PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2675630-6	1989	The data suggest 1) the insulin receptor in muscle stimulates glucose transport by a signaling pathway that is not shared by other insulin-sensitive effector systems, and 2) denervation may affect insulin receptor signal transduction at more than one site.	Glucose	62-69	insulin receptor	Rattus norvegicus	24-40
2484229-3	1989	Epididymal adipocytes from Ni2(+)-fed rats showed an increased insulin binding with a slight increase in apparent insulin affinity (ED50: Ni2(+)-fed rats 2.8 x 10(-9) M and controls 5 x 10(-9) M) with no change in insulin receptor numbers (Ni2(+)-fed rats 143,000 +/- 12,000 (6) receptors/cell and controls 126,000 +/- 13,000 (5].	ni2	27-30	insulin receptor	Rattus norvegicus	214-230
2698304-6	1989	These findings as well as our finding that the thymocytes from diabetic rats possess a normal complement of insulin receptor provide further evidence that post insulin receptor impairment of glucose metabolism occurs in streptozotocin diabetes.	Streptozocin	220-234	insulin receptor	Rattus norvegicus	160-176
2506075-1	1989	In two-dimensional tryptic phosphopeptide mapping, the beta-subunit of the insulin receptor phosphorylated by 12-O-tetradecanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides.	Tetradecanoylphorbol Acetate	110-146	insulin receptor	Rattus norvegicus	75-91
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
2506075-1	1989	In two-dimensional tryptic phosphopeptide mapping, the beta-subunit of the insulin receptor phosphorylated by 12-O-tetradecanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides.	Phosphothreonine	199-215	insulin receptor	Rattus norvegicus	75-91
2506075-1	1989	In two-dimensional tryptic phosphopeptide mapping, the beta-subunit of the insulin receptor phosphorylated by 12-O-tetradecanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides.	Phosphoserine	247-260	insulin receptor	Rattus norvegicus	75-91
2506075-2	1989	The synthetic peptide coding residues 1327-1343 in the C-terminal region of the rat insulin receptor was phosphorylated at the threonine residue by protein kinase C in a phosphatidylserine and oleoylacetylglycerol dependent manner.	Threonine	127-136	insulin receptor	Rattus norvegicus	84-100
2506075-4	1989	These data suggested that Thr 1336 of the insulin receptor is the site of phosphorylation by protein kinase C in intact cells.	Threonine	26-29	insulin receptor	Rattus norvegicus	42-58
2544783-1	1989	To test the hypothesis that sulfonylureas enhance insulin action by activating the insulin receptor tyrosine kinase, the effects of glyburide, a second generation sulfonylurea, and ciglitazone, a nonsulfonylurea hypoglycemic agent, were determined in primary cultures of rat hepatocytes on insulin action and insulin receptor structure and function.	Sulfonylurea Compounds	28-40	insulin receptor	Rattus norvegicus	83-99
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.	Phosphoamino Acids	0-17	insulin receptor	Rattus norvegicus	55-57
2675675-3	1989	The insulin receptor was solubilized in triton x-100 and its properties compared with those of solubilized membranes of rat liver.	Octoxynol	40-52	insulin receptor	Rattus norvegicus	4-20
2544783-1	1989	To test the hypothesis that sulfonylureas enhance insulin action by activating the insulin receptor tyrosine kinase, the effects of glyburide, a second generation sulfonylurea, and ciglitazone, a nonsulfonylurea hypoglycemic agent, were determined in primary cultures of rat hepatocytes on insulin action and insulin receptor structure and function.	Sulfonylurea Compounds	28-41	insulin receptor	Rattus norvegicus	83-99
2475105-0	1989	Insulin receptor dephosphorylation in permeabilized adipocytes is inhibitable by manganese and independent of receptor kinase activity.	Manganese	81-90	insulin receptor	Rattus norvegicus	0-16
2475105-7	1989	Thus, a dephosphorylation reaction involving the membrane-associated insulin receptor is inhibited by manganese and is independent of the receptor kinase activity.	Manganese	102-111	insulin receptor	Rattus norvegicus	69-85
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.	Serine	112-118	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	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
2544783-4	1989	Glyburide"s actions were mediated without altering the following: (1) 125I-insulin binding; (2) the electrophoretic mobility of the affinity labeled alpha-subunit or the autophosphorylated beta-subunit of the insulin receptor; and (3) the insulin-stimulated insulin receptor kinase activity using histone or the beta-subunit of the insulin receptor as phosphoacceptors.	Glyburide	0-9	insulin receptor	Rattus norvegicus	209-225
2544783-4	1989	Glyburide"s actions were mediated without altering the following: (1) 125I-insulin binding; (2) the electrophoretic mobility of the affinity labeled alpha-subunit or the autophosphorylated beta-subunit of the insulin receptor; and (3) the insulin-stimulated insulin receptor kinase activity using histone or the beta-subunit of the insulin receptor as phosphoacceptors.	Glyburide	0-9	insulin receptor	Rattus norvegicus	258-274
2544783-4	1989	Glyburide"s actions were mediated without altering the following: (1) 125I-insulin binding; (2) the electrophoretic mobility of the affinity labeled alpha-subunit or the autophosphorylated beta-subunit of the insulin receptor; and (3) the insulin-stimulated insulin receptor kinase activity using histone or the beta-subunit of the insulin receptor as phosphoacceptors.	Glyburide	0-9	insulin receptor	Rattus norvegicus	258-274
2544783-5	1989	These data suggest that the action of sulfonylureas is distal to the insulin receptor tyrosine kinase.	Sulfonylurea Compounds	38-51	insulin receptor	Rattus norvegicus	69-85
2658980-9	1989	Free thiol groups in the insulin receptor and disulphide bonds between the alpha-subunits are not essential to this process.	Sulfhydryl Compounds	5-10	insulin receptor	Rattus norvegicus	25-41
2542282-8	1989	Moreover, MA-10 inhibits autophosphorylation and protein-tyrosine kinase activity of reduced and purified insulin receptor beta-subunits.	ma-10	10-15	insulin receptor	Rattus norvegicus	106-122
2542282-9	1989	The finding that MA-10 inhibits insulin-stimulated receptor autophosphorylation and reduces insulin-stimulated thymidine incorporation into DNA and receptor down-regulation suggests that the extracellular part of the insulin receptor beta-subunit plays a role in the regulation of insulin receptor protein-tyrosine kinase activity.	ma-10	17-22	insulin receptor	Rattus norvegicus	217-233
2542282-9	1989	The finding that MA-10 inhibits insulin-stimulated receptor autophosphorylation and reduces insulin-stimulated thymidine incorporation into DNA and receptor down-regulation suggests that the extracellular part of the insulin receptor beta-subunit plays a role in the regulation of insulin receptor protein-tyrosine kinase activity.	ma-10	17-22	insulin receptor	Rattus norvegicus	281-297
2542282-9	1989	The finding that MA-10 inhibits insulin-stimulated receptor autophosphorylation and reduces insulin-stimulated thymidine incorporation into DNA and receptor down-regulation suggests that the extracellular part of the insulin receptor beta-subunit plays a role in the regulation of insulin receptor protein-tyrosine kinase activity.	Thymidine	111-120	insulin receptor	Rattus norvegicus	217-233
2542282-1	1989	Anti-insulin receptor monoclonal antibody MA-10 inhibits insulin receptor autophosphorylation of purified rat liver insulin receptors without affecting insulin binding (Cordera, R., Andraghetti, G., Gherzi, R., Adezati, L., Montemurro, A., Lauro, R., Goldfine, I. D., and De Pirro, R. (1987) Endocrinology 121, 2007-2010).	ma-10	42-47	insulin receptor	Rattus norvegicus	5-21
2542282-1	1989	Anti-insulin receptor monoclonal antibody MA-10 inhibits insulin receptor autophosphorylation of purified rat liver insulin receptors without affecting insulin binding (Cordera, R., Andraghetti, G., Gherzi, R., Adezati, L., Montemurro, A., Lauro, R., Goldfine, I. D., and De Pirro, R. (1987) Endocrinology 121, 2007-2010).	ma-10	42-47	insulin receptor	Rattus norvegicus	57-73
2542282-2	1989	The effect of MA-10 on insulin receptor autophosphorylation and on two insulin actions (thymidine incorporation into DNA and receptor down-regulation) was investigated in rat hepatoma Fao cells.	ma-10	14-19	insulin receptor	Rattus norvegicus	23-39
2930502-2	1989	The presence of insulin receptor and its regulation by butyrate and other short-chain fatty acids was studied in C6 cells, a rat glioma cell line.	Butyrates	55-63	insulin receptor	Rattus norvegicus	16-32
2663568-0	1989	Polyamines in rat adipocytes: their localization and their effects on the insulin receptor binding.	Polyamines	0-10	insulin receptor	Rattus norvegicus	74-90
2663568-3	1989	Spermine (0.1-10 mM) dose-dependently enhanced the insulin receptor binding; at a concentration of 5-10 mM spermine the insulin binding was enhanced by 100% above control values.	Spermine	0-8	insulin receptor	Rattus norvegicus	51-67
2663568-3	1989	Spermine (0.1-10 mM) dose-dependently enhanced the insulin receptor binding; at a concentration of 5-10 mM spermine the insulin binding was enhanced by 100% above control values.	Spermine	107-115	insulin receptor	Rattus norvegicus	51-67
2543618-4	1989	Pretreatment of insulin with anti-insulin antibody or the cells with anti-insulin receptor sodium vanadate stimulated synthesis of this phospholipid in rat adipocytes.	Vanadates	91-106	insulin receptor	Rattus norvegicus	74-90
2543618-4	1989	Pretreatment of insulin with anti-insulin antibody or the cells with anti-insulin receptor sodium vanadate stimulated synthesis of this phospholipid in rat adipocytes.	Phospholipids	136-148	insulin receptor	Rattus norvegicus	74-90
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
2468661-6	1989	By phosphoamino acid analysis, all insulin- and Mn2+-dependent phosphorylation in the 95-kDa subunit of the insulin receptor was phosphotyrosine.	Phosphoamino Acids	3-20	insulin receptor	Rattus norvegicus	108-124
2468661-6	1989	By phosphoamino acid analysis, all insulin- and Mn2+-dependent phosphorylation in the 95-kDa subunit of the insulin receptor was phosphotyrosine.	Manganese(2+)	48-52	insulin receptor	Rattus norvegicus	108-124
2468661-6	1989	By phosphoamino acid analysis, all insulin- and Mn2+-dependent phosphorylation in the 95-kDa subunit of the insulin receptor was phosphotyrosine.	Phosphotyrosine	129-144	insulin receptor	Rattus norvegicus	108-124
2468661-8	1989	Dephosphorylation of the insulin receptor was examined by "chasing" labeled ATP after 2 min with a 40-fold excess of unlabeled ATP.	Adenosine Triphosphate	76-79	insulin receptor	Rattus norvegicus	25-41
2468661-8	1989	Dephosphorylation of the insulin receptor was examined by "chasing" labeled ATP after 2 min with a 40-fold excess of unlabeled ATP.	Adenosine Triphosphate	127-130	insulin receptor	Rattus norvegicus	25-41
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
2930502-2	1989	The presence of insulin receptor and its regulation by butyrate and other short-chain fatty acids was studied in C6 cells, a rat glioma cell line.	Fatty Acids, Volatile	74-97	insulin receptor	Rattus norvegicus	16-32
2535848-7	1989	When normalized to the same number of insulin receptors which are autophosphorylated to the same degree, the rat liver insulin receptor catalyzes the transfer of phosphate from ATP to three different substrates, on average, 2.8-fold quicker than receptor from human placenta.	Phosphates	162-171	insulin receptor	Rattus norvegicus	38-54
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
2718780-1	1989	The correlation of insulin receptor occupancy with classic insulin effects, such as stimulation of glucose uptake, have not been examined in osteoblastlike cells.	Glucose	99-106	insulin receptor	Rattus norvegicus	19-35
2643441-5	1989	The intracellularly located insulin receptor rapidly recycled to the plasma membrane at 37 degrees C. An endosomal compartment involved in both the endocytosis and subsequent recycling of [125I]insulin and the insulin receptor to the plasma membrane was identified on sucrose density floatation gradients.	Sucrose	268-275	insulin receptor	Rattus norvegicus	28-44
2643441-5	1989	The intracellularly located insulin receptor rapidly recycled to the plasma membrane at 37 degrees C. An endosomal compartment involved in both the endocytosis and subsequent recycling of [125I]insulin and the insulin receptor to the plasma membrane was identified on sucrose density floatation gradients.	Sucrose	268-275	insulin receptor	Rattus norvegicus	210-226
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
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
2535848-7	1989	When normalized to the same number of insulin receptors which are autophosphorylated to the same degree, the rat liver insulin receptor catalyzes the transfer of phosphate from ATP to three different substrates, on average, 2.8-fold quicker than receptor from human placenta.	Adenosine Triphosphate	177-180	insulin receptor	Rattus norvegicus	38-54
2484434-6	1989	As a whole our data indicate that the insulin receptor kinase is involved in the generation of an early (glucose transport) and late (aminoacid uptake) response to insulin.	Glucose	105-112	insulin receptor	Rattus norvegicus	38-54
2484434-7	1989	Further, conformational changes in phosphotyrosine containing domains of the insulin receptor appear to modulate insulin"s biological effects.	Phosphotyrosine	35-50	insulin receptor	Rattus norvegicus	77-93
2642422-9	1989	This is probably due to reduced affinity for the insulin receptor, since it had 2.5% of insulin"s ability to both bind to the receptor and stimulate glucose oxidation.	Glucose	149-156	insulin receptor	Rattus norvegicus	49-65
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.	Vanadates	0-8	insulin receptor	Rattus norvegicus	55-71
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
2462493-10	1989	Vanadate at 1 mM was more potent as an antilipolytic agent than 10(-9) M insulin (93% vs. 81%), yet increased tyrosine phosphorylation of the 95K insulin receptor beta-subunit only as effectively as 10(-10) M insulin (which inhibited lipolysis only 42%).	Vanadates	0-8	insulin receptor	Rattus norvegicus	146-162
2852008-4	1988	When compared at similar concentrations, 32P-labelled EGF receptor was dephosphorylated at greater than 3 times the rate of 32P-labelled insulin receptor; both dephosphorylations exhibited similar dependence on metal ions and calmodulin.	Phosphorus-32	41-44	insulin receptor	Rattus norvegicus	137-153
2910904-7	1989	The molecular weight of the insulin receptor beta subunit (by SDS-PAGE) was smaller in cells from diabetic than from normal rats (88-90 vs. 95 kD).	Sodium Dodecyl Sulfate	62-65	insulin receptor	Rattus norvegicus	28-44
2852008-4	1988	When compared at similar concentrations, 32P-labelled EGF receptor was dephosphorylated at greater than 3 times the rate of 32P-labelled insulin receptor; both dephosphorylations exhibited similar dependence on metal ions and calmodulin.	Phosphorus-32	124-127	insulin receptor	Rattus norvegicus	137-153
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
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	Sodium Dodecyl Sulfate	139-161	insulin receptor	Rattus norvegicus	30-46
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	Sodium Dodecyl Sulfate	139-161	insulin receptor	Rattus norvegicus	48-50
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	Sodium Dodecyl Sulfate	139-161	insulin receptor	Rattus norvegicus	68-70
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	polyacrylamide	162-176	insulin receptor	Rattus norvegicus	30-46
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	polyacrylamide	162-176	insulin receptor	Rattus norvegicus	48-50
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	polyacrylamide	162-176	insulin receptor	Rattus norvegicus	68-70
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	N-Acetylneuraminic Acid	214-225	insulin receptor	Rattus norvegicus	30-46
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	N-Acetylneuraminic Acid	214-225	insulin receptor	Rattus norvegicus	48-50
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	asparagine n-linked carbohydrate	241-273	insulin receptor	Rattus norvegicus	30-46
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	asparagine n-linked carbohydrate	241-273	insulin receptor	Rattus norvegicus	48-50
3060828-1	1988	Comparison of the adult brain insulin receptor (IR) to other tissue IR demonstrates that the former migrates approximately 10 kD faster on sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to deficient sialic acid content of the asparagine N-linked carbohydrate moieties.	asparagine n-linked carbohydrate	241-273	insulin receptor	Rattus norvegicus	68-70
3060828-4	1988	We further studied the specific brain cell types: neurons, glial cells, and purified microvessel preparation, and demonstrated a heterogeneity in the N-linked glycosylation of the IR within an organ (brain).	Nitrogen	150-151	insulin receptor	Rattus norvegicus	180-182
3060828-5	1988	The neuronal (approximately 125 kD) and microvascular (approximately 125 kD, approximately 135 kD) IR are deficient in sialic acid, thus conferring neuraminidase-insensitivity to the whole brain, whereas the glial cell IR, similar to the liver IR, exhibits neuraminidase sensitivity and migrates intermediate (approximately 128 kD) to the liver and brain IR.	N-Acetylneuraminic Acid	119-130	insulin receptor	Rattus norvegicus	99-101
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.	Dexamethasone	37-50	insulin receptor	Rattus norvegicus	153-169
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
2458910-5	1988	The degree of phosphorylation of the insulin receptor was decreased 34% by dexamethasone treatment compared to the control value when studied in fasted animals.	Dexamethasone	75-88	insulin receptor	Rattus norvegicus	37-53
2458910-7	1988	In addition, the beta-subunit of the insulin receptor extracted from dexamethasone-treated animals migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a slightly increased mobility compared to normal (89 +/- 1.2K vs. 92.5 +/- 0.4K).	Dexamethasone	69-82	insulin receptor	Rattus norvegicus	37-53
2458910-7	1988	In addition, the beta-subunit of the insulin receptor extracted from dexamethasone-treated animals migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a slightly increased mobility compared to normal (89 +/- 1.2K vs. 92.5 +/- 0.4K).	Sodium Dodecyl Sulfate	111-133	insulin receptor	Rattus norvegicus	37-53
2458910-7	1988	In addition, the beta-subunit of the insulin receptor extracted from dexamethasone-treated animals migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a slightly increased mobility compared to normal (89 +/- 1.2K vs. 92.5 +/- 0.4K).	polyacrylamide	134-148	insulin receptor	Rattus norvegicus	37-53
3052449-1	1988	When a highly purified preparation of rat liver insulin receptor is incubated with trypsin, the receptor develops hydrolytic activity towards N alpha-benzoyl-L-arginine ethyl ester, N alpha-p-tosyl-L-arginine methyl ester, and N alpha-benzoyl-DL-arginine-p-nitroanilide, (compounds which are synthetic substrates of trypsin).	n alpha-benzoyl-l-arginine ethyl ester	142-180	insulin receptor	Rattus norvegicus	48-64
3052449-1	1988	When a highly purified preparation of rat liver insulin receptor is incubated with trypsin, the receptor develops hydrolytic activity towards N alpha-benzoyl-L-arginine ethyl ester, N alpha-p-tosyl-L-arginine methyl ester, and N alpha-benzoyl-DL-arginine-p-nitroanilide, (compounds which are synthetic substrates of trypsin).	n alpha-p-tosyl-l-arginine methyl ester	182-221	insulin receptor	Rattus norvegicus	48-64
3052449-1	1988	When a highly purified preparation of rat liver insulin receptor is incubated with trypsin, the receptor develops hydrolytic activity towards N alpha-benzoyl-L-arginine ethyl ester, N alpha-p-tosyl-L-arginine methyl ester, and N alpha-benzoyl-DL-arginine-p-nitroanilide, (compounds which are synthetic substrates of trypsin).	n alpha-benzoyl-dl-arginine-p-nitroanilide	227-269	insulin receptor	Rattus norvegicus	48-64
3052449-3	1988	These data are consistent with the presence of proteolytic activity in the insulin receptor specific for the bonds whose carbonyl functions are provided by arginine but not by lysine.	Arginine	156-164	insulin receptor	Rattus norvegicus	75-91
2843408-7	1988	The study of glutamine-tyrosine (4:1) phosphorylation by the insulin-receptor kinase showed results similar to those of the autophosphorylation study.	glutamine-tyrosine	13-31	insulin receptor	Rattus norvegicus	61-77
3058459-7	1988	These results suggested that glucagon does not necessarily inhibit all of the insulin actions, and that the mechanism of insulin stimulation of glucose transport, which is supposed to be mediated by glucagon-sensitive insulin receptor, is different from those of insulin-induced antilipolysis, glucose oxidation, and lipogenesis.	Glucose	144-151	insulin receptor	Rattus norvegicus	218-234
2905679-2	1988	By exposing control and isoproterenol-treated cells to trypsin (0-150 micrograms/ml for 20 min at 4 degrees C) and measuring the intact insulin receptor pool following detergent solubilization, a differential sensitivity to proteolysis of the cell membrane receptor was observed.	Isoproterenol	24-37	insulin receptor	Rattus norvegicus	136-152
3149924-6	1988	These data indicate that insulin receptor-lipogenesis coupling in rat adipocytes is mediated by protein kinase C-elicited calcium influx and activation of calmodulin.	Calcium	122-129	insulin receptor	Rattus norvegicus	25-41
3417632-2	1988	In in vitro translation assays, the primary L-[35S]cysteine-labeled products of rat liver mRNA specifically immunoprecipitable with insulin receptor antiserum were two closely migrating polypeptides with a Mr range of 160,000-164,000 (n = 7).	l-[35s]cysteine	44-59	insulin receptor	Rattus norvegicus	132-148
3131113-0	1988	Developmental aspects of the rat brain insulin receptor: loss of sialic acid and fluctuation in number characterize fetal development.	N-Acetylneuraminic Acid	65-76	insulin receptor	Rattus norvegicus	39-55
3053388-6	1988	The low plasma insulin level and decreased number of insulin receptor are believed to be possible factors for the elevation of plasma glucose.	Glucose	134-141	insulin receptor	Rattus norvegicus	53-69
2901378-7	1988	These studies suggest, therefore, that metformin may influence cellular metabolism by potentiating certain insulin actions through mechanisms that may be beyond insulin receptor binding.	Metformin	39-48	insulin receptor	Rattus norvegicus	161-177
3064412-1	1988	Evaluation of insulin receptor state in lymphocytes of rats with burns trauma enabled to detect that impairment of carbohydrate metabolism in burns might be considerably dependent on content of insulin and the state of its receptors.	Carbohydrates	115-127	insulin receptor	Rattus norvegicus	14-30
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-37	insulin receptor	Rattus norvegicus	59-75
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-37	insulin receptor	Rattus norvegicus	148-164
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-36	insulin receptor	Rattus norvegicus	59-75
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-36	insulin receptor	Rattus norvegicus	148-164
3048393-1	1988	Elements of the quaternary structure of the native and dithiothreitol- (DTT) reduced rat adipocyte insulin receptor have been elucidated by vectorial probing and subunit cross-linking.	Dithiothreitol	55-69	insulin receptor	Rattus norvegicus	99-115
3048393-1	1988	Elements of the quaternary structure of the native and dithiothreitol- (DTT) reduced rat adipocyte insulin receptor have been elucidated by vectorial probing and subunit cross-linking.	Dithiothreitol	72-75	insulin receptor	Rattus norvegicus	99-115
3281950-0	1988	Internalized insulin-receptor complexes are unidirectionally translocated to chloroquine-sensitive degradative sites.	Chloroquine	77-88	insulin receptor	Rattus norvegicus	13-29
2843448-5	1988	However, basal insulin receptor kinase activity using Glu4: Tyrl as phospho-acceptor was decreased by T3 without altering its insulin responsiveness.	tyrl	60-64	insulin receptor	Rattus norvegicus	15-31
3125181-2	1988	Incubation of ortho[32P]phosphate-labeled Fao cells with TPA increased the phosphorylation of the insulin receptor 2-fold after 30 min.	Phosphorus-32	20-23	insulin receptor	Rattus norvegicus	98-114
2831899-4	1988	Dephosphorylation of the insulin receptor beta-subunit by rat liver membranes was inhibited by Zn+2, and stimulated by EDTA.	Zinc	95-99	insulin receptor	Rattus norvegicus	25-41
2831899-4	1988	Dephosphorylation of the insulin receptor beta-subunit by rat liver membranes was inhibited by Zn+2, and stimulated by EDTA.	Edetic Acid	119-123	insulin receptor	Rattus norvegicus	25-41
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
3125181-0	1988	Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity.	Phorbol Esters	0-13	insulin receptor	Rattus norvegicus	52-68
3125181-0	1988	Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity.	Serine	22-28	insulin receptor	Rattus norvegicus	52-68
3125181-1	1988	The effect of 12-O-tetradecanoylphorbol-13-acetate (TPA) on the function of the insulin receptor was examined in intact hepatoma cells (Fao) and in solubilized extracts purified by wheat germ agglutinin chromatography.	Tetradecanoylphorbol Acetate	14-50	insulin receptor	Rattus norvegicus	80-96
3125181-1	1988	The effect of 12-O-tetradecanoylphorbol-13-acetate (TPA) on the function of the insulin receptor was examined in intact hepatoma cells (Fao) and in solubilized extracts purified by wheat germ agglutinin chromatography.	Tetradecanoylphorbol Acetate	52-55	insulin receptor	Rattus norvegicus	80-96
3125181-2	1988	Incubation of ortho[32P]phosphate-labeled Fao cells with TPA increased the phosphorylation of the insulin receptor 2-fold after 30 min.	Phosphates	24-33	insulin receptor	Rattus norvegicus	98-114
3125181-2	1988	Incubation of ortho[32P]phosphate-labeled Fao cells with TPA increased the phosphorylation of the insulin receptor 2-fold after 30 min.	Tetradecanoylphorbol Acetate	57-60	insulin receptor	Rattus norvegicus	98-114
3125181-8	1988	TPA treatment also decreased the Km of the insulin receptor for ATP.	Tetradecanoylphorbol Acetate	0-3	insulin receptor	Rattus norvegicus	43-59
3125181-8	1988	TPA treatment also decreased the Km of the insulin receptor for ATP.	Adenosine Triphosphate	64-67	insulin receptor	Rattus norvegicus	43-59
3125181-9	1988	Incubation of the insulin receptor purified from TPA-treated cells with alkaline phosphatase decreased the phosphate content of the beta-subunit to the control level and reversed the inhibition, suggesting that the serine phosphorylation of the beta-subunit was responsible for the decreased tyrosine kinase activity.	Tetradecanoylphorbol Acetate	49-52	insulin receptor	Rattus norvegicus	18-34
3125181-9	1988	Incubation of the insulin receptor purified from TPA-treated cells with alkaline phosphatase decreased the phosphate content of the beta-subunit to the control level and reversed the inhibition, suggesting that the serine phosphorylation of the beta-subunit was responsible for the decreased tyrosine kinase activity.	Phosphates	107-116	insulin receptor	Rattus norvegicus	18-34
3125181-9	1988	Incubation of the insulin receptor purified from TPA-treated cells with alkaline phosphatase decreased the phosphate content of the beta-subunit to the control level and reversed the inhibition, suggesting that the serine phosphorylation of the beta-subunit was responsible for the decreased tyrosine kinase activity.	Serine	215-221	insulin receptor	Rattus norvegicus	18-34
3125181-10	1988	Our results support the notion that the insulin receptor is a substrate for protein kinase C in the Fao cell and that the increase in serine phosphorylation of the beta-subunit of the receptor produced by TPA treatment inhibited tyrosine kinase activity in vivo and in vitro.	Tetradecanoylphorbol Acetate	205-208	insulin receptor	Rattus norvegicus	40-56
2965579-1	1988	Two systems in vitro are described that show insulin-stimulated phosphorylation of the insulin receptor on serine residues.	Serine	107-113	insulin receptor	Rattus norvegicus	87-103
2833239-0	1988	Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells.	Hydrogen Peroxide	0-17	insulin receptor	Rattus norvegicus	61-77
2965579-2	1988	In the first system, insulin receptor was purified partially from Fao rat hepatoma cells by direct solubilization of the cells in Triton X-100 and chromatography on wheat-germ-agglutinin-agarose.	Octoxynol	130-142	insulin receptor	Rattus norvegicus	21-37
2965579-2	1988	In the first system, insulin receptor was purified partially from Fao rat hepatoma cells by direct solubilization of the cells in Triton X-100 and chromatography on wheat-germ-agglutinin-agarose.	Sepharose	187-194	insulin receptor	Rattus norvegicus	21-37
2965579-9	1988	Serine kinase activity in these preparations towards the insulin receptor was stimulated up to 10-fold by insulin, and the stoicheiometry of serine phosphorylation was estimated to be approx 0.8 mol/mol of insulin receptor for phosphorylations performed in the presence of insulin.	Serine	141-147	insulin receptor	Rattus norvegicus	206-222
2965579-10	1988	Thus a preparation of insulin receptor is described for the first time that is phosphorylated to high stoicheiometry on serine in an insulin-dependent manner.	Serine	120-126	insulin receptor	Rattus norvegicus	22-38
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
2449432-1	1988	We identified the major autophosphorylation sites in the insulin receptor and correlated their phosphorylation with the phosphotransferase activity of the receptor on synthetic peptides.	Peptides	177-185	insulin receptor	Rattus norvegicus	57-73
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.	Hydrogen Peroxide	41-45	insulin receptor	Rattus norvegicus	155-171
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.	Serine	99-105	insulin receptor	Rattus norvegicus	155-171
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
2833239-6	1988	These data suggest that in intact cell systems, H2O2 may increase the insulin receptor kinase activity by inducing phosphorylation of the beta subunit of insulin receptor.	Hydrogen Peroxide	48-52	insulin receptor	Rattus norvegicus	70-86
2833239-6	1988	These data suggest that in intact cell systems, H2O2 may increase the insulin receptor kinase activity by inducing phosphorylation of the beta subunit of insulin receptor.	Hydrogen Peroxide	48-52	insulin receptor	Rattus norvegicus	154-170
2453505-9	1988	The insulin receptor concentration, studied in parallel, remained practically constant in the investigated period in the presence and absence of digitonin.	Digitonin	145-154	insulin receptor	Rattus norvegicus	4-20
3325314-6	1987	From these results, it can be concluded that the onset of glucose-stimulated insulin secretion appears in fetal rats on D20 of gestation and the elevation of endogeneous insulin rapidly down-regulates the number of hepatic insulin receptor in fetal rats.	Glucose	58-65	insulin receptor	Rattus norvegicus	223-239
3076448-3	1988	[19-Tryptophan-A]insulin displays 4.1 +/- 1.9% of the potency of natural insulin in binding to the insulin receptor from rat liver plasma membranes, 5.0 +/- 2.3% in stimulating lipogenesis in rat adipocytes, and 75.7 +/- 4% of the potency of insulin in radioimmunoassay.	19-tryptophan-a	1-16	insulin receptor	Rattus norvegicus	99-115
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
3315745-8	1987	These results suggested that insulin stimulates the generation of lysophosphatidylinositol 4-phosphate through the insulin-receptor interaction.	lysophosphatidylinositol 4-phosphate	66-102	insulin receptor	Rattus norvegicus	115-131
3317401-0	1987	Role of insulin receptor phosphorylation in the insulinomimetic effects of hydrogen peroxide.	Hydrogen Peroxide	75-92	insulin receptor	Rattus norvegicus	8-24
3317401-2	1987	To determine whether these effects could be mediated by the tyrosine kinase activity of the insulin receptor, the ability of H2O2 to stimulate receptor phosphorylation in intact adipocytes and partially purified insulin receptors has been examined.	Hydrogen Peroxide	125-129	insulin receptor	Rattus norvegicus	92-108
3317401-3	1987	Phosphorylation of the beta subunit of the insulin receptor was increased approximately 2-fold by treatment of intact cells with 3 mM H2O2, a concentration that maximally stimulates 2-deoxyglucose uptake.	Hydrogen Peroxide	134-138	insulin receptor	Rattus norvegicus	43-59
3317401-3	1987	Phosphorylation of the beta subunit of the insulin receptor was increased approximately 2-fold by treatment of intact cells with 3 mM H2O2, a concentration that maximally stimulates 2-deoxyglucose uptake.	Deoxyglucose	182-196	insulin receptor	Rattus norvegicus	43-59
3317401-7	1987	In contrast, the direct addition of H2O2 to partially purified insulin receptors did not stimulate tyrosine kinase activity or insulin receptor autophosphorylation.	Hydrogen Peroxide	36-40	insulin receptor	Rattus norvegicus	63-79
3317401-11	1987	These data demonstrate that, under certain conditions, H2O2 stimulates insulin receptor phosphorylation and tyrosine kinase activity, suggesting that the insulin-like effects of H2O2 may be mediated by stimulation of insulin receptor phosphorylation.	Hydrogen Peroxide	55-59	insulin receptor	Rattus norvegicus	71-87
3317401-11	1987	These data demonstrate that, under certain conditions, H2O2 stimulates insulin receptor phosphorylation and tyrosine kinase activity, suggesting that the insulin-like effects of H2O2 may be mediated by stimulation of insulin receptor phosphorylation.	Hydrogen Peroxide	55-59	insulin receptor	Rattus norvegicus	217-233
3317401-11	1987	These data demonstrate that, under certain conditions, H2O2 stimulates insulin receptor phosphorylation and tyrosine kinase activity, suggesting that the insulin-like effects of H2O2 may be mediated by stimulation of insulin receptor phosphorylation.	Hydrogen Peroxide	178-182	insulin receptor	Rattus norvegicus	71-87
3317401-11	1987	These data demonstrate that, under certain conditions, H2O2 stimulates insulin receptor phosphorylation and tyrosine kinase activity, suggesting that the insulin-like effects of H2O2 may be mediated by stimulation of insulin receptor phosphorylation.	Hydrogen Peroxide	178-182	insulin receptor	Rattus norvegicus	217-233
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.	Serine	80-86	insulin receptor	Rattus norvegicus	123-139
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
2484715-10	1987	Dexamethasone treatment increased the content of the two insulin receptor mRNAs in rat liver by 2-fold.	Dexamethasone	0-13	insulin receptor	Rattus norvegicus	57-73
3315362-6	1987	On the basis of these parameters it is suggested that this group is a histidine residue on the surface of the insulin receptor.	Histidine	70-79	insulin receptor	Rattus norvegicus	110-126
3323092-2	1987	Hydrogen bonding involving peptide bonds of the backbone of the insulin molecule may play an important role in insulin-receptor interaction.	Hydrogen	0-8	insulin receptor	Rattus norvegicus	111-127
3323092-4	1987	To investigate the possible involvement of peptide bonds of this segment in insulin-receptor interaction the [2-N-methylisoleucine-A]insulin and [3-N-methylvaline-A]insulin ([MeIle2-A]- and [MeVal3-A]insulins) were synthesized.	[2-n-methylisoleucine-a	109-132	insulin receptor	Rattus norvegicus	76-92
3323092-4	1987	To investigate the possible involvement of peptide bonds of this segment in insulin-receptor interaction the [2-N-methylisoleucine-A]insulin and [3-N-methylvaline-A]insulin ([MeIle2-A]- and [MeVal3-A]insulins) were synthesized.	[3-n-methylvaline-a	145-164	insulin receptor	Rattus norvegicus	76-92
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
2822510-1	1987	The effect of a polyclonal anti-insulin receptor antibody (pIgG) on the insulin receptor tyrosine kinase (IRTK) activity toward poly-(Glu-Tyr) was examined using wheat germ agglutinin agarose-purified insulin receptors from rat liver membranes.	poly-(glu-tyr	128-141	insulin receptor	Rattus norvegicus	32-48
2822510-1	1987	The effect of a polyclonal anti-insulin receptor antibody (pIgG) on the insulin receptor tyrosine kinase (IRTK) activity toward poly-(Glu-Tyr) was examined using wheat germ agglutinin agarose-purified insulin receptors from rat liver membranes.	poly-(glu-tyr	128-141	insulin receptor	Rattus norvegicus	72-88
2822510-1	1987	The effect of a polyclonal anti-insulin receptor antibody (pIgG) on the insulin receptor tyrosine kinase (IRTK) activity toward poly-(Glu-Tyr) was examined using wheat germ agglutinin agarose-purified insulin receptors from rat liver membranes.	Sepharose	184-191	insulin receptor	Rattus norvegicus	32-48
2822510-1	1987	The effect of a polyclonal anti-insulin receptor antibody (pIgG) on the insulin receptor tyrosine kinase (IRTK) activity toward poly-(Glu-Tyr) was examined using wheat germ agglutinin agarose-purified insulin receptors from rat liver membranes.	Sepharose	184-191	insulin receptor	Rattus norvegicus	72-88
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
3569675-3	1987	In addition, in AR42J cultured rat pancreatic acinar cells, dexamethasone increased insulin-receptor mRNA levels.	Dexamethasone	60-73	insulin receptor	Rattus norvegicus	84-100
2438282-7	1987	Concanavalin A and hydrogen peroxide mimic insulin stimulation of the insulin receptor kinase and enhance the tyrosine phosphorylation of P160.	Hydrogen Peroxide	19-36	insulin receptor	Rattus norvegicus	70-86
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
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
2953724-11	1987	In contrast, in glial cells, IGF-I stimulated 2-deoxyglucose uptake at very high doses, presumably acting via the insulin receptor.	Deoxyglucose	46-60	insulin receptor	Rattus norvegicus	114-130
3310150-7	1987	These results suggest the possible involvement of a metal ion present in the receptor in the formation of the insulin-receptor complex.	Metals	52-57	insulin receptor	Rattus norvegicus	110-126
3295472-8	1987	These studies demonstrate that the sulfonylurea, chlorpropamide, stimulates glucose transport and potentiates insulin"s effect on this process by acting at a site(s) beyond insulin receptor binding and phosphorylation.	Sulfonylurea Compounds	35-47	insulin receptor	Rattus norvegicus	173-189
3295472-8	1987	These studies demonstrate that the sulfonylurea, chlorpropamide, stimulates glucose transport and potentiates insulin"s effect on this process by acting at a site(s) beyond insulin receptor binding and phosphorylation.	Chlorpropamide	49-63	insulin receptor	Rattus norvegicus	173-189
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
3106355-0	1987	Regulation of insulin receptor internalization in vascular endothelial cells by insulin and phorbol ester.	Phorbol Esters	92-105	insulin receptor	Rattus norvegicus	14-30
3106355-1	1987	Phorbol 12-myristate 13-acetate (PMA) was used to examine the role of insulin receptor phosphorylation in the regulation of insulin receptor internalization in vascular endothelial cells.	Tetradecanoylphorbol Acetate	0-31	insulin receptor	Rattus norvegicus	124-140
3106355-5	1987	Internalization of 125I-labeled insulin receptor was determined by the resistance of labeled receptor to trypsinization.	Iodine-125	19-23	insulin receptor	Rattus norvegicus	32-48
3106355-9	1987	When surfaced-labeled cells were preincubated with PMA at 37 degrees C, the rate of insulin receptor internalization was increased by 3.6 +/- 0.2-fold and 2.1 +/- 0.5-fold at 1 and 5 min of insulin exposure, respectively (ED50 at 16 nM PMA).	Tetradecanoylphorbol Acetate	51-54	insulin receptor	Rattus norvegicus	84-100
3106355-9	1987	When surfaced-labeled cells were preincubated with PMA at 37 degrees C, the rate of insulin receptor internalization was increased by 3.6 +/- 0.2-fold and 2.1 +/- 0.5-fold at 1 and 5 min of insulin exposure, respectively (ED50 at 16 nM PMA).	Tetradecanoylphorbol Acetate	236-239	insulin receptor	Rattus norvegicus	84-100
3106355-10	1987	This effect of PMA was associated with an increase in serine phosphorylation of the insulin receptor.	Serine	54-60	insulin receptor	Rattus norvegicus	84-100
3106355-12	1987	The additive effects of PMA and insulin on insulin receptor phosphorylation suggest that the phorbol ester and insulin act via independent signaling mechanisms.	Phorbol Esters	93-106	insulin receptor	Rattus norvegicus	43-59
3304334-0	1987	Generation of oligomeric insulin receptor forms by intramolecular sulfhydryl-disulfide exchange.	sulfhydryl-disulfide	66-86	insulin receptor	Rattus norvegicus	25-41
3304334-9	1987	These results suggest, that the generation of different oligomeric receptor forms detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis is due at least in part to the cleavage of one or both beta-subunits from the insulin receptor.	Sodium Dodecyl Sulfate	94-116	insulin receptor	Rattus norvegicus	230-246
3304334-9	1987	These results suggest, that the generation of different oligomeric receptor forms detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis is due at least in part to the cleavage of one or both beta-subunits from the insulin receptor.	polyacrylamide gels	117-135	insulin receptor	Rattus norvegicus	230-246
3022736-0	1986	Insulin receptor autophosphorylation and kinase activity in streptozotocin diabetic rats.	Streptozocin	60-74	insulin receptor	Rattus norvegicus	0-16
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
3022736-2	1986	Insulin receptor associated kinase activity and its relationships with the insulin resistance of streptozotocin-induced diabetes were investigated in rats, using solubilized, partially purified insulin receptors from liver membranes.	Streptozocin	97-111	insulin receptor	Rattus norvegicus	0-16
3022736-7	1986	Our findings suggest that streptozotocin diabetes is associated with a reduction of insulin receptor kinase activity, which a short fast is not able to reverse.	Streptozocin	26-40	insulin receptor	Rattus norvegicus	84-100
3522388-5	1986	These results support the conclusion that pretreatment of fat cells with phospholipid vesicles inhibits normal insulin receptor cycling.	Phospholipids	73-85	insulin receptor	Rattus norvegicus	111-127
2430467-2	1986	To characterize this type of insulin resistance, autophosphorylation and kinase activity of the insulin receptor on liver was studied with streptozotocin (STZ)-induced and BB diabetic rats.	Streptozocin	139-153	insulin receptor	Rattus norvegicus	96-112
2430467-2	1986	To characterize this type of insulin resistance, autophosphorylation and kinase activity of the insulin receptor on liver was studied with streptozotocin (STZ)-induced and BB diabetic rats.	Streptozocin	155-158	insulin receptor	Rattus norvegicus	96-112
2430467-2	1986	To characterize this type of insulin resistance, autophosphorylation and kinase activity of the insulin receptor on liver was studied with streptozotocin (STZ)-induced and BB diabetic rats.	boeravinone B	172-174	insulin receptor	Rattus norvegicus	96-112
2430467-5	1986	By contrast, insulin-stimulated autophosphorylation of the beta-subunit of the insulin receptor was decreased in proportion to the severity of the diabetic state in the STZ rat.	Streptozocin	169-172	insulin receptor	Rattus norvegicus	79-95
2430467-8	1986	In the BB rat, autophosphorylation and kinase activity of the insulin receptor were both decreased in the diabetic state and partially normalized by insulin treatment.	boeravinone B	7-9	insulin receptor	Rattus norvegicus	62-78
2430467-11	1986	This protein is immunologically distinct from the insulin receptor, but is rich in phosphotyrosine.	Phosphotyrosine	83-98	insulin receptor	Rattus norvegicus	50-66
3817337-0	1986	Effects of metformin on insulin receptor tyrosine kinase activity in rat adipocytes.	Metformin	11-20	insulin receptor	Rattus norvegicus	24-40
3092812-0	1986	A thiol-sensitive degradative process of liver uncouples autophosphorylation of the insulin receptor from insulin binding.	Sulfhydryl Compounds	2-7	insulin receptor	Rattus norvegicus	84-100
3092812-6	1986	Thus a thiol-sensitive, cation-dependent, degrading activity has been identified that can uncouple the insulin-binding activity of the plasma-membrane insulin receptor from its tyrosine kinase activity.	Sulfhydryl Compounds	7-12	insulin receptor	Rattus norvegicus	151-167
3530836-1	1986	When the insulin receptor is tagged with a 125I-photoreactive insulin analogue that can be covalently coupled to it by UV irradiation, the fate of this labeled receptor can be followed both morphologically and biochemically.	Iodine-125	43-47	insulin receptor	Rattus norvegicus	9-25
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
3516226-1	1986	The bimolecular binding reaction between mono[TyrA14-125I]iodoinsulin and the insulin receptor was investigated at 37 degrees C in intact isolated rat adipocytes in which membrane traffic was inhibited by 1 mM KCN.	Potassium Cyanide	210-213	insulin receptor	Rattus norvegicus	78-94
3007472-8	1986	It is proposed that: in intact cells, insulin causes alterations in insulin receptors, such that their kinase activity toward non-receptor substrates increases; increased insulin receptor kinase activity following insulin stimulation in intact cells is, at least in part, the result of an increased phosphate content of the receptors; and effects of insulin on insulin receptors in intact cells can be preserved during receptor isolation and thus can be measured in a cell-free system.	Phosphates	299-308	insulin receptor	Rattus norvegicus	68-84
2421778-7	1986	These data suggest that the stabilization of the subunit structure of the insulin receptor at physiological temperatures may take place via a disulfide interchange reaction catalyzed by glutathione-insulin transhydrogenase.	Disulfides	142-151	insulin receptor	Rattus norvegicus	74-90
3957914-1	1986	The phosphorylation characteristics of insulin receptor from control and insulin-treated rat H-35 hepatoma cells 32P-labeled to equilibrium have been documented.	Phosphorus-32	113-116	insulin receptor	Rattus norvegicus	39-55
3957914-2	1986	The 32P-labeled insulin receptor is isolated by immunoprecipitation with patient-derived insulin receptor antibodies in the presence of phosphatase and protease inhibitors to preserve the native phosphorylation and structural characteristics of the receptor.	Phosphorus-32	4-7	insulin receptor	Rattus norvegicus	16-32
3957914-3	1986	The unstimulated insulin receptor contains predominantly [32P] phosphoserine and trace amounts of [32P]phosphothreonine in its beta subunit.	Phosphorus-32	58-61	insulin receptor	Rattus norvegicus	17-33
3957914-3	1986	The unstimulated insulin receptor contains predominantly [32P] phosphoserine and trace amounts of [32P]phosphothreonine in its beta subunit.	Phosphoserine	63-76	insulin receptor	Rattus norvegicus	17-33
3957914-3	1986	The unstimulated insulin receptor contains predominantly [32P] phosphoserine and trace amounts of [32P]phosphothreonine in its beta subunit.	Phosphorus-32	99-102	insulin receptor	Rattus norvegicus	17-33
3957914-3	1986	The unstimulated insulin receptor contains predominantly [32P] phosphoserine and trace amounts of [32P]phosphothreonine in its beta subunit.	Phosphothreonine	103-119	insulin receptor	Rattus norvegicus	17-33
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
3957914-4	1986	In response to insulin, the insulin receptor beta subunit exhibits marked tyrosine phosphorylation and a 2-fold increase in total [32P]phosphoserine contents.	Phosphorus-32	131-134	insulin receptor	Rattus norvegicus	28-44
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.	Phosphoserine	135-148	insulin receptor	Rattus norvegicus	28-44
3957914-8	1986	The elevated kinase activity of the insulin receptor derived from insulin-treated cells is not due to the presence of hormone bound to the receptor because the receptor kinase activity is assayed while immobilized on insulin-agarose.	Sepharose	225-232	insulin receptor	Rattus norvegicus	36-52
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
3005303-0	1986	Tumor-promoting phorbol esters increase the Km of the ATP-binding site of the insulin receptor kinase from rat adipocytes.	Phorbol Esters	16-30	insulin receptor	Rattus norvegicus	78-94
3005303-0	1986	Tumor-promoting phorbol esters increase the Km of the ATP-binding site of the insulin receptor kinase from rat adipocytes.	Adenosine Triphosphate	54-57	insulin receptor	Rattus norvegicus	78-94
3005303-3	1986	Insulin receptor of tetradecanoyl-beta-phorbol acetate (TPA)-treated adipocytes was solubilized and partially purified, and its kinase activity was studied in vitro.	Tetradecanoylphorbol Acetate	20-54	insulin receptor	Rattus norvegicus	0-16
3521589-0	1986	Evidence that insulin and guanosine triphosphate regulate dephosphorylation of the beta-subunit of the insulin receptor in sarcolemma membranes isolated from skeletal muscle.	Guanosine Triphosphate	26-48	insulin receptor	Rattus norvegicus	103-119
3005303-3	1986	Insulin receptor of tetradecanoyl-beta-phorbol acetate (TPA)-treated adipocytes was solubilized and partially purified, and its kinase activity was studied in vitro.	Tetradecanoylphorbol Acetate	56-59	insulin receptor	Rattus norvegicus	0-16
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
3521589-1	1986	When sarcolemma membranes isolated from rat skeletal muscle were incubated with [gamma-32P]ATP, a membrane protein of apparent Mr 95,000 was rapidly phosphorylated, with the 32P content reaching a maximum within 2 s. On the basis of immunoprecipitation with anti-insulin-receptor antiserum, phosphoamino acid analysis and Mr, this protein probably represents the beta-subunit of the insulin receptor.	[gamma-32p]atp	80-94	insulin receptor	Rattus norvegicus	263-279
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.	Tetradecanoylphorbol Acetate	112-115	insulin receptor	Rattus norvegicus	83-99
3521589-1	1986	When sarcolemma membranes isolated from rat skeletal muscle were incubated with [gamma-32P]ATP, a membrane protein of apparent Mr 95,000 was rapidly phosphorylated, with the 32P content reaching a maximum within 2 s. On the basis of immunoprecipitation with anti-insulin-receptor antiserum, phosphoamino acid analysis and Mr, this protein probably represents the beta-subunit of the insulin receptor.	[gamma-32p]atp	80-94	insulin receptor	Rattus norvegicus	383-399
3005303-11	1986	We conclude from the data that phorbol treatment of rat adipocytes modulates the kinase activity of the insulin receptor by increasing its Km for ATP and that this is part of a mechanism leading to insulin resistance in these cells.	phorbol	31-38	insulin receptor	Rattus norvegicus	104-120
3521589-2	1986	Similarly, on incubation of the membrane with adenosine 5"-[gamma-[35S]thio] triphosphate the 95 kDa protein was thiophosphorylated, indicating thiophosphorylation of the beta-subunit of the insulin receptor on the basis of immunoprecipitation studies.	adenosine 5"-[gamma-[35s]thio] triphosphate	46-89	insulin receptor	Rattus norvegicus	191-207
3005303-11	1986	We conclude from the data that phorbol treatment of rat adipocytes modulates the kinase activity of the insulin receptor by increasing its Km for ATP and that this is part of a mechanism leading to insulin resistance in these cells.	Adenosine Triphosphate	146-149	insulin receptor	Rattus norvegicus	104-120
3521589-10	1986	The possibility that GTP-regulatory proteins are involved in the action of insulin on the phosphorylation of the insulin receptor and other membrane proteins is discussed.	Guanosine Triphosphate	21-24	insulin receptor	Rattus norvegicus	113-129
3513608-7	1986	Sodium orthovanadate (3 mM), a phosphotyrosyl-protein phosphatase inhibitor, also inhibited the increase in insulin binding due to E, implying that E may increase insulin binding by activating a phosphotyrosyl-protein phosphatase which decreases the phosphorylation of a plasma membrane protein, presumably the insulin receptor.	Sodium orthovanadate	0-20	insulin receptor	Rattus norvegicus	311-327
3518707-0	1986	Decreased tyrosine kinase activity of insulin receptor isolated from rat adipocytes rendered insulin-resistant by catecholamine treatment in vitro.	Catecholamines	114-127	insulin receptor	Rattus norvegicus	38-54
3518707-3	1986	To find whether the receptor kinase is modified by catecholamines, we solubilized and partially purified the insulin receptor of isoprenaline-treated adipocytes and studied the effect of insulin on its kinase activity.	Isoproterenol	129-141	insulin receptor	Rattus norvegicus	109-125
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
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.	Catecholamines	91-104	insulin receptor	Rattus norvegicus	62-78
3518707-7	1986	The insulin receptor from catecholamine treated cells bound 25-50% of the amount of insulin bound by the receptor from control cells at insulin concentrations of 10 pM-0.1 muM.	Catecholamines	26-39	insulin receptor	Rattus norvegicus	4-20
3518707-8	1986	Part of the impaired insulin-responsiveness of the receptor kinase of catecholamine-treated cells is therefore explained by impaired binding properties; however, an additional inhibition of the kinase activity of the insulin receptor from catecholamine-treated cells is evident.	Catecholamines	70-83	insulin receptor	Rattus norvegicus	217-233
3518707-8	1986	Part of the impaired insulin-responsiveness of the receptor kinase of catecholamine-treated cells is therefore explained by impaired binding properties; however, an additional inhibition of the kinase activity of the insulin receptor from catecholamine-treated cells is evident.	Catecholamines	239-252	insulin receptor	Rattus norvegicus	217-233
3518707-13	1986	(5) We conclude from the data that catecholamine treatment of rat adipocytes modulates the kinase activity of the insulin receptor by increasing its Km for ATP and that this is part of the mechanism leading to insulin-resistance in these cells.	Catecholamines	35-48	insulin receptor	Rattus norvegicus	114-130
3518707-13	1986	(5) We conclude from the data that catecholamine treatment of rat adipocytes modulates the kinase activity of the insulin receptor by increasing its Km for ATP and that this is part of the mechanism leading to insulin-resistance in these cells.	Adenosine Triphosphate	156-159	insulin receptor	Rattus norvegicus	114-130
3512551-4	1986	The acidtropic agents chloroquine and dibucaine, which have been reported to inhibit the recycling of various receptors, were utilized to study the detailed translocation mechanism of the glucose transporter and the insulin receptor.	Chloroquine	22-33	insulin receptor	Rattus norvegicus	216-232
3512551-4	1986	The acidtropic agents chloroquine and dibucaine, which have been reported to inhibit the recycling of various receptors, were utilized to study the detailed translocation mechanism of the glucose transporter and the insulin receptor.	Dibucaine	38-47	insulin receptor	Rattus norvegicus	216-232
3933576-2	1985	Insulin receptor number was increased in a dose-dependent fashion by dexamethasone added to the medium between 24 and 48 h of culture and reduced by insulin, whereas ligand affinity remained unaltered.	Dexamethasone	69-82	insulin receptor	Rattus norvegicus	0-16
3530111-0	1986	Effects of the type of dietary fatty acid on the insulin receptor function in rat epididymal fat cells.	dietary fatty acid	23-41	insulin receptor	Rattus norvegicus	49-65
3910028-4	1985	These different metabolic responses could be related to the different pattern of insulin-receptor phosphorylation caused by insulin and vanadate.	Vanadates	136-144	insulin receptor	Rattus norvegicus	81-97
3909828-1	1985	Glucose ingestion has been previously shown to rapidly increase both the affinity of the insulin receptor and the cellular sensitivity of target tissues for insulin.	Glucose	0-7	insulin receptor	Rattus norvegicus	89-105
3910030-11	1985	The inhibitory effect of chloroquine on the deactivation may indicate that the insulin-receptor complex can function even after internalization.	Chloroquine	25-36	insulin receptor	Rattus norvegicus	79-95
3904001-3	1985	Preparations enriched in the insulin receptor and calmodulin-binding proteins were isolated from detergent-solubilized rat adipocyte membranes by chromatography with wheat germ agglutinin agarose and calmodulin-conjugated Sepharose, respectively.	Sepharose	188-195	insulin receptor	Rattus norvegicus	29-45
2995376-2	1985	Insulin receptor kinase activity was measured in partially purified receptor preparations from livers of rats fed a standard diet or subjected to either prolonged fasting or a high carbohydrate (CHO) diet, conditions known to decrease (fasting) and increase (CHO) insulin action.	Carbohydrates	181-193	insulin receptor	Rattus norvegicus	0-16
3904001-4	1985	Substantial purification of a manganese-dependent, insulin-sensitive phosphoprotein of 95K identified as the beta subunit of the insulin receptor was accomplished.	Manganese	30-39	insulin receptor	Rattus norvegicus	129-145
3904001-5	1985	Binding and photocovalent cross-linking of iodine-125-labeled calmodulin to these affinity-purified preparations and to isolated plasma membranes, followed by immunoadsorption with insulin receptor antibodies bound to protein A Sepharose, resulted in significant purification of a binding complex of 110K to 140K.	Sepharose	228-237	insulin receptor	Rattus norvegicus	181-197
3900295-5	1985	The presence of an "adipocyte" form of the insulin receptor in clonal cells derived from brain is probably a consequence of transformation and results from more extensive oligosaccharide processing of the 115K receptor expressed in normal brain cells.	Oligosaccharides	171-186	insulin receptor	Rattus norvegicus	43-59
3935910-0	1985	Inhibition of insulin receptor phosphorylation by indomethacin.	Indomethacin	50-62	insulin receptor	Rattus norvegicus	14-30
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
3935910-2	1985	We report that indomethacin inhibited the phosphorylation of the beta-subunit of the solubilized adipocyte insulin receptor.	Indomethacin	15-27	insulin receptor	Rattus norvegicus	107-123
3935910-4	1985	Indomethacin (1 mM) inhibited basal phosphorylation of the beta-subunit of the solubilized insulin receptor by 60% and insulin-stimulated phosphorylation by 30%.	Indomethacin	0-12	insulin receptor	Rattus norvegicus	91-107
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.	Indomethacin	6-18	insulin receptor	Rattus norvegicus	78-94
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
2995376-2	1985	Insulin receptor kinase activity was measured in partially purified receptor preparations from livers of rats fed a standard diet or subjected to either prolonged fasting or a high carbohydrate (CHO) diet, conditions known to decrease (fasting) and increase (CHO) insulin action.	CAV protocol	195-198	insulin receptor	Rattus norvegicus	0-16
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
3907718-1	1985	Using a 125I-photoreactive insulin analogue that can be covalently coupled to its receptor we have shown that in rat hepatocytes the insulin receptor is concomitantly internalized with the labeled hormone and afterwards is progressively recycled back to the cell surface.	Iodine-125	8-12	insulin receptor	Rattus norvegicus	133-149
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
3000458-9	1985	Insulin receptor partially purified by specific immunoprecipitation from detergent extracts of control and isoproterenol-treated cells have similar basal but diminished insulin-stimulated beta subunit autophosphorylation activities when incubated with [gamma-32 P]ATP.	Isoproterenol	107-120	insulin receptor	Rattus norvegicus	0-16
3000458-9	1985	Insulin receptor partially purified by specific immunoprecipitation from detergent extracts of control and isoproterenol-treated cells have similar basal but diminished insulin-stimulated beta subunit autophosphorylation activities when incubated with [gamma-32 P]ATP.	[gamma-32 p]	252-264	insulin receptor	Rattus norvegicus	0-16
3000458-9	1985	Insulin receptor partially purified by specific immunoprecipitation from detergent extracts of control and isoproterenol-treated cells have similar basal but diminished insulin-stimulated beta subunit autophosphorylation activities when incubated with [gamma-32 P]ATP.	Adenosine Triphosphate	264-267	insulin receptor	Rattus norvegicus	0-16
3000458-10	1985	Similarly, the ability of insulin to stimulate the receptor beta subunit phosphorylation in intact isoproterenol-treated adipocytes is greatly attenuated, whereas, the basal phosphorylation of the insulin receptor is slightly increased by the beta-catecholamine.	beta-catecholamine	243-261	insulin receptor	Rattus norvegicus	197-213
3000458-12	1985	Treatment of 32P-labeled H-35 hepatoma cells with phorbol myristate acetate (PMA) results in a marked increase in serine phosphorylation of the insulin receptor beta subunit.	Phosphorus-32	13-16	insulin receptor	Rattus norvegicus	144-160
3000458-12	1985	Treatment of 32P-labeled H-35 hepatoma cells with phorbol myristate acetate (PMA) results in a marked increase in serine phosphorylation of the insulin receptor beta subunit.	Tetradecanoylphorbol Acetate	50-75	insulin receptor	Rattus norvegicus	144-160
3000458-12	1985	Treatment of 32P-labeled H-35 hepatoma cells with phorbol myristate acetate (PMA) results in a marked increase in serine phosphorylation of the insulin receptor beta subunit.	Tetradecanoylphorbol Acetate	77-80	insulin receptor	Rattus norvegicus	144-160
3000458-12	1985	Treatment of 32P-labeled H-35 hepatoma cells with phorbol myristate acetate (PMA) results in a marked increase in serine phosphorylation of the insulin receptor beta subunit.	Serine	114-120	insulin receptor	Rattus norvegicus	144-160
3848433-2	1985	Tryptic peptides containing the phosphorylation sites of the beta-subunit of the insulin receptor were analyzed by reverse-phase high performance liquid chromatography.	Peptides	8-16	insulin receptor	Rattus norvegicus	81-97
3931462-0	1985	Effect of glyburide on in vivo recycling of the hepatic insulin receptor.	Glyburide	10-19	insulin receptor	Rattus norvegicus	56-72
3931462-2	1985	In these studies, a novel technique was used to examine the influence of glyburide on in vivo cycling of the hepatic insulin receptor.	Glyburide	73-82	insulin receptor	Rattus norvegicus	117-133
3931462-9	1985	This suggests that sulfonylureas potentiate the action of insulin either by increasing the dwell time of insulin on its receptor or by affecting an intracellular event that delays the recycling of the insulin receptor back to the cell surface plasma membrane.	Sulfonylurea Compounds	19-32	insulin receptor	Rattus norvegicus	201-217
3899805-9	1985	These data suggest that the chloroquine-accumulating, high-density compartment of hepatic Golgi fractions is the site of dissociation of internalized insulin-receptor complexes before degradation of the ligand and receptor recycling.	Chloroquine	28-39	insulin receptor	Rattus norvegicus	150-166
3848433-8	1985	When the insulin receptor was extracted from the Fao cells and incubated in vitro with [gamma-32P]ATP and Mn2+, very little phosphorylation occurred in the absence of insulin.	[gamma-32p]atp	87-101	insulin receptor	Rattus norvegicus	9-25
3848433-8	1985	When the insulin receptor was extracted from the Fao cells and incubated in vitro with [gamma-32P]ATP and Mn2+, very little phosphorylation occurred in the absence of insulin.	Manganese(2+)	106-110	insulin receptor	Rattus norvegicus	9-25
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
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
2581963-1	1985	Anti-phosphotyrosine antibody and anti-insulin receptor antibody were used to study insulin-stimulated phosphorylation of the beta-subunit of the insulin receptor in [32P]orthophosphate-labeled Fao hepatoma cells.	Phosphotyrosine	5-20	insulin receptor	Rattus norvegicus	146-162
3894560-1	1985	Cortisol implants in normal and diabetic rats reduced body weight, adiposity, insulin receptor concentration and both basal and insulin-stimulated rates of lipogenesis in isolated adipocytes, whilst insulin sensitivity was unchanged.	Hydrocortisone	0-8	insulin receptor	Rattus norvegicus	78-94
3894560-5	1985	The results suggest that cortisol inhibits lipogenesis in adipose tissue without affecting insulin sensitivity, cortisol reduces insulin binding in adipose tissue without a requirement for hyperinsulinaemia, which might itself indirectly lead to down-regulation of the insulin receptor, and in diabetic rats progesterone stimulates lipogenesis in adipose tissue without any increase in food intake or serum insulin concentrations suggesting that progesterone may have a direct anabolic role in adipose tissue.	Hydrocortisone	112-120	insulin receptor	Rattus norvegicus	269-285
3894560-5	1985	The results suggest that cortisol inhibits lipogenesis in adipose tissue without affecting insulin sensitivity, cortisol reduces insulin binding in adipose tissue without a requirement for hyperinsulinaemia, which might itself indirectly lead to down-regulation of the insulin receptor, and in diabetic rats progesterone stimulates lipogenesis in adipose tissue without any increase in food intake or serum insulin concentrations suggesting that progesterone may have a direct anabolic role in adipose tissue.	Progesterone	308-320	insulin receptor	Rattus norvegicus	269-285
3894420-0	1985	Insulin receptor down-regulation is linked to an insulin-induced postreceptor defect in the glucose transport system in rat adipocytes.	Glucose	92-99	insulin receptor	Rattus norvegicus	0-16
2581963-1	1985	Anti-phosphotyrosine antibody and anti-insulin receptor antibody were used to study insulin-stimulated phosphorylation of the beta-subunit of the insulin receptor in [32P]orthophosphate-labeled Fao hepatoma cells.	Phosphorus-32	167-170	insulin receptor	Rattus norvegicus	146-162
2581963-1	1985	Anti-phosphotyrosine antibody and anti-insulin receptor antibody were used to study insulin-stimulated phosphorylation of the beta-subunit of the insulin receptor in [32P]orthophosphate-labeled Fao hepatoma cells.	Phosphates	171-185	insulin receptor	Rattus norvegicus	146-162
2581963-8	1985	These results confirm our notion that insulin initially stimulated tyrosine autophosphorylation and subsequently serine phosphorylation of the insulin receptor in intact cells and suggests that this sequence of reactions occurs faster on receptors that are dephosphorylated before the incubation with insulin.	Serine	113-119	insulin receptor	Rattus norvegicus	143-159
3890451-0	1985	Is copper effect on glucose incorporation mediated by the insulin receptor in rat adipose tissue?	Glucose	20-27	insulin receptor	Rattus norvegicus	58-74
4046209-7	1985	Chloroquine apparently increases insulin binding to cells in vitro, and this is due to the effect of chloroquine on insulin-receptor recyclization to which lysosome contributes [16, 31, 32]; this drug inhibits the function of lysosome which digests insulin-receptor complexes and eventually insulin bound to its receptors is accumulated in intracellular compartments.	Chloroquine	0-11	insulin receptor	Rattus norvegicus	116-132
4046209-7	1985	Chloroquine apparently increases insulin binding to cells in vitro, and this is due to the effect of chloroquine on insulin-receptor recyclization to which lysosome contributes [16, 31, 32]; this drug inhibits the function of lysosome which digests insulin-receptor complexes and eventually insulin bound to its receptors is accumulated in intracellular compartments.	Chloroquine	0-11	insulin receptor	Rattus norvegicus	249-265
4046209-7	1985	Chloroquine apparently increases insulin binding to cells in vitro, and this is due to the effect of chloroquine on insulin-receptor recyclization to which lysosome contributes [16, 31, 32]; this drug inhibits the function of lysosome which digests insulin-receptor complexes and eventually insulin bound to its receptors is accumulated in intracellular compartments.	Chloroquine	101-112	insulin receptor	Rattus norvegicus	116-132
4046209-7	1985	Chloroquine apparently increases insulin binding to cells in vitro, and this is due to the effect of chloroquine on insulin-receptor recyclization to which lysosome contributes [16, 31, 32]; this drug inhibits the function of lysosome which digests insulin-receptor complexes and eventually insulin bound to its receptors is accumulated in intracellular compartments.	Chloroquine	101-112	insulin receptor	Rattus norvegicus	249-265
3884603-13	1985	Based on these observations and on the reported biological effects of monensin, it is suggested (a) that monensin may induce intracellular accumulation of the insulin-receptor complex by blocking the acidification of endocytic vesicles and (b) that the accumulated insulin-receptor complex may retain a weak, but significant, capacity to stimulate both glucose transport and phosphodiesterase activities.	Monensin	70-78	insulin receptor	Rattus norvegicus	159-175
3884603-13	1985	Based on these observations and on the reported biological effects of monensin, it is suggested (a) that monensin may induce intracellular accumulation of the insulin-receptor complex by blocking the acidification of endocytic vesicles and (b) that the accumulated insulin-receptor complex may retain a weak, but significant, capacity to stimulate both glucose transport and phosphodiesterase activities.	Monensin	105-113	insulin receptor	Rattus norvegicus	159-175
3884603-13	1985	Based on these observations and on the reported biological effects of monensin, it is suggested (a) that monensin may induce intracellular accumulation of the insulin-receptor complex by blocking the acidification of endocytic vesicles and (b) that the accumulated insulin-receptor complex may retain a weak, but significant, capacity to stimulate both glucose transport and phosphodiesterase activities.	Monensin	105-113	insulin receptor	Rattus norvegicus	265-281
3884603-13	1985	Based on these observations and on the reported biological effects of monensin, it is suggested (a) that monensin may induce intracellular accumulation of the insulin-receptor complex by blocking the acidification of endocytic vesicles and (b) that the accumulated insulin-receptor complex may retain a weak, but significant, capacity to stimulate both glucose transport and phosphodiesterase activities.	Glucose	353-360	insulin receptor	Rattus norvegicus	159-175
3884603-13	1985	Based on these observations and on the reported biological effects of monensin, it is suggested (a) that monensin may induce intracellular accumulation of the insulin-receptor complex by blocking the acidification of endocytic vesicles and (b) that the accumulated insulin-receptor complex may retain a weak, but significant, capacity to stimulate both glucose transport and phosphodiesterase activities.	Glucose	353-360	insulin receptor	Rattus norvegicus	265-281
3890451-0	1985	Is copper effect on glucose incorporation mediated by the insulin receptor in rat adipose tissue?	Copper	3-9	insulin receptor	Rattus norvegicus	58-74
3890451-5	1985	In addition to its previously noted effect on the in vivo insulin release, copper increased the number of the insulin receptor sites in adipocytes.	Copper	75-81	insulin receptor	Rattus norvegicus	110-126
3893876-3	1985	The results suggest that the insulin receptor on rat adipocytes contains sialic acid in its carbohydrate moiety but does not possess non-reducing alpha-D-galactopyranosyl or 2-acetamido-2-deoxy-alpha-D-galactopyranosyl end groups.	N-Acetylneuraminic Acid	73-84	insulin receptor	Rattus norvegicus	29-45
3893876-3	1985	The results suggest that the insulin receptor on rat adipocytes contains sialic acid in its carbohydrate moiety but does not possess non-reducing alpha-D-galactopyranosyl or 2-acetamido-2-deoxy-alpha-D-galactopyranosyl end groups.	Carbohydrates	92-104	insulin receptor	Rattus norvegicus	29-45
3003353-2	1985	At concentration 0.05% Triton X-100 decreased the insulin receptor binding by 15% and the EGF receptor binding by 70% as compared to controls.	Octoxynol	23-35	insulin receptor	Rattus norvegicus	50-66
3880538-11	1985	In conjunction with our previous observations in vivo, we conclude that 1) estradiol in vitro can decrease (down-regulate) insulin receptors on the plasma membrane of R3230AC mammary tumors; 2) the steroid may reduce degradation of internalized [125I]insulin; and 3) the steroid may enhance insulin receptor reappearance after insulin down-regulation.	Estradiol	75-84	insulin receptor	Rattus norvegicus	123-139
3880538-11	1985	In conjunction with our previous observations in vivo, we conclude that 1) estradiol in vitro can decrease (down-regulate) insulin receptors on the plasma membrane of R3230AC mammary tumors; 2) the steroid may reduce degradation of internalized [125I]insulin; and 3) the steroid may enhance insulin receptor reappearance after insulin down-regulation.	Steroids	198-205	insulin receptor	Rattus norvegicus	123-139
6393128-0	1984	Phorbol esters modulate insulin receptor phosphorylation and insulin action in cultured hepatoma cells.	Phorbol Esters	0-14	insulin receptor	Rattus norvegicus	24-40
6393128-3	1984	PMA (1 microgram/ml) stimulated the phosphorylation of the beta subunit of insulin receptor purified from [32P]phosphate-labeled Fao cells by 1.3-fold in the absence of insulin.	Tetradecanoylphorbol Acetate	0-3	insulin receptor	Rattus norvegicus	75-91
6393128-3	1984	PMA (1 microgram/ml) stimulated the phosphorylation of the beta subunit of insulin receptor purified from [32P]phosphate-labeled Fao cells by 1.3-fold in the absence of insulin.	Phosphorus-32	107-110	insulin receptor	Rattus norvegicus	75-91
6393128-3	1984	PMA (1 microgram/ml) stimulated the phosphorylation of the beta subunit of insulin receptor purified from [32P]phosphate-labeled Fao cells by 1.3-fold in the absence of insulin.	Phosphates	111-120	insulin receptor	Rattus norvegicus	75-91
6393128-9	1984	This report shows that phorbol esters stimulate insulin receptor phosphorylation, inhibit insulin-induced receptor phosphorylation and insulin action, and suggest a physiologic relation between insulin action and the calcium-activated and phospholipid-dependent protein kinase C.	Phorbol Esters	23-37	insulin receptor	Rattus norvegicus	48-64
6389099-0	1984	Increased affinity of insulin receptor on hepatocytes from streptozotocin-induced diabetic rats.	Streptozocin	59-73	insulin receptor	Rattus norvegicus	22-38
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
6387048-7	1984	These results indicate that the insulin receptor in brain is distinguished from those in peripheral tissues by structural alterations, including changes in the carbohydrate moiety of the receptor.	Carbohydrates	160-172	insulin receptor	Rattus norvegicus	32-48
6383574-2	1984	This report provides evidence that the 40 A insulin receptor migrates on dodecyl sulfate - acrylamide gel electrophoresis as a 90 000 dalton protein and that this protein is a single polypeptide chain.	dodecyl sulfate	73-88	insulin receptor	Rattus norvegicus	44-60
6383574-2	1984	This report provides evidence that the 40 A insulin receptor migrates on dodecyl sulfate - acrylamide gel electrophoresis as a 90 000 dalton protein and that this protein is a single polypeptide chain.	Acrylamide	91-101	insulin receptor	Rattus norvegicus	44-60
6389544-0	1984	Decreased autophosphorylation of the insulin receptor-kinase in streptozotocin-diabetic rats.	Streptozocin	64-78	insulin receptor	Rattus norvegicus	37-53
6381501-10	1984	A similar decrease of the oligomeric forms of the insulin receptor and an increase in the free subunits was observed when normal Fao cells are treated with 7 mM dithiothreitol.	Dithiothreitol	161-175	insulin receptor	Rattus norvegicus	50-66
6381501-15	1984	In the native state, the insulin receptor consists of free alpha and beta subunits and several kinds of disulfide-linked oligomers of these subunits.	Disulfides	104-113	insulin receptor	Rattus norvegicus	25-41
6694560-6	1984	These data suggest that: (1) The insulin resistance of the glucose-perfused diabetic heart results from two different post-insulin-receptor defects.	Glucose	59-66	insulin receptor	Rattus norvegicus	123-139
6745484-5	1984	The results show that the native insulin receptor exists under different forms: free alpha and beta subunits and the following combinations of disulphide-linked oligomers: alpha beta, alpha 2, alpha 2 beta and alpha 2 beta 2.	disulphide	143-153	insulin receptor	Rattus norvegicus	33-49
6373760-12	1984	From these observations, we conclude that 1) internalization is not rate-limiting in insulin receptor degradation, 2) chloroquine has no effect on the internalization of insulin receptors but inhibits the intracellular degradation of receptors, 3) cycloheximide interferes with both the internalization and degradation of insulin receptors, and 4) the plateau in the loss of labeled receptors from the cell surface after 60 min at 37 degrees C could be due to a new steady state balance between internalization and recycling of photoaffinity-labeled receptors.	Cycloheximide	248-261	insulin receptor	Rattus norvegicus	322-346
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-p-tosyl-l-arginine methyl ester	6-45	insulin receptor	Rattus norvegicus	180-196
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-p-tosyl-l-arginine methyl ester	6-45	insulin receptor	Rattus norvegicus	226-242
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-p-tosyl-l-arginine methyl ester	6-45	insulin receptor	Rattus norvegicus	226-242
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-benzoyl-l-arginine ethyl ester	49-87	insulin receptor	Rattus norvegicus	180-196
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-benzoyl-l-arginine ethyl ester	49-87	insulin receptor	Rattus norvegicus	226-242
6370244-1	1984	Added N alpha-p-tosyl-l-arginine methyl ester or N alpha-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta.	n alpha-benzoyl-l-arginine ethyl ester	49-87	insulin receptor	Rattus norvegicus	226-242
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
6370738-0	1984	[Ornid but not atropine abolishes the insulin receptor reaction of fat and liver plasma membranes to fasting and hyperinsulinemia].	Bretylium Tosylate	1-6	insulin receptor	Rattus norvegicus	38-54
6385156-0	1984	[Possible effect of bromocriptine on the insulin receptor].	Bromocriptine	20-33	insulin receptor	Rattus norvegicus	41-58
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.	Vanadates	0-8	insulin receptor	Rattus norvegicus	76-92
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.	Vanadates	0-8	insulin receptor	Rattus norvegicus	161-177
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
6427220-10	1984	These results demonstrate that vanadate enhances the phosphorylation of the insulin receptor by stimulating the kinase reaction in a similar but not identical manner to insulin.	Vanadates	31-39	insulin receptor	Rattus norvegicus	76-92
6367041-1	1984	An antiserum to the insulin receptor mimicked insulin"s acute actions on glucose transport, phosphorylation of integral membrane proteins, and internalization of the insulin receptor in isolated rat adipose cells.	Glucose	73-80	insulin receptor	Rattus norvegicus	20-36
6321495-3	1984	A native insulin receptor species with apparent Mr = 350,000 in soleus muscle is revealed by affinity cross-linking to 125I-insulin with disuccinimidyl suberate.	disuccinimidyl	137-151	insulin receptor	Rattus norvegicus	9-25
6321495-6	1984	The stimulatory action of native insulin is closely related to its ability to inhibit the labeling of the insulin receptor by 125I-insulin such that the uptake of xylose and AIB is maximally stimulated when 80% of insulin receptor 125I-affinity labeling is inhibited.	Xylose	163-169	insulin receptor	Rattus norvegicus	106-122
6321495-6	1984	The stimulatory action of native insulin is closely related to its ability to inhibit the labeling of the insulin receptor by 125I-insulin such that the uptake of xylose and AIB is maximally stimulated when 80% of insulin receptor 125I-affinity labeling is inhibited.	Xylose	163-169	insulin receptor	Rattus norvegicus	214-230
6321495-7	1984	In contrast, MSA only displaced 16% of the 125I-labeling of the insulin receptor when it maximally stimulates the uptake of xylose and AIB, indicating that the insulin receptor is not primarily involved in mediating these effects.	Xylose	124-130	insulin receptor	Rattus norvegicus	64-80
6480047-0	1984	Effect of carbon tetrachloride induced toxicity on 125(I)-insulin receptor interaction and U-14(C)glucose/U-14(C)galactose homeostasis in isolated rat hepatocytes.	Carbon Tetrachloride	10-30	insulin receptor	Rattus norvegicus	58-74
6358216-0	1983	Dexamethasone stimulates insulin receptor synthesis in cultured rat hepatocytes.	Dexamethasone	0-13	insulin receptor	Rattus norvegicus	25-41
6368536-2	1984	Incubation of this receptor preparation with [gamma-32P] ATP, Mn2+, and insulin yielded a single insulin-stimulated phosphoprotein of Mr = 95,000 which corresponds to the beta-subunit of the insulin receptor.	[gamma-32p	45-55	insulin receptor	Rattus norvegicus	191-207
6368536-2	1984	Incubation of this receptor preparation with [gamma-32P] ATP, Mn2+, and insulin yielded a single insulin-stimulated phosphoprotein of Mr = 95,000 which corresponds to the beta-subunit of the insulin receptor.	Adenosine Triphosphate	57-60	insulin receptor	Rattus norvegicus	191-207
6368536-2	1984	Incubation of this receptor preparation with [gamma-32P] ATP, Mn2+, and insulin yielded a single insulin-stimulated phosphoprotein of Mr = 95,000 which corresponds to the beta-subunit of the insulin receptor.	Manganese(2+)	62-66	insulin receptor	Rattus norvegicus	191-207
6368260-1	1984	Insulin receptor interaction was examined in fatty plasma membranes of rats given adrenaline hydrochloride for 6 days in a dose producing a 10-20-fold increase in adrenaline excretion.	Epinephrine	82-106	insulin receptor	Rattus norvegicus	0-16
6358216-1	1983	The ability of the glucocorticoid dexamethasone to modulate the insulin receptor was examined directly in primary cultures of hepatocytes prepared from adult male rats.	Dexamethasone	34-47	insulin receptor	Rattus norvegicus	64-80
6358216-3	1983	The exposure of hepatocytes to dexamethasone resulted in a time-dependent (steady state by 32 h) increase in insulin binding in both intact hepatocytes and Triton X-100-soluble extracts (total insulin receptor content).	Dexamethasone	31-44	insulin receptor	Rattus norvegicus	193-209
6358216-4	1983	The enhanced insulin binding found in soluble extracts of dexamethasone-treated hepatocytes was the result of an increase in insulin receptor number without a change in receptor affinity.	Dexamethasone	58-71	insulin receptor	Rattus norvegicus	125-141
6358216-5	1983	In order to assess the mechanism by which dexamethasone "up-regulates" the insulin receptor, the heavy isotope density-shift technique was used to analyze insulin receptor turnover in control and dexamethasone-treated hepatocytes.	Dexamethasone	42-55	insulin receptor	Rattus norvegicus	75-91
6358216-5	1983	In order to assess the mechanism by which dexamethasone "up-regulates" the insulin receptor, the heavy isotope density-shift technique was used to analyze insulin receptor turnover in control and dexamethasone-treated hepatocytes.	Dexamethasone	42-55	insulin receptor	Rattus norvegicus	155-171
6355127-2	1983	Tris(hydroxymethyl)aminomethane and other nonamphoteric amines were found to selectively impair insulin receptor recycling while leaving the insulin-degradative pathway intact.	Tromethamine	0-31	insulin receptor	Rattus norvegicus	96-112
6355127-2	1983	Tris(hydroxymethyl)aminomethane and other nonamphoteric amines were found to selectively impair insulin receptor recycling while leaving the insulin-degradative pathway intact.	Amines	56-62	insulin receptor	Rattus norvegicus	96-112
6134722-10	1983	The decrease in the insulin receptor-binding activity is physiologically expressed as a dose-dependent decrease of insulin responsiveness in the adipocyte with respect to two known responses, stimulation of insulin-like growth factor II receptor binding and activation of the glucose-transport system.	Glucose	276-283	insulin receptor	Rattus norvegicus	20-36
6354263-4	1983	In stimulating labeled glucose incorporation into lipids in rat fat cells, the analogue displayed 33.2% potency relative to insulin; receptor binding affinity for the analogue was 15.9% in rat liver membranes and 17.8% in isolated fat cells.	Glucose	23-30	insulin receptor	Rattus norvegicus	124-141
6351850-0	1983	Calcium-dependence of insulin receptor phosphorylation.	Calcium	0-7	insulin receptor	Rattus norvegicus	22-38
6351850-3	1983	Autoradiography of solubilized immunoprecipitated membrane protein after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that most of the 32P incorporation occurred in a band corresponding to Mr 95 000, which has been identified previously as the beta-subunit of the insulin receptor.	Phosphorus-32	158-161	insulin receptor	Rattus norvegicus	287-303
6351631-1	1983	We have examined the effect of insulin and tunicamycin, which cause decreases in cell surface insulin receptor numbers in peripheral tissues, on insulin receptors in neuron-enriched brain cell cultures.	Tunicamycin	43-54	insulin receptor	Rattus norvegicus	94-110
6351848-0	1983	Reversible reduction of insulin receptor affinity by ATP depletion in rat adipocytes.	Adenosine Triphosphate	53-56	insulin receptor	Rattus norvegicus	24-40
6351848-8	1983	It is suggested that the observed ATP-dependence of insulin receptor affinity reflects a reversible structural alteration of the receptor, or of some closely related membrane protein.	Adenosine Triphosphate	34-37	insulin receptor	Rattus norvegicus	52-68
6849985-2	1983	Bacitracin has been used in insulin-receptor studies to inhibit extracellular degradation of 125I-labelled insulin.	Bacitracin	0-10	insulin receptor	Rattus norvegicus	28-44
6849985-2	1983	Bacitracin has been used in insulin-receptor studies to inhibit extracellular degradation of 125I-labelled insulin.	Iodine-125	93-97	insulin receptor	Rattus norvegicus	28-44
6849985-3	1983	The aim of this study was to investigate bacitracin"s effect on 125I-labelled insulin-receptor interactions in isolated rat hepatocytes.	Bacitracin	41-51	insulin receptor	Rattus norvegicus	78-94
6849985-3	1983	The aim of this study was to investigate bacitracin"s effect on 125I-labelled insulin-receptor interactions in isolated rat hepatocytes.	Iodine-125	64-68	insulin receptor	Rattus norvegicus	78-94
6339507-2	1983	A photoactive insulin analogue (N epsilon-B29-(2-nitro-4-azidophenylacetyl)insulin) which specifically and covalently labels the 138-kDa insulin receptor subunit, is used here to examine the effect of insulin on the subcellular distribution of insulin receptors in the isolated rat adipose cell.	2-nitro-4-azidophenylacetyl)	47-75	insulin receptor	Rattus norvegicus	137-153
6407485-0	1983	Insulin-like effect of vanadate on adipocyte glycogen synthase and on phosphorylation of 95,000 dalton subunit of insulin receptor.	Vanadates	23-31	insulin receptor	Rattus norvegicus	114-130
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.	Vanadates	0-8	insulin receptor	Rattus norvegicus	85-101
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.	Vanadates	0-8	insulin receptor	Rattus norvegicus	170-186
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
6137754-9	1983	These data support our previous suggestion, based on in vitro studies, that sulfonylureas act predominately on processes beyond the binding portion of the insulin receptor.	Sulfonylurea Compounds	76-89	insulin receptor	Rattus norvegicus	155-171
6341991-4	1983	NaDodSO(4)/polyacrylamide gel electrophoretic analysis of the immunoprecipitates under reducing conditions revealed autophosphorylation of the beta subunit (M(r) 95,000) of the insulin receptor; the alpha subunit (M(r) 130,000) was not phosphorylated.	nadodso(4)	0-10	insulin receptor	Rattus norvegicus	177-193
6339486-2	1983	In solubilized, (wheat germ) lectin-purified preparations of rat liver membranes, insulin stimulated the incorporation of 32P from [gamma-32P]ATP into tyrosine residues of insulin receptor, casein, and histones.	Phosphorus-32	122-125	insulin receptor	Rattus norvegicus	172-188
6339486-5	1983	Dephosphorylation of the insulin receptor to 20% of original 32P content only occurred when alkaline phosphatase was added to the preparations.	Phosphorus-32	61-64	insulin receptor	Rattus norvegicus	25-41
6341991-4	1983	NaDodSO(4)/polyacrylamide gel electrophoretic analysis of the immunoprecipitates under reducing conditions revealed autophosphorylation of the beta subunit (M(r) 95,000) of the insulin receptor; the alpha subunit (M(r) 130,000) was not phosphorylated.	polyacrylamide	11-25	insulin receptor	Rattus norvegicus	177-193
6341991-6	1983	To localize more precisely the insulin receptor-related kinase activity, we searched for an ATP-binding site on solubilized insulin receptors.	Adenosine Triphosphate	92-95	insulin receptor	Rattus norvegicus	31-47
6341991-7	1983	By using covalent labeling with oxidized [alpha-(32)P]ATP, a labeled polypeptide with precisely the same electrophoretic mobility as that of the beta subunit of the insulin receptor (M(r) 95,000) was specifically immunoprecipitated with anti-receptor antibodies.	[alpha-(32)p]atp	41-57	insulin receptor	Rattus norvegicus	165-181
6341991-9	1983	In conclusion, we have shown that an insulin-stimulated phosphorylation site and an ATP-binding site coexist on the beta subunit of the insulin receptor.	Adenosine Triphosphate	84-87	insulin receptor	Rattus norvegicus	136-152
6361517-6	1983	The results suggest that (a) theophylline impairs insulin action at a post-receptor level and, at higher concentrations, by a decrease of receptor binding, (b) the reduction of insulin receptor affinity probably reflects ATP depletion of the adipocyte, and (c) the xanthine inhibits glucose transport independently from its effects on lipolysis.	Adenosine Triphosphate	221-224	insulin receptor	Rattus norvegicus	177-193
6756473-0	1982	Modification of the insulin receptor by diethyl pyrocarbonate: effect on insulin binding and action.	Diethyl Pyrocarbonate	40-61	insulin receptor	Rattus norvegicus	20-36
6293588-8	1982	Tolbutamide continued to activate the enzyme in cells in which insulin receptor had been destroyed by trypsin-pretreatment.	Tolbutamide	0-11	insulin receptor	Rattus norvegicus	63-79
6759915-9	1982	The results suggest that adenosine modulates insulin action at a step distal from the insulin receptor, and before, or at, the glucose transport system.	Adenosine	25-34	insulin receptor	Rattus norvegicus	86-102
6757032-1	1982	Using the photoreactive, biologically active insulin analogue, B2-(2 nitro, 4-azidophenylacetyl)des-PheB1 insulin, which can be covalently bound to receptor molecules upon photolysis, the insulin receptor has been studied in three different types of cells or tissues: isolated rat hepatocytes, intact murine soleus muscle and cultured human lymphocytes.	b2-(2 nitro, 4-azidophenylacetyl	63-95	insulin receptor	Rattus norvegicus	188-204
7052124-0	1982	Kinetic relationships between insulin receptor binding and effects on glucose transport in isolated rat adipocytes.	Glucose	70-77	insulin receptor	Rattus norvegicus	30-46
6179940-2	1982	Rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits were identified by immunoprecipitation and sodium dodecyl sulfate-acrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	134-156	insulin receptor	Rattus norvegicus	65-81
7052124-1	1982	The role of insulin receptor occupancy in the stimulation of glucose transport has been studied in isolated rat adipocytes.	Glucose	61-68	insulin receptor	Rattus norvegicus	12-28
7051001-8	1982	These studies show that insulin-receptor complexes are internalized and processed intracellularly at a chloroquine-sensitive site(s).	Chloroquine	103-114	insulin receptor	Rattus norvegicus	24-40
429330-11	1979	It proposes that the effects of the exogenously added glycosides (and Con A) may reflect the presence on the membrane of a native carbohydrate moiety by either mimicking or competitively inhibiting its ability to interact reversibly with a lectin-like carbohydrate binding site associated with the function of the insulin receptor.20	Glycosides	54-64	insulin receptor	Rattus norvegicus	314-330
6274858-9	1982	Fab fragment prepared from anti-insulin receptor IgG completely blocked the stimulation of [35S]sulfate incorporation into macromolecules by insulin while only partially inhibiting the biologic response to insulin-like growth factors, MSA, IGF-I, and IGF-II.	Sulfur-35	92-95	insulin receptor	Rattus norvegicus	32-48
6274858-9	1982	Fab fragment prepared from anti-insulin receptor IgG completely blocked the stimulation of [35S]sulfate incorporation into macromolecules by insulin while only partially inhibiting the biologic response to insulin-like growth factors, MSA, IGF-I, and IGF-II.	Sulfates	96-103	insulin receptor	Rattus norvegicus	32-48
7025891-0	1981	Hydrodynamic characterization of the photoaffinity-labeled insulin receptor solubilized in Triton X-100.	Octoxynol	91-103	insulin receptor	Rattus norvegicus	59-75
7025891-1	1981	The insulin receptor in isolated rat liver plasma membranes was covalently labeled with the photoreactive insulin analogue NB-29-[(4-azido-2-nitrophenyl)acetyl]insulin and solubilized with the nondenaturing detergent Triton X-100.	nb-29-[(4-azido-2-nitrophenyl)acetyl]insulin	123-167	insulin receptor	Rattus norvegicus	4-20
7025891-1	1981	The insulin receptor in isolated rat liver plasma membranes was covalently labeled with the photoreactive insulin analogue NB-29-[(4-azido-2-nitrophenyl)acetyl]insulin and solubilized with the nondenaturing detergent Triton X-100.	Octoxynol	217-229	insulin receptor	Rattus norvegicus	4-20
7025891-8	1981	These results indicate that the solubilized receptor binds significant amounts of detergents, that the insulin binding component of the receptor binds to other receptor components by hydrophobic interactions, and that one or more components of the insulin receptor contain intrachain disulfide bonds.	Disulfides	284-293	insulin receptor	Rattus norvegicus	248-264
6780189-0	1981	Insulin receptor levels and magnitude of insulin-induced responses in 7,12-dimethylbenz(a)anthracene-induced mammary tumors in rats.	7,12-dimethylbenz	70-87	insulin receptor	Rattus norvegicus	0-16
6780189-0	1981	Insulin receptor levels and magnitude of insulin-induced responses in 7,12-dimethylbenz(a)anthracene-induced mammary tumors in rats.	anthracene	90-100	insulin receptor	Rattus norvegicus	0-16
7011799-4	1981	These findings add further support to the concept that the insulin-like growth factors act on glucose metabolism and antilipolysis via the insulin receptor of the adipocyte.	Glucose	94-101	insulin receptor	Rattus norvegicus	139-155
7045094-0	1982	Role of disulfides in the subunit structure of the insulin receptor.	Disulfides	8-18	insulin receptor	Rattus norvegicus	51-67
7045094-2	1982	The native insulin receptor affinity-labeled by covalent cross-linking to 125I-insulin has been proposed to consist of two alpha receptor subunits and two beta-receptor subunits all disulfide-linked as a Mr = 350,000 (beta-S-S-alpha)-S-S-(alpha-S-S-beta) receptor complex (Massague, J., Pilch, P. F., and Czech, M. P. (1981) J. Biol.	Disulfides	182-191	insulin receptor	Rattus norvegicus	11-27
7045094-5	1982	We denote the disulfide bonds linking the two symmetrical (alpha-S-S-beta) receptor halves as class I insulin receptor disulfides, whereas the disulfide bonds linking one alpha receptor subunit to one beta receptor subunit are termed class II disulfides.	Disulfides	14-23	insulin receptor	Rattus norvegicus	102-118
7045094-7	1982	Reduction of class I insulin receptor disulfides did not prevent binding of insulin to the insulin receptor.	Disulfides	38-48	insulin receptor	Rattus norvegicus	21-37
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Disulfides	26-36	insulin receptor	Rattus norvegicus	9-25
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Dithiothreitol	59-73	insulin receptor	Rattus norvegicus	9-25
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Dithiothreitol	59-73	insulin receptor	Rattus norvegicus	105-121
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	125-147	insulin receptor	Rattus norvegicus	9-25
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Sodium Dodecyl Sulfate	125-147	insulin receptor	Rattus norvegicus	105-121
7045094-12	1982	Class I insulin receptor disulfides were partially reoxidized by an incubation mixture consisting of reduced and oxidized glutathione.	Disulfides	25-35	insulin receptor	Rattus norvegicus	8-24
7045094-12	1982	Class I insulin receptor disulfides were partially reoxidized by an incubation mixture consisting of reduced and oxidized glutathione.	Glutathione	122-133	insulin receptor	Rattus norvegicus	8-24
7045094-13	1982	When solubilized insulin receptor containing reduced class I disulfides was exposed to ethylene glycol bis(succinimidyl succinate), the receptor subunits were internally cross-linked and migrated like intact receptor complexes on nonreduced dodecyl sulfate gels.	Disulfides	61-71	insulin receptor	Rattus norvegicus	17-33
7045094-13	1982	When solubilized insulin receptor containing reduced class I disulfides was exposed to ethylene glycol bis(succinimidyl succinate), the receptor subunits were internally cross-linked and migrated like intact receptor complexes on nonreduced dodecyl sulfate gels.	ethylene glycolylbis(succinimidyl succinate)	87-129	insulin receptor	Rattus norvegicus	17-33
7045094-13	1982	When solubilized insulin receptor containing reduced class I disulfides was exposed to ethylene glycol bis(succinimidyl succinate), the receptor subunits were internally cross-linked and migrated like intact receptor complexes on nonreduced dodecyl sulfate gels.	dodecyl sulfate	241-256	insulin receptor	Rattus norvegicus	17-33
7039360-0	1982	Relation of insulin receptor occupancy and deactivation of glucose transport.	Glucose	59-66	insulin receptor	Rattus norvegicus	12-28
7032318-6	1981	The changes in insulin-stimulated hexose uptake following interaction of adipocytes with DOPC-PS vesicles were accompanied by alterations in the Vmax of the uptake process and in affinity of insulin binding, although the similar ED50 values of the control and vesicle-treated groups suggest that the observed effects on insulin sensitivity may be mediated by an uncoupling of the insulin receptor from transport activation.	Hexoses	34-40	insulin receptor	Rattus norvegicus	380-396
6793421-9	1981	They suggest that, in rat adipocytes, a glycosidic moiety participates in the insulin-receptor interaction through N-linked oligosaccharides of the "complex type".	n-linked oligosaccharides	115-140	insulin receptor	Rattus norvegicus	78-94
7004966-6	1980	Thus, in the early stage of high glucose feeding, insulin receptor number, and insulin sensitivity of glucose uptake, and insulin responsiveness of glucose oxidation were increased.	Glucose	33-40	insulin receptor	Rattus norvegicus	50-66
7016200-4	1980	In the case of streptosotocin diabetes (simulated hypoinsulinism) no correlation between insulin binding and its biological effects was observed, which can be accounted for by disturbances in transmission of the signal from the insulin--receptor complex to the enzymatic systems of the cells.	streptosotocin	15-29	insulin receptor	Rattus norvegicus	228-245
291908-2	1979	In the first, an aryl azide derivative of insulin, 125I-labeled 4-azido-2-nitrophenyl-insulin, was synthesized and used to photolabel the binding region of the insulin receptor in rat liver membranes and human placenta membranes.	Azides	17-27	insulin receptor	Rattus norvegicus	160-176
291908-2	1979	In the first, an aryl azide derivative of insulin, 125I-labeled 4-azido-2-nitrophenyl-insulin, was synthesized and used to photolabel the binding region of the insulin receptor in rat liver membranes and human placenta membranes.	2-iodotyrosine	51-55	insulin receptor	Rattus norvegicus	160-176
291908-2	1979	In the first, an aryl azide derivative of insulin, 125I-labeled 4-azido-2-nitrophenyl-insulin, was synthesized and used to photolabel the binding region of the insulin receptor in rat liver membranes and human placenta membranes.	4-azido-2-nitrophenyl phosphate	64-85	insulin receptor	Rattus norvegicus	160-176
291908-8	1979	These results indicate that the insulin receptor of both liver and placenta has a subunit of molecular weight 135,000 that binds insulin and that the receptor may be composed of at least two different subunits that are linked together or greatly stabilized by disulfide bonds.	Disulfides	260-269	insulin receptor	Rattus norvegicus	32-48
429330-11	1979	It proposes that the effects of the exogenously added glycosides (and Con A) may reflect the presence on the membrane of a native carbohydrate moiety by either mimicking or competitively inhibiting its ability to interact reversibly with a lectin-like carbohydrate binding site associated with the function of the insulin receptor.20	Carbohydrates	130-142	insulin receptor	Rattus norvegicus	314-330
579029-0	1977	Changes in insulin receptor concentration in rat fat cells following treatment with the gestagens clomegestone acetate and cyproterone acetate.	clomegestone acetate	98-118	insulin receptor	Rattus norvegicus	11-27
438322-1	1979	Possible evidence for a structural relationship of the insulin receptor to the glucose transport system.	Glucose	79-86	insulin receptor	Rattus norvegicus	55-71
438322-11	1979	The correlation between the effects of cytochalasin B on insulin receptor distribution and glucose transport leads to the speculation that the glycoprotein molecules containing the insulin receptor are functionally linked with the glucose transport system.	Cytochalasin B	39-53	insulin receptor	Rattus norvegicus	57-73
438322-11	1979	The correlation between the effects of cytochalasin B on insulin receptor distribution and glucose transport leads to the speculation that the glycoprotein molecules containing the insulin receptor are functionally linked with the glucose transport system.	Cytochalasin B	39-53	insulin receptor	Rattus norvegicus	181-197
438322-11	1979	The correlation between the effects of cytochalasin B on insulin receptor distribution and glucose transport leads to the speculation that the glycoprotein molecules containing the insulin receptor are functionally linked with the glucose transport system.	Glucose	91-98	insulin receptor	Rattus norvegicus	181-197
438322-11	1979	The correlation between the effects of cytochalasin B on insulin receptor distribution and glucose transport leads to the speculation that the glycoprotein molecules containing the insulin receptor are functionally linked with the glucose transport system.	Glucose	231-238	insulin receptor	Rattus norvegicus	57-73
438322-11	1979	The correlation between the effects of cytochalasin B on insulin receptor distribution and glucose transport leads to the speculation that the glycoprotein molecules containing the insulin receptor are functionally linked with the glucose transport system.	Glucose	231-238	insulin receptor	Rattus norvegicus	181-197
632238-4	1978	Sodium dodecyl sulfate gel electrophoresis of these plasma membrane preparations after solubilization with sodium dodecyl sulfate and reduction with beta-mercaptoethanol showed that a protein having a molecular weight of 130,000 was specifically labeled by the radioactive photosensitive insulin, suggesting that this protein may be the insulin receptor.	Sodium Dodecyl Sulfate	0-22	insulin receptor	Rattus norvegicus	337-353
579029-0	1977	Changes in insulin receptor concentration in rat fat cells following treatment with the gestagens clomegestone acetate and cyproterone acetate.	Cyproterone Acetate	123-142	insulin receptor	Rattus norvegicus	11-27
579029-3	1977	A similar though smaller decrease in insulin receptor concentration was seen in rats after treatment with cyproterone acetate, a compound which did not cause insulin resistance.	Cyproterone Acetate	106-125	insulin receptor	Rattus norvegicus	37-53
5049308-3	1972	The results indicate that the defect responsible for this insulin-resistant state exists in a step subsequent to insulin binding, possibly in transmission of the insulin-receptor "signal" since insensitivity occurs under conditions where glucose transport and oxidative processes are not apparently impaired.	Glucose	238-245	insulin receptor	Rattus norvegicus	162-178
849730-5	1977	Conclusions from these studies are that both disorders in coupling of insulin-receptor complexes to glucose transport systems and intracellular glucose metabolism play major roles in the insulin insensitivity of adipocytes from fasted rats, whereas, in adipocytes from refed rats, intracellular glucose metabolism, rather than glucose transport, is mainly involved in restoring insulin sensitivity.	Glucose	100-107	insulin receptor	Rattus norvegicus	70-86
34002209-8	2021	The INSRR/INSR/IGF1R kinase inhibitor, linsitinib prevented PKB/Akt activation by alkaline pHo, indicating that INSRRs/INSRs/IGF1Rs are required.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	39-49	insulin receptor	Rattus norvegicus	4-8
34009030-11	2021	High-fat diet, with and without pioglitazone, had tissue-specific effects on insulin receptor mRNA expression.	Pioglitazone	32-44	insulin receptor	Rattus norvegicus	77-93
33412188-0	2021	The chemical chaperon 4-phenyl butyric acid restored high-fat diet- induced hippocampal insulin content and insulin receptor level reduction along with spatial learning and memory deficits in male rats.	4-phenylbutyric acid	22-43	insulin receptor	Rattus norvegicus	108-124
33513940-0	2021	The Postnatal Offspring of Finasteride-Treated Male Rats Shows Hyperglycaemia, Elevated Hepatic Glycogen Storage and Altered GLUT2, IR, and AR Expression in the Liver.	Finasteride	27-38	insulin receptor	Rattus norvegicus	132-134
33513940-2	2021	In males, in physiological conditions, testosterone acts via androgen receptors (AR) to increase insulin receptor (IR) expression and glycogen synthesis, and to decrease glucose uptake controlled by liver-specific glucose transporter 2 (GLUT-2).	Testosterone	39-51	insulin receptor	Rattus norvegicus	97-113
33513940-2	2021	In males, in physiological conditions, testosterone acts via androgen receptors (AR) to increase insulin receptor (IR) expression and glycogen synthesis, and to decrease glucose uptake controlled by liver-specific glucose transporter 2 (GLUT-2).	Testosterone	39-51	insulin receptor	Rattus norvegicus	115-117
33513940-5	2021	Therefore, the goal of this study was to assess whether the administration of finasteride had an trans-generational effect on (i) GLUT-2 dependent accumulation of glycogen in the liver, (ii) IR and AR expression in the hepatocytes of male rat offspring, (iii) a relation between serum T and DHT levels and the expression of GLUT2, IR, and AR mRNAs, (iv) a serum glucose level and it correlation with GLUT-2 mRNA.	Finasteride	78-89	insulin receptor	Rattus norvegicus	191-193
33513940-5	2021	Therefore, the goal of this study was to assess whether the administration of finasteride had an trans-generational effect on (i) GLUT-2 dependent accumulation of glycogen in the liver, (ii) IR and AR expression in the hepatocytes of male rat offspring, (iii) a relation between serum T and DHT levels and the expression of GLUT2, IR, and AR mRNAs, (iv) a serum glucose level and it correlation with GLUT-2 mRNA.	Finasteride	78-89	insulin receptor	Rattus norvegicus	331-333
32474115-6	2020	Insulin receptor antagonist S961 (20 nmol/kg) was given by the tail vein and serum, and glucocorticoid-induced protein kinase-1 (SGK-1) inhibitor EMD638683 (20 mg/kg) was administrated intragastrically prior to LPS exposure.	3-(n-boc-aminomethyl)azetidine	28-32	insulin receptor	Rattus norvegicus	0-16
32980348-8	2020	Vitexin improved insulin signaling as analyzed by the levels of functional proteins in the insulin pathways, viz., insulin receptor (IR), insulin receptor substrate (IRS)-1 and IRS-2, glucose transporter -2, and glucose-stimulated insulin secretion.	vitexin	0-7	insulin receptor	Rattus norvegicus	115-131
32980348-8	2020	Vitexin improved insulin signaling as analyzed by the levels of functional proteins in the insulin pathways, viz., insulin receptor (IR), insulin receptor substrate (IRS)-1 and IRS-2, glucose transporter -2, and glucose-stimulated insulin secretion.	vitexin	0-7	insulin receptor	Rattus norvegicus	133-135
32947135-0	2020	Coumarin-chalcone hybrids targeting insulin receptor: Design, synthesis, anti-diabetic activity, and molecular docking.	coumarin	0-8	insulin receptor	Rattus norvegicus	36-52
32947135-0	2020	Coumarin-chalcone hybrids targeting insulin receptor: Design, synthesis, anti-diabetic activity, and molecular docking.	Chalcone	9-17	insulin receptor	Rattus norvegicus	36-52
32947135-2	2020	Synthesized compounds were tested for insulin receptor in silico docking studies (PDB ID: 1IR3); DCCU 13 and DCCT 13 derivatives received the lowest docking score; Streptozocin (STZ) and Nicotinamide (NA) induced type II diabetes was tested for their anti-diabetic activity in rats.	dccu	97-101	insulin receptor	Rattus norvegicus	38-54
32947135-2	2020	Synthesized compounds were tested for insulin receptor in silico docking studies (PDB ID: 1IR3); DCCU 13 and DCCT 13 derivatives received the lowest docking score; Streptozocin (STZ) and Nicotinamide (NA) induced type II diabetes was tested for their anti-diabetic activity in rats.	dcct	109-113	insulin receptor	Rattus norvegicus	38-54
32952944-2	2020	This study aimed to investigate the effects and mechanisms of magnesium supplementation on insulin receptor activity in elderly type 2 diabetes using a rat model and to provide experimental evidence for insulin resistance improvement by magnesium supplementation.	Magnesium	62-71	insulin receptor	Rattus norvegicus	91-107
32952944-8	2020	Results: Magnesium supplementation enhanced insulin sensitivity and decreased insulin resistance in diabetic rats mainly through increasing insulin receptor expression, affinity, and augmenting insulin receptor signaling.	Magnesium	9-18	insulin receptor	Rattus norvegicus	140-156
32952944-8	2020	Results: Magnesium supplementation enhanced insulin sensitivity and decreased insulin resistance in diabetic rats mainly through increasing insulin receptor expression, affinity, and augmenting insulin receptor signaling.	Magnesium	9-18	insulin receptor	Rattus norvegicus	194-210
32952944-12	2020	Conclusion: Magnesium supplementation has a positive effect on insulin receptor activity and insulin sensitivity in type 2 diabetes.	Magnesium	12-21	insulin receptor	Rattus norvegicus	63-79
33273981-0	2021	Hesperidin prevents hyperglycemia in diabetic rats by activating the insulin receptor pathway.	Hesperidin	0-10	insulin receptor	Rattus norvegicus	69-85
33273981-8	2021	Hesperidin was found to regulate glycolysis and gluconeogenesis by enhancing the activity of glucokinase, inducing the phosphorylation of insulin receptor (IR) and phosphoinositide-dependent kinase 1 (PDK1), while decreasing the activity of glucose-6-phosphatase and phosphoenolpyruvate carboxykinase in the liver.	Hesperidin	0-10	insulin receptor	Rattus norvegicus	138-154
33273981-8	2021	Hesperidin was found to regulate glycolysis and gluconeogenesis by enhancing the activity of glucokinase, inducing the phosphorylation of insulin receptor (IR) and phosphoinositide-dependent kinase 1 (PDK1), while decreasing the activity of glucose-6-phosphatase and phosphoenolpyruvate carboxykinase in the liver.	Hesperidin	0-10	insulin receptor	Rattus norvegicus	156-158
33273981-10	2021	Collectively, the present study identified the potent preventive effect of hesperidin against HFD-induced insulin resistance by activating the IR/PDK1 pathway.	Hesperidin	75-85	insulin receptor	Rattus norvegicus	143-145
31886886-1	2021	Insulin signaling through the insulin receptor has long been studied in classic target organs, such as adipose tissue and skeletal muscle, where one of its effects is to increase glucose uptake.	Glucose	179-186	insulin receptor	Rattus norvegicus	30-46
31886886-7	2021	The mobility of the insulin receptor is reduced both by low concentrations of the pro-inflammatory cytokine tumor necrosis factor alpha and by cholesterol depletion, suggesting an association with sphingolipid-rich membrane domains.	Cholesterol	143-154	insulin receptor	Rattus norvegicus	20-36
31886886-7	2021	The mobility of the insulin receptor is reduced both by low concentrations of the pro-inflammatory cytokine tumor necrosis factor alpha and by cholesterol depletion, suggesting an association with sphingolipid-rich membrane domains.	Sphingolipids	197-209	insulin receptor	Rattus norvegicus	20-36
32857721-6	2020	The transcriptional activity of the INSR and IGF-1R genes was reduced in diabetic rats and the administration of the non-specific TNF-alpha blocker - pentoxifylline led to a significant increase only for INSR gene in animals on the 4th week of the experimental diabetes.	Pentoxifylline	150-164	insulin receptor	Rattus norvegicus	36-40
32857721-6	2020	The transcriptional activity of the INSR and IGF-1R genes was reduced in diabetic rats and the administration of the non-specific TNF-alpha blocker - pentoxifylline led to a significant increase only for INSR gene in animals on the 4th week of the experimental diabetes.	Pentoxifylline	150-164	insulin receptor	Rattus norvegicus	204-208
32857721-1	2020	OBJECTIVE: The aim of the present study was to investigate the transcriptional activity of the GLP-1R, DPP-4, SGLT-1, INSR, and IGF-1R genes in GALT cells of rats with streptozotocin-induced diabetes in both untreated and treated with pentoxifylline, as a non-specific blocker of TNF-alpha.	Streptozocin	168-182	insulin receptor	Rattus norvegicus	118-122
31881302-3	2020	Via gene expression analysis, we found that three genes (InsR, GCK and GLUT-2) in the glucose metabolism pathway were significantly increased (P < 0.01, vs. negative group) in the FCM-treated groups and play important roles in hypoglycaemic activity.	Fosfomycin	180-183	insulin receptor	Rattus norvegicus	57-61
32045603-1	2020	In our previous study, we have shown that beta-sitosterol (SIT) enhances glycemic control by increasing the activation of insulin receptor (IR) and glucose transporter 4 (GLUT4) proteins in adipose tissue.	gamma-sitosterol	42-57	insulin receptor	Rattus norvegicus	122-143
32045603-1	2020	In our previous study, we have shown that beta-sitosterol (SIT) enhances glycemic control by increasing the activation of insulin receptor (IR) and glucose transporter 4 (GLUT4) proteins in adipose tissue.	gamma-sitosterol	59-62	insulin receptor	Rattus norvegicus	122-143
32128977-9	2020	The insulin receptor and GLUT2 levels increased, while KCa3.1 (KCNN4) levels decreased with the administration of indomethacin to insulinoma INS-1 cells.	Indomethacin	114-126	insulin receptor	Rattus norvegicus	4-20
31550518-7	2020	Cultured INS-1 cells with 7alpha-25-DHC were associated with increased proliferation and expression of GPR183, INS2, PDX1, NeuroD, and INSR.	25-hydroxy-7-dehydrocholesterol	26-39	insulin receptor	Rattus norvegicus	135-139
31509973-8	2019	Vitamin D deficiency itself also led to decreased LC3 II levels in the liver and decreased insulin receptor staining in the ovaries.	Vitamin D	0-9	insulin receptor	Rattus norvegicus	91-107
31856878-0	2019	Excitotoxic glutamate causes neuronal insulin resistance by inhibiting insulin receptor/Akt/mTOR pathway.	Glutamic Acid	12-21	insulin receptor	Rattus norvegicus	71-87
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.	Glutamic Acid	72-81	insulin receptor	Rattus norvegicus	189-191
31730869-1	2019	AIMS: The present study was designed to ameliorate the integrated efficacy of exogenous melatonin and insulin on tissue biochemical, serological, histopathological architecture and receptor expression of melatonin (MT1, MT2) and insulin receptor (IR) expression against the hepatic injury in diabetic rats.	Melatonin	88-97	insulin receptor	Rattus norvegicus	229-245
31730869-1	2019	AIMS: The present study was designed to ameliorate the integrated efficacy of exogenous melatonin and insulin on tissue biochemical, serological, histopathological architecture and receptor expression of melatonin (MT1, MT2) and insulin receptor (IR) expression against the hepatic injury in diabetic rats.	Melatonin	88-97	insulin receptor	Rattus norvegicus	247-249
31730869-1	2019	AIMS: The present study was designed to ameliorate the integrated efficacy of exogenous melatonin and insulin on tissue biochemical, serological, histopathological architecture and receptor expression of melatonin (MT1, MT2) and insulin receptor (IR) expression against the hepatic injury in diabetic rats.	Melatonin	204-213	insulin receptor	Rattus norvegicus	247-249
31730869-9	2019	However, the combined therapy (Melatonin and insulin treatment) revealed significant recovery and restoration in biochemical, cellular architecture of liver cells and receptor expression pattern of MT1, MT2 and IR.	Melatonin	31-40	insulin receptor	Rattus norvegicus	211-213
31885478-12	2019	The current study suggests that OL and GLB combination could cause herb-drug interactions through modulation of insulin receptor (INR), glucose transporter 2 (Slc2a2) and peroxisome proliferator-activated receptor alpha (PPAR-alpha) genes expression in the liver of diabetic rats.	Glyburide	39-42	insulin receptor	Rattus norvegicus	112-128
31885478-12	2019	The current study suggests that OL and GLB combination could cause herb-drug interactions through modulation of insulin receptor (INR), glucose transporter 2 (Slc2a2) and peroxisome proliferator-activated receptor alpha (PPAR-alpha) genes expression in the liver of diabetic rats.	Glyburide	39-42	insulin receptor	Rattus norvegicus	130-133
31128151-12	2019	CONCLUSION: miR-29a-3p played a functional role in insulin receptor signaling in the liver of ZDF rats.	mir-29a-3p	12-22	insulin receptor	Rattus norvegicus	51-67
31128151-12	2019	CONCLUSION: miR-29a-3p played a functional role in insulin receptor signaling in the liver of ZDF rats.	zdf	94-97	insulin receptor	Rattus norvegicus	51-67
31468522-14	2019	Importantly, pretreatment with the insulin receptor antagonist, GSK1838705, significantly suppressed the insulin-induced potentiation of the mechanical response.	GSK 1838705A	64-74	insulin receptor	Rattus norvegicus	35-51
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
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.	cholecystokinin C-terminal flanking peptide	276-282	insulin receptor	Rattus norvegicus	173-175
31856878-7	2019	These results suggested that excitotoxic glutamate inhibits signalling via the IR/Akt/mTOR pathway at multiple levels, including the IR, resulting in the development of acute neuronal insulin resistance within minutes, as an early pathological event associated with excitotoxicity.	Glutamic Acid	41-50	insulin receptor	Rattus norvegicus	79-81
31856878-7	2019	These results suggested that excitotoxic glutamate inhibits signalling via the IR/Akt/mTOR pathway at multiple levels, including the IR, resulting in the development of acute neuronal insulin resistance within minutes, as an early pathological event associated with excitotoxicity.	Glutamic Acid	41-50	insulin receptor	Rattus norvegicus	133-135
31012948-12	2019	Silencing the expression of the insulin receptor inhibited CCK-8-induced Adipoq expression in pre-adipocytes.	cholecystokinin 8	59-64	insulin receptor	Rattus norvegicus	32-48
31516323-13	2019	Moreover, GLB plus MCFE-500 was the most efficient in restoring INR, Slc2a2 and PPAR-alpha mRNA expression to their normal levels.	Glyburide	10-13	insulin receptor	Rattus norvegicus	64-67
31516323-13	2019	Moreover, GLB plus MCFE-500 was the most efficient in restoring INR, Slc2a2 and PPAR-alpha mRNA expression to their normal levels.	mcfe-500	19-27	insulin receptor	Rattus norvegicus	64-67
31025213-4	2019	In vitro assays also were performed in order to determine the expressions of phosphorylated IR in both cells cultured under 5.5 or 25 mM glucose by immunoblot.	Glucose	137-144	insulin receptor	Rattus norvegicus	92-94
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
31113619-6	2019	Moreover, tyrosine phosphorylation of the IR and IRS-1, and Akt activation is decreased in STZ diabetes compared to control.	Streptozocin	91-94	insulin receptor	Rattus norvegicus	42-44
31025213-8	2019	High glucose (25 mM) increased phosphorylated IR levels in endothelial cells but not in pericytes.	Glucose	5-12	insulin receptor	Rattus norvegicus	46-48
30742965-4	2019	Nonetheless, there are changes in the expression of insulin receptor during the progress of diabetic neuropathy, suggesting that this disorder begins before high glucose blood levels are established.	Glucose	162-169	insulin receptor	Rattus norvegicus	52-68
30461321-9	2019	Results of the study showed that the treatment with beta-sitosterol to diabetes-induced rats normalized the altered levels of blood glucose, serum insulin and testosterone, lipid profile, oxidative stress markers, antioxidant enzymes, insulin receptor (IR), and glucose transporter 4 (GLUT4) proteins.	gamma-sitosterol	52-67	insulin receptor	Rattus norvegicus	235-251
30461321-9	2019	Results of the study showed that the treatment with beta-sitosterol to diabetes-induced rats normalized the altered levels of blood glucose, serum insulin and testosterone, lipid profile, oxidative stress markers, antioxidant enzymes, insulin receptor (IR), and glucose transporter 4 (GLUT4) proteins.	gamma-sitosterol	52-67	insulin receptor	Rattus norvegicus	253-255
30461321-10	2019	Our present findings indicate that beta-sitosterol improves glycemic control through activation of IR and GLUT4 in the adipose tissue of high fat and sucrose-induced type-2 diabetic rats.	gamma-sitosterol	35-50	insulin receptor	Rattus norvegicus	99-101
30461321-10	2019	Our present findings indicate that beta-sitosterol improves glycemic control through activation of IR and GLUT4 in the adipose tissue of high fat and sucrose-induced type-2 diabetic rats.	Sucrose	150-157	insulin receptor	Rattus norvegicus	99-101
30887859-9	2019	The expression of Insr in the amygdala of control animals decreased over time while the opposite effect was seen in the rats that self-administered morphine.	Morphine	148-156	insulin receptor	Rattus norvegicus	18-22
30742965-12	2019	Chronic fructose also increased anoctamin-1 and ASIC3 whereas it reduced insulin receptor-beta, alpha5GABAA receptors and TASK-3 channels protein expression in DRG and sciatic nerve.	Fructose	8-16	insulin receptor	Rattus norvegicus	73-89
30296358-0	2018	Gingerenone A Sensitizes the Insulin Receptor and Increases Glucose Uptake by Inhibiting the Activity of p70 S6 Kinase.	gingerenone	0-11	insulin receptor	Rattus norvegicus	29-45
30471094-12	2019	Moreover, glimepiride increased both total and membrane glucose transporter 4 (GLUT4) levels in muscle and fat, which might be attributed to insulin receptor-independent IRS1/Akt activation.	glimepiride	10-21	insulin receptor	Rattus norvegicus	141-157
30597186-11	2019	DEHP treated rats showed decreased glucose uptake and oxidation, decreased mRNA levels of insulin receptor (IR), GLUT2 and reduced GLUT2 protein in cytosol but unaltered level in plasma membrane.	Diethylhexyl Phthalate	0-4	insulin receptor	Rattus norvegicus	90-106
30597186-11	2019	DEHP treated rats showed decreased glucose uptake and oxidation, decreased mRNA levels of insulin receptor (IR), GLUT2 and reduced GLUT2 protein in cytosol but unaltered level in plasma membrane.	Diethylhexyl Phthalate	0-4	insulin receptor	Rattus norvegicus	108-110
32091018-9	2019	We demonstrated that insulin, both in control animals and in those with hyperinsulinemia, travels bound to the receptor outer portion (ectodomain), which we called soluble insulin receptor, and that is released al higher amounts in response to plasma insulin increase; in rats with metabolic syndrome and hyperinsulinemia, plasma levels are much higher than in controls.	Aluminum	50-52	insulin receptor	Rattus norvegicus	172-188
29791756-8	2019	Insulin (30 nm) increased both parameters in the caudate putamen and nucleus accumbens core of AL rats in an insulin receptor- and PI3-kinase-dependent manner.	Aluminum	95-97	insulin receptor	Rattus norvegicus	109-125
30248393-6	2019	HSP70 was induced and insulin signaling as measured from tyrosine phosphorylation of insulin receptor (IR) &amp; 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) &amp; 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
31695236-9	2019	We demonstrated that insulin, both in control animals and in those with hyperinsulinemia, travels bound to the receptor outer portion (ectodomain), which we called soluble insulin receptor, and that is released al higher amounts in response to plasma insulin increase; in rats with metabolic syndrome and hyperinsulinemia, plasma levels are much higher than in controls.	Aluminum	50-52	insulin receptor	Rattus norvegicus	172-188
30296358-3	2018	This study aims to evaluate if Gin A can sensitize the insulin receptor by inhibiting S6K1 activity.	gingerenone A	31-36	insulin receptor	Rattus norvegicus	55-71
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
29955950-3	2018	We assessed the localization of the InsR and its co-localization with the TRPV1 in PSNs retrogradely labelled with biotin-conjugated wheat germ agglutinin injected into the dorsal hind paw skin, the gastrocnemius muscle, the pancreas and the urinary bladder wall.	Biotin	115-121	insulin receptor	Rattus norvegicus	36-40
29471671-2	2018	The IR can be localized in part to cholesterol-enriched membrane microdomains, but the role of such domains in insulin-mediated events in hepatocytes is not known.	Cholesterol	35-46	insulin receptor	Rattus norvegicus	4-6
30416963-1	2018	Vanadate, a protein tyrosine phosphatase inhibitor which elicits insulin-like effects, has previously been shown to inhibit expression of the insulin receptor gene at the transcriptional level in rat hepatoma cells.	Vanadates	0-8	insulin receptor	Rattus norvegicus	142-158
30250521-10	2018	Sericin may enhance the signaling transduction effect of insulin by upregulating the expression levels of key factors (IR, IRS-1, PI3K and AKT) in the liver insulin-PI3K/AKT signaling pathway, thus promoting glucose transport and liver glycogen synthesis, and further reducing blood glucose.	Glucose	208-215	insulin receptor	Rattus norvegicus	119-121
30250521-10	2018	Sericin may enhance the signaling transduction effect of insulin by upregulating the expression levels of key factors (IR, IRS-1, PI3K and AKT) in the liver insulin-PI3K/AKT signaling pathway, thus promoting glucose transport and liver glycogen synthesis, and further reducing blood glucose.	Glycogen	236-244	insulin receptor	Rattus norvegicus	119-121
30250521-10	2018	Sericin may enhance the signaling transduction effect of insulin by upregulating the expression levels of key factors (IR, IRS-1, PI3K and AKT) in the liver insulin-PI3K/AKT signaling pathway, thus promoting glucose transport and liver glycogen synthesis, and further reducing blood glucose.	Glucose	283-290	insulin receptor	Rattus norvegicus	119-121
30181290-3	2018	DAG activates protein kinase C epsilon (PKCepsilon), which phosphorylates and inhibits the insulin receptor.	Diglycerides	0-3	insulin receptor	Rattus norvegicus	91-107
29471671-8	2018	A subpopulation of IR was found in membrane microdomains enriched in cholesterol.	Cholesterol	69-80	insulin receptor	Rattus norvegicus	19-21
29471671-9	2018	Depletion of cholesterol from plasma membrane resulted in redistribution of the IR along the cells, which was associated with impaired insulin-induced nuclear Ca2+ signals, a signaling event that regulates hepatocyte proliferation.	Cholesterol	13-24	insulin receptor	Rattus norvegicus	80-82
29896241-9	2018	The FBG, GSP, InsR, Tch, TG, ALT and AST levels were significantly lower in the DMix-treated group compared with the model group (P&lt;0.05).	dmix	80-84	insulin receptor	Rattus norvegicus	14-18
29896241-10	2018	In addition, DMix treatment notably improved liver histopathology and significantly increased the gene and protein expression of InsR, PI3K and Akt (P&lt;0.05).	dmix	13-17	insulin receptor	Rattus norvegicus	129-133
29922429-0	2018	Insulin glargine affects the expression of Igf-1r, Insr, and Igf-1 genes in colon and liver of diabetic rats.	Insulin Glargine	8-16	insulin receptor	Rattus norvegicus	51-55
29772703-5	2018	Our results showed that alpha-mangostin stimulated insulin secretion in INS-1 cells by activating insulin receptor (IR) and pancreatic and duodenal homeobox 1 (Pdx1) followed by phosphorylation of phospho-phosphatidylinositol-3 kinase (PI3K), Akt, and extracellular signal regulated kinase (ERK) signaling cascades, whereas it inhibited the phosphorylation of insulin receptor substrate (IRS-1) (Ser1101).	mangostin	24-39	insulin receptor	Rattus norvegicus	98-114
29772703-5	2018	Our results showed that alpha-mangostin stimulated insulin secretion in INS-1 cells by activating insulin receptor (IR) and pancreatic and duodenal homeobox 1 (Pdx1) followed by phosphorylation of phospho-phosphatidylinositol-3 kinase (PI3K), Akt, and extracellular signal regulated kinase (ERK) signaling cascades, whereas it inhibited the phosphorylation of insulin receptor substrate (IRS-1) (Ser1101).	mangostin	24-39	insulin receptor	Rattus norvegicus	116-118
29772703-5	2018	Our results showed that alpha-mangostin stimulated insulin secretion in INS-1 cells by activating insulin receptor (IR) and pancreatic and duodenal homeobox 1 (Pdx1) followed by phosphorylation of phospho-phosphatidylinositol-3 kinase (PI3K), Akt, and extracellular signal regulated kinase (ERK) signaling cascades, whereas it inhibited the phosphorylation of insulin receptor substrate (IRS-1) (Ser1101).	mangostin	24-39	insulin receptor	Rattus norvegicus	360-376
29436382-9	2018	CONCLUSIONS: Our study demonstrates that acupuncture significantly alleviates MS through the IRbeta-ERK1/2-dependent insulin receptor signalling pathway in the DMV.	(2R,3R)-2,3-dihydroxy-3-methylpentanoic acid	160-163	insulin receptor	Rattus norvegicus	117-133
29610268-6	2018	We worked with a transgenic rat model of type 2 diabetes mellitus (Tet29) in which the insulin receptor is knocked down by doxycycline-induced RNA interference.	Doxycycline	123-134	insulin receptor	Rattus norvegicus	87-103
29922429-7	2018	Results: The liver tissue showed overexpression of the Insr and Igf-1r genes (P&gt;0.001) in rats treated with insulin glargine in comparison with the control group.	Insulin Glargine	119-127	insulin receptor	Rattus norvegicus	55-59
29922429-8	2018	Similar results were observed for the Insr gene (P&gt;0.011) in colonic tissue of rats treated with insulin glargine.	Insulin Glargine	108-116	insulin receptor	Rattus norvegicus	38-42
29698491-2	2018	This suggests a mechanism by which impaired neuronal insulin receptor signaling, a hallmark of diet-induced obesity, may contribute to impaired DA transmission.	Dopamine	144-146	insulin receptor	Rattus norvegicus	53-69
29698491-11	2018	Because AMPH induces DA efflux and brain activation, in large part via DAT, these findings suggest that blunted central nervous system insulin receptor signaling through a HF diet can impair DA homeostasis, thereby disrupting cognitive and reward circuitry involved in the regulation of hedonic feeding.	Amphetamine	8-12	insulin receptor	Rattus norvegicus	135-151
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Glucose	145-152	insulin receptor	Rattus norvegicus	4-20
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Glucose	145-152	insulin receptor	Rattus norvegicus	22-26
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Streptozocin	184-198	insulin receptor	Rattus norvegicus	4-20
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Streptozocin	184-198	insulin receptor	Rattus norvegicus	22-26
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Streptozocin	200-203	insulin receptor	Rattus norvegicus	4-20
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Streptozocin	200-203	insulin receptor	Rattus norvegicus	22-26
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Sugars	225-230	insulin receptor	Rattus norvegicus	4-20
29393432-2	2018	The insulin receptor (INSR)/phosphoinositide 3-kinase (PI3K)/AKT signaling pathway is well acknowledged as a predominant pathway associated with glucose uptake; however, the effect of streptozotocin (STZ) plus a high fat and sugar diet (HFSD) on the proteins associated with this pathway requires further elucidation.	Sugars	225-230	insulin receptor	Rattus norvegicus	22-26
29393432-7	2018	Furthermore, compared with other two HFSD types including pre-given and post-given group, the simul-given group that received IM injection with STZ exhibited decreased expression levels of major insulin signal pathway proteins INSR, PI3K, AKT1, PIP5Kalpha, GLUT2 or GLUT4 in the liver and pancreas (P&lt;0.05 or P&lt;0.01), whereas the opposite was observed in the skeletal muscle.	simul	94-99	insulin receptor	Rattus norvegicus	227-231
29393432-7	2018	Furthermore, compared with other two HFSD types including pre-given and post-given group, the simul-given group that received IM injection with STZ exhibited decreased expression levels of major insulin signal pathway proteins INSR, PI3K, AKT1, PIP5Kalpha, GLUT2 or GLUT4 in the liver and pancreas (P&lt;0.05 or P&lt;0.01), whereas the opposite was observed in the skeletal muscle.	Streptozocin	144-147	insulin receptor	Rattus norvegicus	227-231
29289466-3	2018	We presume that AT2R has an inhibitory effect on insulin receptor expression in RPT cells, which may affect renal sodium transport and therefore be of physiological or pathological significance.	Sodium	114-120	insulin receptor	Rattus norvegicus	49-65
29587416-0	2018	Knocking down Insulin Receptor in Pancreatic Beta Cell lines with Lentiviral-Small Hairpin RNA Reduces Glucose-Stimulated Insulin Secretion via Decreasing the Gene Expression of Insulin, GLUT2 and Pdx1.	Glucose	103-110	insulin receptor	Rattus norvegicus	14-30
29164460-5	2018	Exposure to DEHP induced glucose metabolic disorder in the adolescent rats, and the mechanism is that DEHP may interfere with the JAK2/STAT3/SOCS3 pathway, regulated the sensitivity of the insulin receptor and leptin receptor.	Diethylhexyl Phthalate	12-16	insulin receptor	Rattus norvegicus	189-205
29291420-5	2018	Vitamin C disrupted glucose tolerance by attenuating upstream hepatic insulin action through impairing the phosphorylation and activation of insulin receptor and its subsequent substrates; however, vitamin E showed its effect downstream insulin receptor in the insulin signaling pathway, reducing hepatic glucose transporter-2 (GLUT2) and phosphorylated protein kinase (p-Akt).	Ascorbic Acid	0-9	insulin receptor	Rattus norvegicus	141-157
29291420-5	2018	Vitamin C disrupted glucose tolerance by attenuating upstream hepatic insulin action through impairing the phosphorylation and activation of insulin receptor and its subsequent substrates; however, vitamin E showed its effect downstream insulin receptor in the insulin signaling pathway, reducing hepatic glucose transporter-2 (GLUT2) and phosphorylated protein kinase (p-Akt).	Vitamin E	198-207	insulin receptor	Rattus norvegicus	237-253
29205863-6	2018	EC and DHBA also enhanced the tyrosine phosphorylation and total IR and IRS-1 levels, and activated the PI3K/AKT pathway in NRK-52E cells.	Catechin	0-2	insulin receptor	Rattus norvegicus	65-67
29205863-6	2018	EC and DHBA also enhanced the tyrosine phosphorylation and total IR and IRS-1 levels, and activated the PI3K/AKT pathway in NRK-52E cells.	2,3-dihydroxybenzoic acid	7-11	insulin receptor	Rattus norvegicus	65-67
29453923-12	2018	Moreover, INSR and GLUT4 levels were elevated following magnesium supplementation in T2D rats.	Magnesium	56-65	insulin receptor	Rattus norvegicus	10-14
29129772-8	2018	SIGNIFICANCE: Glycyrrhizin ameliorates HFD-induced obesity in rats that may be attributed to its ability to increase insulin receptor expression and to activate NrF2 and subsequent homooxygenase-1 pathway.	Glycyrrhizic Acid	14-26	insulin receptor	Rattus norvegicus	117-133
29453923-13	2018	CONCLUSION: These findings demonstrate that magnesium may mediate effective metabolic control by stimulating the antioxidant defense, and increased levels of INSR and GLUT4 in diabetic rats.	Magnesium	44-53	insulin receptor	Rattus norvegicus	158-162
27730514-0	2017	Intranasal Insulin Administration Ameliorates Streptozotocin (ICV)-Induced Insulin Receptor Dysfunction, Neuroinflammation, Amyloidogenesis, and Memory Impairment in Rats.	Streptozocin	46-60	insulin receptor	Rattus norvegicus	75-91
28923480-0	2017	Impact of morphine on the expression of insulin receptor and protein levels of insulin/IGFs in rat neural stem cells.	Morphine	10-18	insulin receptor	Rattus norvegicus	40-56
28923480-10	2017	The biosynthesis of insulin, insulin-like growth factors, and insulin receptor were reduced (p&lt;0.05) after NSCs exposure to morphine at the concentration of 100muM for 24, 48 and 72h.	Morphine	127-135	insulin receptor	Rattus norvegicus	20-78
28923480-12	2017	It can be concluded that morphine initiated irregularity in NSCs kinetics and activity by reducing the secretion of insulin and insulin-like growth factors and down-regulation of insulin receptor.	Morphine	25-33	insulin receptor	Rattus norvegicus	179-195
29566382-3	2018	We hypothesized that testosterone deprivation aggravates LV dysfunction and cardiac autonomic imbalance via the impairment of cardiac mitochondrial function and dynamics proteins, a reduction in insulin receptor function, and an increase in apoptosis in obese insulin-resistant rats.	Testosterone	21-33	insulin receptor	Rattus norvegicus	195-211
28759757-7	2017	The treatments also enhanced the mRNA expression of insulin receptor beta-subunit, GLUT4 and adiponectin in adipose tissue of STZ/NA-induced type 2 diabetic rats.	Streptozocin	126-129	insulin receptor	Rattus norvegicus	52-68
28759757-8	2017	In conclusion, the navel orange peel hydroethanolic extract, naringin and naringenin have potent anti-diabetic effects in NA/STZ-induced type 2 diabetic rats via their insulinotropic effects and insulin improving action which in turn may be mediated through enhancing insulin receptor, GLUT4 and adiponectin expression in adipose tissue.	hydroethanolic	37-51	insulin receptor	Rattus norvegicus	268-284
28759757-8	2017	In conclusion, the navel orange peel hydroethanolic extract, naringin and naringenin have potent anti-diabetic effects in NA/STZ-induced type 2 diabetic rats via their insulinotropic effects and insulin improving action which in turn may be mediated through enhancing insulin receptor, GLUT4 and adiponectin expression in adipose tissue.	naringin	61-69	insulin receptor	Rattus norvegicus	268-284
28759757-8	2017	In conclusion, the navel orange peel hydroethanolic extract, naringin and naringenin have potent anti-diabetic effects in NA/STZ-induced type 2 diabetic rats via their insulinotropic effects and insulin improving action which in turn may be mediated through enhancing insulin receptor, GLUT4 and adiponectin expression in adipose tissue.	naringenin	74-84	insulin receptor	Rattus norvegicus	268-284
27730514-0	2017	Intranasal Insulin Administration Ameliorates Streptozotocin (ICV)-Induced Insulin Receptor Dysfunction, Neuroinflammation, Amyloidogenesis, and Memory Impairment in Rats.	icv	62-65	insulin receptor	Rattus norvegicus	75-91
27730514-5	2017	STZ (ICV) treated rats had shown memory impairment along with a significant decrease in IR signaling molecules (IR, pIRS-1, pAkt, and pGSK-3alpha/beta expression) and IDE expression in both hippocampus and cerebral cortex.	Streptozocin	0-3	insulin receptor	Rattus norvegicus	88-90
27730514-5	2017	STZ (ICV) treated rats had shown memory impairment along with a significant decrease in IR signaling molecules (IR, pIRS-1, pAkt, and pGSK-3alpha/beta expression) and IDE expression in both hippocampus and cerebral cortex.	Streptozocin	0-3	insulin receptor	Rattus norvegicus	112-114
27730514-5	2017	STZ (ICV) treated rats had shown memory impairment along with a significant decrease in IR signaling molecules (IR, pIRS-1, pAkt, and pGSK-3alpha/beta expression) and IDE expression in both hippocampus and cerebral cortex.	icv	5-8	insulin receptor	Rattus norvegicus	88-90
27730514-5	2017	STZ (ICV) treated rats had shown memory impairment along with a significant decrease in IR signaling molecules (IR, pIRS-1, pAkt, and pGSK-3alpha/beta expression) and IDE expression in both hippocampus and cerebral cortex.	icv	5-8	insulin receptor	Rattus norvegicus	112-114
28870559-9	2017	Brain tissue analyses showed DFO treatment decreased oxidation as measured by oxyblot and increased insulin receptor expression.	Deferoxamine	29-32	insulin receptor	Rattus norvegicus	100-116
28470423-0	2017	Rat brain glucose transporter-2, insulin receptor and glial expression are acute targets of intracerebroventricular streptozotocin: risk factors for sporadic Alzheimer"s disease?	Streptozocin	116-130	insulin receptor	Rattus norvegicus	33-49
28842605-6	2017	Particularly, insulin through insulin receptor/PI3K pathway markedly upregulated ENT2 uptake activity to restores the extracellular basal level of adenosine.	Adenosine	147-156	insulin receptor	Rattus norvegicus	30-46
28495883-6	2017	To describe all data (&gt;140 data points), the model needed three distinct pathways from IR to GLUT4: (i) via protein kinase B (PKB) and Akt substrate of 160 kDa (AS160), (ii) via an AS160-independent pathway from PKB, and (iii) via an additional pathway from IR, e.g. affecting the membrane constitution.	as160	164-169	insulin receptor	Rattus norvegicus	90-92
28495883-6	2017	To describe all data (&gt;140 data points), the model needed three distinct pathways from IR to GLUT4: (i) via protein kinase B (PKB) and Akt substrate of 160 kDa (AS160), (ii) via an AS160-independent pathway from PKB, and (iii) via an additional pathway from IR, e.g. affecting the membrane constitution.	as160	184-189	insulin receptor	Rattus norvegicus	90-92
28470423-2	2017	We have explored whether the insulin receptor (IR) and the glucose transporter-2 (GLUT2), used here as their markers, are the early targets of intracerebroventricularly (icv) administered streptozotocin (STZ) in an STZ-icv rat model of sAD, and whether their changes are associated with the STZ-induced neuroinflammation.	Streptozocin	188-202	insulin receptor	Rattus norvegicus	29-45
28470423-2	2017	We have explored whether the insulin receptor (IR) and the glucose transporter-2 (GLUT2), used here as their markers, are the early targets of intracerebroventricularly (icv) administered streptozotocin (STZ) in an STZ-icv rat model of sAD, and whether their changes are associated with the STZ-induced neuroinflammation.	Streptozocin	188-202	insulin receptor	Rattus norvegicus	47-49
28470423-5	2017	Changes in the GLUT2 (increment) and the IR (decrement) expression were mild in the areas close to the site of the STZ injection/release but pronounced in the ependymal lining cells of the third ventricle, thus indicating the possible metabolic implications.	Streptozocin	115-118	insulin receptor	Rattus norvegicus	41-43
28192884-0	2017	Myoinositol ameliorates high-fat diet and streptozotocin-induced diabetes in rats through promoting insulin receptor signaling.	Inositol	0-11	insulin receptor	Rattus norvegicus	100-116
28505155-11	2017	Moreover, it lowers the insulin receptor inhibitory effect of IOMe-AG538 and modifies the insulin-signaling pathway.	iome	62-66	insulin receptor	Rattus norvegicus	24-40
28505155-11	2017	Moreover, it lowers the insulin receptor inhibitory effect of IOMe-AG538 and modifies the insulin-signaling pathway.	AG 538	67-72	insulin receptor	Rattus norvegicus	24-40
28192884-0	2017	Myoinositol ameliorates high-fat diet and streptozotocin-induced diabetes in rats through promoting insulin receptor signaling.	Streptozocin	42-56	insulin receptor	Rattus norvegicus	100-116
28490763-6	2017	In turn, hypoxia was only observed when MG was combined (HFDMG group), being associated with impaired activation of the insulin receptor (Tyr1163), glucose intolerance and systemic and muscle insulin resistance.	Pyruvaldehyde	40-42	insulin receptor	Rattus norvegicus	120-136
28100702-6	2017	Real-time quantitative polymerase chain reaction results indicated that alkylamides significantly increased the mRNA expression of insulin receptor (InR), IGF1 and insulin-like growth factor 1 receptor (IGF1R) in the liver and skeletal muscle.	alkylamides	72-83	insulin receptor	Rattus norvegicus	131-147
28100702-6	2017	Real-time quantitative polymerase chain reaction results indicated that alkylamides significantly increased the mRNA expression of insulin receptor (InR), IGF1 and insulin-like growth factor 1 receptor (IGF1R) in the liver and skeletal muscle.	alkylamides	72-83	insulin receptor	Rattus norvegicus	149-152
27930980-0	2017	Vitamin D3 intake as regulator of insulin degrading enzyme and insulin receptor phosphorylation in diabetic rats.	Cholecalciferol	0-10	insulin receptor	Rattus norvegicus	63-79
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.	serine312	163-172	insulin receptor	Rattus norvegicus	63-79
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
27930980-11	2017	We concluded that vitamin D3 ameliorated insulin resistance and hyperinsulinemia in diabetic rat model received HFW through reduction of IDE and activation of insulin receptor phosphorylation.	Cholecalciferol	18-28	insulin receptor	Rattus norvegicus	159-175
27930980-9	2017	Vitamin D alleviated also insulin resistance, where both IDE, glucagon levels showed significant decrease along with activation of insulin receptor phosphorylation.	Vitamin D	0-9	insulin receptor	Rattus norvegicus	131-147
27052924-6	2016	The reduction of glucose uptake was associated with a moderately reduced tyrosine phosphorylation of the insulin receptor.	Glucose	17-24	insulin receptor	Rattus norvegicus	105-121
29093331-4	2017	GWBR supplementation also enhanced the expression of GLUT4 and the genes and proteins involved in GLUT4 translocation, such as insulin receptor (IR) and insulin receptor substrate 1 (IRS1), and increased the phosphorylation of phosphoinositide 3-kinase (PI3K) and protein kinase B (PKB, Akt) proteins in skeletal muscle.	gwbr	0-4	insulin receptor	Rattus norvegicus	127-143
29093331-4	2017	GWBR supplementation also enhanced the expression of GLUT4 and the genes and proteins involved in GLUT4 translocation, such as insulin receptor (IR) and insulin receptor substrate 1 (IRS1), and increased the phosphorylation of phosphoinositide 3-kinase (PI3K) and protein kinase B (PKB, Akt) proteins in skeletal muscle.	gwbr	0-4	insulin receptor	Rattus norvegicus	145-147
27704165-3	2017	METHODS: Diabetes was induced by tetracycline-inducible small hairpin RNA (shRNA) knockdown of the insulin receptor in rats, generating TetO rats.	Tetracycline	33-45	insulin receptor	Rattus norvegicus	99-115
29071945-0	2016	[Electroacupuncture Combined with Clomiphene Promotes Pregnancy and Blastocyst Implantation Possibly by Up-regulating Expression of Insulin Receptor and Insulin Receptor Substrate 1 Proteins in Endometrium in Rats with PCOS].	Clomiphene	34-44	insulin receptor	Rattus norvegicus	132-148
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
26988281-5	2016	We investigated insulin receptor activation in the ventral striatum of rats receiving water or 16% glucose either orally or intragastrically.	Water	86-91	insulin receptor	Rattus norvegicus	16-32
27161404-11	2016	To determine the molecular mechanism of action, we followed the molecular docking of Glycosin in its possible targets, dipeptidyl peptidase-IV (DPP-IV), Peroxisome proliferator-activated receptor gamma (PPARgamma), phosphorylated insulin receptor, and protein tyrosine phosphatase 1B (PTP-1B).	glycosine	85-93	insulin receptor	Rattus norvegicus	230-246
27161404-14	2016	Docking simulation confirmed that Glycosin interacted with DPP-IV, Insulin receptor and PTP-1B and PPARgamma with more affinity and binding energy.	glycosine	34-42	insulin receptor	Rattus norvegicus	67-83
26988281-5	2016	We investigated insulin receptor activation in the ventral striatum of rats receiving water or 16% glucose either orally or intragastrically.	Glucose	99-106	insulin receptor	Rattus norvegicus	16-32
26988281-6	2016	We also investigated whether glucose-induced insulin receptor activation was altered in food-restricted (FR) or diet-induced obesity (OB) rat models.	Glucose	29-36	insulin receptor	Rattus norvegicus	45-61
26914282-0	2016	Berberine improves mesenteric artery insulin sensitivity through up-regulating insulin receptor-mediated signalling in diabetic rats.	Berberine	0-9	insulin receptor	Rattus norvegicus	79-95
26914282-10	2016	Mechanistically, berberine up-regulated phosphorylation of the insulin receptor and its downstream signalling molecules AMPK, Akt and eNOS, and increased cell viability and autophagy in cultured endothelial cells.	Berberine	17-26	insulin receptor	Rattus norvegicus	63-79
26914282-12	2016	CONCLUSIONS AND IMPLICATIONS: Berberine improves diabetic vascular insulin sensitivity and mesenteric vasodilatation by up-regulating insulin receptor-mediated signalling in diabetic rats.	Berberine	30-39	insulin receptor	Rattus norvegicus	134-150
26577585-0	2016	Insulin augments serotonin-induced contraction via activation of the IR/PI3K/PDK1 pathway in the rat carotid artery.	Serotonin	17-26	insulin receptor	Rattus norvegicus	69-71
27107134-6	2016	Stimulation of the insulin receptor stimulated Na(+)-K(+)-ATPase activity, whereas pretreatment with PD168077 for 24 hours decreased the inhibitory effects of insulin receptor on Na(+)-K(+)-ATPase activity in WKY cells.	N-((4-(2-cyanophenyl)-1-piperazinyl)methyl)-3-methylbenzamide	101-109	insulin receptor	Rattus norvegicus	159-175
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
25906449-4	2015	RESULTS: The INGAP-PP significantly increased insulin release at high but not at low glucose concentration, glucokinase activity, glucose metabolism, glucokinase, insulin receptor, IRS-2 and PI3K protein concentration, insulin receptor and IRS-1/2 tyrosine phosphorylation, and the association of p85 with IRS-1.	Ingap (104-118)	13-21	insulin receptor	Rattus norvegicus	219-235
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
26188590-6	2015	Whereas insulin receptor level was higher in fructose fed rats, their tyrosine-residue phosphorylation was lower.	Fructose	45-53	insulin receptor	Rattus norvegicus	8-24
26596702-7	2016	Methylation of the Insr, Igf1r, Ins1 and Ins2 genes was influenced in a variable manner by low salt intake during pregnancy.	Salts	95-99	insulin receptor	Rattus norvegicus	19-23
26644274-8	2016	Fructose diet increased level of cardiac PTP1B and pIRS1 (Ser307), while levels of IR and ERK1/2, as well as pIRS1 (Tyr 632), pAkt (Ser473, Thr308) and pERK1/2 were decreased.	Fructose	0-8	insulin receptor	Rattus norvegicus	52-54
26889237-0	2016	Effects of a combination of puerarin, baicalin and berberine on the expression of proliferator-activated receptor-gamma and insulin receptor in a rat model of nonalcoholic fatty liver disease.	baicalin	38-46	insulin receptor	Rattus norvegicus	124-140
26889237-0	2016	Effects of a combination of puerarin, baicalin and berberine on the expression of proliferator-activated receptor-gamma and insulin receptor in a rat model of nonalcoholic fatty liver disease.	Berberine	51-60	insulin receptor	Rattus norvegicus	124-140
26889237-5	2016	Furthermore, as compared with the control group, the levels of PPAR-gamma/IR mRNA and protein expression were significantly decreased in the model group (P&lt;0.01), and significantly increased in the rosiglitazone group and some of the orthogonal experiment groups (P&lt;0.01).	Rosiglitazone	201-214	insulin receptor	Rattus norvegicus	74-76
26889237-6	2016	In conclusion, a combination of puerarin, baicalin and berberine induced favorable effects on NAFLD by upregulating hepatic PPAR-gamma and IR expression levels, and different proportions of monomer compositions exerted variable positive effects on various stages of NAFLD.	puerarin	32-40	insulin receptor	Rattus norvegicus	139-141
26889237-6	2016	In conclusion, a combination of puerarin, baicalin and berberine induced favorable effects on NAFLD by upregulating hepatic PPAR-gamma and IR expression levels, and different proportions of monomer compositions exerted variable positive effects on various stages of NAFLD.	baicalin	42-50	insulin receptor	Rattus norvegicus	139-141
26889237-6	2016	In conclusion, a combination of puerarin, baicalin and berberine induced favorable effects on NAFLD by upregulating hepatic PPAR-gamma and IR expression levels, and different proportions of monomer compositions exerted variable positive effects on various stages of NAFLD.	Berberine	55-64	insulin receptor	Rattus norvegicus	139-141
27579151-0	2016	Nigella sativa Relieves the Altered Insulin Receptor Signaling in Streptozotocin-Induced Diabetic Rats Fed with a High-Fat Diet.	Streptozocin	66-80	insulin receptor	Rattus norvegicus	36-52
27579151-2	2016	In this work, streptozotocin-induced diabetic rats fed with a high-fat diet were treated daily with NS oil (NSO) in order to study the effect on the blood glucose, lipid profile, oxidative stress parameters, and the gene expression of some insulin receptor-induced signaling molecules.	Streptozocin	14-28	insulin receptor	Rattus norvegicus	240-256
27579151-3	2016	This treatment was combined also with some drugs (metformin and glimepiride) and the insulin receptor inhibitor I-OMe-AG538.	i-ome	112-117	insulin receptor	Rattus norvegicus	85-101
27579151-3	2016	This treatment was combined also with some drugs (metformin and glimepiride) and the insulin receptor inhibitor I-OMe-AG538.	AG 538	118-123	insulin receptor	Rattus norvegicus	85-101
26412289-0	2015	Iron Deprivation May Enhance Insulin Receptor and Glut4 Transcription in Skeletal Muscle of Adult Rats.	Iron	0-4	insulin receptor	Rattus norvegicus	29-45
26412289-8	2015	In addition, dietary iron restriction resulted in a twofold increase in mRNA expression of Insr and fourfold increase in Glut4 expression in skeletal muscle.	Iron	21-25	insulin receptor	Rattus norvegicus	91-95
26412289-12	2015	CONCLUSION: Dietary iron deprivation may improve insulin receptor and glucose transporter transcription in muscle; however, our results show that dietary iron restriction can prevent and/or promote oxidative damage in a tissue-specific manner, emphasizing the importance of maintaining optimal iron intake.	Iron	20-24	insulin receptor	Rattus norvegicus	49-65
25761600-12	2015	The effects of aLA was blocked by insulin receptor inhibitor, HNMPA (AM)3.	Thioctic Acid	15-18	insulin receptor	Rattus norvegicus	34-50
25503661-0	2015	Nine-month follow-up of the insulin receptor signalling cascade in the brain of streptozotocin rat model of sporadic Alzheimer"s disease.	Streptozocin	80-94	insulin receptor	Rattus norvegicus	28-44
25503661-3	2015	Brain IR signalling has been explored usually at only one time point in periods <=3 months after the STZ-icv administration.	Streptozocin	101-104	insulin receptor	Rattus norvegicus	6-8
25315006-8	2015	These results show that in ZDF rats, treatment with a synthetic insulin-receptor-activating peptide or with insulin to lower blood glucose is accompanied by different effects on hepatic lipid anabolism and blood TG profiles.	zdf	27-30	insulin receptor	Rattus norvegicus	64-80
25315006-8	2015	These results show that in ZDF rats, treatment with a synthetic insulin-receptor-activating peptide or with insulin to lower blood glucose is accompanied by different effects on hepatic lipid anabolism and blood TG profiles.	Triglycerides	212-214	insulin receptor	Rattus norvegicus	64-80
25761600-13	2015	These results indicate that immediate treatment with aLA after ischemic injury may have significant neurorestorative effects mediated at least partially via insulin receptor activation.	Thioctic Acid	53-56	insulin receptor	Rattus norvegicus	157-173
26294909-0	2015	Alpha-Lipoic Acid Attenuates Cerebral Ischemia and Reperfusion Injury via Insulin Receptor and PI3K/Akt-Dependent Inhibition of NADPH Oxidase.	Thioctic Acid	0-17	insulin receptor	Rattus norvegicus	74-90
25474544-5	2015	Curcumin increased the expression of glucose transporter 2 (GLUT2) and phosphorylation of insulin receptor (IR), insulin receptor substrate-1 (IRS1), phosphatidylinositol-3-kinase (PI3K) and AKT in the INS-1 cells.	Curcumin	0-8	insulin receptor	Rattus norvegicus	90-106
25474544-5	2015	Curcumin increased the expression of glucose transporter 2 (GLUT2) and phosphorylation of insulin receptor (IR), insulin receptor substrate-1 (IRS1), phosphatidylinositol-3-kinase (PI3K) and AKT in the INS-1 cells.	Curcumin	0-8	insulin receptor	Rattus norvegicus	108-110
26294909-6	2015	In this study, we found that ALA could activate insulin receptor and PI3K/Akt signaling pathways, inhibit the expression and activity of NADPH oxidase, and subsequently suppress the generation of superoxide and the augment of oxidative stress indicators including MDA, protein carbonylation, and 8-OHdG.	Thioctic Acid	29-32	insulin receptor	Rattus norvegicus	48-64
26294909-7	2015	In conclusion, ALA attenuates cerebral ischemia and reperfusion injury via insulin receptor and PI3K/Akt-dependent inhibition of NADPH oxidase.	Thioctic Acid	15-18	insulin receptor	Rattus norvegicus	75-91
25352008-11	2015	RSV significantly upregulated liver Sirt1 levels and inhibited InsR and Glut2 expression in the liver.	Resveratrol	0-3	insulin receptor	Rattus norvegicus	63-67
24613802-12	2014	Furthermore, research showed that CK could promote the expression of InsR, IRS1, PI3Kp85, pAkt and Glut4 in skeletal muscle tissue of diabetic rats.	ginsenoside M1	34-36	insulin receptor	Rattus norvegicus	69-73
25365428-11	2014	The expression of IR in various tissues of naive ZDF rats is lower than in naive ZL and long-term taVNS treated ZDF rats.	zdf	49-52	insulin receptor	Rattus norvegicus	18-20
25365428-11	2014	The expression of IR in various tissues of naive ZDF rats is lower than in naive ZL and long-term taVNS treated ZDF rats.	zl	81-83	insulin receptor	Rattus norvegicus	18-20
25365428-11	2014	The expression of IR in various tissues of naive ZDF rats is lower than in naive ZL and long-term taVNS treated ZDF rats.	tavns	98-103	insulin receptor	Rattus norvegicus	18-20
25365428-11	2014	The expression of IR in various tissues of naive ZDF rats is lower than in naive ZL and long-term taVNS treated ZDF rats.	zdf	112-115	insulin receptor	Rattus norvegicus	18-20
25365428-12	2014	Collectively, our results indicate that in ZDF rats, i) depression and T2D develop simultaneously, ii) immobility time and HbAlc concentrations are highly and positively correlated, iii) a low expression of IR may be involved in the comorbidity of depression and T2D, and iv) taVNS is antidiabetic and antidepressive possibly through IR expression upregulation.	zdf	43-46	insulin receptor	Rattus norvegicus	207-209
25365428-12	2014	Collectively, our results indicate that in ZDF rats, i) depression and T2D develop simultaneously, ii) immobility time and HbAlc concentrations are highly and positively correlated, iii) a low expression of IR may be involved in the comorbidity of depression and T2D, and iv) taVNS is antidiabetic and antidepressive possibly through IR expression upregulation.	zdf	43-46	insulin receptor	Rattus norvegicus	334-336
25158313-0	2014	Protection of streptozotocin induced insulin receptor dysfunction, neuroinflammation and amyloidogenesis in astrocytes by insulin.	Streptozocin	14-28	insulin receptor	Rattus norvegicus	37-53
25158313-2	2014	Our earlier studies showed that intracerebroventricular streptozotocin (STZ) induces insulin receptor (IR) signaling defect in the hippocampus, which is associated with memory impairment in rats.	Streptozocin	56-70	insulin receptor	Rattus norvegicus	85-101
25158313-2	2014	Our earlier studies showed that intracerebroventricular streptozotocin (STZ) induces insulin receptor (IR) signaling defect in the hippocampus, which is associated with memory impairment in rats.	Streptozocin	56-70	insulin receptor	Rattus norvegicus	103-105
25158313-2	2014	Our earlier studies showed that intracerebroventricular streptozotocin (STZ) induces insulin receptor (IR) signaling defect in the hippocampus, which is associated with memory impairment in rats.	Streptozocin	72-75	insulin receptor	Rattus norvegicus	85-101
25158313-2	2014	Our earlier studies showed that intracerebroventricular streptozotocin (STZ) induces insulin receptor (IR) signaling defect in the hippocampus, which is associated with memory impairment in rats.	Streptozocin	72-75	insulin receptor	Rattus norvegicus	103-105
25158313-4	2014	However, involvement of astrocytes in STZ induced IR dysfunction has not received much attention.	Streptozocin	38-41	insulin receptor	Rattus norvegicus	50-52
25158313-5	2014	Therefore, the present study was planned to explore the effect of STZ on IR signaling, proinflammatory markers and amyloidogenesis in rat astrocytoma cell line, (C6).	Streptozocin	66-69	insulin receptor	Rattus norvegicus	73-75
25158313-6	2014	STZ (100 muM) treatment in astrocytes (n = 3) for 24 h, resulted significant decrease in IR mRNA and protein expression, phosphorylation of IRS-1, Akt, GSK-3alpha and GSK-3beta (p &lt; 0.01).	Streptozocin	0-3	insulin receptor	Rattus norvegicus	89-91
25086044-7	2014	Data demonstrate that 2 months of pioglitazone significantly increased electroretinogram amplitudes in type 2 diabetic obese rats, which was associated with improved insulin receptor activation.	Pioglitazone	34-46	insulin receptor	Rattus norvegicus	166-182
24888351-2	2014	Activation of the insulin receptor stimulates VSMCs proliferation while dopamine receptors, via D1 and D3 receptors, inhibit the stimulatory effects of norepinephrine on VSMCs proliferation.	Norepinephrine	152-166	insulin receptor	Rattus norvegicus	18-34
24607305-7	2014	The LPHC diet increased the G3P generation from glucose by 270% and the insulin receptor content and the p-AKT insulin stimulation in IBAT by 120% and reduced the beta3-AR content by 50%.	lphc	4-8	insulin receptor	Rattus norvegicus	72-88
24816759-10	2014	Moreover, we demonstrated that 3,5-T2, at physiological levels, reduces lipid content and triggers phosphorylation of Akt in an insulin receptor-independent manner, revealing new interesting properties as a biologically active molecule.	3,5-diiodothyronine	31-37	insulin receptor	Rattus norvegicus	128-144
24407176-5	2014	A proline-rich region in the N-terminus of INSM1 is required for RACK1 binding, which interrupts RACK1-InR interaction and enhances InR signal activation.	Proline	2-9	insulin receptor	Rattus norvegicus	103-106
24407176-5	2014	A proline-rich region in the N-terminus of INSM1 is required for RACK1 binding, which interrupts RACK1-InR interaction and enhances InR signal activation.	Proline	2-9	insulin receptor	Rattus norvegicus	132-135
24456332-6	2014	In addition, myriocin-mediated reductions in hepatic lipid and ceramide levels were associated with constitutive enhancement of insulin signalling through the insulin receptor and IRS-2, reduced hepatic oxidative stress and modulation of ER stress signalling mechanisms.	thermozymocidin	13-21	insulin receptor	Rattus norvegicus	159-175
25391857-0	2014	Oleic acid stimulates glucose uptake into adipocytes by enhancing insulin receptor signaling.	Oleic Acid	0-10	insulin receptor	Rattus norvegicus	66-82
24477262-5	2014	Zinc oxide and silver nanoparticles induce a significant reduced blood glucose, higher serum insulin, higher glucokinase activity higher expression level of insulin, insulin receptor, GLUT-2 and glucokinase genes in diabetic rats treated with zinc oxide, silver nanoparticles and insulin.	Zinc Oxide	0-10	insulin receptor	Rattus norvegicus	166-182
24477262-5	2014	Zinc oxide and silver nanoparticles induce a significant reduced blood glucose, higher serum insulin, higher glucokinase activity higher expression level of insulin, insulin receptor, GLUT-2 and glucokinase genes in diabetic rats treated with zinc oxide, silver nanoparticles and insulin.	Silver	15-21	insulin receptor	Rattus norvegicus	166-182
24477262-5	2014	Zinc oxide and silver nanoparticles induce a significant reduced blood glucose, higher serum insulin, higher glucokinase activity higher expression level of insulin, insulin receptor, GLUT-2 and glucokinase genes in diabetic rats treated with zinc oxide, silver nanoparticles and insulin.	Zinc Oxide	243-253	insulin receptor	Rattus norvegicus	166-182
25391857-6	2014	Taken together, the results of the present study show that oleic acid enhances insulin receptor signaling through a pathway along an insulin receptor/PI3K/PDK1/Akt/Rac1 axis in association with PTP1B inhibition and facilitates insulin-induced glucose uptake into adipocytes.	Oleic Acid	59-69	insulin receptor	Rattus norvegicus	79-95
25391857-0	2014	Oleic acid stimulates glucose uptake into adipocytes by enhancing insulin receptor signaling.	Glucose	22-29	insulin receptor	Rattus norvegicus	66-82
25391857-6	2014	Taken together, the results of the present study show that oleic acid enhances insulin receptor signaling through a pathway along an insulin receptor/PI3K/PDK1/Akt/Rac1 axis in association with PTP1B inhibition and facilitates insulin-induced glucose uptake into adipocytes.	Oleic Acid	59-69	insulin receptor	Rattus norvegicus	133-149
25391857-3	2014	Oleic acid (1 muM) stimulated insulin (0.1 nM)-induced phosphorylation of the insulin receptor at Tyr1185 and increased insulin (0.1 nM)-induced phosphorylation of Akt at Thr308 and Ser473 in differentiated 3T3-L1-GLUT4myc adipocytes.	Oleic Acid	0-10	insulin receptor	Rattus norvegicus	78-94
25391857-6	2014	Taken together, the results of the present study show that oleic acid enhances insulin receptor signaling through a pathway along an insulin receptor/PI3K/PDK1/Akt/Rac1 axis in association with PTP1B inhibition and facilitates insulin-induced glucose uptake into adipocytes.	Glucose	243-250	insulin receptor	Rattus norvegicus	79-95
25391857-6	2014	Taken together, the results of the present study show that oleic acid enhances insulin receptor signaling through a pathway along an insulin receptor/PI3K/PDK1/Akt/Rac1 axis in association with PTP1B inhibition and facilitates insulin-induced glucose uptake into adipocytes.	Glucose	243-250	insulin receptor	Rattus norvegicus	133-149
24377914-6	2014	This enzyme catalyzes the cleavage of insulin at the Phe(B24)-Phe(B25) bond, generating a major clipped molecule, A(1-21)-B(1-24) insulin, that can no longer bind to IR within endosomes.	Phenylalanine	53-56	insulin receptor	Rattus norvegicus	166-168
24377914-6	2014	This enzyme catalyzes the cleavage of insulin at the Phe(B24)-Phe(B25) bond, generating a major clipped molecule, A(1-21)-B(1-24) insulin, that can no longer bind to IR within endosomes.	Phenylalanine	62-65	insulin receptor	Rattus norvegicus	166-168
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
24088998-2	2014	We recently demonstrated that reduction of the extracellular domain of the insulin receptor by degrading proteases may lead to a reduced ability to maintain normal plasma glucose values.	Glucose	171-178	insulin receptor	Rattus norvegicus	75-91
24094269-0	2013	Mitochondrial H2O2 as an enable signal for triggering autophosphorylation of insulin receptor in neurons.	Hydrogen Peroxide	14-18	insulin receptor	Rattus norvegicus	77-93
24094269-4	2013	However, the kinetic characteristics of the H2O2 signal and its functional relationships with the insulin receptor during the autophosphorylation process in neurons remain unexplored to date.	Hydrogen Peroxide	44-48	insulin receptor	Rattus norvegicus	98-114
24094269-10	2013	The observed dose response is highly sigmoidal (Hill coefficient, nH, of 8.0+-2.3; R2=0.97), signifying that insulin receptor autophosphorylation is highly ultrasensitive to the H2O2 signal.	Hydrogen Peroxide	178-182	insulin receptor	Rattus norvegicus	109-125
24094269-12	2013	Both insulin-stimulated receptor autophosphorylation and H2O2 generation were inhibited by pertussis toxin, suggesting that a pertussis toxin-sensitive G protein may link the insulin receptor to the H2O2-generating system in neurons during the autophosphorylation process.	Hydrogen Peroxide	57-61	insulin receptor	Rattus norvegicus	175-191
24094269-12	2013	Both insulin-stimulated receptor autophosphorylation and H2O2 generation were inhibited by pertussis toxin, suggesting that a pertussis toxin-sensitive G protein may link the insulin receptor to the H2O2-generating system in neurons during the autophosphorylation process.	Hydrogen Peroxide	199-203	insulin receptor	Rattus norvegicus	175-191
24094269-15	2013	The neuronal insulin receptor is activated if two conditions are met: 1) insulin binds to the receptor, and 2) the H2O2 signal surpasses a certain threshold, thus, enabling receptor autophosphorylation in all-or-nothing manner.	Hydrogen Peroxide	115-119	insulin receptor	Rattus norvegicus	13-29
24023699-0	2013	The impact of low-dose insulin on peripheral nerve insulin receptor signaling in streptozotocin-induced diabetic rats.	Streptozocin	81-95	insulin receptor	Rattus norvegicus	51-67
24023699-1	2013	BACKGROUND: The precise mechanisms of the neuroprotective effects of insulin in streptozotocin (STZ)-induced diabetic animals remain unknown, but altered peripheral nerve insulin receptor signaling due to insulin deficiency might be one cause.	Streptozocin	96-99	insulin receptor	Rattus norvegicus	171-187
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
23874448-2	2013	Compared with INS-1 cells, INS-IR cells showed improved beta-cell function, including the increase in glucose utilization, calcium mobilization, and insulin secretion, and exhibited a higher rate of cell proliferation, and maintained lower levels of blood glucose in diabetic rats.	Glucose	102-109	insulin receptor	Rattus norvegicus	31-33
23874448-2	2013	Compared with INS-1 cells, INS-IR cells showed improved beta-cell function, including the increase in glucose utilization, calcium mobilization, and insulin secretion, and exhibited a higher rate of cell proliferation, and maintained lower levels of blood glucose in diabetic rats.	Calcium	123-130	insulin receptor	Rattus norvegicus	31-33
23874448-2	2013	Compared with INS-1 cells, INS-IR cells showed improved beta-cell function, including the increase in glucose utilization, calcium mobilization, and insulin secretion, and exhibited a higher rate of cell proliferation, and maintained lower levels of blood glucose in diabetic rats.	Blood Glucose	250-263	insulin receptor	Rattus norvegicus	31-33
23293908-0	2013	Hydrogen sulfide treatment promotes glucose uptake by increasing insulin receptor sensitivity and ameliorates kidney lesions in type 2 diabetes.	Hydrogen Sulfide	0-16	insulin receptor	Rattus norvegicus	65-81
23293908-0	2013	Hydrogen sulfide treatment promotes glucose uptake by increasing insulin receptor sensitivity and ameliorates kidney lesions in type 2 diabetes.	Glucose	36-43	insulin receptor	Rattus norvegicus	65-81
23293908-4	2013	The NaHS effects were blocked by an siRNA-mediated knockdown of the insulin receptor (IR).	sodium bisulfide	4-8	insulin receptor	Rattus norvegicus	68-84
23293908-4	2013	The NaHS effects were blocked by an siRNA-mediated knockdown of the insulin receptor (IR).	sodium bisulfide	4-8	insulin receptor	Rattus norvegicus	86-88
23293908-5	2013	NaHS also increased phosphorylation of the IR, PI3K, and Akt.	sodium bisulfide	0-4	insulin receptor	Rattus norvegicus	43-45
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
23238038-5	2013	Detemir treatment also resulted in changes in hippocampal levels of IDE, insulin receptor (IR), Akt, somatostatin (SST), and Ab.	Insulin Detemir	0-7	insulin receptor	Rattus norvegicus	73-89
23238038-5	2013	Detemir treatment also resulted in changes in hippocampal levels of IDE, insulin receptor (IR), Akt, somatostatin (SST), and Ab.	Insulin Detemir	0-7	insulin receptor	Rattus norvegicus	91-93
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
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.	Serine	372-378	insulin receptor	Rattus norvegicus	55-71
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
23240760-7	2013	Vildagliptin prevented neuronal insulin resistance by restoring insulin-induced long-term depression and neuronal IR phosphorylation, IRS-1 phosphorylation and Akt/PKB-ser phosphorylation.	Vildagliptin	0-12	insulin receptor	Rattus norvegicus	114-116
23240760-9	2013	Vildagliptin effectively restored neuronal IR function, increased glucagon-like-peptide 1 levels and prevented brain mitochondrial dysfunction, thus attenuating the impaired cognitive function caused by HFD.	Vildagliptin	0-12	insulin receptor	Rattus norvegicus	43-45
23654096-0	2013	[Influence of magnesium supplementation on insulin receptor affinity in erythrocytes of type 2 diabetes rats].	Magnesium	14-23	insulin receptor	Rattus norvegicus	43-59
23654096-1	2013	OBJECTIVE: To observe the influence of oral magnesium supplementation on insulin receptor affinity in erythrocytes of type 2 diabetes rats.	Magnesium	44-53	insulin receptor	Rattus norvegicus	73-89
23654096-9	2013	CONCLUSION: Magnesium supplementation could improve erythrocyte insulin receptor affinity and improve insulin resistance in type 2 diabetic rats.	Magnesium	12-21	insulin receptor	Rattus norvegicus	64-80
23343390-8	2013	L-DKP ester insulin bound weakly to the insulin receptor, while synthetic L-DKP insulin derived from the L-DKP ester insulin intermediate was fully active in binding to the insulin receptor.	l-dkp ester	0-11	insulin receptor	Rattus norvegicus	40-56
23343390-8	2013	L-DKP ester insulin bound weakly to the insulin receptor, while synthetic L-DKP insulin derived from the L-DKP ester insulin intermediate was fully active in binding to the insulin receptor.	l-dkp	0-5	insulin receptor	Rattus norvegicus	40-56
23343390-8	2013	L-DKP ester insulin bound weakly to the insulin receptor, while synthetic L-DKP insulin derived from the L-DKP ester insulin intermediate was fully active in binding to the insulin receptor.	l-dkp ester	105-116	insulin receptor	Rattus norvegicus	173-189
23380686-9	2013	The present study indicates beneficial effect of curcumin in diabetic rats by regulating the cholinergic, insulin receptor and GLUT-3 in the brainstem similar to the responses obtained with insulin therapy.	Curcumin	49-57	insulin receptor	Rattus norvegicus	106-122
23762875-4	2013	The data of glucose tolerance test showed that Subetta and RAD of Abs to beta -InsR (similar to Rosiglitazone) prevented significantly (P &lt; 0.01) the age-related spontaneous deterioration of glucose tolerance as seen in the control group.	Glucose	12-19	insulin receptor	Rattus norvegicus	79-83
23762875-4	2013	The data of glucose tolerance test showed that Subetta and RAD of Abs to beta -InsR (similar to Rosiglitazone) prevented significantly (P &lt; 0.01) the age-related spontaneous deterioration of glucose tolerance as seen in the control group.	Rosiglitazone	96-109	insulin receptor	Rattus norvegicus	79-83
23762875-6	2013	Chronic administration of Subetta and RAD of Abs to beta -InsR improves glucose control, to an extent similar to that of Rosiglitazone.	Glucose	72-79	insulin receptor	Rattus norvegicus	58-62
23068094-6	2012	Western blots showed that H(2)O(2) (100 muM) induced rapid, transient phosphorylation of the insulin receptor (IR), the IR substrate-1 (IRS1), and Akt with peak activities at 5 min (Delta 183%, P&lt;0.05), 3 min (Delta 414%, P&lt;0.05), and 10 min (Delta 35%, P&lt;0.05), respectively.	Hydrogen Peroxide	26-34	insulin receptor	Rattus norvegicus	93-109
23001013-10	2012	Pyridoxine treatment restored diabetes induced alterations in dopamine D(1), D(2) receptors, Insulin receptor, IGF-1, GLUT-3 gene expressions in striatum compared to diabetic rats.	Pyridoxine	0-10	insulin receptor	Rattus norvegicus	93-109
22872571-13	2012	In addition, fluoride obviously facilitated the mRNA expression of InsR in vitro.	Fluorides	13-21	insulin receptor	Rattus norvegicus	67-71
23068094-6	2012	Western blots showed that H(2)O(2) (100 muM) induced rapid, transient phosphorylation of the insulin receptor (IR), the IR substrate-1 (IRS1), and Akt with peak activities at 5 min (Delta 183%, P&lt;0.05), 3 min (Delta 414%, P&lt;0.05), and 10 min (Delta 35%, P&lt;0.05), respectively.	Hydrogen Peroxide	26-34	insulin receptor	Rattus norvegicus	111-113
22172158-11	2012	GTF induced a dose- and time-dependent phosphorylation of insulin receptor substrate 1, Akt and mitogen-activated protein kinase independent of insulin receptor phosphorylation.	glucose tolerance factor	0-3	insulin receptor	Rattus norvegicus	58-74
22429571-5	2012	Hepatocyte mitogenesis induced by L-ascorbic acid or L-ascorbic acid 2-glucoside was dose-dependently abolished by treatment with monoclonal antibodies against insulin-like growth factor (IGF)-I receptor, but not by treatment with monoclonal antibodies against insulin receptor or IGF-II receptor.	Ascorbic Acid	34-49	insulin receptor	Rattus norvegicus	261-277
22569684-0	2012	The anti-diabetic bis(maltolato)oxovanadium(IV) decreases lipid order while increasing insulin receptor localization in membrane microdomains.	bis(maltolato)oxovanadium	18-43	insulin receptor	Rattus norvegicus	87-103
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
22579915-0	2012	beta2-adrenoceptor and insulin receptor expression in the skeletal muscle of streptozotocin induced diabetic rats: antagonism by vitamin D3 and curcumin.	Streptozocin	77-91	insulin receptor	Rattus norvegicus	23-39
22579915-0	2012	beta2-adrenoceptor and insulin receptor expression in the skeletal muscle of streptozotocin induced diabetic rats: antagonism by vitamin D3 and curcumin.	Cholecalciferol	129-139	insulin receptor	Rattus norvegicus	23-39
22579915-0	2012	beta2-adrenoceptor and insulin receptor expression in the skeletal muscle of streptozotocin induced diabetic rats: antagonism by vitamin D3 and curcumin.	Curcumin	144-152	insulin receptor	Rattus norvegicus	23-39
22649556-6	2012	Topiramate, on the hepatic molecular level, has opposed the high fat/high fructose diet effect, where it significantly increased adiponectin receptors, GLUT2, and tyrosine kinase activity, while decreased insulin receptor isoforms.	Topiramate	0-10	insulin receptor	Rattus norvegicus	205-221
22473784-5	2012	In turn, an n-3 deficient diet and fructose interventions disrupted insulin receptor signalling in hippocampus as evidenced by a decrease in phosphorylation of the insulin receptor and its downstream effector Akt.	Nitrogen	1-2	insulin receptor	Rattus norvegicus	68-84
22473784-5	2012	In turn, an n-3 deficient diet and fructose interventions disrupted insulin receptor signalling in hippocampus as evidenced by a decrease in phosphorylation of the insulin receptor and its downstream effector Akt.	Nitrogen	1-2	insulin receptor	Rattus norvegicus	164-180
22473784-5	2012	In turn, an n-3 deficient diet and fructose interventions disrupted insulin receptor signalling in hippocampus as evidenced by a decrease in phosphorylation of the insulin receptor and its downstream effector Akt.	Fructose	35-43	insulin receptor	Rattus norvegicus	68-84
22473784-5	2012	In turn, an n-3 deficient diet and fructose interventions disrupted insulin receptor signalling in hippocampus as evidenced by a decrease in phosphorylation of the insulin receptor and its downstream effector Akt.	Fructose	35-43	insulin receptor	Rattus norvegicus	164-180
22473784-10	2012	Results showed that dietary n-3 fatty acid deficiency elevates the vulnerability to metabolic dysfunction and impaired cognitive functions by modulating insulin receptor signalling and synaptic plasticity.	Fatty Acids, Omega-3	28-42	insulin receptor	Rattus norvegicus	153-169
21618539-4	2012	Consistently, clozapine reduced insulin effect on insulin receptor (IR) by 40% and on IR substrate-1 (IRS1) tyrosine phosphorylation by 60%.	Clozapine	14-23	insulin receptor	Rattus norvegicus	50-66
21618539-4	2012	Consistently, clozapine reduced insulin effect on insulin receptor (IR) by 40% and on IR substrate-1 (IRS1) tyrosine phosphorylation by 60%.	Clozapine	14-23	insulin receptor	Rattus norvegicus	68-70
22278188-3	2012	Subsequently, both ZnD-AN and ZnD-EN pups were insulin resistant, and had evidence of elevated serum leptin and depressed insulin receptor phosphorylation with gender-specific differences up to 15 weeks.	znd-an	19-25	insulin receptor	Rattus norvegicus	122-138
22278188-3	2012	Subsequently, both ZnD-AN and ZnD-EN pups were insulin resistant, and had evidence of elevated serum leptin and depressed insulin receptor phosphorylation with gender-specific differences up to 15 weeks.	ZND	19-22	insulin receptor	Rattus norvegicus	122-138
22473784-0	2012	"Metabolic syndrome" in the brain: deficiency in omega-3 fatty acid exacerbates dysfunctions in insulin receptor signalling and cognition.	Fatty Acids, Omega-3	49-67	insulin receptor	Rattus norvegicus	96-112
22611938-0	2012	[Effects of magnesium intake on expression of insulin receptor in type 2 diabetes rats].	Magnesium	12-21	insulin receptor	Rattus norvegicus	46-62
22611938-1	2012	OBJECTIVE: To investigate the effects of magnesium intake on expression of insulin receptor in type 2 diabetes rats.	Magnesium	41-50	insulin receptor	Rattus norvegicus	75-91
22649556-9	2012	The study proved that insulin-resistance has an effect on hepatic molecular level and that the topiramate-mediated insulin sensitivity is ensued partly by modulation of hepatic insulin receptor isoforms, activation of tyrosine kinase, induction of GLUT2 and elevation of adiponectin receptors, as well as their ligand, adiponectin, besides its known improving effect on glucose tolerance and lipid homeostasis.	Topiramate	95-105	insulin receptor	Rattus norvegicus	177-193
21602711-9	2011	These beneficial effects of olmesartan were associated with ANG II and insulin receptor upregulation in sensory neurons as well as deactivation of Erk1/2 in sciatic nerves.	olmesartan	28-38	insulin receptor	Rattus norvegicus	71-87
21466649-0	2011	Vitamin A improves insulin sensitivity by increasing insulin receptor phosphorylation through protein tyrosine phosphatase 1B regulation at early age in obese rats of WNIN/Ob strain.	Vitamin A	0-9	insulin receptor	Rattus norvegicus	53-69
21466649-2	2011	Compared with stock diet-fed obese rats, vitamin A-enriched diet-fed obese rats had reduced body weight gain, visceral adiposity and improved insulin sensitivity as evidenced by decreased fasting plasma insulin and unaltered glucose levels, which could possibly be due to higher phosphorylation of soleus muscle insulin receptor.	Vitamin A	41-50	insulin receptor	Rattus norvegicus	312-328
21301931-0	2011	Sex steroids influence glucose oxidation through modulation of insulin receptor expression and IRS-1 serine phosphorylation in target tissues of adult male rat.	Steroids	4-12	insulin receptor	Rattus norvegicus	63-79
21301931-0	2011	Sex steroids influence glucose oxidation through modulation of insulin receptor expression and IRS-1 serine phosphorylation in target tissues of adult male rat.	Glucose	23-30	insulin receptor	Rattus norvegicus	63-79
21301931-3	2011	Our previous study showed that orchidectomy impairs glucose oxidation through decreased insulin receptor (IR) mRNA expression in skeletal muscles, liver, and adipose tissue of male rat.	Glucose	52-59	insulin receptor	Rattus norvegicus	88-104
21301931-3	2011	Our previous study showed that orchidectomy impairs glucose oxidation through decreased insulin receptor (IR) mRNA expression in skeletal muscles, liver, and adipose tissue of male rat.	Glucose	52-59	insulin receptor	Rattus norvegicus	106-108
21195590-0	2011	Insulin receptor signaling in rat hippocampus: a study in STZ (ICV) induced memory deficit model.	Streptozocin	58-61	insulin receptor	Rattus norvegicus	0-16
21569619-9	2011	The hepatocyte culture showed that BBR was active in enhancing the expression of insulin receptor (InsR) and low-density-lipoprotein receptor (LDLR) mRNA, as well as in activating AMP-activated protein kinase (AMPK).	Berberine	35-38	insulin receptor	Rattus norvegicus	81-97
21569619-9	2011	The hepatocyte culture showed that BBR was active in enhancing the expression of insulin receptor (InsR) and low-density-lipoprotein receptor (LDLR) mRNA, as well as in activating AMP-activated protein kinase (AMPK).	Berberine	35-38	insulin receptor	Rattus norvegicus	99-103
21569619-14	2011	BBR"s metabolites remained to be active on BBR"s targets (InsR, LDLR, and AMPK) but with reduced potency.	Berberine	0-3	insulin receptor	Rattus norvegicus	58-62
20655720-0	2011	Vitamin D3 restores altered cholinergic and insulin receptor expression in the cerebral cortex and muscarinic M3 receptor expression in pancreatic islets of streptozotocin induced diabetic rats.	Cholecalciferol	0-10	insulin receptor	Rattus norvegicus	44-60
21443795-4	2011	Quantitative RT-PCR analysis showed that si-InR, and to a lesser extent si-IGF-2R, broadly inhibited expression of insulin and IGF-2 polypeptides, and insulin, IGF-1, and IGF-2 receptors in the brain.	Silicon	25-27	insulin receptor	Rattus norvegicus	44-47
21443795-5	2011	ELISA studies showed that si-InR increased cerebellar levels of tau, phospho-tau and beta-actin, and inhibited GAPDH.	Silicon	26-28	insulin receptor	Rattus norvegicus	29-32
21443795-6	2011	In addition, si-InR, si-IGF-1R, and si-IGF-2R inhibited expression of choline acetyltransferase, which mediates motor function.	Silicon	13-15	insulin receptor	Rattus norvegicus	16-19
22081770-6	2011	Proteolytic cleavage of the extracellular domain of the beta(2) adrenergic receptor in arteries and arterioles causes vasoconstriction and elevation of the central blood pressure while cleavage of the extracellular domain of the insulin receptor leads to insulin resistance and lack of transmembrane glucose transport.	Glucose	300-307	insulin receptor	Rattus norvegicus	229-245
21195590-0	2011	Insulin receptor signaling in rat hippocampus: a study in STZ (ICV) induced memory deficit model.	icv	63-66	insulin receptor	Rattus norvegicus	0-16
21785619-10	2011	The myricetin treatment was also observed to affect the phosphorylation of the insulin receptor, insulin receptor substrate-1, Akt and Akt substrate of 160 kDa, with subsequent effects on glucose-transporter subtype 4 translocation, all of which were blocked by beta-FNA pretreatment.	myricetin	4-13	insulin receptor	Rattus norvegicus	79-95
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
21215763-9	2011	Results of the present study provide that both testosterone and insulin promote prostatic cell proliferation and change in the level of either of the hormone results in the destabilization of cellular equilibrium, and modulation of the insulin-receptor signaling in the prostate may provide an alternative strategy for the treatment of prostatic enlargement.	Testosterone	47-59	insulin receptor	Rattus norvegicus	236-252
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
21785619-10	2011	The myricetin treatment was also observed to affect the phosphorylation of the insulin receptor, insulin receptor substrate-1, Akt and Akt substrate of 160 kDa, with subsequent effects on glucose-transporter subtype 4 translocation, all of which were blocked by beta-FNA pretreatment.	myricetin	4-13	insulin receptor	Rattus norvegicus	97-113
20823693-6	2011	Insulin-stimulated insulin receptor substrate 1-associated phosphatidylinositol 3-kinase and plasma membrane-associated GLUT4 transporter were substantially increased with losartan treatment in burn-injured animals (59% above sham).	Losartan	172-180	insulin receptor	Rattus norvegicus	19-35
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.	12c	141-144	insulin receptor	Rattus norvegicus	50-66
20640583-11	2010	Although the canonical NF-kappaB cascade was not activated, STZ induced a decrease in insulin pathway proteins including insulin receptor (IR) and substrate (IRS-1) content and phosphorylation compared to control animals.	Streptozocin	60-63	insulin receptor	Rattus norvegicus	121-137
20640583-11	2010	Although the canonical NF-kappaB cascade was not activated, STZ induced a decrease in insulin pathway proteins including insulin receptor (IR) and substrate (IRS-1) content and phosphorylation compared to control animals.	Streptozocin	60-63	insulin receptor	Rattus norvegicus	139-141
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
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
20868513-7	2010	marmelose to diabetic rats reversed the 5-HT content, B(max), Kd of 5-HT, 5-HT(2A) and gene expression of 5-HT(2A), 5-HTT and INSR in hippocampus to near control.	marmelose	0-9	insulin receptor	Rattus norvegicus	126-130
20868513-0	2010	Alterations in hippocampal serotonergic and INSR function in streptozotocin induced diabetic rats exposed to stress: neuroprotective role of pyridoxine and Aegle marmelose.	Streptozocin	61-75	insulin receptor	Rattus norvegicus	44-48
20840603-9	2010	However, the pineal insulin receptor expression was increased after melatonin administration.	Melatonin	68-77	insulin receptor	Rattus norvegicus	20-36
20979642-10	2010	The association fructose plus fiber to seem decrease insulin receptor concentration in the liver, with consequent impair on glucose tolerance.	Fructose	16-24	insulin receptor	Rattus norvegicus	53-69
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
20957214-2	2010	The PTP1B acts as a negative regulator of insulin signaling by blocking the active site where phosphate hydrolysis of the insulin receptor takes place.	Phosphates	94-103	insulin receptor	Rattus norvegicus	122-138
20560104-3	2010	It was shown previously in hepatocytes that the UPR activates c-jun N-terminal kinase (JNK), which phosphorylates insulin receptor substrate (IRS) proteins on serine residues thereby inhibiting insulin signal transduction.	Serine	159-165	insulin receptor	Rattus norvegicus	114-130
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
20130739-1	2010	This study focused on the regulation and affinity modulation of the insulin receptor of coronary endothelium and cardiomyocytes in nondiabetic and STZ-induced type 1 diabetic rats.	Streptozocin	147-150	insulin receptor	Rattus norvegicus	68-84
20068141-5	2010	Furthermore, CYP2J3 treatment prevented fructose-induced decreases in insulin receptor signaling and phosphorylation of AMP-activated protein kinases (AMPKs) in liver, muscle, heart, kidney, and aorta.	Fructose	40-48	insulin receptor	Rattus norvegicus	70-86
19443198-0	2010	Oligomers of grape-seed procyanidin extract activate the insulin receptor and key targets of the insulin signaling pathway differently from insulin.	procyanidin	24-35	insulin receptor	Rattus norvegicus	57-73
19443198-2	2010	Here we show that the oligomeric structures of a grape-seed procyanidin extract (GSPE) interact and induce the autophosphorylation of the insulin receptor in order to stimulate the uptake of glucose.	procyanidin	60-71	insulin receptor	Rattus norvegicus	138-154
19443198-2	2010	Here we show that the oligomeric structures of a grape-seed procyanidin extract (GSPE) interact and induce the autophosphorylation of the insulin receptor in order to stimulate the uptake of glucose.	Glucose	191-198	insulin receptor	Rattus norvegicus	138-154
19443198-4	2010	Oligomers of GSPE phosphorylate protein kinase B at Thr308 lower than insulin does, according to the lower insulin receptor activation by procyanidins.	Proanthocyanidins	138-150	insulin receptor	Rattus norvegicus	107-123
20438933-0	2010	Insulin receptor is downregulated in the nitrofen-induced hypoplastic lung.	nitrofen	41-49	insulin receptor	Rattus norvegicus	0-16
20438933-2	2010	During fetal lung development, the insulin receptor (IR) plays an important role by mediating the cellular uptake of glucose, which is a major substrate for the biosynthesis of surfactant phospholipids.	Glucose	117-124	insulin receptor	Rattus norvegicus	35-56
20438933-2	2010	During fetal lung development, the insulin receptor (IR) plays an important role by mediating the cellular uptake of glucose, which is a major substrate for the biosynthesis of surfactant phospholipids.	Phospholipids	188-201	insulin receptor	Rattus norvegicus	35-56
20438933-5	2010	We hypothesized that pulmonary gene expression of IR is downregulated during the late stages of lung development in the nitrofen-induced CDH model.	nitrofen	120-128	insulin receptor	Rattus norvegicus	50-52
20438933-13	2010	CONCLUSION: Downregulation of IR gene and protein expression in hypoplastic lung during late stages of lung development may interfere with normal surfactant synthesis, causing pulmonary hypoplasia in the nitrofen-induced CDH model.	nitrofen	204-212	insulin receptor	Rattus norvegicus	30-32
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
19785000-6	2009	In addition, ANT activated insulin receptor phosphorylation, suggesting an increased utilization of glucose by tissues.	Glucose	100-107	insulin receptor	Rattus norvegicus	27-43
21132054-6	2010	CONCLUSION: These results suggest that cleavage of the extracellular domain of the insulin receptor, a situation that interferes with the ability for insulin to bind and provide an intracellular signal for glucose transport, may be involved in insulin resistance.	Glucose	206-213	insulin receptor	Rattus norvegicus	83-99
21346324-4	2010	The tyrosine kinase inhibitor AG-1024 abolished the effect of insulin in young rats, suggesting the involvement of the insulin receptor.	tyrphostin AG 1024	30-37	insulin receptor	Rattus norvegicus	119-135
20814553-5	2010	Ethanol-exposed SD rats had intermediate degrees of steatohepatitis, increased ALT, ADH and profibrogenesis gene expression, and suppressed insulin receptor binding and GAPDH expression, while pro-inflammatory cytokines were similarly increased as in LE rats.	Ethanol	0-7	insulin receptor	Rattus norvegicus	140-156
19615701-3	2009	Our recent study indicated that testosterone deprivation decreases insulin receptor expression and glucose oxidation in insulin target tissues.	Testosterone	32-44	insulin receptor	Rattus norvegicus	67-83
18931933-5	2009	(R)-alpha-lipoic acid (LA), a dithiol compound with antioxidant properties, is effective against age-related increases in oxidative stress and has been used to improve glucose utilization through insulin receptor (IR) pathway-mediated Akt phosphorylation.	Thioctic Acid	0-21	insulin receptor	Rattus norvegicus	196-212
19575708-9	2009	These data suggest that IR signaling pathways regulate actin and tubulin cytoskeletal organization in photoreceptors; they also imply that insulin and docosahexaenoic acid activate at least partially overlapping signaling pathways that are essential for the development of normal photoreceptors.	Docosahexaenoic Acids	151-171	insulin receptor	Rattus norvegicus	24-26
19345745-0	2009	Oleoylethanolamide, a natural ligand for PPAR-alpha, inhibits insulin receptor signalling in HTC rat hepatoma cells.	oleoylethanolamide	0-18	insulin receptor	Rattus norvegicus	62-78
18931933-5	2009	(R)-alpha-lipoic acid (LA), a dithiol compound with antioxidant properties, is effective against age-related increases in oxidative stress and has been used to improve glucose utilization through insulin receptor (IR) pathway-mediated Akt phosphorylation.	Thioctic Acid	0-21	insulin receptor	Rattus norvegicus	214-216
19345745-7	2009	OEA dose-dependently activates JNK and p38 MAPK, and inhibits insulin receptor phosphorylation.	oleoylethanolamide	0-3	insulin receptor	Rattus norvegicus	62-78
19345745-8	2009	OEA inhibits insulin receptor activation, blunting insulin signalling in the downstream PI3K pathway, decreasing phosphorylation of PKB and its target GSK-3.	oleoylethanolamide	0-3	insulin receptor	Rattus norvegicus	13-29
18931933-5	2009	(R)-alpha-lipoic acid (LA), a dithiol compound with antioxidant properties, is effective against age-related increases in oxidative stress and has been used to improve glucose utilization through insulin receptor (IR) pathway-mediated Akt phosphorylation.	Glucose	168-175	insulin receptor	Rattus norvegicus	196-212
19541365-7	2009	Specifically, (a) inhibitory responses to insulin were the most common (58-62%), and were dose-dependent with respect to GABA pretreatments and blocked by co-administration of the insulin receptor inhibitor HNMPA.	gamma-Aminobutyric Acid	121-125	insulin receptor	Rattus norvegicus	180-196
19554259-0	2009	Glucose binds to the insulin receptor affecting the mutual affinity of insulin and its receptor.	Glucose	0-7	insulin receptor	Rattus norvegicus	21-37
19554259-2	2009	An unexamined possibility is that the insulin receptor (IR) is sensitive to glucose concentration.	Glucose	76-83	insulin receptor	Rattus norvegicus	38-54
19554259-2	2009	An unexamined possibility is that the insulin receptor (IR) is sensitive to glucose concentration.	Glucose	76-83	insulin receptor	Rattus norvegicus	56-58
19554259-3	2009	We demonstrate here that insulin-like peptides derived from the IR bind glucose at low millimolar, and cytochalasin B at low micromolar, concentrations; several insulin-like IR peptides bind insulin at nanomolar Kd; and this binding is antagonized by increasing glucose concentrations.	Glucose	72-79	insulin receptor	Rattus norvegicus	64-66
19554259-3	2009	We demonstrate here that insulin-like peptides derived from the IR bind glucose at low millimolar, and cytochalasin B at low micromolar, concentrations; several insulin-like IR peptides bind insulin at nanomolar Kd; and this binding is antagonized by increasing glucose concentrations.	Cytochalasin B	103-117	insulin receptor	Rattus norvegicus	64-66
19554259-3	2009	We demonstrate here that insulin-like peptides derived from the IR bind glucose at low millimolar, and cytochalasin B at low micromolar, concentrations; several insulin-like IR peptides bind insulin at nanomolar Kd; and this binding is antagonized by increasing glucose concentrations.	Glucose	262-269	insulin receptor	Rattus norvegicus	64-66
19554259-4	2009	In addition, glucose and cytochalasin B bind to IR isolated from rat liver and increasing glucose decreases insulin binding to this IR preparation.	Glucose	13-20	insulin receptor	Rattus norvegicus	48-50
19554259-4	2009	In addition, glucose and cytochalasin B bind to IR isolated from rat liver and increasing glucose decreases insulin binding to this IR preparation.	Glucose	13-20	insulin receptor	Rattus norvegicus	132-134
19554259-4	2009	In addition, glucose and cytochalasin B bind to IR isolated from rat liver and increasing glucose decreases insulin binding to this IR preparation.	Cytochalasin B	25-39	insulin receptor	Rattus norvegicus	48-50
19554259-4	2009	In addition, glucose and cytochalasin B bind to IR isolated from rat liver and increasing glucose decreases insulin binding to this IR preparation.	Cytochalasin B	25-39	insulin receptor	Rattus norvegicus	132-134
19554259-5	2009	The presence of GLUT 1 in our IR preparation suggests the possibility of additional glucose-mediated allosteric control.	Glucose	84-91	insulin receptor	Rattus norvegicus	30-32
19554259-6	2009	We propose a model in which glucose binds to insulin, the IR, and GLUT; insulin binds to the IR; and the IR binds to GLUT.	Glucose	28-35	insulin receptor	Rattus norvegicus	58-60
19541365-7	2009	Specifically, (a) inhibitory responses to insulin were the most common (58-62%), and were dose-dependent with respect to GABA pretreatments and blocked by co-administration of the insulin receptor inhibitor HNMPA.	HNMPA	207-212	insulin receptor	Rattus norvegicus	180-196
19287336-1	2009	OBJECTIVE: To investigate the action of palmitate on insulin receptor (IR) signaling pathway in rat pancreatic islets.	Palmitates	40-49	insulin receptor	Rattus norvegicus	53-69
19287336-1	2009	OBJECTIVE: To investigate the action of palmitate on insulin receptor (IR) signaling pathway in rat pancreatic islets.	Palmitates	40-49	insulin receptor	Rattus norvegicus	71-73
19287336-8	2009	CONCLUSIONS: Palmitate at physiological concentration associated with 5.6-mmol/L glucose activates IR signaling pathway in pancreatic beta cells.	Palmitates	13-22	insulin receptor	Rattus norvegicus	99-101
19287336-8	2009	CONCLUSIONS: Palmitate at physiological concentration associated with 5.6-mmol/L glucose activates IR signaling pathway in pancreatic beta cells.	Glucose	81-88	insulin receptor	Rattus norvegicus	99-101
19543529-4	2009	Insulin induced a rapid, t(1/2)&lt;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
19543529-1	2009	BACKGROUND: The insulin receptor is localized in caveolae and is dependent on caveolae or cholesterol for signaling in adipocytes.	Cholesterol	90-101	insulin receptor	Rattus norvegicus	16-32
19454822-8	2009	With respect to the concentrations of the insulin receptor, GLUT2, PKC and PKA in the pancreatic islets of the bleomycin group, there was an increase in GLUT2 (48.4%) and PKC (70.8%) and a reduction in PKA (38.5%).	Bleomycin	111-120	insulin receptor	Rattus norvegicus	42-58
19246098-10	2009	More recently a novel class of arylalkylaminevanadium salts have shown potent insulin-mimetic effects downstream of the insulin receptor.	arylalkylaminevanadium salts	31-59	insulin receptor	Rattus norvegicus	120-136
19171190-1	2009	Cellular growth and glucose uptake are regulated by multiple signals generated by the insulin receptor.	Glucose	20-27	insulin receptor	Rattus norvegicus	86-102
19101970-0	2009	Exploring the implications of vitamin B12 conjugation to insulin on insulin receptor binding.	Vitamin B 12	30-41	insulin receptor	Rattus norvegicus	68-84
19101970-5	2009	Furthermore, given that we have previously demonstrated a significant drop in blood glucose concentration following the oral administration of the B(12)-insulin bioconjugate used in this work, it is reasonable to conclude that the IR recognition described herein is associated with maintenance of biological activity for insulin.	Glucose	84-91	insulin receptor	Rattus norvegicus	231-233
19059538-0	2009	Berberine reduces insulin resistance through protein kinase C-dependent up-regulation of insulin receptor expression.	Berberine	0-9	insulin receptor	Rattus norvegicus	89-105
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
19874240-9	2009	Compared to the control group, electron microscopy showed cytoplasm swelling and vacuolization, and marked decrease or absence of dense-core secretory granules in beta cells in rats with diabetes mellitus induced with FK506.Compared to the control group, expression of insulin receptor of hepatic cell decreased in rats of diabetes mellitus models induced with FK506 (P&lt;0.05).	Tacrolimus	218-223	insulin receptor	Rattus norvegicus	269-285
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
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
19049803-5	2009	This induced effect was blocked by insulin receptor antibody, insulin receptor tyrosine kinase inhibitor I-OMe-AG538, PKC inhibitor chelerythrine and NF-kappaB inhibitor pyrrolidine dithiocarbamate ammonium (PDTC).	prolinedithiocarbamate	208-212	insulin receptor	Rattus norvegicus	35-51
19049803-5	2009	This induced effect was blocked by insulin receptor antibody, insulin receptor tyrosine kinase inhibitor I-OMe-AG538, PKC inhibitor chelerythrine and NF-kappaB inhibitor pyrrolidine dithiocarbamate ammonium (PDTC).	prolinedithiocarbamate	208-212	insulin receptor	Rattus norvegicus	62-78
19059538-5	2009	Berberine increased InsR expression in the L6 rat skeletal muscle cells as well.	Berberine	0-9	insulin receptor	Rattus norvegicus	20-24
19059538-6	2009	Berberine-enhanced InsR expression improved cellular glucose consumption only in the presence of insulin.	Berberine	0-9	insulin receptor	Rattus norvegicus	19-23
19059538-6	2009	Berberine-enhanced InsR expression improved cellular glucose consumption only in the presence of insulin.	Glucose	53-60	insulin receptor	Rattus norvegicus	19-23
19059538-8	2009	Berberine induced InsR gene expression through a protein kinase C (PKC)-dependent activation of its promoter.	Berberine	0-9	insulin receptor	Rattus norvegicus	18-22
19017805-5	2008	However, Dox treatment at very low concentrations led to a rapid induction of the siRNA and ablation of INSR protein expression.	Doxycycline	9-12	insulin receptor	Rattus norvegicus	104-108
19340286-3	2009	To this purpose, we employed a tetracycline-inducible shRNA expression system targeting the insulin receptor (IR).	Tetracycline	31-43	insulin receptor	Rattus norvegicus	92-108
19340286-3	2009	To this purpose, we employed a tetracycline-inducible shRNA expression system targeting the insulin receptor (IR).	Tetracycline	31-43	insulin receptor	Rattus norvegicus	110-112
19340286-4	2009	Doxycycline (DOX) treatment of the resulting transgenic rats led to a dose-dependent and reversible increase in blood glucose caused by ubiquitous inhibition of IR expression and signalling.	Doxycycline	0-11	insulin receptor	Rattus norvegicus	161-163
19340286-4	2009	Doxycycline (DOX) treatment of the resulting transgenic rats led to a dose-dependent and reversible increase in blood glucose caused by ubiquitous inhibition of IR expression and signalling.	Doxycycline	13-16	insulin receptor	Rattus norvegicus	161-163
19017805-7	2008	Importantly, this phenotype was reversible (i.e., discontinuation of Dox treatment led to INSR re-expression and remission of diabetes symptoms).	Doxycycline	69-72	insulin receptor	Rattus norvegicus	90-94
18798337-5	2008	Furthermore, insulin-induced calcium signals occur in the nucleus, and are temporally associated with selective depletion of nuclear phosphatidylinositol bisphosphate and translocation of the insulin receptor to the nucleus.	Calcium	29-36	insulin receptor	Rattus norvegicus	192-208
18798337-6	2008	These findings suggest that the insulin receptor translocates to the nucleus to initiate nuclear, inositol 1,4,5-trisphosphate-mediated calcium signals in rat hepatocytes.	Inositol 1,4,5-Trisphosphate	98-126	insulin receptor	Rattus norvegicus	32-48
18798337-6	2008	These findings suggest that the insulin receptor translocates to the nucleus to initiate nuclear, inositol 1,4,5-trisphosphate-mediated calcium signals in rat hepatocytes.	Calcium	136-143	insulin receptor	Rattus norvegicus	32-48
18713797-0	2008	Saturated fatty acids inhibit hepatic insulin action by modulating insulin receptor expression and post-receptor signalling.	Fatty Acids	0-21	insulin receptor	Rattus norvegicus	67-83
18713797-3	2008	Fao hepatoma cells were treated with physiological concentrations of sodium palmitate (0.25 mM) (16:0) for 0.25-48 h. Palmitate decreased insulin receptor (IR) protein and mRNA expression in a dose- and time-dependent manner (35% decrease at 12 h).	Palmitic Acid	69-85	insulin receptor	Rattus norvegicus	138-154
18713797-3	2008	Fao hepatoma cells were treated with physiological concentrations of sodium palmitate (0.25 mM) (16:0) for 0.25-48 h. Palmitate decreased insulin receptor (IR) protein and mRNA expression in a dose- and time-dependent manner (35% decrease at 12 h).	Palmitic Acid	69-85	insulin receptor	Rattus norvegicus	156-158
18713797-9	2008	Thus, the inhibition of insulin signalling by palmitate in hepatoma cells is dependent upon oxidation of fatty acyl-CoA species and requires intact insulin receptor expression.	Palmitates	46-55	insulin receptor	Rattus norvegicus	148-164
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
19083488-8	2008	In conclusion, elevated whey protein, calcium, and vitamin D intake resulted in reduced accumulation of body fat mass and increased lean mass, with a commensurate increase in insulin receptor expression, regardless of the level of calories from fat or sucrose.	Calcium	38-45	insulin receptor	Rattus norvegicus	175-191
19083488-8	2008	In conclusion, elevated whey protein, calcium, and vitamin D intake resulted in reduced accumulation of body fat mass and increased lean mass, with a commensurate increase in insulin receptor expression, regardless of the level of calories from fat or sucrose.	Vitamin D	51-60	insulin receptor	Rattus norvegicus	175-191
18606910-6	2008	We demonstrate with an antibody against the extracellular domain that the insulin receptor-alpha density is reduced in SHRs, in line with elevated blood glucose levels and glycohemoglobin.	Glucose	153-160	insulin receptor	Rattus norvegicus	74-90
18679562-7	2008	It is discussed that both CORT and STZ may act on the neuronal insulin receptor in a similar way.	Streptozocin	35-38	insulin receptor	Rattus norvegicus	63-79
18603396-2	2008	We investigated the glucose-stimulated serum insulin response and subsequent alterations in insulin receptor (IR), Akt, and FoxO1 in the rat liver and quadriceps femoris muscle (QFM).	Glucose	20-27	insulin receptor	Rattus norvegicus	92-108
18603396-2	2008	We investigated the glucose-stimulated serum insulin response and subsequent alterations in insulin receptor (IR), Akt, and FoxO1 in the rat liver and quadriceps femoris muscle (QFM).	Glucose	20-27	insulin receptor	Rattus norvegicus	110-112
18679562-2	2008	The data were compared with results derived from long-term and low dose intracerebroventricular application of the diabetogenic drug streptozotocin (STZ) known to inhibit the function of the neuronal insulin receptor and generating an insulin resistant brain state.	Streptozocin	149-152	insulin receptor	Rattus norvegicus	200-216
18606910-8	2008	Blockade of MMPs with a broad-acting inhibitor (doxycycline, 5.4 mg/kg per day) reduces protease activity in plasma and microvessels; blocks the proteolytic cleavage of the insulin receptor, the reduced glucose transport; normalizes blood glucose levels and glycohemoglobin levels; and reduces blood pressure and enhanced microvascular oxidative stress of SHRs.	Doxycycline	48-59	insulin receptor	Rattus norvegicus	173-189
18606910-8	2008	Blockade of MMPs with a broad-acting inhibitor (doxycycline, 5.4 mg/kg per day) reduces protease activity in plasma and microvessels; blocks the proteolytic cleavage of the insulin receptor, the reduced glucose transport; normalizes blood glucose levels and glycohemoglobin levels; and reduces blood pressure and enhanced microvascular oxidative stress of SHRs.	Glucose	203-210	insulin receptor	Rattus norvegicus	173-189
18606910-8	2008	Blockade of MMPs with a broad-acting inhibitor (doxycycline, 5.4 mg/kg per day) reduces protease activity in plasma and microvessels; blocks the proteolytic cleavage of the insulin receptor, the reduced glucose transport; normalizes blood glucose levels and glycohemoglobin levels; and reduces blood pressure and enhanced microvascular oxidative stress of SHRs.	Glucose	239-246	insulin receptor	Rattus norvegicus	173-189
18638371-0	2008	Genomic actions of 1,25-dihydroxyvitamin D3 on insulin receptor gene expression, insulin receptor number and insulin activity in the kidney, liver and adipose tissue of streptozotocin-induced diabetic rats.	Calcitriol	19-43	insulin receptor	Rattus norvegicus	47-63
18638371-6	2008	Moreover, a computer search in the rat insulin receptor promoter revealed the existence of two candidate vitamin D response element (VDRE) sequences located at -256/-219 bp and -653/-620 bp, the first overlapped by three and the second by four AP-2-like sites.	Vitamin D	105-114	insulin receptor	Rattus norvegicus	39-55
18469022-6	2008	Concordantly, insulin receptor (IR), IR substrate type 1 (IRS1), IRS2, and protein kinase B (AKT) phosphorylation in adipose tissue and skeletal muscle was improved by citrate ICV treatment.	citrate icv	168-179	insulin receptor	Rattus norvegicus	14-30
18426865-6	2008	RSV treatment increased insulin-stimulated whole-body glucose uptake and steady-state glucose uptake of soleus muscle and liver in HCF-fed rats as well as enhanced membrane trafficking activity of GLUT4 and increased phosphorylation of insulin receptor in insulin-resistant soleus muscles.	Resveratrol	0-3	insulin receptor	Rattus norvegicus	236-252
18469022-6	2008	Concordantly, insulin receptor (IR), IR substrate type 1 (IRS1), IRS2, and protein kinase B (AKT) phosphorylation in adipose tissue and skeletal muscle was improved by citrate ICV treatment.	citrate icv	168-179	insulin receptor	Rattus norvegicus	32-34
18089761-5	2008	By itself, H(2)O(2) significantly (P &lt; 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
18401942-0	2008	Effects of dexamethasone on insulin receptor in aging.	Dexamethasone	11-24	insulin receptor	Rattus norvegicus	28-44
18401942-1	2008	The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR).	Dexamethasone	52-65	insulin receptor	Rattus norvegicus	108-124
18401942-1	2008	The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR).	Dexamethasone	52-65	insulin receptor	Rattus norvegicus	126-128
18401942-1	2008	The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR).	Dexamethasone	67-70	insulin receptor	Rattus norvegicus	108-124
18089761-5	2008	By itself, H(2)O(2) significantly (P &lt; 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)).	Serine	209-212	insulin receptor	Rattus norvegicus	180-196
18401942-1	2008	The aim of this study was to examine the effects of dexamethasone (Dex) on functional properties of the rat insulin receptor (IR).	Dexamethasone	67-70	insulin receptor	Rattus norvegicus	126-128
18401942-4	2008	In addition, Dex treatment lowered the liver IR protein level in all analyzed groups, except 21-month-old rats where it remained unchanged, but raised the IR mRNA level in 18-month-old rats.	Dexamethasone	13-16	insulin receptor	Rattus norvegicus	45-47
18089761-5	2008	By itself, H(2)O(2) significantly (P &lt; 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)).	Serine	235-238	insulin receptor	Rattus norvegicus	180-196
18401942-4	2008	In addition, Dex treatment lowered the liver IR protein level in all analyzed groups, except 21-month-old rats where it remained unchanged, but raised the IR mRNA level in 18-month-old rats.	Dexamethasone	13-16	insulin receptor	Rattus norvegicus	155-157
18089761-7	2008	In the presence of CT-98014, a selective GSK-3 inhibitor, the ability of insulin to stimulate glucose transport and glycogen synthesis during exposure to this oxidant stress was enhanced by 20% and 39% (P &lt; 0.05), respectively, and insulin stimulation of the phosphorylation of insulin receptor, Akt, and GSK-3 was significantly increased by 36-58% (P &lt; 0.05).	Chir 98014	19-27	insulin receptor	Rattus norvegicus	281-297
18401942-7	2008	In summary, Dex exerts the strongest effect on the erythrocyte IR of 3- and 6-month-old rats and the hepatic IR of 18-month-old rats.	Dexamethasone	12-15	insulin receptor	Rattus norvegicus	63-65
18401942-7	2008	In summary, Dex exerts the strongest effect on the erythrocyte IR of 3- and 6-month-old rats and the hepatic IR of 18-month-old rats.	Dexamethasone	12-15	insulin receptor	Rattus norvegicus	109-111
18401942-9	2008	The pattern of age-related changes of IR induced by Dex does not correlate with changes of plasma Glu and INS.	Dexamethasone	52-55	insulin receptor	Rattus norvegicus	38-40
18245813-7	2008	Iron depletion of Sprague-Dawley rats increased HIF-1alpha expression, improved glucose clearance, and was associated with up-regulation of insulin receptor and Akt/PKB levels and of glucose transport in hepatic tissue.	Iron	0-4	insulin receptor	Rattus norvegicus	140-156
18245813-10	2008	Thus, iron depletion by deferoxamine up-regulates glucose uptake, and increases insulin receptor activity and signaling in hepatocytes in vitro and in vivo.	Iron	6-10	insulin receptor	Rattus norvegicus	80-96
18245813-4	2008	Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta.	Deferoxamine	37-49	insulin receptor	Rattus norvegicus	17-33
18245813-10	2008	Thus, iron depletion by deferoxamine up-regulates glucose uptake, and increases insulin receptor activity and signaling in hepatocytes in vitro and in vivo.	Deferoxamine	24-36	insulin receptor	Rattus norvegicus	80-96
18245813-4	2008	Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta.	Iron	84-88	insulin receptor	Rattus norvegicus	17-33
18245813-4	2008	Up-regulation of insulin receptor by deferoxamine was mimicked by the intracellular iron chelator deferasirox and the hypoxia inducer CoCl2 and required the HIF-1 obligate partner ARNT/HIF-1beta.	cobaltous chloride	134-139	insulin receptor	Rattus norvegicus	17-33
18331706-0	2008	Early changes in insulin receptor signaling and pain sensation in streptozotocin-induced diabetic neuropathy in rats.	Streptozocin	66-80	insulin receptor	Rattus norvegicus	17-33
18245813-5	2008	Iron depletion increased insulin receptor activity, whereas iron supplementation had the opposite effect.	Iron	0-4	insulin receptor	Rattus norvegicus	25-41
18376071-0	2008	Effect of tetrahydrocurcumin on insulin receptor status in type 2 diabetic rats: studies on insulin binding to erythrocytes.	tetrahydrocurcumin	10-28	insulin receptor	Rattus norvegicus	32-48
18331706-1	2008	UNLABELLED: The objective of the present study was to evaluate the time course of changes in peripheral nerve insulin receptor (IR) signaling and compare observed findings with behavioral responses to noxious mechanical and thermal stimuli in streptozotocin (STZ)-diabetic rats over 12 weeks of diabetes.	Streptozocin	243-257	insulin receptor	Rattus norvegicus	110-126
18331706-4	2008	To our knowledge, the present study is the first to demonstrate that impaired peripheral nerve IR signaling, as indicated by decreased phosphorylated:total IR protein ratio, coincides with early mechanical hyperalgesia and thermal hypoalgesia in STZ-diabetic rats.	Streptozocin	246-249	insulin receptor	Rattus norvegicus	95-97
18331706-4	2008	To our knowledge, the present study is the first to demonstrate that impaired peripheral nerve IR signaling, as indicated by decreased phosphorylated:total IR protein ratio, coincides with early mechanical hyperalgesia and thermal hypoalgesia in STZ-diabetic rats.	Streptozocin	246-249	insulin receptor	Rattus norvegicus	156-158
18331706-6	2008	PERSPECTIVE: This study examined peripheral nerve IR signaling during the early course of altered nociception in STZ-diabetic rats.	Streptozocin	113-116	insulin receptor	Rattus norvegicus	50-52
18331706-7	2008	In diabetic rats, impaired peripheral nerve IR signaling is observed shortly after STZ injection, as is altered nociception.	Streptozocin	83-86	insulin receptor	Rattus norvegicus	44-46
17950991-6	2007	The concentration of cell-surface LH and prolactin receptors were significantly reduced after corticosterone exposure whereas the concentration of insulin receptor was diminished only at 200-800 nM doses of corticosterone.	Corticosterone	207-221	insulin receptor	Rattus norvegicus	147-163
18215309-4	2008	The aim of the present study is to examine: (1) whether a specific respiratory substrate, dicholine salt of succinic acid (CS), can enhance insulin-stimulated insulin receptor autophosphorylation in neurons, and (2) whether CS can ameliorate cognitive deficits of various origins in animal models.	dicholine salt	90-104	insulin receptor	Rattus norvegicus	159-175
18215309-4	2008	The aim of the present study is to examine: (1) whether a specific respiratory substrate, dicholine salt of succinic acid (CS), can enhance insulin-stimulated insulin receptor autophosphorylation in neurons, and (2) whether CS can ameliorate cognitive deficits of various origins in animal models.	Succinic Acid	108-121	insulin receptor	Rattus norvegicus	159-175
18215309-4	2008	The aim of the present study is to examine: (1) whether a specific respiratory substrate, dicholine salt of succinic acid (CS), can enhance insulin-stimulated insulin receptor autophosphorylation in neurons, and (2) whether CS can ameliorate cognitive deficits of various origins in animal models.	Cesium	123-125	insulin receptor	Rattus norvegicus	159-175
18215309-5	2008	RESULTS: In a primary culture of cerebellar granule neurons, CS significantly enhanced insulin-stimulated insulin receptor autophosphorylation.	Cesium	61-63	insulin receptor	Rattus norvegicus	106-122
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.	Melatonin	114-123	insulin receptor	Rattus norvegicus	175-191
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
18078453-5	2008	This indoleamine may regulate growth and differentiation of pancreatic islets by activating IGF-I and insulin receptor signaling pathways.	indolamine	5-16	insulin receptor	Rattus norvegicus	102-118
17950991-7	2007	The levels of LH and prolactin receptor mRNAs were significantly decreased after corticosterone (100-800 nM) exposure whereas the mRNA level of insulin receptor was significantly reduced only at 800 nM dose of corticosterone.	Corticosterone	210-224	insulin receptor	Rattus norvegicus	144-160
17697867-2	2007	In vitro study findings show that chromium picolinate (CrPic) may improve insulin sensitivity by enhancing intracellular insulin receptor.	picolinic acid	34-53	insulin receptor	Rattus norvegicus	121-137
17912465-8	2007	The supplementation of glucose (10, 25, or 50 mg/ml) caused a significant increase in Insr and PI3K mRNA levels in wild-type cells.	Glucose	23-30	insulin receptor	Rattus norvegicus	86-90
17976658-6	2007	Myricetin was found to reverse the defect in expression of insulin receptor substrate-1 (IRS-1) and the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI 3-kinase) in soleus muscle of fructose chow-fed rats under the basal state, despite the protein expression of insulin receptor (IR).	myricetin	0-9	insulin receptor	Rattus norvegicus	59-75
17976658-6	2007	Myricetin was found to reverse the defect in expression of insulin receptor substrate-1 (IRS-1) and the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI 3-kinase) in soleus muscle of fructose chow-fed rats under the basal state, despite the protein expression of insulin receptor (IR).	myricetin	0-9	insulin receptor	Rattus norvegicus	89-91
17976658-6	2007	Myricetin was found to reverse the defect in expression of insulin receptor substrate-1 (IRS-1) and the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI 3-kinase) in soleus muscle of fructose chow-fed rats under the basal state, despite the protein expression of insulin receptor (IR).	Fructose	194-202	insulin receptor	Rattus norvegicus	59-75
17976658-6	2007	Myricetin was found to reverse the defect in expression of insulin receptor substrate-1 (IRS-1) and the p85 regulatory subunit of phosphatidylinositol 3-kinase (PI 3-kinase) in soleus muscle of fructose chow-fed rats under the basal state, despite the protein expression of insulin receptor (IR).	Fructose	194-202	insulin receptor	Rattus norvegicus	89-91
17976658-8	2007	The reduced level of insulin action on phosphorylation of IR, IRS-1 and Akt in soleus muscle of fructose chow-fed rats was reversed by myricetin treatment.	Fructose	96-104	insulin receptor	Rattus norvegicus	58-60
17976658-8	2007	The reduced level of insulin action on phosphorylation of IR, IRS-1 and Akt in soleus muscle of fructose chow-fed rats was reversed by myricetin treatment.	myricetin	135-144	insulin receptor	Rattus norvegicus	58-60
17855644-4	2007	Treatment of insulin resistance in Zucker rats with the insulin-sensitizing drug rosiglitazone partially restored renal insulin receptor levels.	Rosiglitazone	81-94	insulin receptor	Rattus norvegicus	120-136
17855644-5	2007	Conversely, treatment with the angiotensin II type 1 receptor (AT1) antagonist candesartan increased renal insulin receptor expression compared to untreated rats.	candesartan	79-90	insulin receptor	Rattus norvegicus	107-123
17697867-2	2007	In vitro study findings show that chromium picolinate (CrPic) may improve insulin sensitivity by enhancing intracellular insulin receptor.	picolinic acid	55-60	insulin receptor	Rattus norvegicus	121-137
17673259-4	2007	The present study has been designed to assess the impact of testosterone on insulin receptor gene expression and glucose oxidation in target tissues of adult male rat.	Testosterone	60-72	insulin receptor	Rattus norvegicus	76-92
17068109-3	2007	In addition, we attempted to demonstrate the role of 17beta-oestradiol and progesterone on insulin sensitivity, focusing on their effects on key proteins of skeletal muscle, insulin receptor (IR) and glucose transporter-4 (Glut-4).	Estradiol	53-70	insulin receptor	Rattus norvegicus	192-194
17555093-0	2007	[Effect of chronic ethanol intake on insulin receptor, insulin receptor subsrate-1 and phosphoinositide 3-kinase mRNA expression in skeletal muscle of rats].	Ethanol	19-26	insulin receptor	Rattus norvegicus	55-71
17555093-1	2007	OBJECTIVE: To study the effect of chronic ethanol intake on insulin receptor (IR), insulin receptor substrate-1 (IRS-1) and p85 subunit of phosphoinositide 3-kinase (PI-3K) mRNA expression in skeletal muscle of rats and explore the molecular mechanism of ethanol induced insulin resistance.	Ethanol	42-49	insulin receptor	Rattus norvegicus	60-76
17555093-8	2007	RESULTS: In male rats, the fasting plasma glucose of group H, fasting plasma insulin of group L, M and HOMA-IR indexes of all ethanol-fed groups were higher than those of group C (P &lt; 0.05).	Ethanol	126-133	insulin receptor	Rattus norvegicus	108-110
17555093-12	2007	CONCLUSION: The present results suggested that chronic ethanol intake could induce insulin resistance and down-regulated the expression of IR, IRS-land PI-3K mRNA in skeletal muscle could be the molecular mechanism.	Ethanol	55-62	insulin receptor	Rattus norvegicus	139-141
17409686-8	2007	GM3 depletion was able to counteract the TNFalpha-induced inhibition of IR accumulation into DRMs.	gm3	0-3	insulin receptor	Rattus norvegicus	72-74
17274632-0	2007	Alpha-lipoic acid as a directly binding activator of the insulin receptor: protection from hepatocyte apoptosis.	Thioctic Acid	0-17	insulin receptor	Rattus norvegicus	57-73
17274632-9	2007	Alpha-lipoic acid but not other antioxidants protected against actinomycinD/TNF-alpha-induced apoptosis via phosphorylation of the insulin receptor.	Thioctic Acid	0-17	insulin receptor	Rattus norvegicus	131-147
17274632-9	2007	Alpha-lipoic acid but not other antioxidants protected against actinomycinD/TNF-alpha-induced apoptosis via phosphorylation of the insulin receptor.	Dactinomycin	63-75	insulin receptor	Rattus norvegicus	131-147
17274632-10	2007	Computer modeling studies revealed a direct binding site for alpha-lipoic acid at the tyrosine kinase domain of the insulin receptor, suggesting a stabilizing function in loop A that is involved in ATP binding.	Thioctic Acid	61-78	insulin receptor	Rattus norvegicus	116-132
17274632-10	2007	Computer modeling studies revealed a direct binding site for alpha-lipoic acid at the tyrosine kinase domain of the insulin receptor, suggesting a stabilizing function in loop A that is involved in ATP binding.	Adenosine Triphosphate	198-201	insulin receptor	Rattus norvegicus	116-132
17274632-12	2007	CONCLUSIONS: Alpha-lipoic acid mediates its antiapoptotic action via activation of the insulin receptor/PI3-kinase/Akt pathway.	Thioctic Acid	13-30	insulin receptor	Rattus norvegicus	87-103
17274632-13	2007	We show for the first time a direct binding site for alpha-lipoic acid at the insulin receptor tyrosine kinase domain, which might make alpha-lipoic acid a model substance for the development of insulin mimetics.	Thioctic Acid	53-70	insulin receptor	Rattus norvegicus	78-94
17274632-13	2007	We show for the first time a direct binding site for alpha-lipoic acid at the insulin receptor tyrosine kinase domain, which might make alpha-lipoic acid a model substance for the development of insulin mimetics.	Thioctic Acid	136-153	insulin receptor	Rattus norvegicus	78-94
17068109-3	2007	In addition, we attempted to demonstrate the role of 17beta-oestradiol and progesterone on insulin sensitivity, focusing on their effects on key proteins of skeletal muscle, insulin receptor (IR) and glucose transporter-4 (Glut-4).	Progesterone	75-87	insulin receptor	Rattus norvegicus	174-190
17068109-3	2007	In addition, we attempted to demonstrate the role of 17beta-oestradiol and progesterone on insulin sensitivity, focusing on their effects on key proteins of skeletal muscle, insulin receptor (IR) and glucose transporter-4 (Glut-4).	Progesterone	75-87	insulin receptor	Rattus norvegicus	192-194
17426391-6	2007	However, insulin-stimulated phosphorylation of the IR, total Akt levels and total GLUT4 levels were reduced in CORT-treated rats when compared to controls.	Corticosterone	111-115	insulin receptor	Rattus norvegicus	51-53
16880599-8	2006	GM3 depletion was able to counteract the TNFalpha-induced inhibition of IR accumulation into DRMs.	gm3	0-3	insulin receptor	Rattus norvegicus	72-74
16978790-8	2006	Application of the IR sensitizer metformin moderately improved neuronal viability, while the specific IR tyrosine kinase inhibitor tyrphostin A47 was able to dramatically decrease viability; both compounds acted without affecting IR surface expression.	tyrphostin 47	131-145	insulin receptor	Rattus norvegicus	102-104
17064471-1	2006	OBJECTIVE: To explore the effects of pentoxifylline (PTX) on nuclear factor-kappa B (NF-kB) signaling pathway, insulin receptor substrates (IRSs) and glucose transporter 2 (GLUT2) expressions in livers in a rat model of nonalcoholic steatohepatitis (NASH).	Pentoxifylline	53-56	insulin receptor	Rattus norvegicus	111-127
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
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
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.	Glucose	168-175	insulin receptor	Rattus norvegicus	71-75
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
17132543-1	2006	In the present study, we focused on the insulin-receptor binding in circulating erythrocytes of N-benzoyl-D-phenylalanine (NBDP) and metformin in neonatal streptozotocin (nSTZ)-induced male Wistar rats.	benzoylphenylalanine	96-121	insulin receptor	Rattus norvegicus	40-56
17132543-1	2006	In the present study, we focused on the insulin-receptor binding in circulating erythrocytes of N-benzoyl-D-phenylalanine (NBDP) and metformin in neonatal streptozotocin (nSTZ)-induced male Wistar rats.	benzoylphenylalanine	123-127	insulin receptor	Rattus norvegicus	40-56
17132543-1	2006	In the present study, we focused on the insulin-receptor binding in circulating erythrocytes of N-benzoyl-D-phenylalanine (NBDP) and metformin in neonatal streptozotocin (nSTZ)-induced male Wistar rats.	Metformin	133-142	insulin receptor	Rattus norvegicus	40-56
17132543-1	2006	In the present study, we focused on the insulin-receptor binding in circulating erythrocytes of N-benzoyl-D-phenylalanine (NBDP) and metformin in neonatal streptozotocin (nSTZ)-induced male Wistar rats.	Streptozocin	155-169	insulin receptor	Rattus norvegicus	40-56
17132543-1	2006	In the present study, we focused on the insulin-receptor binding in circulating erythrocytes of N-benzoyl-D-phenylalanine (NBDP) and metformin in neonatal streptozotocin (nSTZ)-induced male Wistar rats.	nstz	171-175	insulin receptor	Rattus norvegicus	40-56
16567541-3	2006	Using the streptozotocin-induced diabetic rat model, we tested the hypothesis that diabetes diminishes basal retinal insulin receptor signaling concomitantly with increased diabetes-induced retinal apoptosis.	Streptozocin	10-24	insulin receptor	Rattus norvegicus	117-133
16877964-4	2006	Furthermore, in a previous study we illustrated that obese Zucker rats (OZR) present increased serine 994 (Ser994) phosphorylation of hepatic insulin receptor, and this event seems to be implicated in the regulation of the intrinsic IRK in this model of insulin resistance.	Serine	95-101	insulin receptor	Rattus norvegicus	142-158
16169204-0	2006	Insulin receptor exon 11+/- is expressed in Zucker (fa/fa) rats, and chlorogenic acid modifies their plasma insulin and liver protein and DNA.	Chlorogenic Acid	69-85	insulin receptor	Rattus norvegicus	0-16
16424121-2	2006	Recent in vitro studies suggest that chromium supplementation may improve insulin sensitivity by enhancing insulin receptor signaling, but this has not been demonstrated in vivo.	Chromium	37-45	insulin receptor	Rattus norvegicus	107-123
16424121-3	2006	We investigated the effect of chromium supplementation on insulin receptor signaling in an insulin-resistant rat model, the JCR:LA-corpulent rat.	Chromium	30-38	insulin receptor	Rattus norvegicus	58-74
17207412-10	2006	The improvement in glucose tolerance at 120 min by Gynostemma pentaphyllum in obese Zucker fatty rats but not lean rats suggests that it may improve insulin receptor sensitivity and together with the significant reduction of hypertriglyceridemia, cholesterol and low density lipoprotein cholesterol suggests that Gynostemma should be examined further by oral hypoglycemic/anti-hyperlipidemic therapy.	Glucose	19-26	insulin receptor	Rattus norvegicus	149-165
16052330-7	2005	Activation of AMPK by 5-amino-imidazolecarboxamide riboside (AICAR, 0.5 mmol/l) suppressed Pklr expression, but strongly stimulated gene expression of Igf1r, Insr and Insrr.	5-amino-imidazolecarboxamide riboside	22-59	insulin receptor	Rattus norvegicus	158-162
16052330-0	2005	Glucose concentration and AMP-dependent kinase activation regulate expression of insulin receptor family members in rat islets and INS-1E beta cells.	Glucose	0-7	insulin receptor	Rattus norvegicus	81-97
16237195-16	2006	Our results suggest that the IR and/or IGF-IR signaling pathway may be involved in the mechanism of action of HCB.	Hexachlorobenzene	110-113	insulin receptor	Rattus norvegicus	29-31
16052330-7	2005	Activation of AMPK by 5-amino-imidazolecarboxamide riboside (AICAR, 0.5 mmol/l) suppressed Pklr expression, but strongly stimulated gene expression of Igf1r, Insr and Insrr.	acadesine	61-66	insulin receptor	Rattus norvegicus	158-162
16052330-3	2005	MATERIALS AND METHODS: We hypothesised that glucose concentration might regulate expression of Igf1r, Insr and insulin receptor-related receptor (Insrr) in islets and beta cells.	Glucose	44-51	insulin receptor	Rattus norvegicus	102-106
16052330-5	2005	RESULTS: In rat islets, high glucose exposure (25 mmol/l) increased gene expression of Igf1r, Insr and Insrr but also of the metabolic glycolysis gene liver-type pyruvate kinase (Pklr) compared with intermediate (6.2 mmol/l) or low glucose concentration (1.6 mmol/l) after 24 h. In rat INS-1E beta cells, only Pklr expression was suppressed by low glucose as in islets, while Insr and Insrr were suppressed by high and increased by low glucose levels.	Glucose	29-36	insulin receptor	Rattus norvegicus	94-98
16052330-5	2005	RESULTS: In rat islets, high glucose exposure (25 mmol/l) increased gene expression of Igf1r, Insr and Insrr but also of the metabolic glycolysis gene liver-type pyruvate kinase (Pklr) compared with intermediate (6.2 mmol/l) or low glucose concentration (1.6 mmol/l) after 24 h. In rat INS-1E beta cells, only Pklr expression was suppressed by low glucose as in islets, while Insr and Insrr were suppressed by high and increased by low glucose levels.	Glucose	29-36	insulin receptor	Rattus norvegicus	103-107
15514089-1	2005	Angiotensin II inhibits insulin-induced activation of phosphatidylinositol 3-kinase through a mechanism, at least in part, dependent on serine phosphorylation of the insulin receptor and insulin receptor substrates (IRS)-1/2.	Serine	136-142	insulin receptor	Rattus norvegicus	166-182
15889998-6	2005	Phosphorylation of the insulin receptor, IRS-1, and Akt in response to insulin was also significantly enhanced in high glucose conditions, especially at submaximal insulin concentrations.	Glucose	119-126	insulin receptor	Rattus norvegicus	23-39
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
15514089-6	2005	The inhibition of SOCS-3 expression by a phosphorthioate-modified antisense oligonucleotide partially restores angiotensin II-induced inhibition of insulin-induced insulin receptor, IRS-1 and IRS-2 tyrosine phosphorylation, and IRS-1 and IRS-2 association with p85-phosphatidylinositol 3-kinase and [Ser473] phosphorylation of Akt.	Oligonucleotides	76-91	insulin receptor	Rattus norvegicus	164-180
15692100-4	2005	The insulin receptor signaling pathway was partially activated under physiological conditions, further activated by intravenous insulin injection, and was attenuated in streptozotocin-induced diabetic rats.	Streptozocin	169-183	insulin receptor	Rattus norvegicus	4-20
15514089-6	2005	The inhibition of SOCS-3 expression by a phosphorthioate-modified antisense oligonucleotide partially restores angiotensin II-induced inhibition of insulin-induced insulin receptor, IRS-1 and IRS-2 tyrosine phosphorylation, and IRS-1 and IRS-2 association with p85-phosphatidylinositol 3-kinase and [Ser473] phosphorylation of Akt.	phosphorthioate	41-56	insulin receptor	Rattus norvegicus	164-180
16301821-0	2005	Inhibition of insulin receptor gene expression and insulin signaling by fatty acid: interplay of PKC isoforms therein.	Fatty Acids	72-82	insulin receptor	Rattus norvegicus	14-30
15662227-7	2005	In addition, losartan seemed to mediate the upregulation of insulin receptor density on cardiomyocytes and skeletal muscle, and increase insulin receptor affinity at the coronary endothelial site.	Losartan	13-21	insulin receptor	Rattus norvegicus	60-76
15662227-7	2005	In addition, losartan seemed to mediate the upregulation of insulin receptor density on cardiomyocytes and skeletal muscle, and increase insulin receptor affinity at the coronary endothelial site.	Losartan	13-21	insulin receptor	Rattus norvegicus	137-153
15665515-9	2005	We conclude that IR and GLUT2 form a receptor-transporter complex in hepatocytes, which forms a mechanism of insulin-mediated hepatic glucose regulation.	Glucose	134-141	insulin receptor	Rattus norvegicus	17-19
16301821-8	2005	Time kinetics study showed translocation of palmitate induced phosphorylated PKCepsilon from cell membrane to nuclear region and its possible association with the inhibition of IR gene transcription.	Palmitates	44-53	insulin receptor	Rattus norvegicus	177-179
15717064-5	2005	The liposome is targeted across the BBB via attachment to the tips of 1-2% of the PEG strands of a receptor-specific monoclonal antibody (mAb) directed at a BBB receptor, such as the insulin receptor or transferrin receptor (TfR).	Polyethylene Glycols	82-85	insulin receptor	Rattus norvegicus	183-199
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
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.	Nitric Oxide	266-278	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
15663202-1	2004	Fuji ground water improves hypo-activity of liver insulin receptor in Goto-Kakisaki rats.	Water	12-17	insulin receptor	Rattus norvegicus	50-66
15663202-5	2004	These results suggest that daily treatment with small concentrations of natural vanadium improves hyperglycemia by ameliorating liver insulin receptor activity.	Vanadium	80-88	insulin receptor	Rattus norvegicus	134-150
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
15350185-1	2004	Serine phosphorylation of the insulin receptor (IR) has been proposed to exert an inhibitory influence on its tyrosine kinase activity.	Serine	0-6	insulin receptor	Rattus norvegicus	30-51
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
15350185-2	2004	Previous works using site-directed mutagenesis suggested that serine 994 of the IR (IR Ser 994) might be part of an inhibitory domain of the receptor.	Serine	62-68	insulin receptor	Rattus norvegicus	80-82
15350185-2	2004	Previous works using site-directed mutagenesis suggested that serine 994 of the IR (IR Ser 994) might be part of an inhibitory domain of the receptor.	Serine	62-68	insulin receptor	Rattus norvegicus	84-86
15350185-2	2004	Previous works using site-directed mutagenesis suggested that serine 994 of the IR (IR Ser 994) might be part of an inhibitory domain of the receptor.	Serine	87-90	insulin receptor	Rattus norvegicus	80-82
15350185-2	2004	Previous works using site-directed mutagenesis suggested that serine 994 of the IR (IR Ser 994) might be part of an inhibitory domain of the receptor.	Serine	87-90	insulin receptor	Rattus norvegicus	84-86
15350185-4	2004	We used a site-phosphospecific antibody to determine the extent of phosphorylation of IR Ser 994 in insulin target tissues from two animal models of insulin resistance with different IR kinase (IRK) activity: obese (fa/fa) Zucker rats and transgenic mice overexpressing bovine growth hormone (PEPCK-bGH mice).	Serine	89-92	insulin receptor	Rattus norvegicus	86-88
15350185-5	2004	Phosphorylation at IR Ser 994 was markedly increased in liver of obese rats.	Serine	22-25	insulin receptor	Rattus norvegicus	19-21
15350185-7	2004	On the other hand, the phosphorylation level of IR Ser 994 was very low in liver of PEPCK-bGH mice and did not differ from that of the control group.	Serine	51-54	insulin receptor	Rattus norvegicus	48-50
15350185-8	2004	We have also demonstrated that protein kinase (PK) C isoforms alpha, betaI and zeta are able to promote the in vitro phosphorylation of the IR on Ser 994.	Serine	146-149	insulin receptor	Rattus norvegicus	140-142
15350185-10	2004	Our results suggest that Ser 994 is a novel in vivo IR phosphorylation site that might be involved in the regulation of the IRK in some states of insulin resistance.	Serine	25-28	insulin receptor	Rattus norvegicus	52-54
15326568-7	2004	Insulin resistance in rats induced by excess fructose was associated with the impaired insulin receptor (IR), tyrosine autophosphorylation, and insulin receptor substrate (IRS)-1 protein content in addition to the significant decrease in IRS-1 tyrosine phosphorylation in soleus muscle.	Fructose	45-53	insulin receptor	Rattus norvegicus	87-103
15326568-7	2004	Insulin resistance in rats induced by excess fructose was associated with the impaired insulin receptor (IR), tyrosine autophosphorylation, and insulin receptor substrate (IRS)-1 protein content in addition to the significant decrease in IRS-1 tyrosine phosphorylation in soleus muscle.	Fructose	45-53	insulin receptor	Rattus norvegicus	105-107
15134829-3	2004	The extent and duration of IR endocytosis were markedly increased in response to the H2-analogue and [Asp(B10)]HI compared to wild-type HI, but similar to HI after [Glu(A13),Glu(B10)]HI administration.	Hydrogen	85-87	insulin receptor	Rattus norvegicus	27-29
15018609-6	2004	Complexes of thyronine-insulin analogues with thyroid hormone binding proteins exhibit impaired insulin receptor binding affinities compared with those of the analogues in their free form.	Thyronines	13-22	insulin receptor	Rattus norvegicus	96-112
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
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
15004002-2	2004	In the present study, we tested the hypothesis that these changes in glucose transport in 3- and 7-day HS soleus of juvenile, female Sprague-Dawley rats were due to increased functionality of insulin signaling factors, including insulin receptor (IR), IR substrate-1 (IRS-1), phosphatidylinositol 3-kinase (PI3-kinase), and Akt.	Glucose	69-76	insulin receptor	Rattus norvegicus	229-245
15004002-2	2004	In the present study, we tested the hypothesis that these changes in glucose transport in 3- and 7-day HS soleus of juvenile, female Sprague-Dawley rats were due to increased functionality of insulin signaling factors, including insulin receptor (IR), IR substrate-1 (IRS-1), phosphatidylinositol 3-kinase (PI3-kinase), and Akt.	Glucose	69-76	insulin receptor	Rattus norvegicus	247-249
15134829-3	2004	The extent and duration of IR endocytosis were markedly increased in response to the H2-analogue and [Asp(B10)]HI compared to wild-type HI, but similar to HI after [Glu(A13),Glu(B10)]HI administration.	Aspartic Acid	102-105	insulin receptor	Rattus norvegicus	27-29
15134829-5	2004	A low cell-free endosome-lysosome transfer of the internalized IR was only observed in response to HI and H2-analogue injection.	Histidine	99-101	insulin receptor	Rattus norvegicus	63-65
15134829-5	2004	A low cell-free endosome-lysosome transfer of the internalized IR was only observed in response to HI and H2-analogue injection.	Hydrogen	106-108	insulin receptor	Rattus norvegicus	63-65
14991460-3	2004	Intracerebroventricular injection of streptozotocin (STZ), which inhibits insulin receptor function, develops long-term and progressive deficits in learning, memory and cognitive behavior as well as biochemical changes and neuronal degeneration in rats similar to SAD.	Streptozocin	37-51	insulin receptor	Rattus norvegicus	74-90
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
14991460-3	2004	Intracerebroventricular injection of streptozotocin (STZ), which inhibits insulin receptor function, develops long-term and progressive deficits in learning, memory and cognitive behavior as well as biochemical changes and neuronal degeneration in rats similar to SAD.	Streptozocin	53-56	insulin receptor	Rattus norvegicus	74-90
14607280-3	2004	Decapeptides modelled on insulin receptor sequences surrounding serines 1035 and 1270 were found to inhibit protein kinase C activity in vitro and after microinjection into cells blocked the inhibition of mitogenesis induced by glucose.	Serine	64-71	insulin receptor	Rattus norvegicus	25-41
14607280-3	2004	Decapeptides modelled on insulin receptor sequences surrounding serines 1035 and 1270 were found to inhibit protein kinase C activity in vitro and after microinjection into cells blocked the inhibition of mitogenesis induced by glucose.	Glucose	228-235	insulin receptor	Rattus norvegicus	25-41
14573337-6	2003	The insulin receptor number was significantly lower in both skeletal muscle and liver of fructose-fed rats as compared to controls, whereas no difference was observed in the kidney.	Fructose	89-97	insulin receptor	Rattus norvegicus	4-20
14595539-0	2003	Rosiglitazone produces insulin sensitisation by increasing expression of the insulin receptor and its tyrosine kinase activity in brown adipocytes.	Rosiglitazone	0-13	insulin receptor	Rattus norvegicus	77-93
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.	Rosiglitazone	48-61	insulin receptor	Rattus norvegicus	107-123
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
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.	Rosiglitazone	0-13	insulin receptor	Rattus norvegicus	34-50
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.	Rosiglitazone	0-13	insulin receptor	Rattus norvegicus	108-124
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
14595539-12	2003	CONCLUSIONS/INTERPRETATION: At the insulin receptor level, rosiglitazone-induced improvements of insulin sensitivity result from two convergent mechanisms: increased insulin receptor expression and insulin receptor activation.	Rosiglitazone	59-72	insulin receptor	Rattus norvegicus	35-51
14595539-12	2003	CONCLUSIONS/INTERPRETATION: At the insulin receptor level, rosiglitazone-induced improvements of insulin sensitivity result from two convergent mechanisms: increased insulin receptor expression and insulin receptor activation.	Rosiglitazone	59-72	insulin receptor	Rattus norvegicus	166-182
14595539-12	2003	CONCLUSIONS/INTERPRETATION: At the insulin receptor level, rosiglitazone-induced improvements of insulin sensitivity result from two convergent mechanisms: increased insulin receptor expression and insulin receptor activation.	Rosiglitazone	59-72	insulin receptor	Rattus norvegicus	166-182
14633139-8	2003	An inverse relationship between dietary NaCl content and renal insulin receptor mRNA levels was observed in control but not fructose-fed rats.	Sodium Chloride	40-44	insulin receptor	Rattus norvegicus	63-79
14633139-9	2003	CONCLUSION: Fructose-fed rats appear to have lost the feedback mechanism that limits insulin-induced sodium retention through a down-regulation of the renal insulin receptor when the dietary NaCl content is increased.	Fructose	12-20	insulin receptor	Rattus norvegicus	157-173
14633139-9	2003	CONCLUSION: Fructose-fed rats appear to have lost the feedback mechanism that limits insulin-induced sodium retention through a down-regulation of the renal insulin receptor when the dietary NaCl content is increased.	Sodium Chloride	191-195	insulin receptor	Rattus norvegicus	157-173
14719033-10	2003	High CK activity and hyperglycemia maintain the energy demands of metabolism, and elevated corticosterone desensitizes the insulin receptor in AS.	Corticosterone	91-105	insulin receptor	Rattus norvegicus	123-139
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
14633139-5	2003	When the rats were fed the low-salt diet, the rate of glucose infusion required to maintain euglycemia during a hyperinsulinemic clamp and insulin receptor number and mRNA levels in skeletal muscle were lower in fructose-fed than control rats.	Fructose	212-220	insulin receptor	Rattus norvegicus	139-155
14633139-6	2003	High-salt diet decreased significantly the rate of glucose disposal during the clamp and muscular insulin receptor number and mRNA levels in control, but not fructose-fed rats.	Salts	5-9	insulin receptor	Rattus norvegicus	98-114
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
12937785-2	2003	It is known that intracerebroventricular (icv) injection of nondiabetogenic doses of streptozotocin (STZ) can damage insulin receptor signal transduction.	Streptozocin	85-99	insulin receptor	Rattus norvegicus	117-133
12937785-2	2003	It is known that intracerebroventricular (icv) injection of nondiabetogenic doses of streptozotocin (STZ) can damage insulin receptor signal transduction.	Streptozocin	101-104	insulin receptor	Rattus norvegicus	117-133
12937785-8	2003	Excluding the possibility of a direct action of STZ on central insulin receptor-carrying neurons, the current data suggest that the insulin-sensitive response may be processed through dopaminergic D1 receptors containing neuronal pathways.	Streptozocin	48-51	insulin receptor	Rattus norvegicus	63-79
14506612-0	2003	Rats that are made insulin resistant by glucosamine treatment have impaired skeletal muscle insulin receptor phosphorylation.	Glucosamine	40-51	insulin receptor	Rattus norvegicus	92-108
14506612-1	2003	The current study sought to verify whether glucosamine (GlcN)-induced insulin resistance is associated with impaired insulin receptor (IR) autophosphorylation.	Glucosamine	43-54	insulin receptor	Rattus norvegicus	117-133
14506612-1	2003	The current study sought to verify whether glucosamine (GlcN)-induced insulin resistance is associated with impaired insulin receptor (IR) autophosphorylation.	Glucosamine	43-54	insulin receptor	Rattus norvegicus	135-137
14506612-1	2003	The current study sought to verify whether glucosamine (GlcN)-induced insulin resistance is associated with impaired insulin receptor (IR) autophosphorylation.	Glucosamine	56-60	insulin receptor	Rattus norvegicus	117-133
14506612-1	2003	The current study sought to verify whether glucosamine (GlcN)-induced insulin resistance is associated with impaired insulin receptor (IR) autophosphorylation.	Glucosamine	56-60	insulin receptor	Rattus norvegicus	135-137
14506612-8	2003	Our data show that GlcN-induced insulin resistance is mediated, at least in part, by impaired skeletal muscle IR autophosphorylation.	Glucosamine	19-23	insulin receptor	Rattus norvegicus	110-112
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
14535634-3	2003	LH exposure (100 and 200 ng dose) caused a significant increase in Leydig cell surface and internalized insulin receptor concentrations.	Luteinizing Hormone	0-2	insulin receptor	Rattus norvegicus	104-120
12700235-2	2003	Previous in vitro studies demonstrated ethanol-impaired neuronal survival with reduced signaling through the insulin receptor (IRbeta).	Ethanol	39-46	insulin receptor	Rattus norvegicus	109-125
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
12782313-6	2003	This is the first evidence that short exposure of these cells to 100 microM palmitate activates the early steps of insulin receptor signalling.	Palmitates	76-85	insulin receptor	Rattus norvegicus	115-131
12782313-8	2003	Cerulenin, an acylation inhibitor, abolished the palmitate effect on protein levels and phosphorylation of insulin receptor.	Cerulenin	0-9	insulin receptor	Rattus norvegicus	107-123
12381374-1	2002	We have developed a time-resolved fluorescent assay using Wallac"s DELFIA system (DELFIA assay) to monitor changes in the phosphorylation level of insulin receptor from rat hepatoma (KRC-7) cells in response to ligand and the nonspecific, protein-tyrosine phosphatase inhibitor pervanadate.	pervanadate	278-289	insulin receptor	Rattus norvegicus	147-163
12841357-0	2003	High levels of palmitic acid lead to insulin resistance due to changes in the level of phosphorylation of the insulin receptor and insulin receptor substrate-1.	Palmitic Acid	15-28	insulin receptor	Rattus norvegicus	110-126
12841357-0	2003	High levels of palmitic acid lead to insulin resistance due to changes in the level of phosphorylation of the insulin receptor and insulin receptor substrate-1.	Palmitic Acid	15-28	insulin receptor	Rattus norvegicus	131-147
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
12841357-7	2003	According with this result, we found an increase in the phosphorylations in serine of the insulin receptor after the treatment with palmitate.	Serine	76-82	insulin receptor	Rattus norvegicus	90-106
12841357-7	2003	According with this result, we found an increase in the phosphorylations in serine of the insulin receptor after the treatment with palmitate.	Palmitates	132-141	insulin receptor	Rattus norvegicus	90-106
12882396-7	2003	The insulin receptor expression was not different due to dietary oil, but was markedly reduced with aging.	Dietary Fats, Unsaturated	57-68	insulin receptor	Rattus norvegicus	4-20
12423625-11	2002	Levels of the 2 IGF receptor mRNA and the insulin receptor mRNA were lower in Dex-treated cultures.	Dexamethasone	78-81	insulin receptor	Rattus norvegicus	42-58
12441184-2	2002	In this paper, we attempt to prove the influence of 17beta-estradiol on the insulin receptor of ovariectomized rats treated with different hormonal doses.	Estradiol	52-68	insulin receptor	Rattus norvegicus	76-92
12421375-2	2002	In a yeast two hybrid screen utilizing a proline-rich domain that is highly conserved among the ProSAP/Shank family members, we isolated several cDNA clones coding for the insulin receptor substrate IRSp53.	Proline	41-48	insulin receptor	Rattus norvegicus	172-188
12351437-6	2002	Blocking insulin secretion with diazoxide or insulin action with insulin receptor antibodies inhibited glucose-induced increases in IA-2 protein, but not those of mRNA.	Glucose	103-110	insulin receptor	Rattus norvegicus	65-81
12198647-1	2002	This report examines the effect of FK506 pretreatment on liver insulin receptor expression in partially (70%) hepatectomized rats.	Tacrolimus	35-40	insulin receptor	Rattus norvegicus	63-79
12213585-3	2002	We demonstrated that the regulation of glucagon receptor, insulin receptor and L-type pyruvate kinase (L-PK) gene expression in liver is dependent upon a cross-talk between oxygen and glucose.	Oxygen	173-179	insulin receptor	Rattus norvegicus	58-74
12213585-3	2002	We demonstrated that the regulation of glucagon receptor, insulin receptor and L-type pyruvate kinase (L-PK) gene expression in liver is dependent upon a cross-talk between oxygen and glucose.	Glucose	184-191	insulin receptor	Rattus norvegicus	58-74
12213585-5	2002	In primary rat hepatocyte cultures, the expression of the glucagon receptor and the L-PK mRNA was maximally induced by glucose under arterial pO2 whereas the insulin receptor was maximally induced under perivenous pO2.	PO-2	214-217	insulin receptor	Rattus norvegicus	158-174
12198647-2	2002	FK506 pretreatment led to an increased insulin receptor number 24 hours after hepatectomy, detected by means of insulin binding and cross-linking procedures.	Tacrolimus	0-5	insulin receptor	Rattus norvegicus	39-55
12198647-5	2002	The results show that FK506 pretreatment elicits an increase in the amount of insulin receptor alpha-subunits as measured by Western blot.	Tacrolimus	22-27	insulin receptor	Rattus norvegicus	78-94
12198647-7	2002	Moreover, in FK506-pretreated rat hepatocytes, obtained from remnant livers 24 hours after partial hepatectomy (PH), the increase in insulin receptor number was associated with improved sensitivity to the hormone.	Tacrolimus	13-18	insulin receptor	Rattus norvegicus	133-149
12198647-9	2002	In conclusion, our findings suggest that FK506 pretreatment induces insulin receptor expression in regenerating rat liver and promotes liver regeneration in hepatectomized rats.	Tacrolimus	41-46	insulin receptor	Rattus norvegicus	68-84
12203022-2	2002	In contrast to current chromium-containing nutrition supplements, which only serve as sources of absorbable chromium, the trinuclear cation has been shown in in vitro assays to interact with the insulin receptor, activating its kinase activity, presumably by trapping the receptor in its active conformation.	Chromium	23-31	insulin receptor	Rattus norvegicus	195-211
12203022-2	2002	In contrast to current chromium-containing nutrition supplements, which only serve as sources of absorbable chromium, the trinuclear cation has been shown in in vitro assays to interact with the insulin receptor, activating its kinase activity, presumably by trapping the receptor in its active conformation.	Chromium	108-116	insulin receptor	Rattus norvegicus	195-211
12079879-0	2002	Terguride treatment attenuated prolactin release and enhanced insulin receptor affinity and GLUT 4 content in obese spontaneously hypertensive female, but not male rats.	dironyl	0-9	insulin receptor	Rattus norvegicus	62-78
12467533-3	2002	The rat hepatocytic insulin receptor was partially purified by wheat-germ agglutinin (WGA)-sepharose 4B affinity chromatography.	Sepharose	91-103	insulin receptor	Rattus norvegicus	20-36
12117721-4	2002	METHODS AND RESULTS: Treatment of primary aortic smooth muscle cells from newborn rats with the NO donor S-nitroso-N-acetylpenicillamine reduced cell motility, tyrosine phosphorylation levels of insulin receptor beta subunit and insulin receptor substrate-1, and extracellular signal-regulated kinase activity.	S-Nitroso-N-Acetylpenicillamine	105-136	insulin receptor	Rattus norvegicus	195-211
12117721-4	2002	METHODS AND RESULTS: Treatment of primary aortic smooth muscle cells from newborn rats with the NO donor S-nitroso-N-acetylpenicillamine reduced cell motility, tyrosine phosphorylation levels of insulin receptor beta subunit and insulin receptor substrate-1, and extracellular signal-regulated kinase activity.	S-Nitroso-N-Acetylpenicillamine	105-136	insulin receptor	Rattus norvegicus	229-245
12127266-10	2002	alpha-Lipoic acid was recently shown to stimulate glucose uptake into 3T3-L1 adipocytes by increasing intracellular oxidant levels and/or facilitating insulin receptor autophosphorylation presumably by oxidation of critical thiol groups present in the insulin receptor beta-subunit.	Thioctic Acid	0-17	insulin receptor	Rattus norvegicus	151-167
12127266-10	2002	alpha-Lipoic acid was recently shown to stimulate glucose uptake into 3T3-L1 adipocytes by increasing intracellular oxidant levels and/or facilitating insulin receptor autophosphorylation presumably by oxidation of critical thiol groups present in the insulin receptor beta-subunit.	Thioctic Acid	0-17	insulin receptor	Rattus norvegicus	252-268
12127266-10	2002	alpha-Lipoic acid was recently shown to stimulate glucose uptake into 3T3-L1 adipocytes by increasing intracellular oxidant levels and/or facilitating insulin receptor autophosphorylation presumably by oxidation of critical thiol groups present in the insulin receptor beta-subunit.	Glucose	50-57	insulin receptor	Rattus norvegicus	252-268
12021765-2	2002	We generated an antisense oligodeoxynucleotide directed against the insulin receptor precursor protein and administered this directly into the third cerebral ventricle.	Oligodeoxyribonucleotides	26-46	insulin receptor	Rattus norvegicus	68-84
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
12021765-3	2002	Immunostaining of rat brains after 7-day administration of the oligodeoxynucleotide showed a selective decrease of insulin receptor protein within cells in the medial portion of the arcuate nucleus (decreased by approximately 80% as compared to rats treated with a control oligodeoxynucleotide).	Oligodeoxyribonucleotides	63-83	insulin receptor	Rattus norvegicus	115-131
12021765-3	2002	Immunostaining of rat brains after 7-day administration of the oligodeoxynucleotide showed a selective decrease of insulin receptor protein within cells in the medial portion of the arcuate nucleus (decreased by approximately 80% as compared to rats treated with a control oligodeoxynucleotide).	Oligodeoxyribonucleotides	273-293	insulin receptor	Rattus norvegicus	115-131
12021765-6	2002	During insulin-clamp studies, physiological hyperinsulinemia decreased glucose production by 55% in rats treated with control oligodeoxynucleotides but by only 25% in rats treated with insulin receptor antisense oligodeoxynucleotides.	Oligodeoxyribonucleotides	212-233	insulin receptor	Rattus norvegicus	185-201
11976270-2	2002	We evaluated the direct effect of lignocaine on insulin receptor (IR) kinase activity.	Lidocaine	34-44	insulin receptor	Rattus norvegicus	48-64
11976270-2	2002	We evaluated the direct effect of lignocaine on insulin receptor (IR) kinase activity.	Lidocaine	34-44	insulin receptor	Rattus norvegicus	66-68
11976270-7	2002	The in vitro study revealed that lignocaine directly inhibited both basal and insulin-stimulated tyrosine phosphorylation of IR.	Lidocaine	33-43	insulin receptor	Rattus norvegicus	125-127
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
11976270-9	2002	The inhibitory effect of lignocaine on tyrosine kinase activity of the IR underlies the suppression of insulin signalling with lignocaine.	Lidocaine	25-35	insulin receptor	Rattus norvegicus	71-73
11976270-9	2002	The inhibitory effect of lignocaine on tyrosine kinase activity of the IR underlies the suppression of insulin signalling with lignocaine.	Lidocaine	127-137	insulin receptor	Rattus norvegicus	71-73
11832371-0	2002	N-3 polyunsaturated fatty acids prevent the defect of insulin receptor signaling in muscle.	Fatty Acids, Omega-3	0-31	insulin receptor	Rattus norvegicus	54-70
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
11779865-8	2002	In vivo pepstatin A treatment was without any observable effect on the insulin receptor content of endosomes but augmented the phosphotyrosine content of the endosomal insulin receptor after insulin injection.	pepstatin	8-19	insulin receptor	Rattus norvegicus	168-184
11779865-8	2002	In vivo pepstatin A treatment was without any observable effect on the insulin receptor content of endosomes but augmented the phosphotyrosine content of the endosomal insulin receptor after insulin injection.	Phosphotyrosine	127-142	insulin receptor	Rattus norvegicus	168-184
11832371-8	2002	In conclusion, a high-fat diet enriched in n-3 fatty acids maintained IR, IRS-1 tyrosine phosphorylation, and PI 3"-kinase activity and total GLUT-44 content in muscle but not in liver.	Fatty Acids, Omega-3	43-58	insulin receptor	Rattus norvegicus	70-72
11991250-0	2002	Effect of treatment with different doses of 17-beta-estradiol on the insulin receptor.	Estradiol	44-61	insulin receptor	Rattus norvegicus	69-85
11991250-3	2002	In this paper, we attempted to determine the effect of 17-beta-estradiol on the insulin receptor of ovariectomized rats treated with different doses of hormones.	Estradiol	55-72	insulin receptor	Rattus norvegicus	80-96
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
11779153-4	2002	We report that the epidermal growth factor receptor (EGFR) kinase inhibitor PKI166 blocked both basal and ligand-induced tyrosine phosphorylation of the EGFR (IC(50) = 60 nM), but not of the insulin receptor or c-met.	PKI 166	76-82	insulin receptor	Rattus norvegicus	191-207
11936837-2	2002	Phosphotyrosine phosphatase 1B (PTP1B) dephosphorylates phosphotyrosine (pTyr) residues present on the insulin receptor (IR).	Phosphotyrosine	56-71	insulin receptor	Rattus norvegicus	103-119
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
11936837-2	2002	Phosphotyrosine phosphatase 1B (PTP1B) dephosphorylates phosphotyrosine (pTyr) residues present on the insulin receptor (IR).	Phosphotyrosine	56-71	insulin receptor	Rattus norvegicus	121-123
11936837-2	2002	Phosphotyrosine phosphatase 1B (PTP1B) dephosphorylates phosphotyrosine (pTyr) residues present on the insulin receptor (IR).	Phosphotyrosine	73-77	insulin receptor	Rattus norvegicus	103-119
11936837-2	2002	Phosphotyrosine phosphatase 1B (PTP1B) dephosphorylates phosphotyrosine (pTyr) residues present on the insulin receptor (IR).	Phosphotyrosine	73-77	insulin receptor	Rattus norvegicus	121-123
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
11574415-6	2001	Adding TLK16998 to L7 produced synergistic effects, further indicating that these two compounds act on the IR through separate mechanisms.	TLK 16998	7-15	insulin receptor	Rattus norvegicus	107-109
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
11514062-0	2001	Insulin receptor substrate protein p53 localization in rats suggests mechanism for specific polyglutamine neurodegeneration.	polyglutamine	92-105	insulin receptor	Rattus norvegicus	0-16
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
11473054-6	2001	High-fat feeding markedly decreased insulin receptor substrate (IRS)-1-associated phosphatidylinositol (PI) 3-kinase activity but not insulin-induced tyrosine phosphorylation of the insulin receptor and IRS proteins in muscle.	Phosphatidylinositols	82-102	insulin receptor	Rattus norvegicus	36-52
11162666-2	2001	When three copies of the nucleotides -618 to -593 of the IR promoter were transfected, the reporter activity was significantly increased in the presence of glucose and more increased in the presence of glucose/insulin.	Glucose	156-163	insulin receptor	Rattus norvegicus	57-59
11463579-4	2001	In order to study a putative direct effect of homocysteine on insulin signaling, we have characterized the molecular counter-regulation of the early events in the signal transduction of the insulin receptor, and the metabolic end-point of glycogen synthesis.	Homocysteine	46-58	insulin receptor	Rattus norvegicus	190-206
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.	Homocysteine	21-33	insulin receptor	Rattus norvegicus	149-165
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.	Thiolactone	34-45	insulin receptor	Rattus norvegicus	149-165
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
11463579-10	2001	Glutathione completely abolished the effects of homocysteine thiolactone on insulin-receptor signaling and restored the insulin-stimulated glycogen synthesis.	Glutathione	0-11	insulin receptor	Rattus norvegicus	76-92
11463579-10	2001	Glutathione completely abolished the effects of homocysteine thiolactone on insulin-receptor signaling and restored the insulin-stimulated glycogen synthesis.	Homocysteine	48-60	insulin receptor	Rattus norvegicus	76-92
11463579-10	2001	Glutathione completely abolished the effects of homocysteine thiolactone on insulin-receptor signaling and restored the insulin-stimulated glycogen synthesis.	Thiolactone	61-72	insulin receptor	Rattus norvegicus	76-92
11121405-0	2001	Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control.	Cholesterol	0-11	insulin receptor	Rattus norvegicus	44-60
11484076-0	2001	Insulin-independent and wortmannin-resistant targeting of IRS-3 to the plasma membrane via its pleckstrin homology domain mediates a different interaction with the insulin receptor from that of IRS-1.	Wortmannin	24-34	insulin receptor	Rattus norvegicus	164-180
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
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.	Wortmannin	0-10	insulin receptor	Rattus norvegicus	113-115
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.	Serine	94-97	insulin receptor	Rattus norvegicus	113-115
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.	Threonine	98-101	insulin receptor	Rattus norvegicus	113-115
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
11162666-5	2001	However, similarly to the leptin gene, the IR gene was more responsive to glucose stimulation than the FAS and ACL genes.	Glucose	74-81	insulin receptor	Rattus norvegicus	43-45
11428713-4	2001	The changes in insulin receptor number could be responsible for the improved glucose tolerance observed during morphine addiction.	Glucose	77-84	insulin receptor	Rattus norvegicus	15-31
11428713-4	2001	The changes in insulin receptor number could be responsible for the improved glucose tolerance observed during morphine addiction.	Morphine	111-119	insulin receptor	Rattus norvegicus	15-31
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
11160042-2	2001	Activation of the insulin receptor initiates signaling through both the phosphatidylinositol (PI) 3-kinase and the mitogen-activated protein kinase [MAPK, also referred to as extracellular signal-regulated kinases (ERK1/2)] pathways.	Phosphatidylinositols	72-92	insulin receptor	Rattus norvegicus	18-34
11229432-4	2001	Insulin-stimulated tyrosine phosphorylation of insulin receptor was reduced to 36% (P &lt; .005), as was the phosphorylation of IRS-1 to 34% (P &lt; .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
11101307-5	2000	Insulin gene transcription was stimulated by insulin receptor signaling and insulin mimetic compound (L-783 281) in a glucose- and Grb2-dependent manner.	Glucose	118-125	insulin receptor	Rattus norvegicus	45-61
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
11105093-5	2000	In the present study, we determined the levels and phosphorylation status of the insulin receptor and pp185 (IRS-(1/2)) in liver and muscle of rats submitted to a high-fructose diet evaluated by immunoblotting with specific antibodies.	Fructose	168-176	insulin receptor	Rattus norvegicus	81-97
11262604-7	2000	In rats with streptozotocin-induced diabetes mellitus there was a significant reduction in insulin-induced insulin receptor and STAT-1 phosphorylation in the lacrimal gland but not in the salivary gland; there was no influence on Shc phosphorylation in either tissue.	Streptozocin	13-27	insulin receptor	Rattus norvegicus	107-123
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
10893327-8	2000	The GLP-1 receptor agonist exendin-4 showed similar effects, whereas the receptor antagonist exendin-(9---39) amide inhibited the GLP-1-induced increase in insulin receptor binding.	Amides	110-115	insulin receptor	Rattus norvegicus	156-172
11033073-6	2000	The results showed that streptozotocin-induced diabetic rats showed insulin-resistance through alterations in the kinetics of insulin receptor binding.	Streptozocin	24-38	insulin receptor	Rattus norvegicus	126-142
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
10848643-4	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
10844119-2	2000	We have recently described the cross-talk of pancreastatin with insulin signaling in rat hepatoma cells (HTC), where it inhibits insulin action and signaling through the serine phosphorylation of the insulin receptor, thereby impairing tyrosine kinase activity.	Serine	170-176	insulin receptor	Rattus norvegicus	200-216
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
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.	Chromium	71-73	insulin receptor	Rattus norvegicus	49-51
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.	Aluminum	78-80	insulin receptor	Rattus norvegicus	49-51
10816439-0	2000	Perivenous localization of insulin receptor protein in rat liver, and regulation of its expression by glucose and oxygen in hepatocyte cultures.	Glucose	102-109	insulin receptor	Rattus norvegicus	27-43
10816439-0	2000	Perivenous localization of insulin receptor protein in rat liver, and regulation of its expression by glucose and oxygen in hepatocyte cultures.	Oxygen	114-120	insulin receptor	Rattus norvegicus	27-43
10816439-3	2000	In hepatocyte cultures venous O(2) partial pressure (pO(2)) induced insulin receptor protein expression.	Oxygen	30-34	insulin receptor	Rattus norvegicus	68-84
10816439-4	2000	High glucose concentrations enhanced insulin receptor protein under arterial and venous pO(2).	Glucose	5-12	insulin receptor	Rattus norvegicus	37-53
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
10827205-3	2000	However, tyrosine-phosphorylation of the insulin receptor after insulin stimulation was reduced to 71 +/- 2% (P &lt; 0.05) of control in the liver of the fructose-fed rats.	Tyrosine	9-17	insulin receptor	Rattus norvegicus	41-57
10827205-3	2000	However, tyrosine-phosphorylation of the insulin receptor after insulin stimulation was reduced to 71 +/- 2% (P &lt; 0.05) of control in the liver of the fructose-fed rats.	Fructose	154-162	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
10885459-6	2000	Subsequent studies revealed that the action of vanadium salts is mediated through insulin-receptor independent alternative pathway(s).	vanadium salts	47-61	insulin receptor	Rattus norvegicus	82-98
10801916-3	2000	Insulin receptor mRNA concentrations in the liver and adipose tissue began to decrease 30 min after the refeeding, in contrast to the plasma insulin increase, and continued to decrease until 8 h. The expression of acetyl-CoA carboxylase and fatty acid synthase mRNA began to increase 4-8 h after feeding and reached maximal levels at 16-24 h. Leptin treatment suppressed the expression of lipogenic enzyme mRNA in rats fed the fat-free diet but not in corn oil-fed rats, in which the expression was suppressed by polyunsaturated fatty acids and leptin expression was higher.	Fatty Acids, Unsaturated	513-540	insulin receptor	Rattus norvegicus	0-16
10334307-6	1999	After 1 min of insulin stimulation, phosphorylation of IRS-1 and insulin receptor increased 6- to 8-fold in saline-infused rats and 7- to 10-fold in glucosamine-infused rats.	Sodium Chloride	108-114	insulin receptor	Rattus norvegicus	65-81
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
10385415-0	1999	Effect of diazoxide on brain capillary insulin receptor binding and food intake in hyperphagic obese Zucker rats.	Diazoxide	10-19	insulin receptor	Rattus norvegicus	39-55
10334863-7	1999	In conclusion, the finding that vanadate and bpV compounds are potent inhibitors of G-6-Pase suggests that the blood-glucose-lowering effect of these compounds which is seen in diabetic animals may be partly explained by a direct effect on this enzyme rather than, as presently thought, being the result of inhibition of phosphoprotein tyrosine phosphatases and thereby insulin receptor dephosphorylation.	Vanadates	32-40	insulin receptor	Rattus norvegicus	370-386
10334863-7	1999	In conclusion, the finding that vanadate and bpV compounds are potent inhibitors of G-6-Pase suggests that the blood-glucose-lowering effect of these compounds which is seen in diabetic animals may be partly explained by a direct effect on this enzyme rather than, as presently thought, being the result of inhibition of phosphoprotein tyrosine phosphatases and thereby insulin receptor dephosphorylation.	bromopyruvate	45-48	insulin receptor	Rattus norvegicus	370-386
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
10391142-1	1999	Serine/threonine phosphorylation of insulin receptor has been implicated in the development of insulin resistance.	Serine	0-6	insulin receptor	Rattus norvegicus	36-52
10391142-1	1999	Serine/threonine phosphorylation of insulin receptor has been implicated in the development of insulin resistance.	Threonine	7-16	insulin receptor	Rattus norvegicus	36-52
10391142-2	1999	To investigate whether dephosphorylation of serine/threonine residues of the insulin receptor may restore the decreased insulin-stimulated receptor tyrosine kinase activity in skeletal muscle of obese Zucker rats, insulin receptor tyrosine kinase activity was measured before and after alkaline phosphatase treatment.	Serine	44-50	insulin receptor	Rattus norvegicus	77-93
10391142-2	1999	To investigate whether dephosphorylation of serine/threonine residues of the insulin receptor may restore the decreased insulin-stimulated receptor tyrosine kinase activity in skeletal muscle of obese Zucker rats, insulin receptor tyrosine kinase activity was measured before and after alkaline phosphatase treatment.	Threonine	51-60	insulin receptor	Rattus norvegicus	77-93
10391142-5	1999	In vivo insulin-induced tyrosine phosphorylation of insulin receptor and insulin receptor substrate-1 was depressed by 82% (p &lt; 0.05) and 86% (p &lt; 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 &lt; 0.05) and 86% (p &lt; 0.05), respectively.	Tyrosine	24-32	insulin receptor	Rattus norvegicus	73-89
10391142-8	1999	These findings suggest that excessive serine/threonine phosphorylation of the insulin receptor in obese Zucker rats may be a cause for insulin resistance in skeletal muscle.	Serine	38-44	insulin receptor	Rattus norvegicus	78-94
10391142-8	1999	These findings suggest that excessive serine/threonine phosphorylation of the insulin receptor in obese Zucker rats may be a cause for insulin resistance in skeletal muscle.	Threonine	45-54	insulin receptor	Rattus norvegicus	78-94
10096784-12	1999	Furthermore, pancreastatin produced Ser/Thr phosphorylation of insulin receptor by a staurosporine-sensitive mechanism.	Serine	36-39	insulin receptor	Rattus norvegicus	63-79
10096784-12	1999	Furthermore, pancreastatin produced Ser/Thr phosphorylation of insulin receptor by a staurosporine-sensitive mechanism.	Threonine	40-43	insulin receptor	Rattus norvegicus	63-79
10096784-12	1999	Furthermore, pancreastatin produced Ser/Thr phosphorylation of insulin receptor by a staurosporine-sensitive mechanism.	Staurosporine	85-98	insulin receptor	Rattus norvegicus	63-79
10623881-2	2000	The PI3K inhibitor LY294002 completely blocks insulin-stimulated glycogen synthesis by inhibiting glycogen synthase, PKB (Akt-1), and FRAP (RAFT) autophosphorylation, as well as p70 S6 kinase activation, whereas insulin receptor substrates tyrosine phosphorylation and MEK activity were not affected.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	19-27	insulin receptor	Rattus norvegicus	212-228
10581198-2	1999	During the hypoinsulinemic and hyperglycemic phase in the Zucker diabetic fatty (ZDF) rat liver, insulin-induced phosphorylations of the insulin receptor (IR) and insulin receptor substrate (IRS)-1/2 were significantly enhanced.	zdf	81-84	insulin receptor	Rattus norvegicus	137-158
10581198-5	1999	The restoration of normoglycemia by sodium-dependent glucose transporter (SGLT) inhibitor to ZDF rats normalized elevated PI 3-kinase activation and phosphorylation of IR and IRS-1/2 to lean control rat levels.	zdf	93-96	insulin receptor	Rattus norvegicus	168-170
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
10631616-2	1999	Given that the complexes are proposed to function by interacting with insulin receptor, trapping it in its active conformation, in contrast to current chromium-containing nutrition supplements, which only serve as sources of absorbable chromium, changes in lipid and carbohydrate metabolism would be expected.	Chromium	151-159	insulin receptor	Rattus norvegicus	70-86
10631616-2	1999	Given that the complexes are proposed to function by interacting with insulin receptor, trapping it in its active conformation, in contrast to current chromium-containing nutrition supplements, which only serve as sources of absorbable chromium, changes in lipid and carbohydrate metabolism would be expected.	Carbohydrates	267-279	insulin receptor	Rattus norvegicus	70-86
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
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
10334307-6	1999	After 1 min of insulin stimulation, phosphorylation of IRS-1 and insulin receptor increased 6- to 8-fold in saline-infused rats and 7- to 10-fold in glucosamine-infused rats.	Glucosamine	149-160	insulin receptor	Rattus norvegicus	65-81
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	phosphatidylinositol 3,4,5-triphosphate	66-107	insulin receptor	Rattus norvegicus	17-19
10676486-5	1999	The concentrations of Cr in the subcellular fractions of pancreas, testes, and kidney in the normal rats are higher than those in the diabetic rats, which favor the hypothesis that Cr(III) plays its biological function via interaction with the insulin-sensitive tissues or enhancement of the sensitivity of the insulin receptor.	Chromium	22-24	insulin receptor	Rattus norvegicus	311-327
10676486-5	1999	The concentrations of Cr in the subcellular fractions of pancreas, testes, and kidney in the normal rats are higher than those in the diabetic rats, which favor the hypothesis that Cr(III) plays its biological function via interaction with the insulin-sensitive tissues or enhancement of the sensitivity of the insulin receptor.	tris(1,10-phenanthroline)chromium(III) chloride	181-188	insulin receptor	Rattus norvegicus	311-327
10037256-0	1999	Treatment of streptozotocin-induced diabetic rats with vanadate and phlorizin prevents the over-expression of the liver insulin receptor gene.	Streptozocin	13-27	insulin receptor	Rattus norvegicus	120-136
10037256-0	1999	Treatment of streptozotocin-induced diabetic rats with vanadate and phlorizin prevents the over-expression of the liver insulin receptor gene.	Vanadates	55-63	insulin receptor	Rattus norvegicus	120-136
10037256-0	1999	Treatment of streptozotocin-induced diabetic rats with vanadate and phlorizin prevents the over-expression of the liver insulin receptor gene.	Phlorhizin	68-77	insulin receptor	Rattus norvegicus	120-136
10037256-2	1999	In the present study, the effects of vanadate on various steps of expression of the liver insulin receptor gene in diabetic rats have been analyzed and compared with those of phlorizin, a glucopenic drug devoid of insulinomimetic properties.	Vanadates	37-45	insulin receptor	Rattus norvegicus	90-106
10037256-3	1999	Livers of rats killed 23 days after streptozotocin injection showed a 30-40% increase in the number of cell surface and intracellular insulin receptors, a 50-90% increase in the levels of 9.5 and 7.5 kb insulin receptor mRNA species, and a 20% decrease in the relative abundance of the A (exon 11-) insulin receptor mRNA isotype.	Streptozocin	36-50	insulin receptor	Rattus norvegicus	134-150
10037256-3	1999	Livers of rats killed 23 days after streptozotocin injection showed a 30-40% increase in the number of cell surface and intracellular insulin receptors, a 50-90% increase in the levels of 9.5 and 7.5 kb insulin receptor mRNA species, and a 20% decrease in the relative abundance of the A (exon 11-) insulin receptor mRNA isotype.	Streptozocin	36-50	insulin receptor	Rattus norvegicus	203-219
10037256-4	1999	Daily administration of vanadate or phlorizin from day 5 to day 23 prevented the increase in insulin receptor number and mRNA level, and vanadate treatment also normalized receptor mRNA isotype expression.	Vanadates	24-32	insulin receptor	Rattus norvegicus	93-109
10037256-4	1999	Daily administration of vanadate or phlorizin from day 5 to day 23 prevented the increase in insulin receptor number and mRNA level, and vanadate treatment also normalized receptor mRNA isotype expression.	Phlorhizin	36-45	insulin receptor	Rattus norvegicus	93-109
10037256-5	1999	Unlike observations in vivo, vanadate and phlorizin differentially affected the expression of the insulin receptor gene in Fao hepatoma cells.	Vanadates	29-37	insulin receptor	Rattus norvegicus	98-114
10037256-5	1999	Unlike observations in vivo, vanadate and phlorizin differentially affected the expression of the insulin receptor gene in Fao hepatoma cells.	Phlorhizin	42-51	insulin receptor	Rattus norvegicus	98-114
10037256-6	1999	Vanadate treatment (0.5 mmol/l for 4 h) decreased the levels of the 9.5 and 7.5 kb insulin receptor transcripts by at least twofold, without affecting the relative abundance of the A insulin receptor mRNA isotype.	Vanadates	0-8	insulin receptor	Rattus norvegicus	83-99
10037256-6	1999	Vanadate treatment (0.5 mmol/l for 4 h) decreased the levels of the 9.5 and 7.5 kb insulin receptor transcripts by at least twofold, without affecting the relative abundance of the A insulin receptor mRNA isotype.	Vanadates	0-8	insulin receptor	Rattus norvegicus	183-199
10037256-7	1999	In contrast, phlorizin treatment (5 mmol/l for 4 h) slightly increased or did not affect the levels of the 9.5 and 7.5 kb insulin receptor transcripts respectively, and increased by twofold the relative expression of the A insulin receptor mRNA isotype.	Phlorhizin	13-22	insulin receptor	Rattus norvegicus	223-239
10037256-8	1999	It is suggested that, although mediated in part by a reversal of hyperglycemia, normalization of liver insulin receptor gene expression by vanadate treatment in diabetic rats may also involve a direct inhibitory effect of this drug on gene expression.	Vanadates	139-147	insulin receptor	Rattus norvegicus	103-119
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
9829797-2	1998	The compound streptozotocin (STZ) is known to inhibit insulin receptor function.	Streptozocin	13-27	insulin receptor	Rattus norvegicus	54-70
9829797-2	1998	The compound streptozotocin (STZ) is known to inhibit insulin receptor function.	Streptozocin	29-32	insulin receptor	Rattus norvegicus	54-70
9829797-3	1998	The study was designed to investigate whether intracerebroventricularly (icv) applied STZ would inhibit neuronal insulin receptor function and would induce changes in both behavior and neuronal energy metabolism.	Streptozocin	86-89	insulin receptor	Rattus norvegicus	113-129
9738001-6	1998	The further expression of IRS-1 in 3Y1-GLUT4myc-IR cells led to stimulation of glycogen synthesis but not to glucose uptake or GLUT4myc translocation in response to insulin, although NaF or phorbol 12-myristate 13-acetate did trigger GLUT4myc translocation in the cells.	Tetradecanoylphorbol Acetate	190-221	insulin receptor	Rattus norvegicus	26-28
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
10320054-12	1999	It appears that AII achieves this effect by stimulating serine phosphorylation of the insulin receptor beta-subunit IRS-1, and the p85 regulatory subunit of PI3-kinase.	Serine	56-62	insulin receptor	Rattus norvegicus	86-102
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
9801794-4	1998	Following treatment with captopril there was an improvement in insulin-induced insulin receptor and pp185 phosphorylation in the liver and muscle of obese rats.	Captopril	25-34	insulin receptor	Rattus norvegicus	79-95
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	phosphatidylinositol 3,4,5-triphosphate	66-107	insulin receptor	Rattus norvegicus	50-52
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	4,5-p3	114-120	insulin receptor	Rattus norvegicus	17-19
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	4,5-p3	114-120	insulin receptor	Rattus norvegicus	50-52
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	Glycogen	219-227	insulin receptor	Rattus norvegicus	17-19
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	Glycogen	219-227	insulin receptor	Rattus norvegicus	50-52
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	Glucose	239-246	insulin receptor	Rattus norvegicus	17-19
9738001-5	1998	The 3Y1-GLUT4myc-IR cells expressing GLUT4myc and IR responded to phosphatidylinositol 3,4, 5-trisphosphate (PI-3,4,5-P3) accumulation, Akt activation, the stimulation of DNA synthesis, and membrane ruffling but not to glycogen synthesis, glucose uptake, or GLUT4myc translocation.	Glucose	239-246	insulin receptor	Rattus norvegicus	50-52
9738001-6	1998	The further expression of IRS-1 in 3Y1-GLUT4myc-IR cells led to stimulation of glycogen synthesis but not to glucose uptake or GLUT4myc translocation in response to insulin, although NaF or phorbol 12-myristate 13-acetate did trigger GLUT4myc translocation in the cells.	Glycogen	79-87	insulin receptor	Rattus norvegicus	26-28
9738001-6	1998	The further expression of IRS-1 in 3Y1-GLUT4myc-IR cells led to stimulation of glycogen synthesis but not to glucose uptake or GLUT4myc translocation in response to insulin, although NaF or phorbol 12-myristate 13-acetate did trigger GLUT4myc translocation in the cells.	Sodium Fluoride	183-186	insulin receptor	Rattus norvegicus	26-28
9785467-3	1998	Insulin-like growth factor I (IGF-I) is an important regulator of glucose metabolism in skeletal muscle and acts through its own receptor, which has many structural and functional similarities with the insulin receptor.	Glucose	66-73	insulin receptor	Rattus norvegicus	202-218
9746224-1	1998	Insulin receptor (IR) gene expression at the mRNA level was investigated in hindlimb skeletal muscle, epididymal adipose tissue and in the liver of rats exposed to prolonged in vivo administration of deoxycorticosterone acetate (DOCA).	Desoxycorticosterone Acetate	200-227	insulin receptor	Rattus norvegicus	0-16
9746224-1	1998	Insulin receptor (IR) gene expression at the mRNA level was investigated in hindlimb skeletal muscle, epididymal adipose tissue and in the liver of rats exposed to prolonged in vivo administration of deoxycorticosterone acetate (DOCA).	Desoxycorticosterone Acetate	229-233	insulin receptor	Rattus norvegicus	0-16
9559669-0	1998	Vanadate fully stimulates insulin receptor substrate-1 associated phosphatidyl inositol 3-kinase activity in adipocytes from young and old rats.	Vanadates	0-8	insulin receptor	Rattus norvegicus	26-42
9601071-1	1998	Receptor-mediated endocytosis and subsequent endosomal proteolysis of [125I]TyrA14-[HisA8,HisB4,GluB10,HisB27]in sulin ([125I]TyrA14-H2 analogue), an insulin analogue exhibiting a high affinity for the insulin receptor, has been studied in liver parenchymal cells by quantitative subcellular fractionation and compared with that of wild-type [125I]TyrA14-insulin.	tyra14	76-82	insulin receptor	Rattus norvegicus	202-218
9601071-1	1998	Receptor-mediated endocytosis and subsequent endosomal proteolysis of [125I]TyrA14-[HisA8,HisB4,GluB10,HisB27]in sulin ([125I]TyrA14-H2 analogue), an insulin analogue exhibiting a high affinity for the insulin receptor, has been studied in liver parenchymal cells by quantitative subcellular fractionation and compared with that of wild-type [125I]TyrA14-insulin.	Sulindac	113-118	insulin receptor	Rattus norvegicus	202-218
9601071-1	1998	Receptor-mediated endocytosis and subsequent endosomal proteolysis of [125I]TyrA14-[HisA8,HisB4,GluB10,HisB27]in sulin ([125I]TyrA14-H2 analogue), an insulin analogue exhibiting a high affinity for the insulin receptor, has been studied in liver parenchymal cells by quantitative subcellular fractionation and compared with that of wild-type [125I]TyrA14-insulin.	tyra14	126-132	insulin receptor	Rattus norvegicus	202-218
9601071-1	1998	Receptor-mediated endocytosis and subsequent endosomal proteolysis of [125I]TyrA14-[HisA8,HisB4,GluB10,HisB27]in sulin ([125I]TyrA14-H2 analogue), an insulin analogue exhibiting a high affinity for the insulin receptor, has been studied in liver parenchymal cells by quantitative subcellular fractionation and compared with that of wild-type [125I]TyrA14-insulin.	tyra14	126-132	insulin receptor	Rattus norvegicus	202-218
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
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
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
9559669-1	1998	Vanadate stimulates adipocyte 2-deoxyglucose transport and GLUT-4 translocation to the membrane through an insulin receptor-independent but wortmannin-inhibitable pathway.	Vanadates	0-8	insulin receptor	Rattus norvegicus	107-123
9493493-5	1998	Multiple lines of evidence suggest that isoform-selective activation of PKC phosphorylates and down-regulates one or more substrates involved in glucose transport and metabolism (e.g. glycogen synthase and the insulin receptor) and recent studies have shown increased expression of calcium-independent isozymes (PKC-epsilon and PKC-theta) in the membrane fraction of skeletal muscle in fructose- and fat-fed rat models of insulin resistance.	Glucose	145-152	insulin receptor	Rattus norvegicus	210-226
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
9493493-5	1998	Multiple lines of evidence suggest that isoform-selective activation of PKC phosphorylates and down-regulates one or more substrates involved in glucose transport and metabolism (e.g. glycogen synthase and the insulin receptor) and recent studies have shown increased expression of calcium-independent isozymes (PKC-epsilon and PKC-theta) in the membrane fraction of skeletal muscle in fructose- and fat-fed rat models of insulin resistance.	Calcium	282-289	insulin receptor	Rattus norvegicus	210-226
9493493-5	1998	Multiple lines of evidence suggest that isoform-selective activation of PKC phosphorylates and down-regulates one or more substrates involved in glucose transport and metabolism (e.g. glycogen synthase and the insulin receptor) and recent studies have shown increased expression of calcium-independent isozymes (PKC-epsilon and PKC-theta) in the membrane fraction of skeletal muscle in fructose- and fat-fed rat models of insulin resistance.	Fructose	386-394	insulin receptor	Rattus norvegicus	210-226
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.	Serine	9-15	insulin receptor	Rattus norvegicus	119-135
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
9368067-3	1997	To unravel the molecular basis for this uncoupling in insulin signaling, we undertook to study the interaction of Ser/Thr-phosphorylated IRS-1 and IRS-2 with the insulin receptor.	Serine	114-117	insulin receptor	Rattus norvegicus	162-178
9368067-3	1997	To unravel the molecular basis for this uncoupling in insulin signaling, we undertook to study the interaction of Ser/Thr-phosphorylated IRS-1 and IRS-2 with the insulin receptor.	Threonine	118-121	insulin receptor	Rattus norvegicus	162-178
9468304-2	1998	The present study demonstrates that a decrease in the level of muscle insulin receptor phosphorylation induced by chronic growth hormone (GH) treatment or acute epinephrine infusion is accompanied by a reduction in the level of IRS-1 phosphorylation and in the association with phosphatidylinositol 3-kinase.	Epinephrine	161-172	insulin receptor	Rattus norvegicus	70-86
9585135-5	1998	In rat adipocytes, which represent the physiological target cells of insulin, receptor-mediated activation of GTP-binding protein by adenosine and prostaglandin E2 potentiated the insulin-induced PtdIns(3,4,5)P3 accumulation.	Guanosine Triphosphate	110-113	insulin receptor	Rattus norvegicus	69-86
9585135-5	1998	In rat adipocytes, which represent the physiological target cells of insulin, receptor-mediated activation of GTP-binding protein by adenosine and prostaglandin E2 potentiated the insulin-induced PtdIns(3,4,5)P3 accumulation.	Adenosine	133-142	insulin receptor	Rattus norvegicus	69-86
9585135-5	1998	In rat adipocytes, which represent the physiological target cells of insulin, receptor-mediated activation of GTP-binding protein by adenosine and prostaglandin E2 potentiated the insulin-induced PtdIns(3,4,5)P3 accumulation.	Dinoprostone	147-163	insulin receptor	Rattus norvegicus	69-86
9585135-5	1998	In rat adipocytes, which represent the physiological target cells of insulin, receptor-mediated activation of GTP-binding protein by adenosine and prostaglandin E2 potentiated the insulin-induced PtdIns(3,4,5)P3 accumulation.	phosphatidylinositol 3,4,5-triphosphate	196-211	insulin receptor	Rattus norvegicus	69-86
9439552-12	1997	In conclusion, gliclazide has a glucose-lowering effect in STZ-diabetic rats that could be attributed to an increase in muscle glucose clearance by a post-insulin receptor mechanism, probably related to a normalization of GLUT4 content.	Gliclazide	15-25	insulin receptor	Rattus norvegicus	155-171
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.	Threonine	16-25	insulin receptor	Rattus norvegicus	119-135
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
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Serine	116-119	insulin receptor	Rattus norvegicus	147-163
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Serine	116-119	insulin receptor	Rattus norvegicus	165-167
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Serine	116-119	insulin receptor	Rattus norvegicus	186-202
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Threonine	120-123	insulin receptor	Rattus norvegicus	147-163
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Threonine	120-123	insulin receptor	Rattus norvegicus	165-167
9368067-2	1997	Tumor necrosis factor alpha (TNFalpha) or chronic hyperinsulinemia that induce insulin resistance trigger increased Ser/Thr phosphorylation of the insulin receptor (IR) and of its major insulin receptor substrates, IRS-1 and IRS-2.	Threonine	120-123	insulin receptor	Rattus norvegicus	186-202
9348211-0	1997	Vanadate, but not insulin, inhibits insulin receptor gene expression in rat hepatoma cells.	Vanadates	0-8	insulin receptor	Rattus norvegicus	36-52
9397240-9	1997	Thus, increased plasma insulin response to oral glucose load is associated with normal insulin receptor binding and gene expression in peripheral tissues in rats with Dahl hypertension.	Glucose	48-55	insulin receptor	Rattus norvegicus	87-103
9348211-1	1997	Insulin and vanadate treatments have recently been shown to reverse the overexpression of the hepatic insulin receptor (IR) gene in streptozotocin-induced diabetic rats.	Vanadates	12-20	insulin receptor	Rattus norvegicus	102-118
9348211-1	1997	Insulin and vanadate treatments have recently been shown to reverse the overexpression of the hepatic insulin receptor (IR) gene in streptozotocin-induced diabetic rats.	Vanadates	12-20	insulin receptor	Rattus norvegicus	120-122
9348211-1	1997	Insulin and vanadate treatments have recently been shown to reverse the overexpression of the hepatic insulin receptor (IR) gene in streptozotocin-induced diabetic rats.	Streptozocin	132-146	insulin receptor	Rattus norvegicus	102-118
9348211-1	1997	Insulin and vanadate treatments have recently been shown to reverse the overexpression of the hepatic insulin receptor (IR) gene in streptozotocin-induced diabetic rats.	Streptozocin	132-146	insulin receptor	Rattus norvegicus	120-122
9356012-11	1997	Troglitazone restores insulin action possibly by lowering the FFA concentration of the blood and/or by stimulating glucose uptake at an intracellular point distal to insulin receptor autophosphorylation in muscle.	Troglitazone	0-12	insulin receptor	Rattus norvegicus	166-182
9348211-2	1997	To better understand the mechanisms underlying these effects, the abilities of insulin and vanadate to affect IR gene expression have been comparatively examined in Fao hepatoma cells, an insulin-responsive cell line.	Vanadates	91-99	insulin receptor	Rattus norvegicus	110-112
9348211-3	1997	Exposure of Fao cells to insulin (1 microM) or vanadate (500 microM) for 24 h led to a 2-fold decrease in IR number in total cellular membranes.	Vanadates	47-55	insulin receptor	Rattus norvegicus	106-108
9348211-5	1997	In contrast, vanadate treatment caused a time- and dose-dependent decrease in IR mRNA level, which was maximal (4-fold change) after a 24-h exposure to 500 microM vanadate and was fully reversible.	Vanadates	13-21	insulin receptor	Rattus norvegicus	78-80
9348211-5	1997	In contrast, vanadate treatment caused a time- and dose-dependent decrease in IR mRNA level, which was maximal (4-fold change) after a 24-h exposure to 500 microM vanadate and was fully reversible.	Vanadates	163-171	insulin receptor	Rattus norvegicus	78-80
9348211-7	1997	Vanadate treatment did not modify mRNA half-life (3.5 h) in 5, 6 dichlorobenzimidazole riboside-treated cells but decreased by 4-fold the transcriptional activity of the IR gene.	Vanadates	0-8	insulin receptor	Rattus norvegicus	170-172
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
9348211-8	1997	These data show for the first time that, although both insulin and vanadate decrease total cellular IR number in Fao cells, only vanadate decreases IR mRNA level.	Vanadates	67-75	insulin receptor	Rattus norvegicus	100-102
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
9348211-8	1997	These data show for the first time that, although both insulin and vanadate decrease total cellular IR number in Fao cells, only vanadate decreases IR mRNA level.	Vanadates	129-137	insulin receptor	Rattus norvegicus	148-150
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
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
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
9284059-0	1997	Systemic administration of kainic acid induces selective time dependent decrease in [125I]insulin-like growth factor I, [125I]insulin-like growth factor II and [125I]insulin receptor binding sites in adult rat hippocampal formation.	Kainic Acid	27-38	insulin receptor	Rattus norvegicus	166-182
9284059-10	1997	A kainate-induced decrease in [125I]insulin receptor binding was noted at all time points in the molecular layer of the dentate gyrus whereas binding in CA1-CA3 subfields and discrete layers of the Ammon"s horn was found to be affected only after 12 h of treatment.	Kainic Acid	2-9	insulin receptor	Rattus norvegicus	36-52
9244377-1	1997	Chromatography of extracts from rat liver membranes on wheat-germ lectin-Sepharose resulted in a partial resolution of the insulin receptor from other phosphorylatable proteins.	Sepharose	73-82	insulin receptor	Rattus norvegicus	123-139
9247738-8	1997	In the spontaneously HT rat there is evidence for reduced down-regulation of INSR expression in response to NaCl-loading, consistent with a promoter effect.	Sodium Chloride	108-112	insulin receptor	Rattus norvegicus	77-81
9341114-0	1997	Chloroquine extends the lifetime of the activated insulin receptor complex in endosomes.	Chloroquine	0-11	insulin receptor	Rattus norvegicus	50-66
9341114-6	1997	Chloroquine treatment also increased the insulin receptor content of endosomes after insulin injection (integrated over 0-45 min) by 31% when compared with controls (p &lt; 0.05).	Chloroquine	0-11	insulin receptor	Rattus norvegicus	41-57
9341114-7	1997	Similarly, chloroquine increased both insulin receptor phosphotyrosine content and its exogenous tyrosine kinase activity after insulin injection (64%; p &lt; 0.01 and 96% and p &lt; 0.	Chloroquine	11-22	insulin receptor	Rattus norvegicus	38-54
9341114-7	1997	Similarly, chloroquine increased both insulin receptor phosphotyrosine content and its exogenous tyrosine kinase activity after insulin injection (64%; p &lt; 0.01 and 96% and p &lt; 0.	Phosphotyrosine	55-70	insulin receptor	Rattus norvegicus	38-54
9341114-11	1997	These observations are consistent with the hypothesis that chloroquine-dependent inhibition of endosomal insulin receptor dissociation and subsequent degradation prolongs the half-life of the active endosomal receptor and potentiates insulin signaling from this compartment.	Chloroquine	59-70	insulin receptor	Rattus norvegicus	105-121
9246941-8	1997	The inhibition of insulin-stimulated 2-deoxyglucose uptake by monensin was associated with a 31% decrease in the abundance of insulin receptors in muscles, a 64% decrease in the insulin-induced autophosphorylation of the insulin receptor beta-subunit, and a 44% reduction of the insulin-stimulated phosphatidylinositol 3-kinase activity.	Deoxyglucose	37-51	insulin receptor	Rattus norvegicus	126-142
9246941-8	1997	The inhibition of insulin-stimulated 2-deoxyglucose uptake by monensin was associated with a 31% decrease in the abundance of insulin receptors in muscles, a 64% decrease in the insulin-induced autophosphorylation of the insulin receptor beta-subunit, and a 44% reduction of the insulin-stimulated phosphatidylinositol 3-kinase activity.	Monensin	62-70	insulin receptor	Rattus norvegicus	126-142
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
9187620-0	1997	Dietary soybean protein increases insulin receptor gene expression in Wistar fatty rats when dietary polyunsaturated fatty acid level is low.	Fatty Acids, Unsaturated	101-127	insulin receptor	Rattus norvegicus	34-50
9109644-4	1997	The ability of LMWCr to stimulate insulin receptor tyrosine kinase activity is dependent on its chromium content.	Chromium	96-104	insulin receptor	Rattus norvegicus	34-50
9142881-8	1997	Although a decreased level of the variant with exon 11 correlated with insulin resistance of whole body glucose uptake, our results indicated that changes in the expression of the insulin receptor variants were secondary events and thus not the cause of the insulin resistance in old and mildly insulin-deficient rats.	Glucose	104-111	insulin receptor	Rattus norvegicus	180-196
9089644-0	1997	Tissue-specific modulation of insulin receptor mRNA levels in adrenaline-treated rats.	Epinephrine	62-72	insulin receptor	Rattus norvegicus	30-46
9089644-1	1997	Insulin receptor (IR) gene expression at the mRNA level was investigated in liver, hindlimb skeletal muscle, and epididymal adipose tissue of rats exposed to prolonged in vivo administration of adrenaline in relation to control rats.	Epinephrine	194-204	insulin receptor	Rattus norvegicus	0-16
9089644-1	1997	Insulin receptor (IR) gene expression at the mRNA level was investigated in liver, hindlimb skeletal muscle, and epididymal adipose tissue of rats exposed to prolonged in vivo administration of adrenaline in relation to control rats.	Epinephrine	194-204	insulin receptor	Rattus norvegicus	18-20
9089644-7	1997	These results provide evidence for an in vivo tissue-specific regulation of IR gene expression at the mRNA level in rats under an experimental condition of excess of catecholamines.	Catecholamines	166-180	insulin receptor	Rattus norvegicus	76-78
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aspartic Acid	13-16	insulin receptor	Rattus norvegicus	22-24
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aspartic Acid	13-16	insulin receptor	Rattus norvegicus	153-155
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Thymidine	52-61	insulin receptor	Rattus norvegicus	22-24
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aminoisobutyric Acids	106-126	insulin receptor	Rattus norvegicus	22-24
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aminoisobutyric Acids	106-126	insulin receptor	Rattus norvegicus	153-155
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aminoisobutyric Acids	128-131	insulin receptor	Rattus norvegicus	22-24
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aspartic Acid	144-147	insulin receptor	Rattus norvegicus	22-24
8969279-3	1996	However, the Asp 1048 IR inhibited IGF-I-stimulated thymidine uptake by 45% to 52% and amino acid uptake (aminoisobutyric acid [AIB]) by 58% in Asp 1048 IR cells.	Aspartic Acid	144-147	insulin receptor	Rattus norvegicus	153-155
8969279-5	1996	The inhibition of mitogenesis and AIB uptake was restored with the amelioration of the impaired tyrosine kinase activity and Shc phosphorylation by the introduction of abundant wild-type IGF-IR in Asp 1048 IR cells.	Aspartic Acid	197-200	insulin receptor	Rattus norvegicus	191-193
8969279-5	1996	The inhibition of mitogenesis and AIB uptake was restored with the amelioration of the impaired tyrosine kinase activity and Shc phosphorylation by the introduction of abundant wild-type IGF-IR in Asp 1048 IR cells.	Aspartic Acid	197-200	insulin receptor	Rattus norvegicus	206-208
8969279-6	1996	These results suggest that the Asp 1048 IR causes a dominant negative effect on IGF-IR in transmitting signals to Shc and MAP kinase activation, which leads to decreased IGF-I-stimulated DNA synthesis, and that the kinase-defective insulin receptor does not affect IGF-I-stimulated IRS-I phosphorylation, which leads to the normal IGF-I-stimulated glycogen synthesis.	Aspartic Acid	31-34	insulin receptor	Rattus norvegicus	40-42
8969279-6	1996	These results suggest that the Asp 1048 IR causes a dominant negative effect on IGF-IR in transmitting signals to Shc and MAP kinase activation, which leads to decreased IGF-I-stimulated DNA synthesis, and that the kinase-defective insulin receptor does not affect IGF-I-stimulated IRS-I phosphorylation, which leads to the normal IGF-I-stimulated glycogen synthesis.	Aspartic Acid	31-34	insulin receptor	Rattus norvegicus	84-86
8969279-6	1996	These results suggest that the Asp 1048 IR causes a dominant negative effect on IGF-IR in transmitting signals to Shc and MAP kinase activation, which leads to decreased IGF-I-stimulated DNA synthesis, and that the kinase-defective insulin receptor does not affect IGF-I-stimulated IRS-I phosphorylation, which leads to the normal IGF-I-stimulated glycogen synthesis.	Glycogen	348-356	insulin receptor	Rattus norvegicus	40-42
8914924-2	1996	The incubation of hepatocytes with sodium orthovanadate inhibited PTP activities, measured with labeled polyglutamate tyrosine (4:1) and insulin receptor peptide (1142-1153), in a dose- and time-dependent manner.	Sodium orthovanadate	35-55	insulin receptor	Rattus norvegicus	137-153
9201698-0	1997	Effect of cations on the tyrosine kinase activity of the insulin receptor: inhibition by fluoride is magnesium dependent.	Fluorides	89-97	insulin receptor	Rattus norvegicus	57-73
9201698-0	1997	Effect of cations on the tyrosine kinase activity of the insulin receptor: inhibition by fluoride is magnesium dependent.	Magnesium	101-110	insulin receptor	Rattus norvegicus	57-73
9201698-1	1997	We have recently reported that fluoride interacts directly with the insulin receptor, which causes inhibition of its phosphotransferase activity.	Fluorides	31-39	insulin receptor	Rattus norvegicus	68-84
9201698-7	1997	These results indicate that the Mg-insulin receptor complex is the major fluoride-susceptible form.	Fluorides	73-81	insulin receptor	Rattus norvegicus	35-51
9201698-8	1997	Based on the characteristics of the inhibition of tyrosine kinase shown by fluoride it might be proposed that its action is exerted by the formation of multi-ionic MgF complexes analogous to Pi, which bind to the insulin receptor kinase.	Fluorides	75-83	insulin receptor	Rattus norvegicus	213-229
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	117-132	insulin receptor	Rattus norvegicus	29-45
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
8957742-5	1996	By this method we studied: a) IR distribution in several tissues of the rat, the animal model most frequently used in studies of insulin action; b) IR regulation in streptozotocin-treated, diabetic insulin deficient rats.	Streptozocin	165-179	insulin receptor	Rattus norvegicus	148-150
8930123-0	1996	Phosphotyrosine specifies the phosphorylation by protein kinase CK2 of a peptide reproducing the activation loop of the insulin receptor protein tyrosine kinase.	Phosphotyrosine	0-15	insulin receptor	Rattus norvegicus	120-136
8930123-2	1996	It phosphorylates both threonyl and seryl residue(s) of the insulin receptor beta-subunit.	threonyl	23-31	insulin receptor	Rattus norvegicus	60-76
8930123-2	1996	It phosphorylates both threonyl and seryl residue(s) of the insulin receptor beta-subunit.	seryl	36-41	insulin receptor	Rattus norvegicus	60-76
8930123-3	1996	In this study, a series of peptides, reproducing all the threonyl sites of the intracellular domain of the insulin receptor that display the consensus sequence for CK2, has been synthesized and used as substrate for purified rat liver CK2.	threonyl	57-65	insulin receptor	Rattus norvegicus	107-123
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
8930123-7	1996	It can be concluded, from these data, that T1160 situated in the activation loop of the insulin receptor, represents an excellent target for CK2, its phosphorylation being triggered by the previous autophosphorylation of the three tyrosyl residues surrounding it, with special reference to Y1163.	cyclo(tyrosyl-tyrosyl)	231-238	insulin receptor	Rattus norvegicus	88-104
8895598-11	1996	Feeding was associated with a significantly lower IR concentration in saline-administered animals compared with the fasted state (24.2 +/- 4.0 vs 53.3 +/- 11.1).	Sodium Chloride	70-76	insulin receptor	Rattus norvegicus	50-52
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	117-132	insulin receptor	Rattus norvegicus	47-49
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	117-132	insulin receptor	Rattus norvegicus	101-103
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	188-203	insulin receptor	Rattus norvegicus	29-45
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	188-203	insulin receptor	Rattus norvegicus	47-49
8710883-1	1996	Interaction of the activated insulin receptor (IR) with its substrate, insulin receptor substrate 1 (IRS-1), via the phosphotyrosine binding domain of IRS-1 and the NPXY motif centered at phosphotyrosine 960 of the IR, is important for IRS-1 phosphorylation.	Phosphotyrosine	188-203	insulin receptor	Rattus norvegicus	101-103
8863182-0	1996	Dexamethasone modulates insulin receptor expression and subcellular distribution of the glucose transporter GLUT 1 in UMR 106-01, a clonal osteogenic sarcoma cell line.	Dexamethasone	0-13	insulin receptor	Rattus norvegicus	24-40
8863182-6	1996	By Northern and Western blot analysis, DEX was shown to stimulate insulin receptor mRNA and protein by up to 5.6-fold, but it had no effect on expression of the glucose transporter GLUT 1 mRNA or protein under basal conditions.	Dexamethasone	39-42	insulin receptor	Rattus norvegicus	66-82
8863182-10	1996	These data suggest that (i) DEX impairs basal glucose transport by post-translational mechanisms in UMR 106-01 cells, (ii) DEX increases insulin receptor mRNA, protein and insulin binding and (iii) the inhibition of glucose transport by DEX dominates its effects on the insulin receptor.	Dexamethasone	123-126	insulin receptor	Rattus norvegicus	137-153
8863182-10	1996	These data suggest that (i) DEX impairs basal glucose transport by post-translational mechanisms in UMR 106-01 cells, (ii) DEX increases insulin receptor mRNA, protein and insulin binding and (iii) the inhibition of glucose transport by DEX dominates its effects on the insulin receptor.	Dexamethasone	123-126	insulin receptor	Rattus norvegicus	270-286
8863182-10	1996	These data suggest that (i) DEX impairs basal glucose transport by post-translational mechanisms in UMR 106-01 cells, (ii) DEX increases insulin receptor mRNA, protein and insulin binding and (iii) the inhibition of glucose transport by DEX dominates its effects on the insulin receptor.	Glucose	46-53	insulin receptor	Rattus norvegicus	137-153
8863182-10	1996	These data suggest that (i) DEX impairs basal glucose transport by post-translational mechanisms in UMR 106-01 cells, (ii) DEX increases insulin receptor mRNA, protein and insulin binding and (iii) the inhibition of glucose transport by DEX dominates its effects on the insulin receptor.	Dexamethasone	123-126	insulin receptor	Rattus norvegicus	137-153
8863182-10	1996	These data suggest that (i) DEX impairs basal glucose transport by post-translational mechanisms in UMR 106-01 cells, (ii) DEX increases insulin receptor mRNA, protein and insulin binding and (iii) the inhibition of glucose transport by DEX dominates its effects on the insulin receptor.	Dexamethasone	123-126	insulin receptor	Rattus norvegicus	270-286
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
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
8679660-9	1996	Taken together, these data indicate that cAMP, similar to its effects on the glucose transporter GLUT 4 and the insulin receptor, may increase the proportion of functionally cryptic IGF-II receptors in the PM through mechanisms involving serine phosphorylation, possibly of a docking or coupling protein.	Cyclic AMP	41-45	insulin receptor	Rattus norvegicus	112-128
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.	Phosphotyrosine	81-96	insulin receptor	Rattus norvegicus	56-72
8866828-2	1996	It has been proposed that pervanadate induces insulin-like effects mediated through autophosphorylation and activation of insulin receptor (IR) even in the absence of insulin by inhibiting protein tyrosine phosphatases.	pervanadate	26-37	insulin receptor	Rattus norvegicus	122-138
8866828-2	1996	It has been proposed that pervanadate induces insulin-like effects mediated through autophosphorylation and activation of insulin receptor (IR) even in the absence of insulin by inhibiting protein tyrosine phosphatases.	pervanadate	26-37	insulin receptor	Rattus norvegicus	140-142
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.	pervanadate	26-37	insulin receptor	Rattus norvegicus	167-169
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
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.	Deoxyglucose	218-232	insulin receptor	Rattus norvegicus	167-169
8613274-10	1996	Hepatic insulin receptor mRNA levels were significantly lower in SHR than WKY fed the low salt diet.	Salts	90-94	insulin receptor	Rattus norvegicus	8-24
8613274-11	1996	High salt diet decreased significantly insulin receptor mRNA levels in the liver of WKY but not of SHR.	Salts	5-9	insulin receptor	Rattus norvegicus	39-55
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.	Lovastatin	145-155	insulin receptor	Rattus norvegicus	56-72
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
8611028-11	1996	It is concluded that, in addition to inhibition of Ras farnesylation, lovastatin reduces receptor tyrosine phosphorylation levels which also contributes to the blockade of MAPK activation by the insulin receptor.	Lovastatin	70-80	insulin receptor	Rattus norvegicus	195-211
9162438-9	1996	In these rats, the loss of the capability to down-regulate insulin receptor in the kidney when extracellular fluid volume is expanded can lead to further sodium retention and might play a role in the development and maintenance of hypertension.	Sodium	154-160	insulin receptor	Rattus norvegicus	59-75
8726468-6	1996	However, cell-exposure to insulin and PCMBS in relatively high doses was destructive, as demonstrated by decreased glycogen levels, most probably as a result of insulin-receptor overstimulation and metabolic stress.	4-Chloromercuribenzenesulfonate	38-43	insulin receptor	Rattus norvegicus	161-177
9244182-4	1996	Removal of cell surface insulin-receptor complexes with trypsin showed that the effects on binding exerted by bpV(pic) and vanadate were due to a similar increase in both cell surface binding and intracellular accumulation of radioactivity.	bromopyruvate	110-113	insulin receptor	Rattus norvegicus	24-40
9244182-4	1996	Removal of cell surface insulin-receptor complexes with trypsin showed that the effects on binding exerted by bpV(pic) and vanadate were due to a similar increase in both cell surface binding and intracellular accumulation of radioactivity.	pic	114-117	insulin receptor	Rattus norvegicus	24-40
9244182-4	1996	Removal of cell surface insulin-receptor complexes with trypsin showed that the effects on binding exerted by bpV(pic) and vanadate were due to a similar increase in both cell surface binding and intracellular accumulation of radioactivity.	Vanadates	123-131	insulin receptor	Rattus norvegicus	24-40
8725009-0	1996	Histone H4 stimulates glucose uptake through the insulin receptor.	Glucose	22-29	insulin receptor	Rattus norvegicus	49-65
8725009-6	1996	Also, quercetin, a bioflavenoid that inhibits the insulin receptor tyrosine kinase activity, inhibits the actions of both histone H4 and insulin.	Quercetin	6-15	insulin receptor	Rattus norvegicus	50-66
8725009-6	1996	Also, quercetin, a bioflavenoid that inhibits the insulin receptor tyrosine kinase activity, inhibits the actions of both histone H4 and insulin.	bioflavenoid	19-31	insulin receptor	Rattus norvegicus	50-66
8927024-4	1995	We demonstrated that in rat adipocytes both acute insulin effects, e.g. stimulation of IGF-II and transferrin binding and a chronic effect, insulin receptor downregulation, were stimulated by vanadate.	Vanadates	192-200	insulin receptor	Rattus norvegicus	140-156
8927041-7	1995	The insulin receptor numbers in vanadate-treated obese rats increased (119%) compared to levels in untreated obese animals.	Vanadates	32-40	insulin receptor	Rattus norvegicus	4-20
8549754-0	1995	Glucose- and insulin-induced phosphorylation of the insulin receptor and its primary substrates IRS-1 and IRS-2 in rat pancreatic islets.	Glucose	0-7	insulin receptor	Rattus norvegicus	52-68
8927047-7	1995	Replacement of vanadium with either molybdenum or tungsten resulted in equally potent inhibition of IR dephosphorylation.	Tungsten	50-58	insulin receptor	Rattus norvegicus	100-102
8927024-7	1995	Finally vanadate augmented the extent of activation of the insulin receptor kinase by submaximal insulin concentrations.	Vanadates	8-16	insulin receptor	Rattus norvegicus	59-75
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.	bromopyruvate	26-29	insulin receptor	Rattus norvegicus	106-108
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
8927047-7	1995	Replacement of vanadium with either molybdenum or tungsten resulted in equally potent inhibition of IR dephosphorylation.	Vanadium	15-23	insulin receptor	Rattus norvegicus	100-102
8927027-6	1995	The insulin receptor numbers were significantly (p &lt; 0.01) higher in vanadate-treated obese rats as compared to the untreated ones.	Vanadates	72-80	insulin receptor	Rattus norvegicus	4-20
8927047-7	1995	Replacement of vanadium with either molybdenum or tungsten resulted in equally potent inhibition of IR dephosphorylation.	Molybdenum	36-46	insulin receptor	Rattus norvegicus	100-102
21153221-0	1995	Insulin-like effects of tungstate and molybdate: mediation through insulin receptor independent pathways.	tungstate	24-33	insulin receptor	Rattus norvegicus	67-83
8927052-10	1995	The insulin-stimulated phosphorylation of insulin receptor beta subunit and its tyrosine kinase activity was increased in streptozotocin-induced diabetic rats after treatment with vanadate.	Streptozocin	122-136	insulin receptor	Rattus norvegicus	42-58
8927052-10	1995	The insulin-stimulated phosphorylation of insulin receptor beta subunit and its tyrosine kinase activity was increased in streptozotocin-induced diabetic rats after treatment with vanadate.	Vanadates	180-188	insulin receptor	Rattus norvegicus	42-58
8927052-11	1995	Our results support the view that insulin receptor is one of the sites involved in the insulin-mimetic actions of vanadate.	Vanadates	114-122	insulin receptor	Rattus norvegicus	34-50
7487890-12	1995	We conclude that (1) the decreased autophosphorylation rate of the liver insulin receptor from pregnant rats is associated with the impairment of its autoactivation cascade, probably as a consequence of the basal Ser/Thr phosphorylation; and (2) the inhibition of the autoactivation cascade does not account for the overall inhibition of autophosphorylation observed in receptors from pregnant rats.	Serine	213-216	insulin receptor	Rattus norvegicus	73-89
7487890-12	1995	We conclude that (1) the decreased autophosphorylation rate of the liver insulin receptor from pregnant rats is associated with the impairment of its autoactivation cascade, probably as a consequence of the basal Ser/Thr phosphorylation; and (2) the inhibition of the autoactivation cascade does not account for the overall inhibition of autophosphorylation observed in receptors from pregnant rats.	Threonine	217-220	insulin receptor	Rattus norvegicus	73-89
21153221-0	1995	Insulin-like effects of tungstate and molybdate: mediation through insulin receptor independent pathways.	molybdate	38-47	insulin receptor	Rattus norvegicus	67-83
7653545-3	1995	In the present work we studied the effect of SSG ILI from normal and STZ diabetic rats (ILI-N and ILI-D, respectively) on insulin receptor binding and function in LMH cell line.	Streptozocin	69-72	insulin receptor	Rattus norvegicus	122-138
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
7789629-2	1995	Recently, we demonstrated that high glucose levels may mimic the effects of phorbol esters on protein kinase C (PKC) and insulin receptor function (J Biol Chem 269:3381-3386, 1994).	Glucose	36-43	insulin receptor	Rattus norvegicus	121-137
7789629-2	1995	Recently, we demonstrated that high glucose levels may mimic the effects of phorbol esters on protein kinase C (PKC) and insulin receptor function (J Biol Chem 269:3381-3386, 1994).	Phorbol Esters	76-90	insulin receptor	Rattus norvegicus	121-137
7607300-0	1995	Tannic acid inhibits insulin-stimulated lipogenesis in rat adipose tissue and insulin receptor function in vitro.	Tannins	0-11	insulin receptor	Rattus norvegicus	78-94
7607300-8	1995	However, insulin-stimulated autophosphorylation of the insulin receptor, and receptor-associated tyrosine kinase phosphorylation of RR-SRC peptide, were inhibited by tannic acid at concentrations as low as 25 microM.	Tannins	166-177	insulin receptor	Rattus norvegicus	55-71
8068015-9	1994	The locus of staurosporine"s action appears to be distal from the initial insulin-receptor signalling, at a step that regulates the specific translocation of the glucose transporters to the plasma membranes.	Staurosporine	13-26	insulin receptor	Rattus norvegicus	74-90
7738028-8	1995	Interestingly, preincubation with human-specific anti-insulin receptor antibody abolished the increased insulin sensitivity in glucose incorporation into glycogen in HIR delta 978 cells.	Glucose	127-134	insulin receptor	Rattus norvegicus	54-70
7738028-8	1995	Interestingly, preincubation with human-specific anti-insulin receptor antibody abolished the increased insulin sensitivity in glucose incorporation into glycogen in HIR delta 978 cells.	Glycogen	154-162	insulin receptor	Rattus norvegicus	54-70
7750897-8	1995	During the suckling-weaning transition, insulin receptor mRNA level decreased 2-fold in rats weaned onto a high carbohydrate diet but remained unchanged in rats weaned onto a high fat diet.	Carbohydrates	112-124	insulin receptor	Rattus norvegicus	40-56
7562114-3	1995	On the other hand, the PUFA-mediated suppression of the mRNA concentrations was partially restored by treatment with pioglitazone, a candidate for increasing insulin receptor phosphorylation.	Pioglitazone	117-129	insulin receptor	Rattus norvegicus	158-174
7706987-12	1995	These results suggest that (1) in hyperthyroidism, increased insulin-stimulated glucose transport is associated with an increase of primarily GLUT4 glucose transporters, which may be responsible for the increment of peripheral glucose utilization in hyperthyroidism, and (2) the effect of hypothyroidism on insulin action in adipocytes is characterized by a state of increased insulin sensitivity, as indicated by the increase in insulin receptor affinity and tyrosine kinase activity.	Glucose	80-87	insulin receptor	Rattus norvegicus	430-446
7706987-12	1995	These results suggest that (1) in hyperthyroidism, increased insulin-stimulated glucose transport is associated with an increase of primarily GLUT4 glucose transporters, which may be responsible for the increment of peripheral glucose utilization in hyperthyroidism, and (2) the effect of hypothyroidism on insulin action in adipocytes is characterized by a state of increased insulin sensitivity, as indicated by the increase in insulin receptor affinity and tyrosine kinase activity.	Glucose	148-155	insulin receptor	Rattus norvegicus	430-446
7814420-3	1995	After 2 min of insulin exposure, the specific phosphotyrosine content of the insulin receptor in the internal membranes (IM) peaks at a level 5-6-fold higher than the plasma membrane (PM) receptor and then declines after 5-8 min to a level similar to the PM receptor.	Phosphotyrosine	46-61	insulin receptor	Rattus norvegicus	77-93
8852272-6	1995	In alloxan-induced diabetes metformin (Met) treatment led to an increase in insulin receptor number in liver plasma membranes (before Met: 46.50 +/- 2.69, after Met: 76.00 +/- 3.39 fmol/mg, p &lt; 0.001) and a decrease in plasma lipid peroxidation levels compared to the non-treated group (before Met: 1.85 +/- 0.53, after Met: 1.10 +/- 0.09 nmol MDA/ml, p &lt; 0.05).	Alloxan	3-10	insulin receptor	Rattus norvegicus	76-92
7704100-0	1994	Tissue-specific changes in insulin receptor mRNA concentrations in dexamethasone-treated and adrenalectomized rats.	Dexamethasone	67-80	insulin receptor	Rattus norvegicus	27-43
7704100-3	1994	Dot-Blot assays followed by densitometry indicated that dexamethasone induced an approximately three-fold increase in IR mRNA in liver, but not in epididymal adipose tissue.	Dexamethasone	56-69	insulin receptor	Rattus norvegicus	118-120
7731060-3	1994	It has a high degree of sequence similarity to the insulin receptor (IR), and the putative ligand-specific binding site has been localized to a cysteine-rich region (CRR) of the alpha-chain.	Cysteine	144-152	insulin receptor	Rattus norvegicus	51-67
7731060-3	1994	It has a high degree of sequence similarity to the insulin receptor (IR), and the putative ligand-specific binding site has been localized to a cysteine-rich region (CRR) of the alpha-chain.	Cysteine	144-152	insulin receptor	Rattus norvegicus	69-71
7980535-1	1994	The effect of diabetes on insulin receptor processing was assessed in rat hepatocytes, 2-4 weeks after the induction of diabetes with streptozotocin.	Streptozocin	134-148	insulin receptor	Rattus norvegicus	26-42
8093054-1	1994	To characterize the Leu 193 mutant insulin receptor, which was found in a patient with extreme insulin resistance, the mutant insulin receptor was overexpressed in Rat-1 fibroblasts by transfection of mutated insulin receptor cDNA.	Leucine	20-23	insulin receptor	Rattus norvegicus	126-142
7895667-3	1995	Dexamethasone (1 microM) induced a time- and dose-dependent increase in insulin receptor levels in Fao cells, reaching 135 +/- 3% of basal levels after 24 h (P &lt; 0.05).	Dexamethasone	0-13	insulin receptor	Rattus norvegicus	72-88
7895667-8	1995	When cells were exposed to both insulin and dexamethasone, the effect of insulin to reduce insulin receptor and IRS-1 levels and insulin-stimulated IRS-1 phosphorylation dominated.	Dexamethasone	44-57	insulin receptor	Rattus norvegicus	91-107
7805875-2	1995	We have investigated the effects of BFA on the traffic of the insulin receptor in HIRcB cells, a cell line derived from Rat-1 fibroblasts that over-expresses a normal human insulin receptor.	Brefeldin A	36-39	insulin receptor	Rattus norvegicus	62-78
7805875-8	1995	These findings suggest that BFA blocks an early step in the chain of events that lead to insulin receptor internalization without affecting the interactions of the receptor with insulin, the stimulation of the tyrosine kinase activity of the receptor by the hormone, or other insulin-regulated signalling pathways, such as the activation of MAPK.	Brefeldin A	28-31	insulin receptor	Rattus norvegicus	89-105
8852272-6	1995	In alloxan-induced diabetes metformin (Met) treatment led to an increase in insulin receptor number in liver plasma membranes (before Met: 46.50 +/- 2.69, after Met: 76.00 +/- 3.39 fmol/mg, p &lt; 0.001) and a decrease in plasma lipid peroxidation levels compared to the non-treated group (before Met: 1.85 +/- 0.53, after Met: 1.10 +/- 0.09 nmol MDA/ml, p &lt; 0.05).	Metformin	28-37	insulin receptor	Rattus norvegicus	76-92
16358398-10	1994	Insulin receptor number was significantly reduced in obese WDF rats ( 2.778 +/- 0.617 pmol/mg protein), compared to obese Zucker rats (4.441 +/- 0.913 pmol/mg potein).	potein	159-165	insulin receptor	Rattus norvegicus	0-16
8048924-7	1994	These data indicate that elevation of intracellular cAMP blocks the insulin-stimulated MAP kinase pathway downstream of insulin receptor.	Cyclic AMP	52-56	insulin receptor	Rattus norvegicus	120-136
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
8037757-1	1994	Gene expression of GLUT4 and insulin receptor in soleus muscle of high-fat and high-carbohydrate diet fed rats was studied by measuring mRNA.	Carbohydrates	84-96	insulin receptor	Rattus norvegicus	29-45
8198614-0	1994	High glucose condition activates protein tyrosine phosphatases and deactivates insulin receptor function in insulin-sensitive rat 1 fibroblasts.	Glucose	5-12	insulin receptor	Rattus norvegicus	79-95
8198614-1	1994	To investigate the mechanism for the impairment of insulin receptor kinase activity induced by high glucose (HG) in Rat 1 fibroblasts that expressed human insulin receptors (HIRc), we measured protein tyrosine phosphatase (PTPase) activity in HG cells.	Glucose	100-107	insulin receptor	Rattus norvegicus	51-67
8198614-4	1994	These results indicate that desensitization of insulin receptor function by a high glucose condition is associated with the activation of PTPase activity.	Glucose	83-90	insulin receptor	Rattus norvegicus	47-63
8192673-11	1994	The results suggest that dietary omega-3 and polyunsaturated fatty acids increase insulin binding to sarcolemma by changing the fatty acyl composition of phospholipid surrounding the insulin receptor, and this might be the mechanism by which dietary fatty acids modify insulin action.	omega-3	33-40	insulin receptor	Rattus norvegicus	183-199
8192673-11	1994	The results suggest that dietary omega-3 and polyunsaturated fatty acids increase insulin binding to sarcolemma by changing the fatty acyl composition of phospholipid surrounding the insulin receptor, and this might be the mechanism by which dietary fatty acids modify insulin action.	Fatty Acids, Unsaturated	45-72	insulin receptor	Rattus norvegicus	183-199
8192673-11	1994	The results suggest that dietary omega-3 and polyunsaturated fatty acids increase insulin binding to sarcolemma by changing the fatty acyl composition of phospholipid surrounding the insulin receptor, and this might be the mechanism by which dietary fatty acids modify insulin action.	Phospholipids	154-166	insulin receptor	Rattus norvegicus	183-199
8192673-11	1994	The results suggest that dietary omega-3 and polyunsaturated fatty acids increase insulin binding to sarcolemma by changing the fatty acyl composition of phospholipid surrounding the insulin receptor, and this might be the mechanism by which dietary fatty acids modify insulin action.	Fatty Acids	61-72	insulin receptor	Rattus norvegicus	183-199
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
8179619-1	1994	Dexamethasone treatment of IM-9 lymphocytes and Fao hepatoma cells resulted in an increase in synthesis of the insulin receptor.	Dexamethasone	0-13	insulin receptor	Rattus norvegicus	111-127
8031552-8	1994	Stimulation of insulin receptors alone, with 2.5 pg/mL insulin receptor-specific antibody, stimulates glucose transport by 20%, suggesting transport can be stimulated by an IGF-1 receptor independent mechanism.	Glucose	102-109	insulin receptor	Rattus norvegicus	15-31
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
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
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
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.	Phosphatidylinositols	214-234	insulin receptor	Rattus norvegicus	143-159
8138059-1	1994	Palmitate has been shown to stimulate glucose transport, translocation of GLUT4 and insulin receptor autophosphorylation in isolated rat adipocytes (Biochem Biophys Res Commun 177:343-49, 1991).	Palmitates	0-9	insulin receptor	Rattus norvegicus	84-100
8144537-8	1994	Vanadyl (4+) but not vanadate (5+) inhibits receptor tyrosine kinases such as the insulin receptor (IC50 value = 23 +/- 4 microM) and the insulin-like growth factor-I receptor (IC50 = 19 +/- 3 microM).	Vanadates	0-7	insulin receptor	Rattus norvegicus	82-98
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
7508875-0	1994	Troglitazone prevents glucose-induced insulin resistance of insulin receptor in rat-1 fibroblasts.	Troglitazone	0-12	insulin receptor	Rattus norvegicus	60-76
7508875-0	1994	Troglitazone prevents glucose-induced insulin resistance of insulin receptor in rat-1 fibroblasts.	Glucose	22-29	insulin receptor	Rattus norvegicus	60-76
7508875-10	1994	Acute hyperglycemia (25 mM glucose) induced a significant inhibition of the insulin receptor kinase (IRK) activity within 30 min (inhibition to 30 +/- 12.5% of maximal insulin-stimulated beta-subunit phosphorylation, n = 9, P &lt; 0.01).	Glucose	27-34	insulin receptor	Rattus norvegicus	76-92
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
7508912-0	1994	Glucose-induced translocation of protein kinase C isoforms in rat-1 fibroblasts is paralleled by inhibition of the insulin receptor tyrosine kinase.	Glucose	0-7	insulin receptor	Rattus norvegicus	115-131
7508912-10	1994	There is indirect evidence that this effect is mediated by a glucose-induced PKC translocation/activation and serine phosphorylation of the insulin receptor.	Glucose	61-68	insulin receptor	Rattus norvegicus	140-156
7508912-10	1994	There is indirect evidence that this effect is mediated by a glucose-induced PKC translocation/activation and serine phosphorylation of the insulin receptor.	Serine	110-116	insulin receptor	Rattus norvegicus	140-156
8106400-7	1994	It is concluded, therefore, that activation of wortmannin-sensitive PI 3-kinase plays a pivotal role in the intracellular signaling pathways arising from the insulin receptor autophosphorylation and leading to certain metabolic responses.	Wortmannin	47-57	insulin receptor	Rattus norvegicus	158-174
8306999-9	1994	In conclusion, our data show that, in its native environment, the cardiac insulin receptor couples to at least three GTP-binding proteins.	Guanosine Triphosphate	117-120	insulin receptor	Rattus norvegicus	74-90
8304482-0	1994	Effect of dietary sodium chloride on insulin receptor number and mRNA levels in rat kidney.	Sodium Chloride	18-33	insulin receptor	Rattus norvegicus	37-53
8297340-9	1994	However, the addition of ATP, which allows phosphorylation of IRS-1 by the insulin receptor, also enhances the coupling of PtdIns 3-kinase to the insulin receptor.	Adenosine Triphosphate	25-28	insulin receptor	Rattus norvegicus	75-91
8297340-9	1994	However, the addition of ATP, which allows phosphorylation of IRS-1 by the insulin receptor, also enhances the coupling of PtdIns 3-kinase to the insulin receptor.	Adenosine Triphosphate	25-28	insulin receptor	Rattus norvegicus	146-162
8304482-7	1994	Insulin receptor mRNA, as quantified by Northern and slot blot analysis, was inversely related to salt intake in absence of a change in plasma glucose, insulin, and corticosterone levels.	Salts	98-102	insulin receptor	Rattus norvegicus	0-16
8275968-1	1994	The effect of pervanadate, a potent insulinomimetic agent that inhibits insulin receptor dephosphorylation in vitro, is now assessed in vivo.	pervanadate	14-25	insulin receptor	Rattus norvegicus	72-88
8243832-13	1993	We conclude that glimepiride activates glucose transport by stimulation of GLUT1 and GLUT4 translocation in rat adipocytes via interference at a site downstream of the putative molecular defect in the signaling cascade between the insulin receptor and the glucose transport system induced by high concentrations of glucose and insulin.	glimepiride	17-28	insulin receptor	Rattus norvegicus	231-247
8280122-0	1993	Pioglitazone ameliorates high glucose induced desensitization of insulin receptor kinase in Rat 1 fibroblasts in culture.	Pioglitazone	0-12	insulin receptor	Rattus norvegicus	65-81
8280122-0	1993	Pioglitazone ameliorates high glucose induced desensitization of insulin receptor kinase in Rat 1 fibroblasts in culture.	Glucose	30-37	insulin receptor	Rattus norvegicus	65-81
8280122-2	1993	To clarify the mechanism, we studied in vitro effects of glucose and pioglitazone on the insulin receptor function using Rat 1 fibroblasts which expressed human insulin receptors.	Glucose	57-64	insulin receptor	Rattus norvegicus	89-105
8280122-2	1993	To clarify the mechanism, we studied in vitro effects of glucose and pioglitazone on the insulin receptor function using Rat 1 fibroblasts which expressed human insulin receptors.	Pioglitazone	69-81	insulin receptor	Rattus norvegicus	89-105
8280122-3	1993	Insulin receptor kinase activity was impaired by incubating cells for 4 days in the presence of 27mM D-glucose.	Glucose	101-110	insulin receptor	Rattus norvegicus	0-16
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	31-40	insulin receptor	Rattus norvegicus	137-153
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	31-40	insulin receptor	Rattus norvegicus	290-306
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Pioglitazone	56-68	insulin receptor	Rattus norvegicus	137-153
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Pioglitazone	56-68	insulin receptor	Rattus norvegicus	290-306
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	33-40	insulin receptor	Rattus norvegicus	137-153
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	33-40	insulin receptor	Rattus norvegicus	290-306
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Pioglitazone	187-199	insulin receptor	Rattus norvegicus	137-153
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Pioglitazone	187-199	insulin receptor	Rattus norvegicus	290-306
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	107-114	insulin receptor	Rattus norvegicus	137-153
8280122-6	1993	However, exposure of both 27mM D-glucose and 0.1 microM pioglitazone to the cells completely prevented the glucose-induced impairment of insulin receptor kinase activity, suggesting that pioglitazone might reverse the processes which are critical for the glucose-induced desensitization of insulin receptor kinase.	Glucose	107-114	insulin receptor	Rattus norvegicus	290-306
8243832-13	1993	We conclude that glimepiride activates glucose transport by stimulation of GLUT1 and GLUT4 translocation in rat adipocytes via interference at a site downstream of the putative molecular defect in the signaling cascade between the insulin receptor and the glucose transport system induced by high concentrations of glucose and insulin.	Glucose	39-46	insulin receptor	Rattus norvegicus	231-247
7523848-0	1993	Does the insulin-mimetic action of vanadate involve insulin receptor kinase?	Vanadates	35-43	insulin receptor	Rattus norvegicus	52-68
7523848-1	1993	Effects of vanadate administration on the insulin receptor status in liver were examined in streptozotocin-induced diabetic rats.	Vanadates	11-19	insulin receptor	Rattus norvegicus	42-58
7523848-7	1993	In vitro, vanadate prevented the dephosphorylation of the phosphorylated insulin receptor and increased its tyrosine kinase activity in the absence as well as presence of insulin.	Vanadates	10-18	insulin receptor	Rattus norvegicus	73-89
7523848-8	1993	The findings of this study further support the view that insulin receptor is one of the sites involved in the insulin-mimetic actions of vanadate.	Vanadates	137-145	insulin receptor	Rattus norvegicus	57-73
8226791-2	1993	Peptides from the alpha 1 domain of the major histocompatibility complex class I antigen (MHC class I), e.g. Dk-(61-85) and Dk-(62-85), have been shown previously to augment glucose uptake in insulin-stimulated cells and to inhibit insulin receptor internalization (Stagsted, J., Reaven, G. M., Hansen, T., Goldstein, A., and Olsson, L. (1990) Cell 62, 297-307).	Glucose	174-181	insulin receptor	Rattus norvegicus	232-248
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.	Serine	75-81	insulin receptor	Rattus norvegicus	36-52
7691892-0	1993	Modulation of insulin receptor, insulin receptor substrate-1, and phosphatidylinositol 3-kinase in liver and muscle of dexamethasone-treated rats.	Dexamethasone	119-132	insulin receptor	Rattus norvegicus	14-30
8396020-6	1993	Additionally, polylysine, a polycation postulated to interact with the insulin receptor beta-subunit acidic domain, increased autophosphorylation and facilitated insulin-induced phosphorylation of calmodulin in the wild type as well as the hIR1262 receptors.	Polylysine	14-24	insulin receptor	Rattus norvegicus	71-87
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.	Threonine	83-92	insulin receptor	Rattus norvegicus	36-52
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
8503928-0	1993	Phorbol esters induce insulin receptor phosphorylation in transfected fibroblasts without affecting tyrosine kinase activity.	Phorbol Esters	0-14	insulin receptor	Rattus norvegicus	22-38
8355664-9	1993	The tissue-specific expression of the known insulin receptor isoforms generated by alternative splicing (insulin receptor types A and B), as assessed by polymerase chain reaction amplification with oligonucleotide primers flanking exon 11, was not correlated with the differences in the IC50 values and ratios for insulin and B29,B29"-suberoyl-insulin.	Oligonucleotides	198-213	insulin receptor	Rattus norvegicus	44-60
8226487-7	1993	The results of this study 1) provide evidence that post-insulin receptor binding mechanisms also play a role in the enhanced response of the insulin-dependent pathway for stimulation of glucose transport in unweighted skeletal muscle and 2) indicate that IGF-I action on glucose transport is included in this enhanced response in unweighted muscle.	Glucose	186-193	insulin receptor	Rattus norvegicus	56-72
8226487-7	1993	The results of this study 1) provide evidence that post-insulin receptor binding mechanisms also play a role in the enhanced response of the insulin-dependent pathway for stimulation of glucose transport in unweighted skeletal muscle and 2) indicate that IGF-I action on glucose transport is included in this enhanced response in unweighted muscle.	Glucose	271-278	insulin receptor	Rattus norvegicus	56-72
8428637-0	1993	Regulation of cardiac insulin receptor function by guanosine nucleotides.	guanosine nucleotides	51-72	insulin receptor	Rattus norvegicus	22-38
7683695-7	1993	Cortisone treatment increased the amount of insulin receptor protein by 36%, but decreased the total level of receptor tyrosine phosphorylation (69 +/- 4% of control, P &lt; 0.05).	Cortisone	0-9	insulin receptor	Rattus norvegicus	44-60
7686248-3	1993	We have described a serine kinase (here designated insulin receptor serine (IRS) kinase) from rat liver membranes that co-purifies with IR on wheat germ agglutinin-agarose.	Sepharose	164-171	insulin receptor	Rattus norvegicus	51-67
7686248-3	1993	We have described a serine kinase (here designated insulin receptor serine (IRS) kinase) from rat liver membranes that co-purifies with IR on wheat germ agglutinin-agarose.	Sepharose	164-171	insulin receptor	Rattus norvegicus	76-78
8454619-5	1993	Staurosporine and K-252a were less effective by more than 2 and 1 orders of magnitude, respectively, in inhibiting insulin receptor-catalyzed PolyGlu4Tyr phosphorylation in cell-free experiments.	Staurosporine	0-13	insulin receptor	Rattus norvegicus	115-131
8454619-5	1993	Staurosporine and K-252a were less effective by more than 2 and 1 orders of magnitude, respectively, in inhibiting insulin receptor-catalyzed PolyGlu4Tyr phosphorylation in cell-free experiments.	staurosporine aglycone	18-24	insulin receptor	Rattus norvegicus	115-131
8454619-5	1993	Staurosporine and K-252a were less effective by more than 2 and 1 orders of magnitude, respectively, in inhibiting insulin receptor-catalyzed PolyGlu4Tyr phosphorylation in cell-free experiments.	polyglu4tyr	142-153	insulin receptor	Rattus norvegicus	115-131
8454619-12	1993	These findings explain further vanadate"s post-insulin receptor actions and raise possible application in the management of glucose metabolism in insulin-independent fashion in pathological conditions.	Vanadates	31-39	insulin receptor	Rattus norvegicus	47-63
8444185-5	1993	Maximal insulin-induced Ras.GTP formation is less but in cells overexpressing the insulin receptor a similar high response of Ras.GTP formation is observed after insulin stimulation.	Guanosine Triphosphate	130-133	insulin receptor	Rattus norvegicus	82-98
8444185-7	1993	In the Rat-1-derived cell line, H13IR2000, overexpressing both p21Ha-ras and the insulin receptor, the activated insulin receptor generates approximately 1 mol Ras.GTP/mol activated insulin receptor.	Guanosine Triphosphate	164-167	insulin receptor	Rattus norvegicus	81-97
8444185-7	1993	In the Rat-1-derived cell line, H13IR2000, overexpressing both p21Ha-ras and the insulin receptor, the activated insulin receptor generates approximately 1 mol Ras.GTP/mol activated insulin receptor.	Guanosine Triphosphate	164-167	insulin receptor	Rattus norvegicus	113-129
8444185-7	1993	In the Rat-1-derived cell line, H13IR2000, overexpressing both p21Ha-ras and the insulin receptor, the activated insulin receptor generates approximately 1 mol Ras.GTP/mol activated insulin receptor.	Guanosine Triphosphate	164-167	insulin receptor	Rattus norvegicus	113-129
8382701-12	1993	The complex of tyrosyl-phosphorylated IRS-1.p85 that formed in response to insulin was localized to a very low density vesicle subpopulation that could be distinguished from vesicles containing the GLUT-4 glucose transporter and the insulin receptor.	cyclo(tyrosyl-tyrosyl)	15-22	insulin receptor	Rattus norvegicus	233-249
8472865-0	1993	Insulin receptor beta-subunit serine phosphorylation in permeabilized cultured fetal rat hepatocytes.	Serine	30-36	insulin receptor	Rattus norvegicus	0-16
8472865-3	1993	Considering in particular its immunoprecipitation by a monoclonal antibody directed against insulin receptor, the 32P-labeled 95 kDa protein represented the beta-subunit of the insulin receptor.	Phosphorus-32	114-117	insulin receptor	Rattus norvegicus	92-108
8472865-3	1993	Considering in particular its immunoprecipitation by a monoclonal antibody directed against insulin receptor, the 32P-labeled 95 kDa protein represented the beta-subunit of the insulin receptor.	Phosphorus-32	114-117	insulin receptor	Rattus norvegicus	177-193
8428637-4	1993	In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [35S]GTP-gamma-S to the partially purified insulin receptor.	Adenosine Triphosphate	19-22	insulin receptor	Rattus norvegicus	124-140
8428637-4	1993	In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [35S]GTP-gamma-S to the partially purified insulin receptor.	Adenylyl Imidodiphosphate	26-33	insulin receptor	Rattus norvegicus	124-140
8428637-4	1993	In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [35S]GTP-gamma-S to the partially purified insulin receptor.	Sulfur-35	82-85	insulin receptor	Rattus norvegicus	124-140
8428637-4	1993	In the presence of ATP or AMP-PNP, insulin significantly enhanced the binding of [35S]GTP-gamma-S to the partially purified insulin receptor.	Guanosine 5'-O-(3-Thiotriphosphate)	86-97	insulin receptor	Rattus norvegicus	124-140
1280238-0	1992	Effects of STZ-induced diabetes and fasting on insulin receptor mRNA expression and insulin receptor gene transcription in rat liver.	Streptozocin	11-14	insulin receptor	Rattus norvegicus	47-63
8472851-1	1993	Benzyl succinate inhibited insulin binding and tyrosine receptor kinase in a concentration-dependent manner in the partially purified insulin receptor preparation from rat skeletal muscle.	benzylsuccinate	0-16	insulin receptor	Rattus norvegicus	134-150
8429089-1	1993	In order to clarify the mechanism of regulation of glycogen metabolism in fetal rat liver during gestation, we measured glycogen synthetase activity, and the binding capacity of the insulin receptor.	Glycogen	51-59	insulin receptor	Rattus norvegicus	182-198
1280238-4	1992	Northern blot analysis of either total or poly (A)+ RNA from livers of hypo- and normoinsulinemic rats revealed two major insulin receptor mRNA species of 9.5 and 7.5 kbs.	Poly A	42-50	insulin receptor	Rattus norvegicus	122-138
1280238-6	1992	The effects of STZ administration and fasting on insulin receptor binding and insulin receptor mRNA levels were fully reversed by insulin treatment or refeeding, respectively.	Streptozocin	15-18	insulin receptor	Rattus norvegicus	49-65
1280238-6	1992	The effects of STZ administration and fasting on insulin receptor binding and insulin receptor mRNA levels were fully reversed by insulin treatment or refeeding, respectively.	Streptozocin	15-18	insulin receptor	Rattus norvegicus	78-94
1280238-8	1992	In vitro nuclear transcription assays showed that the rate of transcription of the insulin receptor gene was increased 2-fold in STZ-induced diabetic rats and fasted rats relative to control animals.	Streptozocin	129-132	insulin receptor	Rattus norvegicus	83-99
1420153-2	1992	PTPase activity was measured using a 32P-labeled peptide corresponding to the major site of insulin receptor autophosphorylation.	Phosphorus-32	37-40	insulin receptor	Rattus norvegicus	92-108
1331176-3	1992	In the present study we have examined the levels of IRS-1 and the phosphorylation state of insulin receptor and IRS-1 in liver and muscle after insulin stimulation in vivo in two rat models of insulin resistance, i.e., insulinopenic diabetes and fasting, and a mouse model of non-insulin-dependent diabetes mellitus (ob/ob) by immunoblotting with anti-peptide antibodies to IRS-1 and anti-phosphotyrosine antibodies.	Phosphotyrosine	389-404	insulin receptor	Rattus norvegicus	91-107
1420153-5	1992	Both the cytosolic and particulate PTPase fractions were active toward the tyrosyl-phosphorylated insulin receptor in vitro.	cyclo(tyrosyl-tyrosyl)	75-82	insulin receptor	Rattus norvegicus	98-114
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
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
1324726-0	1992	Quercetin selectively inhibits insulin receptor function in vitro and the bioresponses of insulin and insulinomimetic agents in rat adipocytes.	Quercetin	0-9	insulin receptor	Rattus norvegicus	31-47
1321126-2	1992	A number of protein-tyrosine phosphatase(s) (PTPases) have been shown to dephosphorylate the insulin receptor in vitro; however, it is not known whether any individual PTPase has specificity for certain phosphotyrosine residues of the receptor that regulate its intrinsic tyrosine kinase activity.	Phosphotyrosine	203-218	insulin receptor	Rattus norvegicus	93-109
1386819-0	1992	Tissue-specific regulation of insulin receptor mRNA levels in rats with STZ-induced diabetes mellitus.	Streptozocin	72-75	insulin receptor	Rattus norvegicus	30-46
1637843-9	1992	Addition of exogenous insulin receptor to BBM and BLM increased the phosphorylation of most of the substrates.	Santowhite powder	42-45	insulin receptor	Rattus norvegicus	22-38
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
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.	Sepharose	127-136	insulin receptor	Rattus norvegicus	146-162
1321126-8	1992	The accelerated deactivation of the insulin receptor kinase by LAR and its relative preference for regulatory phosphotyrosine residues further support a potential role for this transmembrane PTPase in the physiological regulation of insulin receptors in intact cells.	Phosphotyrosine	110-125	insulin receptor	Rattus norvegicus	36-52
1321133-3	1992	Phosphorylation of pp160 and autophosphorylation of the insulin receptor increased as a function of Mn2+ concentration in the media with near maximum responses at 10 mM.	Manganese(2+)	100-104	insulin receptor	Rattus norvegicus	56-72
1321133-15	1992	Dephosphorylation of pp160 and the insulin receptor was analyzed directly by permeabilizing prelabeled insulin-treated adipocytes in the presence of EDTA (10 mM).	Edetic Acid	149-153	insulin receptor	Rattus norvegicus	35-51
1321717-1	1992	Phosphatidylinositol (PtdIns) 3-kinase is thought to participate in the signal transduction pathways initiated by the activation of receptor tyrosine kinases including the insulin receptor.	Phosphatidylinositols	0-20	insulin receptor	Rattus norvegicus	172-188
1321133-16	1992	Dephosphorylation of pp160 was especially rapid with a t1/2 of approximately 10 s. The t1/2 for the insulin receptor was 37 s. Zn2+ at 1 mM (a concentration that inhibited the insulin receptor kinase) was a strong inhibitor of dephosphorylation, prolonging the rate of pp160 dephosphorylation more than 12-fold and insulin receptor dephosphorylation 3-fold.	Zinc	127-131	insulin receptor	Rattus norvegicus	100-116
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
1321133-16	1992	Dephosphorylation of pp160 was especially rapid with a t1/2 of approximately 10 s. The t1/2 for the insulin receptor was 37 s. Zn2+ at 1 mM (a concentration that inhibited the insulin receptor kinase) was a strong inhibitor of dephosphorylation, prolonging the rate of pp160 dephosphorylation more than 12-fold and insulin receptor dephosphorylation 3-fold.	Zinc	127-131	insulin receptor	Rattus norvegicus	176-192
1321133-16	1992	Dephosphorylation of pp160 was especially rapid with a t1/2 of approximately 10 s. The t1/2 for the insulin receptor was 37 s. Zn2+ at 1 mM (a concentration that inhibited the insulin receptor kinase) was a strong inhibitor of dephosphorylation, prolonging the rate of pp160 dephosphorylation more than 12-fold and insulin receptor dephosphorylation 3-fold.	Zinc	127-131	insulin receptor	Rattus norvegicus	176-192
1312964-0	1992	Effect of free fatty acids on insulin receptor binding and tyrosine kinase activity in hepatocytes isolated from lean and obese rats.	Fatty Acids, Nonesterified	10-26	insulin receptor	Rattus norvegicus	30-46
1616020-9	1992	It is concluded that testosterone administration in moderate doses to oophorectomized female rats is followed by a rapid deterioration of insulin sensitivity in muscle, mediated mainly by perturbations of the insulin receptor-glycogen synthesis systems apparently coinciding with changes in muscle morphology.	Testosterone	21-33	insulin receptor	Rattus norvegicus	209-225
1339020-2	1992	Insulin receptor activity was assessed by [125I]insulin binding, and basal as well as insulin stimulated kinase activity of the receptor, expressed as phosphorylation of the synthetic peptide poly (Glu-Tyr (4:1)).	poly (glu-tyr	192-205	insulin receptor	Rattus norvegicus	0-16
1374397-0	1992	Decrease in beta-subunit phosphotyrosine correlates with internalization and activation of the endosomal insulin receptor kinase.	Phosphotyrosine	25-40	insulin receptor	Rattus norvegicus	105-121
1374397-12	1992	Exogenous IR kinase activity (poly(Glu:Tyr)) in PM changed only slightly with insulin dose.	poly	30-34	insulin receptor	Rattus norvegicus	10-12
1374397-12	1992	Exogenous IR kinase activity (poly(Glu:Tyr)) in PM changed only slightly with insulin dose.	Glutamic Acid	35-38	insulin receptor	Rattus norvegicus	10-12
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
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
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.	Staurosporine	159-172	insulin receptor	Rattus norvegicus	238-254
1733252-2	1992	Insulin receptor autophosphorylation at a subsaturating ATP concentration (0.5 microM) increased by 10-fold from day 17 to 21 of gestation and decreased by 50% in term growth-retarded fetuses of fasted mothers.	Adenosine Triphosphate	56-59	insulin receptor	Rattus norvegicus	0-16
1572332-5	1992	Insulin receptor tyrosine kinase activity was also significantly decreased (52% of control values) under high-glucose/high-insulin conditions.	Glucose	110-117	insulin receptor	Rattus norvegicus	0-16
1572332-7	1992	High glucose and insulin levels thus result in down-regulation of fetal lung insulin receptors and insulin receptor tyrosine kinase activity late in gestation.	Glucose	5-12	insulin receptor	Rattus norvegicus	77-93
1625677-0	1992	Effects of phorbol esters on insulin receptor function and insulin action in hepatocytes: evidence for heterogeneity.	Phorbol Esters	11-25	insulin receptor	Rattus norvegicus	29-45
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
1309705-0	1992	Effect of glucagon on insulin receptor phosphorylation in intact liver cells.	Glucagon	10-18	insulin receptor	Rattus norvegicus	22-38
1916636-1	1991	Effect of 1,2-diacylglycerols on the insulin receptor function and insulin action in rat adipocytes was studied.	1,2-diacylglycerol	10-29	insulin receptor	Rattus norvegicus	37-53
1838992-3	1991	In streptozotocin-treated rats, insulin receptor number was increased by 25-40% in plasma membrane and total cellular membrane fractions, and by 60-130% in the light Golgi-endosomal (GE) fraction.	Streptozocin	3-17	insulin receptor	Rattus norvegicus	32-48
1657668-6	1991	Partially purified insulin receptor from rat fat cells, which were cultured under high-glucose conditions for 1 or 12 h, showed no alteration of insulin binding but a reduced insulin effect on autophosphorylation (30 +/- 7% of control) and poly(Glu80-Tyr20) phosphorylation (55.5 +/- 9% of control).	Glucose	87-94	insulin receptor	Rattus norvegicus	19-35
1657668-6	1991	Partially purified insulin receptor from rat fat cells, which were cultured under high-glucose conditions for 1 or 12 h, showed no alteration of insulin binding but a reduced insulin effect on autophosphorylation (30 +/- 7% of control) and poly(Glu80-Tyr20) phosphorylation (55.5 +/- 9% of control).	poly	240-244	insulin receptor	Rattus norvegicus	19-35
1339577-4	1992	It suggests that coumestrol effects the insulin receptor activity in this tissue and it could be a cause of glycogen deficiency.	Coumestrol	17-27	insulin receptor	Rattus norvegicus	40-56
1563542-5	1992	Chloroquine and quinacrine treatment also increases the insulin receptor content of endosomal fractions and, in rats injected by native insulin, the ligand-induced accumulation of receptors in endosomal fractions at late times after injection.	Chloroquine	0-11	insulin receptor	Rattus norvegicus	56-72
1563542-5	1992	Chloroquine and quinacrine treatment also increases the insulin receptor content of endosomal fractions and, in rats injected by native insulin, the ligand-induced accumulation of receptors in endosomal fractions at late times after injection.	Quinacrine	16-26	insulin receptor	Rattus norvegicus	56-72
1563542-6	1992	Subfractionation of endosomal fractions on Percoll gradients shows that chloroquine treatment shifts the distribution of both insulin and the insulin receptor towards higher densities, the receptor shift being slightly more pronounced in insulin-injected rats.	Chloroquine	72-83	insulin receptor	Rattus norvegicus	142-158
1722405-2	1991	In vivo, pertussis toxin (2 micrograms/ml/2h) inhibited insulin-stimulated tyrosyl autophosphorylation of the insulin receptor by 50% in FaO cells, and nearly completely inhibited phosphorylation of the cellular insulin receptor substrate pp185.	cyclo(tyrosyl-tyrosyl)	75-82	insulin receptor	Rattus norvegicus	110-126
1722405-3	1991	Similarly, insulin-stimulated autophosphorylation and kinase activity of the insulin receptor purified on wheat germ agglutinin-agarose from pertussis toxin-treated FaO cells was diminished 50%; however, treatment of cells with the catalytically inactive B-oligomer of the toxin had no effect on receptor tyrosine kinase activity in vitro.	Sepharose	128-135	insulin receptor	Rattus norvegicus	77-93
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).	Streptozocin	91-103	insulin receptor	Rattus norvegicus	0-16
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).	poly glutamic acid-tyrosine	191-218	insulin receptor	Rattus norvegicus	0-16
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).	Glutamic Acid	196-199	insulin receptor	Rattus norvegicus	0-16
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
1661694-8	1991	Under conditions of substrate inhibition (0.4 mg/ml H2B), insulin receptor H2B kinase activity from muscles of rats with severe diabetes (85 mg/kg STZ, 7 days) was significantly decreased, whereas the same activity from rats with moderate diabetes (50 mg/kg STZ, 7 days) was not significantly different from control rats.	Streptozocin	147-150	insulin receptor	Rattus norvegicus	58-74
1661694-8	1991	Under conditions of substrate inhibition (0.4 mg/ml H2B), insulin receptor H2B kinase activity from muscles of rats with severe diabetes (85 mg/kg STZ, 7 days) was significantly decreased, whereas the same activity from rats with moderate diabetes (50 mg/kg STZ, 7 days) was not significantly different from control rats.	Streptozocin	258-261	insulin receptor	Rattus norvegicus	58-74
1818950-0	1991	Insulin receptor concentration and gene expression are modulated by sodium intake in the rat kidney.	Sodium	68-74	insulin receptor	Rattus norvegicus	0-16
1778660-5	1991	The decrease in the ability of insulin to either stimulate glucose transport or inhibit catecholamine induced lipolysis in SC cells was associated with a decrease in insulin receptor autophosphorylation and receptor tyrosine kinase activity.	Catecholamines	88-101	insulin receptor	Rattus norvegicus	166-182
2051228-0	1991	High sucrose diet and exercise: effects on insulin-receptor function of 12- and 24-mo-old Sprague-Dawley rats.	Sucrose	5-12	insulin receptor	Rattus norvegicus	43-59
2051228-5	1991	Insulin-receptor number was significantly decreased in 24-mo-old sucrose-fed rats compared to 12-mo-old rats fed the sucrose or sucrose-free diets.	Sucrose	65-72	insulin receptor	Rattus norvegicus	0-16
2051228-5	1991	Insulin-receptor number was significantly decreased in 24-mo-old sucrose-fed rats compared to 12-mo-old rats fed the sucrose or sucrose-free diets.	Sucrose	117-124	insulin receptor	Rattus norvegicus	0-16
2051228-5	1991	Insulin-receptor number was significantly decreased in 24-mo-old sucrose-fed rats compared to 12-mo-old rats fed the sucrose or sucrose-free diets.	Sucrose	117-124	insulin receptor	Rattus norvegicus	0-16
1916636-2	1991	1,2-dioctanoylglycerol (100 micrograms/ml) did not alter insulin binding but it did stimulate phosphorylation of the beta-subunit of the insulin receptor as well as its tyrosine kinase activity.	1,2-dioctanoylglycerol	0-22	insulin receptor	Rattus norvegicus	137-153
1849899-1	1991	In this study, we found that adding iodoacetamide to the homogenization buffer used in the preparation of mouse or rat liver plasma membranes resulted in an increase of insulin receptor autophosphorylation by 4-5-fold and receptor kinase activity by about 2-fold.	Iodoacetamide	36-49	insulin receptor	Rattus norvegicus	169-185
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
2026614-7	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.	Phenylalanine	213-227	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
1816977-0	1991	Dephosphorylation of the insulin receptor partially restores the decreased autophosphorylation in streptozotocin induced diabetic rats.	Streptozocin	98-112	insulin receptor	Rattus norvegicus	25-41
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).	Serine	50-56	insulin receptor	Rattus norvegicus	90-106
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).	Threonine	64-73	insulin receptor	Rattus norvegicus	90-106
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
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).	Streptozocin	150-164	insulin receptor	Rattus norvegicus	90-106
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).	Streptozocin	188-191	insulin receptor	Rattus norvegicus	90-106
1816977-4	1991	Both basal and insulin-stimulated autophosphorylations of the insulin receptor from STZ-D rats were significantly impaired to those from normal rats.	Streptozocin	84-87	insulin receptor	Rattus norvegicus	62-78
1816977-5	1991	Dephosphorylation of the insulin receptor by alkaline phosphatase resulted in an increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats (43 +/- 13% to 66 +/- 14%, P less than 0.05), but not from normal rats (100% to 109 +/- 12%, NS).	Streptozocin	161-164	insulin receptor	Rattus norvegicus	25-41
1816977-5	1991	Dephosphorylation of the insulin receptor by alkaline phosphatase resulted in an increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats (43 +/- 13% to 66 +/- 14%, P less than 0.05), but not from normal rats (100% to 109 +/- 12%, NS).	Streptozocin	161-164	insulin receptor	Rattus norvegicus	139-155
1816977-5	1991	Dephosphorylation of the insulin receptor by alkaline phosphatase resulted in an increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats (43 +/- 13% to 66 +/- 14%, P less than 0.05), but not from normal rats (100% to 109 +/- 12%, NS).	Nitrogen	265-267	insulin receptor	Rattus norvegicus	25-41
1816977-5	1991	Dephosphorylation of the insulin receptor by alkaline phosphatase resulted in an increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats (43 +/- 13% to 66 +/- 14%, P less than 0.05), but not from normal rats (100% to 109 +/- 12%, NS).	Nitrogen	265-267	insulin receptor	Rattus norvegicus	139-155
1816977-6	1991	Although maximal autophosphorylation of the dephosphorylated insulin receptor was still lower in STZ-D rats than in normal rats, the increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats by dephosphorylation was higher than that from normal (159.2 +/- 27.2% vs 108.0 +/- 12.4%, p less than 0.01), supporting the idea that the residues of the insulin receptor of STZ-D rats was highly phosphorylated.	Streptozocin	97-100	insulin receptor	Rattus norvegicus	61-77
1816977-6	1991	Although maximal autophosphorylation of the dephosphorylated insulin receptor was still lower in STZ-D rats than in normal rats, the increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats by dephosphorylation was higher than that from normal (159.2 +/- 27.2% vs 108.0 +/- 12.4%, p less than 0.01), supporting the idea that the residues of the insulin receptor of STZ-D rats was highly phosphorylated.	Streptozocin	213-216	insulin receptor	Rattus norvegicus	191-207
1816977-6	1991	Although maximal autophosphorylation of the dephosphorylated insulin receptor was still lower in STZ-D rats than in normal rats, the increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats by dephosphorylation was higher than that from normal (159.2 +/- 27.2% vs 108.0 +/- 12.4%, p less than 0.01), supporting the idea that the residues of the insulin receptor of STZ-D rats was highly phosphorylated.	Streptozocin	213-216	insulin receptor	Rattus norvegicus	191-207
1816977-6	1991	Although maximal autophosphorylation of the dephosphorylated insulin receptor was still lower in STZ-D rats than in normal rats, the increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats by dephosphorylation was higher than that from normal (159.2 +/- 27.2% vs 108.0 +/- 12.4%, p less than 0.01), supporting the idea that the residues of the insulin receptor of STZ-D rats was highly phosphorylated.	Streptozocin	213-216	insulin receptor	Rattus norvegicus	191-207
1816977-6	1991	Although maximal autophosphorylation of the dephosphorylated insulin receptor was still lower in STZ-D rats than in normal rats, the increase in insulin-stimulated autophosphorylation of the insulin receptor from STZ-D rats by dephosphorylation was higher than that from normal (159.2 +/- 27.2% vs 108.0 +/- 12.4%, p less than 0.01), supporting the idea that the residues of the insulin receptor of STZ-D rats was highly phosphorylated.	Streptozocin	213-216	insulin receptor	Rattus norvegicus	191-207
1849899-4	1991	The enhancing effect of iodoacetamide on insulin receptor autophosphorylation was the result of a more than 2-fold decrease in the Km and a more than 3-fold increase in Vmax for ATP.	Iodoacetamide	24-37	insulin receptor	Rattus norvegicus	41-57
1849899-4	1991	The enhancing effect of iodoacetamide on insulin receptor autophosphorylation was the result of a more than 2-fold decrease in the Km and a more than 3-fold increase in Vmax for ATP.	Adenosine Triphosphate	178-181	insulin receptor	Rattus norvegicus	41-57
1849899-5	1991	The presence of iodoacetamide in the preparation of plasma membranes also greatly increased the solubilization of the insulin receptor from the plasma membrane by Triton X-100.	Iodoacetamide	16-29	insulin receptor	Rattus norvegicus	118-134
1849899-5	1991	The presence of iodoacetamide in the preparation of plasma membranes also greatly increased the solubilization of the insulin receptor from the plasma membrane by Triton X-100.	Octoxynol	163-175	insulin receptor	Rattus norvegicus	118-134
1849899-6	1991	We propose that iodoacetamide acts to alkylate some unknown thiols released during tissue homogenization and that in its absence these thiols formed mixed disulfides with the insulin receptor, thus adversely affecting the process of receptor activation by insulin.	Sulfhydryl Compounds	135-141	insulin receptor	Rattus norvegicus	175-191
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
1720228-2	1991	In addition, a recent investigation showed that there is a good correlation between the presence of the insulin receptor and phosphotyrosine-containing proteins in these regions, indicating a possible functional activity of insulin receptors in vivo.	Phosphotyrosine	125-140	insulin receptor	Rattus norvegicus	104-120
1846101-1	1991	Insulin receptor tyrosine kinase activity solubilized from liver of control and streptozotocin diabetic rats was studied using histone H2b and poly-Glu-Tyr (4:1) as phosphoacceptors.	Streptozocin	80-94	insulin receptor	Rattus norvegicus	0-16
1846101-1	1991	Insulin receptor tyrosine kinase activity solubilized from liver of control and streptozotocin diabetic rats was studied using histone H2b and poly-Glu-Tyr (4:1) as phosphoacceptors.	poly-glu-tyr	143-155	insulin receptor	Rattus norvegicus	0-16
1846101-6	1991	Insulin receptor kinase activity toward the substrate poly-Glu-Tyr (4:1) was unaltered by insulinopenic diabetes.	poly-glu-tyr	54-66	insulin receptor	Rattus norvegicus	0-16
2256908-1	1990	Indomethacin inhibits autophosphorylation of the insulin receptor.	Indomethacin	0-12	insulin receptor	Rattus norvegicus	49-65
2249624-6	1990	Binding studies at 15 C in the presence of potassium cyanide revealed that this effect was associated with an increase in insulin receptor affinity.	Potassium Cyanide	43-60	insulin receptor	Rattus norvegicus	122-138
2249624-13	1990	We conclude that 1) low concentrations of vanadate (less than 200 microM) increase insulin receptor affinity and consequent insulin uptake in rat adipocytes; 2) the excess cell-associated insulin exists largely as intact hormone; and 3) the increased binding at low insulin concentrations results in an apparent increase in insulin sensitivity.	Vanadates	42-50	insulin receptor	Rattus norvegicus	83-99
1701386-2	1990	(a) Polylysine stimulated both tyrosine and serine phosphorylation of the insulin receptor and of additional proteins present in lectin-purified membrane preparations from rat liver.	Polylysine	4-14	insulin receptor	Rattus norvegicus	74-90
1701386-2	1990	(a) Polylysine stimulated both tyrosine and serine phosphorylation of the insulin receptor and of additional proteins present in lectin-purified membrane preparations from rat liver.	Serine	44-50	insulin receptor	Rattus norvegicus	74-90
1701386-3	1990	(b) Polylysine synergized with insulin to enhance phosphorylation of the insulin receptor and of additional proteins (pp40 and pp110).	Polylysine	4-14	insulin receptor	Rattus norvegicus	73-89
1701386-8	1990	The same effects of polylysine were obtained with highly purified insulin receptor preparations.	Polylysine	20-30	insulin receptor	Rattus norvegicus	66-82
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.	Polylysine	23-33	insulin receptor	Rattus norvegicus	91-107
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.	Polylysine	23-33	insulin receptor	Rattus norvegicus	167-183
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.	Polylysine	23-33	insulin receptor	Rattus norvegicus	167-183
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
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.	Polylysine	125-135	insulin receptor	Rattus norvegicus	91-107
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.	Polylysine	125-135	insulin receptor	Rattus norvegicus	167-183
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.	Polylysine	125-135	insulin receptor	Rattus norvegicus	167-183
2249648-1	1990	Insulin receptor mRNA was demonstrated in rat brain slices by in situ hybridization with three 35S-oligonucleotide probes and contact film autoradiography.	35s-oligonucleotide	95-114	insulin receptor	Rattus norvegicus	0-16
2222423-4	1990	In contrast, affinity cross-linking of membranes prepared with iodoacetamide (IAN) or N-ethylmaleimide identified predominantly the alpha 2 beta 2 heterotetrameric insulin receptor complex.	Iodoacetamide	63-76	insulin receptor	Rattus norvegicus	164-180
2282071-1	1990	Insulin receptor activity and its relationship with catecholamines and serotonin were investigated in rat whole brain membranes, synaptosomes and choroid plexus in alloxan induced short term and long term hyperglycemia and hyperinsulinemia.	Catecholamines	52-66	insulin receptor	Rattus norvegicus	0-16
2220947-3	1990	Long-term glucose infusions to maternal rats resulted in maternal and fetal hyperglycemia and mild hyperinsulinemia, which decreases the liver insulin receptor abundance of the mother but increased that of the fetus.	Glucose	10-17	insulin receptor	Rattus norvegicus	143-159
2282071-3	1990	While choroid plexus insulin receptors modulate along with norepinephrine, dopamine and serotonin with the changes in insulin and/or plasma glucose levels, insulin receptor activity in synaptosomes and total membranes is not affected to a great extent except in long term hyperglycemia.	Dopamine	75-83	insulin receptor	Rattus norvegicus	21-37
2222423-4	1990	In contrast, affinity cross-linking of membranes prepared with iodoacetamide (IAN) or N-ethylmaleimide identified predominantly the alpha 2 beta 2 heterotetrameric insulin receptor complex.	Ethylmaleimide	86-102	insulin receptor	Rattus norvegicus	164-180
2282071-3	1990	While choroid plexus insulin receptors modulate along with norepinephrine, dopamine and serotonin with the changes in insulin and/or plasma glucose levels, insulin receptor activity in synaptosomes and total membranes is not affected to a great extent except in long term hyperglycemia.	Serotonin	88-97	insulin receptor	Rattus norvegicus	21-37
2282071-3	1990	While choroid plexus insulin receptors modulate along with norepinephrine, dopamine and serotonin with the changes in insulin and/or plasma glucose levels, insulin receptor activity in synaptosomes and total membranes is not affected to a great extent except in long term hyperglycemia.	Glucose	140-147	insulin receptor	Rattus norvegicus	21-37
2282079-2	1990	Loss of insulin receptor activity is linear with cellular ageing and norepinephrine and epinephrine levels increase with age together with levels of glycosylated hemoglobin in control animals and this correlation is altered in hyperglycemia and hyperinsulinemia.	Norepinephrine	69-83	insulin receptor	Rattus norvegicus	8-24
2282071-1	1990	Insulin receptor activity and its relationship with catecholamines and serotonin were investigated in rat whole brain membranes, synaptosomes and choroid plexus in alloxan induced short term and long term hyperglycemia and hyperinsulinemia.	Serotonin	71-80	insulin receptor	Rattus norvegicus	0-16
2282071-2	1990	Insulin receptor activity was measured by [125I]insulin binding and catecholamines by high performance liquid chromatography with electrochemical detection.	Catecholamines	68-82	insulin receptor	Rattus norvegicus	0-16
2118351-0	1990	Modulation of guanine nucleotide effects on the insulin receptor by MgCl2.	Guanine Nucleotides	14-32	insulin receptor	Rattus norvegicus	48-64
2119296-2	1990	Digestion of the receptor from IM-9 lymphocytes with E. freundii endo-beta-galactosidase increased the migration of the insulin receptor alpha- and beta-subunits on sodium dodecyl sulfate-polyacrylamide gels and sharpened the electrophoretic bands; the alpha-subunit was converted from an apparent mol wt (Mr) of 123,000 to a Mr of 118,000, and the beta-subunit from a Mr of 92,000 to 89,000.	Sodium Dodecyl Sulfate	165-187	insulin receptor	Rattus norvegicus	120-136
2119296-2	1990	Digestion of the receptor from IM-9 lymphocytes with E. freundii endo-beta-galactosidase increased the migration of the insulin receptor alpha- and beta-subunits on sodium dodecyl sulfate-polyacrylamide gels and sharpened the electrophoretic bands; the alpha-subunit was converted from an apparent mol wt (Mr) of 123,000 to a Mr of 118,000, and the beta-subunit from a Mr of 92,000 to 89,000.	polyacrylamide	188-202	insulin receptor	Rattus norvegicus	120-136
2119296-4	1990	Affinity chromatography of receptor glycopeptides on Concanavalin-A-Sepharose revealed that the poly-N-acetyllactosamine units were attached to multiantennary glycopeptides that accounted for over 75% of the [3H]glucosamine incorporated into the IM-9 lymphocyte insulin receptor; the remaining radioactivity was present in polymannose units (primarily Man8GlcNAc2) and biantennary complex saccharides.	poly-N-acetyllactosamine	96-120	insulin receptor	Rattus norvegicus	262-278
2119296-5	1990	Several differences in the carbohydrate chains of the insulin receptor from the Fao and IM-9 cells indicated that glycosylation was cell specific despite the occurrence of poly-N-acetyllactosamine chains in both cell types.	Carbohydrates	27-39	insulin receptor	Rattus norvegicus	54-70
2269579-6	1990	With increasing palmitate concentration, a dose-dependent decline in cell-surface insulin receptor binding was observed.	Palmitates	16-25	insulin receptor	Rattus norvegicus	82-98
2269579-11	1990	This decrease was proportional to the reduction in cell-surface insulin receptor density at palmitate concentrations of 0.05-0.5 mM, but was disproportionally greater at higher fatty acid concentrations.	Palmitates	92-101	insulin receptor	Rattus norvegicus	64-80
2269579-11	1990	This decrease was proportional to the reduction in cell-surface insulin receptor density at palmitate concentrations of 0.05-0.5 mM, but was disproportionally greater at higher fatty acid concentrations.	Fatty Acids	177-187	insulin receptor	Rattus norvegicus	64-80
2169240-0	1990	Insulin receptor function is inhibited by guanosine 5"-[gamma-thio]triphosphate (GTP[S]).	Guanosine 5'-O-(3-Thiotriphosphate)	42-79	insulin receptor	Rattus norvegicus	0-16
2169240-0	1990	Insulin receptor function is inhibited by guanosine 5"-[gamma-thio]triphosphate (GTP[S]).	Guanosine Triphosphate	81-84	insulin receptor	Rattus norvegicus	0-16
2169240-1	1990	The regulatory role of GTP-binding proteins (G-proteins) in insulin receptor function was investigated using isolated insulin receptors and plasma membranes from rat adipocytes.	Guanosine Triphosphate	23-26	insulin receptor	Rattus norvegicus	60-76
2169240-3	1990	Phosphorylation of calmodulin by the insulin receptor kinase was also inhibited by 1 mM-GTP[S] both in the absence (by 88%) and in the presence (by 81%) of insulin.	Guanosine Triphosphate	87-91	insulin receptor	Rattus norvegicus	37-53
2169240-10	1990	These results indicate that GTP inhibits insulin receptor function, but does so through a mechanism that does not require a conventional GTP-binding protein.	Guanosine Triphosphate	28-31	insulin receptor	Rattus norvegicus	41-57
2169240-10	1990	These results indicate that GTP inhibits insulin receptor function, but does so through a mechanism that does not require a conventional GTP-binding protein.	Guanosine Triphosphate	137-140	insulin receptor	Rattus norvegicus	41-57
1697468-1	1990	A Mn2(+)-dependent serine/threonine protein kinase from rat liver membranes copurifies with the insulin receptor (IR) on wheat germ agglutinin (WGA)-sepharose.	Sepharose	149-158	insulin receptor	Rattus norvegicus	96-112
1697468-1	1990	A Mn2(+)-dependent serine/threonine protein kinase from rat liver membranes copurifies with the insulin receptor (IR) on wheat germ agglutinin (WGA)-sepharose.	Sepharose	149-158	insulin receptor	Rattus norvegicus	114-116
2118351-0	1990	Modulation of guanine nucleotide effects on the insulin receptor by MgCl2.	Magnesium Chloride	68-73	insulin receptor	Rattus norvegicus	48-64
2354998-1	1990	Phosphorylation of the insulin receptor beta-subunit on serine/threonine residues by protein kinase C reduces both receptor kinase activity and insulin action in cultured cells.	Serine	56-62	insulin receptor	Rattus norvegicus	23-39
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.	ethyl N-alpha-acetyl-tyrosinate	22-26	insulin receptor	Rattus norvegicus	89-105
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
2200529-10	1990	A major ATEE site is very close to phosphorylation of the beta-subunit of the insulin receptor.	ethyl N-alpha-acetyl-tyrosinate	8-12	insulin receptor	Rattus norvegicus	78-94
2164785-0	1990	Effect of a high-fat-sucrose diet on in vivo insulin receptor kinase activation.	Sucrose	21-28	insulin receptor	Rattus norvegicus	45-61
2164785-5	1990	In control rats insulin receptor kinase activity was maximally stimulated threefold in liver at 5 min and fourfold in muscle at 15 min after insulin-glucose injection.	insulin-glucose	141-156	insulin receptor	Rattus norvegicus	16-32
2354998-1	1990	Phosphorylation of the insulin receptor beta-subunit on serine/threonine residues by protein kinase C reduces both receptor kinase activity and insulin action in cultured cells.	Threonine	63-72	insulin receptor	Rattus norvegicus	23-39
2354998-9	1990	These findings suggest that in starved, insulin-resistant animals, an increase in hepatic protein kinase C activity is associated with increased Ser/Thr phosphorylation which in turn decreases autophosphorylation and function of the insulin receptor kinase.	Serine	145-148	insulin receptor	Rattus norvegicus	233-249
2354998-9	1990	These findings suggest that in starved, insulin-resistant animals, an increase in hepatic protein kinase C activity is associated with increased Ser/Thr phosphorylation which in turn decreases autophosphorylation and function of the insulin receptor kinase.	Threonine	149-152	insulin receptor	Rattus norvegicus	233-249
2162756-6	1990	Potential sites of action of metformin are the insulin receptor and the glucose transporters.	Metformin	29-38	insulin receptor	Rattus norvegicus	47-63
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
2189597-6	1990	In contrast, both sequential and CDMO treatments prevented the insulin receptor alterations induced by the CD diet.	cdmo	33-37	insulin receptor	Rattus norvegicus	63-79
2189597-6	1990	In contrast, both sequential and CDMO treatments prevented the insulin receptor alterations induced by the CD diet.	Cadmium	33-35	insulin receptor	Rattus norvegicus	63-79
2189597-7	1990	These data demonstrate that the CD diet-induced insulin receptor alterations occur concurrently with the induction of ODC activity.	Cadmium	32-34	insulin receptor	Rattus norvegicus	48-64
2189597-8	1990	But insulin receptor changes and the increased ODC activity are affected differently by CDMO treatment, suggesting that their induction by the CD diet is through distinct mechanisms and only the receptor alterations correspond with the tumor-promoting action of CD diet regimen.	Cadmium	88-90	insulin receptor	Rattus norvegicus	4-20
1693770-0	1990	Location of phosphotyrosine-containing proteins by immunocytochemistry in the rat forebrain corresponds to the distribution of the insulin receptor.	Phosphotyrosine	12-27	insulin receptor	Rattus norvegicus	131-147
1693770-9	1990	Importantly, the distribution of the areas positive for phosphotyrosine agreed to a remarkable extent with the distribution of the brain insulin receptor, which itself has tyrosine kinase activity.	Phosphotyrosine	56-71	insulin receptor	Rattus norvegicus	137-153
1693770-10	1990	These findings suggest a relationship between the insulin receptor and the increased phosphotyrosine content of these neurons and support the concept that the brain insulin receptor is active in vivo.	Phosphotyrosine	85-100	insulin receptor	Rattus norvegicus	50-66
1693770-10	1990	These findings suggest a relationship between the insulin receptor and the increased phosphotyrosine content of these neurons and support the concept that the brain insulin receptor is active in vivo.	Phosphotyrosine	85-100	insulin receptor	Rattus norvegicus	165-181
1966886-3	1990	In this study, similar defects in insulin receptor of aortic endothelial cells cultured from diabetic BB rats were found.	boeravinone B	102-104	insulin receptor	Rattus norvegicus	34-50
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
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
1966886-7	1990	Insulin-induced tyrosine kinase activity of partially purified insulin receptor measured using poly-glutyr as substrate was also lower in cells from diabetic rats (normal:1.4 +/- 0.6-fold; diabetic 0.5 +/- 0.3-fold above baseline; (p less than 0.05).	poly-glutyr	95-106	insulin receptor	Rattus norvegicus	63-79
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
2180315-4	1990	In wheat germ agglutinin purified receptors, 125I-labeled porcine insulin binding, basal and insulin-stimulated insulin receptor kinase activities for both the autophosphorylation of the beta-subunit and the phosphorylation of the artificial substrate poly (Glu-Tyr) 4:1, were found identical in diabetic and control rats, treated or not with vanadate.	Iodine-125	45-49	insulin receptor	Rattus norvegicus	112-128
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
2180315-4	1990	In wheat germ agglutinin purified receptors, 125I-labeled porcine insulin binding, basal and insulin-stimulated insulin receptor kinase activities for both the autophosphorylation of the beta-subunit and the phosphorylation of the artificial substrate poly (Glu-Tyr) 4:1, were found identical in diabetic and control rats, treated or not with vanadate.	poly (glu-tyr) 4	252-268	insulin receptor	Rattus norvegicus	112-128
2180315-4	1990	In wheat germ agglutinin purified receptors, 125I-labeled porcine insulin binding, basal and insulin-stimulated insulin receptor kinase activities for both the autophosphorylation of the beta-subunit and the phosphorylation of the artificial substrate poly (Glu-Tyr) 4:1, were found identical in diabetic and control rats, treated or not with vanadate.	Vanadates	343-351	insulin receptor	Rattus norvegicus	112-128
2180315-6	1990	Thus, in that model of non-insulin-dependent diabetes, 1) oral vanadate exerts a corrective insulin-like effect on impaired insulin action both at the level of liver and peripheral tissues, 2) impaired insulin action with no alteration of the insulin receptor tyrosine kinase is observed in the liver of untreated rats, and 3) corrective effect of vanadate on liver glucose metabolism is probably distal to the insulin receptor kinase activity.	Vanadates	63-71	insulin receptor	Rattus norvegicus	411-427
2262933-14	1990	The data suggests that (i) fundamental differences exist between the receptor state in intact cells and isolated plasma membranes and (ii) that a disulphide-rich region within the insulin receptor, other than the previously reported class I and class II disulphide bridges, is critical for insulin binding and cellular response.	disulphide	146-156	insulin receptor	Rattus norvegicus	180-196
2154464-15	1990	The insulin receptor kinase is a likely candidate as its activity is markedly enhanced either by insulin (plus H2O2) or by H2O2/vanadate.	Hydrogen Peroxide	111-115	insulin receptor	Rattus norvegicus	4-20
2154464-15	1990	The insulin receptor kinase is a likely candidate as its activity is markedly enhanced either by insulin (plus H2O2) or by H2O2/vanadate.	Hydrogen Peroxide	123-127	insulin receptor	Rattus norvegicus	4-20
2154464-15	1990	The insulin receptor kinase is a likely candidate as its activity is markedly enhanced either by insulin (plus H2O2) or by H2O2/vanadate.	Vanadates	128-136	insulin receptor	Rattus norvegicus	4-20
2153971-7	1990	The effects of this agent reveal a striking difference in insulin receptor-mediated stimulation of glucose transport between 3T3-L1 fatty fibroblasts and the mature rat adipocyte.	Glucose	99-106	insulin receptor	Rattus norvegicus	58-74
2153102-3	1990	In the presence of insulin, selenate enhances insulin receptor kinase activity and phosphorylations of insulin-stimulated tyrosyl phosphoproteins.	Selenic Acid	28-36	insulin receptor	Rattus norvegicus	46-62
2158467-1	1990	We have studied autophosphorylation and tyrosine kinase activity of the insulin receptor purified from liver and muscle of fasted rats before and after infusion of insulin (100 mU/h) during a 2.5 h glucose clamp.	Glucose	198-205	insulin receptor	Rattus norvegicus	72-88
2158467-3	1990	Autophosphorylation of the insulin receptor beta subunit was increased in liver receptors prepared from rats at the end of the glucose clamp compared to rats in the basal state both in the absence of insulin in vitro (109% increase, p less than 0.001) and after in vitro stimulation with 10(-7) mol/l insulin (clamped vs fasted; 96% increase, p less than 0.001).	Glucose	127-134	insulin receptor	Rattus norvegicus	27-43
2196058-1	1990	Insulin receptor activity and its relationship with catecholamines and serotonin were investigated in rat brain using Triton X-100 extracts from total membranes, synaptosomes and choroid plexus in experimental hypothyroidism and hyperthyroidism.	Catecholamines	52-66	insulin receptor	Rattus norvegicus	0-16
2196058-1	1990	Insulin receptor activity and its relationship with catecholamines and serotonin were investigated in rat brain using Triton X-100 extracts from total membranes, synaptosomes and choroid plexus in experimental hypothyroidism and hyperthyroidism.	Serotonin	71-80	insulin receptor	Rattus norvegicus	0-16
2196058-1	1990	Insulin receptor activity and its relationship with catecholamines and serotonin were investigated in rat brain using Triton X-100 extracts from total membranes, synaptosomes and choroid plexus in experimental hypothyroidism and hyperthyroidism.	Octoxynol	118-130	insulin receptor	Rattus norvegicus	0-16
2196058-2	1990	Insulin receptor activity was assessed by binding to [125I]insulin and catecholamines by high performance liquid chromatography.	Catecholamines	71-85	insulin receptor	Rattus norvegicus	0-16
2201297-1	1990	Insulin receptor activity and its relationship with catecholamines in rat young, middle aged and old red blood cells were investigated in experimental hypothyroidism and hyperthyroidism.	Catecholamines	52-66	insulin receptor	Rattus norvegicus	0-16
2201297-2	1990	In control animals, a loss of insulin receptor activity was found with cellular ageing and increased levels of norepinephrine, epinephrine and glycosylated hemoglobin.	Norepinephrine	111-125	insulin receptor	Rattus norvegicus	30-46
2201297-2	1990	In control animals, a loss of insulin receptor activity was found with cellular ageing and increased levels of norepinephrine, epinephrine and glycosylated hemoglobin.	Epinephrine	114-125	insulin receptor	Rattus norvegicus	30-46
2201297-4	1990	These results suggest that loss of insulin receptor in cellular ageing is probably part of a more generalised alteration and rat serves as an excellent model in defining the role of thyroid hormones in carbohydrate tolerance.	Carbohydrates	202-214	insulin receptor	Rattus norvegicus	35-51
2404022-9	1990	Polyethylene glycol (PEG) precipitation of insulin-receptor complexes revealed that endosomal degradation augmented the dissociation of insulin from its receptor and that dissociated insulin was serving as substrate to the endosomal protease(s).	Polyethylene Glycols	0-19	insulin receptor	Rattus norvegicus	43-59
2404022-9	1990	Polyethylene glycol (PEG) precipitation of insulin-receptor complexes revealed that endosomal degradation augmented the dissociation of insulin from its receptor and that dissociated insulin was serving as substrate to the endosomal protease(s).	Polyethylene Glycols	21-24	insulin receptor	Rattus norvegicus	43-59
34836374-6	2021	In addition, EGCG+LTA inhibited the expression of liver kinase B1, insulin receptor and insulin receptor substrate, and promoted the phosphorylation level of acetyl-CoA carboxylase.	epigallocatechin gallate	13-17	insulin receptor	Rattus norvegicus	67-83
34946771-10	2021	Stevioside effectively inhibits oxidative stress and promotes glucose uptake in diabetic gastrocnemius muscles by activating IR/IRS-1/Akt/GLUT 4 pathway.	stevioside	0-10	insulin receptor	Rattus norvegicus	125-127
34537857-4	2021	Diabetes was induced preconceptionally via doxycycline-induced knock down of the insulin receptor in transgenic rats.	Doxycycline	43-54	insulin receptor	Rattus norvegicus	81-97
33907035-4	2021	Insulin and the insulin receptor inhibitor S961 were intranasally administered to investigate the regulatory effects of insulin signaling on Sirtuin 1.	3-(n-boc-aminomethyl)azetidine	43-47	insulin receptor	Rattus norvegicus	16-32
33907035-6	2021	Conversely, S961 administration resulted in more severe cognitive dysfunction and reduced the expression levels of phosphorylated insulin receptor, phosphorylated insulin receptor substrate 1, and Sirtuin 1.	3-(n-boc-aminomethyl)azetidine	12-16	insulin receptor	Rattus norvegicus	130-146
34946771-0	2021	Stevioside Attenuates Insulin Resistance in Skeletal Muscle by Facilitating IR/IRS-1/Akt/GLUT 4 Signaling Pathways: An In Vivo and In Silico Approach.	stevioside	0-10	insulin receptor	Rattus norvegicus	76-78
34946771-7	2021	In diabetic gastrocnemius muscles, Setvioside normalized the altered levels of lipid peroxidase (LPO), hydrogen peroxide (H2O2) and hydroxyl radical (OH*), antioxidant enzymes (CAT, SOD, GPx and GSH) and molecules of insulin signaling including insulin receptor (IR), insulin receptor substrate-1 (IRS-1) and Akt mRNA levels.	setvioside	35-45	insulin receptor	Rattus norvegicus	245-261
34946771-7	2021	In diabetic gastrocnemius muscles, Setvioside normalized the altered levels of lipid peroxidase (LPO), hydrogen peroxide (H2O2) and hydroxyl radical (OH*), antioxidant enzymes (CAT, SOD, GPx and GSH) and molecules of insulin signaling including insulin receptor (IR), insulin receptor substrate-1 (IRS-1) and Akt mRNA levels.	setvioside	35-45	insulin receptor	Rattus norvegicus	263-265
34836374-6	2021	In addition, EGCG+LTA inhibited the expression of liver kinase B1, insulin receptor and insulin receptor substrate, and promoted the phosphorylation level of acetyl-CoA carboxylase.	theanine	18-21	insulin receptor	Rattus norvegicus	67-83
34566639-10	2021	In adipose tissue, domperidone reverted dopamine- and bromocriptine-mediated potentiation of insulin-induced glucose uptake, but in turn increased the insulin receptor, Akt, AMPK, HSL, ACC, and ACL, phosphorylation.	Domperidone	19-30	insulin receptor	Rattus norvegicus	151-167
34727320-8	2021	mRNA levels of BDNF, PSD95, SIRT1, GLUT4, insulin receptor, and ZnT3 were found to be reduced by icv-STZ and reestablished by zinc supplementation.	Streptozocin	101-104	insulin receptor	Rattus norvegicus	42-58
34302794-10	2021	Moreover, we show that stimulation of the insulin receptor activates cyclic AMP response element (CRE)-controlled transcription, involving the transcription factor CREB.	Cyclic AMP	69-79	insulin receptor	Rattus norvegicus	42-58
34484117-6	2021	Metformin significantly decreased the risk of body weight gain and increased INSR expression in F1 female offspring in PCOS-IR rats, contributing to the improvement in obesity, hyperinsulinemia, and IR.	Metformin	0-9	insulin receptor	Rattus norvegicus	77-81
34432988-3	2021	The study aimed to evaluate the effect of Genistein and Momordica charantia L. fruit on oxidative stress, markers of inflammation, and their role on proglucagon and insulin receptor mRNA expression by RT-PCR in diabetic rats.	Genistein	42-51	insulin receptor	Rattus norvegicus	165-181
34432988-9	2021	Treatment with MCF and Genistein significant increased the expression of proglucagon mRNA in the small intestine and insulin receptor mRNA in the liver of diabetic rats.	Genistein	23-32	insulin receptor	Rattus norvegicus	117-133
34432988-10	2021	In conclusion, MCF and Genistein ameliorate type 2 diabetes complications by preventing the loss of insulin-positive cells, inhibiting IL-1beta and TNFalpha and up-regulating proglucagon and insulin receptor mRNA expression.	Genistein	23-32	insulin receptor	Rattus norvegicus	191-207
34177815-9	2021	Similarly, only in HFD-exposed male from nicotine-administered dams showed decreases in the insulin receptor expression in the liver.	Nicotine	41-49	insulin receptor	Rattus norvegicus	92-108
34394002-7	2021	Insulin receptor downstream MPAK/ERK signaling was involved in the protection of miR-344-5p against cholesterol-induced pancreatic beta-cell dysfunction.	mir-344-5p	81-91	insulin receptor	Rattus norvegicus	0-16
34394002-7	2021	Insulin receptor downstream MPAK/ERK signaling was involved in the protection of miR-344-5p against cholesterol-induced pancreatic beta-cell dysfunction.	Cholesterol	100-111	insulin receptor	Rattus norvegicus	0-16
34394002-8	2021	Moreover, miR-344-5p directly targeted Cav1; Cav1 silencing could partially reverse the functions of miR-344-5p inhibition upon cholesterol-induced beta-cell dysfunction, beta-cell apoptosis, the apoptotic caspase 3/Bax signaling, and insulin receptor downstream MPAK/ERK signaling.	mir-344-5p	10-20	insulin receptor	Rattus norvegicus	235-251
34209137-8	2021	These findings suggest that DPIN might be a candidate to treat brain insulin-resistance associated disorders by activating insulin response beyond the insulin receptor.	Diphenyliodonium nitrate	28-32	insulin receptor	Rattus norvegicus	151-167
34065446-0	2021	The Insulin Receptor: A Potential Target of Amarogentin Isolated from Gentiana rigescens Franch That Induces Neurogenesis in PC12 Cells.	amarogentin	44-55	insulin receptor	Rattus norvegicus	4-20
34149862-2	2021	This study aims to investigate whether the brain IR/IRS-1 signaling pathway is involved in the therapeutic effect of ZJJ on depression-like behavior in diabetic rats.	3,3-difluorocyclobutyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate	117-120	insulin receptor	Rattus norvegicus	49-51
34149862-12	2021	Furthermore, we found the upregulation of protein expression of phospho-IR, phospho-IRS-1, phospho-PI3K, and phospho-AKT in the hippocampus of diabetic rats after being treated with ZJJ.	3,3-difluorocyclobutyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate	182-185	insulin receptor	Rattus norvegicus	72-74
34149862-15	2021	Conclusions: These findings suggest that ZJJ improves the depression-like behavior of diabetic rats by activating the IR/IRS-1 signaling pathway in both hippocampal neuron and astrocyte.	3,3-difluorocyclobutyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate	41-44	insulin receptor	Rattus norvegicus	118-120
34149862-16	2021	And the brain IR/IRS-1 signaling pathway plays an important role in astrocyte-neuron metabolic coupling, providing a potential mechanism by which the IR/IRS-1 signaling pathway may contribute to the treatment of ZJJ on diabetes-related depression.	3,3-difluorocyclobutyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate	212-215	insulin receptor	Rattus norvegicus	14-16
34149862-16	2021	And the brain IR/IRS-1 signaling pathway plays an important role in astrocyte-neuron metabolic coupling, providing a potential mechanism by which the IR/IRS-1 signaling pathway may contribute to the treatment of ZJJ on diabetes-related depression.	3,3-difluorocyclobutyl {(2R,4S,6S,12Z,13aS,14aR,16aS)-2-[(7-methoxy-3-methylquinoxalin-2-yl)oxy]-14a-[(1-methylcyclopropane-1-sulfonyl)carbamoyl]-5,16-dioxo-1,2,3,5,6,7,8,9,10,11,13a,14,14a,15,16,16a-hexadecahydrocyclopropa[e]pyrrolo[1,2-a][1,4]diazacyclopentadecin-6-yl}carbamate	212-215	insulin receptor	Rattus norvegicus	150-152
35502961-5	2022	EC and DHBA also increased the tyrosine phosphorylated and total insulin receptor (IR) levels, and activated the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway in cardiac H9c2 cells.	Catechin	0-2	insulin receptor	Rattus norvegicus	65-81
34137676-11	2021	Berberine also effectively decreased the expression of hippocampal tau protein, phosphorylated Tau, and increased insulin receptor antibodies.	Berberine	0-9	insulin receptor	Rattus norvegicus	114-130
35502961-5	2022	EC and DHBA also increased the tyrosine phosphorylated and total insulin receptor (IR) levels, and activated the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway in cardiac H9c2 cells.	Catechin	0-2	insulin receptor	Rattus norvegicus	83-85
35502961-5	2022	EC and DHBA also increased the tyrosine phosphorylated and total insulin receptor (IR) levels, and activated the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway in cardiac H9c2 cells.	2,3-dihydroxybenzoic acid	7-11	insulin receptor	Rattus norvegicus	65-81
35502961-5	2022	EC and DHBA also increased the tyrosine phosphorylated and total insulin receptor (IR) levels, and activated the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway in cardiac H9c2 cells.	2,3-dihydroxybenzoic acid	7-11	insulin receptor	Rattus norvegicus	83-85
35369824-5	2022	Furthermore, administrations of myricetin significantly increased the expression of insulin receptor (InsR) and glucose transporter 4 (GLUT4) gene and increased the expression of glucose-6-phosphatase (G-6-Pase) and phosphoenolpyruvate carboxykinase (PEPCK) gene.	myricetin	32-41	insulin receptor	Rattus norvegicus	84-100
35582969-10	2022	M-VDD increased time to fatigue during ex vivo contractions of EDL muscles and showed an increase in the phosphorylation levels of IGF-1/insulin receptor and their downstream targets related to anabolic processes and myogenic activation, including Ser 473 Akt and Ser 21/9 GSK-3beta.	m-vdd	0-5	insulin receptor	Rattus norvegicus	137-153
35582969-10	2022	M-VDD increased time to fatigue during ex vivo contractions of EDL muscles and showed an increase in the phosphorylation levels of IGF-1/insulin receptor and their downstream targets related to anabolic processes and myogenic activation, including Ser 473 Akt and Ser 21/9 GSK-3beta.	Serine	248-251	insulin receptor	Rattus norvegicus	137-153
35582969-10	2022	M-VDD increased time to fatigue during ex vivo contractions of EDL muscles and showed an increase in the phosphorylation levels of IGF-1/insulin receptor and their downstream targets related to anabolic processes and myogenic activation, including Ser 473 Akt and Ser 21/9 GSK-3beta.	Serine	264-267	insulin receptor	Rattus norvegicus	137-153
35394252-7	2022	Insulin-receptor binding studies using rat erythrocytes demonstrated that mean specific binding of insulin with insulin receptors was significantly increased in Mcy-treated diabetic rats when compared to diabetic control rats.	5-methyldeoxycytidine	161-164	insulin receptor	Rattus norvegicus	0-16
35559247-12	2022	Molecular docking results showed that Diosgenin, Kaempferol, Quercetin, Hederagenin, Isorhamnetin may act on the related pathways by docking EGFR, IGF1R and INSR.	Diosgenin	38-47	insulin receptor	Rattus norvegicus	157-161
35559247-12	2022	Molecular docking results showed that Diosgenin, Kaempferol, Quercetin, Hederagenin, Isorhamnetin may act on the related pathways by docking EGFR, IGF1R and INSR.	kaempferol	49-59	insulin receptor	Rattus norvegicus	157-161
35559247-12	2022	Molecular docking results showed that Diosgenin, Kaempferol, Quercetin, Hederagenin, Isorhamnetin may act on the related pathways by docking EGFR, IGF1R and INSR.	Quercetin	61-70	insulin receptor	Rattus norvegicus	157-161
35559247-12	2022	Molecular docking results showed that Diosgenin, Kaempferol, Quercetin, Hederagenin, Isorhamnetin may act on the related pathways by docking EGFR, IGF1R and INSR.	hederagenin	72-83	insulin receptor	Rattus norvegicus	157-161
35559247-12	2022	Molecular docking results showed that Diosgenin, Kaempferol, Quercetin, Hederagenin, Isorhamnetin may act on the related pathways by docking EGFR, IGF1R and INSR.	3-methylquercetin	85-97	insulin receptor	Rattus norvegicus	157-161
35369824-5	2022	Furthermore, administrations of myricetin significantly increased the expression of insulin receptor (InsR) and glucose transporter 4 (GLUT4) gene and increased the expression of glucose-6-phosphatase (G-6-Pase) and phosphoenolpyruvate carboxykinase (PEPCK) gene.	myricetin	32-41	insulin receptor	Rattus norvegicus	102-106
34791109-9	2022	CORT113176 pretreatment decreased baseline insulin receptor sensitive gene mRNAs Akt2, Irs1, Pik3r1, and Srebp1c at PD2.	CORT113176	0-10	insulin receptor	Rattus norvegicus	43-59