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J. Med., 79, 12, 10.1016\u002FS0002-9343(85)80003-6\nOlefsky, 1995, Insulin resistance and non-insulin-dependent diabetes mellitus: cellular and molecular mechanisms, Am. J. Clin. Nutr., 61, 980S, 10.1093\u002Fajcn\u002F61.4.980S\nArner, 2002, Insulin resistance in type 2 diabetes: role of fatty acids, Diabetes Metab. Res. Rev., 18, S5, 10.1002\u002Fdmrr.254\nLebovitz, 2001, Insulin resistance: definition and consequences, Exp. Clin. Endocrinol. Diabetes, 109, S135, 10.1055\u002Fs-2001-18576\nReaven, 1993, Role of insulin resistance in human disease (syndrome X): an expanded definition, Annu. Rev. Med., 44, 121, 10.1146\u002Fannurev.me.44.020193.001005\nReaven, 1995, Pathophysiology of insulin resistance in human disease, Physiol. Rev., 75, 473, 10.1152\u002Fphysrev.1995.75.3.473\nSaltiel, 1996, Thiazolidinediones in the treatment of insulin resistance and type II diabetes, Diabetes, 45, 1661, 10.2337\u002Fdiabetes.45.12.1661\nLebovitz, 2001, Insulin resistance and its treatment by thiazolidinediones, Recent Prog. Horm. Res., 56, 265, 10.1210\u002Frp.56.1.265\nOlefsky, 2000, PPARγ and the treatment of insulin resistance, Trends Endocrinol. Metab., 11, 362, 10.1016\u002FS1043-2760(00)00306-4\nStumvoll, 2002, Glitazones: clinical effects and molecular mechanisms, Ann. Med., 34, 217, 10.1080\u002F713782132\nStumvoll, 2001, Insulin resistance and insulin sensitizers, Horm. Res., 55, 3, 10.1159\u002F000063466\nDeFronzo, 1992, Pathogenesis of NIDDM. A balanced overview, Diabetes Care, 15, 318, 10.2337\u002Fdiacare.15.3.318\nKitamura, 2003, Insulin receptor knockout mice, Annu. Rev. Physiol., 65, 313, 10.1146\u002Fannurev.physiol.65.092101.142540\nMauvais-Jarvis, 2002, Knockout models are useful tools to dissect the pathophysiology and genetics of insulin resistance, Clin. Endocrinol. (Oxf.), 57, 1, 10.1046\u002Fj.1365-2265.2002.01563.x\nBluher, 2002, Adipose tissue selective insulin receptor knockout protects against obesity and obesity-related glucose intolerance, Dev. Cell, 3, 25, 10.1016\u002FS1534-5807(02)00199-5\nGuerra, 2001, Brown adipose tissue-specific insulin receptor knockout shows diabetic phenotype without insulin resistance, J. Clin. Invest., 108, 1205, 10.1172\u002FJCI13103\nMichael, 2000, Loss of insulin signaling in hepatocytes leads to severe insulin resistance and progressive hepatic dysfunction, Mol. Cell, 6, 87, 10.1016\u002FS1097-2765(00)00010-1\nKulkarni, 1999, Tissuespecific knockout of the insulin receptor in pancreatic-β cells creates an insulin secretory defect similar to that in type 2 diabetes, Cell, 96, 329, 10.1016\u002FS0092-8674(00)80546-2\nBruning, 1998, A muscle-specific insulin receptor knockout exhibits features of the metabolic syndrome of NIDDM without altering glucose tolerance, Mol. Cell, 2, 559, 10.1016\u002FS1097-2765(00)80155-0\nBruning, 2000, Role of brain insulin receptor in control of body weight and reproduction, Science, 289, 2122, 10.1126\u002Fscience.289.5487.2122\nKennedy, 2000, Protein tyrosine phosphatase-1B in diabetes, Biochem. Pharmacol., 60, 877, 10.1016\u002FS0006-2952(00)00305-1\nJiang, 2002, Pi 3-kinase and its up- and down-stream modulators as potential targets for the treatment of type II diabetes, Front Biosci., 7, d903, 10.2741\u002Fjiang\nKahn, 1996, Lilly lecture 1995. Glucose transport: pivotal step in insulin action, Diabetes, 45, 1644, 10.2337\u002Fdiabetes.45.11.1644\nWhite, 2002, IRS proteins and the common path to diabetes, Am. J. Physiol. Endocrinol. Metab., 283, E413, 10.1152\u002Fajpendo.00514.2001\nGoldstein, 2002, Insulin resistance as the core defect in type 2 diabetes mellitus, Am. J. Cardiol., 90, 3G, 10.1016\u002FS0002-9149(02)02553-5\nTrayhurn, 2001, Physiological role of adipose tissue: white adipose tissue as an endocrine and secretory organ, Proc. Nutr. Soc., 60, 329, 10.1079\u002FPNS200194\nDeFronzo, 1985, Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus, J. Clin. Invest., 76, 149, 10.1172\u002FJCI111938\nMartin, 1992, Role of glucose and insulin resistance in development of type 2 diabetes mellitus: results of a 25-year follow-up study, Lancet, 340, 925, 10.1016\u002F0140-6736(92)92814-V\nLillioja, 1993, Insulin resistance and insulin secretory dysfunction as 24 precursors of non-insulin-dependent diabetes mellitus. Prospective studies of Pima Indians, N Engl. J. Med., 329, 1988, 10.1056\u002FNEJM199312303292703\nYu, 2002, Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activity in muscle, J. Biol. Chem., 277, 50230, 10.1074\u002Fjbc.M200958200\nKruszynska, 2002, Fatty acid-induced insulin resistance: decreased muscle PI3K activation but unchanged Akt phosphorylation, J. Clin. Endocrinol. Metab., 87, 226, 10.1210\u002Fjc.87.1.226\nBoden, 1994, Mechanisms of fatty acid-induced inhibition of glucose uptake, J. Clin. Invest, 93, 2438, 10.1172\u002FJCI117252\nStaehr, 2003, Effects of free fatty acids per se on glucose production, gluconeogenesis, and glycogenolysis, Diabetes, 52, 260, 10.2337\u002Fdiabetes.52.2.260\nLaws, 1996, Free fatty acids, insulin resistance and lipoprotein metabolism, Curr. Opin. Lipidol., 7, 172, 10.1097\u002F00041433-199606000-00011\nSaxena, 1989, Release of endothelial cell lipoprotein lipase by plasma lipoproteins and free fatty acids, J. Biol. Chem., 264, 4349, 10.1016\u002FS0021-9258(18)83748-6\nShimabukuro, 1998, Fatty acid-induced-β cell apoptosis: a link between obesity and diabetes, Proc. Natl. Acad. Sci. U.S.A., 95, 2498, 10.1073\u002Fpnas.95.5.2498\nRuan, 2002, Profiling gene transcription in vivo reveals adipose tissue as an immediate target of TNF-α: implications for insulin resistance, Diabetes, 51, 3176, 10.2337\u002Fdiabetes.51.11.3176\nCarswell, 1975, An endotoxininduced serum factor that causes necrosis of tumors, Proc. Natl. Acad. Sci. U.S.A., 72, 3666, 10.1073\u002Fpnas.72.9.3666\nBeutler, 1985, Identity of tumour necrosis factor and the macrophage-secreted factor cachectin, Nature, 316, 552, 10.1038\u002F316552a0\nKawakami, 1982, Lipoprotein lipase suppression in 3T3-L1 cells by an endotoxin-induced mediator from exudate cells, Proc. Natl. Acad. Sci. U.S.A., 79, 912, 10.1073\u002Fpnas.79.3.912\nKawakami, 1981, Studies of endotoxin-induced decrease in lipoprotein lipase activity, J. Exp. Med., 154, 631, 10.1084\u002Fjem.154.3.631\nTracey, 1986, Shock and tissue injury induced by recombinant human cachectin, Science, 234, 470, 10.1126\u002Fscience.3764421\nTracey, 1988, Cachectin\u002Ftumor necrosis factor induces cachexia, anemia, and inflammation, J. Exp. Med., 167, 1211, 10.1084\u002Fjem.167.3.1211\nKriegler, 1988, A novel form of TNF\u002Fcachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF, Cell, 53, 45, 10.1016\u002F0092-8674(88)90486-2\nMaskos, 1998, Crystal structure of the catalytic domain of human tumor necrosis factor-α-converting enzyme, Proc. Natl. Acad. Sci. U.S.A., 95, 3408, 10.1073\u002Fpnas.95.7.3408\nBlack, 1997, A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells, Nature, 385, 729, 10.1038\u002F385729a0\nWallach, 1999, Tumor necrosis factor receptor and Fas signaling mechanisms, Annu. Rev. Immunol., 17, 331, 10.1146\u002Fannurev.immunol.17.1.331\nHotamisligil, 1993, Spiegelman BM. Adipose expression of tumor necrosis factor-α: direct role in obesity-linked insulin resistance, Science, 259, 87, 10.1126\u002Fscience.7678183\nHotamisligil, 1995, Increased adipose tissue expression of tumor necrosis factor-α in human obesity and insulin resistance, J. Clin. Invest., 95, 2409, 10.1172\u002FJCI117936\nMontague, 1998, Depot-related gene expression in human subcutaneous and omental adipocytes, Diabetes, 47, 1384, 10.2337\u002Fdiabetes.47.9.1384\nKern, 1995, The expression of tumor necrosis factor in human adipose tissue. Regulation by obesity, weight loss, and relationship to lipoprotein lipase, J. Clin. Invest, 95, 2111, 10.1172\u002FJCI117899\nHotamisligil, 1994, Tumor necrosis factor-α inhibits signaling from the insulin receptor, Proc. Natl. Acad. Sci. U.S.A., 91, 4854, 10.1073\u002Fpnas.91.11.4854\nLang, 1992, Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output, Endocrinology, 130, 43, 10.1210\u002Fen.130.1.43\nHotamisligil, 1994, Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes. Central role of tumor necrosis factor-α, J. Clin. Invest, 94, 1543, 10.1172\u002FJCI117495\nUysal, 1997, Protection from obesityinduced insulin resistance in mice lacking TNF-α function, Nature, 389, 610, 10.1038\u002F39335\nUysal, 1998, Functional analysis of tumor necrosis factor (TNF) receptors in TNF-α-mediated insulin resistance in genetic obesity, Endocrinology, 139, 4832, 10.1210\u002Fen.139.12.4832\nOfei, 1996, Effects of an engineered human anti-TNF-α antibody (CDP571) on insulin sensitivity and glycemic control in patients with NIDDM, Diabetes, 45, 881, 10.2337\u002Fdiabetes.45.7.881\nRandle, 1963, The glucose fatty-acid cycle. Its role in insulin sensitivity and the metabolic disturbances of diabetes mellitus, Lancet, 1, 785, 10.1016\u002FS0140-6736(63)91500-9\nRandle, 1965, The glucose fatty acid cycle in obesity and maturity onset diabetes mellitus, Ann. N Y Acad. Sci., 131, 324, 10.1111\u002Fj.1749-6632.1965.tb34800.x\nBoden, 1991, Effects of fat on insulin-stimulated carbohydrate metabolism in normal men, J. Clin. Invest, 88, 960, 10.1172\u002FJCI115399\nBogardus, 1984, Correlation between muscle glycogen synthase activity and in vivo insulin action in man, J. Clin. Invest, 73, 1185, 10.1172\u002FJCI111304\nShulman, 1990, Quantitation of muscle glycogen synthesis in normal subjects and subjects with non-insulin-dependent diabetes by 13C nuclear magnetic resonance spectroscopy, N Engl. J. Med., 322, 223, 10.1056\u002FNEJM199001253220403\nSaloranta, 1991, Modulation of hepatic glucose production by non-esterified fatty acids in type 2 (non-insulindependent) diabetes mellitus, Diabetologia, 34, 409, 10.1007\u002FBF00403179\nRuderman, 1969, Role of free fatty acids in glucose homeostasis, Arch Intern Med., 123, 299, 10.1001\u002Farchinte.123.3.299\nByrne, 1991, Interaction of non-esterified fatty acid and insulin in control of triacylglycerol secretion by Hep G2 cells, Biochem. J., 280, 99, 10.1042\u002Fbj2800099\nByrne, 1992, Control of Hep G2-cell triacylglycerol and apolipoprotein B synthesis and secretion by polyunsaturated non-esterified fatty acids and insulin, Biochem. J., 288, 101, 10.1042\u002Fbj2880101\nDixon, 1993, Regulation of hepatic secretion of apolipoprotein Bcontaining lipoproteins: information obtained from cultured liver cells, J. Lipid Res., 34, 167, 10.1016\u002FS0022-2275(20)40744-8\nBoden, 1996, Fatty acids and insulin resistance, Diabetes Care, 19, 394, 10.2337\u002Fdiacare.19.4.394\nRoden, 1996, Mechanism of free fatty acid-induced insulin resistance in humans, J. Clin. Invest, 97, 2859, 10.1172\u002FJCI118742\nFerrannini, 1983, Effect of fatty acids on glucose production and utilization in man, J. Clin. Invest, 72, 1737, 10.1172\u002FJCI111133\nReaven, 1988, Lowering of plasma glucose in diabetic rats by antilipolytic agents, Am. J. Physiol., 254, E23\nReaven, 1988, Additive hypoglycemic effects of drugs that modify free-fatty acid metabolism by different mechanisms in rats with streptozocininduced diabetes, Diabetes, 37, 28, 10.2337\u002Fdiabetes.37.1.28\nBalasse, 1973, Influence of nicotinic acid on the rates of turnover and oxidation of plasma glucose in man, Metabolism, 22, 1193, 10.1016\u002F0026-0495(73)90207-2\nBoden, 1998, Acute lowering of plasma fatty acids lowers basal insulin secretion in diabetic and nondiabetic subjects, Diabetes, 47, 1609, 10.2337\u002Fdiabetes.47.10.1609\nBonadonna, 1990, Dose-dependent effect of insulin on plasma free fatty acid turnover and oxidation in humans, Am. J. Physiol., 259, E736\nSwislocki, 1987, Insulin suppression of plasma-free fatty acid concentration in normal individuals and patients with type 2 (noninsulin-dependent) diabetes, Diabetologia, 30, 622, 10.1007\u002FBF00277318\nSkowronski, 1991, Regulation of non-esterified fatty acid and glycerol concentration by insulin in normal individuals and patients with type 2 diabetes, Diabet. Med., 8, 330, 10.1111\u002Fj.1464-5491.1991.tb01605.x\nLaws, 1997, Differences in insulin suppression of free fatty acid levels by gender and glucose tolerance status. Relation to plasma triglyceride and apolipoprotein B concentrations. Insulin Resistance Atherosclerosis Study (IRAS) Investigators, Arterioscler. Thromb. Vasc. Biol., 17, 64, 10.1161\u002F01.ATV.17.1.64\nLavoie, 1993, Increased insulin suppression of plasma free fatty acid concentration in exercise-trained rats, J. Appl. Physiol., 74, 293, 10.1152\u002Fjappl.1993.74.1.293\nChen, 1987, Resistance to insulin suppression of plasma free fatty acid concentrations and insulin stimulation of glucose uptake in noninsulin-dependent diabetes mellitus, J. Clin. Endocrinol. Metab., 64, 17, 10.1210\u002Fjcem-64-1-17\nStralfors, 1984, Hormonal regulation of hormone-sensitive lipase in intact adipocytes: identification of phosphorylated sites and effects on the phosphorylation by lipolytic hormones and insulin, Proc. Natl. Acad. Sci. U.S.A., 81, 3317, 10.1073\u002Fpnas.81.11.3317\nStralfors, 1989, Insulin-induced dephosphorylation of hormone-sensitive lipase. Correlation with lipolysis and cAMP-dependent protein kinase activity, Eur. J. Biochem., 182, 379, 10.1111\u002Fj.1432-1033.1989.tb14842.x\nJensen, 1989, Insulin regulation of lipolysis in nondiabetic and IDDM subjects, Diabetes, 38, 1595, 10.2337\u002Fdiabetes.38.12.1595\nCampbell, 1992, Regulation of free fatty acid metabolism by insulin in humans: role of lipolysis and reesterification, Am. J. Physiol., 263, E1063\nElks, 1985, Antilipolytic action of insulin: role of cAMP phosphodiesterase activation, Endocrinology, 116, 2119, 10.1210\u002Fendo-116-5-2119\nBelfrage, 1985, Molecular mechanisms for hormonal control of adipose tissue lipolysis, Int. J. Obes., 9, 129\nBelfrage, 1981, Regulation of adipose-tissue lipolysis by phosphorylation of hormone-sensitive lipase, Int. J. Obes., 5, 635\nIgal, 2001, Mitochondrial glycerol phosphate acyltransferase directs the incorporation of exogenous fatty acids into triacylglycerol, J. Biol. Chem., 276, 42205, 10.1074\u002Fjbc.M103386200\nRuan, 2001, Overexpression of 1-acyl-glycerol-3-phosphate acyltransferase-α enhances lipid storage in cellular models of adipose tissue and skeletal muscle, Diabetes, 50, 233, 10.2337\u002Fdiabetes.50.2.233\nScherer, 1995, A novel serum protein similar to C1q, produced exclusively in adipocytes, J. Biol. Chem., 270, 26746, 10.1074\u002Fjbc.270.45.26746\nNakano, 1996, Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma, J. Biochem. (Tokyo), 120, 803, 10.1093\u002Foxfordjournals.jbchem.a021483\nMaeda, 1996, cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (adipose most abundant gene transcript 1), Biochem. Biophys. Res. Commun., 221, 286, 10.1006\u002Fbbrc.1996.0587\nHu, 1996, AdipoQ is a novel adipose-specific gene dysregulated in obesity, J. Biol. Chem., 271, 10697, 10.1074\u002Fjbc.271.18.10697\nBerg, 2002, ACRP30\u002Fadiponectin: an adipokine regulating glucose and lipid metabolism, Trends Endocrinol. Metab., 13, 84, 10.1016\u002FS1043-2760(01)00524-0\nShapiro, 1998, The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor, Curr. Biol., 8, 335, 10.1016\u002FS0960-9822(98)70133-2\nBogan, 2001, Insulin-responsive compartments containing GLUT4 in 3T3-L1 and CHO cells: regulation by amino acid concentrations, Mol Cell Biol., 21, 4785, 10.1128\u002FMCB.21.14.4785-4806.2001\nRuan, 2002, Tumor necrosis factor-α suppresses adipocyte-specific genes and activates expression of preadipocyte genes in 3T3-L1 adipocytes: nuclear factor-κB activation by TNF-α is obligatory, Diabetes, 51, 1319, 10.2337\u002Fdiabetes.51.5.1319\nArita, 1999, Paradoxical 33 decrease of an adipose-specific protein, adiponectin, in obesity, Biochem. Biophys. Res. Commun., 257, 79, 10.1006\u002Fbbrc.1999.0255\nCombs, 2002, Induction of adipocyte complement-related protein of 30 kDa by PPARγ agonists: a potential mechanism of insulin sensitization, Endocrinology, 143, 998, 10.1210\u002Fen.143.3.998\nFruebis, 2001, Proteolytic cleavage product of 30 kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice, Proc. Natl. Acad. Sci. U.S.A., 98, 2005, 10.1073\u002Fpnas.041591798\nYamauchi, 2002, Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase, Nat. Med., 8, 1288, 10.1038\u002Fnm788\nTomas, 2002, Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation, Proc. Natl. Acad. Sci. U.S.A., 99, 16309, 10.1073\u002Fpnas.222657499\nCombs, 2001, Endogenous glucose production is inhibited by the adipose-derived protein Acrp30, J. Clin. Invest, 108, 1875, 10.1172\u002FJCI14120\nBerg, 2001, The adipocyte-secreted protein Acrp30 enhances hepatic insulin action, Nat. Med., 7, 947, 10.1038\u002F90992\nKubota, 2002, Disruption of adiponectin causes insulin resistance and neointimal formation, J. Biol. Chem., 277, 25863, 10.1074\u002Fjbc.C200251200\nMaeda, 2002, Diet-induced insulin resistance in mice lacking adiponectin\u002FACRP30, Nat. Med., 8, 731, 10.1038\u002Fnm724\nMa, 2002, Increased β-oxidation but no insulin resistance or glucose intolerance in mice lacking adiponectin, J. Biol. Chem., 277, 34658, 10.1074\u002Fjbc.C200362200\nPajvani, 2003, Structure-function studies of the adipocyte-secreted hormone Acrp30\u002Fadiponectin. Implications for metabolic regulation and bioactivity, J. Biol. Chem., 278, 9073, 10.1074\u002Fjbc.M207198200\nHotamisligil, 1996, IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance, Science, 271, 665, 10.1126\u002Fscience.271.5249.665\nYuan, 2001, Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkβ, Science, 293, 1673, 10.1126\u002Fscience.1061620\nTamori, 2002, Role of peroxisome proliferatoractivated receptor-γ in maintenance of the characteristics of mature 3T3-L1 adipocytes, Diabetes, 51, 2045, 10.2337\u002Fdiabetes.51.7.2045\nRuan, 2003, Troglitazone antagonizes TNF-α-induced reprogramming of adipocyte gene expression by inhibiting the transcriptional regulatory functions of NF-kB, J Biol Chem, 278, 28181, 10.1074\u002Fjbc.M303141200",{"EN":134},"Insulin resistance in adipose tissue: direct and indirect effects of tumor necrosis factor-α",{"VOID":136},"10.1016\u002Fs1359-6101(03)00052-2","PUBLICATION","VERIFIED","Auto 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2001, Cloning and characterization of IL-1HY2, a novel interleukin-1 family member, J. Biol. Chem., 276, 20597, 10.1074\u002Fjbc.M010095200\nBensen, 2001, Identification of a novel human cytokine gene in the interleukin gene cluster on chromosome 2q12-14, J. Interferon Cytokine Res., 21, 899, 10.1089\u002F107999001753289505\nDinarello, 2010, IL-1 family nomenclature, Nat. Immunol., 11, 973, 10.1038\u002Fni1110-973\nCarta, 2013, Different members of the IL-1 family come out in different ways: DAMPs vs. cytokines?, Front. Immunol., 4, 123, 10.3389\u002Ffimmu.2013.00123\nTakenaka, 2015, IL-38: a new factor in rheumatoid arthritis, Biochem. Biophys. Rep., 4, 386\nPalomo, 2015, The interleukin (IL)-1 cytokine family—balance between agonists and antagonists in inflammatory diseases, Cytokine, 76, 25, 10.1016\u002Fj.cyto.2015.06.017\nJung, 2010, The interleukin-1 family gene polymorphisms in Korean patients with rheumatoid arthritis, Scand. J. Rheumatol., 39, 190, 10.3109\u002F03009740903447028\nMonnet, 2012, Association between the IL-1 family gene cluster and spondyloarthritis, Ann. Rheum. Dis., 71, 885, 10.1136\u002Fannrheumdis-2011-200439\nGuo, 2010, Association of IL-1 gene complex members with ankylosing spondylitis in Chinese Han population, Int. J. Immunogenet., 37, 33, 10.1111\u002Fj.1744-313X.2009.00889.x\nChou, 2006, Replication of association of IL1 gene complex members with ankylosing spondylitis in Taiwanese Chinese, Ann. Rheum. Dis., 65, 1106, 10.1136\u002Fard.2005.046847\nLea, 2012, The associations between interleukin-1 polymorphisms and susceptibility to ankylosing spondylitis: a meta-analysis, Joint Bone Spine Rev. Rhum., 79, 370, 10.1016\u002Fj.jbspin.2011.06.010\nRahman, 2006, Association between the interleukin-1 family gene cluster and psoriatic arthritis, Arthritis Rheum., 54, 2321, 10.1002\u002Fart.21928\nStock, 2008, Comprehensive association study of genetic variants in the IL-1 gene family in systemic juvenile idiopathic arthritis, Genes Immun., 9, 349, 10.1038\u002Fgene.2008.24\nDehghan, 2011, Meta-analysis of genome-wide association studies in >80 000 subjects identifies multiple loci for C-reactive protein levels, Circulation, 123, 731, 10.1161\u002FCIRCULATIONAHA.110.948570\nSoto López, 2013, The interleukin-1 gene cluster polymorphisms are associated with Takayasu’s arteritis in Mexican patients, J. Interferon Cytokine Res., 33, 369, 10.1089\u002Fjir.2012.0126\nHerder, 2014, Genetic determinants of circulating interleukin-1 receptor antagonist levels and their association with glycemic traits, Diabetes, 63, 4343, 10.2337\u002Fdb14-0731\nvan de Veerdonk, 2012, IL-38 binds to the IL-36 receptor and has biological effects on immune cells similar to IL-36 receptor antagonist, Proc. Natl. Acad. Sci. U. S. A., 109, 3001, 10.1073\u002Fpnas.1121534109\nRudloff, 2015, Brief report interleukin-38 exerts antiinflammatory functions and is associated with disease activity in systemic lupus erythematosus, Arthritis Rheumatol. (Hoboken, NJ), 67, 3219, 10.1002\u002Fart.39328\nMora, 2016, Interleukin-38 is released from apoptotic cells to limit inflammatory macrophage responses, J. Mol. Cell Biol., 8, 426, 10.1093\u002Fjmcb\u002Fmjw006\nBoutet, 2017, IL-38 overexpression induces anti-inflammatory effects in mice arthritis models and in human macrophages in vitro, Ann. Rheum. Dis., 76, 1304, 10.1136\u002Fannrheumdis-2016-210630\nJha, 2011, Chlamydia pneumoniae heat shock protein 60 is associated with apoptotic signaling pathway in human atheromatous plaques of coronary artery disease patients, J. Cardiol., 58, 216, 10.1016\u002Fj.jjcc.2011.07.010\nCiccia, 2015, Interleukin-36α axis is modulated in patients with primary Sjögren’s syndrome, Clin. Exp. Immunol., 181, 230, 10.1111\u002Fcei.12644\nZhao, 2015, Expression profile of IL-1 family cytokines in aqueous humor and sera of patients with HLA-B27 associated anterior uveitis and idiopathic anterior uveitis, Exp. Eye Res., 138, 80, 10.1016\u002Fj.exer.2015.06.018\nZhong, 2015, Elevated plasma IL-38 concentrations in patients with acute ST-segment elevation myocardial infarction and their dynamics after reperfusion treatment, Mediators Inflamm., 2015, 490120, 10.1155\u002F2015\u002F490120\nBoutet, 2016, Distinct expression of interleukin (IL)-36α, β and γ, their antagonist IL-36Ra and IL-38 in psoriasis, rheumatoid arthritis and Crohn’s disease, Clin. Exp. Immunol., 184, 159, 10.1111\u002Fcei.12761\nYuan, 2016, IL-38 alleviates concanavalin A-induced liver injury in mice, Int. Immunopharmacol., 40, 452, 10.1016\u002Fj.intimp.2016.09.023\nWang, 2016, Elevated serum interleukin-38 level at baseline predicts virological response in telbivudine-treated patients with chronic hepatitis B, World J. Gastroenterol., 22, 4529, 10.3748\u002Fwjg.v22.i18.4529\nChu, 2016, Aberrant expression of novel cytokine IL-38 and regulatory T lymphocytes in childhood asthma, Molecules (Basel, Switz.), 21\nKim, 2016, Up-regulation of receptor antagonist interleukin-1 family members in psoriasis and their regulation by pro-inflammatory cytokines, J. Dermatol. Sci., 82, 204, 10.1016\u002Fj.jdermsci.2016.02.003\nWang, 2016, Detection of the novel IL-1 family cytokines by QAH-IL1F-1 assay in rheumatoid arthritis, Cell. Mol. Biol. (Noisy–Gd., Fr.), 62, 31\nZhang, 2017, The effect of interleukin 38 on angiogenesis in a model of oxygen-induced retinopathy, Sci. Rep., 7, 2756, 10.1038\u002Fs41598-017-03079-z\nLi, 2017, New interleukins in psoriasis and psoriatic arthritis patients: the possible roles of interleukin-33 to interleukin-38 in disease activities and bone erosions, Dermatology (Basel, Switz.), 233, 37, 10.1159\u002F000471798\nChu, 2017, In vivo anti-inflammatory activities of novel cytokine IL-38 in Murphy Roths Large (MRL)\u002Flpr mice, Immunobiology, 222, 483, 10.1016\u002Fj.imbio.2016.10.012\nTominaga, 2017, Overexpression of IL-38 protein in anticancer drug-induced lung injury and acute exacerbation of idiopathic pulmonary fibrosis, Respir. Investig., 55, 293, 10.1016\u002Fj.resinv.2017.06.001\nTakada, 2017, Clinical implications of the novel cytokine IL-38 expressed in lung adenocarcinoma: possible association with PD-L1 expression, PLoS One, 12, 10.1371\u002Fjournal.pone.0181598\nSabater-Lleal, 2013, Multiethnic meta-analysis of genome-wide association studies in >100 000 subjects identifies 23 fibrinogen-associated loci but no strong evidence of a causal association between circulating fibrinogen and cardiovascular disease, Circulation, 128, 1310, 10.1161\u002FCIRCULATIONAHA.113.002251\nHessam, 2017, IL-36 in hidradenitis suppurativa: evidence for a distinctive pro-inflammatory role and a key factor in the development of an inflammatory loop, Br. J. Dermatol.\nYu, 2017, IL-37 and 38 signalling in gestational diabetes, J. Reprod. Immunol., 124, 8, 10.1016\u002Fj.jri.2017.09.011\nAfonina, 2015, Proteolytic processing of interleukin-1 family cytokines: variations on a common theme, Immunity, 42, 991, 10.1016\u002Fj.immuni.2015.06.003\nClancy, 2017, Neutrophil extracellular traps can serve as platforms for processing and activation of IL-1 family cytokines, FEBS J., 284, 1712, 10.1111\u002Ffebs.14075\nTowne, 2011, Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36α, IL-36β, and IL-36γ) or antagonist (IL-36Ra) activity, J. Biol. Chem., 286, 42594, 10.1074\u002Fjbc.M111.267922\nAinscough, 2017, Cathepsin S is the major activator of the psoriasis-associated proinflammatory cytokine IL-36γ, Proc. Natl. Acad. Sci., 114, E2748, 10.1073\u002Fpnas.1620954114\nAoyagi, 2017, IL-36 receptor deletion attenuates lung injury and decreases mortality in murine influenza pneumonia, Mucosal Immunol., 10, 1043, 10.1038\u002Fmi.2016.107\nEllisdon, 2017, Homodimerization attenuates the anti-inflammatory activity of interleukin-37, Sci. Immunol., 2, 10.1126\u002Fsciimmunol.aaj1548\nNold, 2010, IL-37 is a fundamental inhibitor of innate immunity, Nat. Immunol., 11, 1014, 10.1038\u002Fni.1944\nGarlanda, 2013, The interleukin-1 family: back to the future, Immunity, 39, 1003, 10.1016\u002Fj.immuni.2013.11.010\nBulau, 2014, Role of caspase-1 in nuclear translocation of IL-37, release of the cytokine, and IL-37 inhibition of innate immune responses, Proc. Natl. Acad. Sci. U. S. A., 111, 2650, 10.1073\u002Fpnas.1324140111\nYuan, 2016, Production of recombinant human interleukin-38 and its inhibitory effect on the expression of proinflammatory cytokines in THP-1 cells, Mol. Biol. (Mosk.), 50, 466, 10.1134\u002FS0026893316030134\nLopez-Castejon, 2011, Understanding the mechanism of IL-1β secretion, Cytokine Growth Factor Rev., 22, 189, 10.1016\u002Fj.cytogfr.2011.10.001\nJiang, 2017, Dendritic cells should not be overlooked when studying the effect of IL-38 administration in arthritis, Ann. Rheum. Dis.\nBoutet, 2017, Response to: “Does IL-38 act on macrophages and\u002For dendritic cells in arthritis?” by Jiang, et al, Ann. Rheum. Dis.\nGabay, 2015, Regulation and function of interleukin-36 cytokines in homeostasis and pathological conditions, J. Leukoc. Biol., 97, 645, 10.1189\u002Fjlb.3RI1014-495R\nHahn, 2017, The novel interleukin-1 cytokine family members in inflammatory diseases, Curr. Opin. Rheumatol., 29, 208, 10.1097\u002FBOR.0000000000000361\nShaik, 2013, IL-36 receptor antagonist with special emphasis on IL-38, Int. J. Immunopathol. Pharmacol., 26, 27, 10.1177\u002F039463201302600103\nvan de Veerdonk, 2013, New insights in the immunobiology of IL-1 family members, Front. Immunol., 4, 167, 10.3389\u002Ffimmu.2013.00167\nHu, 2015, Expression, purification of IL-38 in Escherichia coli and production of polyclonal antibodies, Protein Expr. Purif., 107, 76, 10.1016\u002Fj.pep.2014.10.016\nTortola, 2012, Psoriasiform dermatitis is driven by IL-36–mediated DC-keratinocyte crosstalk, J. Clin. Invest., 122, 3965, 10.1172\u002FJCI63451\nDietrich, 2016, Interleukin-36 potently stimulates human M2 macrophages, Langerhans cells and keratinocytes to produce pro-inflammatory cytokines, Cytokine, 84, 88, 10.1016\u002Fj.cyto.2016.05.012\nMutamba, 2012, Expression of IL-1Rrp2 by human myelomonocytic cells is unique to DCs and facilitates DC maturation by IL-1F8 and IL-1F9, Eur. J. Immunol., 42, 607, 10.1002\u002Feji.201142035\nVigne, 2011, IL-36R ligands are potent regulators of dendritic and T cells, Blood, 118, 5813, 10.1182\u002Fblood-2011-05-356873\nPenha, 2016, IL-36 receptor is expressed by human blood and intestinal T lymphocytes and is dose–dependently activated via IL-36β and induces CD4+ lymphocyte proliferation, Cytokine, 85, 18, 10.1016\u002Fj.cyto.2016.05.023\nGresnigt, 2013, The IL-36 receptor pathway regulates Aspergillus fumigatus- induced Th1 and Th17 responses: immunity to infection, Eur. J. Immunol., 43, 416, 10.1002\u002Feji.201242711\nVigne, 2012, IL-36 signaling amplifies Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells, Blood, 120, 3478, 10.1182\u002Fblood-2012-06-439026\nChi, 2017, IL-36 signaling facilitates activation of the NLRP3 inflammasome and IL-23\u002FIL-17 axis in renal inflammation and fibrosis, J. Am. Soc. Nephrol., 28, 2022, 10.1681\u002FASN.2016080840\nLamacchia, 2013, The severity of experimental arthritis is independent of IL-36 receptor signaling, Arthritis Res. Ther., 15, R38, 10.1186\u002Far4192\nDerer, 2014, Blockade of IL-36 receptor signaling does not prevent from TNF-induced arthritis, PLoS One, 9, 10.1371\u002Fjournal.pone.0101954\nBoraschi, 2013, The interleukin-1 receptor family, Semin. Immunol., 25, 394, 10.1016\u002Fj.smim.2013.10.023\nBorn, 2000, Identification and characterization of two members of a novel class of the interleukin-1 receptor (IL-1R) family. Delineation Of a new class of IL-1R-related proteins based on signaling, J. Biol. Chem., 275, 29946, 10.1074\u002Fjbc.M004077200\nPiton, 2008, Mutations in the calcium-related gene IL1RAPL1 are associated with autism, Hum. Mol. Genet., 17, 3965, 10.1093\u002Fhmg\u002Fddn300\nNawara, 2008, Novel mutation of IL1RAPL1 gene in a nonspecific X-linked mental retardation (MRX) family, Am. J. Med. Genet. A, 146A, 3167, 10.1002\u002Fajmg.a.32613\nLaino, 2016, Clinical and molecular characterization of a boy with intellectual disability, facial dysmorphism, minor digital anomalies and a complex IL1RAPL1 intragenic rearrangement, Eur. J. Paediatr. Neurol., 20, 971, 10.1016\u002Fj.ejpn.2016.07.003\nRamos-Brossier, 2015, Novel IL1RAPL1 mutations associated with intellectual disability impair synaptogenesis, Hum. Mol. Genet., 24, 1106, 10.1093\u002Fhmg\u002Fddu523\nYoshida, 2011, IL-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation by trans-synaptic interaction with protein tyrosine phosphatase, J. Neurosci., 31, 13485, 10.1523\u002FJNEUROSCI.2136-11.2011\nYasumura, 2015, IL1RAPL1 knockout mice show spine density decrease, learning deficiency, hyperactivity and reduced anxiety-like behaviours, Sci. Rep., 4, 10.1038\u002Fsrep06613\nPavlowsky, 2010, Neuronal JNK pathway activation by IL-1 is mediated through IL1RAPL1, a protein required for development of cognitive functions, Commun. Integr. Biol., 3, 245, 10.4161\u002Fcib.3.3.11414\nGambino, 2007, IL1-receptor accessory protein-like 1 (IL1RAPL1), a protein involved in cognitive functions, regulates N-type Ca2+-channel and neurite elongation, Proc. Natl. Acad. Sci., 104, 9063, 10.1073\u002Fpnas.0701133104\nKhan, 2004, Crystal structure of the Toll\u002Finterleukin-1 receptor domain of human IL-1RAPL, J. Biol. Chem., 279, 31664, 10.1074\u002Fjbc.M403434200\nHayashi, 2013, IL1RAPL1 associated with mental retardation and autism regulates the formation and stabilization of glutamatergic synapses of cortical neurons through RhoA signaling pathway, PLoS One, 8, 10.1371\u002Fjournal.pone.0066254\nMarques, 2017, Suggestive association between variants in IL1RAPL and asthma symptoms in Latin American children, Eur. J. Hum. Genet., 25, 439, 10.1038\u002Fejhg.2016.197\nMolgora, 2016, Regulatory role of IL-1R8 in immunity and disease, Front. Immunol., 7, 10.3389\u002Ffimmu.2016.00149\nCostelloe, 2008, IL-1F5 mediates anti-inflammatory activity in the brain through induction of IL-4 following interaction with SIGIRR\u002FTIR8, J. Neurochem., 105, 1960, 10.1111\u002Fj.1471-4159.2008.05304.x\nZhao, 2017, Interleukin 37 promotes angiogenesis through TGF-β signaling, Sci. Rep., 7, 6113, 10.1038\u002Fs41598-017-06124-z\nKeermann, 2015, Expression of IL-36 family cytokines and IL-37 but not IL-38 is altered in psoriatic skin, J. Dermatol. Sci., 80, 150, 10.1016\u002Fj.jdermsci.2015.08.002\nFullerton, 2016, Resolution of inflammation: a new therapeutic frontier, Nat. Rev. Drug Discov., 15, 551, 10.1038\u002Fnrd.2016.39\nHong, 2000, The inhibitory effect of interleukin-10 on mouse osteoclast formation involves novel tyrosine-phosphorylated proteins, J. Bone Miner., 15, 911, 10.1359\u002Fjbmr.2000.15.5.911\nSong, 2017, Role of interleukin (IL)-17 and T-helper (Th)17 cells in cancer, Biochem. Biophys. Res. Commun., 493, 1, 10.1016\u002Fj.bbrc.2017.08.109\nRobak, 2013, Correlations between concentrations of interleukin (IL)-17A, IL-17 B and IL-17F, and endothelial cells and proangiogenic cytokines in systemic lupus erythematosus patients, Eur. Cytokine Netw., 24, 60, 10.1684\u002Fecn.2013.0330\nSingh, 2013, Involvement of IL-9 in Th17-associated inflammation and angiogenesis of psoriasis, PLoS One, 8\nCoxon, 2002, Inhibition of interleukin-1 but not tumor necrosis factor suppresses neovascularization in rat models of corneal angiogenesis and adjuvant arthritis, Arthritis Rheum., 46, 2604, 10.1002\u002Fart.10546\nCelis, 2012, Synovial cytokine expression in psoriatic arthritis and associations with lymphoid neogenesis and clinical features, Arthritis Res. Ther., 14, R93, 10.1186\u002Far3817\nvan Baarsen, 2014, Heterogeneous expression pattern of interleukin 17A (IL-17A), IL-17F and their receptors in synovium of rheumatoid arthritis, psoriatic arthritis and osteoarthritis: possible explanation for nonresponse to anti-IL-17 therapy?, Arthritis Res. Ther., 16, 426, 10.1186\u002Fs13075-014-0426-z\nMiossec, 2017, Update on interleukin-17: a role in the pathogenesis of inflammatory arthritis and implication for clinical practice, RMD Open, 3, 10.1136\u002Frmdopen-2016-000284\nCarrier, 2011, Inter-regulation of Th17 cytokines and the IL-36 cytokines in vitro and in vivo: implications in psoriasis pathogenesis, J. Invest. Dermatol., 131, 2428, 10.1038\u002Fjid.2011.234\nKotake, 2017, The plasticity of Th17 cells in the pathogenesis of rheumatoid arthritis, J. Clin. Med., 6, 67, 10.3390\u002Fjcm6070067\nJones, 2017, Advances in rheumatoid arthritis, Med. J. Aust., 206, 221, 10.5694\u002Fmja16.01287\nMcInnes, 2015, Cytokines in rheumatoid arthritis – shaping the immunological landscape, Nat. Rev. Rheumatol., 12, 63, 10.1038\u002Fnrrheum.2015.171\nMcInnes, 2017, Pathogenetic insights from the treatment of rheumatoid arthritis, Lancet (Lond., Engl.), 389, 2328, 10.1016\u002FS0140-6736(17)31472-1\nRossi-Semerano, 2013, First clinical description of an infant with interleukin-36-receptor antagonist deficiency successfully treated with anakinra, Pediatrics, 132, e1043, 10.1542\u002Fpeds.2012-3935\nUmmarino, 2017, Experimental arthritis: IL-38 promotes anti-inflammatory effects, Nat. Rev. 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2006, Expression and regulation of IL-22 in the IL-17-producing CD4+ T lymphocytes, Cell Research, 16, 902, 10.1038\u002Fsj.cr.7310106\nLiang, 2006, Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides, Journal of Experimental Medicine, 203, 2271, 10.1084\u002Fjem.20061308\nCella, 2009, A human natural killer cell subset provides an innate source of IL-22 for mucosal immunity, Nature, 457, 722, 10.1038\u002Fnature07537\nDuhen, 2009, Production of interleukin 22 but not interleukin 17 by a subset of human skin-homing memory T cells, Nature Immunology, 10, 857, 10.1038\u002Fni.1767\nTrifari, 2009, Identification of a human helper T cell population that has abundant production of interleukin 22 and is distinct from T(H)-17, T(H)1 and T(H)2 cells, Nature Immunology, 10, 864, 10.1038\u002Fni.1770\nPan, 2009, Decreased serum IL-22 levels in patients with systemic lupus erythematosus, Clinica Chimica Acta, 401, 179, 10.1016\u002Fj.cca.2008.11.009\nCheng, 2009, Decreased plasma IL22 levels, but not increased IL17 and IL23 levels, correlate with disease activity in patients with systemic lupus erythematosus, Annals of the Rheumatic Diseases, 68, 604, 10.1136\u002Fard.2008.097089\nZiesche, 2009, Dexamethasone suppresses interleukin-22 associated with bacterial infection in vitro and in vivo, Clinical and Experimental Immunology, 157, 370, 10.1111\u002Fj.1365-2249.2009.03969.x\nMcKinley, 2008, TH17 cells mediate steroid-resistant airway inflammation and airway hyperresponsiveness in mice, Journal of Immunology, 181, 4089, 10.4049\u002Fjimmunol.181.6.4089\nQin, 2011, Expressions of IL-22 in circulating CD4+\u002FCD8+ T cells and their correlation with disease activity in SLE patients, Clinical and Experimental Medicine, 11, 245, 10.1007\u002Fs10238-011-0134-9\nYu, 2011, Copy number variations of interleukin-17F, interleukin-21, and interleukin-22 are associated with systemic lupus erythematosus, Arthritis and Rheumatism, 63, 3487, 10.1002\u002Fart.30595\nIkeuchi, 2005, Expression of interleukin-22 in rheumatoid arthritis: potential role as a proinflammatory cytokine, Arthritis and Rheumatism, 52, 1037, 10.1002\u002Fart.20965\nGeboes, 2009, Proinflammatory role of the Th17 cytokine interleukin-22 in collagen-induced arthritis in C57BL\u002F6 mice, Arthritis and Rheumatism, 60, 390, 10.1002\u002Fart.24220\nda Rocha, 2012, Increased serum interleukin 22 in patients with rheumatoid arthritis and correlation with disease activity, Journal of Rheumatology, 10.3899\u002Fjrheum.111027\nLeipe, 2011, Interleukin 22 serum levels are associated with radiographic progression in rheumatoid arthritis, Annals of the Rheumatic Diseases, 70, 1453, 10.1136\u002Fard.2011.152074\nKim, 2012, Interleukin-22 promotes osteoclastogenesis in rheumatoid arthritis through induction of RANKL in human synovial fibroblasts, Arthritis and Rheumatism, 64, 1015, 10.1002\u002Fart.33446\nVandenbroeck, 2012, A cytokine gene screen uncovers SOCS1 as genetic risk factor for multiple sclerosis, Genes and Immunity, 13, 21, 10.1038\u002Fgene.2011.44\nBeyeen, 2010, IL-22RA2 associates with multiple sclerosis and macrophage effector mechanisms in experimental neuroinflammation, Journal of Immunology, 185, 6883, 10.4049\u002Fjimmunol.1001392\nKreymborg, 2007, IL-22 is expressed by Th17 cells in an IL-23-dependent fashion, but not required for the development of autoimmune encephalomyelitis, Journal of Immunology, 179, 8098, 10.4049\u002Fjimmunol.179.12.8098\nLavoie, 2011, Expression of interleukin-22 in Sjogren's syndrome: significant correlation with disease parameters, Scandinavian Journal of Immunology, 74, 377, 10.1111\u002Fj.1365-3083.2011.02583.x\nCiccia, 2012, Potential involvement of IL-22 and IL-22-producing cells in the inflamed salivary glands of patients with Sjogren's syndrome, Annals of the Rheumatic Diseases, 71, 295, 10.1136\u002Fard.2011.154013\nWolk, 2009, IL-22 and IL-20 are key mediators of the epidermal alterations in psoriasis while IL-17 and IFN-gamma are not, Journal of Molecular Medicine (Berlin), 87, 523, 10.1007\u002Fs00109-009-0457-0\nZheng, 2007, Interleukin-22, a T(H)17 cytokine, mediates IL-23-induced dermal inflammation and acanthosis, Nature, 445, 648, 10.1038\u002Fnature05505\nSabat, 2010, IL-10 family of cytokines, Cytokine and Growth Factor Reviews, 21, 315, 10.1016\u002Fj.cytogfr.2010.11.001\nDumoutier, 2000, Cloning and characterization of IL-10-related T cell-derived inducible factor (IL-TIF), a novel cytokine structurally related to IL-10 and inducible by IL-9, Journal of Immunology, 164, 1814, 10.4049\u002Fjimmunol.164.4.1814\nWolk, 2006, Interleukin-22: a novel T- and NK-cell derived cytokine that regulates the biology of tissue cells, Cytokine and Growth Factor Reviews, 17, 367, 10.1016\u002Fj.cytogfr.2006.09.001\nWolk, 2004, IL-22 increases the innate immunity of tissues, Immunity, 21, 241, 10.1016\u002Fj.immuni.2004.07.007\nWolk, 2007, IL-22 induces lipopolysaccharide-binding protein in hepatocytes: a potential systemic role of IL-22 in Crohn's disease, Journal of Immunology, 178, 5973, 10.4049\u002Fjimmunol.178.9.5973\nZhou, 2008, TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by antagonizing RORgammat function, Nature, 453, 236, 10.1038\u002Fnature06878\nVeldhoen, 2008, The aryl hydrocarbon receptor links TH17-cell-mediated autoimmunity to environmental toxins, Nature, 453, 106, 10.1038\u002Fnature06881\nZhang, 2011, Th22 in inflammatory and autoimmune disease: prospects for therapeutic intervention, Molecular and Cellular Biochemistry, 353, 41, 10.1007\u002Fs11010-011-0772-y\nEyerich, 2009, Th22 cells represent a distinct human T cell subset involved in epidermal immunity and remodeling, Journal of Clinical Investigation, 119, 3573\nSimonian, 2010, gammadelta T cells protect against lung fibrosis via IL-22, Journal of Experimental Medicine, 207, 2239, 10.1084\u002Fjem.20100061\nGuo, 2010, Interleukin-22 (IL-22) production by pulmonary natural killer cells and the potential role of IL-22 during primary influenza virus infection, Journal of Virology, 84, 7750, 10.1128\u002FJVI.00187-10\nZenewicz, 2011, Recent advances in IL-22 biology, International Immunology, 23, 159, 10.1093\u002Fintimm\u002Fdxr001\nCupedo, 2009, Human fetal lymphoid tissue-inducer cells are interleukin 17-producing precursors to RORC+ CD127+ natural killer-like cells, Nature Immunology, 10, 66, 10.1038\u002Fni.1668\nTakatori, 2009, Lymphoid tissue inducer-like cells are an innate source of IL-17 and IL-22, Journal of Experimental Medicine, 206, 35, 10.1084\u002Fjem.20072713\nSonnenberg, 2010, Functional biology of the IL-22-IL-22R pathway in regulating immunity and inflammation at barrier surfaces, Advances in Immunology, 107, 1, 10.1016\u002FB978-0-12-381300-8.00001-0\nXie, 2000, Interleukin (IL)-22, a novel human cytokine that signals through the interferon receptor-related proteins CRF2-4 and IL-22R, Journal of Biological Chemistry, 275, 31335, 10.1074\u002Fjbc.M005304200\nLejeune, 2002, Interleukin-22 (IL-22) activates the JAK\u002FSTAT, ERK JNK, and p38 MAP kinase pathways in a rat hepatoma cell line. Pathways that are shared with and distinct from IL-10, Journal of Biological Chemistry, 277, 33676, 10.1074\u002Fjbc.M204204200\nDumoutier, 2009, New activation modus of STAT3: a tyrosine-less region of the interleukin-22 receptor recruits STAT3 by interacting with its coiled-coil domain, Journal of Biological Chemistry, 284, 26377, 10.1074\u002Fjbc.M109.007955\nPickert, 2009, STAT3 links IL-22 signaling in intestinal epithelial cells to mucosal wound healing, Journal of Experimental Medicine, 206, 1465, 10.1084\u002Fjem.20082683\nTagoe, 2012, JAK2 inhibition in murine systemic lupus erythematosus, Immunotherapy, 4, 369, 10.2217\u002Fimt.12.20\nJia, 2011, Amelioration of experimental autoimmune encephalomyelitis by plumbagin through down-regulation of JAK-STAT and NF-kappaB signaling pathways, PLoS One, 6, e27006, 10.1371\u002Fjournal.pone.0027006\nJiang, 2009, MOG(35-55) i.v suppresses experimental autoimmune encephalomyelitis partially through modulation of Th17 and JAK\u002FSTAT pathways, European Journal of Immunology, 39, 789, 10.1002\u002Feji.200838427\nArumugam, 2012, Involvement of AMPK and MAPK signaling during the progression of experimental autoimmune myocarditis in rats and its blockade using a novel antioxidant, Experimental and Molecular Pathology, 10.1016\u002Fj.yexmp.2012.04.012\nNoubade, 2011, Activation of p38 MAPK in CD4 T cells controls IL-17 production and autoimmune encephalomyelitis, Blood, 118, 3290, 10.1182\u002Fblood-2011-02-336552\nCope, 2004, Emerging approaches for the therapy of autoimmune and chronic inflammatory disease, Current Opinion in Immunology, 16, 780, 10.1016\u002Fj.coi.2004.09.005\nChatenoud, 2006, Immune therapies of autoimmune diseases: are we approaching a real cure?, Current Opinion in Immunology, 18, 710, 10.1016\u002Fj.coi.2006.09.004\nKunz, 2009, Cytokines and cytokine profiles in human autoimmune diseases and animal models of autoimmunity, Mediators of Inflammation, 2009, 979258, 10.1155\u002F2009\u002F979258\nPan, 2008, Type 17 T-helper cells might be a promising therapeutic target for systemic lupus erythematosus, Nature Clinical Practice. Rheumatology, 4, 352, 10.1038\u002Fncprheum0815\nAggarwal, 2003, Interleukin-23 promotes a distinct CD4 T cell activation state characterized by the production of interleukin-17, Journal of Biological Chemistry, 278, 1910, 10.1074\u002Fjbc.M207577200\nGarrett-Sinha, 2008, IL-17 and the Th17 lineage in systemic lupus erythematosus, Current Opinion in Rheumatology, 20, 519, 10.1097\u002FBOR.0b013e328304b6b5\nvan den Berg, 2009, IL-17 as a future therapeutic target for rheumatoid arthritis, Nature Reviews Rheumatology, 5, 549, 10.1038\u002Fnrrheum.2009.179\nPollinger, 2012, IL-17 producing T cells in mouse models of multiple sclerosis and rheumatoid arthritis, Journal of Molecular Medicine (Berlin), 90, 613, 10.1007\u002Fs00109-011-0841-4\nMieliauskaite, 2012, Expression of IL-17 IL-23 and their receptors in minor salivary glands of patients with primary Sjogren's syndrome, Clinical & Developmental Immunology, 2012, 187258, 10.1155\u002F2012\u002F187258\nGirolomoni, 2012, Psoriasis: rationale for targeting IL-17, British Journal of Dermatology, 10.1111\u002Fj.1365-2133.2012.11099.x\nSemerano, 2012, Anti-cytokine vaccination: a new biotherapy of autoimmunity?, Autoimmunity Reviews, 10.1016\u002Fj.autrev.2012.02.003\nKe, 2011, IL-22-induced regulatory CD11b+ APCs suppress experimental autoimmune uveitis, Journal of Immunology, 187, 2130, 10.4049\u002Fjimmunol.1100482\nZenewicz, 2008, IL-22 inflammation: leukin’ through a glass F onion, European Journal of Immunology, 38, 3265, 10.1002\u002Feji.200838655\nSchmechel, 2008, Linking genetic susceptibility to Crohn's disease with Th17 cell function: IL-22 serum levels are increased in Crohn's disease and correlate with disease activity and IL23R genotype status, Inflammatory Bowel Diseases, 14, 204, 10.1002\u002Fibd.20315\nLo, 2010, Serum IL-22 correlates with psoriatic severity and serum IL-6 correlates with susceptibility to phototherapy, Journal of Dermatological Science, 58, 225, 10.1016\u002Fj.jdermsci.2010.03.018\nOuyang, 2010, Distinct roles of IL-22 in human psoriasis and inflammatory bowel disease, Cytokine and Growth Factor Reviews, 21, 435, 10.1016\u002Fj.cytogfr.2010.10.007\nZenewicz, 2007, Interleukin-22 but not interleukin-17 provides protection to hepatocytes during acute liver inflammation, Immunity, 27, 647, 10.1016\u002Fj.immuni.2007.07.023\nRadaeva, 2004, Interleukin 22 (IL-22) plays a protective role in T cell-mediated murine hepatitis: IL-22 is a survival factor for hepatocytes via STAT3 activation, Hepatology, 39, 1332, 10.1002\u002Fhep.20184\nFeng, 2012, Interleukin-22 ameliorates cerulein-induced pancreatitis in mice by inhibiting the autophagic pathway, International Journal of Biological Sciences, 8, 249, 10.7150\u002Fijbs.3967\nMa, 2008, IL-22 is required for Th17 cell-mediated pathology in a mouse model of psoriasis-like skin inflammation, Journal of Clinical Investigation, 118, 597\nVan Belle, 2012, IL-22 is required for 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2000, The effects of insulin-like growth factors on tumorigenesis and neoplastic growth, Endocr Rev, 21, 215, 10.1210\u002Fer.21.3.215\nPollak, 2004, Insulin-like growth factors and neoplasia, Nat Rev Cancer, 4, 505, 10.1038\u002Fnrc1387\nBaumann, 2002, Genetic characterization of growth hormone deficiency and resistance: implications for treatment with recombinant growth hormone, Am J Pharmacogenomics, 2, 93, 10.2165\u002F00129785-200202020-00003\nLaron, 2004, Laron syndrome (primary growth hormone resistance or insensitivity): the personal experience, J Clin Endocrinol Metab, 89, 1031, 10.1210\u002Fjc.2003-031033\nO’Connor, 2003, Regulation of IGF-I receptor signaling in tumor cells, Horm Metab Res, 35, 771, 10.1055\u002Fs-2004-814166\nKim, 2002, Signalling through IGF-I and insulin receptors: where is the specificity?, Growth Horm IGF Res, 12, 84, 10.1054\u002Fghir.2002.0265\nRinderknecht, 1978, The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin, J Biol Chem, 253, 2769, 10.1016\u002FS0021-9258(17)40889-1\nCooke, 1991, Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study, Biochemistry, 30, 5484, 10.1021\u002Fbi00236a022\nSato, 1993, Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry, Int J Pept Protein Res, 41, 433, 10.1111\u002Fj.1399-3011.1993.tb00462.x\nSchaffer, 2003, Complex with a phage display-derived peptide provides insight into the function of insulin-like growth factor I, Biochemistry, 42, 9324, 10.1021\u002Fbi034386c\nVajdos, 2001, Crystal structure of human insulin-like growth factor-1: detergent binding inhibits binding protein interactions, Biochemistry, 40, 11022, 10.1021\u002Fbi0109111\nZeslawski, 2001, The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5, EMBO J, 20, 3638, 10.1093\u002Femboj\u002F20.14.3638\nBrzozowski, 2002, Structural origins of the functional divergence of human insulin-like growth factor-I and insulin, Biochemistry, 41, 9389, 10.1021\u002Fbi020084j\nSiwanowicz, 2005, Structural basis for the regulation of insulin-like growth factors by IGF binding proteins, Structure, 13, 155, 10.1016\u002Fj.str.2004.11.009\nTerasawa, 1994, Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins, EMBO J, 13, 5590, 10.1002\u002Fj.1460-2075.1994.tb06896.x\nTorres, 1995, Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions, J Mol Biol, 248, 385, 10.1016\u002FS0022-2836(95)80058-1\nBentley, 1976, Structure of insulin in 4-zinc insulin, Nature, 261, 166, 10.1038\u002F261166a0\nBaker, 1988, The structure of 2Zn pig insulin crystals at 1.5 A resolution, Philos Trans R Soc Lond B Biol Sci, 319, 369, 10.1098\u002Frstb.1988.0058\nWeiss, 1990, NMR and photo-CIDNP studies of human proinsulin and prohormone processing intermediates with application to endopeptidase recognition, Biochemistry, 29, 8389, 10.1021\u002Fbi00488a028\nWalenkamp, 2005, Homozygous and heterozygous expression of a novel insulin-like growth factor-I mutation, J Clin Endocrinol Metab, 90, 2855, 10.1210\u002Fjc.2004-1254\nDenley, 2005, Structural and functional characteristics of the Val44Met insulin-like growth factor I missense mutation: correlation with effects on growth and development, Mol Endocrinol, 19, 711, 10.1210\u002Fme.2004-0409\nWoods, 1997, Insulin-like growth factor I gene deletion causing intrauterine growth retardation and severe short stature, Acta Paediatr Suppl, 423, 39, 10.1111\u002Fj.1651-2227.1997.tb18367.x\nLiu, 1993, Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r), Cell, 75, 59\nDeChiara, 1990, A growth-deficiency phenotype in heterozygous mice carrying an insulin-like growth factor II gene disrupted by targeting, Nature, 345, 78, 10.1038\u002F345078a0\nPandini, 2003, Differential gene expression induced by insulin and insulin-like growth factor-II through the insulin receptor isoform A, J Biol Chem, 278, 42178, 10.1074\u002Fjbc.M304980200\nPandini, 2004, Igf-ii binding to insulin receptor isoform a induces a partially different gene expression profile from insulin binding, Ann NY Acad Sci, 450, 10.1196\u002Fannals.1322.053\nNakae, 2001, Distinct and overlapping functions of insulin and IGF-I receptors, Endocr Rev, 22, 818, 10.1210\u002Fer.22.6.818\nDenley, 2003, The insulin receptor isoform exon 11− (IR-A) in cancer and other diseases: a review, Horm Metab Res, 35, 778, 10.1055\u002Fs-2004-814157\nSesti, 2000, Insulin receptor variant forms and type 2 diabetes mellitus, Pharmacogenomics, 1, 49, 10.1517\u002F14622416.1.1.49\nPandini, 1999, Insulin and insulin-like growth factor-I (IGF-I) receptor overexpression in breast cancers leads to insulin\u002FIGF-I hybrid receptor overexpression: evidence for a second mechanism of IGF-I signaling, Clin Cancer Res, 5, 1935\nAdams, 2000, Structure and function of the type 1 insulin-like growth factor receptor, Cell Mol Life Sci, 57, 1050, 10.1007\u002FPL00000744\nCzech, 1982, Structural and functional homologies in the receptors for insulin and the insulin-like growth factors, Cell, 31, 8, 10.1016\u002F0092-8674(82)90399-3\nBhaumick, 1981, Somatomedin receptor of human placenta: solubilization, photolabeling, partial purification, and comparison with insulin receptor, Proc Natl Acad Sci USA, 78, 4279, 10.1073\u002Fpnas.78.7.4279\nChernausek, 1981, Structural similarities between human receptors for somatomedin C and insulin: analysis by affinity labeling, Biochemistry, 20, 7345, 10.1021\u002Fbi00529a004\nSiddle, 2001, Specificity in ligand binding and intracellular signalling by insulin and insulin-like growth factor receptors, Biochem Soc Trans, 29, 513, 10.1042\u002Fbst0290513\nDe Meyts, 2002, Structural biology of insulin and IGF1 receptors: implications for drug design, Nat Rev Drug Discov, 1, 769, 10.1038\u002Fnrd917\nSchaefer, 1990, Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric alpha-subunit, J Biol Chem, 265, 13248, 10.1016\u002FS0021-9258(19)38291-2\nBrandt, 2001, Dimeric fragment of the insulin receptor alpha-subunit binds insulin with full holoreceptor affinity, J Biol Chem, 276, 12378, 10.1074\u002Fjbc.M009402200\nKasuga, 1982, Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor, Science, 215, 185, 10.1126\u002Fscience.7031900\nRubin, 1983, Stimulation of tyrosine-specific phosphorylation in vitro by insulin-like growth factor I, Nature, 305, 438, 10.1038\u002F305438a0\nGarrett, 1998, Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor, Nature, 394, 395, 10.1038\u002F28668\nSchumacher, 1991, Insulin and insulin-like growth factor-1 binding specificity is determined by distinct regions of their cognate receptors, J Biol Chem, 266, 19288, 10.1016\u002FS0021-9258(18)54996-6\nWhittaker, 2001, Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site, J Biol Chem, 276, 43980, 10.1074\u002Fjbc.M102863200\nSorensen, 2004, Mapping of the insulin-like growth factor II binding site of the Type I insulin-like growth factor receptor by alanine scanning mutagenesis, FEBS Lett, 565, 19, 10.1016\u002Fj.febslet.2004.03.077\nAndersen, 1990, Changing the insulin receptor to possess insulin-like growth factor I ligand specificity, Biochemistry, 29, 7363, 10.1021\u002Fbi00484a002\nKjeldsen, 1991, The ligand specificities of the insulin receptor and the insulin-like growth factor I receptor reside in different regions of a common binding site, Proc Natl Acad Sci USA, 88, 4404, 10.1073\u002Fpnas.88.10.4404\nWedekind, 1989, Hormone binding site of the insulin receptor: analysis using photoaffinity-mediated avidin complexing, Biol Chem Hoppe Seyler, 370, 251, 10.1515\u002Fbchm3.1989.370.1.251\nFabry, 1992, Detection of a new hormone contact site within the insulin receptor ectodomain by the use of a novel photoreactive insulin, J Biol Chem, 267, 8950, 10.1016\u002FS0021-9258(19)50372-6\nKurose, 1994, Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the alpha-subunit of the insulin receptor. Identification of a new insulin-binding domain in the insulin receptor, J Biol Chem, 269, 29190, 10.1016\u002FS0021-9258(19)62029-6\nWilliams, 1995, Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis, J Biol Chem, 270, 3012, 10.1074\u002Fjbc.270.7.3012\nMynarcik, 1996, Alanine-scanning mutagenesis of a C-terminal ligand binding domain of the insulin receptor alpha subunit, J Biol Chem, 271, 2439, 10.1074\u002Fjbc.271.5.2439\nWhittaker, 2002, Comparison of the functional insulin binding epitopes of the A and B isoforms of the insulin receptor, J Biol Chem, 277, 47380, 10.1074\u002Fjbc.M208371200\nFirth, 2002, Cellular actions of the insulin-like growth factor binding proteins, Endocr Rev, 23, 824, 10.1210\u002Fer.2001-0033\nClemmons, 2001, Use of mutagenesis to probe IGF-binding protein structure\u002Ffunction relationships, Endocr Rev, 22, 800, 10.1210\u002Fer.22.6.800\nFrystyk, 2004, Free insulin-like growth factors – measurements and relationships to growth hormone secretion and glucose homeostasis, Growth Horm IGF Res, 14, 337, 10.1016\u002Fj.ghir.2004.06.001\nBaxter, 2000, Insulin-like growth factor (IGF)-binding proteins: interactions with IGFs and intrinsic bioactivities, Am J Physiol Endocrinol Metab, 278, E967, 10.1152\u002Fajpendo.2000.278.6.E967\nHwa, 1999, The insulin-like growth factor-binding protein (IGFBP) superfamily, Endocr Rev, 20, 761, 10.1210\u002Fer.20.6.761\nCarrick, 2001, The interaction of insulin-like growth factors (IGFs) with insulin-like growth factor binding proteins (IGFBPs): a review, Lett Pept Sci, 8, 147, 10.1007\u002FBF02446511\nHeadey, 2004, C-terminal domain of insulin-like growth factor binding protein-6: structure and interaction with insulin-like growth factor-II, Mol Endocrinol, 10.1210\u002Fme.2004-0248\nHeadey, 2004, Binding site for the C-domain of insulin-like growth factor (IGF) binding protein-6 on IGF-II; implications for inhibition of IGF actions, FEBS Lett, 568, 19, 10.1016\u002Fj.febslet.2004.04.091\nScott, 2004, The role of the M6P\u002FIGF-II receptor in cancer: tumor suppression or garbage disposal?, Horm Metab Res, 36, 261, 10.1055\u002Fs-2004-814477\nDe Souza, 1995, M6P\u002FIGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity, Nat Genet, 11, 447, 10.1038\u002Fng1295-447\nOka, 2002, M6P\u002FIGF2R tumor suppressor gene mutated in hepatocellular carcinomas in Japan, Hepatology, 35, 1153, 10.1053\u002Fjhep.2002.32669\nJamieson, 2003, M6P\u002FIGF2R loss of heterozygosity in head and neck cancer associated with poor patient prognosis, BMC Cancer, 3, 4, 10.1186\u002F1471-2407-3-4\nLee, 1986, Identification of receptors for insulin-like growth factor II in two insulin-like growth factor II producing cell lines, Biochem Biophys Res Commun, 134, 595, 10.1016\u002FS0006-291X(86)80461-2\nEwton, 1987, The type II insulin-like growth factor (IGF) receptor has low affinity for IGF-I analogs: pleiotypic actions of IGFs on myoblasts are apparently mediated by the type I receptor, Endocrinology, 120, 115, 10.1210\u002Fendo-120-1-115\nTong, 1988, The cation-independent mannose 6-phosphate receptor binds insulin-like growth factor II, J Biol Chem, 263, 2585, 10.1016\u002FS0021-9258(18)69105-7\nMorgan, 1987, Insulin-like growth factor II receptor as a multifunctional binding protein, Nature, 329, 301, 10.1038\u002F329301a0\nOshima, 1988, The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells, J Biol Chem, 263, 2553, 10.1016\u002FS0021-9258(18)69243-9\nKornfeld, 1992, Structure and function of the mannose 6-phosphate\u002Finsulinlike growth factor II receptors, Annu Rev Biochem, 61, 307, 10.1146\u002Fannurev.bi.61.070192.001515\nDevi, 1998, An insulin-like growth factor II (IGF-II) affinity-enhancing domain localized within extracytoplasmic repeat 13 of the IGF-II\u002Fmannose 6-phosphate receptor, Mol Endocrinol, 12, 1661, 10.1210\u002Fme.12.11.1661\nTong, 1989, Ligand interactions of the cation-independent mannose 6-phosphate receptor. The stoichiometry of mannose 6-phosphate binding, J Biol Chem, 264, 7962, 10.1016\u002FS0021-9258(18)83136-2\nWestlund, 1991, The bovine mannose 6-phosphate\u002Finsulin-like growth factor II receptor. Localization of mannose 6-phosphate binding sites to domains 1–3 and 7–11 of the extracytoplasmic region, J Biol Chem, 266, 23233, 10.1016\u002FS0021-9258(18)54487-2\nBrown, 2002, Structure of a functional IGF2R fragment determined from the anomalous scattering of sulfur, EMBO J, 21, 1054, 10.1093\u002Femboj\u002F21.5.1054\nGarmroudi, 1994, Localization of the insulin-like growth factor II (IGF-II) binding\u002Fcross-linking site of the IGF-II\u002Fmannose 6-phosphate receptor to extracellular repeats 10–11, J Biol Chem, 269, 26944, 10.1016\u002FS0021-9258(18)47110-4\nBayne, 1988, Structural analogs of human insulin-like growth factor I with reduced affinity for serum binding proteins and the type 2 insulin-like growth factor receptor, J Biol Chem, 263, 6233, 10.1016\u002FS0021-9258(18)68777-0\nShooter, 1996, Insulin-like growth factor (IGF)-I A- and B-domain analogues with altered type 1 IGF and insulin receptor binding specificities, J Mol Endocrinol, 17, 237, 10.1677\u002Fjme.0.0170237\nHodgson, 1995, Mutations at positions 11 and 60 of insulin-like growth factor 1 reveal differences between its interactions with the type I insulin-like-growth-factor receptor and the insulin receptor, Eur J Biochem, 233, 299, 10.1111\u002Fj.1432-1033.1995.299_1.x\nCascieri, 1988, Mutants of human insulin-like growth factor I with reduced affinity for the type 1 insulin-like growth factor receptor, Biochemistry, 27, 3229, 10.1021\u002Fbi00409a016\nBayne, 1990, The roles of tyrosines 24, 31, and 60 in the high affinity binding of insulin-like growth factor-I to the type 1 insulin-like growth factor receptor, J Biol Chem, 265, 15648, 10.1016\u002FS0021-9258(18)55447-8\nMagee, 1999, Insulin-like growth factor I and its binding proteins: a study of the binding interface using B-domain analogues, Biochemistry, 38, 15863, 10.1021\u002Fbi9910070\nJansson, 1998, The insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis, J Biol Chem, 273, 24701, 10.1074\u002Fjbc.273.38.24701\nJansson, 1997, Structural changes in insulin-like growth factor (IGF) I mutant proteins affecting binding kinetic rates to IGF binding protein 1 and IGF-I receptor, Biochemistry, 36, 4108, 10.1021\u002Fbi961553i\nSakano, 1991, The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II\u002Fcation-independent mannose 6-phosphate receptor or IGF-I receptor, J Biol Chem, 266, 20626, 10.1016\u002FS0021-9258(18)54755-4\nRoth, 1991, Mutants of human insulin-like growth factor II: expression and characterization of analogs with a substitution of TYR27 and\u002For a deletion of residues 62–67, Biochem Biophys Res Commun, 181, 907, 10.1016\u002F0006-291X(91)91277-J\nHashimoto, 1995, N-terminal deletion mutants of insulin-like growth factor-II (IGF-II) show Thr7 and Leu8 important for binding to insulin and IGF-I receptors and Leu8 critical for all IGF-II functions, J Biol Chem, 270, 18013, 10.1074\u002Fjbc.270.30.18013\nBagley, 1989, A key functional role for the insulin-like growth factor 1 N-terminal pentapeptide, Biochem J, 259, 665, 10.1042\u002Fbj2590665\nCara, 1990, An insulin-like growth factor I\u002Finsulin hybrid exhibiting high potency for interaction with the type I insulin-like growth factor and insulin receptors of placental plasma membranes, J Biol Chem, 265, 17820, 10.1016\u002FS0021-9258(18)38237-1\nBayne, 1989, The C region of human insulin-like growth factor (IGF) I is required for high affinity binding to the type 1 IGF receptor, J Biol Chem, 264, 11004, 10.1016\u002FS0021-9258(18)60418-1\nGill, 1996, Engineering the C-region of human insulin-like growth factor-1: implications for receptor binding, Protein Eng, 9, 1011, 10.1093\u002Fprotein\u002F9.11.1011\nDe Wolf, 1996, Solution structure of a mini IGF-1, Protein Sci, 5, 2193, 10.1002\u002Fpro.5560051106\nZhang, 1994, Positively charged side chains in the insulin-like growth factor-1 C- and D-regions determine receptor binding specificity, J Biol Chem, 269, 10609, 10.1016\u002FS0021-9258(17)34103-0\nDenley, 2004, Structural determinants for high-affinity binding of insulin-like growth factor II to insulin receptor (IR)-A, the exon 11 minus isoform of the IR, Mol Endocrinol, 18, 2502, 10.1210\u002Fme.2004-0183\nKobayashi, 1986, Receptor binding and negative cooperativity of a mutant insulin, [LeuA3]-insulin, Biochem Biophys Res Commun, 137, 250, 10.1016\u002F0006-291X(86)91203-9\nNanjo, 1987, Insulin Wakayama: familial mutant insulin syndrome in Japan, Diabetologia, 30, 87, 10.1007\u002FBF00274577\nXu, 2004, Diabetes-associated mutations in insulin identify invariant receptor contacts, Diabetes, 53, 1599, 10.2337\u002Fdiabetes.53.6.1599\nHua, 1991, Receptor binding redefined by a structural switch in a mutant human insulin, Nature, 354, 238, 10.1038\u002F354238a0\nCascieri, 1989, Structural analogs of human insulin-like growth factor (IGF) I with altered affinity for type 2 IGF receptors, J Biol Chem, 264, 2199, 10.1016\u002FS0021-9258(18)94162-1\nForbes, 2001, Contribution of residues A54 and L55 of the human insulin-like growth factor-II (IGF-II) A domain to Type 2 IGF receptor binding specificity, Growth Factors, 19, 163, 10.3109\u002F08977190109001084\nSchaffer, 1994, A model for insulin binding to the insulin receptor, Eur J Biochem, 221, 1127, 10.1111\u002Fj.1432-1033.1994.tb18833.x\nDe Meyts, 1994, The structural basis of insulin and insulin-like growth factor-I receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signalling, Diabetologia, 37, S135, 10.1007\u002FBF00400837\nDe Meyts, 2004, Insulin and its receptor: structure, function and evolution, Bioessays, 26, 1351, 10.1002\u002Fbies.20151\nXu, 2004, Diabetes-associated mutations in insulin: consecutive residues in the B chain contact distinct domains of the insulin receptor(,), Biochemistry, 43, 8356, 10.1021\u002Fbi0497796\nWan, 2004, Enhancing the activity of insulin at the receptor interface: crystal structure and photo-cross-linking of A8 analogues, Biochemistry, 43, 16119, 10.1021\u002Fbi048223f\nHuang, 2004, How insulin binds: the B-chain alpha-helix contacts the L1 beta-helix of the insulin receptor, J Mol Biol, 341, 529, 10.1016\u002Fj.jmb.2004.05.023\nHodgson, 1996, Involvement of phenylalanine 23 in the binding of IGF-1 to the insulin and type I IGF receptor, Regul Pept, 66, 191, 10.1016\u002FS0167-0115(96)00102-4\nKristensen, 1995, A single-chain insulin-like growth factor I\u002Finsulin hybrid binds with high affinity to the insulin receptor, Biochem J, 305, 981, 10.1042\u002Fbj3050981\nSato, 1992, 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution, J Biochem (Tokyo), 111, 529, 10.1093\u002Foxfordjournals.jbchem.a123791\nLaajoki L, Milner S, Francis G, Carver J, Keniry M. BioMagResBank (http:\u002F\u002Fwww.bmrb.wisc.edu\u002F) entry number 4278; 1998.\nDubaquie, 2001, Binding protein-3-selective insulin-like growth factor I variants: engineering, biodistributions, and clearance, Endocrinology, 142, 165, 10.1210\u002Fen.142.1.165\nDubaquie, 1999, Total alanine-scanning mutagenesis of insulin-like growth factor I (IGF-I) identifies differential binding epitopes for IGFBP-1 and IGFBP-3, Biochemistry, 38, 6386, 10.1021\u002Fbi990089p\nClemmons, 1992, Competition for binding to insulin-like growth factor (IGF) binding protein-2, 3, 4, and 5 by the IGFs and IGF analogs, Endocrinology, 131, 890, 10.1210\u002Fen.131.2.890\nBach, 1993, Binding of mutants of human insulin-like growth factor II to insulin-like growth factor binding proteins 1–6, J Biol Chem, 268, 9246, 10.1016\u002FS0021-9258(18)98342-0\nClemmons, 1990, Discrete alterations of the insulin-like growth factor I molecule which alter its affinity for insulin-like growth factor-binding proteins result in changes in bioactivity, J Biol Chem, 265, 12210, 10.1016\u002FS0021-9258(19)38332-2\nMoss, 1991, Insulin-like growth factor (IGF)-I and IGF-II binding to an IGF binding protein. An investigation using chemical modification of tyrosine residues as a structural probe for the sites of interaction, J Biol Chem, 266, 909, 10.1016\u002FS0021-9258(17)35259-6\nKalus, 1998, Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions, EMBO J, 17, 6558, 10.1093\u002Femboj\u002F17.22.6558\nCarrick FE, Hinds MG, McNeil KA, Wallace JC, Forbes BE, Norton RS. Interaction of insulin-like growth factor (IGF)-I and -II with IGF binding protein-2: mapping the binding surfaces by nuclear magnetic resonance. J Mol Endocrinol, in press.\nOh, 1993, Characterization of the affinities of insulin-like growth factor (IGF)-binding proteins 1–4 for IGF-I, IGF-II, IGF-I\u002Finsulin hybrid, and IGF-I analogs, Endocrinol, 132, 1337, 10.1210\u002Fen.132.3.1337\nBurgisser, 1991, Mutants of human insulin-like growth factor II with altered affinities for the type 1 and type 2 insulin-like growth factor receptor, J Biol Chem, 266, 1029, 10.1016\u002FS0021-9258(17)35278-X\nYandell, 1999, Kangaroo IGF-II is structurally and functionally similar to the human, J Endocrinol, 161, 445, 10.1677\u002Fjoe.0.1610445\nBlundell, 1978, Insulin-like growth factor: a model for tertiary structure accounting for immunoreactivity and receptor binding, Proc Natl Acad Sci USA, 75, 180, 10.1073\u002Fpnas.75.1.180\nPandini, 2002, Insulin\u002Finsulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved, J Biol Chem, 277, 39684, 10.1074\u002Fjbc.M202766200\nKing, 1992, Production and characterization of recombinant insulin-like growth factor-I (IGF-I) and potent analogues of IGF-I, with Gly or Arg substituted for Glu3, following their expression in Escherichia coli as fusion proteins, J Mol Endocrinol, 8, 29, 10.1677\u002Fjme.0.0080029\nFrancis, 1992, Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency, J Mol Endocrinol, 8, 213, 10.1677\u002Fjme.0.0080213",{"EN":475},"Molecular interactions of the IGF system",{"VOID":477},"10.1016\u002Fj.cytogfr.2005.04.004","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1359610105000559",[480,497,512,531,543],{"id":481,"sortIndex":261,"researcher":18,"roles":482,"affiliations":483,"properties":494},"f2baed0c-4809-433a-aac4-c18dc062432c",[146],[484],{"id":18,"sortIndex":140,"affiliation":485,"properties":18},{"id":486,"createTime":487,"updateTime":488,"relativeEntities":489,"slug":490,"properties":491,"entityType":63,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"syncStatus":17,"languages":18,"translateLanguages":18,"viewCount":140},"7a2cf110-70c2-4f9f-a969-11543dc7fb08","2023-12-06T08:20:58.177+00:00","2024-10-14T10:56:02.262+00:00",[],"School-of-Molecular-and-Biomedical-Science-The-University-of-Adelaide-SA-5005-Australia",{"title":492},{"VI":493},"School of Molecular and Biomedical Science, The University of Adelaide, SA 5005, Australia",{"title":495},{"VI":496},"John C. 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Engl. J. Med., 382, 1708, 10.1056\u002FNEJMoa2002032\nNikolich-Žugich, 2018, The twilight of immunity: emerging concepts in aging of the immune system, Nat. Immunol., 19, 10, 10.1038\u002Fs41590-017-0006-x\nScully, 2020, Considering how biological sex impacts immune responses and COVID-19 outcomes, Nat. Rev. Immunol., 20, 442, 10.1038\u002Fs41577-020-0348-8\nKoff, 2020, Covid-19 and immunity in aging populations — a new research agenda, N. Engl. J. Med., 10.1056\u002FNEJMp2006761\nMurin, 2019, Antibody responses to viral infections: a structural perspective across three different enveloped viruses, Nat. Microbiol., 4, 734, 10.1038\u002Fs41564-019-0392-y\nWoo, 2004, Longitudinal profile of immunoglobulin g (IgG), IgM, and IgA antibodies against the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein in patients with pneumonia due to the SARS coronavirus, Clin. Diagnostic Lab. Immunol., 11, 665\nNi, 2020, Detection of SARS-CoV-2-specific humoral and cellular immunity in COVID-19 convalescent individuals, Immunity, 52, 971, 10.1016\u002Fj.immuni.2020.04.023\nZhao, 2020, Antibody responses to SARS-CoV-2 in patients of novel coronavirus disease 2019, Clin. Infect. Dis., 10.1093\u002Fcid\u002Fciaa344\nBloch, 2020, Deployment of convalescent plasma for the prevention and treatment of COVID-19, J. Clin. Invest., 130, 2757, 10.1172\u002FJCI138745\nDuan, 2020, Effectiveness of convalescent plasma therapy in severe COVID-19 patients, Proc. Natl. Acad. Sci., 117, 9490, 10.1073\u002Fpnas.2004168117\nChen, 2020, Convalescent plasma as a potential therapy for COVID-19, Lancet Infect. Dis., 20, 398, 10.1016\u002FS1473-3099(20)30141-9\nBastard, 2020, Auto-antibodies against type I IFNs in patients with life-threatening COVID-19, Science (80-.), 10.1126\u002Fscience.abd4585\nHartmann, 2017, Nucleic acid immunity, Adv. Immunol., 121, 10.1016\u002Fbs.ai.2016.11.001\nKikkert, 2020, Innate immune evasion by human respiratory RNA viruses, J. Innate Immun., 12, 4, 10.1159\u002F000503030\nMesev, 2019, Decoding type I and III interferon signalling during viral infection, Nat. Microbiol., 4, 914, 10.1038\u002Fs41564-019-0421-x\nSchurz, 2019, The X chromosome and sex-specific effects in infectious disease susceptibility, Hum. Genomics, 13, 2, 10.1186\u002Fs40246-018-0185-z\nKlein, 2016, Sex differences in immune responses, Nat. Rev. Immunol., 16, 626, 10.1038\u002Fnri.2016.90\nNewton, 2016, The host immune response in respiratory virus infection: balancing virus clearance and immunopathology, Semin. Immunopathol., 38, 471, 10.1007\u002Fs00281-016-0558-0\nKlein, 2010, The Xs and Y of immune responses to viral vaccines, Lancet Infect, Dis., 10, 338\nKlein, 2010, The impact of sex, gender and pregnancy on 2009 H1N1 disease, Biol. Sex Differ., 1, 5, 10.1186\u002F2042-6410-1-5\nNussinovitch, 2012, The role of gender and organ specific autoimmunity, Autoimmun. Rev., 11, A377, 10.1016\u002Fj.autrev.2011.11.001\nCarrel, 2005, X-inactivation profile reveals extensive variability in X-linked gene expression in females, Nature, 434, 400, 10.1038\u002Fnature03479\nTukiainen, 2017, Landscape of X chromosome inactivation across human tissues, Nature., 550, 244, 10.1038\u002Fnature24265\nKwon, 2019, Editorial: long non-coding RNAs and immunity, Front. Immunol., 10, 10.3389\u002Ffimmu.2019.02378\nSouyris, 2018, TLR7 escapes X chromosome inactivation in immune cells, Sci. Immunol., 3, 10.1126\u002Fsciimmunol.aap8855\nNusbaum, 2020, Sex differences in systemic lupus erythematosus, mayo clin, Proc., 95, 384\nBlanco, 2001, Induction of dendritic cell differentiation by IFN-alpha in systemic lupus erythematosus, Science (80-.), 294, 1540, 10.1126\u002Fscience.1064890\nM.K, 2003, Microarray analysis of gene expression in lupus, Arthritis Res. Ther., 279\nFukuyama, 2000, Systemic lupus erythematosus after α-Interferon therapy for chronic hepatitis C: a case report and review of the literature, Am. J. Gastroenterol., 95, 310\nSantiago-Raber, 2003, Type-I interferon receptor deficiency reduces lupus-like disease in NZB mice, J. Exp. Med., 197, 777, 10.1084\u002Fjem.20021996\nChristensen, 2006, Toll-like receptor 7 and TLR9 dictate autoantibody specificity and have opposing inflammatory and regulatory roles in a murine model of lupus, Immunity., 25, 417, 10.1016\u002Fj.immuni.2006.07.013\nTan, 2018, Detection of microbial infections through innate immune sensing of nucleic acids, Annu. Rev. Microbiol., 72, 447, 10.1146\u002Fannurev-micro-102215-095605\nKassiotis, 2016, Immune responses to endogenous retroelements: taking the bad with the good, Nat. Rev. Immunol., 16, 207, 10.1038\u002Fnri.2016.27\nOdhams, 2019, Interferon inducible X-linked gene CXorf21 may contribute to sexual dimorphism in systemic lupus erythematosus, Nat. Commun., 10, 10.1038\u002Fs41467-019-10106-2\nHarris, 2019, Lysosomal pH is regulated in a sex dependent manner in immune cells expressing CXorf21, Front. Immunol., 10, 578, 10.3389\u002Ffimmu.2019.00578\nSwiecki, 2015, The multifaceted biology of plasmacytoid dendritic cells, Nat. Rev. Immunol., 15, 471, 10.1038\u002Fnri3865\nJaillon, 2019, Sexual dimorphism in innate immunity, Clin. Rev. Allergy Immunol., 56, 308, 10.1007\u002Fs12016-017-8648-x\nMeier, 2009, Sex differences in the TLR-mediated response of pDCs to HIV-1 are associated with higher immune activation in infected women, Nat. Med., 15, 955, 10.1038\u002Fnm.2004\nBerghöfer, 2006, TLR7 ligands induce higher IFN-α production in females, J. Immunol., 177, 2088, 10.4049\u002Fjimmunol.177.4.2088\nLaffont, 2014, X-chromosome complement and estrogen receptor signaling independently contribute to the enhanced TLR7-Mediated IFN-α production of plasmacytoid dendritic cells from women, J. Immunol., 193, 5444, 10.4049\u002Fjimmunol.1303400\nSeillet, 2012, The TLR-mediated response of plasmacytoid dendritic cells is positively regulated by estradiol in vivo through cell-intrinsic estrogen receptor α signaling, Blood., 119, 454, 10.1182\u002Fblood-2011-08-371831\nGriesbeck, 2015, Sex differences in plasmacytoid dendritic cell levels of IRF5 drive higher IFN- production in women, J. Immunol., 195, 5327, 10.4049\u002Fjimmunol.1501684\nSyrett, 2019, Diversity of epigenetic features of the inactive X-chromosome in NK cells, dendritic cells, and macrophages, Front. Immunol., 9, 3087, 10.3389\u002Ffimmu.2018.03087\nCiancanelli, 2015, Life-threatening influenza and impaired interferon amplification in human IRF7 deficiency, Science (80-.), 348, 448, 10.1126\u002Fscience.aaa1578\nBlanco-Melo, 2020, Imbalanced host response to SARS-CoV-2 drives development of COVID-19, Cell., 181, 1036, 10.1016\u002Fj.cell.2020.04.026\nZhang, 2020, Inborn errors of type I IFN immunity in patients with life-threatening COVID-19, Science (80-.), 10.1126\u002Fscience.abd4570\nJefferies, 2019, Regulating IRFs in IFN driven disease, Front. Immunol., 10, 325, 10.3389\u002Ffimmu.2019.00325\nYu, 2018, Inflammasome activation negatively regulates MyD88-IRF7 type I IFN signaling and anti-malaria immunity, Nat. Commun., 9, 10.1038\u002Fs41467-018-07384-7\nOng, 2020, A dynamic immune response shapes COVID-19 progression, Cell Host Microbe, 27, 879, 10.1016\u002Fj.chom.2020.03.021\nTailor, 2007, The feedback phase of type I interferon induction in dendritic cells requires interferon regulatory factor 8, Immunity., 27, 228, 10.1016\u002Fj.immuni.2007.06.009\nBanchereau, 2004, Autoimmunity through cytokine-induced dendritic cell activation, Immunity, 20, 539, 10.1016\u002FS1074-7613(04)00108-6\nParmigiani, 2013, Impaired antibody response to influenza vaccine in HIV-Infected and uninfected aging women is associated with immune activation and inflammation, PLoS One, 8, 10.1371\u002Fjournal.pone.0079816\nBrowne, 2009, Myd88 is required for an antibody response to retroviral infection, PLoS Pathog., 5, 10.1371\u002Fjournal.ppat.1000298\nYu, 2012, Nucleic acid-sensing toll-like receptors are essential for the control of endogenous retrovirus viremia and ERV-Induced tumors, Immunity, 37, 867, 10.1016\u002Fj.immuni.2012.07.018\nClingan, 2013, B cell–Intrinsic TLR7 signaling is required for optimal B cell responses during chronic viral infection, J. Immunol., 191, 810, 10.4049\u002Fjimmunol.1300244\nKasturi, 2011, Programming the magnitude and persistence of antibody responses with innate immunity, Nature, 470, 543, 10.1038\u002Fnature09737\nWang, 2016, Unusual maintenance of X chromosome inactivation predisposes female lymphocytes for increased expression from the inactive X, Proc. Natl. Acad. Sci., 113, E2029, 10.1073\u002Fpnas.1520113113\nJego, 2003, Plasmacytoid dendritic cells induce plasma cell differentiation through type I interferon and interleukin 6, Immunity., 19, 225, 10.1016\u002FS1074-7613(03)00208-5\nBekeredjian-Ding, 2005, Plasmacytoid dendritic cells control TLR7 sensitivity of naive B cells via type I IFN, J. Immunol., 174, 4043, 10.4049\u002Fjimmunol.174.7.4043\nSchuh, 2017, Human plasmacytoid dendritic cells display and shed B cell maturation antigen upon TLR engagement, J. Immunol., 198, 3081, 10.4049\u002Fjimmunol.1601746\nLaurent, 2015, γ-secretase directly sheds the survival receptor BCMA from plasma cells, Nat. Commun., 6, 10.1038\u002Fncomms8333\nVincent, 2019, Analysis of serum B cell‐activating factor from the tumor necrosis factor family (\u003Cscp>BAFF\u003C\u002Fscp>) and its soluble receptors in systemic lupus erythematosus, Clin. Transl. Immunol., 8, 10.1002\u002Fcti2.1047\nMenon, 2016, A regulatory feedback between plasmacytoid dendritic cells and regulatory B cells is aberrant in systemic lupus erythematosus, Immunity, 44, 683, 10.1016\u002Fj.immuni.2016.02.012\nCervantes-Barragan, 2007, Control of coronavirus infection through plasmacytoid dendritic-cell–derived type I interferon, Blood, 109, 1131, 10.1182\u002Fblood-2006-05-023770\nDeal, 2013, Plasmacytoid dendritic cells promote rotavirus-induced human and murine B cell responses, J. Clin. Invest., 123, 2464, 10.1172\u002FJCI60945\nPanem, 1982, ALPHA INTERFERON AND ANTIBODY TO ALPHA INTERFERON IN SYSTEMIC LUPUS ERYTHEMATOSUS11This work was supported by grants MV 129 from the American Cancer Society (to S.P.), AI-07057 and AI-12948 from the National Institute of Allergy and Infectious Diseases\nWang, 2020, Retrospective multicenter cohort study shows early interferon therapy is associated with favorable clinical responses in COVID-19 patients, Cell Host Microbe, 10.1016\u002Fj.chom.2020.07.005\nNetea, 2020, Trained immunity: a tool for reducing susceptibility to and the severity of SARS-CoV-2 infection, Cell, 181, 969, 10.1016\u002Fj.cell.2020.04.042\nArts, 2018, BCG vaccination protects against experimental viral infection in humans through the induction of cytokines associated with trained immunity, Cell Host Microbe, 23, 89, 10.1016\u002Fj.chom.2017.12.010\nde Bree, 2018, The impact of sex hormones on BCG-induced trained immunity, J. Leukoc. Biol., 104, 573, 10.1002\u002FJLB.5MA0118-027R\nNetea, 2020, Defining trained immunity and its role in health and disease, Nat. Rev. Immunol., 20, 375, 10.1038\u002Fs41577-020-0285-6\nSarai, 2013, WHSC1 links transcription elongation to HIRA-mediated histone H3.3 deposition, EMBO J., 32, 2392, 10.1038\u002Femboj.2013.176\nKamada, 2018, Interferon stimulation creates chromatin marks and establishes transcriptional memory, Proc. Natl. Acad. Sci., 115, E9162, 10.1073\u002Fpnas.1720930115\nBarrat, 2019, Interferon target-gene expression and epigenomic signatures in health and disease, Nat. Immunol., 20, 1574, 10.1038\u002Fs41590-019-0466-2\nHole, 2019, Induction of memory-like dendritic cell responses in vivo, Nat. Commun., 10, 10.1038\u002Fs41467-019-10486-5\nPrakash, 2013, Impaired secretion of interferons by dendritic cells from aged subjects to influenza, Age (Omaha), 35, 1785, 10.1007\u002Fs11357-012-9477-8\nMa, 2017, Epigenetic regulator CXXC5 recruits DNA demethylase Tet2 to regulate TLR7\u002F9-elicited IFN response in pDCs, J. Exp. Med., 214, 1471, 10.1084\u002Fjem.20161149\nGubbels Bupp, 2015, Sex, the aging immune system, and chronic disease, Cell. Immunol., 294, 102, 10.1016\u002Fj.cellimm.2015.02.002\nJing, 2009, Aging is associated with a numerical and functional decline in plasmacytoid dendritic cells, whereas myeloid dendritic cells are relatively unaltered in human peripheral blood, Hum. Immunol., 70, 777, 10.1016\u002Fj.humimm.2009.07.005\nBlomberg, 2013, Age effects on mouse and human B cells, Immunol. Res., 57, 354, 10.1007\u002Fs12026-013-8440-9\nFrasca, 2017, Human peripheral late\u002Fexhausted memory B cells express a senescent-associated secretory phenotype and preferentially utilize metabolic signaling pathways, Exp. Gerontol., 87, 113, 10.1016\u002Fj.exger.2016.12.001\nNevalainen, 2019, CD27- IgD- B cell memory subset associates with inflammation and frailty in elderly individuals but only in males, Immun. Ageing, 16, 19, 10.1186\u002Fs12979-019-0159-6\nvan der Geest, 2016, Aging-dependent decline of IL-10 producing B cells coincides with production of antinuclear antibodies but not rheumatoid factors, Exp. Gerontol., 10.1016\u002Fj.exger.2015.12.009\nBerggren, 2017, Plasmacytoid dendritic cells and RNA-containing immune complexes drive expansion of peripheral B cell subsets with an SLE-like phenotype, PLoS One, 10.1371\u002Fjournal.pone.0183946\nCastelo-Branco, 2014, The immune system and aging: a review, Gynecol. Endocrinol., 30, 16, 10.3109\u002F09513590.2013.852531\nLi, 2020, Therapeutic options for the 2019 novel coronavirus (2019-nCoV), Nat. Rev. Drug Discov., 10.1038\u002Fd41573-020-00016-0\nHung, 2020, Triple combination of interferon beta-1b, lopinavir–ritonavir, and ribavirin in the treatment of patients admitted to hospital with COVID-19: an open-label, randomised, phase 2 trial, Lancet, 10.1016\u002FS0140-6736(20)31042-4\nXie, 2020, Combination antiviral therapy with lopinavir\u002Fritonavir, arbidol and interferon-α1b for COVID-19Combination antiviral therapy with lopinavir\u002Fritonavir, arbidol and interferon-α1b for COVID-19, Antivir. Ther. (Lond.), 10.3851\u002FIMP3362\nZuo, 2020, Lopinavir\u002Fritonavir and interferon combination therapy may help shorten the duration of viral shedding in patients with COVID‐19: a retrospective study in two designated hospitals in Anhui, China, J. Med. 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Rev. Neurosci., 24, 677, 10.1146\u002Fannurev.neuro.24.1.677\nBruno, 2006, Activity-dependent release of precursor nerve growth factor, conversion to mature nerve growth factor, and its degradation by a protease cascade, Proc. Natl. Acad. Sci. U. S. A., 103, 6735, 10.1073\u002Fpnas.0510645103\nReichardt, 2006, Neurotrophin-regulated signalling pathways, Philos. Trans. R. Soc. Lond. B Biol. Sci., 361, 1545, 10.1098\u002Frstb.2006.1894\nMarlin, 2015, Biogenesis and function of the NGF\u002FTrkA signaling endosome, Int. Rev. Cell Mol. Biol., 314, 239, 10.1016\u002Fbs.ircmb.2014.10.002\nChao, 2003, Neurotrophins and their receptors: a convergence point for many signalling pathways, Nat. Rev. Neurosci., 4, 299, 10.1038\u002Fnrn1078\nSchecterson, 2010, Neurotrophin receptors: old friends with new partners, Dev. Neurobiol., 70, 332\nBlöchl, 2007, A cell-biological model of p75NTR signaling, J. Neurochem., 102, 289, 10.1111\u002Fj.1471-4159.2007.04496.x\nNykjaer, 2004, Sortilin is essential for proNGF-induced neuronal cell death, Nature, 427, 15, 10.1038\u002Fnature02319\nLevi-montalcini, 1987, The nerve growth factor: thirty-five years later, EMBO J., 6, 1145, 10.1002\u002Fj.1460-2075.1987.tb02347.x\nLevi-Montalcini, 1996, Nerve growth factor: from neurotrophin to neurokine, Trends Neurosci., 19, 514, 10.1016\u002FS0166-2236(96)10058-8\nLambiase, 2004, Nerve growth factor and the immune system: old and new concepts in the cross-talk between immune and resident cells during pathophysiological conditions, Curr. Opin. Allergy Clin. Immunol., 4, 425, 10.1097\u002F00130832-200410000-00015\nAloe, 2012, Nerve growth factor: from the early discoveries to the potential clinical use, J. Transl. Med., 10, 239, 10.1186\u002F1479-5876-10-239\nFreed, 1976, The role of nerve-growth factor (NGF) in the central nervous system, Brain Res. Bull., 1, 393, 10.1016\u002F0361-9230(76)90033-2\nKorsching, 1986, The role of nerve growth factor in the CNS, Trends Neurosci., 9, 570, 10.1016\u002F0166-2236(86)90179-7\nEbendal, 1988, Detection of nerve growth factor mRNA in the developing chicken embryo, Development, 102, 101, 10.1242\u002Fdev.102.1.101\nTurner, 1979, Retinal ganglion cell response to axotomy and nerve growth factor in the regenerating visual system of the newt (Notophthalmus viridescens): an ultrastructural morphometric analysis, Brain Res., 171, 197, 10.1016\u002F0006-8993(79)90327-5\nYip, 1983, Retrograde transport of nerve growth factor in lesioned goldfish retinal ganglion cells, J. Neurosci., 3, 2172, 10.1523\u002FJNEUROSCI.03-11-02172.1983\nCarmignoto, 1989, Effect of NGF on the survival of rat retinal ganglion cells following optic nerve section, J. Neurosci., 9, 1263, 10.1523\u002FJNEUROSCI.09-04-01263.1989\nMicera, 2004, Nerve growth factor involvement in the visual system: implications in allergic and neurodegenerative diseases, Cytokine Growth Factor Rev., 15, 411, 10.1016\u002Fj.cytogfr.2004.09.003\nFrade, 1996, Induction of cell death by endogenous nerve growth factor through its p75 receptor, Nature, 383, 166, 10.1038\u002F383166a0\nFrade, 1998, Microglia-derived nerve growth factor causes cell death in the developing retina, Neuron, 20, 35, 10.1016\u002FS0896-6273(00)80432-8\nKarlsson, 2001, Nerve growth factor is expressed by postmitotic avian retinal horizontal cells and supports their survival during development in an autocrine mode of action, Development, 128, 471, 10.1242\u002Fdev.128.4.471\nHarada, 2006, Effect of p75NTR on the regulation of naturally occurring cell death and retinal ganglion cell number in the mouse eye, Dev. Biol., 290, 57, 10.1016\u002Fj.ydbio.2005.08.051\nFrade, 1999, Genetic evidence for cell death mediated by nerve growth factor and the neurotrophin receptor p75 in the developing mouse retina and spinal cord, Development, 126, 683, 10.1242\u002Fdev.126.4.683\nBradshaw, 2015, NGF and ProNGF: Regulation of neuronal and neoplastic responses through receptor signaling, Adv. Biol. Regul., 58, 16, 10.1016\u002Fj.jbior.2014.11.003\nWässle, 2004, Parallel processing in the mammalian retina, Nat. Rev. Neurosci., 5, 1, 10.1038\u002Fnrn1497\nMasland, 2012, The neuronal organization of the retina, Neuron, 76, 266, 10.1016\u002Fj.neuron.2012.10.002\nHelga, 2001, Cellular organization of the vertebrate retina, Prog. Brain Res., 131, 3, 10.1016\u002FS0079-6123(01)31005-1\nBringmann, 2009, Role of retinal glial cells in neurotransmitter uptake and metabolism, Neurochem. Int., 54, 143, 10.1016\u002Fj.neuint.2008.10.014\nCuenca, 2014, Cellular responses following retinal injuries and therapeutic approaches for neurodegenerative diseases, Prog. Retin. Eye Res., 43, 17, 10.1016\u002Fj.preteyeres.2014.07.001\nBringmann, 2009, Cellular signaling and factors involved in Müller cell gliosis: neuroprotective and detrimental effects, Prog. Retin. Eye Res., 28, 423, 10.1016\u002Fj.preteyeres.2009.07.001\nNewman, 1996, The Müller cell: a functional element of the retina, Trends Neurosci., 19, 307, 10.1016\u002F0166-2236(96)10040-0\nHollander, 1991, Structure of the macroglia of the retina: sharing and division of labour between astrocytes and Müller Cells, J. Comp. Neurol., 313, 587, 10.1002\u002Fcne.903130405\nCunha-Vaz, 1997, The blood-ocular barriers: past, present, and future, Doc. Ophtalmol., 149, 10.1007\u002FBF02569055\nVon Bartheld, 1998, Neurotrophins in the developing and regenerating visual system, Histol. Histopathol., 13, 437\nQuigley, 2000, Retrograde axonal transport of BDNF in retinal ganglion cells is blocked by acute IOP elevation in rats, Invest. Ophthalmol. Vis. Sci., 41, 3460\nMatsumoto, 2014, Strain difference in photoreceptor cell death after retinal detachment in mice, Invest. Ophthalmol. Vis. Sci., 55, 4165, 10.1167\u002Fiovs.14-14238\nCui, 2002, Expression of trkA trkB, and trkC in injured and regenerating retinal ganglion cells of adult rats, Invest. Ophthalmol. Vis. Sci., 43, 1954\nGuo, 2009, Does elevated intraocular pressure reduce retinal TRKB-mediated survival signaling in experimental glaucoma?, Exp. Eye Res., 89, 921, 10.1016\u002Fj.exer.2009.08.003\nSoligo, 2015, The mature\u002Fpro nerve growth factor ratio is decreased in the brain of diabetic rats: analysis by ELISA methods, Brain Res., 1624, 455, 10.1016\u002Fj.brainres.2015.08.005\nSrinivasan, 2004, Microglia-derived pronerve growth factor promotes photoreceptor cell death via p75 neurotrophin receptor, J. Biol. Chem., 279, 41839, 10.1074\u002Fjbc.M402872200\nSantos, 2012, Sortilin participates in light-dependent photoreceptor degeneration in vivo, PLoS One, 7, 1, 10.1371\u002Fjournal.pone.0036243\nAl-Gayyar, 2011, Epicatechin blocks pro-nerve growth factor (proNGF)-mediated retinal neurodegeneration via inhibition of p75 neurotrophin receptor proNGF expression in a rat model of diabetes, Diabetologia, 54, 669, 10.1007\u002Fs00125-010-1994-3\nAli, 2011, Diabetes-induced peroxynitrite impairs the balance of pro-nerve growth factor and nerve growth factor, and causes neurovascular injury, Diabetologia, 54, 657, 10.1007\u002Fs00125-010-1935-1\nMysona, 2013, Modulation of p75NTR prevents diabetes- and proNGF-induced retinal inflammation and blood-retina barrier breakdown in mice and rats, Diabetologia, 56, 2329, 10.1007\u002Fs00125-013-2998-6\nLebrun-Julien, 2009, Inhibition of p75(NTR) in glia potentiates TrkA-mediated survival of injured retinal ganglion cells, Mol. Cell. Neurosci., 40, 410, 10.1016\u002Fj.mcn.2008.12.005\nWei, 2012, Enhanced expression of proneurotrophins in elevated introcular, Chin. Med. J. (Engl.), 125, 3875\nYang, 2013, Minocycline inhibits the production of the precursor form of nerve growth factor by retinal microglial, Neural Regener. Res., 8, 320\nBarcelona, 2016, p75NTR and its ligand proNGF activate paracrine mechanisms etiological to the vascular, inflammatory, and neurodegenerative pathologies of diabetic retinopathy, J. Neurosci., 36, 8826, 10.1523\u002FJNEUROSCI.4278-15.2016\nLebrun-Julien, 2010, ProNGF induces TNFalpha-dependent death of retinal ganglion cells through a p75NTR non-cell-autonomous signaling pathway, Proc. Natl. Acad. Sci. U. S. A., 107, 3817, 10.1073\u002Fpnas.0909276107\nBraunger, 2013, TGFβ signaling protects retinal neurons from programmed cell death during the development of the mammalian eye, J. Neurosci., 33, 14246, 10.1523\u002FJNEUROSCI.0991-13.2013\nBronzetti, 2007, Expression of neurotransmitters and neurotrophins in neurogenic inflammation of the rat retina, Eur. J. Histochem., 51, 251\nChakrabarti, 1990, Nerve growth factor (NGF), proNGF and NGF receptor-like immunoreactivity in BB rat retina, Brain Res., 523, 11, 10.1016\u002F0006-8993(90)91630-Y\nGarcia, 2014, Nerve growth factor inhibits osmotic swelling of rat retinal glial (Müller) and bipolar cells by inducing glial cytokine release, J. Neurochem., 131, 303, 10.1111\u002Fjnc.12822\nJansen, 2007, Roles for the pro-neurotrophin receptor sortilin in neuronal development, aging and brain injury, Nat. Neurosci., 10, 1449, 10.1038\u002Fnn2000\nCoassin, 2008, Retinal p75 and bax overexpression is associated with retinal ganglion cells apoptosis in a rat model of glaucoma, Graefes Arch, Clin. Exp. Ophthalmol., 246, 1743, 10.1007\u002Fs00417-008-0913-5\nColafrancesco, 2011, Ocular application of nerve growth factor protects degenerating retinal ganglion cells in a rat model of glaucoma, J. Glaucoma, 20, 100, 10.1097\u002FIJG.0b013e3181d787e5\nTaylor, 2003, Glutamate stimulates neurotrophin expression in cultured Müller cells, Brain Res. Mol. Brain Res., 111, 189, 10.1016\u002FS0169-328X(03)00030-5\nAgarwal, 2007, Comparison of expression profile of neurotrophins and their receptors in primary and transformed rat retinal ganglion cells, Mol. Vis., 13, 1311\nSun, 2008, Nerve growth factor helps protect retina in experimental retinal detachment, Ophthalmologica, 222, 58, 10.1159\u002F000109281\nVecino, 1998, Immunohistochemical distribution of neurotrophins and their receptors in the rat retina and the effects of ischemia and reperfusion, Gen. Pharmacol., 30, 305, 10.1016\u002FS0306-3623(97)00361-3\nLiu, 2010, Neuronal-driven angiogenesis: role of NGF in retinal neovascularization in an oxygen-induced retinopathy model, Invest. Ophthalmol. Vis. Sci., 51, 3749, 10.1167\u002Fiovs.09-4226\nBalzamino, 2015, NGF expression in reelin-deprived retinal cells: a potential neuroprotective effect, NeuroMolecular Med., 17, 314, 10.1007\u002Fs12017-015-8360-z\nHarada, 2002, Microglia-Müller glia cell interactions control neurotrophic factor production during light-induced retinal degeneration, J. Neurosci., 22, 9228, 10.1523\u002FJNEUROSCI.22-21-09228.2002\nDi Polo, 2000, Colocalization of TrkB and brain-derived neurotrophic factor proteins in green-red-sensitive cone outer segments, Invest. Ophthalmol. Vis. Sci., 41, 4014\nHarada, 2000, Modification of glial-neuronal cell interactions prevents photoreceptor apoptosis during light-induced retinal degeneration, Neuron, 26, 533, 10.1016\u002FS0896-6273(00)81185-X\nSrinivasan, 2007, Photic injury promotes cleavage of p75NTR by TACE and nuclear trafficking of the p75 intracellular domain, Mol. Cell. Neurosci., 36, 449, 10.1016\u002Fj.mcn.2007.08.005\nKokona, 2012, The neurosteroid dehydroepiandrosterone (DHEA) protects the retina from AMPA-induced excitotoxicity: NGF TrkA receptor involvement, Neuropharmacology, 62, 2106, 10.1016\u002Fj.neuropharm.2012.01.006\nRocco, 2015, Effect of purified murine NGF on isolated photoreceptors of a rodent developing retinitis pigmentosa, PLoS One, 10, 1, 10.1371\u002Fjournal.pone.0124810\nSheedlo, 2002, Expression of p75 NTR in photoreceptor cells of dystrophic rat retinas, Mol. Brain Res., 103, 71, 10.1016\u002FS0169-328X(02)00185-7\nWexler, 1998, Role of the low-affinity NGF receptor (p75) in survival of retinal bipolar cells, Vis. Neurosci., 15, 211, 10.1017\u002FS095252389815201X\nCarmignoto, 1991, Expression of NGF receptor and NGF receptor mRNA in the developing and adult rat retina, Exp. Neurol., 111, 302, 10.1016\u002F0014-4886(91)90097-V\nZanellato, 1993, Developing rat retinal ganglion cells express the Functional NGF receptor p140trka, Dev. Biol., 159, 105, 10.1006\u002Fdbio.1993.1224\nRudzinski, 2004, Changes in retinal expression of neurotrophins and neurotrophin receptors induced by ocular hypertension, J. Neurobiol., 58, 341, 10.1002\u002Fneu.10293\nHu, 1998, Localization of p75 neurotrophin receptor in the retina of the adult SD rat: an immunocytochemical study at light and electron microscopic levels, Glia, 24, 187, 10.1002\u002F(SICI)1098-1136(199810)24:2\u003C187::AID-GLIA4>3.0.CO;2-1\nHu, 1999, Expression of p75 neurotrophin receptor in the injured and regenerating rat retina, Neuroreport, 10, 1293, 10.1097\u002F00001756-199904260-00026\nXu, 2009, Immunohistochemical localization of sortilin and p75 NTR in normal and ischemic rat retina, Neurosci. Lett., 454, 81, 10.1016\u002Fj.neulet.2009.02.036\nDing, 2001, Study of the role of the low-affinity neurotrophin receptor p75 in naturally occurring cell death during development of the rat retina, Dev. Neurosci., 23, 390, 10.1159\u002F000048725\nAl-gayyar, 2013, Diabetes and overexpression of proNGF cause retinal neurodegeneration via activation of RhoA pathway, PLoS One, 8, 10.1371\u002Fjournal.pone.0054692\nButowt, 2005, Anterograde axonal transport of BDNF and NT-3 by retinal ganglion cells: roles of neurotrophin receptors, Mol. Cell. Neurosci., 29, 11, 10.1016\u002Fj.mcn.2005.02.004\nSuzuki, 1998, Localization of mRNAs for trkB isoforms and p75 in rat retinal ganglion cells, J. Neurosci. Res., 54, 27, 10.1002\u002F(SICI)1097-4547(19981001)54:1\u003C27::AID-JNR4>3.0.CO;2-J\nShen, 2013, Involvement of NT3 and P75 NTR in photoreceptor degeneration following selective Müller cell ablation, J. Neuroinflammation, 10, 137, 10.1186\u002F1742-2094-10-137\nWang, 2016, NGF increases VEGF expression and promotes cell proliferation via ERK1\u002F2 and AKT signaling in Müller cells, Mol. Vis., 22, 254\nHammes, 1995, Nerve growth factor prevents both neuroretinal programmed cell death and capillary pathology in experimental diabetes, Mol. Med., 1, 527, 10.1007\u002FBF03401589\nJian, 2015, Acute retinal injury and the relationship between nerve growth factor, Notch1 transcription and short-lived dedifferentiation transient changes of mammalian Müller cells, Vis. Res., 110, 107, 10.1016\u002Fj.visres.2015.01.030\nKim, 2013, Nerve growth factor-mediated vascular endothelial growth factor expression of astrocyte in retinal vascular development, Biochem. Biophys. Res. Commun., 431, 740, 10.1016\u002Fj.bbrc.2013.01.045\nNakamura, 2005, Effect of p75NTR on the regulation of photoreceptor apoptosis in the rd mouse, Mol. Vis., 11, 1229\nWei, 2007, Enhanced protein expressions of sortilin and p75NTR in retina of rat following elevated intraocular pressure-induced retinal ischemia, Neurosci. Lett., 429, 169, 10.1016\u002Fj.neulet.2007.10.012\nAmendola, 2003, Postnatal changes in nerve growth factor and brain derived neurotrophic factor levels in the retina, visual cortex, and geniculate nucleus in rats with retinitis pigmentosa, Neurosci. Lett., 345, 37, 10.1016\u002FS0304-3940(03)00491-9\nLenzi, 2005, Effect of exogenous administration of nerve growth factor in the retina of rats with inherited retinitis pigmentosa, Vis. Res., 45, 1491, 10.1016\u002Fj.visres.2004.12.020\nSancho-pelluz, 2008, Photoreceptor cell death mechanisms in inherited retinal degeneration, Mol. Neurobiol., 38, 253, 10.1007\u002Fs12035-008-8045-9\nAthanasiou, 2013, The cell stress machinery and retinal degeneration, FEBS Lett., 587, 2008, 10.1016\u002Fj.febslet.2013.05.020\nMachalinska, 2010, Sodium iodate selectively injuries the posterior pole of the retina in a dose-dependent manner: morphological and electrophysiological study, Neurochem. Res., 35, 1819, 10.1007\u002Fs11064-010-0248-6\nWang, 2014, Direct effect of sodium iodate on neurosensory retina, Invest. Ophthalmol. Vis. Sci., 55, 1941, 10.1167\u002Fiovs.13-13075\nBouhenni, 2012, Animal models of glaucoma, J. Biomed. Biotechnol., 2012, 10.1155\u002F2012\u002F692609\nYou, 2013, Optic neuropathies: characteristic features and mechanisms of retinal ganglion cell loss, Rev. Neurosci., 24, 301, 10.1515\u002Frevneuro-2013-0003\nAhmed, 2010, Optic nerve and vitreal inflammation are both RGC neuroprotective but only the latter is RGC axogenic, Neurobiol. Dis., 37, 441, 10.1016\u002Fj.nbd.2009.10.024\nHarada, 2015, TrkB signaling in retinal glia stimulates neuroprotection after optic nerve injury, Am. J. Pathol., 185, 3238, 10.1016\u002Fj.ajpath.2015.08.005\nMysona, 2014, Nerve growth factor in diabetic retinopathy: beyond neurons, Expert Rev. Ophthalmol., 9, 99, 10.1586\u002F17469899.2014.903157\nSimó, 2014, Neurodegeneration in the diabetic eye: new insights and therapeutic perspectives, Trends Endocrinol. Metab., 25, 23, 10.1016\u002Fj.tem.2013.09.005\nKern, 2008, Retinal ganglion cells in diabetes, J. Physiol., 18, 4401, 10.1113\u002Fjphysiol.2008.156695\nStem, 2013, Neurodegeneration in the pathogenesis of diabetic retinopathy: molecular mechanisms and therapeutic implications, Curr. Med. Chem., 20, 3241, 10.2174\u002F09298673113209990027\nOla, 2015, Neuroprotective effects of rutin in streptozotocin-induced diabetic rat retina, J. Mol. Neurosci., 56, 440, 10.1007\u002Fs12031-015-0561-2\nColafrancesco, 2011, Effect of eye NGF administration on two animal models of retinal ganglion cells degeneration, Ann. Ist. Super. Sanita, 47, 284\nLe Moan, 2011, Oxygen-dependent cleavage of the p75 neurotrophin receptor triggers stabilization of HIF-1α, Mol. Cell, 44, 476, 10.1016\u002Fj.molcel.2011.08.033\nOsborne, 2004, Retinal ischemia: mechanisms of damage and potential therapeutic strategies, Prog. Retin. Eye Res., 23, 91, 10.1016\u002Fj.preteyeres.2003.12.001\nBringmann, 2005, Neuronal versus glial cell swelling in the ischaemic retina, Acta Ophthalmol. Scand., 83, 528, 10.1111\u002Fj.1600-0420.2005.00565.x\nNakamura, 2007, Intracellular sortilin expression pattern regulates proNGF-induced naturally occurring cell death during development, Cell Death Differ., 14, 1552, 10.1038\u002Fsj.cdd.4402173\nSivilia, 2009, Intravitreal NGF administration counteracts retina degeneration after permanent carotid artery occlusion in rat, BMC Dev. Biol., 10, 1\nGuo, 2014, Dysregulation of neurotrophic and in fl ammatory systems accompanied by decreased CREB signaling in ischemic rat retina, Exp. Eye Res., 125, 156, 10.1016\u002Fj.exer.2014.06.003\nMorrison, 2008, Rat models for glaucoma research, Prog. Brain Res., 173, 285, 10.1016\u002FS0079-6123(08)01121-7\nKrady, 2005, Activation in a rodent model of diabetic retinopathy, Diabetes, 54, 1559, 10.2337\u002Fdiabetes.54.5.1559\nTomita, 1998, Increased expression of low-affinity NGF receptor in rat retinal Müller cells after ischemia and reperfusion, Cell Struct. Funct., 23, 201, 10.1247\u002Fcsf.23.201\nHempstead, 2009, Regulating proNGF action: multiple targets for therapeutic intervention, Neurotox. Res., 16, 255, 10.1007\u002Fs12640-009-9054-9\nLambiase, 1996, Nerve growth factor delays retinal degeneration in C3H mice, Graefes Arch. Clin. Exp. Ophthalmol., 234, S96, 10.1007\u002FBF02343055\nHuo, 2012, Transplanted olfactory ensheathing cells reduce retinal degeneration in Royal College of Surgeons Rats, Curr. Eye Res., 37, 749, 10.3109\u002F02713683.2012.697972\nJian, 2015, Rat BMSCs initiate retinal endogenous repair through NGF\u002FTrkA signaling, Exp. Eye Res., 132, 34, 10.1016\u002Fj.exer.2015.01.008\nMead, 2014, Paracrine-mediated neuroprotection and neuritogenesis of axotomised retinal ganglion cells by human dental pulp stem cells: comparison with human bone marrow and adipose-derived mesenchymal stem cells, PLoS One, 9, 10.1371\u002Fjournal.pone.0109305\nSun, 2007, Effects of nerve growth factor for retinal cell survival in experimental retinal detachment, Curr. Eye Res., 32, 765, 10.1080\u002F02713680701531082\nRohrer, 2003, Lack of p75 receptor does not protect photoreceptors from light-induced cell death, Exp. Eye Res., 76, 125, 10.1016\u002FS0014-4835(02)00258-0\nLaVail, 1992, Multiple growth factors cytokines, and neurotrophins rescue photoreceptors from the damaging effects of constant light, Proc. Natl. Acad. Sci. U. S. A., 89, 11249, 10.1073\u002Fpnas.89.23.11249\nShi, 2007, Neurotrophic rationale in glaucoma: a TrkA agonist, but not NGF or a p75 antagonist, protects retinal ganglion cells in vivo, Dev. Neurobiol., 67, 884, 10.1002\u002Fdneu.20360\nMatragoon, 2012, Electroporation-mediated gene delivery of cleavage-resistant pro-nerve growth factor causes retinal neuro- and vascular degeneration, Mol. Vis., 18, 2993\nLambiase, 2009, Experimental and clinical evidence of neuroprotection by nerve growth factor eye drops: implications for glaucoma, Proc. Natl. Acad. Sci. U. S. A., 106, 13469, 10.1073\u002Fpnas.0906678106\nBai, 2010, Chronic and acute models of retinal neurodegeneration TrkA activity are neuroprotective whereas p75NTR activity is neurotoxic through a paracrine mechanism, J. Biol. Chem., 285, 39392, 10.1074\u002Fjbc.M110.147801\nRabacchi, 1994, Nerve growth factor reduces apoptosis of axotomized retinal ganglion cells in the neonatal rat, Neuroscience, 63, 969, 10.1016\u002F0306-4522(94)90565-7\nRodríguez-Muela, 2012, Autophagy promotes survival of retinal ganglion cells after optic nerve axotomy in mice, Cell Death Differ., 19, 162, 10.1038\u002Fcdd.2011.88\nMead, 2013, Intravitreally transplanted dental pulp stem cells promote neuroprotection and axon regeneration of retinal ganglion cells after optic nerve injury, Vis. Neurosci., 54, 7544\nMaliartchouk, 2007, A designed peptidomimetic agonistic ligand of TrkA nerve growth factor receptors, Mol. Pharmacol., 57, 385\nBringmann, 2006, Müller cells in the healthy and diseased retina, Prog. 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Biosci., 37, 289, 10.1007\u002Fs12038-012-9191-9\nMcSherry, 2007, Molecular basis of invasion in breast cancer, Cell. Mol. Life Sci., 64, 3201, 10.1007\u002Fs00018-007-7388-0\nKoontongkaew, 2013, The tumor microenvironment contribution to development, growth, invasion and metastasis of head and neck squamous cell carcinomas, J. Cancer, 4, 66, 10.7150\u002Fjca.5112\nHadler-Olsen, 2013, Matrix metalloproteinases in cancer: their value as diagnostic and prognostic markers and therapeutic targets, Tumour Biol., 34, 2041, 10.1007\u002Fs13277-013-0842-8\nGiordano, 2016, Activated FXR inhibits leptin signaling and counteracts tumor-promoting activities of cancer-associated fibroblasts in breast malignancy, Sci. Rep., 6, 21782, 10.1038\u002Fsrep21782\nAhn, 2015, Leptin promotes human endometriotic cell migration and invasion by up-regulating MMP-2 through the JAK2\u002FSTAT3 signaling pathway, Mol. Hum. Reprod., 21, 792, 10.1093\u002Fmolehr\u002Fgav039\nBerg, 2014, Circulating and adipose tissue matrix metalloproteinases in cardiometabolic risk environments: pathophysiological aspects, Horm. Mol. Biol. Clin. Investig., 17, 79\nMartínez-Martínez, 2014, The potential role of leptin in the vascular remodeling associated with obesity, Int. J. Obes. (Lond.), 38, 1565, 10.1038\u002Fijo.2014.37\nCui, 2013, Thrombospondin 1 mediates renal dysfunction in a mouse model of high-fat diet-induced obesity, Am. J. Physiol. Renal Physiol., 305, F871, 10.1152\u002Fajprenal.00209.2013\nRay, 2012, Obesity and breast cancer: a clinical biochemistry perspective, Clin. Biochem., 45, 189, 10.1016\u002Fj.clinbiochem.2011.11.016\nStrong, 2015, Leptin produced by obese adipose stromal\u002Fstem cells enhances proliferation and metastasis of estrogen receptor positive breast cancers, Breast Cancer Res., 17, 112, 10.1186\u002Fs13058-015-0622-z\nChoi, 2010, Leptin promotes the myofibroblastic phenotype in hepatic stellate cells by activating the hedgehog pathway, J. Biol. Chem., 285, 36551, 10.1074\u002Fjbc.M110.168542\nYan, 2012, Leptin-induced epithelial-mesenchymal transition in breast cancer cells requires β-catenin activation via Akt\u002FGSK3- and MTA1\u002FWnt1 protein-dependent pathways, J. Biol. Chem., 287, 8598, 10.1074\u002Fjbc.M111.322800\nFeng, 2013, Leptin promotes metastasis by inducing an epithelial-mesenchymal transition in A549 lung cancer cells, Oncol. Res., 21, 165, 10.3727\u002F096504014X13887748696662\nWang, 2015, Activation of IL-8 via PI3 K\u002FAkt-dependent pathway is involved in leptin-mediated epithelial-mesenchymal transition in human breast cancer cells, Cancer Biol. Ther., 16, 1220, 10.1080\u002F15384047.2015.1056409\nKato, 2015, Leptin stimulates migration and invasion and maintains cancer stem-like properties in ovarian cancer cells: an explanation for poor outcomes in obese women, Oncotarget, 6, 21100, 10.18632\u002Foncotarget.4228\nNieman, 2013, Adipose tissue and adipocytes support tumorigenesis and metastasis, Biochim. Biophys. Acta, 1831, 1533, 10.1016\u002Fj.bbalip.2013.02.010\nXiong, 2015, Hematopoietic stem cell-derived adipocytes and fibroblasts in the tumor microenvironment, World J. Stem Cells, 7, 253, 10.4252\u002Fwjsc.v7.i2.253\nXiang, 2016, Omental adipocytes enhance the invasiveness of gastric cancer cells by oleic acid-induced activation of the PI3K-Akt signaling pathway, Int. J. Biochem. Cell Biol., 84, 14, 10.1016\u002Fj.biocel.2016.12.002\nWen, 2017, Adipocytes activate mitochondrial fatty acid oxidation and autophagy to promote tumor growth in colon cancer, Cell Death Dis., 8, e2593, 10.1038\u002Fcddis.2017.21\nMeyer, 2016, Adipocytes promote pancreatic cancer cell proliferation via glutamine transfer, Biochem. Biophys. Rep., 7, 144\nMoreira, 2015, Adipocyte secreted factors enhance aggressiveness of prostate carcinoma cells, PLoS One, 10, e0123217, 10.1371\u002Fjournal.pone.0123217\nIto, 2015, Adipocyte-derived monocyte chemotactic protein-1 (MCP-1) promotes prostate cancer progression through the induction of MMP-2 activity, Prostate, 75, 1009, 10.1002\u002Fpros.22972\nRibeiro, 2012, Human periprostatic adipose tissue promotes prostate cancer aggressiveness in vitro, J. Exp. Clin. Cancer Res., 31, 32, 10.1186\u002F1756-9966-31-32\nZhu, 2017, Invasive breast cancer preferably and predominantly occurs at the interface between fibroglandular and adipose tissue, Clin. Breast Cancer, 17, e11, 10.1016\u002Fj.clbc.2016.07.009\nFletcher, 2017, Human breast adipose tissue: characterization of factors that change during tumor progression in human breast cancer, J. Exp. Clin. Cancer Res., 36, 26, 10.1186\u002Fs13046-017-0494-4\nDivella, 2016, Obesity and cancer: the role of adipose tissue and adipo-cytokines-induced chronic inflammation, J. Cancer, 7, 2346, 10.7150\u002Fjca.16884\nHefetz-Sela, 2013, Adipocytes: impact on tumor growth and potential sites for therapeutic intervention, Pharmacol. Ther., 138, 197, 10.1016\u002Fj.pharmthera.2013.01.008\nMassa, 2016, Interaction between breast cancer cells and adipose tissue cells derived from fat grafting, Aesthet. Surg. J., 36, 358, 10.1093\u002Fasj\u002Fsjv194\nD'Esposito, 2016, Adipose microenvironment promotes triple negative breast cancer cell invasiveness and dissemination by producing CCL5, Oncotarget, 7, 24495, 10.18632\u002Foncotarget.8336\nLee, 2015, Adipocytes can induce epithelial-mesenchymal transition in breast cancer cells, Breast Cancer Res. Treat., 153, 323, 10.1007\u002Fs10549-015-3550-9\nYao-Borengasser, 2015, Adipocyte hypoxia promotes epithelial-mesenchymal transition-related gene expression and estrogen receptor-negative phenotype in breast cancer cells, Oncol. Rep., 33, 2689, 10.3892\u002For.2015.3880\nFujisaki, 2015, Cancer-mediated adipose reversion promotes cancer cell migration via IL-6 and MCP-1, Breast Cancer Res. Treat., 150, 255, 10.1007\u002Fs10549-015-3318-2\nWang, 2015, Human adipocytes stimulate invasion of breast cancer MCF-7 cells by secreting IGFBP-2, PLoS One, 10, e0119348, 10.1371\u002Fjournal.pone.0119348\nPark, 2011, Paracrine and endocrine effects of adipose tissue on cancer development and progression, Endocr Rev., 32, 550, 10.1210\u002Fer.2010-0030\nDirat, 2011, Cancer-associated adipocytes exhibit an activated phenotype and contribute to breast cancer invasion, Cancer Res., 71, 2455, 10.1158\u002F0008-5472.CAN-10-3323\nWolfson, 2015, Adipocyte activation of cancer stem cell signaling in breast cancer, World J. Biol Chem., 6, 39, 10.4331\u002Fwjbc.v6.i2.39\nLiu, 2013, Local adipocytes enable estrogen-dependent breast cancer growth: role of leptin and aromatase, Adipocyte, 2, 165, 10.4161\u002Fadip.23645\nMarwarha, 2012, Leptin signaling and Alzheimer's disease, Am. J. Neurodegener. Dis., 1, 245\nProkop, 2012, Leptin and leptin receptor: analysis of a structure to function relationship in interaction and evolution from humans to fish, Peptides, 38, 326, 10.1016\u002Fj.peptides.2012.10.002\nZhang, 2005, Leptin: structure, function and biology, Vitam. Horm., 71, 345, 10.1016\u002FS0083-6729(05)71012-8\nChimal-Vega, 2015, Exploring the structure and conformational landscape of human leptin. A molecular dynamics approach, J. Theor. Biol., 385, 90, 10.1016\u002Fj.jtbi.2015.08.014\nPeelman, 2014, 20 years of leptin: insights into signaling assemblies of the leptin receptor, J. Endocrinol., 223, 10.1530\u002FJOE-14-0264\nDozio, 2009, Leptin, ciliary neurotrophic factor, leukemia inhibitory factor and interleukin-6: class-I cytokines involved in the neuroendocrine regulation of the reproductive function, Curr. Protein Pept. Sci., 10, 577, 10.2174\u002F138920309789630561\nFrühbeck, 2006, Intracellular signalling pathways activated by leptin, Biochem. J., 393, 7, 10.1042\u002FBJ20051578\nHan, 2015, Leptin and its receptor in hematologic malignancies, Int. J. Clin. Exp. Med., 8, 19840\nJiang, 2014, Leptin signaling molecular actions and drug target in hepatocellular carcinoma, Drug Des. Devel. Ther., 8, 2295\nSiveen, 2014, Targeting the STAT3 signaling pathway in cancer: role of synthetic and natural inhibitors, Biochim. Biophys. Acta, 1845, 136\nKim, 2016, Signal transducer and activator of transcription 3 as a therapeutic target for cancer and the tumor microenvironment, Arch. Pharm. Res., 39, 1085, 10.1007\u002Fs12272-016-0795-8\nLi, 2017, Regulation of EMT by STAT3 in gastrointestinal cancer (review), Int. J. Oncol., 50, 753, 10.3892\u002Fijo.2017.3846\nYoon, 2015, Signal transducers and activators of transcription 3-induced metastatic potential in gastric cancer cells is enhanced by glycogen synthase kinase-3β, APMIS, 123, 373, 10.1111\u002Fapm.12370\nZhang, 2015, STAT3 cooperates with Twist to mediate epithelial-mesenchymal transition in human hepatocellular carcinoma cells, Oncol. Rep., 33, 1872, 10.3892\u002For.2015.3783\nYang, 2017, STAT3 overexpression promotes metastasis in intrahepatic cholangiocarcinoma and correlates negatively with surgical outcome, Oncotarget, 8, 7710, 10.18632\u002Foncotarget.13846\nChen, 2015, Prognostic and clinical significance of STAT3 and MMP9 in patients with gastric cancer: a meta-analysis of a Chinese cohort, Int. J Clin. Exp. Med., 8, 546\nYu, 2016, The prognostic value of pSTAT3 in gastric cancer: a meta-analysis, J. Cancer Res Clin. Oncol., 142, 649, 10.1007\u002Fs00432-015-2023-1\nDeng, 2014, STAT3 regulation the expression of VEGF-D in HGC-27 gastric cancer cell, Am. J. Transl. Res., 6, 756\nSong, 2014, STAT3, p-STAT3 and HIF-1α are associated with vasculogenic mimicry and impact on survival in gastric adenocarcinoma, Oncol. Lett., 8, 431, 10.3892\u002Fol.2014.2059\nZhong, 2014, Expressions of STAT3, p-STAT3 and E-cadherin in colorectal cancer and clinical implications, Zhonghua Wei Chang Wai Ke Za Zhi (Chinese Journal of Gastrointestinal Surgery), 17, 594\nJi, 2016, The role of p-STAT3 as a prognostic and clinicopathological marker in colorectal cancer: a systematic review and meta-analysis, PLoS One, 11, e0160125, 10.1371\u002Fjournal.pone.0160125\nXu, 2014, A meta-analysis of STAT3 and phospho-STAT3 expression and survival of patients with non-small-cell lung cancer, Eur. J. Surg. Oncol., 40, 311, 10.1016\u002Fj.ejso.2013.11.012\nZhao, 2011, JAK2\u002FSTAT3 signaling pathway activation mediates tumor angiogenesis by upregulation of VEGF and bFGF in non-small-cell lung cancer, Lung Cancer, 73, 366, 10.1016\u002Fj.lungcan.2011.01.002\nYu, 2015, Activated STAT3 correlates with prognosis of non-small cell lung cancer and indicates new anticancer strategies, Cancer Chemother. Pharmacol., 75, 917, 10.1007\u002Fs00280-015-2710-2\nLiu, 2014, Activation of STAT3 is involved in malignancy mediated by CXCL12-CXCR4 signaling in human breast cancer, Oncol. Rep., 32, 2760, 10.3892\u002For.2014.3536\nWei, 2015, Expression of signal transducer and activator of transcription 3 in breast cancer and its clinical significance, J. Cancer Res. Ther., 11, C56, 10.4103\u002F0973-1482.163840\nMcDaniel, 2017, Genomic regulation of invasion by STAT3 in triple negative breast cancer, Oncotarget, 8, 8226, 10.18632\u002Foncotarget.14153\nDonato, 2010, The PI3 K signaling pathway mediates the biological effects of leptin, Arq. Bras. Endocrinol. Metabol., 54, 591, 10.1590\u002FS0004-27302010000700002\nSheen, 2016, Constitutively activated PI3 K accelerates tumor initiation and modifies histopathology of breast cancer, Oncogenesis, 5, e267, 10.1038\u002Foncsis.2016.65\nZardavas, 2014, PIK3CA mutations in breast cancer: reconciling findings from preclinical and clinical data, Breast Cancer Res., 16, 201, 10.1186\u002Fbcr3605\nArsenic, 2014, Analysis of PIK3CA mutations in breast cancer subtypes, Appl. Immunohistochem. Mol. Morphol., 22, 50, 10.1097\u002FPDM.0b013e318297afea\nFiroozinia, 2014, PIK3CA gene amplification and PI3 K p110α protein expression in breast carcinoma, Int. J. Med. Sci., 11, 620, 10.7150\u002Fijms.8251\nMendelová, 2014, Correlation between the incidence of PIK3CA mutations in breast cancer and histopathological characteristics of the tumor, Ceska Gynekol., 79, 283\nTserga, 2016, Mutation of genes of the PI3 K\u002FAKT pathway in breast cancer supports their potential importance as biomarker for breast cancer aggressiveness, Virchows Arch., 469, 35, 10.1007\u002Fs00428-016-1938-5\nHarada, 2016, Prognostic and clinical impact of PIK3CA mutation in gastric cancer: pyrosequencing technology and literature review, BMC. Cancer, 16, 400, 10.1186\u002Fs12885-016-2422-y\nShi, 2012, Highly frequent PIK3CA amplification is associated with poor prognosis in gastric cancer, BMC. Cancer, 12, 50, 10.1186\u002F1471-2407-12-50\nLiu, 2010, Up-regulation of PIK3CA promotes metastasis in gastric carcinoma, World J. Gastroenterol., 16, 4986, 10.3748\u002Fwjg.v16.i39.4986\nGu, 2014, Clinicopathological significance of PI3 K, Akt and survivin expression in gastric cancer, Biomed. Pharmacother., 68, 471, 10.1016\u002Fj.biopha.2014.03.010\nZhu, 2012, PI3 K expression and PIK3CA mutations are related to colorectal cancer metastases, World J. Gastroenterol., 18, 3745, 10.3748\u002Fwjg.v18.i28.3745\nDent, 2014, Crosstalk between ERK, AKT, and cell survival, Cancer Biol. Ther., 15, 245, 10.4161\u002Fcbt.27541\nDai, 2014, Interaction of mTOR and Erk1\u002F2 signaling to regulate oligodendrocyte differentiation, Glia, 62, 2096, 10.1002\u002Fglia.22729\nErsahin, 2015, The PI3 K\u002FAKT\u002FmTOR interactive pathway, Mol. Biosyst., 11, 1946, 10.1039\u002FC5MB00101C\nGungorduk, 2014, Immunolocalization of ERK1\u002F2 and p-AKT in normal endometrium, endometrial hyperplasia, and early and advanced stage endometrioid endometrial adenocancer and their prognostic significance in malignant group, Eur. J. Obstet. Gynecol. Reprod. Biol., 179, 147, 10.1016\u002Fj.ejogrb.2014.05.040\nLi, 2015, Expression of CD44 in pancreatic cancer and its significance, Int. J. Clin. Exp. Pathol., 8, 6724\nWang, 2015, High EGFR and low p-Akt expression is associated with better outcome after nimotuzumab-containing treatment in esophageal cancer patients: preliminary clinical result and testable hypothesis, Oncotarget, 6, 18674, 10.18632\u002Foncotarget.4367\nLin, 2006, Morphoproteomic and molecular concomitants of an overexpressed and activated mTOR pathway in renal cell carcinomas, Ann. Clin. Lab. Sci., 36, 283\nAleskandarany, 2011, Clinicopathologic and molecular significance of phospho-Akt expression in early invasive breast cancer, Breast Cancer Res. Treat., 127, 407, 10.1007\u002Fs10549-010-1012-y\nYun, 2013, Clinicopathological significance of PTEN and PI3K\u002FAKT signal transduction pathway in non-small cell lung cancer, Int. J. Clin. Exp. Pathol., 6, 2112\nChen, 2015, Expression and prognostic role of MEKK3 and pERK in patients with renal clear cell carcinoma, Asian Pac. J Cancer Prev., 16, 2495, 10.7314\u002FAPJCP.2015.16.6.2495\nHolck, 2016, Localization of active, dually phosphorylated extracellular signal-regulated kinase 1 and 2 in colorectal cancer with or without activating BRAF and KRAS mutations, Hum. Pathol., 54, 37, 10.1016\u002Fj.humpath.2016.03.001\nDavid, 2004, Phospho-Akt overexpression in non-small cell lung cancer confers significant stage-independent survival disadvantage, Clin. Cancer Res., 10, 6865, 10.1158\u002F1078-0432.CCR-04-0174\nJia, 2014, REDD1 and p-AKT over-expression may predict poor prognosis in ovarian cancer, Int. J. Clin. Exp. Pathol., 7, 5940\nBaba, 2011, Phosphorylated AKT expression is associated with PIK3CA mutation, low stage, and favorable outcome in 717 colorectal cancers, Cancer, 117, 1399, 10.1002\u002Fcncr.25630\nPantuck, 2007, Prognostic relevance of the mTOR pathway in renal cell carcinoma: implications for molecular patient selection for targeted therapy, Cancer, 109, 2257, 10.1002\u002Fcncr.22677\nYip, 2014, Phosphorylated Akt expression is a prognostic marker in early-stage non-small cell lung cancer, J. Clin. Pathol., 67, 333, 10.1136\u002Fjclinpath-2013-201870\nCampbell, 2009, Activated extracellular signal-regulated kinase is an independent prognostic factor in clinically confined renal cell carcinoma, Cancer, 115, 3457, 10.1002\u002Fcncr.24389\nTsujino, 2016, Increased phosphorylation of ERK1\u002F2 is associated with worse chemotherapeutic outcome and a poor prognosis in advanced lung adenocarcinoma, Med. Mol. Morphol., 49, 98, 10.1007\u002Fs00795-015-0130-3\nMa, 2012, Epidermal growth factor (EGF) and interleukin (IL)-1β synergistically promote ERK1\u002F2-mediated invasive breast ductal cancer cell migration and invasion, Mol. Cancer, 11, 79, 10.1186\u002F1476-4598-11-79\nTasioudi, 2012, pERK activation in esophageal carcinomas: clinicopathological associations, Pathol. Res. Pract., 208, 398, 10.1016\u002Fj.prp.2012.05.009\nTai, 2013, High nuclear expression of phosphorylated extracellular signal-regulated kinase in tumor cells in colorectal glands is associated with poor outcome in colorectal cancer, Ann. Diagn. Pathol., 17, 165, 10.1016\u002Fj.anndiagpath.2012.09.004\nThrift, 2016, Determination of risk for Barrett's esophagus and esophageal adenocarcinoma, Curr. Opin. Gastroenterol., 32, 319, 10.1097\u002FMOG.0000000000000274\nTercioti-Junior, 2011, Adenocarcinoma versus squamous cell carcinoma: analysis of 306 patients in university hospital, Arq. Bras. Cir Dig., 24, 272, 10.1590\u002FS0102-67202011000400005\nTrevellin, 2015, Esophageal adenocarcinoma and obesity: peritumoral adipose tissue plays a role in lymph node invasion, Oncotarget, 6, 11203, 10.18632\u002Foncotarget.3587\nDuan, 2014, Expression of leptin and adiponectin in esophageal squamous cell carcinoma and their clinical significance, Zhonghua Zhong Liu Za Zhi (Chinese Journal of Oncology), 36, 839\nChoi, 2015, Implication of leptin-signaling proteins and epstein-barr virus in gastric carcinomas, PLoS One, 10, e0130839, 10.1371\u002Fjournal.pone.0130839\nEspejo Romero, 2003, Classification of stomach adenocarcinomas, Rev. Gastroenterol. Peru, 23, 199\nZhao, 2007, Correlation between expression of leptin and clinicopathological features and prognosis in patients with gastric cancer, J. Gastroenterol. Hepatol, 22, 1317, 10.1111\u002Fj.1440-1746.2007.04941.x\nGeng, 2012, Leptin and HER-2 are associated with gastric cancer progression and prognosis of patients, Biomed. Pharmacother., 66, 419, 10.1016\u002Fj.biopha.2012.03.002\nIshikawa, 2006, Expression pattern of leptin and leptin receptor (OB-R) in human gastric cancer, World J. Gastroenterol., 12, 5517, 10.3748\u002Fwjg.v12.i34.5517\nDong, 2013, Leptin-mediated regulation of MT1-MMP localization is KIF1 B dependent and enhances gastric cancer cell invasion, Carcinogenesis, 34, 974, 10.1093\u002Fcarcin\u002Fbgt028\nDong, 2014, Leptin-mediated regulation of ICAM-1 is Rho\u002FROCK dependent and enhances gastric cancer cell migration, Br. J. Cancer, 110, 1801, 10.1038\u002Fbjc.2014.70\nMakrilia, 2009, Cell adhesion molecules: role and clinical significance in cancer, Cancer Invest., 27, 1023, 10.3109\u002F07357900902769749\nBain, 2014, Tumour expression of leptin is associated with chemotherapy resistance and therapy-independent prognosis in gastro-oesophageal adenocarcinomas, Br. J. Cancer, 110, 1525, 10.1038\u002Fbjc.2014.45\nCatalano, 2015, A novel leptin antagonist peptide inhibits breast cancer growth in vitro and in vivo, J. Cell. Mol. Med., 19, 1122, 10.1111\u002Fjcmm.12517\nZou, 2016, Leptin promotes proliferation and metastasis of human gallbladder cancer through OB-Rb leptin receptor, Int. J. Oncol., 49, 197, 10.3892\u002Fijo.2016.3530\nYunusova, 2015, Serum adipokines and their receptors in endometrial and colon cancer patients: relationship with tumor invasion and metastasis, Vopr. Onkol., 61, 619\nHealy, 2012, Metabolic syndrome and leptin are associated with adverse pathological features in male colorectal cancer patients, Colorectal Dis., 14, 157, 10.1111\u002Fj.1463-1318.2011.02562.x\nWang, 2012, Leptin regulates proliferation and apoptosis of colorectal carcinoma through PI3 K\u002FAkt\u002FmTOR signalling pathway, J. Biosci., 37, 91, 10.1007\u002Fs12038-011-9172-4\nLiu, 2011, Expression and biological significance of leptin, leptin receptor, VEGF, and CD34 in colorectal carcinoma, Cell Biochem. Biophys., 60, 241, 10.1007\u002Fs12013-010-9145-5\nRatke, 2010, Leptin stimulates the migration of colon carcinoma cells by multiple signaling pathways, Endocr. Relat. Cancer, 17, 179, 10.1677\u002FERC-09-0225\nErkasap, 2013, Leptin receptor (Ob-R) mRNA expression and serum leptin concentration in patients with colorectal and metastatic colorectal cancer, Braz. J. Med. Biol. Res., 46, 306, 10.1590\u002F1414-431X20122559\nFan, 2015, Leptin signaling enhances cell invasion and promotes the metastasis of human pancreatic cancer via increasing MMP-13 production, Oncotarget, 6, 16120, 10.18632\u002Foncotarget.3878\nRen, 2014, Hypoxia inducible factor (HIF)-1α directly activates leptin receptor (Ob-R) in pancreatic cancer cells, Cancer Lett., 354, 172, 10.1016\u002Fj.canlet.2014.08.001\nMasoud, 2015, HIF-1α pathway: role, regulation and intervention for cancer therapy, Acta Pharm, Sin. B, 5, 378\nSchmid, 2015, Adiposity and risk of thyroid cancer: a systematic review and meta-analysis, Obes. Rev., 16, 1042, 10.1111\u002Fobr.12321\nPappa, 2014, Obesity and thyroid cancer: a clinical update, Thyroid, 24, 190, 10.1089\u002Fthy.2013.0232\nFan, 2015, Expression of leptin and its receptor in thyroid carcinoma: distinctive prognostic significance in different subtypes, Clin. Endocrinol. (Oxf.), 83, 261, 10.1111\u002Fcen.12598\nZhang, 2013, Clinicopathological implications of leptin and leptin receptor expression in papillary thyroid cancer, Oncol. Lett., 5, 797, 10.3892\u002Fol.2013.1125\nCheng, 2010, Clinicopathologic significance of leptin and leptin receptor expressions in papillary thyroid carcinoma, Surgery, 147, 847, 10.1016\u002Fj.surg.2009.11.004\nUddin, 2010, Leptin-R and its association with PI3 K\u002FAKT signaling pathway in papillary thyroid carcinoma, Endocr. Relat. Cancer, 17, 191, 10.1677\u002FERC-09-0153\nCheng, 2011, Leptin enhances migration of human papillary thyroid cancer cells through the PI3 K\u002FAKT and MEK\u002FERK signaling pathways, Oncol. Rep., 26, 1265\nZhang, 2014, Correlation analysis between the expressions of leptin and its receptor (ObR) and clinicopathology in endometrial cancer, Cancer Biomark., 14, 353, 10.3233\u002FCBM-140415\nGui, 2017, The association between obesity related adipokines and risk of breast cancer: a systematic review and meta-analysis, Oncotarget, 8, 75389, 10.18632\u002Foncotarget.17853\nEngin, 2017, Obesity-associated breast cancer: analysis of risk factors, Adv. Exp. Med. Biol., 960, 571, 10.1007\u002F978-3-319-48382-5_25\nMadeddu, 2014, Role of inflammation and oxidative stress in post-menopausal oestrogen-dependent breast cancer, J. Cell. Mol. Med., 18, 2519, 10.1111\u002Fjcmm.12413\nAssiri, 2015, Resistin, visfatin, adiponectin, and leptin: risk of breast cancer in pre- and postmenopausal Saudi females and their possible diagnostic and predictive implications as novel biomarkers, Dis. Markers, 2015, 253519, 10.1155\u002F2015\u002F253519\nHou, 2007, Adipocytokines and breast cancer risk, Chin. Med. J. (Engl.), 120, 1592, 10.1097\u002F00029330-200709020-00009\nChen, 2006, Serum adiponectin and leptin levels in Taiwanese breast cancer patients, Cancer Lett., 237, 109, 10.1016\u002Fj.canlet.2005.05.047\nGrossmann, 2010, Obesity and breast cancer: status of leptin and adiponectin in pathological processes, Cancer Metastasis Rev., 29, 641, 10.1007\u002Fs10555-010-9252-1\nIshikawa, 2004, Enhanced expression of leptin and leptin receptor (OB-R) in human breast cancer, Clin. Cancer Res., 10, 4325, 10.1158\u002F1078-0432.CCR-03-0749\nXia, 2009, Overexpression of leptin and leptin receptors in breast cancer positively correlates with clinicopathological features, Chin. Med. J. (Engl.), 122, 3078\nAlshaker, 2014, Leptin induces upregulation of sphingosine kinase 1 in oestrogen receptor-negative breast cancer via Src family kinase-mediated, janus kinase 2-independent pathway, Breast Cancer Res., 16, 426, 10.1186\u002Fs13058-014-0426-6\nPark, 2010, Leptin receptor signaling supports cancer cell metabolism through suppression of mitochondrial respiration in vivo, Am. J. Pathol., 177, 3133, 10.2353\u002Fajpath.2010.100595\nGuo, 2011, Notch, IL-1 and leptin crosstalk outcome (NILCO) is critical for leptin-induced proliferation, migration and VEGF\u002FVEGFR-2 expression in breast cancer, PLoS One, 6, e21467, 10.1371\u002Fjournal.pone.0021467\nMcMurtry, 2009, Leptin utilizes Jun N-terminal kinases to stimulate the invasion of MCF-7 breast cancer cells, Clin. Exp. Metastasis, 26, 197, 10.1007\u002Fs10585-008-9231-x\nLi, 2016, Leptin promotes breast cancer cell migration and invasion via IL-18 expression and secretion, Int. J. Oncol., 48, 2479, 10.3892\u002Fijo.2016.3483\nZhang, 2015, Regulation of epithelial-mesenchymal transition by tumor-associated macrophages in cancer, Am. J. Transl. Res., 7, 1699\nBonde, 2012, Intratumoral macrophages contribute to epithelial-mesenchymal transition in solid tumors, BMC Cancer, 12, 35, 10.1186\u002F1471-2407-12-35\nYang, 2016, Macrophage phenotypic subtypes diametrically regulate epithelial-mesenchymal plasticity in breast cancer cells, BMC Cancer, 16, 419, 10.1186\u002Fs12885-016-2411-1\nCao, 2016, Leptin promotes migration and invasion of breast cancer cells by stimulating IL-8 production in M2 macrophages, Oncotarget, 7, 65441, 10.18632\u002Foncotarget.11761\nTempleton, 2015, Breast cancer cell colonization of the human bone marrow adipose tissue niche, Neoplasia, 17, 849, 10.1016\u002Fj.neo.2015.11.005\nPerera, 2008, Leptin-regulated gene expression in MCF-7 breast cancer cells: mechanistic insights into leptin-regulated mammary tumor growth and progression, J. Endocrinol., 199, 221, 10.1677\u002FJOE-08-0215\nSaxena, 2008, Bidirectional crosstalk between leptin and insulin-like growth factor-I signaling promotes invasion and migration of breast cancer cells via transactivation of epidermal growth factor receptor, Cancer Res., 68, 9712, 10.1158\u002F0008-5472.CAN-08-1952\nHuang, 2011, Leptin increases motility and integrin up-regulation in human prostate cancer cells, J. Cell. Physiol., 226, 1274, 10.1002\u002Fjcp.22455\nYang, 2009, Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor, Carcinogenesis, 30, 566, 10.1093\u002Fcarcin\u002Fbgp023\nLiu, 2008, Integrin alpha(v)beta(3)-targeted cancer therapy, Drug Dev. Res., 69, 329, 10.1002\u002Fddr.20265\nGrossmann, 2009, Role of the adiponectin leptin ratio in prostate cancer, Oncol. Res., 18, 269, 10.3727\u002F096504009X12596189659367\nHoriguchi, 2006, Increased serum leptin levels and over expression of leptin receptors are associated with the invasion and progression of renal cell carcinoma, J. Urol., 176, 1631, 10.1016\u002Fj.juro.2006.06.039\nOba, 2016, Elevated serum leptin levels are associated with an increased risk of sentinel lymph node metastasis in cutaneous melanoma, Medicine (Baltimore), 95, e3073, 10.1097\u002FMD.0000000000003073\nClement, 2017, Obesity and melanoma: could fat be fueling malignancy?, Pigment Cell Melanoma Res., 30, 294, 10.1111\u002Fpcmr.12584\nFont-Clos, 2017, Integrative analysis of pathway deregulation in obesity, N. P. J. Syst. Biol. Appl., 3, 18, 10.1038\u002Fs41540-017-0018-z\nMalvi, 2015, Obesity induced rapid melanoma progression is reversed by orlistat treatment and dietary intervention: role of adipokines, Mol. Oncol., 9, 689, 10.1016\u002Fj.molonc.2014.11.006\nQi, 2014, Type 2 diabetes mellitus and risk of malignant melanoma: a systematic review and meta-analysis of cohort studies, Iran. J. Public Health, 43, 857\nTorisu-Itakura, 2007, Molecular characterization of inflammatory genes in sentinel and nonsentinel nodes in melanoma, Clin. Cancer Res., 13, 3125, 10.1158\u002F1078-0432.CCR-06-2645\nXu, 2011, Expression and clinical significance of leptin, the functional receptor of leptin (OB-Rb) and HER-2 in non-small-cell lung cancer: a retrospective analysis, J. Cancer Res Clin. Oncol., 137, 1841, 10.1007\u002Fs00432-011-1054-5\nYan, 2010, Effects of dietary fat on spontaneous metastasis of Lewis lung carcinoma in mice, Clin. Exp. Metastasis., 27, 581, 10.1007\u002Fs10585-010-9347-7\nBarrichon, 2015, Dose-dependent biphasic leptin-induced proliferation is caused by non-specific IL-6\u002FNF-(B pathway activation in human myometrial cells, Br. J. Pharmacol., 172, 2974, 10.1111\u002Fbph.13100\nFazolini, 2015, Leptin activation of mTOR pathway in intestinal epithelial cell triggers lipid droplet formation, cytokine production and increased cell proliferation, Cell Cycle, 14, 2667, 10.1080\u002F15384101.2015.1041684\nBlanquer-Rosselló Mdel, 2016, Leptin regulates energy metabolism in MCF-7 breast cancer cells, Int. J. Biochem. Cell Biol., 72, 18, 10.1016\u002Fj.biocel.2016.01.002\nChen, 2013, Leptin stimulates ovarian cancer cell growth and inhibits apoptosis by increasing cyclin D1 and Mcl-1 expression via the activation of the MEK\u002FERK1\u002F2 and PI3 K\u002FAkt signaling pathways, Int. J. Oncol., 42, 1113, 10.3892\u002Fijo.2013.1789\nChin, 2017, Leptin OB3 peptide suppresses leptin-induced signaling and progression in ovarian cancer cells, J. Biomed. Sci., 24, 51, 10.1186\u002Fs12929-017-0356-6\nDubois, 2014, Leptin induces a proliferative response in breast cancer cells but not in normal breast cells, Nutr. Cancer, 66, 645, 10.1080\u002F01635581.2014.894104\nHabib, 2015, Leptin influences estrogen metabolism and accelerates prostate cell proliferation, Life Sci., 121, 10, 10.1016\u002Fj.lfs.2014.11.007\nHarbuzariu, 2017, Leptin-Notch signaling axis is involved in pancreatic cancer progression, Oncotarget, 8, 7740, 10.18632\u002Foncotarget.13946\nKim, 2017, Leptin induces CREB-dependent aromatase activation through COX-2 expression in breast cancer cells, Food Chem Toxicol., 106, 232, 10.1016\u002Fj.fct.2017.05.058\nLiu, 2013, Leptin promotes human endometrial carcinoma cell proliferation by enhancing aromatase (P450arom) expression and estradiol formation, Eur. J. Obstet. Gynecol. Reprod. Biol., 170, 198, 10.1016\u002Fj.ejogrb.2013.04.004\nNepal, 2015, Autophagy induction by leptin contributes to suppression of apoptosis in cancer cells and xenograft model: involvement of p53\u002FFoxO3A axis, Oncotarget, 6, 7166, 10.18632\u002Foncotarget.3347\nPtak, 2013, Leptin stimulation of cell cycle and inhibition of apoptosis gene and protein expression in OVCAR-3 ovarian cancer cells, Endocrine, 43, 394, 10.1007\u002Fs12020-012-9788-7\nQian, 2015, ObRb downregulation increases breast cancer cell sensitivity to tamoxifen, Tumour Biol., 36, 6813, 10.1007\u002Fs13277-015-3375-5\nShouman, 2016, Leptin influences estrogen metabolism and increases DNA adduct formation in breast cancer cells, Cancer Biol. Med., 13, 505, 10.20892\u002Fj.issn.2095-3941.2016.0079\nXu, 2013, The upregulation of signal transducer and activator of transcription 5-dependent microRNA-182 and microRNA-96 promotes ovarian cancer cell proliferation by targeting forkhead box O3 upon leptin stimulation, Int. J. Biochem. Cell Biol., 45, 536, 10.1016\u002Fj.biocel.2012.12.010\nYoon, 2014, Leptin-induced adhesion and invasion in colorectal cancer cell lines, Oncol. Rep., 31, 2493, 10.3892\u002For.2014.3128\nYu, 2016, Adipocytes secreted leptin is a pro-tumor factor for survival of multiple myeloma under chemotherapy, Oncotarget, 7, 86075, 10.18632\u002Foncotarget.13342\nZhou, 2015, Leptin inhibits the apoptosis of endometrial carcinoma cells through activation of the nuclear factor κB-inducing kinase\u002FIκB kinase pathway, Int. J. Gynecol. Cancer, 25, 770, 10.1097\u002FIGC.0000000000000440\nValladares, 2014, Association between obesity and ovarian cancer, Rev. Med. Chil., 142, 593, 10.4067\u002FS0034-98872014000500007\nYuan, 2013, Leptin induces cell proliferation and reduces cell apoptosis by activating c-myc in cervical cancer, Oncol. Rep., 29, 2291, 10.3892\u002For.2013.2390\nShen, 2009, Leptin promotes the immune escape of lung cancer by inducing proinflammatory cytokines and resistance to apoptosis, Mol. Med. Rep., 2, 295\nGonzalez-Perez, 2013, Leptin's pro-angiogenic signature in breast cancer, Cancers (Basel), 5, 1140, 10.3390\u002Fcancers5031140\nRibatti, 2008, Leptin-leptin receptor are involved in angiogenesis in human hepatocellular carcinoma, Peptides, 29, 1596, 10.1016\u002Fj.peptides.2008.05.011\nWicki, 2008, The angiogenic switch in tumorigenesis, 67\nHunter, 2008, Mechanisms of metastasis, Breast Cancer Res., 10, S2, 10.1186\u002Fbcr1988\nBloomfield, 2016, Inherent variability of cancer-specific aneuploidy generates metastases, Mol. Cytogenet., 9, 90, 10.1186\u002Fs13039-016-0297-x\nCaswell, 2017, The role of tumour heterogeneity and clonal cooperativity in metastasis, immune evasion and clinical outcome, BMC. Med., 15, 133, 10.1186\u002Fs12916-017-0900-y\nYang, 2017, Intratumor heterogeneity predicts metastasis of triple-negative breast cancer, Carcinogenesis, 38, 900, 10.1093\u002Fcarcin\u002Fbgx071\nWerner, 2017, Epigenetics and precision oncology, Cancer J., 23, 262, 10.1097\u002FPPO.0000000000000281\nEll, 2013, Transcriptional control of cancer metastasis, Trends Cell Biol., 23, 603, 10.1016\u002Fj.tcb.2013.06.001\nBochukova, 2010, Large, rare chromosomal deletions associated with severe early-onset obesity, Nature, 463, 666, 10.1038\u002Fnature08689\nUriarte, 2013, Shifting to a control diet after a high-fat, high-sucrose diet intake induces epigenetic changes in retroperitoneal adipocytes of Wistar rats, J. Physiol. Biochem., 69, 601, 10.1007\u002Fs13105-012-0231-6\nPokrywka, 2014, DNA methylation in obesity, Postepy Hig Med. Dosw. (Online), 68, 1383, 10.5604\u002F17322693.1130084\nHair, 2015, Body mass index associated with genome-wide methylation in breast tissue, Breast Cancer Res. Treat., 151, 453, 10.1007\u002Fs10549-015-3401-8\nDel Carmen Martínez-Jiménez, 2017, miRNAs in nutrition, obesity, and cancer: the biology of miRNAs in metabolic disorders and its relationship with cancer development, Mol. Nutr. Food Res.\nCrujeiras, 2015, Leptin resistance in obesity: an epigenetic landscape, Life Sci., 140, 57, 10.1016\u002Fj.lfs.2015.05.003\nYan, 2013, Metastasis suppressor genes, Histol. Histopathol., 28, 285\nBruno, 2005, Apoptotic pathways are inhibited by leptin receptor activation in neutrophils, J. Immunol., 174, 8090, 10.4049\u002Fjimmunol.174.12.8090\nHajagos-Tóth, 2017, Obesity in pregnancy: a novel concept on the roles of adipokines in uterine contractility, Croat. Med. J., 58, 96, 10.3325\u002Fcmj.2017.58.96\nBlouet, 2012, TXNIP in Agrp neurons regulates adiposity, energy expenditure, and central leptin sensitivity, J. Neurosci., 32, 9870, 10.1523\u002FJNEUROSCI.0353-12.2012\nPachmayr, 2017, Underlying mechanisms for distant metastasis − Molecular biology, Visc. Med., 33, 11, 10.1159\u002F000454696\nDing, 2016, APPL1-mediating leptin signaling contributes to proliferation and migration of cancer cells, PLoS One, 11, e0166172, 10.1371\u002Fjournal.pone.0166172\nFava, 2008, Leptin enhances cholangiocarcinoma cell growth, Cancer Res., 68, 6752, 10.1158\u002F0008-5472.CAN-07-6682\nFrankenberry, 2004, Leptin induces cell migration and the expression of growth factors in human prostate cancer cells, Am. J. Surg., 188, 560, 10.1016\u002Fj.amjsurg.2004.07.031\nGhasemi, 2017, RhoA\u002FROCK pathway mediates leptin-induced uPA expression to promote cell invasion in ovarian cancer cells, Cell. Signal., 32, 104, 10.1016\u002Fj.cellsig.2017.01.020\nGhasemi, 2017, Leptin induces matrix metalloproteinase 7 expression to promote ovarian cancer cell invasion by activating ERK and JNK pathways, J. Cell Biochem\nHuang, 2017, Leptin promotes the migration and invasion of breast cancer cells by upregulating ACAT2, Cell. Oncol (Dordr.), 10.1007\u002Fs13402-017-0342-8\nKnight, 2011, Survivin upregulation, dependent on leptin-EGFR-Notch1 axis, is essential for leptin-induced migration of breast carcinoma cells, Endocr. Relat. Cancer, 18, 413, 10.1530\u002FERC-11-0075\nMartín, 2017, A dangerous liaison: leptin and sPLA2-IIA join forces to induce proliferation and migration of astrocytoma cells, PLoS One, 12, e0170675, 10.1371\u002Fjournal.pone.0170675\nMendonsa, 2015, Modulation of the leptin receptor mediates tumor growth and migration of pancreatic cancer cells, PLoS One, 10, e0126686, 10.1371\u002Fjournal.pone.0126686\nMishra, 2017, Leptin signals via TGFB1 to promote metastatic potential and stemness in breast cancer, PLoS One, 12, e0178454, 10.1371\u002Fjournal.pone.0178454\nNoda, 2015, Long term exposure to leptin enhances the growth of prostate cancer cells, Int. J. Oncol., 46, 1535, 10.3892\u002Fijo.2015.2845\nSaxena, 2007, Concomitant activation of the JAK\u002FSTAT, PI3 K\u002FAKT, and ERK signaling is involved in leptin-mediated promotion of invasion and migration of hepatocellular carcinoma cells, Cancer Res., 67, 2497, 10.1158\u002F0008-5472.CAN-06-3075\nSobrinho Santos, 2017, Leptin acts on neoplastic behavior and expression levels of genes related to hypoxia, angiogenesis, and invasiveness in oral squamous cell carcinoma, Tumor Biol., 39, 10.1177\u002F1010428317699130\nWang, 2013, The effect of leptin and its mechanisms on the migration and invasion of human breast cancer MCF-7 cells, Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi (Chinese Journal of Cellular and Molecular Immunology), 29, 1272\nWei, 2016, Leptin promotes epithelial-mesenchymal transition of breast cancer via the upregulation of pyruvate kinase M2, J. Exp. Clin. Cancer Res., 35, 166, 10.1186\u002Fs13046-016-0446-4\nYeh, 2009, Leptin induces migration and invasion of glioma cells through MMP-13 production, Glia, 57, 454, 10.1002\u002Fglia.20773\nYuan, 2014, Leptin promotes the proliferation and migration of human breast cancer through the extracellular-signal regulated kinase pathway, Mol. Med. Rep., 9, 350, 10.3892\u002Fmmr.2013.1786\nRabold, 2017, Cellular metabolism of tumor-associated macrophages − functional impact and consequences, FEBS. Lett., 591, 3022, 10.1002\u002F1873-3468.12771\nZhao, 2017, Prognostic significance of tumor-associated macrophages in breast cancer: a meta-analysis of the literature, Oncotarget, 8, 30576, 10.18632\u002Foncotarget.15736\nYuan, 2017, Prognostic significance of tumor-associated macrophages in ovarian cancer: a meta-analysis, Gynecol. Oncol., 147, 181, 10.1016\u002Fj.ygyno.2017.07.007\nSousa, 2016, The role of tumour-associated macrophages in bone metastasis, J. Bone Oncol., 5, 135, 10.1016\u002Fj.jbo.2016.03.004\nRhee, 2016, Diverse macrophages polarization in tumor microenvironment, Arch. Pharm. Res., 39, 1588, 10.1007\u002Fs12272-016-0820-y\nBraune, 2017, IL-6 regulates M2 polarization and local proliferation of adipose tissue macrophages in obesity, J. Immunol., 198, 2927, 10.4049\u002Fjimmunol.1600476\nJung, 2015, High-fat diet-induced obesity increases lymphangiogenesis and lymph node metastasis in the B16F10 melanoma allograft model: roles of adipocytes and M2-macrophages, Int. J. Cancer, 136, 258, 10.1002\u002Fijc.28983\nAcedo, 2013, Participation of leptin in the determination of the macrophage phenotype: an additional role in adipocyte and macrophage crosstalk, In Vitro Cell. Dev. Biol. Anim., 49, 473, 10.1007\u002Fs11626-013-9629-x\nSeyfried, 2013, On the origin of cancer metastasis, Crit. Rev. Oncog., 18, 43, 10.1615\u002FCritRevOncog.v18.i1-2.40\nClawson, 2017, Stealth dissemination of macrophage-tumor cell fusions cultured from blood of patients with pancreatic ductal adenocarcinoma, PLoS One, 12, e0184451, 10.1371\u002Fjournal.pone.0184451\nDing, 2012, Tumor associated macrophage × cancer cell hybrids may acquire cancer stem cell properties in breast cancer, PLoS One, 7, e41942, 10.1371\u002Fjournal.pone.0041942\nPawlina, 2016\nChapnik, 2013, A superactive leptin antagonist alters metabolism and locomotion in high-leptin mice, J. Endocrinol., 217, 283, 10.1530\u002FJOE-13-0033\nMacht, 2017, Leptin resistance elicits depressive-like behaviors in rats, Brain Behav. Immun., 60, 151, 10.1016\u002Fj.bbi.2016.10.008\nSøgaard, 2013, The impact of comorbidity on cancer survival: a review, Clin. Epidemiol., 5, S3, 10.2147\u002FCLEP.S47150\nCheung, 2014, A pegylated leptin antagonist ameliorates CKD-associated cachexia in mice, J. Am. 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1996, Targeted disruption of TRAF3 leads to postnatal lethality and defective T-dependent immune responses, Immunity, 5, 407, 10.1016\u002FS1074-7613(00)80497-5\nXie, 2007, TRAF3 is a critical regulator of B cell homeostasis in secondary lymphoid organs, Immunity, 27, 253, 10.1016\u002Fj.immuni.2007.07.012\nGardam, 2008, TRAF2 and TRAF3 signal adapters act cooperatively to control the maturation and survival signals delivered to B cells by the BAFF receptor, Immunity, 28, 391, 10.1016\u002Fj.immuni.2008.01.009\nHildebrand, 2011, Roles of TRAF3 and TRAF5 in immune cell function, Immunol Rev, 244, 55, 10.1111\u002Fj.1600-065X.2011.01055.x\nMackay, 2003, BAFF AND APRIL: a tutorial on B cell survival, Annu Rev Immunol, 21, 231, 10.1146\u002Fannurev.immunol.21.120601.141152\nWeih, 2001, Essential role of RelB in germinal center and MZ formation and proper expression of homing chemokines, J Immunol, 167, 1909, 10.4049\u002Fjimmunol.167.4.1909\nFranzoso, 1998, Mice deficient in NF-κB\u002Fp52 present with defects in humoral responses, GC reactions, and splenic microarchitecture, J Exp Med, 187, 147, 10.1084\u002Fjem.187.2.147\nXie, 2011, TRAF3 is required for T cell-mediated immunity and TCR\u002FCD28 signaling, J Immunol, 186, 143, 10.4049\u002Fjimmunol.1000290\nKeats, 2007, Promiscuous mutations activate the noncanonical NF-κB pathway in MM, Cancer Cell, 12, 131, 10.1016\u002Fj.ccr.2007.07.003\nAnnunziata, 2007, Frequent engagement of the classical and alternative NF-κB pathways by diverse genetic abnormalities in multiple myeloma, Cancer Cell, 12, 115, 10.1016\u002Fj.ccr.2007.07.004\nOtto, 2012, Genetic lesions of the TRAF3 and MAP3K14 genes in classical Hodgkin lymphoma, Br J Haematol, 157, 702, 10.1111\u002Fj.1365-2141.2012.09113.x\nNagel, 2009, Biallelic inactivation of TRAF3 in a subset of B-cell lymphomas with interstitial del(14)(q24.1q32.33), Leukemia, 23, 2153, 10.1038\u002Fleu.2009.149\nMoore, 2012, Specific deletion of TRAF3 in B lymphocytes leads to B-lymphoma development in mice, Leukemia, 26, 1122, 10.1038\u002Fleu.2011.309\nHu, 1994, A novel RING finger protein interacts with the cytoplasmic domain of CD40, J Biol Chem, 269, 30069, 10.1016\u002FS0021-9258(18)43772-6\nCheng, 1995, Involvement of CRAF1, a relative of TRAF, in CD40 signaling, Science, 267, 1494, 10.1126\u002Fscience.7533327\nHostager, 1999, Cutting edge: contrasting roles of TRAF2 and TRAF3 in CD40-mediated B lymphocyte activation, J Immunol, 162, 6307, 10.4049\u002Fjimmunol.162.11.6307\nPullen, 1998, CD40-TRAF interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization, Biochemistry, 37, 11836, 10.1021\u002Fbi981067q\nHostager, 2003, TRAF2-deficient B lymphocytes reveal novel roles for TRAF2 in CD40 signaling, J Biol Chem, 278, 45382, 10.1074\u002Fjbc.M306708200\nHaxhinasto, 2003, A novel interaction between PKD and TRAFs regulates BCR-CD40 synergy, J Immunol, 171, 4655, 10.4049\u002Fjimmunol.171.9.4655\nXie, 2004, Requirement for TRAF3 in signaling by LMP1, but not CD40, in B lymphocytes, J Exp Med, 199, 661, 10.1084\u002Fjem.20031255\nBishop, 2001, Signaling by CD40 and its mimics in B cell activation, Immunol Res, 24, 97, 10.1385\u002FIR:24:2:097\nGraham, 2010, Differential B lymphocyte regulation by CD40 and its viral mimic, LMP1, Immunol Rev, 237, 226, 10.1111\u002Fj.1600-065X.2010.00932.x\nBishop, 2002, Mechanisms of TRAF regulation in B lymphocytes, J Leukoc Biol, 72, 19, 10.1189\u002Fjlb.72.1.19\nSoni, 2007, LMP1 TRAFficking activates growth and survival pathways, Adv Exp Med Biol, 597, 173, 10.1007\u002F978-0-387-70630-6_14\nArcipowski, 2011, Molecular mechanisms of TRAF6 utilization by the oncogenic viral mimic of CD40, LMP1, J Biol Chem, 286, 9948, 10.1074\u002Fjbc.M110.185983\nKraus, 2009, TRAF5 is a critical mediator of in vitro signals and in vivo functions of LMP1, the viral oncogenic mimic of CD40, Proc Natl Acad Sci USA, 106, 17140, 10.1073\u002Fpnas.0903786106\nWu, 2005, LMP1 protein from EBV is a structural decoy in B lymphocytes for binding to TRAF3, J Biol Chem, 280, 33620, 10.1074\u002Fjbc.M502511200\nArdila-Osorio, 1999, Evidence of LMP1–TRAF3 interactions in glycosphingolipid-rich complexes of lymphoblastoid and nasopharyngeal carcinoma cells, Int J Cancer, 81, 645, 10.1002\u002F(SICI)1097-0215(19990517)81:4\u003C645::AID-IJC22>3.0.CO;2-0\nHostager, 2000, Recruitment of CD40, TRAF2 and TRAF3 to membrane microdomains during CD40 signaling, J Biol Chem, 275, 15392, 10.1074\u002Fjbc.M909520199\nKaykas, 2001, CD40 and LMP-1 both signal from lipid rafts but LMP-1 assembles a distinct, more efficient signaling complex, EMBO J, 20, 2641, 10.1093\u002Femboj\u002F20.11.2641\nBrown, 2001, Differential signaling and TRAF degradation by CD40 and the EBV oncoprotein LMP1, J Exp Med, 193, 943, 10.1084\u002Fjem.193.8.943\nMoore, 2005, Differential regulation of CD40-mediated TRAF degradation in B lymphocytes, J Immunol, 175, 3780, 10.4049\u002Fjimmunol.175.6.3780\nYe, 1999, The structural basis for the recognition of diverse receptor sequences by TRAF2, Mol Cell, 4, 321, 10.1016\u002FS1097-2765(00)80334-2\nGraham, 2009, Roles of the TRAF2\u002F3 binding site in differential B cell signaling by CD40 and its oncogenic mimic, LMP1, J Immunol, 183, 2966, 10.4049\u002Fjimmunol.0900442\nPeters, 2008, A novel polymorphism of the human CD40 receptor with enhanced function, Blood, 112, 1863, 10.1182\u002Fblood-2008-02-138925\nPeters, 2010, Differential TRAF3 utilization by a variant human CD40 receptor with enhanced signaling, J Immunol, 185, 6555, 10.4049\u002Fjimmunol.1000135\nKhare, 2001, The role of TALL-1 and APRIL in immune regulation, Trends Immunol, 22, 61, 10.1016\u002FS1471-4906(00)01843-3\nDo, 2002, Mechanisms of BLyS action in B cell immunity, Cytokine Growth Factor Rev, 13, 19, 10.1016\u002FS1359-6101(01)00025-9\nCancro, 2004, The BLyS family of ligands and receptors: an archetype for niche-specific homeostatic regulation, Immunol Rev, 202, 237, 10.1111\u002Fj.0105-2896.2004.00212.x\nXu, 2002, TRAF3 is associated with BAFF-R and negatively regulates BAFF-R-mediated NF-kB activation and IL-10 production, J Immunol, 169, 6883, 10.4049\u002Fjimmunol.169.12.6883\nMorrison, 2005, An atypical TRAF binding motif of BAFFR mediates induction of the noncanonical NF-κB signaling pathway, J Biol Chem, 280, 10018, 10.1074\u002Fjbc.M413634200\nHatzoglou, 2000, TNF receptor family member BCMA associates with TRAF1, TRAF2, and TRAF3 and activates NF-κB, elk-1, JNK, and p38 MAPK, J Immunol, 165, 1322, 10.4049\u002Fjimmunol.165.3.1322\nShu, 2000, B cell maturation protein is a receptor for the TNF family member TALL-1, Proc Natl Acad Sci USA, 97, 9156, 10.1073\u002Fpnas.160213497\nXia, 2000, TACI is a TRAF-interacting receptor for TALL-1, a TNF family member involved in B cell regulation, J Exp Med, 192, 137, 10.1084\u002Fjem.192.1.137\nHildebrand, 2010, A BAFF-R mutation associated with Non-Hodgkin's lymphoma exhibits altered TRAF association and reveals new insights into proximal BAFF-R signaling, J Exp Med, 207, 2569, 10.1084\u002Fjem.20100857\nLiao, 2004, Regulation of NIK by TRAF3-induced degradation, J Biol Chem, 279, 26243, 10.1074\u002Fjbc.M403286200\nLin, 2013, A complex relationship between TRAF3 and non-canonical NF-κB activation in B lymphocytes, Front Immunol, 4, 10.3389\u002Ffimmu.2013.00477\nQian, 2004, Act1, a negative regulator in CD40 and BAFF-mediated B cell survival, Immunity, 21, 575, 10.1016\u002Fj.immuni.2004.09.001\nClaudio, 2009, The adaptor protein CIKS\u002FAct1 is essential for IL-25-mediated allergic airway inflammation, J Immunol, 182, 1617, 10.4049\u002Fjimmunol.182.3.1617\nQian, 2007, The adaptor Act1 is required for IL-17-dependent signaling associated with autoimmune and inflammatory disease, Nat Immunol, 8, 247, 10.1038\u002Fni1439\nChang, 2006, Act1 adaptor protein is an immediate and essential signaling component of IL-17R, J Biol Chem, 281, 35603, 10.1074\u002Fjbc.C600256200\nZhu, 2010, Modulation of EAE through TRAF3-mediated suppression of IL-17 receptor signaling, J Exp Med, 207, 2647, 10.1084\u002Fjem.20100703\nHauer, 2005, TRAF3 serves as an inhibitor of TRAF2\u002F5-mediated activation of the noncanonical NF-κB pathway by TRAF-binding TNFRs, Proc Natl Acad Sci USA, 102, 2874, 10.1073\u002Fpnas.0500187102\nRothe, 1995, The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins, Cell, 83, 1243, 10.1016\u002F0092-8674(95)90149-3\nMunroe, 2004, Role of TRAF2 in distinct and overlapping CD40 and TNFR2\u002FCD120b-mediated B lymphocyte activation, J Biol Chem, 279, 53222, 10.1074\u002Fjbc.M410539200\nHostager, 2002, Role of TRAF2 in the activation of IgM secretion by CD40 and CD120b, J Immunol, 168, 3318, 10.4049\u002Fjimmunol.168.7.3318\nPeng, 2005, Signaling to B cells by TLRs, Curr Opin Immunol, 17, 230, 10.1016\u002Fj.coi.2005.03.003\nFillatreau, 2011, Novel regulatory functions for TLR-activated B cells during intracellular bacterial infection, Immunol Rev, 240, 52, 10.1111\u002Fj.1600-065X.2010.00991.x\nGreen, 2011, TLR driven B cell activation in the induction of systemic autoimmunity, Semin Immunol, 23, 106, 10.1016\u002Fj.smim.2011.01.016\nAderem, 2000, TLRs in the induction of the innate immune response, Nature, 406, 782, 10.1038\u002F35021228\nHäcker, 2006, Specificity in TLR signalling through distinct effector functions of TRAF3 and TRAF6, Nature, 439, 204, 10.1038\u002Fnature04369\nOganesyan, 2006, Critical role of TRAF3 in the TLR-dependent and independent antiviral response, Nature, 439, 208, 10.1038\u002Fnature04374\nPerkins, 2013, Reprogramming of murine macrophages through TLR2 confers viral resistance via TRAF3-mediated, enhanced interferon production, PLoS Pathog, e1003479, 10.1371\u002Fjournal.ppat.1003479\nPérez de Diego, 2010, Human TRAF3 adaptor molecule deficiency leads to impaired TLR3 response and susceptibility to Herpes simplex encephalitis, Immunity, 33, 400, 10.1016\u002Fj.immuni.2010.08.014\nXie, 2011, Enhanced TLR responses of TRAF3-deficient B lymphocytes, J Leukoc Biol, 90, 1149, 10.1189\u002Fjlb.0111044\nBuchta, 2014, TRAF5 negatively regulates TLR signaling in B lymphocytes, J Immunol, 192, 145, 10.4049\u002Fjimmunol.1301901\nSun, 2004, The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes, Mol Cell, 14, 289, 10.1016\u002FS1097-2765(04)00236-9\nXie, 2013, TRAF6 regulates TCR signaling via interaction with and modification of LAT adapter, J Immunol, 190, 4027, 10.4049\u002Fjimmunol.1202742\nYi, 2013, TRAF3 plays a key role in the development and function of iNKT cells, J Exp Med, 210, 1079, 10.1084\u002Fjem.20122135\nLee, 2001, A critical role for Dnmt1 and DNA methylation in T cell development, function, and survival, Immunity, 15, 763, 10.1016\u002FS1074-7613(01)00227-8\nTanigaki, 2004, Regulation of αβ\u002Fγδ T cell lineage commitment and peripheral T cell responses by Notch\u002FRBP-J signaling, Immunity, 20, 611, 10.1016\u002FS1074-7613(04)00109-8\nGodfrey, 2010, Raising the NKT cell family, Nat Immunol, 11, 197, 10.1038\u002Fni.1841\nBajenoff, 2002, Repeated antigen exposure is necessary for the differentiation, but not the initial proliferation, of naive CD4+ T cells, J Immunol, 168, 1723, 10.4049\u002Fjimmunol.168.4.1723\nMatsuoka, 2004, T-bet upregulation and subsequent IL-12 stimulation are essential for induction of Th1 mediated immunopathology in Crohn's disease, Gut, 53, 1303, 10.1136\u002Fgut.2003.024190\nMatsuda, 2007, Temporal dissection of T-bet functions, J Immunol, 178, 3457, 10.4049\u002Fjimmunol.178.6.3457\nTownsend, 2004, T-bet regulates the terminal maturation and homeostasis of NK and Vα14i NKT cells, Immunity, 20, 477, 10.1016\u002FS1074-7613(04)00076-7\nBennett, 2001, The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3, Nat Genet, 27, 20, 10.1038\u002F83713\nFontenot, 2003, Foxp3 programs the development and function of CD4+CD25+ regulatory T cells, Nat Immunol, 4, 330, 10.1038\u002Fni904\nKhattri, 2003, An essential role for Scurfin in CD4+CD25+ T regulatory cells, Nat Immunol, 4, 337, 10.1038\u002Fni909\nKim, 2007, Regulatory T cells prevent catastrophic autoimmunity throughout the lifespan of mice, Nat Immunol, 8, 191, 10.1038\u002Fni1428\nLahl, 2007, Selective depletion of Foxp3+ regulatory T cells induces a scurfy-like disease, J Exp Med, 204, 57, 10.1084\u002Fjem.20061852\nWortzman, 2013, The contextual role of TNFR family members in CD8+ T-cell control of viral infections, Immunol Rev, 255, 125, 10.1111\u002Fimr.12086\nMunroe, 2009, Functional roles for T cell CD40 in infection and autoimmune disese: the role of CD40 in lymphocyte homeostasis, Semin Immunol, 21, 283, 10.1016\u002Fj.smim.2009.05.008\nSo, 2012, Regulation of the PKCθ-NF-κB axis in T lymphocytes by the TNF-R family member OX40, Front Immunol, 3, 133, 10.3389\u002Ffimmu.2012.00133\nArch, 1998, 4-1BB and Ox40 are members of a TNF-R subfamily that bind TRAFs and activate NF-κB, Mol Cell Biol, 18, 558, 10.1128\u002FMCB.18.1.558\nKawamata, 1998, Activation of OX40 signal transduction pathways leads to TRAF2 and TRAF5-mediated NF-κB activation, J Biol Chem, 273, 5805, 10.1074\u002Fjbc.273.10.5808\nTakaori-Kondo, 2000, Both amino- and carboxyl-terminal domains of TRAF3 negatively regulate NF-κB activation induced by OX40 signaling, Biochem Biophys Res Commun, 272, 856, 10.1006\u002Fbbrc.2000.2860\nSong, 2004, The costimulation-regulated duration of PKB activation controls T cell longevity, Nat Immunol, 5, 150, 10.1038\u002Fni1030\nSong, 2008, Activation of NF-κB1 by OX40 contributes to antigen-driven T cell expansion and survival, J Immunol, 180, 7240, 10.4049\u002Fjimmunol.180.11.7240\nSo, 2013, Regulation of PI-3 K and Akt signaling in T lymphocytes and other cells by TNFR family molecules, Front Immunol, 4, 139, 10.3389\u002Ffimmu.2013.00139\nSo, 2008, Immune regulation and control of regulatory T cells by OX40 and 4-1BB, Cytokine Growth Factor Rev, J19, 253, 10.1016\u002Fj.cytogfr.2008.04.003\nLin, 2013, GITR-dependent regulation of 4-1BB expression: implications for T cell memory and anti-4-1BB-induced pathology, J Immunol, 190, 4627, 10.4049\u002Fjimmunol.1201854\nLee, 2003, 4-1BB cross-linking enhances the survival and cell cycle progression of CD4 T lymphocytes, Cell Immunol, 223, 143, 10.1016\u002FS0008-8749(03)00169-2\nLin, 2012, Contribution of 4-1BBL on radioresistant cells in providing survival signals through 4-1BB expressed on CD8+ memory T cells in the bone marrow, Eur J Immunol, 42, 2861, 10.1002\u002Feji.201242503\nJang, 1998, Human 4-1BB (CD137) signals are mediated by TRAF2 and activate NF-κB, Biochem Biophys Res Commun, 242, 613, 10.1006\u002Fbbrc.1997.8016\nSaoulli, 1998, CD28-independent, TRAF2-dependent costimulation of resting T cells by 4-1BB ligand, J Exp Med, 187, 1849, 10.1084\u002Fjem.187.11.1849\nMcPherson, 2012, Opposing roles for TRAF1 in the alternative versus classical NF-κB pathway in T cells, J Biol Chem, 287, 23010, 10.1074\u002Fjbc.M112.350538\nSabbagh, 2006, A critical role for TRAF1 and Bim down-regulation in CD8 memory T cell survival, Proc Natl Acad Sci USA, 103, 18703, 10.1073\u002Fpnas.0602919103\nLee, 2002, 4-1BB promotes the survival of CD8+ T lymphocytes by increasing expression of Bcl-xL and Bfl-1, J Immunol, 169, 4882, 10.4049\u002Fjimmunol.169.9.4882\nLee do, 2013, 4-1BB signaling activates the TCF-1 effector\u002Fβ-catenin pathway with delayed kinetics via ERK signaling and delayed PI3 K\u002FAKT activation to promote the proliferation of CD8+ T cells, PLoS ONE, 8, e69677, 10.1371\u002Fjournal.pone.0069677\nWare, 2009, Targeting the LIGHT–HVEM pathway, Adv Exp Med Biol, 647, 146, 10.1007\u002F978-0-387-89520-8_10\nMarsters, 1997, HVEM, a member of the TNFR family, interacts with members of the TRAF family and activates the transcription factors NF-κB and AP-1, J Biol Chem, 272, 14029, 10.1074\u002Fjbc.272.22.14029\nSoroosh, 2011, HVEM (TNFRSF14) regulates the persistence of T helper memory cell populations, J Exp Med, 208, 797, 10.1084\u002Fjem.20101562\nGurney, 1999, Identification of a new member of the TNF family and its receptor, a human ortholog of mouse GITR, Curr Biol, 9, 215, 10.1016\u002FS0960-9822(99)80093-1\nKwon, 1999, Identification of a novel activation-inducible protein of the TNFR superfamily and its ligand, J Biol Chem, 274, 6056, 10.1074\u002Fjbc.274.10.6056\nSnell, 2010, CD8 T cell-intrinsic GITR is required for T cell clonal expansion and mouse survival following severe influenza infection, J Immunol, 185, 7223, 10.4049\u002Fjimmunol.1001912\nKim, 2010, Blockade of GITR–GITRL interaction maintains Treg function to prolong allograft survival, Eur J Immunol, 40, 1369, 10.1002\u002Feji.200940046\nAizawa, 1997, TRAF5 and TRAF2 are involved in CD30-mediated NF-κB activation, J Biol Chem, 272, 2042, 10.1074\u002Fjbc.272.4.2042\nBoucher, 1997, Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other members of the TNFR superfamily, Biochem Biophys Res Commun, 233, 592, 10.1006\u002Fbbrc.1997.6509\nNishimura, 2005, A novel role of CD30\u002FCD30 ligand signaling in the generation of long-lived memory CD8+ T cells, J Immunol, 175, 4627, 10.4049\u002Fjimmunol.175.7.4627\nSun, 2010, CD30L\u002FCD30 plays a critical role in Th17 differentiation in mice, J Immunol, 185, 2222, 10.4049\u002Fjimmunol.1000024\nReynolds, 2013, TLR regulation of effector T lymphocyte function, Trends Immunol, 34, 511, 10.1016\u002Fj.it.2013.06.003\nGelman, 2004, TLR ligands directly promote activated CD4+ T cell survival, J Immunol, 172, 6065, 10.4049\u002Fjimmunol.172.10.6065\nReynolds, 2012, TLR4 signaling in T cells promotes autoimmune inflammation, Proc Natl Acad Sci USA, 109, 13064, 10.1073\u002Fpnas.1120585109\nLiu, 2007, TLRs and immune regulation: their direct and indirect modulation on regulatory CD4+CD25+ T cells, Immunology, 122, 149, 10.1111\u002Fj.1365-2567.2007.02651.x\nLoo, 2011, Immune signaling by RIG-I-like receptors, Immunity, 34, 680, 10.1016\u002Fj.immuni.2011.05.003\nNakhaei, 2009, RIG-I-like receptors: sensing and responding to RNA virus infection, Semin Immunol, 21, 215, 10.1016\u002Fj.smim.2009.05.001\nSaha, 2006, Regulation of antiviral responses by a direct and specific interaction between TRAF3 and Cardif, EMBO J, 25, 3257, 10.1038\u002Fsj.emboj.7601220\nNakhaei, 2009, The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I\u002FMAVS signaling pathway by targeting TRAF3 for degradation, PLoS Pathog, 5, e1000650, 10.1371\u002Fjournal.ppat.1000650\nSuthar, 2012, The RIG-I-like receptor LGP2 controls CD8+ T cell survival and fitness, Immunity, 37, 235, 10.1016\u002Fj.immuni.2012.07.004\nde Jong, 2010, Activation of noncanonical NF-κB signaling by the oncoprotein Tio, J Biol Chem, 285, 16495, 10.1074\u002Fjbc.M110.102848\nKatsch, 2012, Species restriction of Herpesvirus saimiri and Herpesvirus ateles: human lymphocyte transformation correlates with distinct signaling properties of viral oncoproteins, Virus Res, 165, 179, 10.1016\u002Fj.virusres.2012.02.014\nAlbrecht, 1999, Herpesvirus ateles gene product Tio interacts with nonreceptor protein tyrosine kinases, J Virol, 73, 4631, 10.1128\u002FJVI.73.6.4631-4639.1999\nHeinemann, 2006, NFκB signaling is induced by the oncoprotein Tio through direct interaction with TRAF6, J Biol Chem, 281, 8565, 10.1074\u002Fjbc.M510891200\nde Jong, 2013, Noncanonical NF-κB activation by the oncoprotein Tio occurs through a nonconserved TRAF3-binding motif, Sci Signal, 6, ra27, 10.1126\u002Fscisignal.2003309\nAlbrecht, 2005, Tyrosine phosphorylation of the Tio oncoprotein is essential for transformation of primary human T cells, J Virol, 79, 10507, 10.1128\u002FJVI.79.16.10507-10513.2005\nAbraham, 2012, HIV-1 Nef: a multifaceted modulator of TCR signaling, Cell Commun Signal, 10, 39, 10.1186\u002F1478-811X-10-39\nMangino, 2011, HIV-1 Nef induces proinflammatory state in macrophages through its acidic cluster domain: involvement of TRAF2, PLoS ONE, 6, e22982, 10.1371\u002Fjournal.pone.0022982\nMishra, 2012, HIV-1 Tat C-mediated regulation of TRAF3 by microRNA 32 in human microglia, J Neuroinflamm, 9, 131, 10.1186\u002F1742-2094-9-131\nAya, 2005, NIK controls lymphocyte and osteoclast activities in inflammatory arthritis, J Clin Invest, 115, 1848, 10.1172\u002FJCI23763\nJin, 2009, Regulation of Th17 cell differentiation and EAE induction by MAP3K NIK, Blood, 113, 6603, 10.1182\u002Fblood-2008-12-192914\nHofmann, 2011, NIK signaling in DC but not in T cells is required for the development of effector T cells and cell-mediated immune responses, J Exp Med, 208, 1917, 10.1084\u002Fjem.20110128\nBoehm, 2003, Thymic medullary epithelial cell differentiation, thymocyte emigration, and the control of autoimmunity require lympho-epithelial cross talk via LTβR, J Exp Med, 198, 757, 10.1084\u002Fjem.20030794\nZhu, 2006, NF-κB2 is required for the establishment of central tolerance through an Aire-dependent pathway, J Clin Invest, 116, 2964, 10.1172\u002FJCI28326\nElewaut, 2003, NIK-dependent RelB activation defines a unique signaling pathway for the development of Vα 14i NKT cells, J Exp Med, 197, 1623, 10.1084\u002Fjem.20030141\nSivakumar, 2003, Differential requirement for Rel\u002FNF-κB family members in NKT cell development, J Exp Med, 197, 1613, 10.1084\u002Fjem.20022234\nMurray, 2013, Cell-intrinsic role for NIK in peripheral maintenance but not thymic development of Foxp3+ regulatory T cells in mice, PLoS ONE, 8, e76216, 10.1371\u002Fjournal.pone.0076216\nVallabhapurapu, 2008, Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling, Nat Immunol, 9, 1364, 10.1038\u002Fni.1678\nZarnegar, 2008, Noncanonical NF-κB 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