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Adiponectin Sensitizes Insulin Signaling by Reducing p70 S6 Kinase-mediated Serine Phosphorylation of IRS-1
Open accessAbstract
Adiponectin functions as an insulin sensitizer, and yet the underlying molecular mechanism(s) remains largely unknown. We found that treating C2C12 myotubes with adiponectin or rapamycin enhanced the ability of insulin to stimulate IRS-1 tyrosine phosphorylation and Akt phosphorylation, concurrently with reduced p70 S6 kinase phosphorylation at Thr389 as well as IRS-1 phosphorylation at Ser302 and Ser636/639. Overexpression of dominant-negative AMP kinase (AMPK), but not dominant-negative p38 MAPK, reduced the insulin-sensitizing effect of adiponectin. Rapamycin, but not adiponectin, enhanced insulin-stimulated Akt phosphorylation in HeLa cells, which lack LKB1, and exogenous expression of LKB1 in HeLa cells rescued the insulin-sensitizing effect of adiponectin. Finally, overexpression of wild-type Rheb (Ras homology-enriched in brain) or the TSC2 mutant lacking the AMPK phosphorylation site (TSC2S1345A) inhibited the insulin-sensitizing effect of adiponectin in C2C12 cells. These results indicate that activation of the LKB1/AMPK/TSC1/2 pathway alleviates the p70 S6 kinase-mediated negative regulation of insulin signaling, providing a mechanism by which adiponectin increases insulin sensitivity in cells.
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“Recent studies have shown that the activation of AMPK by adiponectin enhances the ability of insulin to stimulate IRS1 and Akt phosphorylation concurrently, with reduced S6K1 phosphorylation at T389 as well as IRS1 phosphorylation at S302 and S636/639 [160].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [160]
Citations
Cites
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
Yamauchi, T., Kamon, J., Waki, H., Terauchi, Y., Kubota, N., Hara, K., Mori, Y., Ide, T., Murakami, K., Tsuboyama-Kasaoka, N., et al. (2001) · Nature Medicine · doi:10.1038/90984 · Cited by 4,915
TSC2 Mediates Cellular Energy Response to Control Cell Growth and Survival
Inoki, K., Zhu, T., & Guan, K.-L. (2003) · Cell · doi:10.1016/s0092-8674(03)00929-2 · Cited by 3,914
Self-citationCloning of adiponectin receptors that mediate antidiabetic metabolic effects
Yamauchi, T., Kamon, J., Ito, Y., Tsuchida, A., Yokomizo, T., Kita, S., Sugiyama, T., Miyagishi, M., Hara, K., Tsunoda, M., et al. (2003) · Nature · doi:10.1038/nature01705 · Cited by 3,176
Adiponectin and Adiponectin Receptors
Kadowaki, T., & Yamauchi, T. (2005) · Endocrine Reviews · doi:10.1210/er.2005-0005 · Cited by 2,634
AdipoQ Is a Novel Adipose-specific Gene Dysregulated in Obesity
Hu, E., Liang, P., & Spiegelman, B. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10697 · Cited by 2,261
Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
Self-citationAbsence 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
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
Woods, A., Johnstone, S. R., Dickerson, K., Leiper, F. C., Fryer, L. G. D., Neumann, D., Schlattner, U., Wallimann, T., Carlson, M., & Carling, D. (2003) · Current Biology · doi:10.1016/j.cub.2003.10.031 · Cited by 1,650
The TSC1-2 tumor suppressor controls insulin–PI3K signaling via regulation of IRS proteins
Harrington, L. S., Findlay, G. M., Gray, A., Толкачева, Т. А., Wigfield, S., Rebholz, H., Barnett, J., Leslie, N. R., Cheng, S., Shepherd, P. R., et al. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200403069 · Cited by 1,123
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Globular adiponectin induces LKB1/AMPK-dependent glucose uptake via actin cytoskeleton remodeling
Vu, V. P., Bui, P., Eguchi, M., Xu, A., & Sweeney, G. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0059 · Cited by 34
Sevillano, J., de Castro, J., Bocos, C., Herrera, E., & Ramos, P. (2007) · Endocrinology · doi:10.1210/en.2007-0352 · Cited by 33
The Place for Glycemic Control in the Surgical Patient
May, A. K., Kauffmann, R. M., & Collier, B. R. (2011) · Surgical Infections · doi:10.1089/sur.2011.019 · Cited by 33
Adiponectin and insulin cross talk: The microvascular connection
Zhao, L., Fu, Z., & Liu, Z. (2014) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2014.08.001 · Cited by 34
Xu, X., Tu, L., Feng, W., Ma, B., Li, R., Zheng, C., Li, G., & Wang, D. W. (2013) · Endocrinology · doi:10.1210/en.2012-2012 · Cited by 31
Dietary camphene attenuates hepatic steatosis and insulin resistance in mice
Kim, S., Choi, Y., Choi, S., Choi, Y., & Park, T. (2013) · Obesity · doi:10.1002/oby.20554 · Cited by 29
Aerobic Exercise Ameliorates Cancer Cachexia-Induced Muscle Wasting through Adiponectin Signaling
Morinaga, M., Sako, N., Isobe, M., Lee-Hotta, S., Sugiura, H., & Kametaka, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063110 · Cited by 23
Role of Adipose Tissue in Metabolic System Disorders
Rezaee, F. (2013) · Journal of Diabetes & Metabolism · doi:10.4172/2155-6156.s13-008 · Cited by 30
AMPK Control of mTOR Signaling and Growth
Gwinn, D. M., & Shaw, R. J. (2010) · The Enzymes · doi:10.1016/s1874-6047(10)28003-4 · Cited by 25
Energy Homoeostasis: The Roles of Adipose Tissue-Derived Hormones, Peptide YY and Ghrelin
Hall, J., Roberts, R. E., & Vora, N. (2009) · Obesity Facts · doi:10.1159/000208517 · Cited by 24
Rajan, M. R., Fagerholm, S., Jönsson, C., Kjølhede, P., Turkina, M. V., & Strålfors, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059725 · Cited by 24
Singh, A., Fernandes, J. R. D., Chhabra, G., Krishna, A., & Banerjee, A. (2019) · Endocrine · doi:10.1007/s12020-019-01891-3 · Cited by 24
d-Allulose Ameliorates Skeletal Muscle Insulin Resistance in High-Fat Diet-Fed Rats
Gou, Y., Liu, B., Cheng, M., Yamada, T., Iida, T., Wang, S., Banno, R., & Koike, T. (2021) · Molecules · doi:10.3390/molecules26206310 · Cited by 25
Pioglitazone upregulates adiponectin receptor 2 in 3T3-L1 adipocytes
Kudoh, A., Satoh, H., Hirai, H., & Watanabe, T. (2011) · Life Sciences · doi:10.1016/j.lfs.2011.04.001 · Cited by 23
Leptin prevents the metabolic effects of adiponectin in L6 myotubes
Fang, X., Fetros, J., Dadson, K., Xu, A., & Sweeney, G. (2009) · Diabetologia · doi:10.1007/s00125-009-1462-0 · Cited by 23
Globular adiponectin stimulates glucose transport in type 2 diabetic muscle
Kuoppamaa, H., Skrobuk, P., Sihvo, M., Hiukka, A., Chibalin, A., Zierath, J. R., & Koistinen, H. A. (2008) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.883 · Cited by 23
Dzhemileva, L. U., Захарова, Е. Н., Goncharenko, A. O., Vorontsova, M. V., Roumiantsev, S. A., Mokrysheva, N. G., Loguinova, M. Y., & Chekhonin, V. P. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1497298 · Cited by 24
Hall, J. I., Vora, N., Langworthy, R., Stock, S., Momin, A., Sherwood, R. A., le Roux, C. W., & Alaghband‐Zadeh, J. (2011) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/acb.2011.010199 · Cited by 21
Yoo, Y. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12064 · Cited by 20
Short-Term Regulation of Adiponectin Secretion in Rat Adipocytes
Szkudelski, T., Nogowski, L., & Szkudelska, K. (2011) · Physiological Research · doi:10.33549/physiolres.931971 · Cited by 19
Li, X., Choi, Y. J., Yanakawa, Y., & Park, T. (2013) · International Journal of Obesity · doi:10.1038/ijo.2013.70 · Cited by 18
Adiponectin’s roles in lipid and glucose metabolism modulation in fish: Mechanisms and perspectives
Ji, R., Xu, X., Turchini, G. M., Mai, K., & Ai, Q. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12569 · Cited by 17
Pathogenesis of Nonalcoholic Fatty Liver Disease
Machado, M. V., & Diehl, A. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-37591-7.00025-2 · Cited by 17
Suzuki, M., Vázquez‐Medina, J. P., Viscarra, J. A., Soñanez‐Organis, J. G., Crocker, D. E., & Rudy, O. (2013) · Journal of Experimental Biology · doi:10.1242/jeb.085225 · Cited by 17
Fraterrigo, G., Fabbrini, E., Mittendorfer, B., O’Rahilly, S., Scherer, P. E., Patterson, B. W., & Klein, S. (2012) · Cardiorenal Medicine · doi:10.1159/000340037 · Cited by 16
Fat, fire and muscle – The role of adiponectin in pulmonary vascular inflammation and remodeling
Medoff, B. D. (2012) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2012.06.006 · Cited by 16
Kim, J., Kim, C., Jo, K., Lee, I. S., Kim, J., & Kim, J. S. (2020) · Nutrients · doi:10.3390/nu12123612 · Cited by 17
Mechanism of Action and Risk Prediction of Adiponectin in Cardiovascular Diseases
Li, S., Han, X., Song, J., Dong, M., & Xie, T. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2908286 · Cited by 18
Chang, E., Choi, J. M., Park, S. E., Rhee, E., Lee, W., Oh, K.-W., Park, S., & Park, C. (2015) · Life Sciences · doi:10.1016/j.lfs.2015.02.013 · Cited by 15
Jeon, H.-J., Yoon, K.-Y., Koh, E., Choi, J., Kim, K., Choi, H., & Lee, B.-Y. (2015) · Journal of Food and Nutrition Research · doi:10.12691/jfnr-3-10-5 · Cited by 15
Tanyanskiy, D. A., & Denisenko, A. D. (2021) · Obesity and metabolism · doi:10.14341/omet12754 · Cited by 13
Prediction of functional phosphorylation sites by incorporating evolutionary information
Niu, S., Wang, Z., Ge, D., Zhang, G., & Li, Y. (2012) · Protein & Cell · doi:10.1007/s13238-012-2048-z · Cited by 13
Karschin, J., Lagerpusch, M., Enderle, J., Eggeling, B., Müller, M. J., & Bosy‐Westphal, A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0117865 · Cited by 13
Rashtiani, S., Goudarzi, I., Jafari, A., & Rohampour, K. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135721 · Cited by 13
Pulmonary Arterial Hypertension and Insulin Resistance
Bradley, D. B. E. A. (2014) · Journal of Molecular and Genetic Medicine · doi:10.4172/1747-0862.s1-015 · Cited by 12
Kawabeta, K., Hase-Tamaru, S., Yuasa, M., Suruga, K., Sugano, M., & Koba, K. (2019) · Journal of Oleo Science · doi:10.5650/jos.ess18232 · Cited by 12
Sarsani, V., Brotman, S. M., Yin, X., Silva, L. F., Laakso, M., & Spracklen, C. N. (2023) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2023.100252 · Cited by 13
Sun, L., & Liu, X. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0062 · Cited by 11
Cersósimo, E., Xu, X., Terasawa, T., & Dong, L. (2020) · Molecular Biology Reports · doi:10.1007/s11033-020-05707-w · Cited by 12
Self-citationOjeda, M. L., Nogales, F., Carreras, O., Pajuelo, E., Gallego‐López, M. D. C., Herrera, I. R., Begines, B., Moreno‐Fernández, J., Díaz‐Castro, J., & Alcudia, A. (2022) · Nutrients · doi:10.3390/nu14173571 · Cited by 13
Insulin Inhibits the Expression of Adiponectin and AdipoR2 mRNA in Cultured Bovine Adipocytes
Sun, Y. G., Zan, L., Wang, H. B., Guo, H., Yang, D.-C., Zhao, X. L., & Gui, L. (2009) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2009.90159 · Cited by 11
Insulin‐regulated expression of adiponectin receptors in muscle and fat cells
Sattar, A. A., & Sattar, R. (2012) · Cell Biology International · doi:10.1042/cbi20120294 · Cited by 10
Anwar, C., Lin, J., Tsai, M., Ho, C., & Lai, C. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176789 · Cited by 10
From diabetes to renal aging: the therapeutic potential of adiponectin
Karamian, M., Moossavi, M., & Hemmati, M. (2021) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-021-00790-4 · Cited by 9
Sadashiv, Tiwari, S., Paul, B. N., Kumar, S., Chandra, A., Dhananjai, S., & Negi, M. P. S. (2013) · HORMONES · doi:10.1007/bf03401293 · Cited by 8
Tan, Y., Liu, H., Zhao, B., Xia, Z., Zhang, Y., Zhang, D., Li, M., Cao, Y., Zhang, Z., Bi, Y., et al. (2016) · Endocrine Journal · doi:10.1507/endocrj.ej16-0158 · Cited by 9
Self-citationMorakinyo, A., Ajiboye, K. I., Oludare, G. O., & Samuel, T. A. (2016) · Nigerian Journal of Physiological Sciences · Cited by 8
Vu, V. P., Dadson, K., Odisho, T., Kim, W. I., Zhou, X., Thong, F. S. L., & Sweeney, G. (2010) · International Journal of Obesity · doi:10.1038/ijo.2010.160 · Cited by 9
Zheng, W., Yang, J., Zhang, Q., Cheng, M., Shaukat, H., & Qin, H. (2023) · Plant Foods for Human Nutrition · doi:10.1007/s11130-023-01108-z · Cited by 8
Globular adiponectin activates Akt in cultured myocytes
Sattar, A. A., & Sattar, R. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.027 · Cited by 8
Will, K., Kuzinski, J., Kalbe, C., Palin, M., & Rehfeldt, C. (2013) · Domestic Animal Endocrinology · doi:10.1016/j.domaniend.2013.09.002 · Cited by 8
Al-Suhaimi, E. A., Alkulaifi, F. M., Ravinayagam, V., & Al-Qahtani, M. H. (2012) · The Open Endocrinology Journal · doi:10.2174/1874216501106010110 · Cited by 8
Clinical Implication of Adiponectin
Lim, S. K., & Jang, H. C. (2008) · Korean Diabetes Journal · doi:10.4093/kdj.2008.32.2.85 · Cited by 8
The Gut Microbiome After Bariatric Surgery
Solar, C., Escalona, A., & Garrido, D. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815249-2.00024-5 · Cited by 8
Activation of mTOR for the loss of skeletal muscle in a hindlimb-suspended rat model
Yoo, Y., Park, J. H., Seo, D.-H., Eom, S., Jung, Y., Kim, T., Han, T.-Y., & Kim, H. S. (2015) · International Journal of Precision Engineering and Manufacturing · doi:10.1007/s12541-015-0130-1 · Cited by 8
Herrera, I. R., Nogales, F., Gallego‐López, M. D. C., Díaz‐Castro, J., Moreno‐Fernández, J., Ochoa, J. J., Carreras, O., & Ojeda, M. L. (2023) · The Journal of Physiology · doi:10.1113/jp285362 · Cited by 7
Shan, Q., Liu, J., Qu, F., Chen, A., & He, W. (2024) · Environmental Toxicology · doi:10.1002/tox.24094 · Cited by 7
Hashim, K.-N., Chin, K., & Ahmad, F. (2023) · Molecules · doi:10.3390/molecules28062790 · Cited by 12
Wen, F., Hou, J., Ji, X., Chu, X., Liu, X., Shi, Z., & Song, Z. (2023) · Gene · doi:10.1016/j.gene.2023.147193 · Cited by 6
Molecular Mechanisms Linking Adiponectin Receptor Signalling and Cancer
Nakajima, A., Endo, H., Yoneda, K., Fujisawa, T., Sugiyama, M., Hosono, K., Nozaki, Y., Takahashi, H., Fujita, K., Yoneda, M., et al. (2010) · The Open Obesity Journal · doi:10.2174/1876823701002010043 · Cited by 6
Ritchie, I. R. W., Wright, D. C., & Dyck, D. J. (2014) · Physiological Reports · doi:10.14814/phy2.12146 · Cited by 6
Garcia, D., Mihaylova, M. M., & Shaw, R. J. (2020) · Wiley eBooks · doi:10.1002/9781119436812.ch38 · Cited by 6
Cao, Y., Xu, R., & Zhang, J. (2026) · Frontiers in Pediatrics · doi:10.3389/fped.2026.1679527 · Cited by 5
Inflammatory markers and body mass index amoung hispanic children
Lang, H., Loudermilk, E. N., Clark, W. A., Marrs, J., Joyner, T. A., Wang, L., Gerber, K. S., & Alamian, A. (2024) · PLoS ONE · doi:10.1371/journal.pone.0289523 · Cited by 5
Self-citationNakamura, S., Asaba, S., Tanaka, M., & Matsui, T. (2024) · ACS Omega · doi:10.1021/acsomega.4c09030 · Cited by 6
Fasting glucose to adiponectin ratio is associated with the development of type 2 diabetes mellitus
Islam, N., Hossain, M., Hafizur, R. M., Khan, I., Rashid, M., Shefin, S., Haque, M., Faruque, M., & Ali, L. (2011) · Journal of Diabetology · doi:10.4103/2078-7685.197964 · Cited by 5
Adiponectin and Adiponectin Signaling
Hadley, J. T., Ryu, J., & Dong, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819801-8.00013-2 · Cited by 6
Self-citationJang, J., Park, Y.-H., Lee, D., Lee, H., Lim, J., Yoon, S. A., Lee, H., Ahn, J., Jeong, S., Shin, S. S., et al. (2019) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2019.111943 · Cited by 4
Adiponectin and Leptin—Considerations in Adult Patients with Spinal Muscular Atrophy Type 3
Miletić, M., Stević, Z., Perić, S., Tančić‐Gajić, M., Rakočević, J., Stojanovic, M. M., Marković, B., & Žarković, M. (2025) · Diagnostics · doi:10.3390/diagnostics15050529 · Cited by 4
Engin, A. B., & Engin, A. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-49844-3_2 · Cited by 4
Amatya, R., Min, K. A., & Shin, M. C. (2022) · Journal of Pharmaceutical Investigation · doi:10.1007/s40005-022-00566-y · Cited by 4
Barquissau, V., & Morio, B. (2011) · Nutrition Clinique et Métabolisme · doi:10.1016/j.nupar.2011.07.003 · Cited by 5
Ho, G. J., Takamatsu, Y., Waragai, M., Wada, R., Sugama, S., Takenouchi, T., Fujita, M., Ali, A., Hsieh, M. H.-I., & Hashimoto, M. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1649141 · Cited by 4
Insulin and the Physiology of Carbohydrate Metabolism
Pereira, S., & Giacca, A. (2011) · Energy balance and cancer · doi:10.1007/978-1-4419-9911-5_1 · Cited by 3
Will, K., Kuzinski, J., Palin, M., Hildebrandt, J., & Rehfeldt, C. (2014) · Archives animal breeding/Archiv für Tierzucht · doi:10.7482/0003-9438-57-029 · Cited by 3
Maintaining Energy Balance in Health and Disease: Role of the AMP-Activated Protein Kinase
Scott, J. W. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_9 · Cited by 2
Susceptibility to insulin resistance in indigenous Australians may be down stream of resistin.
Good, D. M., Cardinal, J. W., Ware, R. S., Marks, L. H., Kesting, J. B., Chan, L. C. K., & Shaw, J. T. E. (2019) · International Journal of Diabetes and Metabolism · doi:10.1159/000497645 · Cited by 2
Yu, M., Shen, Z., Qiu, X.-S., & Mo, Q. (2012) · Journal of Investigative Medicine · doi:10.2310/jim.0b013e3182746ce8 · Cited by 2
Amato, A. C. M., Amato, J. L. S., & Benitti, D. A. (2025) · medRxiv · doi:10.64898/2025.12.01.25341350 · Cited by 2
Al-Zahrani, I. (2012) · Journal of Diabetes and Endocrinology · doi:10.5897/jde12.013 · Cited by 1
ADIPONECTIN AS AN ENDOGENOUS REGULATOR OF THE HYPOTHALAMIC-PITUITARY-GONADAL AXIS
Ryzhov, J. R., & Shpakov, A. O. (2018) · Translational Medicine · doi:10.18705/2311-4495-2018-5-5- · Cited by 1
Adiponectin, Diabetes, and the Cardiovascular System
Gasbarrino, K., Boutari, C., Filippaios, A., Gianopoulos, I., Daskalopoulou, S. S., & Mantzoros, C. S. (2023) · Contemporary cardiology · doi:10.1007/978-3-031-13177-6_8 · Cited by 1
Rashtiani, S., Goudarzi, I., Jafari, A., & Rohampour, K. (2023) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1871524923666230908092530 · Cited by 1
Richard, A. J., & Stephens, J. M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813814-4.00020-1 · Cited by 1
Bai, Y., Yuan, P., Zhang, H., Ramachandran, R., Yang, N., & Song, J. (2020) · Poultry Science · doi:10.1016/j.psj.2020.06.004 · Cited by 1
Adiponectin and insulin: molecular mechanisms of metabolic disorders
Учасова, Е. Г., Gruzdeva, O. V., Belik, E. V., & Dyleva, Y. A. (2020) · Bulletin of Siberian Medicine · doi:10.20538/1682-0363-2020-3-188-197 · Cited by 1
AMPK: Central Regulator of Glucose and Lipid Metabolism
Mihaylova, M. M., & Shaw, R. J. (2009) · Wiley eBooks · doi:10.1002/9780470747919.ch35 · Cited by 1
The novel adiponectin-resistin (AR) and insulin resistance (IR~AR~) indexesPreprint
Lau, C., & Muniandy, S. (2010) · Nature Precedings · doi:10.1038/npre.2010.4191.1 · Cited by 1
Insulin signalling in human adipocytes mechanisms of insulin resistance in type 2 diabetes
Danielsson, A. (2007) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1
Papizan, J. B. (2007) · Cited by 1
Glund, S. (2007) · Figshare
Cerqueira, F. M. (2012) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2012.tde-24022013-151501
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Vázquez, I. N., Fernández‐Veledo, S., García‐Guerra, L., Vila‐Bedmar, R., & Lorenzo, M. (2008) · Anales de la Real Academia Nacional de Farmacia
Nyman, E. (2014) · Linköping University Electronic Press eBooks · doi:10.3384/diss.diva-104725
Alert, T. (2007)
Insulin signaling dynamics in human adipocytes
Nyman, E. (2014)
Obesity and Cardiac Dysfunction
Sweeney, G., Litwin, S. E., & Abel, E. D. (2010) · Springer eBooks · doi:10.1007/978-1-4419-1607-5_14
Dashty, M. (2014) · Journal of Diabetes & Metabolism · doi:10.4172/2155-6156.1000406
Schofield, C. J. (2011) · OpenGrey (Institut de l'Information Scientifique et Technique)
Metadata
- Authors
- Wang, C., Mao, X., Wang, L., Liu, M., Wetzel, M. D., Guan, K.-L., Dong, L. Q., & Liu, F.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- University of Michigan (US)
- Corresponding author
- Liu, Feng
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 282
- Issue
- 11
- Pages
- 7991-7996
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2164663878
- Cited by
- 210
- References
- 37
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 5 · 2023: 11 · 2022: 5 · 2021: 15 · 2020: 12 · 2019: 10 · 2018: 10 · 2017: 2 · 2016: 6 · 2015: 8 · 2014: 11 · 2013: 18 · 2012: 16
- FWCI
- 12.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK069930)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- adiponectin, insulin sensitivity, insulin signaling, IRS-1 serine phosphorylation, p70 S6 kinase, Akt phosphorylation, LKB1, AMPK, TSC2, Rheb, TSC1, rapamycin, myotubes
- MeSH terms
- Tuberous Sclerosis Complex 1 Protein, Tuberous Sclerosis Complex 2 Protein, Animals, Insulin, Models, Biological, Phosphoproteins, Phosphorylation, Serine, Transfection, Signal Transduction, Protein Serine-Threonine Kinases, Tumor Suppressor Proteins, Ribosomal Protein S6 Kinases, 70-kDa, p38 Mitogen-Activated Protein Kinases, Mice, Adiponectin, AMP-Activated Protein Kinases, Insulin Receptor Substrate Proteins
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 ›
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