Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle

Chopra, I.; Li, H. F.; Wang, H.; Webster, K. A.

doi:10.1007/s00125-011-2407-y

Cited by 117Metabolism, Diabetes, and CancerPI3K/AKT/mTOR signaling in cancerProtein Kinase Regulation and GTPase Signaling

Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle

Open access

Chopra, I., Li, H. F., Wang, H., Webster, K. A.·2012·Diabetologia

DOI 10.1007/s00125-011-2407-yPMC PMC4648248

Open this paper in CoChat — free account Open PDF

Abstract

Aims/hypothesis Muscle may experience hypoglycaemia during ischaemia or insulin infusion. During severe hypoglycaemia energy production is blocked, and an increase of AMP:ATP activates the energy sensor and putative insulin-sensitiser AMP-activated protein kinase (AMPK). AMPK promotes energy conservation and survival by shutting down anabolism and activating catabolic pathways. We investigated the molecular mechanism of a unique glucose stress defence pathway involving AMPK-dependent, insulin-independent activation of the insulin signalling pathway.Methods Cardiac or skeletal myocytes were subjected to glucose and insulin-free incubation for increasing intervals up to 20 h. AMPK, and components of the insulin signalling pathway and their targets were quantified by western blot using phosphor-specific antibodies. Phosphomimetics were used to determine the function of IRS-1 Ser789 phosphorylation and in vitro [³²P]ATP kinase assays were used to measure the phosphorylation of the purified insulin receptor by AMPK.Results Glucose deprivation increased Akt-Thr308 and Akt-Ser473 phosphorylation by almost tenfold. Phosphorylation of glycogen synthase kinase 3 beta increased in parallel, but phosphorylation of ribosomal 70S subunit-S6 protein kinase and mammalian target of rapamycin decreased. AMPK inhibitors blocked and aminoimidazole carboxamide ribonucleotide (AICAR) mimicked the effects of glucose starvation. Glucose deprivation increased the phosphorylation of IRS-1 on serine-789, but phosphomimetics revealed that this conferred negative regulation. Glucose deprivation enhanced tyrosine phosphorylation of IRS-1 and the insulin receptor, effects that were blocked by AMPK inhibition and mimicked by AICAR. In vitro kinase assays using purified proteins confirmed that the insulin receptor is a direct target of AMPK.Conclusions/interpretation AMPK phosphorylates and activates the insulin receptor, providing a direct link between AMPK and the insulin signalling pathway; this pathway promotes energy conservation and survival of muscle exposed to severe glucose deprivation.

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/s00125-011-2407-y

Cites

51 of 51 references verified0 citation errors · 0 not checkable

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?

IRS1 S789 phosphorylation is negatively associated with insulin signaling.
“Alternative studies show that IRS1 S789 phosphorylation is negatively associated with insulin signaling [146-149].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [146]
Activation of AMPK by glucose deprivation or AICAR promotes tyrosine phosphorylation of IR and IRS-1 as well as Akt T308 and S473 phosphorylation.
“Instead, activation of AMPK by glucose deprivation or AICAR promotes tyrosine phosphorylation of IR and IRS-1 as well as Akt T308 and S473 phosphorylation [146].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [146]
AMPK was found to phosphorylate the IR in response to glucose deprivation; conditions that also suppresses mTOR activity.
“Recently, AMPK was found to phosphorylate the IR in response to glucose deprivation; conditions that also suppresses mTOR activity [146].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [146]

Self-check

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

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

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
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849 · see citing works
Anorexigenic and Orexigenic Hormone Modulation of Mammalian Target of Rapamycin Complex 1 Activity and the Regulation of Hypothalamic Agouti-Related Protein mRNA Expression
Watterson, K. R., Bestow, D., Gallagher, J. R., Hamilton, D. L., Ashford, F. B., Meakin, P. J., & Ashford, M. L. J. (2012) · Neurosignals · doi:10.1159/000334144 · Cited by 3,395 · see citing works
Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
Um, S. H., Frigerio, F., Watanabe, M., Picard, F., Joaquin, M., Sticker, M., Fumagalli, S., Allegrini, P. R., Kozma, S. C., Auwerx, J., et al. (2004) · Nature · doi:10.1038/nature02866 · Cited by 1,677 · see citing works
AMPK in Health and Disease
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,633 · see citing works
Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway
Manning, B. D., Tee, A. R., Logsdon, M. N., Blenis, J., & Cantley, L. C. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00568-3 · Cited by 1,555 · see citing works
AMP-Activated Protein Kinase in Metabolic Control and Insulin Signaling
Towler, M. C., & Hardie, D. G. (2007) · Circulation Research · doi:10.1161/01.res.0000256090.42690.05 · Cited by 1,248 · see citing works
AMPK: An Emerging Drug Target for Diabetes and the Metabolic Syndrome
Zhang, B. B., Zhou, G., & Li, C. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.012 · Cited by 1,028 · see citing works
Positive and negative regulation of insulin signaling through IRS-1 phosphorylation
Gual, P., Le Marchand-Brustel, Y., & Tanti, J.-F. (2005) · Biochimie · doi:10.1016/j.biochi.2004.10.019 · Cited by 912 · cited 1× · see citing works
“Although positive regulatory IRS-1-Ser/Thr sites have been reported [11, 17, 48, 49], none of these sites contain sequences with significant homology to the AMPK consensus.”
AMP-Activated Protein Kinase – Development of the Energy Sensor Concept
Hardie, D. G., Hawley, S. A., & Scott, J. W. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2006.108944 · Cited by 813 · see citing works
Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1
Um, S. H., D'Alessio, D., & Thomas, G. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.05.003 · Cited by 690 · see citing works
Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
Hahn-Windgassen, A., Nogueira, V., Chen, C.-C., Skeen, J. E., Sonenberg, N., & Hay, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502876200 · Cited by 539 · see citing works
Insulin receptor phosphorylation, insulin receptor substrate-1 phosphorylation, and phosphatidylinositol 3-kinase activity are decreased in intact skeletal muscle strips from obese subjects.
Goodyear, L. J., Giorgino, F., Sherman, L., Carey, J., Smith, R. J., & Dohm, G. L. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117909 · Cited by 525 · see citing works
Hypoxia and acidosis activate cardiac myocyte death through the Bcl-2 family protein BNIP3
Kubasiak, L. A., Hernandez, O. M., Bishopric, N. H., & Webster, K. A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202474099 · Cited by 438 · see citing works
Self-citation
Restraining PI3K: mTOR signalling goes back to the membrane
Harrington, L. S., Findlay, G. M., & Lamb, R. F. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2004.11.003 · Cited by 362 · see citing works
AMP-Activated Protein Kinase in the Heart
Arad, M., Seidman, C. E., & Seidman, J. G. (2007) · Circulation Research · doi:10.1161/01.res.0000258446.23525.37 · Cited by 356 · see citing works
Role of Glycogen Synthase Kinase-3β in Cardioprotection
Juhaszova, M., Zorov, D. B., Yaniv, Y., Nuss, H. B., Wang, S., & Sollott, S. J. (2009) · Circulation Research · doi:10.1161/circresaha.109.197996 · Cited by 353 · see citing works
Insulin Antagonizes Ischemia-induced Thr172 Phosphorylation of AMP-activated Protein Kinase α-Subunits in Heart via Hierarchical Phosphorylation of Ser485/491
Horman, S., Vertommen, D., Heath, R. B., Neumann, D., Mouton, V., Woods, A., Schlattner, U., Wallimann, T., Carling, D., Hue, L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506850200 · Cited by 345 · see citing works
Ser/Thr Phosphorylation of IRS Proteins: A Molecular Basis for Insulin Resistance
Zick, Y. (2005) · Science s STKE · doi:10.1126/stke.2682005pe4 · Cited by 320 · see citing works
Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity.
Bollag, G. E., Roth, R. A., Beaudoin, J. D., Mochly‐Rosen, D., & Koshland, D. E. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.16.5822 · Cited by 273 · see citing works
Convergent signal transduction pathways controlling cardiomyocyte survival and function: the role of PI 3-kinase and Akt
Matsui, T., & Rosenzweig, A. (2004) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2004.11.005 · Cited by 263 · see citing works
5′-AMP-activated Protein Kinase Phosphorylates IRS-1 on Ser-789 in Mouse C2C12 Myotubes in Response to 5-Aminoimidazole-4-carboxamide Riboside
Jakobsen, S. N., Hardie, D. G., Morrice, N., & Tornqvist, H. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100483200 · Cited by 238 · cited 1× · see citing works
“Whereas positive regulation by Ser789 has been suggested [20], such positive regulation has not been confirmed, and in light of more recent studies including the results described here, it seems likely that Ser789 exerts only negative regulation of IRS-1 [18, 19, 21, 22].”
Insulin Resistance in Obesity as the Underlying Cause for the Metabolic Syndrome
Gallagher, E. J., LeRoith, D., & Karnieli, E. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20212 · Cited by 236 · see citing works
Glucose transport in the heart
Abel, E. D. (2004) · Frontiers in bioscience · doi:10.2741/1216 · Cited by 234 · see citing works
Metformin and rapamycin have distinct effects on the AKT pathway and proliferation in breast cancer cells
Zakikhani, M., Blouin, M.-J., Piura, E., & Pollak, M. N. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-0763-9 · Cited by 213 · see citing works
Nuclear Targeting of Akt Enhances Kinase Activity and Survival of Cardiomyocytes
Shiraishi, I., Melendez, J., Ahn, Y., Skavdahl, M., Murphy, E., Welch, S., Schaefer, E., Walsh, K., Rosenzweig, A., Torella, D., et al. (2004) · Circulation Research · doi:10.1161/01.res.0000124394.01180.be · Cited by 212 · see citing works
Modulation of Insulin-stimulated Degradation of Human Insulin Receptor Substrate-1 by Serine 312 Phosphorylation
Greene, M. W., Sakaue, H., Wang, L., Alessi, D. R., & Roth, R. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209153200 · Cited by 201 · see citing works
Tyr612 and Tyr632 in Human Insulin Receptor Substrate-1 Are Important for Full Activation of Insulin-Stimulated Phosphatidylinositol 3-Kinase Activity and Translocation of GLUT4 in Adipose Cells
Esposito, D. L., Li, Y., Cama, A., & Quon, M. J. (2001) · Endocrinology · doi:10.1210/endo.142.7.8283 · Cited by 161 · see citing works
Adipose-specific Expression, Phosphorylation of Ser794 in Insulin Receptor Substrate-1, and Activation in Diabetic Animals of Salt-inducible Kinase-2
Horike, N., Takemori, H., Katoh, Y., Doi, J., Min, L., Asano, T., Sun, X. J., Yamamoto, H., Kasayama, S., Muraoka, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211770200 · Cited by 161 · see citing works
TSC1–TSC2: a complex tale of PKB-mediated S6K regulation
McManus, E. J., & Alessi, D. R. (2002) · Nature Cell Biology · doi:10.1038/ncb0902-e214 · Cited by 153 · see citing works
AKT Signaling in Physiology and Disease
Vasudevan, K. M., & Garraway, L. A. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_66 · Cited by 131 · see citing works
Phosphorylation of Purified Insulin Receptor by cAMP Kinase
Roth, R. A., & Beaudoin, J. D. (1987) · Diabetes · doi:10.2337/diab.36.1.123 · Cited by 106 · see citing works
Molecular Mechanisms of Skeletal Muscle Insulin Resistance in Type 2 Diabetes
Bouzakri, K., Koistinen, H., & Zierath, J. (2005) · Current Diabetes Reviews · doi:10.2174/1573399054022785 · Cited by 106 · see citing works
In Vivo Phosphorylation of Insulin Receptor Substrate 1 at Serine 789 by a Novel Serine Kinase in Insulin-resistant Rodents
Qiao, L.-Y., Zhande, R., Jetton, T. L., Zhou, G., & Sun, X. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201494200 · Cited by 104 · see citing works
Glucose transport activity in L6 muscle cells is regulated by the coordinate control of subcellular glucose transporter distribution, biosynthesis, and mRNA transcription.
Walker, P. S., Ramlal, T., Sarabia, V., Koivisto, U., Bilan, P. J., Pessin, J. E., & Klip, A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40047-1 · Cited by 100 · see citing works
Nutrient-dependent and Insulin-stimulated Phosphorylation of Insulin Receptor Substrate-1 on Serine 302 Correlates with Increased Insulin Signaling
Giraud, J., Leshan, R. L., Lee, Y.-H., & White, M. F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308631200 · Cited by 100 · see citing works
Glucose Autoregulates Its Uptake in Skeletal Muscle
Itani, S. I., Saha, A. K., Kurowski, T. G., Coffin, H. R., Tornheim, K., & Ruderman, N. B. (2003) · Diabetes · doi:10.2337/diabetes.52.7.1635 · Cited by 96 · see citing works
AMP-Activated Protein Kinase Inhibits IGF-I Signaling and Protein Synthesis in Vascular Smooth Muscle Cells via Stimulation of Insulin Receptor Substrate 1 S794 and Tuberous Sclerosis 2 S1345 Phosphorylation
Ning, J., & Clemmons, D. R. (2010) · Molecular Endocrinology · doi:10.1210/me.2009-0474 · Cited by 89 · see citing works
Atypical protein kinase C (PKCζ/λ) is a convergent downstream target of the insulin-stimulated phosphatidylinositol 3-kinase and TC10 signaling pathways
Kanzaki, M., Mora, S., Hwang, J., Saltiel, A. R., & Pessin, J. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200306152 · Cited by 88 · see citing works
Hypoxia regulates the adenosine transporter, mENT1, in the murine cardiomyocyte cell line, HL-1
Chaudary, N. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2003.11.031 · Cited by 79 · see citing works
Interplay and Effects of Temporal Changes in the Phosphorylation State of Serine-302, -307, and -318 of Insulin Receptor Substrate-1 on Insulin Action in Skeletal Muscle Cells
Weigert, C., Kron, M., Kalbacher, H., Pohl, A. K., Runge, H., Häring, H., Schleicher, E. D., & Lehmann, R. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0102 · Cited by 66 · see citing works
Identification of Insulin Receptor Substrate 1 Serine/Threonine Phosphorylation Sites Using Mass Spectrometry Analysis: Regulatory Role of Serine 1223
Luo, M., Reyna, S. M., Wang, L., Yi, Z.-P., Carroll, C. A., Dong, L., Langlais, P. R., Weintraub, S. T., & Mandarino, L. J. (2005) · Endocrinology · doi:10.1210/en.2005-0260 · Cited by 58 · see citing works
Evidence that insulin plus ATP may induce a conformational change in the beta subunit of the insulin receptor without inducing receptor autophosphorylation.
Maddux, B. A., & Goldfine, I. D. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)89560-x · Cited by 48 · see citing works
Activation of the Cbl insulin signaling pathway in cardiac muscle; Dysregulation in obesity and diabetes
Gupte, A. A., & Mora, S. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.02.023 · Cited by 42 · see citing works
Murine muscle cell models for Pompe disease and their use in studying therapeutic approaches
Takikita, S., Myerowitz, R., Zaal, K. J. M., Raben, N., & Plötz, P. H. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2008.12.012 · Cited by 42 · see citing works
Substrate autoregulation of glucose transport: hexose 6-phosphate mediates the cellular distribution of glucose transporters
Sasson, S., Kaiser, Ν., Dan‐Goor, M., Oron, R., Koren, S., Wertheimer, E., Unluhizarci, K., & Cerasi, E. (1997) · Diabetologia · doi:10.1007/s001250050639 · Cited by 41 · see citing works
Dephosphorylation of insulin-receptor autophosphorylation sites by particulate and soluble phosphotyrosyl-protein phosphatases
King, M. J., & Sale, G. J. (1990) · Biochemical Journal · doi:10.1042/bj2660251 · Cited by 37 · see citing works
Phosphorylation of purified insulin receptor by cAMP kinase
Roth, R. A., & Beaudoin, J. (1987) · Diabetes · doi:10.2337/diabetes.36.1.123 · Cited by 26 · see citing works
Regulation of the insulin receptor by protein kinase C isoenzymes: preferential interaction with β isoenzymes and interaction with the catalytic domain of βII
Pillay, T. S., Xiao, S., Keranen, L. M., & Olefsky, J. M. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(03)00090-1 · Cited by 21 · see citing works
Differential role of insulin receptor autophosphorylation sites 1162 and 1163 in the long-term insulin stimulation of glucose transport, glycogenesis, and protein synthesis.
Desbois‐Mouthon, C., Capeau, J., Hainault, I., Wicek, D., Reynet, C., Veissière, D., Caron, M., Picard, J., Guerre-Millo, M., & Cherqui, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42238-7 · Cited by 20 · see citing works
Serine residues 1177/78/82 of the insulin receptor are required for substrate phosphorylation but not autophosphorylation.
Bossenmaier, B., Strack, V., Stoyanov, B., Krützfeldt, J., Beck, A., Lehmann, R., Kellerer, M., Klein, H., Ullrich, A., Lammers, R., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.6.889 · Cited by 20 · see citing works

Flagged first, then by citations

Sorted by citations

Role of free fatty acids in endothelial dysfunction
Ghosh, A., Gao, L., Thakur, A., Siu, P. M., & Lai, C. W. K. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0357-5 · Cited by 418 · 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
Salidroside ameliorates insulin resistance through activation of a mitochondria‐associated AMPK / PI3K / A kt/ GSK 3β pathway
Zheng, T., Yang, X., Wu, D., Xing, S., Bian, F., Li, W., Chi, J., Bai, X., Wu, G., Chen, X., et al. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13120 · Cited by 221 · see citing works
Vitamin D supplementation inhibits oxidative stress and upregulate SIRT1/AMPK/GLUT4 cascade in high glucose-treated 3T3L1 adipocytes and in adipose tissue of high fat diet-fed diabetic mice
Manna, P., Achari, A. E., & Jain, S. K. (2017) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2017.01.002 · Cited by 181 · see citing works
The PI3K pathway in B cell metabolism
Jellusova, J., & Rickert, R. C. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1215288 · Cited by 145 · see citing works
Metformin; an old antidiabetic drug with new potentials in bone disorders
Bahrambeigi, S., Yousefi, B., Rahimi, M., & Shafiei‐Irannejad, V. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.11.032 · Cited by 122 · see citing works
Antidiabetic Potential of Monoterpenes: A Case of Small Molecules Punching above Their Weight
Habtemariam, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010004 · Cited by 100 · see citing works
ERK2 Mediates Metabolic Stress Response to Regulate Cell Fate
Shin, S., Buel, G. R., Wolgamott, L., Plas, D. R., Asara, J. M., Blenis, J., & Yoon, S.-O. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.020 · Cited by 96 · see citing works
Regulation of Carbohydrate Metabolism, Lipid Metabolism, and Protein Metabolism by AMPK
Angın, Y., Beauloye, C., Horman, S., & Bertrand, L. (2016) · Proceedings of the Fourth International Symposium on Polarization Phenomena in Nuclear Reactions · doi:10.1007/978-3-319-43589-3_2 · Cited by 98 · see citing works
AMPK activation is involved in hypoglycemic and hypolipidemic activities of mogroside-rich extract from Siraitia grosvenorii (Swingle) fruits on high-fat diet/streptozotocin-induced diabetic mice
Liu, H., Qi, X., Yu, K., Lu, A., Lin, K. L., Zhu, J., Zhang, M., & Sun, Z. (2018) · Food & Function · doi:10.1039/c8fo01486h · Cited by 97 · see citing works
Dissecting the role of AMP-activated protein kinase in human diseases
Li, J., Zhong, L., Wang, F., & Zhu, H. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2016.12.003 · Cited by 89 · see citing works
Interactions between dietary carbohydrate and metformin: Implications on energy sensing, insulin signaling pathway, glycolipid metabolism and glucose tolerance in blunt snout bream Megalobrama amblycephala
Xu, C., Liu, W., Zhang, D., Cao, X., Shi, H., & Li, X. (2017) · Aquaculture · doi:10.1016/j.aquaculture.2017.10.022 · Cited by 89 · see citing works
Progress in understanding the mechanisms of resistance to BCL-2 inhibitors
Xu, Y., & Ye, H. (2022) · Experimental Hematology and Oncology · doi:10.1186/s40164-022-00283-0 · Cited by 86 · see citing works
Phosphatidylinositol-3,4,5-Triphosphate and Cellular Signaling: Implications for Obesity and Diabetes
Manna, P., & Jain, S. K. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373949 · Cited by 84 · see citing works
Efficacy and safety of PXL770, a direct AMP kinase activator, for the treatment of non-alcoholic fatty liver disease (STAMP-NAFLD): a randomised, double-blind, placebo-controlled, phase 2a study
Cusi, K. J., Alkhouri, N., Harrison, S. A., Fouqueray, P., Moller, D. E., Hallakou‐Bozec, S., Bolze, S., Grouin, J., Megnien, S. J., Dubourg, J., et al. (2021) · The Lancet. Gastroenterology & hepatology · doi:10.1016/s2468-1253(21)00300-9 · Cited by 78 · see citing works
Therapeutic Potential of Oxytocin in Atherosclerotic Cardiovascular Disease: Mechanisms and Signaling Pathways
Wang, P., Wang, S. C., Yang, H.-P., Lv, C., Jia, S., Liu, X., Wang, X., Meng, D., Qin, D., Zhu, H. F., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00454 · Cited by 73 · see citing works
New Insights into AMPK, as a Potential Therapeutic Target in Metabolic Dysfunction-Associated Steatotic Liver Disease and Hepatic Fibrosis
An, H., Jang, Y., Choi, J.-I., Hur, J., Kim, S., & Kwon, Y. (2024) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2024.188 · Cited by 72 · see citing works
Long-Term Supplementation With a Cystine-Based Antioxidant Delays Loss of Muscle Mass in Aging
Sinha‐Hikim, I., Sinha‐Hikim, A. P., Parveen, M., Shen, R., Goswami, R., Tran, P., Crum, A., & Norris, K. C. (2013) · The Journals of Gerontology Series A · doi:10.1093/gerona/gls334 · Cited by 68 · see citing works
Small Molecule Adenosine 5′-Monophosphate Activated Protein Kinase (AMPK) Modulators and Human Diseases
Rana, S., Blowers, E. C., & Natarajan, A. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401994c · Cited by 62 · see citing works
Effect of CAPE-pNO2 against type 2 diabetes mellitus via the AMPK/GLUT4/ GSK3β/PPARα pathway in HFD/STZ-induced diabetic mice
Li, S., Huang, Q., Zhang, L., Qiao, X., Zhang, Y., Tang, F., & Li, Z. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.03.027 · Cited by 57 · see citing works
Emerging Role of Adipocyte Dysfunction in Inducing Heart Failure Among Obese Patients With Prediabetes and Known Diabetes Mellitus
Berezin, A. Е., Berezin, A. A., & Lichtenauer, M. (2020) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.583175 · Cited by 55 · see citing works
Therapeutic effect of oxyberberine on obese non-alcoholic fatty liver disease rats
Li, Q., Dou, Y., Huang, Z., Chen, H., Li, Y., Chen, J.-N., Liu, Y., Huang, X., Zeng, H., Yang, X., et al. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153550 · Cited by 55 · see citing works
AdipoRon induces AMPK activation and ameliorates Alzheimer's like pathologies and associated cognitive impairment in APP/PS1 mice.
Khandelwal, M., Manglani, K., Upadhyay, P., Azad, M., & Gupta, S. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105876 · Cited by 55 · see citing works
A systematic review on the mechanisms of vitamin K effects on the complications of diabetes and pre‐diabetes
Karamzad, N., Maleki, V., Carson‐Chahhoud, K., Azizi, S., Sahebkar, A., & Gargari, B. P. (2019) · BioFactors · doi:10.1002/biof.1569 · Cited by 54 · see citing works
Polyphenols targeting diabetes via the AMP-activated protein kinase pathway; future approach to drug discovery
Momtaz, S., Maghsoudi, A. S., Abdolghaffari, A. H., Jasemi, E., Rezazadeh, S., Hassani, S., Ziaee, M., Abdollahi, M. R., Behzad, S., & Nabavi, S. M. (2019) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408363.2019.1648376 · Cited by 55 · see citing works
Regulation and role of glycophagy in skeletal muscle energy metabolism
Heden, T. D., Chow, L. S., Hughey, C. C., & Mashek, D. G. (2021) · Autophagy · doi:10.1080/15548627.2021.1969633 · Cited by 52 · see citing works
Pharmacodynamic effects of direct AMP kinase activation in humans with insulin resistance and non-alcoholic fatty liver disease: A phase 1b study
Fouqueray, P., Bolze, S., Dubourg, J., Hallakou‐Bozec, S., Theurey, P., Grouin, J., Chevalier, C., Dagorn, P. G., Moller, D. E., & Cusi, K. J. (2021) · Cell Reports Medicine · doi:10.1016/j.xcrm.2021.100474 · Cited by 52 · see citing works
Immune-mediated anti-tumor effects of metformin; targeting metabolic reprogramming of T cells as a new possible mechanism for anti-cancer effects of metformin
Bahrambeigi, S., & Shafiei‐Irannejad, V. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113787 · Cited by 51 · see citing works
The AMPK-SIRT signaling network regulates glucose tolerance under calorie restriction conditions
Silvestre, M. P., Viollet, B., Caton, P., Leclerc, J., Sakakibara, I., Foretz, M., Holness, M., & Sugden, M. C. (2014) · Life Sciences · doi:10.1016/j.lfs.2014.01.080 · Cited by 51 · see citing works
The hypoglycemic mechanism of catalpol involves increased AMPK-mediated mitochondrial biogenesis
Xu, D., Li, C., Jiang, Z., Wang, L., Huang, H., Li, Z., Sun, L., Fan, S., Zhang, L., & Wang, T. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0345-2 · Cited by 49 · see citing works
Targeting the Inositol Pyrophosphate Biosynthetic Enzymes in Metabolic Diseases
Mukherjee, S. K., Haubner, J., & Chakraborty, A. (2020) · Molecules · doi:10.3390/molecules25061403 · Cited by 47 · see citing works
A Descriptive Review of the Action Mechanisms of Berberine, Quercetin and Silymarin on Insulin Resistance/Hyperinsulinemia and Cardiovascular Prevention
Bellavite, P., Fazio, S., & Affuso, F. (2023) · Molecules · doi:10.3390/molecules28114491 · Cited by 46 · see citing works
Regulation of a truncated isoform of AMP-activated protein kinase α (AMPKα) in response to hypoxia in the muscle of Pacific oyster Crassostrea gigas
Guévélou, É., Huvet, A., Sussarellu, R., Milan, M., Guo, X., Li, L., Zhang, G., Quillien, V., Daniel, J., Quéré, C., et al. (2013) · Journal of Comparative Physiology B · doi:10.1007/s00360-013-0743-6 · Cited by 41 · see citing works
Insulin resistance/hyperinsulinemia: an important cardiovascular risk factor that has long been underestimated
Fazio, S., Mercurio, V., Tibullo, L., Fazio, V., & Affuso, F. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1380506 · Cited by 39 · see citing works
Anti-Diabetic Therapies and Cancer: From Bench to Bedside
Kounatidis, D. C., Vallianou, N. G., Karampela, Ι., Rebelos, E., Kouveletsou, M., Dalopoulos, V., Koufopoulos, P., Diakoumopoulou, E., Tentolouris, N., & Dalamaga, Μ. (2024) · Biomolecules · doi:10.3390/biom14111479 · Cited by 45 · see citing works
The effect of chronic, mild heat stress on metabolic changes of nutrition and adaptations in rumen papillae of lactating dairy cows
Eslamizad, M., Albrecht, D., & Kuhla, B. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18417 · Cited by 38 · see citing works
Proteomics insights into the effects of MSTN on muscle glucose and lipid metabolism in genetically edited cattle
Xin, X., Yang, S., Li, X., Liu, X., Zhang, L.-L., Ding, X., Zhang, S., Li, G., & Guo, H. (2019) · General and Comparative Endocrinology · doi:10.1016/j.ygcen.2019.113237 · Cited by 37 · see citing works
Myocardial glycogen dynamics: New perspectives on disease mechanisms
Chandramouli, C., Varma, U., Stevens, E. M., Xiao, R., Stapleton, D., Mellor, K. M., & Delbridge, L. M. D. (2015) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.12370 · Cited by 36 · see citing works
Chicoric acid promotes glucose uptake and Akt phosphorylation via AMP-activated protein kinase α-dependent pathway
Peng, Y., Sun, Q., & Park, Y. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.05.020 · Cited by 36 · see citing works
Effect of metformin and flutamide on insulin, lipogenic and androgen-estrogen signaling, and cardiometabolic risk in a PCOS-prone metabolic syndrome rodent model
Kupreeva, M., Diané, A., Lehner, R. S., Watts, R., Ghosh, M., Proctor, S. D., & Vine, D. F. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00018.2018 · Cited by 34 · see citing works
AMPK in myocardial infarction and diabetes: the yin/yang effect
Moussa, A., & Li, J. (2012) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2012.06.001 · Cited by 32 · see citing works
Artemisia scoparia Enhances Adipocyte Development and Endocrine Function In Vitro and Enhances Insulin Action In Vivo
Richard, A. J., Fuller, S., Fedorcenco, V., Beyl, R., Burris, T. P., Mynatt, R., Ribnicky, D. M., & Stephens, J. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098897 · Cited by 30 · see citing works
The Potential Therapeutic Role of Metformin in Diabetic and Non-Diabetic Bone Impairment
Mu, W., Liang, G., Feng, Y., Jiang, Y., & Qu, F. (2022) · Pharmaceuticals · doi:10.3390/ph15101274 · Cited by 30 · see citing works
Berberine attenuates fructose-induced insulin resistance by stimulating the hepatic LKB1/AMPK/PGC1α pathway in mice
Li, Y., Wang, B., Shen, J.-D., Bai, M., & Xu, E. (2020) · Pharmaceutical Biology · doi:10.1080/13880209.2020.1756349 · Cited by 32 · see citing works
Anti-diabetic effects of a phenolic-rich extract from Hypericum attenuatum Choisy in KK-Ay mice mediated through AMPK /PI3K/Akt/GSK3β signaling and GLUT4, PPARγ, and PPARα expression
Lv, Y., Hao, J., Liu, C., Huang, H., Ma, Y., Yang, X., & Tang, L. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103506 · Cited by 30 · see citing works
Differential activation of the mTOR/autophagy pathway predicts cognitive performance in APP/PS1 mice
Vartak, R. S., Rodin, A., & Oddo, S. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.08.018 · Cited by 28 · see citing works
Active ingredients and mechanisms of Phellinus linteus (grown on Rosa multiflora) for alleviation of Type 2 diabetes mellitus through network pharmacology
Oh, K., Adnan, M., & Cho, D. H. (2020) · Gene · doi:10.1016/j.gene.2020.145320 · Cited by 29 · see citing works
Points of integration between the intracellular energy sensor AMP-activated protein kinase (AMPK) activity and the somatotroph axis function
Tulipano, G., Faggi, L., Sibilia, V., & Giustina, A. (2012) · Endocrine · doi:10.1007/s12020-012-9732-x · Cited by 28 · see citing works
Selenium and Selenoproteins at the Intersection of Type 2 Diabetes and Thyroid Pathophysiology
Gorini, F., & Vassalle, C. (2022) · Antioxidants · doi:10.3390/antiox11061188 · Cited by 27 · see citing works
Increased intracellular iron in mouse primary hepatocytes in vitro causes activation of the Akt pathway but decreases its response to insulin
Varghese, J., James, J., Vaulont, S., McKie, A. T., & Jacob, M. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.05.022 · Cited by 27 · see citing works
GnRH Regulates Gonadotropin Gene Expression Through NADPH/Dual Oxidase-Derived Reactive Oxygen Species
Kim, T., & Lawson, M. A. (2015) · Endocrinology · doi:10.1210/en.2014-1709 · Cited by 25 · see citing works
A ~24 kDa protein isolated from protein isolates of Hawaijar, popular fermented soy food of North-East India exhibited promising antidiabetic potential via stimulating PI3K/AKT/GLUT4 signaling pathway of muscle glucose metabolism
Das, D., Afzal, N. U., Wann, S. B., Kalita, J., & Manna, P. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.187 · Cited by 24 · see citing works
Chronic Treatment with the AMP-Kinase Activator AICAR Increases Glycogen Storage and Fatty Acid Oxidation in Skeletal Muscles but Does Not Reduce Hyperglucagonemia and Hyperglycemia in Insulin Deficient Rats
Vitzel, K. F., Bikopoulos, G. J., Hung, S., Pistor, K., Patterson, J. D., Curi, R., & Ceddia, R. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062190 · Cited by 24 · see citing works
NGBR Is Required to Ameliorate Type 2 Diabetes in Mice by Enhancing Insulin Sensitivity
Chen, Y., Hu, W., Li, Q., Zhao, S., Zhao, D., Zhang, S., Wei, Z., Yang, X., Chen, Y., Li, X., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100624 · Cited by 23 · see citing works
Diabetic Kinome Inhibitors—A New Opportunity for β-Cells Restoration
Pucelik, B., Barzowska, A., Dąbrowski, J. M., & Czarna, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22169083 · Cited by 23 · see citing works
Metabolic and transcriptome responses of RNAi-mediated AMPKα knockdown in Tribolium castaneum
Jiang, H., Zhang, N., Ji, C., Meng, X., Qian, K., Zheng, Y., & Wang, J. (2020) · BMC Genomics · doi:10.1186/s12864-020-07070-3 · Cited by 23 · see citing works
Supplementation of scopoletin improves insulin sensitivity by attenuating the derangements of insulin signaling through AMPK
Kalaivanan, K., Priya, C. S., Nanda, D., Vidhya, R., & Anuradha, C. V. (2018) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-018-3432-7 · Cited by 22 · see citing works
Adiponectin: a potential target for obesity-associated Alzheimer’s disease
Samant, N. P., & Gupta, G. L. (2021) · Metabolic Brain Disease · doi:10.1007/s11011-021-00756-x · Cited by 21 · see citing works
Site‐specific separation and detection of phosphopeptide isomers with p H ‐mediated stacking capillary electrophoresis‐electrospray ionization‐tandem mass spectrometry
Dong, Y., Chien, K., Chen, J.-T., Lin, S., Wang, T. V., & Yu, J. (2013) · Journal of Separation Science · doi:10.1002/jssc.201300054 · Cited by 21 · see citing works
Angelica gigas Ameliorates Hyperglycemia and Hepatic Steatosis in C57BL/KsJ-db/db Mice via Activation of AMP-Activated Protein Kinase Signaling Pathway
Bae, U., Choi, E., Oh, M., Jung, S., Park, J., Jung, T.-S., Park, T.-S., Chae, S., & Park, B. (2016) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x16500919 · Cited by 21 · see citing works
Propylene glycol guluronate sulfate (PGGS) reduces lipid accumulation via AMP-activated kinase activation in palmitate-induced HepG2 cells
Xin, M., Sun, Y., Chen, H., Li, Q., Dun, Y., Guan, H., Hao, J., & Li, C. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.03.068 · Cited by 21 · see citing works
Atorvastatin promotes AMPK signaling to protect against high fat diet‑induced non‑alcoholic fatty liver in golden hamsters
Zhang, B., Zhang, C., Zhang, X., Li, N., Dong, Z., Sun, G., & Sun, X. (2020) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2020.8465 · Cited by 21 · see citing works
Entada phaseoloides extract suppresses hepatic gluconeogenesis via activation of the AMPK signaling pathway
Zheng, T., Hao, X., Wang, Q., Chen, L., Jin, S., & Bian, F. (2016) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2016.10.039 · Cited by 21 · see citing works
Imaging Methods Applicable in the Diagnostics of Alzheimer’s Disease, Considering the Involvement of Insulin Resistance
Hnilicová, P., Kantorová, E., Šutovský, S., Grofik, M., Zeleňák, K., Kurča, E., Žilka, N., Parvanovova, P., & Kolísek, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043325 · Cited by 21 · see citing works
PAS Kinase as a Nutrient Sensor in Neuroblastoma and Hypothalamic Cells Required for the Normal Expression and Activity of Other Cellular Nutrient and Energy Sensors
Hurtado-Carneiro, V., Roncero, I., Blázquez, E., Álvarez, E., & Sanz, C. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8476-9 · Cited by 20 · see citing works
Effects of exogenous adiponectin supplementation in early pregnant PCOS mice on the metabolic syndrome of adult female offspring
Zuo, M., Liao, G., Zhang, W., Xu, D., Lü, J., Tang, M., Yan, Y., Hong, C., & Wang, Y. (2021) · Journal of Ovarian Research · doi:10.1186/s13048-020-00755-z · Cited by 19 · see citing works
Multi-omics reveals the molecular mechanisms of rapid growth in distant hybrid fish
Zhang, X., Liu, F., Li, B., Duan, L., Yu, J., Huang, Z., Huang, S., Liu, H., Liu, Q., & Liu, S. (2024) · Aquaculture · doi:10.1016/j.aquaculture.2024.741783 · Cited by 18 · see citing works
Permethrin decreased insulin-stimulated AKT phosphorylation dependent on extracellular signal-regulated kinase-1 (ERK), but not AMP-activated protein kinase α (AMPKα), in C2C12 myotubes
Sun, Q., Peng, Y., Qi, W., Kim, Y., Clark, J. M., Kim, D., & Park, Y. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.08.046 · Cited by 18 · see citing works
Vitexin attenuates autoimmune hepatitis in mouse induced by syngeneic liver cytosolic proteins via activation of AMPK/AKT/GSK-3β/Nrf2 pathway
Zhang, L., Chen, D., Tu, Y., Sang, T., Pan, T., Lin, H., Cai, C., Jin, X., Wu, F.-L., Xu, L., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174720 · Cited by 17 · see citing works
Prospective and challenges of locally applied repurposed pharmaceuticals for periodontal tissue regeneration
El-Nablaway, M., Rashed, F., Taher, E. S., Abdeen, A., Taymour, N., Soliman, M. M., Shalaby, H. K., Fericean, L. M., Bănățean-Dunea, I., El-Sherbiny, M., et al. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1400472 · Cited by 17 · see citing works
Camel milk protein hydrosylate alleviates hepatic steatosis and hypertension in high fructose-fed rats
Alshuniaber, M. A., Alshammari, G. M., Eleawa, S. M., Yagoub, A. E. A., Al-Khalifah, A. S., Alhussain, M. H., Al‐Harbi, L. N., & Yahya, M. A. (2022) · Pharmaceutical Biology · doi:10.1080/13880209.2022.2079678 · Cited by 16 · see citing works
Cassia Abbreviata Enhances Glucose Uptake and Glucose Transporter 4 Translocation in C2C12 Mouse Skeletal Muscle Cells
Kamga-Simo, F. D. Y., Kamatou, G., Ssemakalu, C. C., & Shai, L. J. (2021) · Journal of Evidence-Based Integrative Medicine · doi:10.1177/2515690x211006333 · Cited by 16 · see citing works
Aqueous extract of Scrophularia ningpoensis improves insulin sensitivity through AMPK-mediated inhibition of the NLRP3 inflammasome
Yan, S., Lu, W., Zhou, J. Y., Guo, X., Li, J., Cheng, H., Zhu, X., Zhao, Y., Duan, M., Yang, H., et al. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154308 · Cited by 15 · see citing works
Impact of Metabolic disrupting chemicals on redox homeostasis, energy sensors, receptor modulation, and hormone metabolism: A comparative account in Teleost and mammalian model organisms
Mukherjee, U., & Maitra, S. (2023) · Aquaculture and Fisheries · doi:10.1016/j.aaf.2023.05.004 · Cited by 15 · see citing works
Insulin Resistance/Hyperinsulinemia, Neglected Risk Factor for the Development and Worsening of Heart Failure with Preserved Ejection Fraction
Fazio, S., Mercurio, V., Fazio, V., Ruvolo, A., & Affuso, F. (2024) · Biomedicines · doi:10.3390/biomedicines12040806 · Cited by 16 · see citing works
Thymus serpyllum Exhibits Anti-Diabetic Potential in Streptozotocin-Induced Diabetes Mellitus Type 2 Mice: A Combined Biochemical and In Vivo Study
Azhar, J., John, P. C. L., & Bhatti, A. (2022) · Nutrients · doi:10.3390/nu14173561 · Cited by 15 · see citing works
Dual effect of the heart-targeting cytokine cardiotrophin-1 on glucose transport in cardiomyocytes
Asrih, M., Gardier, S., Papageorgiou, I., & Montessuit, C. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.12.015 · Cited by 15 · see citing works
Crosstalk of LKB1‐regulated and PTEN‐regulated signals in liver morphogenesis and tumor development in mice
Jia, C., Medina, V., Liu, C., He, L., Qian, D., Tu, T., Okamoto, C. T., & Stiles, B. L. (2017) · Hepatology Communications · doi:10.1002/hep4.1027 · Cited by 14 · see citing works
The Negative Impact of Insulin Resistance/Hyperinsulinemia on Chronic Heart Failure and the Potential Benefits of Its Screening and Treatment
Fazio, S., Mercurio, V., Affuso, F., & Bellavite, P. (2023) · Biomedicines · doi:10.3390/biomedicines11112928 · Cited by 13 · see citing works
Lectin rich horsegram protein and myricetin activates insulin signaling – A study targeting PTP1β
Lalitha, N., Bettadahalli, S., Talahalli, R. R., & Singh, S. A. (2020) · Journal of Functional Foods · doi:10.1016/j.jff.2020.103845 · Cited by 13 · see citing works
The Lipid-Oxidative Stress Axis: Novel Therapeutic Targets for Podocytopathy
Liu, Y., Zou, M., & Wang, Y. (2025) · Journal of Inflammation Research · doi:10.2147/jir.s530737 · Cited by 13 · see citing works
Glucose deprivation promotes activation of mTOR signaling pathway and protein synthesis in rat skeletal muscle cells
Miniaci, M. C., Dattolo, M. G., Irace, C., Capuozzo, A., Santamaria, R., & Scotto, P. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1583-2 · Cited by 12 · see citing works
Empagliflozin and memantine combination ameliorates cognitive impairment in scopolamine + heavy metal mixture-induced Alzheimer’s disease in rats: role of AMPK/mTOR, BDNF, BACE-1, neuroinflammation, and oxidative stress
Abdel-Lah, E. S., Sherkawy, H. S., Mohamed, W. H., Fawy, M. A., Hasan, A. A., Muhammed, A. A., Taha, A. F., Tony, A. A., Hamad, N., & Gamea, M. G. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01755-5 · Cited by 12 · see citing works
Dietary inclusion of Clostridium butyricum cultures alleviated impacts of high-carbohydrate diets in largemouth bass (Micropterus salmoides)
Tao, J., Gong, Y., Chen, S., Li, W., Xie, R., Zhang, H., Chen, N., Huang, X., & Li, S. (2023) · British Journal Of Nutrition · doi:10.1017/s0007114523002842 · Cited by 11 · see citing works
Alpha-Mangosteen lessens high-fat/high-glucose diet and low-dose streptozotocin induced-hepatic manifestations in the insulin resistance rat model
Soetikno, V., Andini, P., Iskandar, M., Matheos, C. C., Herdiman, J. A., Kyle, I. K., Suma, M. N. I., Louisa, M., & Estuningtyas, A. (2023) · Pharmaceutical Biology · doi:10.1080/13880209.2023.2166086 · Cited by 10 · see citing works
l‐ Arginine supplementation of gilts during early gestation modulates energy sensitive pathways in pig conceptuses
Garcia, I. S., Teixeira, S. A., Costa, K. A., Marques, D. B. D., Rodrigues, G. D. A., Costa, T. C., Guimarães, J. D., Otto, P. I., Saraiva, A., Ibelli, A. M. G., et al. (2020) · Molecular Reproduction and Development · doi:10.1002/mrd.23397 · Cited by 10 · see citing works
Role of the AMP-Activated Protein Kinase in the Pathogenesis of Polycystic Ovary Syndrome
Jalil, A. T., Zair, M. A., Hanthal, Z. R., Naser, S. J., Aslandook, T., Abosaooda, M., & Fadhil, A. A. (2023) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-023-01139-y · Cited by 9 · see citing works
A Comprehensive Insight into Potential Roles of Taurine on Metabolic Variables in Type 2 Diabetes: A Systematic Review
Maleki, V., Mahdavi, R., Hajizadeh‐Sharafabad, F., & Alizadeh, M. (2020) · Pharmaceutical Sciences · doi:10.34172/ps.2020.17 · Cited by 9 · see citing works
Activation of insulin signaling and energy sensing network by AICAR, an AMPK activator in insulin resistant rat tissues
Radika, M. K., & Anuradha, C. V. (2015) · Journal of Basic and Clinical Physiology and Pharmacology · doi:10.1515/jbcpp-2014-0122 · Cited by 9 · see citing works
Exercising with blocked muscle glycogenolysis: Adaptation in the McArdle mouse
Nielsen, T. L., Pinós, T., Brull, A., Vissing, J., & Krag, T. O. B. (2017) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2017.11.006 · Cited by 8 · see citing works
Common Genetic Variation in the Human CTF1 Locus, Encoding Cardiotrophin-1, Determines Insulin Sensitivity
Lutz, S. Z., Franck, O., Böhm, A., Machann, J., Schick, F., Machicao, F. E., Fritsche, A., Häring, H., & Staiger, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100391 · Cited by 7 · see citing works
Influence of Diet on Visceral Adipose Remodeling in NONcNZO10 Mice With Polygenic Susceptibility for Type 2 Diabetes
Adi, N., Adi, J., Cesar, L., Agatston, A. S., Kurlansky, P. A., & Webster, K. A. (2012) · Obesity · doi:10.1038/oby.2012.167 · Cited by 7 · see citing works
Self-citation
Enhanced insulin signaling and its downstream effects in iron-overloaded primary hepatocytes from hepcidin knock-out mice
James, J. V., Varghese, J., McKie, A. T., Vaulont, S., & Jacob, M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118621 · Cited by 7 · see citing works
Plantain flour: A potential anti-obesity ingredient for intestinal flora regulation and improved hormone secretion
Fu, J., Xiao, J., Tu, S., Sheng, Q., Yi, G., Wang, J., & Sheng, O. (2022) · Frontiers in Sustainable Food Systems · doi:10.3389/fsufs.2022.1027762 · Cited by 5 · see citing works
Gut microbial community and host intestinal gene expression with combined fish oil and soluble corn fiber compared with corn oil and maltodextrin: A randomized crossover trial in healthy older individuals
Moosavi, D., Mullens, D. A., Davidson, L. A., Fan, Y.-Y., Goldsby, J. S., Ivanov, I. V., Levy, L., Kahsai, O. J., Curtis, K. R., Raftery, D., et al. (2025) · American Journal of Clinical Nutrition · doi:10.1016/j.ajcnut.2025.04.031 · Cited by 5 · see citing works
Antidiabetic effects of Agaricus bisporus polysaccharide in HFD/STZ-induced mice
Wang, Z., Ouyang, Q., Guo, H., Li, H., & Liu, R. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.150671 · Cited by 4 · see citing works
Self-citation
The Long-Term Treatment of Drug-Resistant Migraine with the Modified Atkins Ketogenic Diet: A Single-Center, Retrospective Study
Francini‐Pesenti, F., Favaretto, S., D’Angelo, M., Cacciapuoti, M., & Calò, L. A. (2024) · Nutrients · doi:10.3390/nu16244324 · Cited by 3 · see citing works
HM-chromanone reverses the blockade of insulin signaling induced by high glucose levels in human HepG2 cells
Park, J. E., & Han, J.-S. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175358 · Cited by 3 · see citing works
Metabolic Reprogramming of Anti-cancer T Cells: Targeting AMPK and PPAR to Optimize Cancer Immunotherapy
Jalil, A. T., Al-Kazzaz, H. H., Hassan, F., Mohammed, S. H., Merza, M. S., Aslandook, T., Elewadi, A., Fadhil, A. A., & Alsalamy, A. (2024) · Indian Journal of Clinical Biochemistry · doi:10.1007/s12291-023-01166-9 · Cited by 3 · see citing works
The Effects of Estrogen, Grape Pomace, and Resveratrol Supplementation on Glucose Tolerance and Insulin Signaling in Ovariectomized Rats.
Anderson, E. (2017) · The Atrium (University of Guelph) · Cited by 3 · see citing works

Molecular Mechanisms of AMPK- and Akt- Dependent Survival of Glucose-Starved Cardiac Myocytes
Chopra, I. (2012) · Cited by 1 · see citing works
Self-citation
Abstract 15679: Phosphorylation Of The Insulin Receptor By AMPK Promotes Ligand-independent Activation Of The Insulin-signaling Pathway And Promotes Survival Of Glucose-stressed Cardiac Myocytes
Chopra, I., Li, H.-F., Wang, H., & Webster, K. A. (2011) · Circulation
Self-citation
Insulin signalling downstream of protein kinase B is potentiated by 5′AMP-activated protein kinase in rat hearts in vivo
Longnus, S. L., Ségalen, C., Giudicelli, J., Sajan, M. P., Farese, R. V., & Van Obberghen, E. (2005) · Diabetologia · doi:10.1007/s00125-005-0016-3 · Cited by 58 · see citing works
Abstract 3783: An Insulin-independent AMPK-dependent Survival Pathway Is Activated In Glucose-starved Cardiac Myocytes through IRS-1/PI3-kinase and Rictor-mediated Activation of PDK1 and PDK2
Chopra, I., Li, H., Bishopric, N. H., & Webster, K. A. (2008) · Circulation · doi:10.1161/circ.118.suppl_18.s_486 · Cited by 1 · see citing works
Self-citation
Inhibition of AMPK via phosphorylation at Ser485/491: Multiple mechanisms of regulation
Coughlan, K. A. (2015) · OpenBU (Boston University)

Authors: Chopra, I., Li, H. F., Wang, H., & Webster, K. A.
Affiliations: University of Miami (US)
Corresponding author: Webster, K. A.
ORCID: Webster, K. A.
Venue: Diabetologia
Publisher: Springer Science and Business Media LLC
Published: 2011-12-30
Volume: 55
Issue: 3
Pages: 783-794
ISSN: 0012-186X (ISSN-L)
1432-0428
DOI: 10.1007/s00125-011-2407-y
PMC: PMC4648248
OpenAlex: W2038901278
Cited by: 116
References: 51
Citations by year: 2026: 4 · 2025: 5 · 2024: 9 · 2023: 8 · 2022: 10 · 2021: 9 · 2020: 12 · 2019: 12 · 2018: 8 · 2017: 10 · 2016: 4 · 2015: 6 · 2014: 6 · 2013: 7 · 2012: 6
FWCI: 2.46
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
Locations: Diabetologia (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (1r21hl069812-01)
National Heart, Lung, and Blood Institute (HL-69812, HL44578, R01HL072924, R01HL044578)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: AMPK, insulin receptor, insulin signaling pathway, glucose deprivation, hypoglycemia, Akt phosphorylation, glycogen synthase kinase-3β, AICAR, skeletal myocytes, cardiomyocytes
MeSH terms: Animals, Animals, Newborn, Cells, Cultured, Humans, Hypoglycemia, Hypoglycemic Agents, Ligands, Phosphorylation, Protein Processing, Post-Translational, Receptor, Insulin, Recombinant Proteins, Signal Transduction, Muscle, Skeletal, Myocytes, Cardiac, Protein Kinase Inhibitors, Mutant Proteins, Rats, AMP-Activated Protein Kinases, Insulin Receptor Substrate Proteins, Hep G2 Cells

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

Phosphorylation of the insulin receptor by AMP-activated protein kinase (AMPK) promotes ligand-independent activation of the insulin signalling pathway in rodent muscle

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks