[1] D. H. Wasserman and J. E. Ayala, “Interaction of physiological mechanisms in control of muscle glucose uptake.,” Clin. Exp. Pharmacol. Physiol., vol. 32, no. 4, pp. 319–23, Apr. 2005.
[2] F. H. Nystrom and M. J. Quon, “Insulin signalling: metabolic pathways and mechanisms for specificity.,” Cell. Signal., vol. 11, no. 8, pp. 563–74, Aug. 1999.
[3] K. Shi et al., “Protein-tyrosine phosphatase 1B associates with insulin receptor and negatively regulates insulin signaling without receptor internalization.,” J. Biochem., vol. 136, no. 1, pp. 89–96, Jul. 2004.
[4] A. R. Saltiel and C. R. Kahn, “Insulin signalling and the regulation of glucose and lipid metabolism.,” Nature, vol. 414, no. 6865, pp. 799–806, Dec. 2001.
[5] N. J. Bryant, R. Govers, and D. E. James, “Regulated transport of the glucose transporter GLUT4,” Nat. Rev. Mol. Cell Biol., vol. 3, no. 4, pp. 267–277, Apr. 2002.
[6] R. Fragoso and J. T. Barata, “PTEN and leukemia stem cells.,” Adv. Biol. Regul., vol. 56, pp. 22–9, Sep. 2014.
[7] S. Alsadat, H. Khorami, A. Movahedi, K. Kuzwah, A. Mutalib, and M. Sokhini, “PI3K / AKT pathway in modulating glucose homeostasis and its alteration in Diabetes,” Ann. Med. Biomed. Sci., vol. 1, no. 2, pp. 46–55, 2015.
[8] N. R. Leslie, M. J. Dixon, M. Schenning, A. Gray, and I. H. Batty, “Distinct inactivation of PI3K signalling by PTEN and 5-phosphatases.,” Adv. Biol. Regul., vol. 52, no. 1, pp. 205–13, Jan. 2012.
[9] A. M. Johnston, L. Pirola, and E. Van Obberghen, “Molecular mechanisms of insulin receptor substrate protein-mediated modulation of insulin signalling.,” FEBS Lett., vol. 546, no. 1, pp. 32–6, Jul. 2003.
[10] L. V Ravichandran, H. Chen, Y. Li, and M. J. Quon, “Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor.,” Mol. Endocrinol., vol. 15, no. 10, pp. 1768–80, Oct. 2001.
[11] D. P. Choi et al., “Serum 25-Hydroxyvitamin D and Insulin Resistance in Apparently Healthy Adolescents,” PLoS One, vol. 9, no. 7, p. e103108, Jul. 2014.
[12] C. C. Borges, A. F. Salles, I. Bringhenti, V. Souza-Mello, C. A. Mandarim-de-Lacerda, and M. B. Aguila, “Adverse effects of vitamin D deficiency on the Pi3k/Akt pathway and pancreatic islet morphology in diet-induced obese mice,” Mol. Nutr. Food Res., vol. 60, no. 2, pp. 346–357, Feb. 2016.
[13] J. Yang et al., “The role of 1,25-dyhydroxyvitamin D3 in mouse liver ischemia reperfusion injury: regulation of autophagy through activation of MEK/ERK signaling and PTEN/PI3K/Akt/mTORC1 signaling.,” Am. J. Transl. Res., vol. 7, no. 12, pp. 2630–45, 2015.
[14] A. S. Zaulkffali et al., “Vitamins D and E Stimulate the PI3K-AKT Signalling Pathway in Insulin-Resistant SK-N-SH Neuronal Cells,” Nutrients, vol. 11, no. 10, p. 2525, Oct. 2019.
[15] K. J. Livak and T. D. Schmittgen, “Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method,” Methods, vol. 25, no. 4, pp. 402–408, Dec. 2001.
[16] U. Turpeinen, U. Hohenthal, and U.-H. Stenman, “Determination of 25-Hydroxyvitamin D in Serum by HPLC and Immunoassay,” Clin. Chem., vol. 49, no. 9, 2003.
[17] S. S. Schwartz, S. Epstein, B. E. Corkey, S. F. A. Grant, J. R. Gavin, and R. B. Aguilar, “The Time Is Right for a New Classification System for Diabetes: Rationale and Implications of the β-Cell–Centric Classification Schema,” Diabetes Care, vol. 39, no. 2, pp. 179–186, Feb. 2016.
[18] J. T. Wong et al., “Pten (phosphatase and tensin homologue gene) haploinsufficiency promotes insulin hypersensitivity.,” Diabetologia, vol. 50, no. 2, pp. 395–403, Feb. 2007.
[19] J. Zhou et al., “Inhibition of PTEN Activity Aggravates Post Renal Fibrosis in Mice with Ischemia Reperfusion-Induced Acute Kidney Injury.,” Cell. Physiol. Biochem., vol. 43, no. 5, pp. 1841–1854, 2017.
[20] J. Yang and Q. Chen, “The Effects of Acetylation of PTEN on Hepatic Gluconeogenesis,” J. Alzheimer’s Dis. Park., vol. 6, no. 3, pp. 1–7, Jun. 2016.
[21] J. Zhou et al., “Inhibition of PTEN activity aggravates cisplatin-induced acute kidney injury,” Oncotarget, vol. 8, no. 61, pp. 103154–103166, Nov. 2017.
[22] C. S. Choi, Y.-B. Kim, F. N. Lee, J. M. Zabolotny, B. B. Kahn, and J. H. Youn, “Lactate induces insulin resistance in skeletal muscle by suppressing glycolysis and impairing insulin signaling.,” Am. J. Physiol. Endocrinol. Metab., vol. 283, no. 2, pp. E233-40, Aug. 2002.
[23] G. Frangioudakis, J.-M. Ye, and G. J. Cooney, “Both saturated and n-6 polyunsaturated fat diets reduce phosphorylation of insulin receptor substrate-1 and protein kinase B in muscle during the initial stages of in vivo insulin stimulation.,” Endocrinology, vol. 146, no. 12, pp. 5596–603, Dec. 2005.
[24] L. P. Singh, D. Gennerette, S. Simmons, and E. D. Crook, “Glucose-induced insulin resistance of phosphatidylinositol 3’-OH kinase and AKT/PKB is mediated by the hexosamine biosynthesis pathway.,” J. Diabetes Complications, vol. 15, no. 2, pp. 88–96, Jan. .
[25] R. M. O’Brien, R. S. Streeper, J. E. Ayala, B. T. Stadelmaier, and L. A. Hornbuckle, “Insulin-regulated gene expression.,” Biochem. Soc. Trans., vol. 29, no. Pt 4, pp. 552–8, Aug. 2001.
[26] P. Carlsson and M. Mahlapuu, “Forkhead transcription factors: key players in development and metabolism.,” Dev. Biol., vol. 250, no. 1, pp. 1–23, Oct. 2002.
[27] A. Pal et al., “PTEN Mutations as a Cause of Constitutive Insulin Sensitivity and Obesity,” N. Engl. J. Med., vol. 367, no. 11, pp. 1002–1011, Sep. 2012.
[28] A. S. Paintlia, M. K. Paintlia, A. K. Singh, J. K. Orak, and I. Singh, “Activation of PPAR-γ and PTEN cascade participates in lovastatin-mediated accelerated differentiation of oligodendrocyte progenitor cells,” Glia, vol. 58, no. 14, pp. 1669–1685, Nov. 2010.
[29] P. Gual, Y. Le Marchand-Brustel, and J. Tanti, “Positive and negative regulation of glucose uptake by hyperosmotic stress.,” Diabetes Metab., vol. 29, no. 6, pp. 566–75, Dec. 2003.
[30] K. Morino, K. F. Petersen, and G. I. Shulman, “Molecular mechanisms of insulin resistance in humans and their potential links with mitochondrial dysfunction.,” Diabetes, vol. 55 Suppl 2, pp. S9–S15, Dec. 2006.
[31] M. Colomiere, M. Permezel, C. Riley, G. Desoye, and M. Lappas, “Defective insulin signaling in placenta from pregnancies complicated by gestational diabetes mellitus.,” Eur. J. Endocrinol., vol. 160, no. 4, pp. 567–78, Apr. 2009.
[32] K. I. Ishibashi, T. Imamura, P. M. Sharma, J. Huang, S. Ugi, and J. M. Olefsky, “Chronic endothelin-1 treatment leads to heterologous desensitization of insulin signaling in 3T3-L1 adipocytes.,” J. Clin. Invest., vol. 107, no. 9, pp. 1193–202, May 2001.
[33] Y. F. Liu et al., “Insulin stimulates PKCzeta -mediated phosphorylation of insulin receptor substrate-1 (IRS-1). A self-attenuated mechanism to negatively regulate the function of IRS proteins.,” J. Biol. Chem., vol. 276, no. 17, pp. 14459–65, Apr. 2001.
[34] Y. Zick, “Molecular basis of insulin action.,” Novartis Found. Symp., vol. 262, pp. 36–50; disucssion 50-5, 265–8, Jan. 2004.
[35] Y. Zick, “Ser/Thr phosphorylation of IRS proteins: a molecular basis for insulin resistance.,” Sci. STKE, vol. 2005, no. 268, p. pe4, Jan. 2005.
[36] K. E. Wellen and G. S. Hotamisligil, “Inflammation, stress, and diabetes.,” J. Clin. Invest., vol. 115, no. 5, pp. 1111–9, May 2005.
[37] L. Simpson et al., “PTEN expression causes feedback upregulation of insulin receptor substrate 2.,” Mol. Cell. Biol., vol. 21, no. 12, pp. 3947–58, Jun. 2001.
[38] R. V Farese, M. P. Sajan, and M. L. Standaert, “Insulin-sensitive protein kinases (atypical protein kinase C and protein kinase B/Akt): actions and defects in obesity and type II diabetes.,” Exp. Biol. Med. (Maywood)., vol. 230, no. 9, pp. 593–605, Oct. 2005.
[39] P. H. Ducluzeau et al., “Regulation by insulin of gene expression in human skeletal muscle and adipose tissue. Evidence for specific defects in type 2 diabetes.,” Diabetes, vol. 50, no. 5, pp. 1134–42, May 2001.
[40] N. Nakashima, P. M. Sharma, T. Imamura, R. Bookstein, and J. M. Olefsky, “The tumor suppressor PTEN negatively regulates insulin signaling in 3T3-L1 adipocytes.,” J. Biol. Chem., vol. 275, no. 17, pp. 12889–95, Apr. 2000.
[41] H. Ono et al., “Regulation of phosphoinositide metabolism, Akt phosphorylation, and glucose transport by PTEN (phosphatase and tensin homolog deleted on chromosome 10) in 3T3-L1 adipocytes.,” Mol. Endocrinol., vol. 15, no. 8, pp. 1411–22, Aug. 2001.
[42] M. Butler et al., “Specific inhibition of PTEN expression reverses hyperglycemia in diabetic mice.,” Diabetes, vol. 51, no. 4, pp. 1028–34, Apr. 2002.
[43] Z. Tong et al., “Pancreas-specific Pten deficiency causes partial resistance to diabetes and elevated hepatic AKT signaling.,” Cell Res., vol. 19, no. 6, pp. 710–9, Jun. 2009.
[44] N. Wijesekara et al., “Muscle-specific Pten deletion protects against insulin resistance and diabetes.,” Mol. Cell. Biol., vol. 25, no. 3, pp. 1135–45, Feb. 2005.
[45] M. Delibegovic et al., “Improved glucose homeostasis in mice with muscle-specific deletion of protein-tyrosine phosphatase 1B.,” Mol. Cell. Biol., vol. 27, no. 21, pp. 7727–34, Nov. 2007.
[46] B. Wang et al., “Differences in myocardial PTEN expression and Akt signalling in type 2 diabetic and nondiabetic patients undergoing coronary bypass surgery,” Clin. Endocrinol. (Oxf)., vol. 74, no. 6, pp. 705–713, Jun. 2011.
[47] Y. Ye et al., “Phosphodiesterase-3 inhibition augments the myocardial infarct size-limiting effects of exenatide in mice with type 2 diabetes,” Am. J. Physiol. Circ. Physiol., vol. 304, no. 1, pp. H131–H141, Jan. 2013.
[48] J. Qian, S. Ling, A. C. Castillo, B. Long, Y. Birnbaum, and Y. Ye, “Regulation of phosphatase and tensin homolog on chromosome 10 in response to hypoxia,” Am. J. Physiol. Circ. Physiol., vol. 302, no. 9, pp. H1806–H1817, May 2012.
[49] Z. Hu et al., “PTEN Inhibition Improves Muscle Regeneration in Mice Fed a High-Fat Diet,” Diabetes, vol. 59, no. 6, pp. 1312–1320, Jun. 2010.
[50] D. Ryu et al., “Endoplasmic Reticulum Stress Promotes LIPIN2-Dependent Hepatic Insulin Resistance,” Diabetes, vol. 60, no. 4, pp. 1072–1081, Apr. 2011.
[51] R. Neto-Ferreira, V. N. Rocha, V. Souza-Mello, C. A. Mandarim-de-Lacerda, and J. J. de Carvalho, “Pleiotropic effects of rosuvastatin on the glucose metabolism and the subcutaneous and visceral adipose tissue behavior in C57Bl/6 mice,” Diabetol. Metab. Syndr., vol. 5, no. 1, p. 32, Jul. 2013.
[52] T. Sasaki, J. Sasaki, T. Sakai, S. Takasuga, and A. Suzuki, “The physiology of phosphoinositides.,” Biol. Pharm. Bull., vol. 30, no. 9, pp. 1599–604, Sep. 2007.
[53] W. S. Park et al., “Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging.,” Mol. Cell, vol. 30, no. 3, pp. 381–92, May 2008.
[54] P. Várnai et al., “Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners.,” J. Cell Sci., vol. 118, no. Pt 20, pp. 4879–88, Oct. 2005.
[55] P. Manna and S. K. Jain, “Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (A,” J. Biol. Chem., vol. 286, no. 46, pp. 39848–59, Nov. 2011.
[56] J. L. Rains and S. K. Jain, “Oxidative stress, insulin signaling, and diabetes.,” Free Radic. Biol. Med., vol. 50, no. 5, pp. 567–75, Mar. 2011.
[57] C.-Y. Chen, J. Chen, L. He, and B. L. Stiles, “PTEN: Tumor Suppressor and Metabolic Regulator,” Front. Endocrinol. (Lausanne)., vol. 9, p. 338, Jul. 2018.
[58] N. M. McLoughlin, C. Mueller, and T. N. Grossmann, “The Therapeutic Potential of PTEN Modulation: Targeting Strategies from Gene to Protein.,” Cell Chem. Biol., vol. 25, no. 1, pp. 19–29, Jan. 2018.
[59] R. Xue et al., “Selective inhibition of PTEN preserves ischaemic post-conditioning cardioprotection in STZ-induced Type 1 diabetic rats: role of the PI3K/Akt and JAK2/STAT3 pathways.,” Clin. Sci. (Lond)., vol. 130, no. 5, pp. 377–92, Mar. 2016.
[60] A. Pal et al., “PTEN mutations as a cause of constitutive insulin sensitivity and obesity.,” N. Engl. J. Med., vol. 367, no. 11, pp. 1002–11, Sep. 2012.
[61] X. Wang et al., “Cross talk between miR-214 and PTEN attenuates glomerular hypertrophy under diabetic conditions,” Sci. Rep., vol. 6, no. 1, p. 31506, Nov. 2016.
[62] T. Sumita et al., “Mediobasal hypothalamic PTEN modulates hepatic insulin resistance independently of food intake in rats,” Am. J. Physiol. Metab., vol. 307, no. 1, pp. E47–E60, Jul. 2014.
[63] B. Wang et al., “Differences in myocardial PTEN expression and Akt signalling in type 2 diabetic and nondiabetic patients undergoing coronary bypass surgery.,” Clin. Endocrinol. (Oxf)., vol. 74, no. 6, pp. 705–13, Jun. 2011.
[64] Y. Arkun, “Dynamic Modeling and Analysis of the Cross-Talk between Insulin/AKT and MAPK/ERK Signaling Pathways,” PLoS One, vol. 11, no. 3, p. e0149684, Mar. 2016.
[65] P. R. Somvanshi, M. Tomar, and V. Kareenhalli, “Computational Analysis of Insulin-Glucagon Signalling Network: Implications of Bistability in Metabolic Homeostasis and Disease states,” 2019.
[66] G. Wang, “Raison d’être of insulin resistance: the adjustable threshold hypothesis.,” J. R. Soc. Interface, vol. 11, no. 101, p. 20140892, Dec. 2014.
[67] N. Sulaimanov, M. Klose, H. Busch, and M. Boerries, “Understanding the mTOR signaling pathway via mathematical modeling.,” Wiley Interdiscip. Rev. Syst. Biol. Med., vol. 9, no. 4, 2017.
[68] G. Wang, “Global quantitative biology can illuminate ontological connections between diseases,” Quant. Biol., vol. 5, no. 2, pp. 191–198, Jun. 2017.
[69] L. Giri, V. K. Mutalik, and K. V Venkatesh, “A steady state analysis indicates that negative feedback regulation of PTP1B by Akt elicits bistability in insulin-stimulated GLUT4 translocation.,” Theor. Biol. Med. Model., vol. 1, p. 2, 2004.
[70] S.-X. Tan et al., “Amplification and demultiplexing in insulin-regulated Akt protein kinase pathway in adipocytes.,” J. Biol. Chem., vol. 287, no. 9, pp. 6128–38, Feb. 2012.
[71] J. E. Ferrell, “Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability.,” Curr. Opin. Cell Biol., vol. 14, no. 2, pp. 140–8, Apr. 2002.
[72] D. Angeli, J. E. Ferrell, and E. D. Sontag, “Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems.,” Proc. Natl. Acad. Sci. U. S. A., vol. 101, no. 7, pp. 1822–7, Feb. 2004.
[73] J. E. Ferrell, “Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs.,” Trends Biochem. Sci., vol. 21, no. 12, pp. 460–6, Dec. 1996.
[74] Z. Harel, P. Flanagan, M. Forcier, and D. Harel, “Low Vitamin D Status Among Obese Adolescents: Prevalence and Response to Treatment,” J. Adolesc. Heal., vol. 48, no. 5, pp. 448–452, May 2011.
[75] C. A. Peterson, A. K. Tosh, and A. M. Belenchia, “Vitamin D insufficiency and insulin resistance in obese adolescents.,” Ther. Adv. Endocrinol. Metab., vol. 5, no. 6, pp. 166–89, Dec. 2014.
[76] B. Garanty-Bogacka et al., “Serum 25-hydroxyvitamin D (25-OH-D) in obese adolescents.,” Endokrynol. Pol., vol. 62, no. 6, pp. 506–11, 2011.
[77] J. R. Ortlepp, J. Metrikat, M. Albrecht, A. von Korff, P. Hanrath, and R. Hoffmann, “The vitamin D receptor gene variant and physical activity predicts fasting glucose levels in healthy young men.,” Diabet. Med., vol. 20, no. 6, pp. 451–4, Jun. 2003.
[78] B. J. Boucher, N. Mannan, K. Noonan, C. N. Hales, and S. J. Evans, “Glucose intolerance and impairment of insulin secretion in relation to vitamin D deficiency in east London Asians.,” Diabetologia, vol. 38, no. 10, pp. 1239–45, Oct. 1995.
[79] S. Iyengar, R. F. Hamman, J. A. Marshall, P. P. Majumder, and R. E. Ferrell, “On the role of vitamin D binding globulin in glucose homeostasis: results from the San Luis Valley Diabetes Study.,” Genet. Epidemiol., vol. 6, no. 6, pp. 691–8, 1989.
[80] C. Calle et al., “Genomic actions of 1,25-dihydroxyvitamin D3 on insulin receptor gene expression, insulin receptor number and insulin activity in the kidney, liver and adipose tissue of streptozotocin-induced diabetic rats,” BMC Mol. Biol., vol. 9, no. 1, p. 65, 2008.
[81] K. T. Peeyush, B. Savitha, A. Sherin, T. R. Anju, P. Jes, and C. S. Paulose, “Cholinergic, dopaminergic and insulin receptors gene expression in the cerebellum of streptozotocin-induced diabetic rats: functional regulation with Vitamin D3 supplementation.,” Pharmacol. Biochem. Behav., vol. 95, no. 2, pp. 216–22, Apr. 2010.
[82] C. Blanco-Aparicio, O. Renner, J. F. M. Leal, and A. Carnero, “PTEN, more than the AKT pathway,” Carcinogenesis, vol. 28, no. 7, pp. 1379–1386, Jul. 2007.
[83] B. Stiles, M. Groszer, S. Wang, J. Jiao, and H. Wu, “PTENless means more,” Dev. Biol., vol. 273, no. 2, pp. 175–184, Sep. 2004.
[84] M. Butler et al., “Specific Inhibition of PTEN Expression Reverses Hyperglycemia in Diabetic Mice,” Diabetes, vol. 51, no. 4, pp. 1028–1034, Apr. 2002.
[85] C. Kurlawalla-Martinez, B. Stiles, Y. Wang, S. U. Devaskar, B. B. Kahn, and H. Wu, “Insulin Hypersensitivity and Resistance to Streptozotocin-Induced Diabetes in Mice Lacking PTEN in Adipose Tissue,” Mol. Cell. Biol., vol. 25, no. 6, pp. 2498–2510, Mar. 2005.
[86] N. Kamo, B. Ke, R. W. Busuttil, and J. W. Kupiec-Weglinski, “PTEN-mediated akt/β-Catenin/foxo1 signaling regulates innate immune responses in mouse liver ischemia/reperfusion injury,” Hepatology, vol. 57, no. 1, pp. 289–298, Jan. 2013.
[87] M. Peyrou et al., “Hepatic PTEN deficiency improves muscle insulin sensitivity and decreases adiposity in mice,” J. Hepatol., vol. 62, no. 2, pp. 421–429, Feb. 2015.
[88] G. Xu et al., “MiR-26b modulates insulin sensitivity in adipocytes by interrupting the PTEN/PI3K/AKT pathway,” Int. J. Obes., vol. 39, no. 10, pp. 1523–1530, Oct. 2015.
[89] G. Li et al., “miR-26b Promotes 3T3-L1 Adipocyte Differentiation Through Targeting PTEN,” DNA Cell Biol., vol. 36, no. 8, pp. 672–681, Aug. 2017.
[90] M. Malek et al., “PTEN Regulates PI(3,4)P2 Signaling Downstream of Class I PI3K,” Mol. Cell, vol. 68, no. 3, pp. 566-580.e10, Nov. 2017.
[91] A. Li, M. Qiu, H. Zhou, T. Wang, and W. Guo, “PTEN, Insulin Resistance and Cancer,” Curr. Pharm. Des., vol. 23, no. 25, pp. 3667–3676, Sep. 2017.
[92] P. Manna and S. K. Jain, “Hydrogen sulfide and L-cysteine increase phosphatidylinositol 3,4,5-trisphosphate (PIP3) and glucose utilization by inhibiting phosphatase and tensin homolog (PTEN) protein and activating phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (A,” J. Biol. Chem., vol. 286, no. 46, pp. 39848–59, Nov. 2011.
[93] P. T. Hawkins and L. R. Stephens, “Emerging evidence of signalling roles for PI(3,4)P2 in Class I and II PI3K-regulated pathways,” Biochem. Soc. Trans., vol. 44, no. 1, pp. 307–314, Feb. 2016.
[94] B. D. Manning and A. Toker, “AKT/PKB Signaling: Navigating the Network,” Cell, vol. 169, no. 3, pp. 381–405, Apr. 2017.
[95] N. Jethwa et al., “Endomembrane PtdIns(3,4,5)P3 activates the PI3K-Akt pathway,” J. Cell Sci., vol. 128, no. 18, pp. 3456–3465, Sep. 2015.
[96] R. Govers, “Cellular regulation of glucose uptake by glucose transporter GLUT4.,” Adv. Clin. Chem., vol. 66, pp. 173–240, 2014.
[97] Y. Ng, G. Ramm, J. A. Lopez, and D. E. James, “Rapid Activation of Akt2 Is Sufficient to Stimulate GLUT4 Translocation in 3T3-L1 Adipocytes,” Cell Metab., vol. 7, no. 4, pp. 348–356, Apr. 2008.
[98] G. Risso, M. Blaustein, B. Pozzi, P. Mammi, and A. Srebrow, “Akt/PKB: one kinase, many modifications,” Biochem. J., vol. 468, no. 2, pp. 203–214, Jun. 2015.
[99] C. Wang et al., “Glutamine Enhances the Hypoglycemic Effect of Insulin in L6 Cells via Phosphatidylinositol-3-Kinase (PI3K)/Protein Kinase B (AKT)/Glucose Transporter 4 (GLUT4) Signaling Pathway.,” Med. Sci. Monit., vol. 24, pp. 1241–1250, Mar. 2018.
[100] J. Choi, K.-J. Kim, E.-J. Koh, and B.-Y. Lee, “Gelidium elegans Extract Ameliorates Type 2 Diabetes via Regulation of MAPK and PI3K/Akt Signaling,” Nutrients, vol. 10, no. 1, p. 51, Jan. 2018.
[101] N. Yu et al., “Anti-Diabetic Effects of Jiang Tang Xiao Ke Granule via PI3K/Akt Signalling Pathway in Type 2 Diabetes KKAy Mice,” PLoS One, vol. 12, no. 1, p. e0168980, Jan. 2017.