PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22996137-7 2013 Though microtubule mediated actin remodeling through PKCzeta, reorganization of microtubule depended on tyrosine phosphorylation of insulin receptor, the mechanism is different from insulin-induced actin remodeling, which relied on the activity of PI3-kinase and PKCzeta. Tyrosine 104-112 insulin receptor Rattus norvegicus 132-148 22546076-5 2012 We also found that the liver mRNA, protein levels, and tyrosine phosphorylation (pY) of insulin receptor (InsR) substrate (IRS) 2, but not IRS1, were decreased in OLETF rats; pY of InsR and Akt protein and phospho-Akt (ser437) were also reduced; but protein tyrosine phosphatase-1B protein was overexpressed. Tyrosine 55-63 insulin receptor Rattus norvegicus 88-104 22546076-5 2012 We also found that the liver mRNA, protein levels, and tyrosine phosphorylation (pY) of insulin receptor (InsR) substrate (IRS) 2, but not IRS1, were decreased in OLETF rats; pY of InsR and Akt protein and phospho-Akt (ser437) were also reduced; but protein tyrosine phosphatase-1B protein was overexpressed. Tyrosine 55-63 insulin receptor Rattus norvegicus 106-110 21185755-9 2011 It also diminished insulin-stimulated tyrosine phosphorylation of IRS1 and serine phosphorylation of Akt without affecting the phosphorylation of IR, ERK1/2, p38, or JNK. Tyrosine 38-46 insulin receptor Rattus norvegicus 66-68 20801894-4 2010 In PF-fed rats, total tyrosine phosphorylation of insulin receptor (IR) in the liver induced by insulin injection was enhanced compared with 12C pair-fed rats due to an increase in IR protein level. Tyrosine 22-30 insulin receptor Rattus norvegicus 50-66 21072680-6 2011 It also diminished insulin-stimulated tyrosine phosphorylation of IRS-1, PI3K (p85), and serine phosphorylation of Akt without affecting the phosphorylation of IR, ERK1/2, P38, and JNK. Tyrosine 38-46 insulin receptor Rattus norvegicus 66-68 20801894-4 2010 In PF-fed rats, total tyrosine phosphorylation of insulin receptor (IR) in the liver induced by insulin injection was enhanced compared with 12C pair-fed rats due to an increase in IR protein level. Tyrosine 22-30 insulin receptor Rattus norvegicus 68-70 20149705-5 2010 From age two months, the following changes in liver IR protein expression were observed: (1) decreased IR-beta level in whole homogenates, but increased IR-beta levels in endosomal fractions; (2) increased IR-beta tyrosine phosphorylation; and (3) at four months, increased levels of both intact IR-beta (95 kDa) and IR-beta fragments (72 and 52 kDa) in lysosomal fractions, along with decreased stability in vivo of the IR. Tyrosine 214-222 insulin receptor Rattus norvegicus 52-54 20388825-5 2010 Ad vector infection significantly reduced total levels of the insulin receptor (IR), and insulin receptor substrates 1 and 2 (IRS-1, IRS-2) in the liver of rats, resulting in decreased insulin-induced tyrosine phosphorylation of IR, IRS-1, and IRS-2, and decreased interaction of IRS-1 and IRS-2 with phosphoinositide 3-kinase (PI3K). Tyrosine 201-209 insulin receptor Rattus norvegicus 62-78 20388825-5 2010 Ad vector infection significantly reduced total levels of the insulin receptor (IR), and insulin receptor substrates 1 and 2 (IRS-1, IRS-2) in the liver of rats, resulting in decreased insulin-induced tyrosine phosphorylation of IR, IRS-1, and IRS-2, and decreased interaction of IRS-1 and IRS-2 with phosphoinositide 3-kinase (PI3K). Tyrosine 201-209 insulin receptor Rattus norvegicus 80-82 20388825-5 2010 Ad vector infection significantly reduced total levels of the insulin receptor (IR), and insulin receptor substrates 1 and 2 (IRS-1, IRS-2) in the liver of rats, resulting in decreased insulin-induced tyrosine phosphorylation of IR, IRS-1, and IRS-2, and decreased interaction of IRS-1 and IRS-2 with phosphoinositide 3-kinase (PI3K). Tyrosine 201-209 insulin receptor Rattus norvegicus 126-128 18974235-7 2009 RESULTS: Insulin (100 nmol/L) increased tyrosine phosphorylation of insulin receptor in peritoneal mesothelial cells. Tyrosine 40-48 insulin receptor Rattus norvegicus 68-84 19543529-4 2009 Insulin induced a rapid, t(1/2)<3 min, endocytosis of the insulin receptor in parallel with receptor tyrosine autophosphorylation. Tyrosine 104-112 insulin receptor Rattus norvegicus 61-77 19543529-10 2009 CONCLUSION: It is concluded that in response to insulin stimulation the autophosphorylated insulin receptor in primary adipocytes is rapidly endocytosed in a caveolae-mediated process, involving tyrosine phosphorylation of caveolin-1. Tyrosine 195-203 insulin receptor Rattus norvegicus 91-107 19226537-4 2009 The results show that E2 decreased insulin receptor (IR) tyrosine phosphorylation, while it did not alter IR protein and mRNA content. Tyrosine 57-65 insulin receptor Rattus norvegicus 53-55 18089761-5 2008 By itself, H(2)O(2) significantly (P < 0.05) activated basal glucose transport activity, net glycogen synthesis, and glycogen synthase activity and increased phosphorylation of insulin receptor (Tyr), Akt (Ser(473)), and GSK-3beta (Ser(9)). Tyrosine 198-201 insulin receptor Rattus norvegicus 180-196 18679708-0 2009 Tyrosine phosphorylation of insulin receptor substrates during ischemia/reperfusion-induced apoptosis in rat liver. Tyrosine 0-8 insulin receptor Rattus norvegicus 28-44 18803226-7 2008 Extract of LT (T) dramatically stimulated tyrosine phosphorylation of the insulin receptor, while fraction C of LT also significantly stimulated the same. Tyrosine 42-50 insulin receptor Rattus norvegicus 74-90 17121043-1 2006 OBJECTIVE: To investigate the effects of Huanglian Jiedu decoction (HLJD) on protein expressions and tyrosine phosphorylation levels of insulin receptor (InsR) and insulin receptor substrate-1 (IRS-1) in adipose tissue of insulin resistant (IR) rats, and explore its possible molecular mechanism in improving IR. Tyrosine 101-109 insulin receptor Rattus norvegicus 136-152 18078453-3 2008 By using immunoprecipitation and immunoblotting analysis we demonstrated, in isolated rat pancreatic islets, that melatonin induces insulin growth factor receptor (IGF-R) and insulin receptor (IR) tyrosine phosphorylation and mediates the activities of the PI3K/AKT and MEK/ERKs pathways, which are involved in cell survival and growth, respectively. Tyrosine 197-205 insulin receptor Rattus norvegicus 175-191 17121043-4 2006 Fasting serum glucose and insulin were determined, and protein expressions and tyrosine phosphorylation levels of InsR and IRS-1 in adipose tissue of epididymides were detected by immunoprecipitation and Western blot. Tyrosine 79-87 insulin receptor Rattus norvegicus 114-118 17121043-5 2006 RESULTS: The protein expression of IRS-1 and the tyrosine phosphorylation levels of InsR and IRS-1 increased significantly in model rats treated with HLJD, compared with those in the untreated model rats. Tyrosine 49-57 insulin receptor Rattus norvegicus 84-88 17121043-6 2006 CONCLUSION: HLJD could increase the tyrosine phosphorylation levels of InsR and IRS-1 in adipose tissue in IR rats, which maybe one of its mechanisms in lowering blood glucose and improving insulin sensitivity of the target tissues. Tyrosine 36-44 insulin receptor Rattus norvegicus 71-75 15004002-4 2004 Insulin-stimulated tyrosine phosphorylation of IR and Ser(473) phosphorylation of Akt was not altered by unweighting. Tyrosine 19-27 insulin receptor Rattus norvegicus 47-49 15797682-3 2005 RESULTS: The results indicated that aging was accompanied by a significant decrease in IR tyrosine phosphorylation after insulin stimulation in live and skeletal muscle, which was associated with a significant increase in the activity of protein tyrosine phosphatase-1B. Tyrosine 90-98 insulin receptor Rattus norvegicus 87-89 15165993-6 2004 Cold exposure promoted significantly lower insulin-induced tyrosine phosphorylation of the insulin receptor (IR) and Ser473 phosphorylation of acute transforming retrovirus thymoma (Akt) and an insulin-independent increase of Thr172 phosphorylation of adenosine 5"-monophosphate-activated protein kinase (AMPK). Tyrosine 59-67 insulin receptor Rattus norvegicus 91-107 15165993-6 2004 Cold exposure promoted significantly lower insulin-induced tyrosine phosphorylation of the insulin receptor (IR) and Ser473 phosphorylation of acute transforming retrovirus thymoma (Akt) and an insulin-independent increase of Thr172 phosphorylation of adenosine 5"-monophosphate-activated protein kinase (AMPK). Tyrosine 59-67 insulin receptor Rattus norvegicus 109-111 16445997-2 2006 This study examines the compartmentalization and the insulin-induced translocation and tyrosine phosphorylation of insulin receptor substrates (IRS-1 and IRS-3) in epididymal white adipose tissue from adult and insulin-resistant old rats. Tyrosine 87-95 insulin receptor Rattus norvegicus 115-131 15561930-4 2004 We show that IL-1beta decreases insulin-induced tyrosine phosphorylation of the insulin receptor (IR) and insulin receptor substrate (IRS) proteins as well as phosphatidylinositol 3-kinase (PI3K) activation, and that this action is not due to the IL-1beta-dependent nitric oxide (NO) production in RINm5F cells. Tyrosine 48-56 insulin receptor Rattus norvegicus 80-101 15337529-7 2004 PP2 inhibition of Src also decreased insulin-induced IR tyrosine phosphorylation, IR-PKCdelta association and association of Src with both PKCdelta and IR. Tyrosine 56-64 insulin receptor Rattus norvegicus 53-55 15337529-10 2004 Thus, Src tyrosine kinase may play an important role in insulin-induced tyrosine phosphorylation of both IR and PKCdelta. Tyrosine 10-18 insulin receptor Rattus norvegicus 105-107 15247064-3 2004 The results indicated that aging was accompanied by a significant decline in insulin receptor tyrosine phosphorylation (pY-IR) upon insulin stimulation in both tissues, which was correlated with a significant increase in the activity of protein tyrosine phosphatase 1B (PTP-1B). Tyrosine 94-102 insulin receptor Rattus norvegicus 77-93 15247064-3 2004 The results indicated that aging was accompanied by a significant decline in insulin receptor tyrosine phosphorylation (pY-IR) upon insulin stimulation in both tissues, which was correlated with a significant increase in the activity of protein tyrosine phosphatase 1B (PTP-1B). Tyrosine 94-102 insulin receptor Rattus norvegicus 123-125 12970169-8 2003 As native insulin, native proinsulin induced a dose- and time-dependent endocytosis and tyrosine phosphorylation of the insulin receptor; but at an inframaximal dose, proinsulin effects on these processes were of longer duration. Tyrosine 88-96 insulin receptor Rattus norvegicus 120-136 14730380-1 2004 AIMS/HYPOTHESIS: Recruitment of the protein c-Cbl to the insulin receptor (IR) and its tyrosine phosphorylation via a pathway that is independent from phosphatidylinositol 3"-kinase is necessary for insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes. Tyrosine 87-95 insulin receptor Rattus norvegicus 57-78 14595539-8 2003 This effect correlated with the potentiation by rosiglitazone of insulin-stimulated Tyr phosphorylation of insulin receptor substrate-1 and to a greater extent of insulin receptor substrate-2. Tyrosine 84-87 insulin receptor Rattus norvegicus 107-123 12897373-0 2003 Regulation of insulin receptor substrate-2 tyrosine phosphorylation in animal models of insulin resistance. Tyrosine 43-51 insulin receptor Rattus norvegicus 14-30 14595539-10 2003 Rosiglitazone treatment increased insulin receptor expression and insulin-stimulated Tyr phosphorylation of insulin receptor beta-chain, but decreased insulin-stimulated Ser phosphorylation. Tyrosine 85-88 insulin receptor Rattus norvegicus 108-124 14595539-11 2003 It also potentiated insulin-induced Tyr phosphorylation of insulin receptor beta-chain and protein tyrosine phosphatase 1B in co-immunoprecipitates and impaired insulin activation of protein tyrosine phosphatase 1B activity. Tyrosine 36-39 insulin receptor Rattus norvegicus 59-75 14571618-1 2003 OBJECTIVE: To investigate the effect of Bushen Tongmai recipe (BSTMR) on the tyrosine phosphorylation of insulin receptor (InsR) and insulin receptor substrate-1 (IRS-1) after insulin stimulation in muscle and fat tissues of insulin resistant (IR) rats induced by high-fat forage. Tyrosine 77-85 insulin receptor Rattus norvegicus 105-121 14571618-1 2003 OBJECTIVE: To investigate the effect of Bushen Tongmai recipe (BSTMR) on the tyrosine phosphorylation of insulin receptor (InsR) and insulin receptor substrate-1 (IRS-1) after insulin stimulation in muscle and fat tissues of insulin resistant (IR) rats induced by high-fat forage. Tyrosine 77-85 insulin receptor Rattus norvegicus 123-127 14571618-5 2003 Meanwhile, the density of electrophoresis bands of tyrosine phosphorylated InsR and IRS-1 proteins in muscular and fatty tissues in the treated group increased obviously. Tyrosine 51-59 insulin receptor Rattus norvegicus 75-79 14571618-6 2003 CONCLUSION: BSTMR could attenuate the insulin resistance in rats, its pharmaceutical mechanisms might be closely related with the elevation of the tyrosine phosphorylation levels of InsR and IRS-1 in muscular and fatty tissues after insulin stimulation, and improvement of insulin signal transduction in target tissues. Tyrosine 147-155 insulin receptor Rattus norvegicus 182-186 12192891-4 2002 In the present study, measurements of tyrosine phosphorylation and protein content of the insulin receptor and expression of its gene in liver, skeletal muscle and adipose tissue indicate that during pregnancy significant changes occur in these parameters. Tyrosine 38-46 insulin receptor Rattus norvegicus 90-106 12742637-8 2003 Fraction 1 significantly stimulated tyrosine phosphorylation of the insulin receptor, whereas ERK I/II were stimulated by fractions 1, 2 and 4. Tyrosine 36-44 insulin receptor Rattus norvegicus 68-84 12782313-5 2003 Exposure of pancreatic islets to palmitate caused up-regulation of several insulin-induced activities including tyrosine phosphorylation of insulin receptor and pp185. Tyrosine 112-120 insulin receptor Rattus norvegicus 140-156 12841357-4 2003 We measured the changes in protein phosphorylation in samples from abdominus rectus muscle and there was a decrease of 64 and 75% in the levels of phosphorylation in tyrosine of the insulin receptor and insulin receptor substrate-1, respectively. Tyrosine 166-174 insulin receptor Rattus norvegicus 182-198 11563846-5 2001 Insulin induced rapid tyrosine-phosphorylation of the IR and IRS-1 and caused a 2.8-fold increase of IRS-1-bound PI3K. Tyrosine 22-30 insulin receptor Rattus norvegicus 54-56 11850117-6 2002 Thus, mutation of tyrosine 1162 and 1163 was also sufficient to inactivate signaling by the insulin receptor. Tyrosine 18-26 insulin receptor Rattus norvegicus 92-108 11739098-9 2002 After saline injection, tyrosine phosphorylation (pY) of IR, IRS-1, and IRS-2 was not significantly different between groups. Tyrosine 24-32 insulin receptor Rattus norvegicus 57-59 11786380-9 2002 The amount of insulin receptor was smaller in the liver of the transgenic rat, resulting in decreased tyrosine phosphorylation in response to insulin stimulation. Tyrosine 102-110 insulin receptor Rattus norvegicus 14-30 11574415-5 2001 Tyrosine phosphorylation of an endogenous 185-kDa IR substrate was also significantly enhanced by both Merck L7 alone and TLK16998 plus insulin. Tyrosine 0-8 insulin receptor Rattus norvegicus 50-52 11976270-7 2002 The in vitro study revealed that lignocaine directly inhibited both basal and insulin-stimulated tyrosine phosphorylation of IR. Tyrosine 97-105 insulin receptor Rattus norvegicus 125-127 12112939-5 2002 RESULTS: In rat muscle, increases in tyrosine phosphorylation of insulin receptor (IR) and activity of the insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol (PI) 3-kinase activity by insulin were similar or higher in freeze-dried and purified muscle than wet muscle. Tyrosine 37-45 insulin receptor Rattus norvegicus 65-81 12112939-5 2002 RESULTS: In rat muscle, increases in tyrosine phosphorylation of insulin receptor (IR) and activity of the insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol (PI) 3-kinase activity by insulin were similar or higher in freeze-dried and purified muscle than wet muscle. Tyrosine 37-45 insulin receptor Rattus norvegicus 83-85 11692173-6 2001 RESULTS: In L6 cells, physiological concentrations of C-peptide (0.3-3 nmol/l) significantly activated insulin receptor tyrosine kinase, IRS-1 tyrosine phosphorylation, PI 3-kinase activity, MAPK phosphorylation, p90Rsk, and GSK3 phosphorylation. Tyrosine 120-128 insulin receptor Rattus norvegicus 103-119 11484076-4 2001 RESULTS: In contrast to IRS-1, IRS-3 was tyrosine-phosphorylated by the insulin receptor altering Tyr960 to Phe (Y960F), which disrupts the binding site of the PTB domain of IRSs, to an extent comparable to the wild-type receptor. Tyrosine 41-49 insulin receptor Rattus norvegicus 72-88 11484076-5 2001 The tyrosine phosphorylation of IRS-3 with the PH domain replacement via the Y960F insulin receptor markedly decreased, whereas that of IRS-3 with the PTB domain alteration was mildly impaired. Tyrosine 4-12 insulin receptor Rattus norvegicus 83-99 11463579-6 2001 A 10 min exposure to homocysteine thiolactone (50 microM) resulted in a significant inhibition of insulin-stimulated tyrosine phosphorylation of the insulin receptor beta-subunit and its substrates IRS-1 and p60-70, as well as their association with the p85 regulatory subunit of phosphatidylinositol 3-kinase. Tyrosine 117-125 insulin receptor Rattus norvegicus 149-165 11278339-2 2001 Incubation of rat hepatoma Fao cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins. Tyrosine 79-82 insulin receptor Rattus norvegicus 102-118 11278339-4 2001 Wortmannin, a phosphatidylinositol 3-kinase (PI3K) inhibitor, abolished the increase in the P-Ser/Thr content of IRS-1, its dissociation from the IR, and the decrease in its P-Tyr content following 60 min of insulin treatment, indicating that the Ser kinases that negatively regulate IRS-1 function are downstream effectors of PI3K. Tyrosine 176-179 insulin receptor Rattus norvegicus 113-115 11229432-4 2001 Insulin-stimulated tyrosine phosphorylation of insulin receptor was reduced to 36% (P < .005), as was the phosphorylation of IRS-1 to 34% (P < .0001) of control. Tyrosine 19-27 insulin receptor Rattus norvegicus 47-63 11229432-8 2001 These results provide evidence that long-term denervation results in insulin resistance because of derangements at multiple points, including tyrosine phosphorylation of insulin receptor and its downstream signaling molecule, IRS-1, protein expression of IRS-1, and activation of PI 3-K. Tyrosine 142-150 insulin receptor Rattus norvegicus 170-186 11147799-1 2001 The regulation of insulin receptor (IR) tyrosine (tyr) phosphorylation is a key step in the control of insulin signaling. Tyrosine 40-48 insulin receptor Rattus norvegicus 18-34 11147799-1 2001 The regulation of insulin receptor (IR) tyrosine (tyr) phosphorylation is a key step in the control of insulin signaling. Tyrosine 40-43 insulin receptor Rattus norvegicus 18-34 10848643-4 2000 In insulin-treated rats, tyrosine-phosphorylated IR was 79% higher for CR vs. AL; tyrosine-phosphorylated IRS1 was 109% higher for CR vs. AL; IRS1-associated PI3K protein and IRS1-associated PI3K activity were unaffected by diet. Tyrosine 25-33 insulin receptor Rattus norvegicus 49-51 11121098-4 2001 Insulin caused tyrosine phosphorylation of the insulin receptor beta-subunit but EGF did not. Tyrosine 15-23 insulin receptor Rattus norvegicus 47-63 11105093-1 2000 Insulin stimulates the tyrosine kinase activity of its receptor resulting in the tyrosine phosphorylation of pp185, which contains insulin receptor substrates IRS-1 and IRS-2. Tyrosine 23-31 insulin receptor Rattus norvegicus 131-147 10924321-12 2000 Elevated PTPase 1B activity through enhanced tyrosine dephosphorylation of the insulin receptor and its substrates, may lead to impaired glucose tolerance and insulin resistance in GK rats. Tyrosine 45-53 insulin receptor Rattus norvegicus 79-95 10848643-0 2000 Calorie restriction increases insulin-stimulated tyrosine phosphorylation of insulin receptor and insulin receptor substrate-1 in rat skeletal muscle. Tyrosine 49-57 insulin receptor Rattus norvegicus 77-93 11027626-2 2000 Under these conditions, we have found a 70-kDa protein (pp70) in fat cells that is tyrosine-phosphorylated by the activated insulin receptor. Tyrosine 83-91 insulin receptor Rattus norvegicus 124-140 10842668-5 1999 Insulin-stimulated phosphorylation of tyrosine residues on the insulin receptor and on the associated docking protein IRS-1 are reduced in skeletal muscle and liver compared to SHR, due mainly to diminished expression of insulin receptor and IRS-1 proteins. Tyrosine 38-46 insulin receptor Rattus norvegicus 63-79 10847582-3 2000 We show that AT2 receptor interferes at the initial step of insulin signaling cascade, by impairing tyrosine phosphorylation of the insulin receptor (IR) beta-chain. Tyrosine 100-108 insulin receptor Rattus norvegicus 132-148 10692429-1 2000 Protein-tyrosine phosphatases (PTPases) play a key role in maintaining the steady-state tyrosine phosphorylation of the insulin receptor (IR) and its substrate proteins such as insulin receptor substrate 1 (IRS-1). Tyrosine 8-16 insulin receptor Rattus norvegicus 120-136 10692429-1 2000 Protein-tyrosine phosphatases (PTPases) play a key role in maintaining the steady-state tyrosine phosphorylation of the insulin receptor (IR) and its substrate proteins such as insulin receptor substrate 1 (IRS-1). Tyrosine 8-16 insulin receptor Rattus norvegicus 138-140 10574963-8 1999 Although IR showed a low level of in vivo tyrosine phosphorylation, an insulin-stimulated increase of in vitro Tyr phosphorylation of IR was detected in trained animals, suggesting that learning may induce IR functional changes, such as enhanced receptor sensitivity. Tyrosine 42-50 insulin receptor Rattus norvegicus 9-11 10574963-8 1999 Although IR showed a low level of in vivo tyrosine phosphorylation, an insulin-stimulated increase of in vitro Tyr phosphorylation of IR was detected in trained animals, suggesting that learning may induce IR functional changes, such as enhanced receptor sensitivity. Tyrosine 111-114 insulin receptor Rattus norvegicus 134-136 10574963-8 1999 Although IR showed a low level of in vivo tyrosine phosphorylation, an insulin-stimulated increase of in vitro Tyr phosphorylation of IR was detected in trained animals, suggesting that learning may induce IR functional changes, such as enhanced receptor sensitivity. Tyrosine 111-114 insulin receptor Rattus norvegicus 134-136 10827205-3 2000 However, tyrosine-phosphorylation of the insulin receptor after insulin stimulation was reduced to 71 +/- 2% (P < 0.05) of control in the liver of the fructose-fed rats. Tyrosine 9-17 insulin receptor Rattus norvegicus 41-57 10781929-8 2000 These results suggest that G-protein regulates DG-PKC signalling by binding of Gialpha-2 with GTP and PI 3-kinase-PKC zeta signalling by releasing of Gbetagamma via dissociation of trimeric G-protein after insulin receptor tyrosine phosphorylation in insulin-sensitive tissues. Tyrosine 223-231 insulin receptor Rattus norvegicus 206-222 10600915-3 1999 Peak insulin receptor (IR) tyrosine phosphorylation was reached after 6 (soleus) and 20 (Epi and EDL) min, with sustained activity throughout insulin exposure (40 min). Tyrosine 27-35 insulin receptor Rattus norvegicus 5-21 10600915-3 1999 Peak insulin receptor (IR) tyrosine phosphorylation was reached after 6 (soleus) and 20 (Epi and EDL) min, with sustained activity throughout insulin exposure (40 min). Tyrosine 27-35 insulin receptor Rattus norvegicus 23-25 10842668-5 1999 Insulin-stimulated phosphorylation of tyrosine residues on the insulin receptor and on the associated docking protein IRS-1 are reduced in skeletal muscle and liver compared to SHR, due mainly to diminished expression of insulin receptor and IRS-1 proteins. Tyrosine 38-46 insulin receptor Rattus norvegicus 221-237 9843961-1 1998 c-Cbl-associated protein (CAP) is a signaling protein that interacts with both c-Cbl and the insulin receptor that may be involved in the specific insulin-stimulated tyrosine phosphorylation of c-Cbl. Tyrosine 166-174 insulin receptor Rattus norvegicus 93-109 10216198-0 1999 Insulin induces tyrosine phosphorylation of the insulin receptor and SHC, and SHC/GRB2 association in cerebellum but not in forebrain cortex of rats. Tyrosine 16-24 insulin receptor Rattus norvegicus 48-64 10391142-5 1999 In vivo insulin-induced tyrosine phosphorylation of insulin receptor and insulin receptor substrate-1 was depressed by 82% (p < 0.05) and 86% (p < 0.05), respectively. Tyrosine 24-32 insulin receptor Rattus norvegicus 52-68 10391142-5 1999 In vivo insulin-induced tyrosine phosphorylation of insulin receptor and insulin receptor substrate-1 was depressed by 82% (p < 0.05) and 86% (p < 0.05), respectively. Tyrosine 24-32 insulin receptor Rattus norvegicus 73-89 10320054-5 1999 Results generated in the in vivo studies indicate that, like insulin, AII stimulates tyrosine phosphorylation of the insulin receptor substrates IRS-1 and IRS-2. Tyrosine 85-93 insulin receptor Rattus norvegicus 117-133 9571242-5 1998 The tyrosine phosphorylation of several proteins, including the beta-subunit of the insulin receptor, insulin receptor substrate-1, p85 regulatory subunit of phosphatidylinositol-3-kinase, and ras-guanosine triphosphatase-activating protein, was observed in AFP+ clones, whereas the same proteins were not phosphorylated in AFP- clones. Tyrosine 4-12 insulin receptor Rattus norvegicus 84-100 9802896-2 1998 Early studies using cell lines that overexpress the insulin receptor demonstrated that insulin caused a rapid reversible disassembly of actin filaments that coincided with the rapid tyrosine dephosphorylation of focal adhesion kinase. Tyrosine 182-190 insulin receptor Rattus norvegicus 52-68 9571242-5 1998 The tyrosine phosphorylation of several proteins, including the beta-subunit of the insulin receptor, insulin receptor substrate-1, p85 regulatory subunit of phosphatidylinositol-3-kinase, and ras-guanosine triphosphatase-activating protein, was observed in AFP+ clones, whereas the same proteins were not phosphorylated in AFP- clones. Tyrosine 4-12 insulin receptor Rattus norvegicus 102-118 9571242-6 1998 We also observed that fetal hepatocytes and the AFP+ clones express 4 times more of the insulin receptor beta-subunit compared with adult hepatocytes and AFP- clones and, accordingly, that these AFP+ clones were more responsive to exogenous insulin in terms of protein tyrosine phosphorylation. Tyrosine 269-277 insulin receptor Rattus norvegicus 88-104 9392479-10 1997 The acute administration of bradykinin increased insulin-stimulated tyrosine phosphorylation of the insulin receptor and IRS-1 in the liver and muscle. Tyrosine 68-76 insulin receptor Rattus norvegicus 100-116 9507031-10 1998 (i) A peptide corresponding to p125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor; and (ii) p125(Fak) phosphorylation by the insulin receptor is prevented by addition of this peptide. Tyrosine 97-106 insulin receptor Rattus norvegicus 182-198 9507031-10 1998 (i) A peptide corresponding to p125(Fak) sequence comprising amino acids 568-582, which contains tyrosines 576 and 577 of the kinase domain regulatory loop, is phosphorylated by the insulin receptor; and (ii) p125(Fak) phosphorylation by the insulin receptor is prevented by addition of this peptide. Tyrosine 97-106 insulin receptor Rattus norvegicus 242-258 9452421-9 1998 IR and IGF-IR Tyr phosphorylation motifs were not identified in the complete SH2-B primary structure, suggesting that it may participate as an adapter rather than a substrate in the IGF-I and insulin signaling pathways. Tyrosine 14-17 insulin receptor Rattus norvegicus 11-13 9374689-7 1997 Insulin-stimulated tyrosine phosphorylation of the insulin receptor beta-subunit and insulin receptor substrate-1 (IRS-1) in intact skeletal muscle of SHROB was reduced by 36 and 23%, respectively, compared with SHR, due primarily to 32 and 60% decreases in insulin receptor and IRS-1 protein expression, respectively. Tyrosine 19-27 insulin receptor Rattus norvegicus 51-67 9368067-1 1997 Elevated serine/threonine phosphorylation of IRS-1 and IRS-2 inhibits their binding to the juxtamembrane region of the insulin receptor and impairs their ability to undergo insulin-induced tyrosine phosphorylation. Tyrosine 189-197 insulin receptor Rattus norvegicus 119-135 9374689-7 1997 Insulin-stimulated tyrosine phosphorylation of the insulin receptor beta-subunit and insulin receptor substrate-1 (IRS-1) in intact skeletal muscle of SHROB was reduced by 36 and 23%, respectively, compared with SHR, due primarily to 32 and 60% decreases in insulin receptor and IRS-1 protein expression, respectively. Tyrosine 19-27 insulin receptor Rattus norvegicus 85-101 9374689-7 1997 Insulin-stimulated tyrosine phosphorylation of the insulin receptor beta-subunit and insulin receptor substrate-1 (IRS-1) in intact skeletal muscle of SHROB was reduced by 36 and 23%, respectively, compared with SHR, due primarily to 32 and 60% decreases in insulin receptor and IRS-1 protein expression, respectively. Tyrosine 19-27 insulin receptor Rattus norvegicus 85-101 8665940-1 1996 Tumor necrosis factor-alpha (TNF-alpha) is a proposed mediator of insulin resistance in obese/diabetic animals through its effects on tyrosine phosphorylation of the insulin receptor and its substrate, insulin receptor substrate-1. Tyrosine 134-142 insulin receptor Rattus norvegicus 166-182 9023010-4 1996 In addition, insulin-stimulated tyrosine phosphorylation of the endogenous insulin receptor substrates IRS-1 and Shc were decreased to 57% and 73% of control, respectively, and IRS-1 associated phosphatidylinositol 3"-kinase activity was reduced to 47% of control of the cells overexpressing LAR. Tyrosine 32-40 insulin receptor Rattus norvegicus 75-91 8895369-0 1996 A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo. Tyrosine 11-19 insulin receptor Rattus norvegicus 77-93 9312146-6 1997 Insulin-induced tyrosine kinase activity of insulin receptor (IR) and tyrosine phosphorylation of IRS-1 were also attenuated. Tyrosine 16-24 insulin receptor Rattus norvegicus 44-60 9312146-6 1997 Insulin-induced tyrosine kinase activity of insulin receptor (IR) and tyrosine phosphorylation of IRS-1 were also attenuated. Tyrosine 16-24 insulin receptor Rattus norvegicus 62-64 9264035-2 1997 Tyrosine phosphorylation of the insulin receptor and IRS-1 was increased by insulin. Tyrosine 0-8 insulin receptor Rattus norvegicus 32-48 8930123-4 1996 The only peptide readily phosphorylated is the one reproducing the activation loop of the insulin receptor (EIYET1160DYYA), including three tyrosines (Y1158, Y1162 and Y1163) whose phosphorylation through an intermolecular autocatalytic process promotes the activation of the receptor kinase. Tyrosine 140-149 insulin receptor Rattus norvegicus 90-106 8770882-0 1996 A 60-kilodalton protein in rat hepatoma cells overexpressing insulin receptor was tyrosine phosphorylated and associated with Syp, phophatidylinositol 3-kinase, and Grb2 in an insulin-dependent manner. Tyrosine 82-90 insulin receptor Rattus norvegicus 61-77 8611028-8 1996 Furthermore, immunodetection of the beta-subunit of the insulin receptor in anti-phosphotyrosine immunoprecipitates revealed that treatment with lovastatin reduced the tyrosine phosphorylation levels of the receptor. Tyrosine 88-96 insulin receptor Rattus norvegicus 56-72 8866828-4 1996 Both insulin (100 nM) and pervanadate (100 microM), a protein tyrosine phosphatase inhibitor, induced a marked increase in the phosphorylation at tyrosine residues of IR and insulin receptor substrate 1 (IRS-1) and in 2-deoxyglucose uptake in 3T3-L1 adipocytes. Tyrosine 62-70 insulin receptor Rattus norvegicus 167-169 8144649-0 1994 Mutation of the two carboxyl-terminal tyrosines in the insulin receptor results in enhanced activation of mitogen-activated protein kinase. Tyrosine 38-47 insulin receptor Rattus norvegicus 55-71 8927047-13 1995 Finally administration of bpV(phen) and insulin led to a synergism, where tyrosine phosphorylation of the IR beta-subunit increased by 20-fold and led to the appearance of four insulin-dependent in vivo substrates. Tyrosine 74-82 insulin receptor Rattus norvegicus 106-108 7653545-7 1995 However, after ILI treatment of intact cells and immunoprecipitation of insulin receptors, ILI induced a dose-dependent tyrosine phosphorylation of the insulin receptor beta-subunit. Tyrosine 120-128 insulin receptor Rattus norvegicus 72-88 7762655-4 1995 Insulin increased tyrosine phosphorylation of the insulin receptor and IRS-1, whereas contraction alone had no effect. Tyrosine 18-26 insulin receptor Rattus norvegicus 50-66 8175658-7 1994 These data suggest that: 1) p62 GAP-associated protein is tyrosine phosphorylated after insulin stimulation of cells; 2) p62 and IRS-1 form separate complexes with p85; 3) p62-GAP complex may be linked to p85 that is not bound to p110; 4) p85 may serve as an adaptor molecule in insulin receptor signaling, interacting with and regulating other intracellular proteins via SH2 domains. Tyrosine 58-66 insulin receptor Rattus norvegicus 279-295 8144649-5 1994 To explore the early signaling events that might account for this increase in responsiveness, we evaluated the tyrosine phosphorylation of the insulin receptor substrate, IRS-1, and its subsequent association with phosphatidylinositol (PI)-3 kinase. Tyrosine 111-119 insulin receptor Rattus norvegicus 143-159 1457763-1 1992 Insulin stimulates tyrosine phosphorylation of the insulin receptor and of an endogenous substrate of approximately 185 kd (insulin receptor substrate 1 or IRS-1) in most cell types. Tyrosine 19-27 insulin receptor Rattus norvegicus 51-67 8106400-5 1994 The effect of insulin to induce membrane PI 3-kinase activity was mostly abolished, but its effects to tyrosine-phosphorylate the beta-subunit of the insulin receptor or other cellular substrate proteins including insulin-receptor-substrate-1 were not at all antagonized, by wortmannin added to the cell incubation medium. Tyrosine 103-111 insulin receptor Rattus norvegicus 150-166 8349691-1 1993 IRS-1, a principal substrate of the insulin receptor, is phosphorylated on serine, threonine, and tyrosine residues in a variety of tissues during insulin stimulation. Tyrosine 98-106 insulin receptor Rattus norvegicus 36-52 8087096-2 1994 Insulin stimulates tyrosine phosphorylation of the insulin receptor and of an endogenous substrate of approximately 185 kDa (insulin receptor substrate 1 or IRS-1). Tyrosine 19-27 insulin receptor Rattus norvegicus 51-67 7513124-7 1994 Moreover, the purified Tyr(P) form of IRS-1, either isolated from 3T3-L1 adipocytes or obtained by phosphorylation of the recombinant protein with the insulin receptor, markedly stimulated the activity of purified rat liver PI 3-kinase. Tyrosine 23-26 insulin receptor Rattus norvegicus 151-167 8015549-6 1994 In intact HTC cells expressing mutated receptors, basal insulin receptor tyrosine autophosphorylation was 2-fold elevated when compared to cells expressing normal receptors. Tyrosine 73-81 insulin receptor Rattus norvegicus 56-72 1457763-2 1992 Tyrosine phosphorylation of insulin receptor and of IRS-1 have been implicated in insulin signal transmission based on studies with insulin receptor mutants. Tyrosine 0-8 insulin receptor Rattus norvegicus 28-44 1457763-2 1992 Tyrosine phosphorylation of insulin receptor and of IRS-1 have been implicated in insulin signal transmission based on studies with insulin receptor mutants. Tyrosine 0-8 insulin receptor Rattus norvegicus 132-148 1321717-6 1992 Taken together these results suggest that, upon insulin stimulation of fat cells, PtdIns-3-kinase itself is tyrosine phosphorylated and/or associated with an insulin receptor substrate, such as p185, which could function as a link between the insulin receptor and PtdIns-3-kinase. Tyrosine 108-116 insulin receptor Rattus norvegicus 243-259 1380438-2 1992 Insulin-dependent tyrosine phosphorylation of a monomeric 195K glycoprotein (pp195) was observed in wheatgerm agglutinin (WGA)-Sepharose-purified insulin receptor preparations from rat liver and muscle. Tyrosine 18-26 insulin receptor Rattus norvegicus 146-162 1314657-5 1992 NGF-stimulated tyrosine phosphorylation of the pp140c-trk NGF receptor and tyrosine phosphorylation of pp70trk are also inhibited by similar concentrations of staurosporine and K252A, whereas tyrosine phosphorylation of the EGF receptor, insulin receptor, and v-src is not affected. Tyrosine 15-23 insulin receptor Rattus norvegicus 238-254 1374397-12 1992 Exogenous IR kinase activity (poly(Glu:Tyr)) in PM changed only slightly with insulin dose. Tyrosine 39-42 insulin receptor Rattus norvegicus 10-12 1816977-2 1991 It has been suggested that the phosphorylation of serine and/or threonine residues of the insulin receptor may reduce tyrosine autophosphorylation in streptozotocin-induced diabetic rats (STZ-D rats). Tyrosine 118-126 insulin receptor Rattus norvegicus 90-106 1531627-1 1992 The effects of experimental diabetes on in vivo tyrosine phosphorylation of the insulin receptor (IR) and non-receptor proteins were investigated in rat skeletal muscle. Tyrosine 48-56 insulin receptor Rattus norvegicus 80-101 1531627-5 1992 In both control and diabetic rats, insulin stimulated tyrosine phosphorylation of the IR beta-subunit and a major nonreceptor 170,000 mol wt (Mr) endogenous protein (pp170) in a dose- and time-dependent manner. Tyrosine 54-62 insulin receptor Rattus norvegicus 86-88 1661694-2 1991 Insulin receptor tyrosine kinase activity solubilized from hind limb muscle of control and streptozocin-induced diabetic (STZ-D) rats (2-3 wk) was studied with the substrates histone H2B and poly glutamic acid-tyrosine (glu-tyr) (4:1). Tyrosine 17-20 insulin receptor Rattus norvegicus 0-16 2026614-0 1991 Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signaling but enhanced mitogenic signaling properties. Tyrosine 38-47 insulin receptor Rattus norvegicus 62-78 2026614-7 1991 To explore further the regulatory role of the insulin receptor carboxyl terminus, a mutant insulin receptor was constructed in which the two tyrosines (Y1316 and Y1322) on the carboxyl terminus were replaced with phenylalanines. Tyrosine 141-150 insulin receptor Rattus norvegicus 91-107 2026614-12 1991 Thus, the two tyrosines of the insulin receptor carboxyl terminus do not modulate the kinase function of the insulin receptor, although they are autophosphorylated in native receptors. Tyrosine 14-23 insulin receptor Rattus norvegicus 31-47 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 62-70 insulin receptor Rattus norvegicus 13-29 1849850-2 1991 In these cells, insulin rapidly stimulated tyrosine phosphorylation of the 95,000-Mr beta-subunit of the insulin receptor and a 175,000-Mr phosphoprotein (pp175). Tyrosine 43-51 insulin receptor Rattus norvegicus 105-121 1701386-9 1990 Under these conditions polylysine enhanced both serine and tyrosine phosphorylation of the insulin receptor, suggesting that polylysine stimulates the activity of the insulin receptor kinase, and of a serine kinase that is tightly associated with the insulin receptor. Tyrosine 59-67 insulin receptor Rattus norvegicus 91-107 2200529-3 1990 In intact adipocytes, ATEE inhibited tyrosine phosphorylation of the beta-subunit of the insulin receptor, a 170 kDa protein and a 60 kDa protein at almost the same concentration (ID50 = 0.24 +/- 0.05 mM, n = 4, mean +/- S.E. Tyrosine 37-45 insulin receptor Rattus norvegicus 89-105 2161833-7 1990 In the latter experiment, cells expressing HIR delta ex16 receptors exhibit tyrosine phosphorylation of insulin receptor beta-subunits as well as of pp 185, a putative substrate of the receptor. Tyrosine 76-84 insulin receptor Rattus norvegicus 104-120 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 62-70 insulin receptor Rattus norvegicus 150-166 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 62-70 insulin receptor Rattus norvegicus 198-214 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 261-269 insulin receptor Rattus norvegicus 13-29 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 261-269 insulin receptor Rattus norvegicus 150-166 1691994-6 1990 Because anti-insulin-receptor antibodies immunoprecipitated a tyrosine-phosphorylated 95,000-Mr protein, this protein must be the beta-subunit of the insulin receptor; i.e., the beta-subunit of the insulin receptor and two other proteins were phosphorylated at tyrosine residues in vivo by insulin injection. Tyrosine 261-269 insulin receptor Rattus norvegicus 198-214 1691994-7 1990 These data suggest that the tyrosine phosphorylation and tyrosine kinase activity of the insulin receptor may have important roles in in vivo insulin action. Tyrosine 28-36 insulin receptor Rattus norvegicus 89-105 1691570-5 1990 Basal as well as insulin-stimulated tyrosine kinase activity per insulin receptor was higher in the high-fat fed group, accompanied by increased autophosphorylation of the beta-subunit of the receptor and higher proportion of tyrosine-phosphorylated insulin receptors. Tyrosine 36-44 insulin receptor Rattus norvegicus 65-81 1691570-6 1990 In contrast, both in the skeletal muscle and the liver the insulin-stimulated tyrosine kinase activity per insulin receptor was significantly lower in high-fat fed animals, accompanied by diminished autophosphorylation of the beta-subunit of the receptor and lower proportion of tyrosine-phosphorylated receptors. Tyrosine 78-86 insulin receptor Rattus norvegicus 107-123 2643441-11 1989 These results suggest: (1) [125I]insulin and the insulin receptor are internalized by parametrial adipocytes into an early endosomal compartment (primary endosomes), from which the receptor, intact [125I]insulin, and [125I]tyrosine are returned to the cell surface; and (2) the damping of the insulin signal observed in parametrial adipocytes from lactating rats is not expressed at the level of altered endocytotic processing of [125I]insulin and the insulin receptor. Tyrosine 223-231 insulin receptor Rattus norvegicus 49-65 2547842-11 1989 Since tyrosine phosphorylation plays a central role in the cellular action of insulin receptor, an increase in PTPase activity may be an important factor in the altered insulin action associated with these diabetic states. Tyrosine 6-14 insulin receptor Rattus norvegicus 78-94 2470095-0 1989 Tyrosine phosphorylation of the insulin receptor is not required for receptor internalization: studies in 2,4-dinitrophenol-treated cells. Tyrosine 0-8 insulin receptor Rattus norvegicus 32-48 2546941-13 1989 Phosphoamino acid analyses revealed that the activated IR of intact PM was autophosphorylated in vitro, at both serine (55%) and tyrosine (45%) residues; whereas the activated IR of intact ENs was phosphorylated in vitro exclusively on tyrosine autophosphorylation specific activity for the activated IR of ENs was 3- to 4-fold that of the IR of PM. Tyrosine 129-137 insulin receptor Rattus norvegicus 55-57 2546941-13 1989 Phosphoamino acid analyses revealed that the activated IR of intact PM was autophosphorylated in vitro, at both serine (55%) and tyrosine (45%) residues; whereas the activated IR of intact ENs was phosphorylated in vitro exclusively on tyrosine autophosphorylation specific activity for the activated IR of ENs was 3- to 4-fold that of the IR of PM. Tyrosine 236-244 insulin receptor Rattus norvegicus 55-57 2468662-0 1989 Tyrosine phosphorylation of pp185 by insulin receptor kinase in a cell-free system. Tyrosine 0-8 insulin receptor Rattus norvegicus 37-53 2468662-7 1989 These results suggest that tyrosine phosphorylation of pp185 is catalyzed directly by IR kinase in this cell-free system. Tyrosine 27-35 insulin receptor Rattus norvegicus 86-88 2466044-0 1989 Autoantibodies to the insulin receptor (B-10) can stimulate tyrosine phosphorylation of the beta-subunit of the insulin receptor and a 185,000 molecular weight protein in rat hepatoma cells. Tyrosine 60-68 insulin receptor Rattus norvegicus 22-38 2466044-2 1989 Partially purified insulin receptor from H-35 cells, when incubated with B-10 IgG, had increased tyrosine kinase activity for a synthetic peptide sequentially similar to the site of tyrosine phosphorylation in pp60v-arc (the gene product responsible for cellular transformation by the Rous sarcoma virus). Tyrosine 97-105 insulin receptor Rattus norvegicus 19-35 2466044-5 1989 These results suggest that antiinsulin receptor antibodies (B-10) may initiate their insulin-like effects via tyrosine phosphorylation of the insulin receptor, activation of its tyrosine kinase activity, and phosphorylation of a cellular protein substrate of 185,000 mol wt. Tyrosine 110-118 insulin receptor Rattus norvegicus 31-47 2458910-4 1988 In hepatocytes from both control and dexamethasone-treated animals labeled with 32P, insulin induced tyrosine phosphorylation of the beta-subunit of the insulin receptor as well as of a 175K protein believed to be its endogenous substrate. Tyrosine 101-109 insulin receptor Rattus norvegicus 153-169 2463986-0 1989 Tyrosine phosphorylation of the insulin receptor during insulin-stimulated internalization in rat hepatoma cells. Tyrosine 0-8 insulin receptor Rattus norvegicus 32-48 2462493-1 1989 Tyrosine phosphorylation of the insulin receptor and other intracellular proteins in rat adipocytes was examined using an immunoblot technique with antiphosphotyrosine antibody. Tyrosine 0-8 insulin receptor Rattus norvegicus 32-48 2462493-2 1989 Insulin at 10(-7) M increased the tyrosine phosphorylation of the 95K subunit of the insulin receptor (15-fold) and proteins of 180K (7-fold) and 60K (23-fold). Tyrosine 34-42 insulin receptor Rattus norvegicus 85-101 2462493-6 1989 Vanadate increased tyrosine phosphorylation of the 95K insulin receptor beta-subunit and the 120K and 60K proteins similarly, with increases of 1.5- to 3-fold at 1 mM and 2-fold or less at 200 and 50 microM. Tyrosine 19-27 insulin receptor Rattus norvegicus 55-71 2844584-1 1988 Synthetic peptide 1142-1153 of the insulin receptor was phosphorylated on tyrosine by the insulin receptor and found to be a potent substrate for dephosphorylation by rat liver particulate and soluble phosphotyrosyl protein phosphatases. Tyrosine 74-82 insulin receptor Rattus norvegicus 35-51 2438282-9 1987 Analysis of the insulin dose-response relationship between P160 tyrosine phosphorylation and insulin receptor kinase activity reveals that maximal phosphorylation of P160 occurs when only a fraction (25%) of the receptor kinase is activated by the hormone. Tyrosine 64-72 insulin receptor Rattus norvegicus 93-109 2449432-0 1988 A cascade of tyrosine autophosphorylation in the beta-subunit activates the phosphotransferase of the insulin receptor. Tyrosine 13-21 insulin receptor Rattus norvegicus 102-118 3275643-0 1988 Identification of the insulin receptor tyrosine residues undergoing insulin-stimulated phosphorylation in intact rat hepatoma cells. Tyrosine 39-47 insulin receptor Rattus norvegicus 22-38 3275643-2 1988 Two major insulin-stimulated, Tyr(P) proteins were recovered: an Mr 95,000 protein (identified as the insulin receptor beta subunit by its immunoprecipitation by a patient-derived anti-insulin receptor serum and several anti-insulin receptor (peptide) antisera) and an Mr 180,000 protein (which was unreactive with all anti-insulin receptor antibodies). Tyrosine 30-33 insulin receptor Rattus norvegicus 102-118 3292965-4 1988 In addition, insulin stimulated the dose-dependent phosphorylation of exogenous tyrosine containing substrate and a 95,000 MW plasma membrane associated protein, in a lectin-purified insulin receptor preparation. Tyrosine 80-88 insulin receptor Rattus norvegicus 183-199 2833239-0 1988 Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells. Tyrosine 29-37 insulin receptor Rattus norvegicus 61-77 2833239-2 1988 The incubation of these cells with 10 mM-H2O2 for 10 min increased the phosphorylation of both the serine and tyrosine residues of the beta subunit of the insulin receptor. Tyrosine 110-118 insulin receptor Rattus norvegicus 155-171 3124751-3 1988 Under conditions where insulin treatment of H4 cells clearly activated receptor serine and tyrosine phosphorylation on the insulin receptor beta-subunit in situ, activated receptor tyrosine kinase activity in vitro, and activated glycogen synthase and p33 mRNA accumulation in situ, PMA alone did not influence the insulin receptor phosphorylation state or tyrosine kinase activity and did not affect glycogen synthase activity, but markedly increased p33 mRNA accumulation. Tyrosine 91-99 insulin receptor Rattus norvegicus 123-139 2439512-1 1987 Using antiphosphotyrosine antibodies, we have characterized the tyrosine phosphorylation of an endogenous substrate of the insulin receptor in Fao hepatoma cells and in Chinese hamster ovary cells transfected with a eukaryotic expression vector containing the human insulin receptor cDNA. Tyrosine 17-25 insulin receptor Rattus norvegicus 123-139 2438282-11 1987 The close correlation between the level of P160 phosphorylation and insulin receptor kinase activity suggests that P160 may be tyrosine phosphorylated by the receptor kinase following receptor kinase activation by the hormone or insulin-like agents. Tyrosine 127-135 insulin receptor Rattus norvegicus 68-84 3555483-0 1987 Inhibition of tyrosine autophosphorylation of the solubilized insulin receptor by an insulin-stimulating peptide derived from bovine serum albumin. Tyrosine 14-22 insulin receptor Rattus norvegicus 62-78 3036804-2 1987 Autophosphorylation of the insulin receptor on tyrosine residues and activation of the endogenous insulin receptor kinase is postulated to be a critical step in the mechanism of action of insulin. Tyrosine 47-55 insulin receptor Rattus norvegicus 27-43 3957914-0 1986 Tyrosine phosphorylation of insulin receptor beta subunit activates the receptor tyrosine kinase in intact H-35 hepatoma cells. Tyrosine 0-8 insulin receptor Rattus norvegicus 28-44 2433277-9 1987 These data suggest that tyrosine phosphorylation of pp 185 may occur during activation of both the type I IGF receptor and the insulin receptor, and it could be a common substrate that transmits important metabolic signals during ligand binding. Tyrosine 24-32 insulin receptor Rattus norvegicus 127-143 3957914-4 1986 In response to insulin, the insulin receptor beta subunit exhibits marked tyrosine phosphorylation and a 2-fold increase in total [32P]phosphoserine contents. Tyrosine 74-82 insulin receptor Rattus norvegicus 28-44 3957914-10 1986 The correlation between the insulin-stimulated site specific tyrosine phosphorylation on receptor beta subunit and the elevation of receptor tyrosine kinase activity strongly suggests that the insulin receptor kinase is activated by hormone-stimulated autophosphorylation on tyrosine residues in intact cells, as previously demonstrated for the purified receptor. Tyrosine 61-69 insulin receptor Rattus norvegicus 193-209 3957914-10 1986 The correlation between the insulin-stimulated site specific tyrosine phosphorylation on receptor beta subunit and the elevation of receptor tyrosine kinase activity strongly suggests that the insulin receptor kinase is activated by hormone-stimulated autophosphorylation on tyrosine residues in intact cells, as previously demonstrated for the purified receptor. Tyrosine 141-149 insulin receptor Rattus norvegicus 193-209 3848433-13 1985 Our results indicate that: tyrosine phosphorylation of the insulin receptor occurs rapidly following insulin binding to intact cells; the level of tyrosine phosphorylation remains constant for up to 1 h; the specificity of the receptor kinase or accessibility of the phosphorylation sites are different in vivo and in vitro. Tyrosine 27-35 insulin receptor Rattus norvegicus 59-75 3005303-4 1986 We found that insulin (10(-7) M) increased the tyrosine autophosphorylation of the insulin receptor kinase from TPA-treated cells only 3-fold in contrast to a 12-fold stimulation in control cells. Tyrosine 47-55 insulin receptor Rattus norvegicus 83-99 3518707-4 1986 (1) Insulin increased the tyrosine autophosphorylation of the insulin receptor kinase from catecholamine-treated cells only 4-fold, compared with a 12-fold stimulation in control cells. Tyrosine 26-34 insulin receptor Rattus norvegicus 62-78 3935910-1 1985 Insulin stimulated phosphorylation of tyrosine residues by the insulin receptor kinase may be part of a signalling mechanism associated with insulin"s action. Tyrosine 38-46 insulin receptor Rattus norvegicus 63-79 3935910-8 1985 Thus, indomethacin partially inhibited autophosphorylation of the solubilized insulin receptor on tyrosine and partially inhibited some but not all of insulin"s actions. Tyrosine 98-106 insulin receptor Rattus norvegicus 78-94 3000458-2 1985 Under in vitro conditions, the tyrosine kinase activity of the insulin receptor toward histone is markedly activated when the receptor either undergoes autophosphorylation or is phosphorylated by a purified preparation of src tyrosine kinase on tyrosine residues of its beta subunit. Tyrosine 31-39 insulin receptor Rattus norvegicus 63-79 3000458-4 1985 Analysis of tryptic digests of phosphorylated insulin receptor using reverse-phase high pressure liquid chromatography suggests that phosphorylation of a specific tyrosine site on the receptor beta subunit may be involved in the mechanism of the receptor kinase activation. Tyrosine 163-171 insulin receptor Rattus norvegicus 46-62 3000458-5 1985 Further studies indicate that tyrosine phosphorylation-mediated increase in insulin receptor activity also occurs in intact cells. Tyrosine 30-38 insulin receptor Rattus norvegicus 76-92 3000458-8 1985 Taken together, these results indicate that tyrosine phosphorylation of the insulin receptor beta subunit exerts a major stimulatory effect on the kinase activity of the receptor. Tyrosine 44-52 insulin receptor Rattus norvegicus 76-92 3848433-13 1985 Our results indicate that: tyrosine phosphorylation of the insulin receptor occurs rapidly following insulin binding to intact cells; the level of tyrosine phosphorylation remains constant for up to 1 h; the specificity of the receptor kinase or accessibility of the phosphorylation sites are different in vivo and in vitro. Tyrosine 147-155 insulin receptor Rattus norvegicus 59-75 6427220-5 1984 Vanadate stimulated the phosphorylation of the 95,000-dalton subunit of the insulin receptor on tyrosine residues both in intact adipocytes and in a solubilized insulin receptor fraction. Tyrosine 96-104 insulin receptor Rattus norvegicus 76-92 6389544-7 1984 Phosphorylation of an exogenously added synthetic peptide (similar in sequence to the tyrosine phosphorylation site in pp60src) by the insulin receptor-kinase was also decreased by 25% in diabetic rats. Tyrosine 86-94 insulin receptor Rattus norvegicus 135-151 31856878-6 2019 RESULTS: When significant mitochondrial depolarisations occurred due to glutamate-evoked massive influxes of Ca2+ into the cells, insulin induced 48% less activation of the IR (assessed by IR tyrosine phosphorylation, pY1150/1151), 72% less activation of Akt (assessed by Akt serine phosphorylation, pS473), 44% less activation of mTOR (assessed by mTOR pS2448), and 38% less inhibition of glycogen synthase kinase beta (GSK3beta) (assessed by GSK3beta pS9) compared with respective controls. Tyrosine 192-200 insulin receptor Rattus norvegicus 173-175 6370772-1 1984 Imaging and quantitative analysis of insulin-receptor interaction was studied in vivo in lean and obese Zucker rats, using a recently developed technique in which purified Tyr A14 123I-monoiodoinsulin is intravenously injected and the tracer followed by scintillation scanning. Tyrosine 172-175 insulin receptor Rattus norvegicus 37-53 6407485-4 1983 Vanadate also enhanced the degree of phosphorylation of the 95,000 dalton subunit of insulin receptor, selectively on tyrosine residues, in the solubilized rat adipocyte insulin receptor system. Tyrosine 118-126 insulin receptor Rattus norvegicus 85-101 28063625-9 2017 We demonstrated that the favorable effect of antidepressans on insulin receptor phosphorylation in the frontal cortex was mainly related with the normalization of serine312 and tyrosine IRS-1 phosphorylation, while in the hippocampus, it was related with the adaptor proteins Shc1/Grb2. Tyrosine 177-185 insulin receptor Rattus norvegicus 63-79 30248393-6 2019 HSP70 was induced and insulin signaling as measured from tyrosine phosphorylation of insulin receptor (IR) & insulin receptor substrate-1 (IRS-1) and serine phosphorylation of Akt was attenuated in comparison to those in untreated myotubes. Tyrosine 57-65 insulin receptor Rattus norvegicus 85-101 30248393-6 2019 HSP70 was induced and insulin signaling as measured from tyrosine phosphorylation of insulin receptor (IR) & insulin receptor substrate-1 (IRS-1) and serine phosphorylation of Akt was attenuated in comparison to those in untreated myotubes. Tyrosine 57-65 insulin receptor Rattus norvegicus 103-105 31113619-6 2019 Moreover, tyrosine phosphorylation of the IR and IRS-1, and Akt activation is decreased in STZ diabetes compared to control. Tyrosine 10-18 insulin receptor Rattus norvegicus 42-44 30296358-5 2018 Western blot and immunoprecipitation analysis reveal that Gin A increases insulin receptor tyrosine phosphorylation in L6 myotubes and IRS-1 binding to the PI3K in 3T3-L1 adipocytes. Tyrosine 91-99 insulin receptor Rattus norvegicus 74-90 26658505-10 2015 Insulin lispro released from the hydrogels was biologically active by increasing insulin receptor tyrosine and Akt serine phosphorylation of ex vivo retinas. Tyrosine 98-106 insulin receptor Rattus norvegicus 81-97 26099503-10 2016 Compared with control cells, INS-1 cells overexpressing PTP1B showed decrease in insulin-stimulated tyrosine phosphorylation of the insulin receptor (IR) and insulin receptor substrate-1(IRS-1) by 56.4% and 53.1%, respectively. Tyrosine 100-108 insulin receptor Rattus norvegicus 132-148 26675491-8 2016 In addition, osteoblastic insulin resistance, as indicated by a decrease in tyrosine phosphorylation of the insulin receptor and Akt, were observed in all groups except the sham-operated ND-fed rats (NDS) rats. Tyrosine 76-84 insulin receptor Rattus norvegicus 108-124 27052924-6 2016 The reduction of glucose uptake was associated with a moderately reduced tyrosine phosphorylation of the insulin receptor. Tyrosine 73-81 insulin receptor Rattus norvegicus 105-121 22286902-4 2013 Insulin receptor tyrosine phosphorylation (Tyr1162/1163) was unaltered by exercise in either muscle. Tyrosine 17-25 insulin receptor Rattus norvegicus 0-16 24377914-7 2014 Concomitant with, or shortly after, the tyrosine-phosphorylated IR is deactivated by two independent processes: its rapid dephosphorylation by endosome-associated phosphotyrosine phosphatase(s) and its association with the molecular adaptor Grb14, with resulting inhibition of IR catalytic activity. Tyrosine 40-48 insulin receptor Rattus norvegicus 64-66 23749991-4 2013 In PC12 cells, tyrosine phosphorylation of INSR and IRS-1 is dependent upon the functional TrkA kinase domain. Tyrosine 15-23 insulin receptor Rattus norvegicus 43-47 23279876-4 2013 For insulin signaling transduction, phosphorylation of insulin receptor (IR), insulin receptor substrate-1 (IRS1) at the tyrosine residue, Akt, and AMP-activated protein kinase (AMPK), were attenuated in the liver, while negative regulators of insulin action, including phosphorylation of p38, c-Jun N-terminal kinase (JNK), and insulin receptor substrate-1 (IRS1) at the serine residue, were increased. Tyrosine 121-129 insulin receptor Rattus norvegicus 55-71 23279876-4 2013 For insulin signaling transduction, phosphorylation of insulin receptor (IR), insulin receptor substrate-1 (IRS1) at the tyrosine residue, Akt, and AMP-activated protein kinase (AMPK), were attenuated in the liver, while negative regulators of insulin action, including phosphorylation of p38, c-Jun N-terminal kinase (JNK), and insulin receptor substrate-1 (IRS1) at the serine residue, were increased. Tyrosine 121-129 insulin receptor Rattus norvegicus 73-75