chain fragmentation as a potential marker of protein degradation in response to resistance training and disuse atrophy
Plotkin, D. L., Mattingly, M. L., Anglin, D. A., Michel, J. M., Godwin, J. S., McIntosh, M. C., Kontos, N. J., Bergamasco, J. G. A., Scarpelli, M. C., Angleri, V., et al. (2024) · Experimental Physiology · doi:10.1113/ep092093 · Cited by 7
The Role of Skeletal Muscle Mitochondria in Colorectal Cancer Related Cachexia: Friends or Foes?
van de Haterd, B., Verboven, K., Vandenabeele, F., & Agten, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314833 · Cited by 10
Effects of 2-week HMB-FA supplementation with or without eccentric resistance exercise on expression of some genes related to muscle protein turnover and serum irisin and IGF-1 concentrations
Shirvani, H., Rahmati-Ahmadabad, S., Kowsari, E., Fry, H. L., Kazemi, M., & Kaviani, M. (2020) · Gene · doi:10.1016/j.gene.2020.145018 · Cited by 10
Measuring Protein Turnover in the Field: Implications for Military Research
Hinde, K., O’Leary, T. J., Greeves, J. P., & Wardle, S. L. (2020) · Advances in Nutrition · doi:10.1093/advances/nmaa123 · Cited by 10
Fish Protein Ingestion Induces Neural, but Not Muscular Adaptations, Following Resistance Training in Young Adults
Watanabe, K., Holobar, A., Uchida, K., & Mita, Y. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.645747 · Cited by 10
Myofibrillar Protein Synthesis and Acute Intracellular Signaling with Elastic Band Resistance Exercise in Young and Older Men
Marshall, R. N., Morgan, P. T., Smeuninx, B., Quinlan, J. I., Brook, M. S., Atherton, P. J., Smith, K., Wilkinson, D. J., & Breen, L. (2022) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000003061 · Cited by 9
Limited effect of over-the-counter doses of ibuprofen on mechanisms regulating muscle hypertrophy during resistance training in young adults
Lilja, M. R., Moberg, M., Apró, W., Martínez-Aranda, L. M., Rundqvist, H., Langlet, B. S., Gustafsson, T. P., & Lundberg, T. R. (2023) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00698.2022 · Cited by 11
Acute Effect of a Protein Supplement on Targeted Plasma Amino Acid Profile among Healthy Asian Indians: A Randomized Controlled Trial
Kurien, A., Sharma, N., Marathe, M., Joshi, N. A., Selvam, S., Devi, S., & Sambashivaiah, S. (2020) · Journal of Nutrition and Metabolism · doi:10.1155/2020/8946820 · Cited by 9
L-leucine stimulation of glucose uptake and utilization involves modulation of glucose – lipid metabolic switch and improved bioenergetic homeostasis in isolated rat psoas muscle ex vivo
Erukainure, O. L., Salau, V. F., Atolanı, O., Ravichandran, R., Banerjee, P., Preißner, R., Koorbanally, N. A., & Islam, M. S. (2021) · Amino Acids · doi:10.1007/s00726-021-03021-8 · Cited by 9
Proteasome- and Calpain-Mediated Proteolysis, but Not Autophagy, Is Required for Leucine-Induced Protein Synthesis in C2C12 Myotubes
Osburn, S. C., Vann, C. G., Church, D. D., Ferrando, A. A., & Roberts, M. D. (2021) · Physiologia · doi:10.3390/physiologia1010005 · Cited by 9
The effect of branched-chain amino acids supplementation in physical exercise: A systematic review of human randomized controlled trials
Marcon, M., & Zanella, P. B. (2022) · Science & Sports · doi:10.1016/j.scispo.2021.05.006 · Cited by 11
The effects of elective abdominal surgery on protein turnover: A meta-analysis of stable isotope techniques to investigate postoperative catabolism
Jaconelli, M., Greenhaff, P. L., Atherton, P. J., Lobo, D. N., & Brook, M. S. (2022) · Clinical Nutrition · doi:10.1016/j.clnu.2022.01.023 · Cited by 9
Resistance exercise training improves disuse-induced skeletal muscle atrophy in humans: a meta-analysis of randomized controlled trials
Guo, X., Zhou, Y., Li, X., & Mu, J. (2025) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-025-08384-7 · Cited by 8
Gintonin-enriched fraction improves sarcopenia by maintaining immune homeostasis in 20- to 24-month-old C57BL/6J mice
Oh, H., Jin, H., Nah, S.-Y., & Lee, B.-Y. (2021) · Journal of Ginseng Research · doi:10.1016/j.jgr.2021.07.006 · Cited by 8
Prevalence of low energy availability and associations with seasonal changes in salivary hormones and IgA in elite male Gaelic footballers
McGuire, A., Warrington, G. D., & Doyle, L. (2023) · European Journal of Nutrition · doi:10.1007/s00394-023-03112-0 · Cited by 10
The Role of Exogenous Ketones in Road Cycling: Evidence, Mechanisms, and Performance Claims
Sitko, S. (2024) · Physiologia · doi:10.3390/physiologia4040029 · Cited by 8
Effects of multidomain interventions on skeletal muscle architecture and function in pre-frail older women: The WiiProtein study
Filho, J. M., Biesek, S., Vojciechowski, A. S., Tormes, G. D. A., & Gomes, A. R. S. (2022) · Geriatric Nursing · doi:10.1016/j.gerinurse.2022.10.009 · Cited by 7

Authors: Tipton, K. D., Hamilton, D. L., & Gallagher, I. J.
Affiliations: University of Stirling (GB)
Corresponding author: Tipton, Kevin D.
ORCID: Tipton, Kevin D.
Hamilton, D. Lee
Gallagher, Iain J.
Venue: Sports Medicine
Publisher: Springer Science and Business Media LLC
Published: 2018-01-24
Volume: 48
Issue: S1
Pages: 53-64
ISSN: 0112-1642 (ISSN-L)
1179-2035
DOI: 10.1007/s40279-017-0845-5
PMC: PMC5790854
OpenAlex: W2785778503
Cited by: 152
References: 103
Citations by year: 2026: 12 · 2025: 16 · 2024: 20 · 2023: 20 · 2022: 28 · 2021: 26 · 2020: 16 · 2019: 8 · 2018: 6
FWCI: 1.57
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (tdm)
Locations: Sports Medicine (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Durham Research Online (Durham University) (acceptedVersion, cc-by)
Durham Research Online (Durham University) (submittedVersion, cc-by)
Deakin Research Online (Deakin University) (submittedVersion)
Stirling Online Research Repository (University of Stirling) (submittedVersion, cc-by)
Figshare (submittedVersion, cc-by)
Funders: PepsiCo
Gran Sasso Science Institute
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
Keywords: muscle protein degradation, muscle protein synthesis, resistance training, post-exercise nutrition, autophagy, calpain, ubiquitin-proteasome system, hyperaminoacidemia, hyperinsulinemia, muscle remodeling, muscle mass
MeSH terms: Humans, Muscle Proteins, Nutritional Status, Exercise, Muscle, Skeletal

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

Assessing the role of muscle protein breakdown in response to nutrition and exercise in humans.

Abstract

Overview

Integrity signals

Figures

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks