Mammalian target of rapamycin complex 2 regulates muscle glucose uptake during exercise in mice

MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification

Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works

The Perseus computational platform for comprehensive analysis of (prote)omics data

Tyanova, S., Temu, T., Sinitcyn, P. G., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 7,977 · see citing works

Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216 · see citing works

Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment

Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,349 · see citing works

Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

Jacinto, E., Loewith, R., Schmidt, A., Lin, S., Rüegg, M. A., Hall, A., & Hall, M. N. (2004) · Nature Cell Biology · doi:10.1038/ncb1183 · Cited by 2,097 · see citing works

Exercise, GLUT4, and skeletal muscle glucose uptake

Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407 · see citing works

The nuts and bolts of AGC protein kinases

Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294 · see citing works

mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)

García-Martínez, J. M., & Alessi, D. R. (2008) · Biochemical Journal · doi:10.1042/bj20081668 · Cited by 907 · see citing works

Sgk1-Dependent Stimulation of Cardiac Na+/H+Exchanger Nhe1 by Dexamethasone

Voelkl, J. G. J., Pasham, V., Ahmed, M. S. E., Walker, B., Szteyn, K., Kuhl, D., Metzler, B., Alesutan, I., & Lang, F. J. W. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350120 · Cited by 859 · see citing works

mSin1 Is Necessary for Akt/PKB Phosphorylation, and Its Isoforms Define Three Distinct mTORC2s

Frías, M. A., Thoreen, C. C., Jaffe, J. D., Schroder, W. A., Sculley, T. B., Carr, S. A., & Sabatini, D. M. (2006) · Current Biology · doi:10.1016/j.cub.2006.08.001 · Cited by 690 · see citing works

CAP defines a second signalling pathway required for insulin-stimulated glucose transport

Baumann, C. A., Ribon, V., Kanzaki, M., Thurmond, D. C., Mora, S., Shigematsu, S., Bickel, P. E., Pessin, J. E., & Saltiel, A. R. (2000) · Nature · doi:10.1038/35025089 · Cited by 660 · see citing works

Activation of mTORC2 by Association with the Ribosome

Zinzalla, V., Stracka, D., Oppliger, W., & Hall, M. N. (2011) · Cell · doi:10.1016/j.cell.2011.02.014 · Cited by 648 · see citing works

Skeletal Muscle-Specific Ablation of raptor, but Not of rictor, Causes Metabolic Changes and Results in Muscle Dystrophy

Bentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.002 · Cited by 640 · see citing works

Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling

Ikenoue, T., Inoki, K., Yang, Q., Zhou, X., & Guan, K. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.119 · Cited by 605 · see citing works

The mechanistic target of rapamycin: the grand conducTOR of metabolism and aging

Kennedy, B. K., & Lamming, D. W. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.009 · Cited by 544 · see citing works

mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology

Betz, C., Stracka, D., Prescianotto-Baschong, C., Frieden, M., Demaurex, N., & Hall, M. N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302455110 · Cited by 538 · see citing works

Exercise-stimulated glucose uptake — regulation and implications for glycaemic control

Sylow, L., Kleinert, M., Richter, E. A., & Jensen, T. E. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2016.162 · Cited by 498 · see citing works

STIMulating store-operated Ca2+ entry

Cahalan, M. D. (2009) · Nature Cell Biology · doi:10.1038/ncb0609-669 · Cited by 451 · see citing works

Global Phosphoproteomic Analysis of Human Skeletal Muscle Reveals a Network of Exercise-Regulated Kinases and AMPK Substrates

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., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.001 · Cited by 426 · see citing works

TORC-Specific Phosphorylation of Mammalian Target of Rapamycin (mTOR): Phospho-Ser2481 Is a Marker for Intact mTOR Signaling Complex 2

Copp, J., Manning, G., & Hunter, T. R. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3014 · Cited by 422 · see citing works

Acute exercise induces GLUT4 translocation in skeletal muscle of normal human subjects and subjects with type 2 diabetes

Kennedy, J. W., Hirshman, M. F., Gervino, E. V., Ocel, J. V., Forse, R. A., Hoenig, S. J., Aronson, D., Goodyear, L. J., & Horton, E. S. (1999) · Diabetes · doi:10.2337/diabetes.48.5.1192 · Cited by 415 · see citing works

Ca2+ and AMPK Both Mediate Stimulation of Glucose Transport by Muscle Contractions

Wright, D. C., Hucker, K. A., Holloszy, J. O., & Han, D. H. (2004) · Diabetes · doi:10.2337/diabetes.53.2.330 · Cited by 398 · see citing works

PtdIns(3,4,5) P 3-Dependent Activation of the mTORC2 Kinase Complex

Liu, P., Gan, W., Chin, Y. R., Ogura, K., Guo, J., Zhang, J., Wang, B., Blenis, J., Cantley, L. C., Toker, A., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0460 · Cited by 385 · see citing works

mTORC2 can associate with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide

Oh, W. J., Wu, C. C., Kim, S. J., Facchinetti, V., Julien, L.-A., Finlan, M., Roux, P. P., Su, B., & Jacinto, E. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.271 · Cited by 333 · see citing works

A Positive Feedback Loop between Akt and mTORC2 via SIN1 Phosphorylation

Yang, G., Murashige, D., Humphrey, S. J., & James, D. E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.016 · Cited by 297 · see citing works

A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation

Frödin, M., Antal, T. L., Dümmler, B. A., Jensen, C. J., Deak, M., Gammeltoft, S., & Biondi, R. M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf551 · Cited by 275 · see citing works

Regulation and Physiological Roles of Serum- and Glucocorticoid-Induced Protein Kinase Isoforms

Lang, F. J. W., & Cohen, P. (2001) · Science s STKE · doi:10.1126/stke.2001.108.re17 · Cited by 274 · see citing works

Selective enrichment of sialic acid–containing glycopeptides using titanium dioxide chromatography with analysis by HILIC and mass spectrometry

Palmisano, G., Lendal, S. E., Engholm‐Keller, K., Leth‐Larsen, R., Parker, B. L., & Larsen, M. R. (2010) · Nature Protocols · doi:10.1038/nprot.2010.167 · Cited by 241 · see citing works

The Ca 2+ /Calmodulin/CaMKK2 Axis: Nature's Metabolic CaMshaft

Marcelo, K. L., Means, A. R., & York, B. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.06.001 · Cited by 226 · see citing works

Muscle-Specific Deletion of Rictor Impairs Insulin-Stimulated Glucose Transport and Enhances Basal Glycogen Synthase Activity

Kumar, A. T., Harris, T. E., Keller, S. R., Choi, K. M., Magnuson, M. A., & Lawrence, J. C. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01405-07 · Cited by 216 · see citing works

Localization of mTORC2 activity inside cells

Ebner, M., Sinkovics, B., Szczygieł, M., Ribeiro, D., & Yudushkin, I. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201610060 · Cited by 181 · see citing works

Protor-1 is required for efficient mTORC2-mediated activation of SGK1 in the kidney

Pearce, L. R., Sommer, E. M., Sakamoto, K., Wullschleger, S., & Alessi, D. R. (2011) · Biochemical Journal · doi:10.1042/bj20102103 · Cited by 179 · see citing works

TiSH — a robust and sensitive global phosphoproteomics strategy employing a combination of TiO2, SIMAC, and HILIC

Engholm‐Keller, K., Birck, P. K., Størling, J., Pociot, F., Mandrup-Poulsen, T. R., & Larsen, M. R. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2012.08.007 · Cited by 174 · see citing works

Rac1 signalling towards GLUT4/glucose uptake in skeletal muscle

Chiu, T. T., Jensen, T. E., Sylow, L., Richter, E. A., & Klip, A. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.05.022 · Cited by 145 · see citing works

Rac1 Is a Novel Regulator of Contraction-Stimulated Glucose Uptake in Skeletal Muscle

Sylow, L., Jensen, T. E., Kleinert, M., Mouatt, J. R., Maarbjerg, S., Jeppesen, J. F., Prats, C., Chiu, T. T., Boguslavsky, S., Klip, A., et al. (2012) · Diabetes · doi:10.2337/db12-0491 · Cited by 143 · see citing works

Improving Type 2 Diabetes Through a Distinct Adrenergic Signaling Pathway Involving mTORC2 That Mediates Glucose Uptake in Skeletal Muscle

Sato, M., Dehvari, N., Öberg, A. I., Dallner, O. S., Sandström, A. L., Olsen, J. M., Csikasz, R. I., Summers, R. J., Hutchinson, D. S., & Bengtsson, T. (2014) · Diabetes · doi:10.2337/db13-1860 · Cited by 130 · see citing works

Stat5 is a physiological substrate of the insulin receptor

Chen, J., Sadowski, H. B., Kohanski, R. A., & Wang, L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2295 · Cited by 124 · see citing works

Undesirable Charge-Enhancement of Isobaric Tagged Phosphopeptides Leads to Reduced Identification Efficiency

Thingholm, T. E., Palmisano, G., Kjeldsen, F., & Larsen, M. R. (2010) · Journal of Proteome Research · doi:10.1021/pr100230q · Cited by 121 · see citing works

Signal transducer and activator of transcription 5A/B in prostate and breast cancers

Tan, S., & Nevalainen, M. (2008) · Endocrine Related Cancer · doi:10.1677/erc-08-0013 · Cited by 115 · see citing works

Rac1 governs exercise‐stimulated glucose uptake in skeletal muscle through regulation of GLUT4 translocation in mice

Sylow, L., Nielsen, I. L., Kleinert, M., Møller, L. L. V., Ploug, T., Schjerling, P., Bilan, P. J., Klip, A., Jensen, T. E., & Richter, E. A. (2016) · The Journal of Physiology · doi:10.1113/jp272039 · Cited by 114 · see citing works

The Molecular Basis for Load-Induced Skeletal Muscle Hypertrophy

Marcotte, G. R., West, D. W. D., & Baar, K. (2014) · Calcified Tissue International · doi:10.1007/s00223-014-9925-9 · Cited by 108 · see citing works

A FOXO–Pak1 transcriptional pathway controls neuronal polarityPreprint

de la Torre-Ubieta, L., Gaudilliere, B. L., Yang, Y., Ikeuchi, Y., Yamada, T., DiBacco, S., Stegmüller, J., Schüller, U., Salih, D. A. M., Rowitch, D. H., et al. (2010) · Genes & Development · doi:10.1101/gad.1880510 · Cited by 97 · see citing works

The Abl/Arg substrate ArgBP2/nArgBP2 coordinates the function of multiple regulatory mechanisms converging on the actin cytoskeleton

Cestra, G., Toomre, D. K., Chang, S., & Camilli, P. V. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409376102 · Cited by 96 · see citing works

Hepatic signaling by the mechanistic target of rapamycin complex 2 (mTORC2)

Lamming, D. W., Demirkan, G., Boylan, J. M., Mihaylova, M. M., Peng, T., Ferreira, J., Neretti, N., Salomon, A. R., Sabatini, D. M., & Gruppuso, P. A. (2013) · The FASEB Journal · doi:10.1096/fj.13-237743 · Cited by 86 · see citing works

Contraction-stimulated glucose transport in muscle is controlled by AMPK and mechanical stress but not sarcoplasmatic reticulum Ca2+ release

Jensen, T. E., Sylow, L., Rose, A. J., Madsen, A. B., Angin, Y., Maarbjerg, S. J., & Richter, E. A. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.07.005 · Cited by 83 · see citing works

Acute mTOR inhibition induces insulin resistance and alters substrate utilization in vivo

Kleinert, M., Sylow, L., Fazakerley, D. J., Krycer, J. R., Thomas, K. C., Oxboll, A., Jordy, A. B., Jensen, T. E., Yang, G., Schjerling, P., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.06.004 · Cited by 81 · see citing works

Regulation of Endothelial Cell Proliferation and Vascular Assembly through Distinct mTORC2 Signaling Pathways

Wang, S., Amato, K. R., Song, W., Youngblood, V., Lee, K., Boothby, M. R., Brantley‐Sieders, D. M., & Chen, J. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00306-14 · Cited by 71 · see citing works

Rac1 – a novel regulator of contraction‐stimulated glucose uptake in skeletal muscle

Sylow, L., Møller, L. L. V., Kleinert, M., Richter, E. A., & Jensen, T. E. (2014) · Experimental Physiology · doi:10.1113/expphysiol.2014.079194 · Cited by 69 · see citing works

mTORC2 and AMPK differentially regulate muscle triglyceride content via Perilipin 3

Kleinert, M., Parker, B. L., Chaudhuri, R., Fazakerley, D. J., Serup, A. K., Thomas, K. C., Krycer, J. R., Sylow, L., Fritzen, A. M., Hoffman, N. J., et al. (2016) · Molecular Metabolism · doi:10.1016/j.molmet.2016.06.007 · Cited by 61 · see citing works

The Rac1 Polybasic Region Is Required for Interaction with Its Effector PRK1

Modha, R., Campbell, L. J., Nietlispach, D., Buhecha, H. R., Owen, D., & Mott, H. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706760200 · Cited by 55 · see citing works

mTOR Directs Breast Morphogenesis through the PKC-alpha-Rac1 Signaling Axis

Morrison, M. M., Young, C. D., Wang, S., Sobolik, T., Sanchez, V. M., Hicks, D. J., Cook, R. S., & Brantley‐Sieders, D. M. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005291 · Cited by 46 · see citing works

Hyperosmotic-induced Protein Kinase N 1 Activation in a Vesicular Compartment Is Dependent upon Rac1 and 3-Phosphoinositide-dependent Kinase 1

Torbett, N. E., Casamassima, A., & Parker, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303532200 · Cited by 36 · see citing works

mTORC2 is a tyrosine kinase

Wang, X., & Proud, C. G. (2015) · Cell Research · doi:10.1038/cr.2015.134 · Cited by 30 · see citing works

Phosphorylation of the JAK2-STAT5 Pathway in Response to Acute Aerobic Exercise

Consitt, L. A., Wideman, L., Hickey, M. S., & Morrison, R. F. (2008) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0b013e3181690760 · Cited by 22 · see citing works

Transmembrane Inhibitor of RICTOR/mTORC2 in Hematopoietic Progenitors

Lee, D., Sykes, S. M., Kalaitzidis, D., Lane, A. A., Kfoury, Y. S., Raaijmakers, M. H. G. P., Wang, Y., Armstrong, S. A., & Scadden, D. T. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.08.011 · Cited by 20 · see citing works

Regulation and metabolic functions of mTORC1 and mTORC2.

Szwed, A., Kim, E., & Jacinto, E. (2021) · Physiological Reviews · doi:10.1152/physrev.00026.2020 · Cited by 723 · see citing works

Metabolic Basis of Creatine in Health and Disease: A Bioinformatics-Assisted Review

Bonilla, D. A., Kreider, R. B., Stout, J. R., Forero, D. A., Kerksick, C. M., Roberts, M. D., & Rawson, E. S. (2021) · Nutrients · doi:10.3390/nu13041238 · Cited by 223 · see citing works

A novel rapamycin analog is highly selective for mTORC1 in vivo

Schreiber, K. H., Apelo, S. I. A., Yu, D., Brinkman, J. A., Velarde, M. C., Syed, F. A., Liao, C., Baar, E. L., Carbajal, K. A., Sherman, D. S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11174-0 · Cited by 194 · see citing works

The central moTOR of metabolism

Simcox, J., & Lamming, D. W. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.02.024 · Cited by 162 · see citing works

Integrin signaling: linking mechanical stimulation to skeletal muscle hypertrophy

Boppart, M. D., & Mahmassani, Z. S. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00009.2019 · Cited by 157 · see citing works

Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function

Blazev, R., Carl, C. S., Ng, Y., Molendijk, J., Voldstedlund, C. T., Zhao, Y., Xiao, D., Kueh, A. J., Miotto, P. M., Haynes, V. R., et al. (2022) · Cell Metabolism · doi:10.1016/j.cmet.2022.07.003 · Cited by 111 · see citing works

Exercise and GLUT4

Flores-Opazo, M., McGee, S. L., & Hargreaves, M. (2020) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000224 · Cited by 102 · see citing works

The IKK‐related kinase TBK1 activates mTORC1 directly in response to growth factors and innate immune agonists

Bodur, Ç., Kazyken, D., Huang, K., Üstünel, B. E., Siroky, K. A., Tooley, A. S., Gonzalez, I. E., Foley, D. H., Acosta-Jaquez, H. A., Barnes, T. M., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201696164 · Cited by 97 · see citing works

Interactions between insulin and exercise

Richter, E. A., Sylow, L., & Hargreaves, M. (2021) · Biochemical Journal · doi:10.1042/bcj20210185 · Cited by 99 · see citing works

Calorie-Restriction-Induced Insulin Sensitivity Is Mediated by Adipose mTORC2 and Not Required for Lifespan Extension

Yu, D., Tomasiewicz, J. L., Yang, S. E., Miller, B. R., Wakai, M. H., Sherman, D. S., Cummings, N. E., Baar, E. L., Brinkman, J. A., Syed, F. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.084 · Cited by 94 · see citing works

Phosphoproteomics reveals conserved exercise‐stimulated signaling and AMPK regulation of store‐operated calcium entry

Nelson, M. E., Parker, B. L., Burchfield, J. G., Hoffman, N. J., Needham, E. J., Cooke, K. C., Naim, T., Sylow, L., Ling, N. X. Y., Francis, D., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2019102578 · Cited by 81 · see citing works

A comprehensive view of muscle glucose uptake: regulation by insulin, contractile activity, and exercise

Richter, E. A., Bilan, P. J., & Klip, A. (2025) · Physiological Reviews · doi:10.1152/physrev.00033.2024 · Cited by 64 · see citing works

Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities

Mesquita, P. H. C., Vann, C. G., Phillips, S. M., McKendry, J., Young, K. C., Kavazis, A. N., & Roberts, M. D. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.725866 · Cited by 62 · see citing works

Resistance Exercise-Induced Hypertrophy: A Potential Role for Rapamycin-Insensitive mTOR

Ogasawara, R., Jensen, T. E., Goodman, C. A., & Hornberger, T. A. (2019) · Exercise and Sport Sciences Reviews · doi:10.1249/jes.0000000000000189 · Cited by 56 · see citing works

Next generation strategies for geroprotection via mTORC1 inhibition.

Dumas, S., & Lamming, D. (2019) · The journals of gerontology. Series A, Biological sciences and medical sciences · doi:10.1093/gerona/glz056 · Cited by 38 · see citing works

Growth Factor-Dependent and -Independent Activation of mTORC2

Knudsen, J. R., Fritzen, A. M., James, D. E., Jensen, T. E., Kleinert, M., & Richter, E. A. (2019) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2019.09.005 · Cited by 52 · see citing works

Quantitative proteomic characterization of cellular pathways associated with altered insulin sensitivity in skeletal muscle following high-fat diet feeding and exercise training

Kleinert, M., Parker, B. L., Jensen, T. E., Raun, S. H., Pham, T. C. P., Han, X., James, D. E., Richter, E. A., & Sylow, L. (2018) · Scientific Reports · doi:10.1038/s41598-018-28540-5 · Cited by 46 · see citing works

Pharmacological targeting of exercise adaptations in skeletal muscle: Benefits and pitfalls

Weihrauch, M., & Handschin, C. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.10.006 · Cited by 37 · see citing works

Ovariectomy uncouples lifespan from metabolic health and reveals a sex-hormone-dependent role of hepatic mTORC2 in aging

Apelo, S. I. A., Lin, A., Brinkman, J. A., Meyer, E. J., Morrison, M., Tomasiewicz, J. L., Pumper, C. P., Baar, E. L., Richardson, N. E., Alotaibi, M., et al. (2020) · eLife · doi:10.7554/elife.56177 · Cited by 37 · see citing works

Molecular Regulation of Skeletal Muscle Growth and Organelle Biosynthesis: Practical Recommendations for Exercise Training

Solsona, R., Pavlin, L., Bernardi, H., & Sanchez, A. M. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052741 · Cited by 39 · see citing works

Feedback, Crosstalk and Competition: Ingredients for Emergent Non-Linear Behaviour in the PI3K/mTOR Signalling Network

Ghomlaghi, M., Hart, A., Hoang, N., Shin, S., & Nguyen, L. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136944 · Cited by 36 · see citing works

Recombinant Uncarboxylated Osteocalcin Per Se Enhances Mouse Skeletal Muscle Glucose Uptake in both Extensor Digitorum Longus and Soleus Muscles

Lin, X., Parker, L., McLennan, E. D., Zhang, X., Hayes, A., McConell, G. K., Brennan‐Speranza, T. C., & Levinger, I. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00330 · Cited by 37 · see citing works

Who does TORC2 talk to?

Xie, J.-L., Wang, X.-M., & Proud, C. (2018) · Biochemical Journal · doi:10.1042/bcj20180130 · Cited by 26 · see citing works

Glucometabolic consequences of acute and prolonged inhibition of fatty acid oxidation

Lundsgaard, A., Fritzen, A. M., Nicolaisen, T. S., Carl, C. S., Sjøberg, K. A., Raun, S. H., Klein, A. B., Sanchez-Quant, E., Langer, J., Ørskov, C., et al. (2019) · Journal of Lipid Research · doi:10.1194/jlr.ra119000177 · Cited by 33 · see citing works

ER–Mitochondria Contacts and Insulin Resistance Modulation through Exercise Intervention

Sun, Y., & Ding, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249587 · Cited by 27 · see citing works

Targeting mTOR Signaling in Type 2 Diabetes Mellitus and Diabetes Complications

Yang, L., Zhang, Z., Wang, D., Jiang, Y., & Liu, Y. (2022) · Current Drug Targets · doi:10.2174/1389450123666220111115528 · Cited by 27 · see citing works

Geroprotector drugs and exercise: friends or foes on healthy longevity?

Elliehausen, C. J., Anderson, R. M., Diffee, G. M., Rhoads, T. W., Lamming, D. W., Hornberger, T. A., & Konopka, A. R. (2023) · BMC Biology · doi:10.1186/s12915-023-01779-9 · Cited by 24 · see citing works

Effects of short-term high-intensity interval and continuous exercise training on body composition and cardiac function in obese sarcopenic rats

França, G. D. O., Frantz, E. D. C., Magliano, D. C., Bargut, T. C. L., Sepúlveda-Fragoso, V., Silvares, R. R., Daliry, A., do Nascimento, A. R., & Borges, J. P. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117920 · Cited by 23 · see citing works

Trained Integrated Postexercise Myofibrillar Protein Synthesis Rates Correlate with Hypertrophy in Young Males and Females

Sawan, S. A., Hodson, N. W., Malowany, J. M., West, D. W. D., Tinline‐Goodfellow, C. T., Brook, M. S., Smith, K., Atherton, P. J., Kumbhare, D. A., & Moore, D. R. (2022) · Medicine & Science in Sports & Exercise · doi:10.1249/mss.0000000000002878 · Cited by 23 · see citing works

Characterization of tumors with ultralow tumor mutational burden in Japanese cancer patients

Hatakeyama, K., Nagashima, T., Ohshima, K., Ohnami, S., Ohnami, S., Shimoda, Y., Naruoka, A., Maruyama, K., Iizuka, A., Ashizawa, T., et al. (2020) · Cancer Science · doi:10.1111/cas.14572 · Cited by 21 · see citing works

Mitochondria-Associated Membranes as Key Regulators in Cellular Homeostasis and the Potential Impact of Exercise on Insulin Resistance

Li, X., Yang, Y., Shi, X., Zhang, Z., & Ding, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063196 · Cited by 16 · see citing works

METTL3 regulates glucose transporter expression in placenta exposed to hyperglycemia through the mTOR signaling pathway

Ning, J., Huai, J., Wang, S., Yan, J., Su, R., Zhang, M., Liu, M., & Yang, H. (2023) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002840 · Cited by 16 · see citing works

Passive stretch regulates skeletal muscle glucose uptake independent of nitric oxide synthase

Kerris, J. P., Betik, A. C., Li, J., & McConell, G. K. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00368.2018 · Cited by 13 · see citing works

Skeletal muscle and intermuscular adipose tissue gene expression profiling identifies new biomarkers with prognostic significance for insulin resistance progression and intervention response

Lutter, D., Sachs, S., Walter, M., Kerege, A. A., Perreault, L., KAHN, D. E., Wolide, A. D., Kleinert, M., Bergman, B. C., & Hofmann, S. M. (2023) · Diabetologia · doi:10.1007/s00125-023-05874-y · Cited by 12 · see citing works

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 15 · see citing works

Pharmacological targeting of α3β4 nicotinic receptors improves peripheral insulin sensitivity in mice with diet-induced obesity

Jall, S., Angelis, M. D., Lundsgaard, A., Fritzen, A. M., Nicolaisen, T. S., Klein, A. B., Novikoff, A., Sachs, S., Richter, E. A., Kiens, B., et al. (2020) · Diabetologia · doi:10.1007/s00125-020-05117-4 · Cited by 11 · see citing works

CaMKII and Kalirin, a Rac1-GEF, regulate Akt phosphorylation involved in contraction-induced glucose uptake in skeletal muscle cells

Liu, S., Zhang, J., Qi, R., Deng, B., Ni, Y., Zhang, C., & Niu, W. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.03.152 · Cited by 10 · see citing works

The skeletal muscle fiber periphery: A nexus of mTOR-related anabolism

Tinline-Goodfellow, C. T., Lees, M., & Hodson, N. (2022) · Sports Medicine and Health Science · doi:10.1016/j.smhs.2022.11.004 · Cited by 9 · see citing works

Affinity Purification-Mass Spectrometry and Single Fiber Physiology/Proteomics Reveals Mechanistic Insights of C18ORF25

Ng, Y., Blazev, R., McNamara, J. W., Dutt, M., Molendijk, J., Porrello, E. R., Elliott, D. A., & Parker, B. L. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00716 · Cited by 9 · see citing works

Exercise increases phosphorylation of the putative mTORC2 activity readout NDRG1 in human skeletal muscle

Knudsen, J. R., Persson, K. W., Meister, J., Carl, C. S., Raun, S. H., Andersen, N. R., Sylow, L., Kiens, B., Jensen, T. E., Richter, E. A., et al. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00389.2021 · Cited by 9 · see citing works

The female syndecan-4−/− heart has smaller cardiomyocytes, augmented insulin/pSer473-Akt/pSer9-GSK-3β signaling, and lowered SCOP, pThr308-Akt/Akt and GLUT4 levels

Støle, T. P., Lunde, M., Shen, X. M., Martinsen, M., Lunde, P., Li, J., Lockwood, F., Sjaastad, I., Louch, W. E., Aronsen, J. M., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.908126 · Cited by 9 · see citing works

Rapamycin Does Not Compromise Exercise‐Induced Muscular Adaptations in Female Mice

Elliehausen, C. J., Olszewski, S. S., Minton, D. M., Shult, C. G., Ailiani, A. R., Trautman, M. E., Babygirija, R., Lamming, D. W., Hornberger, T. A., & Konopka, A. R. (2025) · Aging Cell · doi:10.1111/acel.70183 · Cited by 7 · see citing works

mTOR Ser1261 is an AMPK ‐dependent phosphosite in mouse and human skeletal muscle not required for mTORC2 activity

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 5 · see citing works

Exercise-Regulated Skeletal Muscle Glucose Uptake

Jensen, T. E., Knudsen, J. R., Henríquez‐Olguín, C., Sylow, L., McConell, G. K., & Richter, E. A. (2022) · Physiology in health and disease · doi:10.1007/978-3-030-94305-9_6 · Cited by 4 · see citing works

Rationale for the use of metformin and exercise to counteract statin‐associated side effects

Haxhi, J., & Thompson, P. D. (2020) · International Journal of Clinical Practice · doi:10.1111/ijcp.13900 · Cited by 4 · see citing works

Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes

Bremner, S., Berends, R. F., Kaupisch, A., Roccisana, J., Sutherland, C. D., Bryant, N. J., & Gould, G. W. (2023) · PeerJ · doi:10.7717/peerj.15630 · Cited by 2 · see citing works

Methylglyoxal‐derived hydroimidazolone ( MG ‐ H1 ) is a novel marker of insulin resistance in Japanese individuals, disturbing insulin signalling via mTORC2 in cultured myocytes

Kitao, S., Okura, T., Ito, Y., Endo, S., Ichihara, Y., Sawano, T., Nakamura, R., Matsuzawa, K., Nomi, Y., Ueta, E., et al. (2026) · Diabetes Obesity and Metabolism · doi:10.1111/dom.70489 · Cited by 1 · see citing works

Rapamycin does not compromise physical performance or muscle hypertrophy after PoWeR while intermittent rapamycin alleviates glucose disruptions by frequent rapamycinPreprint

Elliehausen, C. J., Olszewski, S. S., Shult, C. G., Ailiani, A. R., Trautman, M. E., Babygirija, R., Lamming, D. W., Hornberger, T. A., Minton, D. M., & Konopka, A. R. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.10.642477 · Cited by 1 · see citing works

The effects of undercarboxylated osteocalcin on oxidative versus glycolytic skeletal muscle

Lin, X. (2018) · Victoria University Research Repository (Victoria University)

Regulation of Skeletal Muscle Glucose Uptake: A Focus on Nitric Oxide Synthase and Rac1 Signalling

Kerris, J. P. (2020) · Victoria University Research Repository (Victoria University)

Faculty Opinions recommendation of Calorie-Restriction-Induced Insulin Sensitivity Is Mediated by Adipose mTORC2 and Not Required for Lifespan Extension.

Müller, R. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736691002.793572463

Peer Review #1 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.1/reviews/1

Peer Review #2 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.1/reviews/2

Peer Review #2 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.2)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.2/reviews/2

Peer Review #3 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.1)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.1/reviews/3

Peer Review #1 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.2)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.2/reviews/1

Peer Review #3 of "Phosphorylation of the N-terminus of Syntaxin-16 controls interaction with mVps45 and GLUT4 trafficking in adipocytes (v0.2)"

(2023) · PeerJ · doi:10.7287/peerj.15630v0.2/reviews/3

Cell-matrix mechanosensing and cellular metabolic demand are linked through SKT and mTORC2Preprint

Collins, M., Young, L. E., Goodall, E., Hammond, B., Newman, D., Atherton, P., Caswell, P. T., & Zech, T. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.03.702586

Effect of High Intensity Interval Training on Visceral Adipose Tissue Levels of Isthmin-1 and Insulin Resistance in Obese Diabetic Rat

Rahmani, Z., Rezaeian, N., Cheragh-Birjandi, S., Yaghoubi, A., & Rezaei, V. (2026) · North Khorasan University of Medical Sciences · doi:10.66224/nkums.18.1.69

Genetic impairment of AMPKα2 signaling does not reduce muscle glucose uptake during treadmill exercise in mice

Maarbjerg, S., Jørgensen, S. B., Rose, A. J., Jeppesen, J. F., Jensen, T. E., Treebak, J. T., Birk, J. B., Schjerling, P., Wojtaszewski, J. F. P., & Richter, E. A. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90653.2008 · Cited by 93 · see citing works

Rac1 and AMPK Account for the Majority of Muscle Glucose Uptake Stimulated by Ex Vivo Contraction but Not In Vivo Exercise

Sylow, L., Møller, L. L. V., Kleinert, M., D’Hulst, G., Groote, E. D., Schjerling, P., Steinberg, G. R., Jensen, T. E., & Richter, E. A. (2017) · Diabetes · doi:10.2337/db16-1138 · Cited by 63 · see citing works

Rac1 governs exercise‐stimulated glucose uptake in skeletal muscle through regulation of GLUT4 translocation in mice

Sylow, L., Nielsen, I. L., Kleinert, M., Møller, L. L. V., Ploug, T., Schjerling, P., Bilan, P. J., Klip, A., Jensen, T. E., & Richter, E. A. (2016) · The Journal of Physiology · doi:10.1113/jp272039 · Cited by 114 · see citing works

Measurement of skeletal muscle glucose uptake in mice in response to acute treadmill running

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 · see citing works

Muscle‐specific deletion of mTORC2 (Rictor) blocks insulin stimulated Akt Ser 473 phosphorylation and impairs submaximal but not maximal insulin induced glucose uptake

Kleinert, M., Sylow, L., Jensen, T. E., Oxboll, A., & Richter, E. A. (2013) · The FASEB Journal · doi:10.1096/fasebj.27.1_supplement.1109.10 · Cited by 1 · see citing works