PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23653049-1 2013 AIMS/HYPOTHESIS: In vitro, insulin glargine (A21Gly,B31Arg,B32Arg human insulin) has an insulin receptor (IR) profile similar to that of human insulin, but a slightly higher affinity for the IGF-1 receptor (IGF1R). Insulin Glargine 35-43 insulin receptor Homo sapiens 88-104 25697343-6 2015 In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types. Insulin Glargine 28-36 insulin receptor Homo sapiens 80-96 25697343-6 2015 In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types. Insulin Glargine 28-36 insulin receptor Homo sapiens 98-102 23653049-1 2013 AIMS/HYPOTHESIS: In vitro, insulin glargine (A21Gly,B31Arg,B32Arg human insulin) has an insulin receptor (IR) profile similar to that of human insulin, but a slightly higher affinity for the IGF-1 receptor (IGF1R). Insulin Glargine 35-43 insulin receptor Homo sapiens 106-108 23653049-6 2013 Glargine treatment resulted in phosphorylation levels of IR and Akt that were comparable with those achieved with human insulin, although delayed in time in some tissues. Insulin Glargine 0-8 insulin receptor Homo sapiens 57-59 23251042-5 2012 In this paper we have studied insulin receptor binding of lispro and glargine; the two commonly used recombinant insulins using tools of computational biology. Insulin Glargine 69-77 insulin receptor Homo sapiens 30-46 23251042-6 2012 We have observed that the binding pattern of insulin receptor (L1-CR-L2 ectodomain) with lispro and glargine is different when compared with human insulin. Insulin Glargine 100-108 insulin receptor Homo sapiens 45-61 19145584-10 2009 Furthermore, glargine induced both insulin receptor (IR) and IGF-IR phosphorylation. Insulin Glargine 13-21 insulin receptor Homo sapiens 35-56 20835859-11 2010 Dose-dependency experiments showed that insulin glargine was able to phosphorylate the IGF-IR at fivefold lower doses than those required to activate the insulin receptor. Insulin Glargine 48-56 insulin receptor Homo sapiens 154-170 20209060-3 2010 The aim of this study was to characterize the glargine metabolites in vitro with regard to their insulin receptor (IR) and IGF-1 receptor (IGF1R) binding and signaling properties as well as their metabolic and mitogenic activities. Insulin Glargine 46-54 insulin receptor Homo sapiens 97-113 20209060-3 2010 The aim of this study was to characterize the glargine metabolites in vitro with regard to their insulin receptor (IR) and IGF-1 receptor (IGF1R) binding and signaling properties as well as their metabolic and mitogenic activities. Insulin Glargine 46-54 insulin receptor Homo sapiens 115-117 20209060-8 2010 CONCLUSIONS: The binding of insulin glargine and its metabolites M1 and M2 to the IR were similar and correlated well with their corresponding autophosphorylation and metabolic activities in vitro. Insulin Glargine 36-44 insulin receptor Homo sapiens 82-84 18585815-4 2008 Regarding the metabolic signalling, glargine and insulin-induced comparable dose-dependent phosphorylation of insulin receptor, IRS-1, Akt, and GSK3, whereas detemir-induced kinetics were markedly lower in 3T3-L1 adipocytes and L6 myocytes. Insulin Glargine 36-44 insulin receptor Homo sapiens 110-126 15281015-9 2004 While binding of glargine to the insulin receptor was identical to insulin, degradation of glargine was reduced compared to insulin (16.3% +/- 0.3% v 21.6% +/- 0.4% degraded/h, P < .01). Insulin Glargine 17-25 insulin receptor Homo sapiens 33-49 18316392-7 2008 The insulin receptor was downregulated to a similar degree by glargine and regular human insulin at high insulin concentrations (P < 0.0001 for glargine, P = 0.002 for regular human insulin). Insulin Glargine 62-70 insulin receptor Homo sapiens 4-20 18316392-7 2008 The insulin receptor was downregulated to a similar degree by glargine and regular human insulin at high insulin concentrations (P < 0.0001 for glargine, P = 0.002 for regular human insulin). Insulin Glargine 147-155 insulin receptor Homo sapiens 4-20 14656737-2 2004 Structural changes in a long-acting insulin analog, insulin glargine, may change its binding properties to insulin receptor and structurally homologous receptors, such as the insulin-like growth factor-1 receptor, and thereby alter its vascular effects. Insulin Glargine 60-68 insulin receptor Homo sapiens 107-123 29874257-3 2018 METHODS: An endothelial/dendritic cell-based innate immune model was used to study antigen-presenting cell activation, cytokine secretion, and insulin receptor signalling pathways induced by originator and non-originator insulin glargine products. Insulin Glargine 229-237 insulin receptor Homo sapiens 143-159 29874257-6 2018 In studies aimed at addressing the mechanisms leading to differential cytokine production by these products, we found (1) the inflammatory response was not mediated by bacterial contaminants, (2) the innate response was driven by the native insulin receptor through the MAPK pathway, and (3) the removal of insulin glargine significantly reduced their capacity to induce innate activity. Insulin Glargine 315-323 insulin receptor Homo sapiens 241-257