Contraction regulates site-specific phosphorylation of TBC1D1 in skeletal muscle
Open accessAbstract
TBC1D1 (tre-2/USP6, BUB2, cdc16 domain family member 1) is a Rab-GAP (GTPase-activating protein) that is highly expressed in skeletal muscle, but little is known about TBC1D1 regulation and function. We studied TBC1D1 phosphorylation on three predicted AMPK (AMP-activated protein kinase) phosphorylation sites (Ser231, Ser660 and Ser700) and one predicted Akt phosphorylation site (Thr590) in control mice, AMPKα2 inactive transgenic mice (AMPKα2i TG) and Akt2-knockout mice (Akt2 KO). Muscle contraction significantly increased TBC1D1 phosphorylation on Ser231 and Ser660, tended to increase Ser700 phosphorylation, but had no effect on Thr590. AICAR (5-aminoimidazole-4-carboxyamide ribonucleoside) also increased phosphorylation on Ser231, Ser660 and Ser700, but not Thr590, whereas insulin only increased Thr590 phosphorylation. Basal and contraction-stimulated TBC1D1 Ser231, Ser660 and Ser700 phosphorylation were greatly reduced in AMPKα2i TG mice, although contraction still elicited a small increase in phosphorylation. Akt2 KO mice had blunted insulin-stimulated TBC1D1 Thr590 phosphorylation. Contraction-stimulated TBC1D1 Ser231 and Ser660 phosphorylation were normal in high-fat-fed mice. Glucose uptake in vivo was significantly decreased in tibialis anterior muscles overexpressing TBC1D1 mutated on four predicted AMPK phosphorylation sites. In conclusion, contraction causes site-specific phosphorylation of TBC1D1 in skeletal muscle, and TBC1D1 phosphorylation on AMPK sites regulates contraction-stimulated glucose uptake. AMPK and Akt regulate TBC1D1 phosphorylation, but there must be additional upstream kinases that mediate TBC1D1 phosphorylation in skeletal muscle.
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
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?
In response to muscle contractions, increases in TBC1D1 phosphorylation are important for 14-3-3 binding, inhibition of GAP domain function and subsequent increases in glucose uptake.
“In response to muscle contractions, increases in TBC1D1 phosphorylation are important for 14-3-3 binding, inhibition of GAP domain function and subsequent increases in glucose uptake [95,102].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
TBC1D1 is phosphorylated in response to AICAR and muscle contractions/exercise.
“Like TBC1D4, TBC1D1 is phosphorylated in response to AICAR and muscle contractions/exercise [74,95,101,102,117].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
Muscle contractions/exercise predominantly induces TBC1D1 phosphorylation on S231 in both humans and mice.
“AMPK phosphorylates multiple sites on TBC1D1 (S231, S499, T590, S660, S700), and muscle contractions/exercise predominately induces TBC1D1 phosphorylation on S231 in both humans and mice [74,102,117].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
Inactivating 4 predicted TBC1D1 phosphorylation sites (4P mutant) results in 25% to 30% reduction in contraction-mediated glucose uptake.
“Interestingly, two separate studies inactivating 4 predicated TBC1D1 phosphorylation sites (4P mutant) results in 25% to 30% reduction in contraction-mediated glucose uptake [95,102].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
TBC1D1 expression is reduced by ~50% in skeletal muscle of AMPK α2 KO, α2 KD, α2iTg and β1β2 M-KO mice.
“In contrast, TBC1D1 expression is reduced by ~50% in skeletal muscle of AMPK α2 KO, α2 KD, α2iTg and β1β2 M-KO mice [30,74,102,117], and this may be compensatory for the lack of phosphorylation and inhibition by AMPK, or alternatively, reduced muscle glucose uptake in AMPK β1β2 M-KO mice.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
TBC1D1 T590 is predominantly phosphorylated in response to muscle contractions, but this has not been observed in all studies.
“TBC1D1 T590 is also predominately phosphorylated in response to muscle contractions [74]; however, this has not been observed in all studies [102].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
AMPK phosphorylates multiple sites on TBC1D1 (S231, S499, T590, S660, S700).
“AMPK phosphorylates multiple sites on TBC1D1 (S231, S499, T590, S660, S700), and muscle contractions/exercise predominately induces TBC1D1 phosphorylation on S231 in both humans and mice [74,102,117].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [102]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cho, H., Mu, J., Kim, J. K., Thorvaldsen, J. L., Chu, Q., Crenshaw, E. B., Kaestner, K. H., Bartolomei, M. S., Shulman, G. I., & Birnbaum, M. J. (2001) · Science · doi:10.1126/science.292.5522.1728 · Cited by 1,837 · see citing works
DeFronzo, R. A., Jacot, E., Jequier, E., Maeder, E., Wahren, J., & Felber, J. P. (1981) · Diabetes · doi:10.2337/diab.30.12.1000 · Cited by 1,770 · see citing works
Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., & Gygi, S. P. (2006) · Nature Biotechnology · doi:10.1038/nbt1240 · Cited by 1,577 · see citing works
Gene transfer into muscle by electroporation in vivo
Aihara, H., & Miyazaki, J. (1998) · Nature Biotechnology · doi:10.1038/nbt0998-867 · Cited by 945 · see citing works
Mu, J., Brozinick, J. T., Valladares, O., Bucan, M., & Birnbaum, M. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00251-9 · Cited by 924 · see citing works
Hayashi, T., Hirshman, M. F., Kurth, E. J., Winder, W. W., & Goodyear, L. J. (1998) · Diabetes · doi:10.2337/diab.47.8.1369 · Cited by 774 · see citing works
Self-citationHayashi, T., Hirshman, M. F., Kurth, E. J., Winder, W. W., & Goodyear, L. J. (1998) · Diabetes · doi:10.2337/diabetes.47.8.1369 · Cited by 774 · see citing works
Self-citationRates and tissue sites of non-insulin- and insulin-mediated glucose uptake in humans
Baron, A., Brechtel, G., Wallace, P., & Edelman, S. V. (1988) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1988.255.6.e769 · Cited by 645 · see citing works
Jørgensen, S. B., Viollet, B., Andreelli, F., Frøsig, C., Birk, J. B., Schjerling, P., Vaulont, S., Richter, E. A., & Wojtaszewski, J. F. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306205200 · Cited by 553 · see citing works
DeFronzo, R. A., Simonson, D. C., & Ferrannini, E. (1982) · Diabetologia · doi:10.1007/bf00253736 · Cited by 539 · see citing works
Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic
Sakamoto, K., & Holman, G. D. (2008) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90331.2008 · Cited by 481 · see citing works
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
Self-citationDale, S. J., Wilson, W. A., Edelman, A. M., & Hardie, D. G. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00172-6 · Cited by 324 · see citing works
Kramer, H. F., Witczak, C. A., Fujii, N., Jessen, N., Taylor, E. B., Arnolds, D. E., Sakamoto, K., Hirshman, M. F., & Goodyear, L. J. (2006) · Diabetes · doi:10.2337/db06-0150 · Cited by 315 · see citing works
Self-citationContraction signaling to glucose transport in skeletal muscle
Jessen, N., & Goodyear, L. J. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00175.2005 · Cited by 311 · see citing works
Self-citationPloug, T., van Deurs, B., Ai, H., Cushman, S. W., & Ralston, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.6.1429 · Cited by 302 · see citing works
Dohm, G. L., Tapscott, E. B., Pories, W. J., Dabbs, D. J., Flickinger, E. G., Meelheim, D., Fushiki, T., Atkinson, S., Elton, C. W., & Caro, J. F. (1988) · Journal of Clinical Investigation · doi:10.1172/jci113622 · Cited by 297 · see citing works
Insulin action on glucose transporters through molecular switches, tracks and tethers
Zaid, H., Antonescu, C. N., Randhawa, V. K., & Klip, A. (2008) · Biochemical Journal · doi:10.1042/bj20080723 · Cited by 286 · see citing works
AS160 Regulates Insulin- and Contraction-stimulated Glucose Uptake in Mouse Skeletal Muscle
Kramer, H. F., Witczak, C. A., Taylor, E. B., FUJII, N. L., Hirshman, M. F., & Goodyear, L. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605461200 · Cited by 285 · see citing works
Self-citationBruss, M. D., Arias, E. B., Lienhard, G. E., & Cartee, G. D. (2005) · Diabetes · doi:10.2337/diabetes.54.1.41 · Cited by 273 · see citing works
Taylor, E. B., An, D., Kramer, H. F., Yu, H., FUJII, N. L., Röckl, K. S. C., Bowles, N. P., Hirshman, M. F., Xie, J., Feener, E. P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708839200 · Cited by 268 · see citing works
Self-citationComplementary regulation of TBC1D1 and AS160 by growth factors, insulin and AMPK activators
Chen, S., Murphy, J. E., Toth, R. L., Campbell, D. G., MORRICE, N. A., & MacKintosh, C. (2007) · Biochemical Journal · doi:10.1042/bj20071114 · Cited by 207 · see citing works
Contraction Regulation of Akt in Rat Skeletal Muscle
Sakamoto, K., Hirshman, M. F., Aschenbach, W. G., & Goodyear, L. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112410200 · Cited by 192 · see citing works
Self-citationSubstrate specificity and effect on GLUT4 translocation of the Rab GTPase-activating protein Tbc1d1
Roach, W. G., Chavez, J. A., Mı̂inea, C. P., & Lienhard, G. E. (2007) · Biochemical Journal · doi:10.1042/bj20061798 · Cited by 192 · see citing works
Role of Akt substrate of 160 kDa in insulin-stimulated and contraction-stimulated glucose transport
Cartee, G. D., & Wojtaszewski, J. F. P. (2007) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/h07-026 · Cited by 183 · see citing works
Fujii, N., Hirshman, M. F., Kane, E. M., Ho, R. C., Peter, L. E., Seifert, M. M., & Goodyear, L. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504208200 · Cited by 177 · see citing works
Self-citationOakes, N. D., Bell-Anderson, K. S., Furler, S. M., Camilleri, S., Saha, A. K., Ruderman, N. B., Chisholm, D. J., & Kraegen, E. W. (1997) · Diabetes · doi:10.2337/diab.46.12.2022 · Cited by 176 · see citing works
Pehmøller, C., Treebak, J. T., Birk, J. B., Chen, S., MacKintosh, C., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00115.2009 · Cited by 171 · see citing works
Chavez, J. A., Roach, W. G., Keller, S. R., Lane, W. S., & Lienhard, G. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708934200 · Cited by 161 · see citing works
Splanchnic and muscle metabolism during exercise in NIDDM patients
Martin, I. K., Katz, A., & Wahren, J. (1995) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1995.269.3.e583 · Cited by 149 · see citing works
TBC1D1 Regulates Insulin- and Contraction-Induced Glucose Transport in Mouse Skeletal Muscle
An, D., Toyoda, T., Taylor, E. B., Yu, H., Fujii, N., Hirshman, M. F., & Goodyear, L. J. (2010) · Diabetes · doi:10.2337/db09-1266 · Cited by 147 · see citing works
Self-citationGlucoregulatory and metabolic response to exercise in obese noninsulin-dependent diabetes
Minuk, H. L., Vranic, M., Marliss, E. B., Hanna, A. K., Albisser, A. M., & Zinman, B. (1981) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1981.240.5.e458 · Cited by 142 · see citing works
Gene Transfer into Muscle by Electroporation In Vivo
Miyazaki, J., & Aihara, H. (2003) · Humana Press eBooks · doi:10.1385/1-59259-141-8:049 · Cited by 140 · see citing works
Muscle cells engage Rab8A and myosin Vb in insulin-dependent GLUT4 translocation
Ishikura, S., & Klip, A. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00277.2008 · Cited by 139 · see citing works
Exercise-Induced Increase in Glucose Transporters in Plasma Membranes of Rat Skeletal Muscle*
Douen, A. G., Ramlal, T., Klip, A., YOUNG, D. A., Cartee, G. D., & Holloszy, J. O. (1989) · Endocrinology · doi:10.1210/endo-124-1-449 · Cited by 135 · see citing works
Deshmukh, A. S., Coffey, V. G., Zhong, Z., Chibalin, A., Hawley, J. A., & Zierath, J. R. (2006) · Diabetes · doi:10.2337/db05-1419 · Cited by 126 · see citing works
Acute exercise increases the number of plasma membrane glucose transporters in rat skeletal muscle
Hirshman, M. F., Wallberg‐Henriksson, H., Wardzala, L. J., Horton, E. D., & Horton, E. S. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80486-1 · Cited by 113 · see citing works
Self-citationPeck, G. R., Chavez, J. A., Roach, W. G., Budnik, B. A., Lane, W. S., Karlsson, H. K. R., Zierath, J. R., & Lienhard, G. E. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.035568 · Cited by 95 · see citing works
Koh, H.-J., Toyoda, T., Fujii, N., Jung, M. M., Rathod, A., Middelbeek, R. J.-W., Lessard, S. J., Treebak, J. T., Tsuchihara, K., Esumi, H., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008131107 · Cited by 94 · see citing works
Self-citationRoy, D., & Marette, A. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.0860 · Cited by 89 · see citing works
Kinetics of Contraction-Induced GLUT4 Translocation in Skeletal Muscle Fibers From Living Mice
Lauritzen, H. P. M. M., Galbo, H., Toyoda, T., & Goodyear, L. J. (2010) · Diabetes · doi:10.2337/db10-0233 · Cited by 80 · see citing works
Self-citationFunai, K., & Cartee, G. D. (2009) · Diabetes · doi:10.2337/db08-1477 · Cited by 76 · see citing works
Lauritzen, H. P. M. M., Galbo, H., Brandauer, J., Goodyear, L. J., & Ploug, T. (2007) · Diabetes · doi:10.2337/db06-1578 · Cited by 70 · see citing works
Self-citationFunai, K., Schweitzer, G. G., Castorena, C. M., Kanzaki, M., & Cartee, G. D. (2010) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00758.2009 · Cited by 63 · see citing works
Kramer, H. F., Taylor, E. B., Witczak, C. A., FUJII, N. L., Hirshman, M. F., & Goodyear, L. J. (2007) · Diabetes · doi:10.2337/db07-0681 · Cited by 56 · see citing works
Self-citationOverexpression or ablation of JNK in skeletal muscle has no effect on glycogen synthase activity
FUJII, N. L., Boppart, M. D., Dufresne, S. D., Crowley, P. F., Jozsi, A. C., Sakamoto, K., Yu, H., Aschenbach, W. G., Kim, S., Miyazaki, H., et al. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00415.2003 · Cited by 53 · see citing works
Self-citationHigh-field fast-risetime pulse failures in 4H- and 6H-SiC pn junction diodes
Neudeck, P. G., & Fazi, C. (1996) · Journal of Applied Physics · doi:10.1063/1.362922 · Cited by 42 · see citing works
Dietary fat modifies exercise-dependent glucose transport in skeletal muscle
Liu, S., Baracos, V. E., Quinney, H. A., & Clandinin, M. T. (1996) · Journal of Applied Physiology · doi:10.1152/jappl.1996.80.4.1219 · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
AMPK in skeletal muscle function and metabolism
Kjøbsted, R., Hingst, J. R., Fentz, J., Foretz, M., Sanz, M.-N., Pehmøller, C. K., Shum, M., Marette, A., Mounier, R., Treebak, J. T., et al. (2017) · The FASEB Journal · doi:10.1096/fj.201700442r · Cited by 496 · 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
O'Neill, H. M., Maarbjerg, S. J., Crane, J. D., Jeppesen, J., Jørgensen, S. B., Schertzer, J. D., Shyroka, O., Kiens, B., van Denderen, B. J., Tarnopolsky, M. A., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105062108 · Cited by 406 · see citing works
Exercise and type 2 diabetes: molecular mechanisms regulating glucose uptake in skeletal muscle
Stanford, K. I., & Goodyear, L. J. (2014) · AJP Advances in Physiology Education · doi:10.1152/advan.00080.2014 · Cited by 346 · see citing works
Self-citationGLUT4 Mobilization Supports Energetic Demands of Active Synapses
Ashrafi, G., Wu, Z., Farrell, R. J., & Ryan, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.020 · Cited by 320 · see citing works
AMPK and Exercise: Glucose Uptake and Insulin Sensitivity
O'Neill, H. M. (2013) · Diabetes & Metabolism Journal · doi:10.4093/dmj.2013.37.1.1 · Cited by 295 · see citing works
Enhanced muscle insulin sensitivity after contraction/exercise is mediated by AMPK
Kjøbsted, R., Munk-Hansen, N., Birk, J. B., Foretz, M., Viollet, B., Björnholm, M., Zierath, J. R., Treebak, J. T., & Wojtaszewski, J. F. P. (2017) · Diabetes · doi:10.2337/db16-0530 · Cited by 178 · see citing works
Zong, Y., Zhang, C., Li, M., Wang, W., Wang, Z., Hawley, S. A., Ma, T., Feng, J.-W., Tian, X., Qu, Q., et al. (2019) · Cell Research · doi:10.1038/s41422-019-0163-6 · Cited by 167 · see citing works
Roles of TBC1D1 and TBC1D4 in insulin- and exercise-stimulated glucose transport of skeletal muscle
Cartee, G. D. (2014) · Diabetologia · doi:10.1007/s00125-014-3395-5 · Cited by 153 · see citing works
Exercise and regulation of carbohydrate metabolism
Mul, J. D., Stanford, K. I., Hirshman, M. F., & Goodyear, L. J. (2015) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2015.07.020 · Cited by 151 · see citing works
Self-citationKjøbsted, R., Treebak, J. T., Fentz, J., Lantier, L., Viollet, B., Birk, J. B., Schjerling, P., Björnholm, M., Zierath, J. R., & Wojtaszewski, J. F. P. (2014) · Diabetes · doi:10.2337/db14-1402 · Cited by 135 · see citing works
Pusswald, G., Tropper, E., Kryspin-Exner, I., Moser, D., Klug, S., Auff, E., Dal-Bianco, P., & Lehrner, J. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150284 · Cited by 85 · see citing works
Human muscle fibre type‐specific regulation of AMPK and downstream targets by exercise
Steenberg, D. E., Albers, P. H., Prats, C., Baba, O., Birk, J. B., & Wojtaszewski, J. F. P. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.283267 · Cited by 118 · see citing works
Rab8a as a mitochondrial receptor for lipid droplets in skeletal muscle
Ouyang, Q., Chen, Q., Ke, S., Ding, L., Yang, X., Rong, P., Feng, W., Cao, Y., Wang, Q., Li, M., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.01.007 · Cited by 116 · see citing works
Treebak, J. T., Pehmøller, C., Kristensen, J. M., Kjøbsted, R., Birk, J. B., Schjerling, P., Richter, E. A., Goodyear, L. J., & Wojtaszewski, J. F. P. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2013.266338 · Cited by 113 · see citing works
Self-citationInfluence of Acute and Chronic Exercise on Glucose Uptake
Röhling, M., Herder, C., Stemper, T., & Müssig, K. (2016) · Journal of Diabetes Research · doi:10.1155/2016/2868652 · Cited by 108 · see citing works
Current understanding of increased insulin sensitivity after exercise – emerging candidates
Maarbjerg, S. J., Sylow, L., & Richter, E. A. (2011) · Acta Physiologica · doi:10.1111/j.1748-1716.2011.02267.x · Cited by 104 · see citing works
AMPK and TBC1D1 Regulate Muscle Glucose Uptake After, but Not During, Exercise and Contraction
Kjøbsted, R., Roll, J. L. W., Jørgensen, N. O., Birk, J. B., Foretz, M., Viollet, B., Chadt, A., Al-Hasani, H., & Wojtaszewski, J. F. P. (2019) · Diabetes · doi:10.2337/db19-0050 · Cited by 97 · see citing works
Lee, J. O., Lee, H. J., Lee, Y. W., Han, J. A., Kang, M. J., Moon, J., Shin, M.-J., Lee, H. J., Chung, J. H., Lee, J., et al. (2020) · FEBS Journal · doi:10.1111/febs.15301 · Cited by 97 · see citing works
Interactive Roles for AMPK and Glycogen from Cellular Energy Sensing to Exercise Metabolism
Janzen, N. R., Whitfield, J., & Hoffman, N. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113344 · Cited by 86 · see citing works
Fentz, J., Kjøbsted, R., Birk, J. B., Jordy, A. B., Jeppesen, J. F., Thorsen, K., Schjerling, P., Kiens, B., Jessen, N., Viollet, B., et al. (2015) · The FASEB Journal · doi:10.1096/fj.14-266650 · Cited by 82 · see citing works
Self-citationSkeletal muscle nitric oxide signaling and exercise: a focus on glucose metabolism
McConell, G. K., Rattigan, S., Lee, R. S., Wadley, G. D., & Merry, T. L. (2012) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00667.2011 · Cited by 83 · see citing works
Kjøbsted, R., Pedersen, A. J. T., Hingst, J. R., Sabaratnam, R., Birk, J. B., Kristensen, J. M., Højlund, K., & Wojtaszewski, J. F. P. (2016) · Diabetes · doi:10.2337/db15-1034 · Cited by 75 · see citing works
Vendelbo, M. H., Clasen, B. F., Treebak, J. T., Møller, L. L. V., Krusenstjerna-Hafstrøm, T., Madsen, M. A., Nielsen, T. S., Stødkilde‐Jørgensen, H., Pedersen, S. B., Jørgensen, J. O. L., et al. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00207.2011 · Cited by 75 · see citing works
Self-citationHan, X., Møller, L. L. V., Groote, E. D., Bojsen-Møller, K. N., Davey, J. R., Henríquez‐Olguín, C., Li, Z., Knudsen, J. R., Jensen, T. E., Madsbad, S., et al. (2019) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12474 · Cited by 73 · see citing works
Glucose transporters in cardiovascular system in health and disease
Bertrand, L., Auquier, J., Renguet, E., Angé, M., Cumps, J., Horman, S., & Beauloye, C. (2020) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-020-02444-8 · Cited by 71 · see citing works
Exercise increases TBC1D1 phosphorylation in human skeletal muscle
Jessen, N., An, D., Lihn, A. S., Nygren, J., Hirshman, M. F., Thorell, A., & Goodyear, L. J. (2011) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00042.2011 · Cited by 67 · see citing works
Self-citationTBC1D4 Is Necessary for Enhancing Muscle Insulin Sensitivity in Response to AICAR and Contraction
Kjøbsted, R., Chadt, A., Eskesen, N. O., Kido, K., Larsen, J. K., de Wendt, C., Al‐Hasani, H., & Wojtaszewski, J. F. P. (2019) · Diabetes · doi:10.2337/db18-0769 · Cited by 62 · see citing works
Endurance exercise training-responsive miR-19b-3p improves skeletal muscle glucose metabolism
Massart, J., Sjögren, R. J. O., Egan, B., Garde, C., Lindgren, M., Gu, W.-F., Ferreira, D. M., Katayama, M., Ruas, J., Barrès, R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26095-0 · Cited by 51 · see citing works
Hingst, J. R., Kjøbsted, R., Birk, J. B., Eskesen, N. O., Larsen, M. R., Kido, K., Larsen, J. K., Kjeldsen, S. A. S., Fentz, J., Frøsig, C., et al. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.101028 · Cited by 54 · see citing works
Exercise and Insulin Resistance
Whillier, S. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1792-1_9 · Cited by 53 · see citing works
Redox signaling and skeletal muscle adaptation during aerobic exercise
Zhou, Y., Zhang, X., Baker, J. S., Davison, G. W., & Yan, X. (2024) · iScience · doi:10.1016/j.isci.2024.109643 · Cited by 52 · see citing works
Weikel, K., Ruderman, N. B., & Cacicedo, J. M. (2016) · Metabolism · doi:10.1016/j.metabol.2016.01.005 · Cited by 49 · see citing works
Viollet, B., & Foretz, M. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3 · Cited by 47 · see citing works
Hormones, Metabolism and the Benefits of Exercise
(2017) · Research and Perspectives in Endocrine Interactions · doi:10.1007/978-3-319-72790-5 · Cited by 44 · see citing works
Li, Z., Yue, Y., Hu, F., Zhang, C., Ma, X., Li, N., Qiu, L., Fu, M., Chen, L., Yao, Z., et al. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00103.2017 · Cited by 44 · see citing works
Stocks, B., & Zierath, J. R. (2021) · Endocrine Reviews · doi:10.1210/endrev/bnab038 · Cited by 43 · see citing works
Insulin stimulation regulates AS160 and TBC1D1 phosphorylation sites in human skeletal muscle
Middelbeek, R. J. W., Chambers, M. A., Tantiwong, P., Treebak, J. T., An, D., Hirshman, M. F., Musi, N., & Goodyear, L. J. (2013) · Nutrition and Diabetes · doi:10.1038/nutd.2013.13 · Cited by 40 · see citing works
Self-citationMafakheri, S., FLÖRKE, R., Kanngießer, S., Hartwig, S., Espelage, L., de Wendt, C., Schönberger, T., Hamker, N., Lehr, S., Chadt, A., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005040 · Cited by 40 · see citing works
Cheng, K. K. Y., Zhu, W., Chen, B., Wang, Y., Wu, D., Sweeney, G., Wang, B., Lam, K. S. L., & Xu, A. (2014) · Diabetes · doi:10.2337/db14-0337 · Cited by 39 · see citing works
de Wendt, C., Espelage, L., Eickelschulte, S., Springer, C. A., Toska, L., Scheel, A. K., Bedou, A. D., Benninghoff, T., Cames, S., Stermann, T., et al. (2021) · Diabetes · doi:10.2337/db21-0587 · Cited by 39 · see citing works
Hu, F., Li, N., Li, Z., Zhang, C., Yue, Y., Liu, Q., Chen, L., Bilan, P. J., & Niu, W. (2018) · FEBS Letters · doi:10.1002/1873-3468.12982 · Cited by 38 · see citing works
Vendelbo, M. H., Møller, A. B., Treebak, J. T., Gormsen, L. C., Goodyear, L. J., Wojtaszewski, J. F. P., Jørgensen, J. O. L., Møller, N., & Jessen, N. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00044.2014 · Cited by 34 · see citing works
Self-citationThe Energy Sensor AMPK: Adaptations to Exercise, Nutritional and Hormonal Signals
Viollet, B. (2017) · Research and perspectives in endocrine interactions · doi:10.1007/978-3-319-72790-5_2 · Cited by 33 · see citing works
Peifer‐Weiß, L., Al‐Hasani, H., & Chadt, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031910 · Cited by 34 · see citing works
AMPK activator O304 improves metabolic and cardiac function, and exercise capacity in aged mice
Ericsson, M., Steneberg, P., Nyrén, R., & Edlund, H. (2021) · Communications Biology · doi:10.1038/s42003-021-02837-0 · Cited by 30 · see citing works
Mo, Z., Li, L., Hai-wen, Y., Wu, Y., & Li, H. (2019) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2019.01.001 · Cited by 29 · see citing works
Wang, H., Arias, E. B., Pataky, M. W., Goodyear, L. J., & Cartee, G. D. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00020.2018 · Cited by 26 · see citing works
Self-citationAMPKγ3 Controls Muscle Glucose Uptake in Recovery From Exercise to Recapture Energy Stores
Kido, K., Eskesen, N. O., Henriksen, N. S., Onslev, J., Kristensen, J. M., Larsen, M. R., Hingst, J. R., Knudsen, J. R., Birk, J. B., Andersen, N. R., et al. (2023) · Diabetes · doi:10.2337/db23-0358 · Cited by 25 · see citing works
TBC1D1 interacting proteins, VPS13A and VPS13C, regulate GLUT4 homeostasis in C2C12 myotubes
Hook, S. C., Chadt, A., Heesom, K. J., Kishida, S., Al‐Hasani, H., Tavaré, J. M., & Thomas, E. C. (2020) · Scientific Reports · doi:10.1038/s41598-020-74661-1 · Cited by 25 · see citing works
Role of AMP-Activated Protein Kinase for Regulating Post-exercise Insulin Sensitivity
Kjøbsted, R., Wojtaszewski, J. F. P., & Treebak, J. T. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_5 · Cited by 26 · see citing works
Wang, H., Sharma, N., Arias, E. B., & Cartee, G. D. (2015) · The Journals of Gerontology Series A · doi:10.1093/gerona/glv142 · Cited by 24 · see citing works
A muscle-specific UBE2O/AMPKα2 axis promotes insulin resistance and metabolic syndrome in obesity
Vila, I. K., Park, M. K., Setijono, S. R., Yao, Y., Kim, H., Badin, P.-M., Choi, S., Narkar, V. A., Choi, S., Chung, J., et al. (2019) · JCI Insight · doi:10.1172/jci.insight.128269 · Cited by 23 · see citing works
Hatakeyama, H., & Kanzaki, M. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-10-0725 · Cited by 22 · see citing works
Tobias, I. S., Lazauskas, K. K., Siu, J. W., Costa, P. B., Coburn, J. W., & Galpin, A. J. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00704.2019 · Cited by 22 · see citing works
Wang, H., Arias, E. B., & Cartee, G. D. (2016) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00449.2015 · Cited by 21 · see citing works
TBC1D1 reduces palmitate oxidation by inhibiting β-HAD activity in skeletal muscle
Maher, A. C., McFarlan, J. T., Lally, J., Snook, L. A., & Bonen, A. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00014.2014 · Cited by 19 · see citing works
Hinkley, J. M., Ferey, J. L. A., Brault, J. J., Smith, C. A. S., Gilliam, L. A. A., & Witczak, C. A. (2013) · Diabetes · doi:10.2337/db13-0452 · Cited by 18 · see citing works
Iwabe, M., Kawamoto, E., Koshinaka, K., & Kawanaka, K. (2014) · Physiological Reports · doi:10.14814/phy2.12162 · Cited by 17 · see citing works
Kakehi, S., Tamura, Y., Ikeda, S., Kaga, N., Taka, H., Ueno, N., Shiuchi, T., Kubota, A., Sakuraba, K., Kawamori, R., et al. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00254.2020 · Cited by 16 · see citing works
Kristensen, J. M., Kjøbsted, R., Larsen, T. J., Carl, C. S., Hingst, J. R., Onslev, J., Birk, J. B., Thorup, A., Steenberg, D. E., Knudsen, J. R., et al. (2024) · Nature Metabolism · doi:10.1038/s42255-024-01153-1 · Cited by 17 · see citing works
Muscle injury, impaired muscle function and insulin resistance in Chromogranin A-knockout mice
Tang, K., Pasqua, T., Biswas, A., Mahata, S., Tang, J., Tang, A., Bandyopadhyay, G. K., Sinha‐Hikim, A. P., Chi, N., Webster, N. J. G., et al. (2016) · Journal of Endocrinology · doi:10.1530/joe-16-0370 · Cited by 15 · see citing works
Knudsen, J. R., Henríquez‐Olguín, C., Li, Z., & Jensen, T. E. (2019) · Experimental Physiology · doi:10.1113/ep087545 · Cited by 15 · see citing works
Hong, Y. H., Yang, C., Betik, A. C., Lee, R. S., & McConell, G. K. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00513.2015 · Cited by 15 · see citing works
Tbc1d1 deletion suppresses obesity in leptin-deficient mice
Dokas, J., Chadt, A., Joost, H., & Al‐Hasani, H. (2016) · International Journal of Obesity · doi:10.1038/ijo.2016.45 · Cited by 14 · see citing works
Mann, G., Riddell, M. C., & Adegoke, O. A. J. (2022) · Diabetology · doi:10.3390/diabetology3030032 · Cited by 14 · see citing works
Kawamoto, E., Koshinaka, K., Yoshimura, T., Masuda, H., & Kawanaka, K. (2016) · Physiological Reports · doi:10.14814/phy2.12876 · Cited by 13 · see citing works
Viollet, B., & Foretz, M. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_18 · Cited by 13 · see citing works
Furuzono, S., Kubota, T., Taura, J., Konishi, M., Naito, A., Tsutsui, M., Karasawa, H., Kubota, N., & Kadowaki, T. (2021) · Communications Biology · doi:10.1038/s42003-021-02491-6 · Cited by 11 · see citing works
Legrand, M. A., Jourdan, M., & Pinieux, G. D. B. D. (2023) · PubMed · doi:10.14670/hh-18-532 · Cited by 11 · see citing works
Møller, C. L., Kjøbsted, R., Enriori, P. J., Jensen, T. E., Garcia‐Rudaz, C., Litwak, S. A., Raun, K., Wojtaszewski, J. F. P., Wulff, B. S., & Cowley, M. A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157027 · Cited by 11 · see citing works
Arcaro, A., Lepore, A., Cetrangolo, G. P., Paventi, G., Ames, P. R. J., & Gentile, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167787 · Cited by 10 · see citing works
Petrocelli, J. J., Liu, J., Yee, E. M., Ferrara, P. J., Bourrant, P., de Hart, N. M. M. P., Tatum, S. M., Holland, W. J., Funai, K., & Drummond, M. J. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00261.2023 · Cited by 10 · see citing works
Wang, Q., Rong, P., Zhang, W., Yang, X., Chen, L., Cao, Y., Liu, M., Feng, W., Ouyang, Q., Chen, Q., et al. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2628-1 · Cited by 9 · see citing works
Takahashi, Y., Matsunaga, Y., Banjo, M., Takahashi, K., Sato, Y., Seike, K., Nakano, S., & Hatta, H. (2019) · Nutrients · doi:10.3390/nu11112555 · Cited by 9 · see citing works
Radhakrishnan, J., Baetiong, A., Kaufman, H., Huynh, M. L., Leschinsky, A., Fresquez, A. M., White, C., DiMario, J. X., & Gazmuri, R. J. (2019) · The FASEB Journal · doi:10.1096/fj.201802238r · Cited by 9 · see citing works
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 · see citing works
Chou, C., & Barton, E. R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241511950 · Cited by 6 · see citing works
Wang, H., Zheng, A., Arias, E. B., & Cartee, G. D. (2022) · FACETS · doi:10.1139/facets-2021-0166 · Cited by 5 · see citing works
Effect of resistance exercise on insulin sensitivity of skeletal muscle
Wang, B., Luo, X. W., Li, R., Li, Y., & Zhao, Y. (2021) · World Journal of Meta-Analysis · doi:10.13105/wjma.v9.i2.101 · Cited by 4 · see citing works
Ferraretti, G., Abondio, P., Alberti, M., Dezi, A., Sherpa, P. T., Cocco, P., Tiriticco, M., Marcello, M. D., Gnecchi‐Ruscone, G. A., Natali, L., et al. (2024) · eLife · doi:10.7554/elife.89815.3 · Cited by 4 · see citing works
Secreted EMC10 inhibits muscle GLUT4 activity and glucose uptake in mice
Jin, S., Wu, W., Liu, S., Wang, Y., Huang, Q., He, K., Ni, Y., Chen, K., Huang, J., Liu, L., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110296 · Cited by 4 · see citing works
Meteorin-like (Metrnl) adipomyokine improves glucose tolerance in type 2 diabetes via AMPK pathwayPreprint
Lee, J. O., Lee, H. J., Lee, Y. W., Han, J. A., Kang, M. J., Moon, J., Shin, M., Lee, H. J., Chung, J. H., Lee, J., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/420489 · Cited by 4 · see citing works
The role of 5′-adenosine monophosphate-activated protein kinase (AMPK) in skeletal muscle atrophy
Dang, K., Farooq, H. M. U., GAO, Y., Deng, X., & Qian, A. (2022) · Biocell · doi:10.32604/biocell.2023.023766 · Cited by 3 · see citing works
Ferraretti, G., Abondio, P., Alberti, M., Dezi, A., Sherpa, P. T., Cocco, P., Tiriticco, M., Marcello, M. D., Gnecchi‐Ruscone, G. A., Natali, L., et al. (2023) · eLife · doi:10.7554/elife.89815 · Cited by 3 · see citing works
Vidal, P., Janzen, N. R., & Brozinick, J. T. (2025) · Skeletal Muscle · doi:10.1186/s13395-025-00405-2 · Cited by 2 · see citing works
AMPK signaling in cancer: dual roles, molecular mechanisms, and therapeutic potential
Dërmaku‐Sopjani, M., Morina, R., Sermaxhaj, F., Kurti, F., Latifi, J., & Sopjani, M. (2026) · Advances in Medical Sciences · doi:10.1016/j.advms.2026.05.001 · Cited by 2 · see citing works
Radhakrishnan, J., Baetiong, A., & Gazmuri, R. J. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2021.756659 · Cited by 2 · see citing works
Han, X., Møller, L. L. V., Groote, E. D., Bojsen-Møller, K. N., Davey, J., Henríquez-Olguin, C., Li, Z., Knudsen, J. R., Jensen, T. E., Madsbad, S., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/568097 · Cited by 2 · see citing works
Satoh, T. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.111979 · Cited by 1 · see citing works
A role for ataxia telangiectasia mutated in insulin-independent stimulation of glucose transport.
Spears, L. D., Renth, A. L., McKuin, M. R., Kennedy, A. R., Andrisse, S., Briggs, N. E., & Fisher, J. S. (2017) · PubMed · Cited by 1 · see citing works
Molecular Review: Effects of Physical Exercise in Skeletal Muscle Glucose Uptake
Rahmi, . (2021) · Sumatera Medical Journal · doi:10.32734/sumej.v4i1.4785 · Cited by 1 · see citing works
Ferraretti, G., Abondio, P., Alberti, M., Dezi, A., Sherpa, P. T., Cocco, P., Tiriticco, M., Marcello, M. D., Gnecchi‐Ruscone, G. A., Natali, L., et al. (2024) · eLife · doi:10.7554/elife.89815.2 · Cited by 1 · see citing works
Influence of protein nutrition and exercise on muscle metabolism.
Breen, L. (2011) · University of Birmingham Institutional Research Archive (University of Birmingham)
McConell, G. K., Rattigan, S., Lee, R. S., Wadley, G. D., & Merry, T. L. (2012)
Effects of Postmeal Walking on Postprandial Glucose Control and Oxidative Stress
Knurick, J. R. (2015)
Role of Exercise in NAFLD/NASH: What is the Right Prescription?
Bertot, L. C., & Adams, L. A. (2017) · Current Hepatology Reports · doi:10.1007/s11901-017-0374-6
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 GLUT4 mobilization supports energetic demands of active synapses.
Chapman, E. R., & Vevea, J. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727228790.793544965
- Authors
- Vichaiwong, K., Purohit, S., An, D., Toyoda, T., Jessen, N., Hirshman, M. F., & Goodyear, L. J.
- Affiliations
- Joslin Diabetes Center (US)
- Research Division, Joslin Diabetes Center, One Joslin Place, Boston, MA 02215, U.S.A.
- Brigham and Women's Hospital (US)
- Corresponding author
- Vichaiwong, Kanokwan
- Purohit, Suneet
- An, Ding
- Jessen, Niels
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2010-09-28
- Volume
- 431
- Issue
- 2
- Pages
- 311-320
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2947193
- OpenAlex
- W2058860541
- Cited by
- 102
- References
- 48
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 6 · 2023: 6 · 2022: 4 · 2021: 8 · 2020: 7 · 2019: 11 · 2018: 6 · 2017: 7 · 2016: 14 · 2015: 6 · 2014: 7 · 2013: 6 · 2012: 2
- FWCI
- 1.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Biochemical Journal (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- American Diabetes Association
- University of Pennsylvania
- Joslin Diabetes Center (P30DK36836)
- Uehara Memorial Foundation
- Thailand Research Fund
- Royal Golden Jubilee (RGJ) Ph.D. Programme
- National Institutes of Health (DK 36836)
- Canadian Institutes of Health Research (83802_1)
- Japan Society for the Promotion of Science
- National Institute of Diabetes and Digestive and Kidney Diseases (T32DK007260, P30DK036836)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR042238, R01AR045670)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Keywords
- TBC1D1, skeletal muscle contraction, AMPK phosphorylation, Akt2 phosphorylation, site-specific phosphorylation, muscle glucose uptake, AMPKα2, insulin signaling, AICAR, high-fat feeding, tibialis anterior, skeletal muscle glucose metabolism
- MeSH terms
- Aminoimidazole Carboxamide, Animals, Dietary Fats, Glucose, Insulin, Muscle Contraction, Mutation, Nuclear Proteins, Phosphorylation, Phosphoserine, Ribonucleotides, Consensus Sequence, Muscle, Skeletal, GTPase-Activating Proteins, Antibodies, Phospho-Specific, Mutant Proteins, Proto-Oncogene Proteins c-akt, Mice, AMP-Activated Protein Kinases, In Vitro Techniques
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
