PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18691010-4	2008	Recent studies have revealed that DGK isozymes play pivotal roles in a wide variety of mammalian signal transduction pathways conducting growth factor/cytokine-dependent cell proliferation and motility, seizure activity, immune responses, cardiovascular responses and insulin receptor-mediated glucose metabolism.	Glucose	294-301	insulin receptor	Homo sapiens	268-284
18436806-1	2008	BACKGROUND: In the endothelium, insulin promotes nitric oxide (NO) production, through the insulin receptor/IRS-1/PI3-Kinase/Akt/eNOS signaling pathway.	Nitric Oxide	49-61	insulin receptor	Homo sapiens	91-107
18513965-0	2008	5-Substituted isophthalamides as insulin receptor sensitizers.	5-substituted isophthalamides	0-29	insulin receptor	Homo sapiens	33-49
18513965-1	2008	A novel series of 5-substituted isophthalamides and their structure-activity relationship as insulin receptor sensitizers is discussed.	5-substituted isophthalamides	18-47	insulin receptor	Homo sapiens	93-109
18316392-7	2008	The insulin receptor was downregulated to a similar degree by glargine and regular human insulin at high insulin concentrations (P < 0.0001 for glargine, P = 0.002 for regular human insulin).	Insulin Glargine	62-70	insulin receptor	Homo sapiens	4-20
19035155-8	2008	The number and affinity constant of erythrocyte insulin receptor recovered more quickly in intensive glucose controlled group than in hyperglycemia group.	Glucose	101-108	insulin receptor	Homo sapiens	48-64
19035155-10	2008	Intensive insulin therapy and glucose control may improve function recovery of insulin receptor.	Glucose	30-37	insulin receptor	Homo sapiens	79-95
18093597-6	2008	At the molecular level, significant increases in tyrosine-phosphorylation of the hepatic insulin receptor and IRS-1 were observed for rosuvastatin-treated hamsters (+37% and +58%, respectively) compared to fructose-fed controls following an intravenous (IV) bolus of insulin (p<0.05).	Tyrosine	49-57	insulin receptor	Homo sapiens	89-105
18316392-7	2008	The insulin receptor was downregulated to a similar degree by glargine and regular human insulin at high insulin concentrations (P < 0.0001 for glargine, P = 0.002 for regular human insulin).	Insulin Glargine	147-155	insulin receptor	Homo sapiens	4-20
18093597-6	2008	At the molecular level, significant increases in tyrosine-phosphorylation of the hepatic insulin receptor and IRS-1 were observed for rosuvastatin-treated hamsters (+37% and +58%, respectively) compared to fructose-fed controls following an intravenous (IV) bolus of insulin (p<0.05).	Rosuvastatin Calcium	134-146	insulin receptor	Homo sapiens	89-105
18093597-6	2008	At the molecular level, significant increases in tyrosine-phosphorylation of the hepatic insulin receptor and IRS-1 were observed for rosuvastatin-treated hamsters (+37% and +58%, respectively) compared to fructose-fed controls following an intravenous (IV) bolus of insulin (p<0.05).	Fructose	206-214	insulin receptor	Homo sapiens	89-105
18218307-7	2008	Treatment with steroid pulse and subsequent high dose of prednisolone resulted in restoration of euglycemia associated with disappearance of insulin receptor antibodies and improvement of both serum hypocomplementemia and the high titer of ANA.	Steroids	15-22	insulin receptor	Homo sapiens	141-157
18245813-3	2008	In HepG2 cells, deferoxamine stabilized HIF-1alpha and induced the constitutive glucose transporter Glut1 and the insulin receptor.	Deferoxamine	16-28	insulin receptor	Homo sapiens	114-130
18029081-1	2008	The N-terminal glycine of the A-chain in insulin is reported to be one of the residues that binds to the insulin receptor.	Glycine	15-22	insulin receptor	Homo sapiens	105-121
18089699-1	2008	CONTEXT: Complex glycosphingolipids, in majority the ganglioside GM3, surround the insulin receptor in a special membrane compartment (raft) and modulate signaling through this receptor.	Glycosphingolipids	17-35	insulin receptor	Homo sapiens	83-99
18089699-1	2008	CONTEXT: Complex glycosphingolipids, in majority the ganglioside GM3, surround the insulin receptor in a special membrane compartment (raft) and modulate signaling through this receptor.	Gangliosides	53-64	insulin receptor	Homo sapiens	83-99
18089699-1	2008	CONTEXT: Complex glycosphingolipids, in majority the ganglioside GM3, surround the insulin receptor in a special membrane compartment (raft) and modulate signaling through this receptor.	gm3	65-68	insulin receptor	Homo sapiens	83-99
18089699-10	2008	CONCLUSION: Gaucher disease, a lysosomal glycosphingolipid storage disorder, is associated with (peripheral) insulin resistance, possibly through the influence of glycosphingolipids on insulin receptor functioning.	Glycosphingolipids	163-181	insulin receptor	Homo sapiens	185-201
17957771-0	2008	N-linked glycans of the human insulin receptor and their distribution over the crystal structure.	n-linked glycans	0-16	insulin receptor	Homo sapiens	30-46
17957771-1	2008	The human insulin receptor (IR) homodimer is heavily glycosylated and contains a total of 19 predicted N-linked glycosylation sites in each monomer.	Nitrogen	103-104	insulin receptor	Homo sapiens	10-26
18310298-0	2008	The insulin receptor: a new anticancer target for peroxisome proliferator-activated receptor-gamma (PPARgamma) and thiazolidinedione-PPARgamma agonists.	2,4-thiazolidinedione	115-132	insulin receptor	Homo sapiens	4-20
18310298-3	2008	Herein, we studied the effects of PPARgamma and the PPARgamma agonists thiazolidinediones (TZDs) on the insulin receptor (IR), a cell membrane tyrosine kinase receptor protein, whose role is of paramount importance in mediating the metabolic and growth-promoting effects of the peptide hormone insulin.	Thiazolidinediones	71-89	insulin receptor	Homo sapiens	104-120
18310298-3	2008	Herein, we studied the effects of PPARgamma and the PPARgamma agonists thiazolidinediones (TZDs) on the insulin receptor (IR), a cell membrane tyrosine kinase receptor protein, whose role is of paramount importance in mediating the metabolic and growth-promoting effects of the peptide hormone insulin.	Thiazolidinediones	71-89	insulin receptor	Homo sapiens	122-124
18310298-3	2008	Herein, we studied the effects of PPARgamma and the PPARgamma agonists thiazolidinediones (TZDs) on the insulin receptor (IR), a cell membrane tyrosine kinase receptor protein, whose role is of paramount importance in mediating the metabolic and growth-promoting effects of the peptide hormone insulin.	Thiazolidinediones	91-95	insulin receptor	Homo sapiens	104-120
18310298-3	2008	Herein, we studied the effects of PPARgamma and the PPARgamma agonists thiazolidinediones (TZDs) on the insulin receptor (IR), a cell membrane tyrosine kinase receptor protein, whose role is of paramount importance in mediating the metabolic and growth-promoting effects of the peptide hormone insulin.	Thiazolidinediones	91-95	insulin receptor	Homo sapiens	122-124
18310298-6	2008	Using glutathione S-transferase pull-down assays combined with electrophoretic mobility shift assay and chromatin immunoprecipitation, we demonstrated that by interacting with Sp1, C/EBPbeta, and AP-2, PPARgamma can prevent Sp1/AP-2 protein-protein association and inhibit binding of Sp1 and C/EBPbeta to DNA, thus reducing IR gene transcription.	Glutathione	6-17	insulin receptor	Homo sapiens	324-326
18218307-7	2008	Treatment with steroid pulse and subsequent high dose of prednisolone resulted in restoration of euglycemia associated with disappearance of insulin receptor antibodies and improvement of both serum hypocomplementemia and the high titer of ANA.	Prednisolone	57-69	insulin receptor	Homo sapiens	141-157
17644209-5	2007	Basal IR phosphorylation was higher in SkMC-H than in SkMC-L (P<0.01) but after acute insulin stimulation (10nM insulin for 10 min), IR phosphorylation increased (P<0.01) in SkMC-L, but not in SkMC-H.	skmc-l	180-186	insulin receptor	Homo sapiens	136-138
17675299-6	2007	DGK inhibition was also accompanied by increased protein kinase C-alpha (PKCalpha) activity, reduced glucose-induced insulin receptor activation, and GLUT4 translocation.	Glucose	101-108	insulin receptor	Homo sapiens	117-133
17675299-8	2007	However, antisense silencing of DGKdelta, but not of DGKalpha expression, was sufficient to prevent the effect of high glucose on PKCalpha activity, insulin receptor signaling, and glucose uptake.	Glucose	119-126	insulin receptor	Homo sapiens	149-165
17675299-9	2007	Thus, the short term exposure of skeletal muscle cells to glucose causes a rapid induction of DGK, followed by a reduction of PKCalpha activity and transactivation of the insulin receptor signaling.	Glucose	58-65	insulin receptor	Homo sapiens	171-187
18070930-2	2008	We found recently that the cyclolignan picropodophyllin (PPP) inhibits phosphorylation of IGF-1R and phosphatidyl-3 kinase/Akt (protein kinase B) signaling molecules without interfering with the highly homologous insulin receptor.	picropodophyllin	39-55	insulin receptor	Homo sapiens	213-229
18070930-2	2008	We found recently that the cyclolignan picropodophyllin (PPP) inhibits phosphorylation of IGF-1R and phosphatidyl-3 kinase/Akt (protein kinase B) signaling molecules without interfering with the highly homologous insulin receptor.	picropodophyllin	57-60	insulin receptor	Homo sapiens	213-229
18171427-3	2008	It has been shown that these two SOCS members are able to inhibit the insulin signalling pathway by three different mechanisms: (1) inhibition of tyrosine phosphorylation of insulin receptor substrate (IRS) proteins because of competition at the docking site on the insulin receptor (IR), (2) induction of the proteasomal degradation of the IRS and (3) inhibition of the IR kinase.	Tyrosine	146-154	insulin receptor	Homo sapiens	174-190
18171427-3	2008	It has been shown that these two SOCS members are able to inhibit the insulin signalling pathway by three different mechanisms: (1) inhibition of tyrosine phosphorylation of insulin receptor substrate (IRS) proteins because of competition at the docking site on the insulin receptor (IR), (2) induction of the proteasomal degradation of the IRS and (3) inhibition of the IR kinase.	Tyrosine	146-154	insulin receptor	Homo sapiens	202-204
18296327-8	2008	In addition to IRS and Akt, diamide inhibited insulin receptor auto-phosphorylation.	Diamide	28-35	insulin receptor	Homo sapiens	46-62
17849478-6	2008	The inhibitory potency of NYQQN for insulin receptor drastically decreased, whereas QNAQYLR inhibited autophosphorylation of insulin receptor as well as EGFR.	nyqqn	26-31	insulin receptor	Homo sapiens	36-52
18691043-2	2008	Visfatin binds to the insulin receptor at a site distinct from that of insulin and causes hypoglycaemia by reducing glucose release from liver cells and stimulating glucose utilization in adipocytes and myocytes.	Glucose	116-123	insulin receptor	Homo sapiens	22-38
18691043-2	2008	Visfatin binds to the insulin receptor at a site distinct from that of insulin and causes hypoglycaemia by reducing glucose release from liver cells and stimulating glucose utilization in adipocytes and myocytes.	Glucose	165-172	insulin receptor	Homo sapiens	22-38
17644209-5	2007	Basal IR phosphorylation was higher in SkMC-H than in SkMC-L (P<0.01) but after acute insulin stimulation (10nM insulin for 10 min), IR phosphorylation increased (P<0.01) in SkMC-L, but not in SkMC-H.	skmc-h	39-45	insulin receptor	Homo sapiens	6-8
17644209-5	2007	Basal IR phosphorylation was higher in SkMC-H than in SkMC-L (P<0.01) but after acute insulin stimulation (10nM insulin for 10 min), IR phosphorylation increased (P<0.01) in SkMC-L, but not in SkMC-H.	skmc-l	54-60	insulin receptor	Homo sapiens	6-8
17952759-4	2007	We hypothesized that the administration of an isoform of inositol (myo-inositol), belonging to the vitamin B complex, would improve the insulin-receptor activity, restoring normal ovulatory function.	Inositol	57-65	insulin receptor	Homo sapiens	136-152
17952759-4	2007	We hypothesized that the administration of an isoform of inositol (myo-inositol), belonging to the vitamin B complex, would improve the insulin-receptor activity, restoring normal ovulatory function.	Inositol	67-79	insulin receptor	Homo sapiens	136-152
17952759-4	2007	We hypothesized that the administration of an isoform of inositol (myo-inositol), belonging to the vitamin B complex, would improve the insulin-receptor activity, restoring normal ovulatory function.	Niacinamide	99-108	insulin receptor	Homo sapiens	136-152
17644209-5	2007	Basal IR phosphorylation was higher in SkMC-H than in SkMC-L (P<0.01) but after acute insulin stimulation (10nM insulin for 10 min), IR phosphorylation increased (P<0.01) in SkMC-L, but not in SkMC-H.	skmc-h	199-205	insulin receptor	Homo sapiens	136-138
17644209-9	2007	Finally, SkMC-H showed a complete, but significantly delayed recycling of IR to plasma membrane (t(1/2)=20 min versus SkMC-L t(1/2)=7 min).	skmc-h	9-15	insulin receptor	Homo sapiens	74-76
17644209-9	2007	Finally, SkMC-H showed a complete, but significantly delayed recycling of IR to plasma membrane (t(1/2)=20 min versus SkMC-L t(1/2)=7 min).	skmc	9-13	insulin receptor	Homo sapiens	74-76
17919343-1	2007	BACKGROUND: Accumulated evidence suggests that hydrogen peroxide (H2O2) generated in cells during insulin stimulation plays an integral role in insulin receptor signal transduction.	Hydrogen Peroxide	47-64	insulin receptor	Homo sapiens	144-160
17919343-1	2007	BACKGROUND: Accumulated evidence suggests that hydrogen peroxide (H2O2) generated in cells during insulin stimulation plays an integral role in insulin receptor signal transduction.	Hydrogen Peroxide	66-70	insulin receptor	Homo sapiens	144-160
17919343-3	2007	The aim of the present study is to test the following hypotheses (1) whether insulin-induced H2O2 is required for insulin receptor autophosphorylation in neurons, and (2) whether mitochondrial respiratory chain is involved in insulin-stimulated H2O2 production, thus playing an integral role in insulin receptor autophosphorylation in neurons.	Hydrogen Peroxide	93-97	insulin receptor	Homo sapiens	114-130
17919343-7	2007	Dicholine salt of succinic acid, a respiratory substrate, significantly enhanced the effect of suboptimal insulin concentration on the insulin receptor autophosphorylation in CGN.	dicholine salt	0-14	insulin receptor	Homo sapiens	135-151
17919343-7	2007	Dicholine salt of succinic acid, a respiratory substrate, significantly enhanced the effect of suboptimal insulin concentration on the insulin receptor autophosphorylation in CGN.	Succinic Acid	18-31	insulin receptor	Homo sapiens	135-151
17919343-8	2007	CONCLUSION: Results of the present study suggest that insulin-induced H2O2 is required for the enhancement of insulin receptor autophosphorylation in neurons.	Hydrogen Peroxide	70-74	insulin receptor	Homo sapiens	110-126
17919343-9	2007	The mitochondrial respiratory chain is involved in insulin-stimulated H2O2 production, thus playing an integral role in the insulin receptor autophosphorylation in neurons.	Hydrogen Peroxide	70-74	insulin receptor	Homo sapiens	124-140
17686957-7	2007	Finally, we discuss a potential role for regulation of insulin receptor signaling in the kidney in contributing to sodium balance and blood pressure.	Sodium	115-121	insulin receptor	Homo sapiens	55-71
21357158-3	2007	The expression and phosphorylation of human Gab-1 with the insulin receptor kinase in vitro are summarized as an example of this approach to identifying phosphorylated tyrosine residues.	Tyrosine	168-176	insulin receptor	Homo sapiens	59-75
17490855-7	2007	Oligo(dT)18 primed cDNA was synthesized from HepG2 and HT29 total RNA to amplify IR and cSRC kinase ORFs, respectively.	oligo(dt)18	0-11	insulin receptor	Homo sapiens	81-83
17618942-0	2007	Photoperiodic changes in hypothalamic insulin receptor gene expression are regulated by gonadal testosterone.	Testosterone	96-108	insulin receptor	Homo sapiens	38-54
17618942-5	2007	Castration abolished IR mRNA expression induced by long-day conditions, whereas the testosterone administration mimicked induction of IR mRNA expression induced by long-day conditions.	Testosterone	84-96	insulin receptor	Homo sapiens	134-136
17618942-6	2007	These results suggested that the photoperiodic regulation of the IR mRNA in the infundibular nucleus is mediated by testosterone from the testes.	Testosterone	116-128	insulin receptor	Homo sapiens	65-67
17556377-11	2007	The actions of IGF-II but not those of IGF-I were sensitive to inhibition by the insulin receptor inhibitor HNMPA(AM)3.	HNMPA	108-113	insulin receptor	Homo sapiens	81-97
17179152-7	2007	Protein tyrosine phosphatases (PTPs) appear to be important for the IRS-1 cleavage because tyrosine phosphorylation of the insulin receptor was decreased in hypoxia and IRS-1 cleavage could be blocked either with H(2)O(2) or with vanadate, each of which inhibits PTPs.	Tyrosine	8-16	insulin receptor	Homo sapiens	123-139
17914241-5	2007	Isoleucine 137 was conserved for insulin receptor and regulatory subunit of a phosphorylating enzyme.	isoleucine 137	0-14	insulin receptor	Homo sapiens	33-49
17914241-6	2007	Whereas residues valine, leucine, methionine were highly conserved for insulin receptor.	Valine	17-23	insulin receptor	Homo sapiens	71-87
17914241-6	2007	Whereas residues valine, leucine, methionine were highly conserved for insulin receptor.	Leucine	25-32	insulin receptor	Homo sapiens	71-87
17914241-6	2007	Whereas residues valine, leucine, methionine were highly conserved for insulin receptor.	Methionine	34-44	insulin receptor	Homo sapiens	71-87
17434141-0	2007	Fatty acid represses insulin receptor gene expression by impairing HMGA1 through protein kinase Cepsilon.	Fatty Acids	0-10	insulin receptor	Homo sapiens	21-37
18220662-1	2007	The dissection of mechanisms that regulate glucose transport by insulin has revealed an intricate network of signaling molecules scattered from the insulin receptor to the intracellular glucose transporter GLUT4.	Glucose	43-50	insulin receptor	Homo sapiens	148-164
17347799-4	2007	Activation of the IR can be impaired by post-translational modifications of the protein involving serine phosphorylation, or by binding to inhibiting proteins such as PC-1 or members of the SOCS or Grb protein families.	Serine	98-104	insulin receptor	Homo sapiens	18-20
17179152-7	2007	Protein tyrosine phosphatases (PTPs) appear to be important for the IRS-1 cleavage because tyrosine phosphorylation of the insulin receptor was decreased in hypoxia and IRS-1 cleavage could be blocked either with H(2)O(2) or with vanadate, each of which inhibits PTPs.	Hydrogen Peroxide	213-221	insulin receptor	Homo sapiens	123-139
17179152-7	2007	Protein tyrosine phosphatases (PTPs) appear to be important for the IRS-1 cleavage because tyrosine phosphorylation of the insulin receptor was decreased in hypoxia and IRS-1 cleavage could be blocked either with H(2)O(2) or with vanadate, each of which inhibits PTPs.	Vanadates	230-238	insulin receptor	Homo sapiens	123-139
17340225-5	2007	The expression and tyrosine phosphorylation of IR, IR substrate-1 (IRS-1), and IRS-2 were determined by immunoprecipitation and immunoblotting.	Tyrosine	19-27	insulin receptor	Homo sapiens	47-49
17340225-10	2007	We found that visfatin induced tyrosine phosphorylation of IR, IRS-1, and IRS-2.	Tyrosine	31-39	insulin receptor	Homo sapiens	59-61
17340225-11	2007	Moreover, the effects of visfatin - glucose uptake, proliferation, and type I collagen enhancement of cultured human osteoblast-like cells - bore a close resemblance to those of insulin and were inhibited by hydroxy-2-naphthalenylmethylphosphonic acid tris-acetoxymethyl ester, a specific inhibitor of IR tyrosine kinase activity.	(hydroxy-2-naphthalenylmethyl)phosphonic acid	208-251	insulin receptor	Homo sapiens	302-304
17234168-5	2007	Inhibition of insulin receptor (IR) maturation via inhibition of its activating convertase furin with the pharmacological furin-inhibitor decanoyl-RVKR-chloromethylketone, as well as blocking of IGF-1R function with a IGF-1R blocking antibody, demonstrated that insulin mediates increases in MMP-9 via IR activation.	decanoylRVKRchloromethylketone	138-170	insulin receptor	Homo sapiens	14-30
17234168-5	2007	Inhibition of insulin receptor (IR) maturation via inhibition of its activating convertase furin with the pharmacological furin-inhibitor decanoyl-RVKR-chloromethylketone, as well as blocking of IGF-1R function with a IGF-1R blocking antibody, demonstrated that insulin mediates increases in MMP-9 via IR activation.	decanoylRVKRchloromethylketone	138-170	insulin receptor	Homo sapiens	32-34
17346204-7	2007	This article presents the evidence about FFA-induced insulin secretion in vitro and in vivo, recent advances in the molecular mechanism of FFA action in beta-cells, a role of GPR40 in the development of insulin resistance, and the negative feedback loop of the insulin receptor signal pathway.	Fatty Acids, Nonesterified	41-44	insulin receptor	Homo sapiens	261-277
17435330-1	2007	Free fatty acids are known to play a key role in promoting loss of insulin sensitivity,thereby causing insulin resistance and type 2 diabetes.However,the underlying mechanism involved is still unclear.In searching for the cause of the mechanism,it has been found that palmitate inhibits insulin receptor (IR)gene expression,leading to a reduced amount of IR protein in insulin target cells.	Fatty Acids, Nonesterified	0-16	insulin receptor	Homo sapiens	287-303
17435330-1	2007	Free fatty acids are known to play a key role in promoting loss of insulin sensitivity,thereby causing insulin resistance and type 2 diabetes.However,the underlying mechanism involved is still unclear.In searching for the cause of the mechanism,it has been found that palmitate inhibits insulin receptor (IR)gene expression,leading to a reduced amount of IR protein in insulin target cells.	Palmitates	268-277	insulin receptor	Homo sapiens	287-303
17435330-2	2007	PDK1-independent phosphorylation of PKC(eta) causes this reduction in insulin receptor gene expression.One of the pathways through which fatty acid can induce insulin resistance in insulin target cells is suggested by these studies.We provide an overview of this important area,emphasizing the current status.	Fatty Acids	137-147	insulin receptor	Homo sapiens	70-86
16934761-9	2006	Using site-specific antibodies against phosphorylated tyrosines of the insulin receptor, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	54-63	insulin receptor	Homo sapiens	71-87
16956746-1	2007	The present study examined the dose-dependent effects of diethylhexyl phthalate (DEHP) on insulin receptor concentration and glucose oxidation in Chang liver cells.	Diethylhexyl Phthalate	57-79	insulin receptor	Homo sapiens	90-106
16956746-1	2007	The present study examined the dose-dependent effects of diethylhexyl phthalate (DEHP) on insulin receptor concentration and glucose oxidation in Chang liver cells.	Diethylhexyl Phthalate	81-85	insulin receptor	Homo sapiens	90-106
16956746-4	2007	Both insulin receptor concentration and glucose oxidation in Chang liver cells were significantly reduced by high doses (200 and 400 microM) of phthalate exposure.	phthalic acid	144-153	insulin receptor	Homo sapiens	5-21
17085043-4	2006	A mechanism-based bisubstrate analog strategy has given X-ray crystallographic insights into how several topical PTKs, including the insulin receptor, Abl and epidermal growth factor receptor, interact with tyrosine-containing peptide substrates.	Tyrosine	207-215	insulin receptor	Homo sapiens	133-149
17340225-13	2007	These data indicate that the regulation of glucose uptake, proliferation, and type I collagen production by visfatin in human osteoblasts involves IR phosphorylation, the same signal-transduction pathway used by insulin.	Glucose	43-50	insulin receptor	Homo sapiens	147-149
17259395-4	2007	We have characterized a novel class of arylalkylamine vanadium salts that exert potent insulin-mimetic effects downstream of the insulin receptor in adipocytes.	arylalkylamine vanadium salts	39-68	insulin receptor	Homo sapiens	129-145
17078079-0	2007	The location and characterisation of the O-linked glycans of the human insulin receptor.	o-linked glycans	41-57	insulin receptor	Homo sapiens	71-87
17419944-5	2007	The recent publication of the three-dimensional structure of the IGF-IR kinase domain has facilitated the development of IGF-IR inhibitors of the cyclolignan family, that is picropodophyllin, with capacity to distinguish also in vivo between the IGF-IR and the insulin receptor.	cyclolignan	146-157	insulin receptor	Homo sapiens	261-277
16934761-9	2006	Using site-specific antibodies against phosphorylated tyrosines of the insulin receptor, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	130-139	insulin receptor	Homo sapiens	71-87
16934761-9	2006	Using site-specific antibodies against phosphorylated tyrosines of the insulin receptor, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	54-62	insulin receptor	Homo sapiens	71-87
16934761-11	2006	Our work suggests that Grb14 may regulate signalling through the insulin receptor by controlling its tyrosine-dephosphorylation in a site-specific manner.	Tyrosine	101-109	insulin receptor	Homo sapiens	65-81
17161616-13	2006	Several new target genes previously documented to influence bone formation were up-regulated by DHEA such as Notch 2, insulin receptor, thrombin receptor (PAR1).	Dehydroepiandrosterone	96-100	insulin receptor	Homo sapiens	118-134
16957736-6	2006	The structure reveals the domain arrangement in the disulphide-linked ectodomain dimer, showing that the insulin receptor adopts a folded-over conformation that places the ligand-binding regions in juxtaposition.	disulphide	52-62	insulin receptor	Homo sapiens	105-121
16886086-0	2006	A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment.	Lanthanoid Series Elements	11-21	insulin receptor	Homo sapiens	124-140
16962112-10	2006	Normal fibroblasts respond to increasing glucose concentrations by increasing the expression levels of the IR, IGF-IR, and IGF-I, whereas adhesion fibroblasts respond by decreasing the expression of the IR, IGF-IR, and IGF-I.	Glucose	41-48	insulin receptor	Homo sapiens	107-109
16962112-10	2006	Normal fibroblasts respond to increasing glucose concentrations by increasing the expression levels of the IR, IGF-IR, and IGF-I, whereas adhesion fibroblasts respond by decreasing the expression of the IR, IGF-IR, and IGF-I.	Glucose	41-48	insulin receptor	Homo sapiens	115-117
17003275-9	2006	These data suggest that, in Ir(P1195L/wt) mice, normal levels of plasma glucose were maintained due to high levels of plasma insulin resulting from increased numbers of beta-cells, which in turn was due to increased beta-cell proliferation rather than decreased beta-cell apoptosis.	Glucose	72-79	insulin receptor	Homo sapiens	28-30
16761106-1	2006	AIMS/HYPOTHESIS: Recently we reported the coexistence of postprandial hypoglycaemia and moderate insulin resistance in heterozygous carriers of the Arg1174Gln mutation in the insulin receptor gene (INSR).	arg1174gln	148-158	insulin receptor	Homo sapiens	175-191
16761106-1	2006	AIMS/HYPOTHESIS: Recently we reported the coexistence of postprandial hypoglycaemia and moderate insulin resistance in heterozygous carriers of the Arg1174Gln mutation in the insulin receptor gene (INSR).	arg1174gln	148-158	insulin receptor	Homo sapiens	198-202
16839860-4	2006	Several mechanisms have been described as responsible for the inhibition of insulin-stimulated tyrosine phosphorylation of IR and the IR substrate (IRS) proteins, including proteasome-mediated degradation, phosphatase-mediated dephosphorylation, and kinase-mediated serine/threonine phosphorylation.	Tyrosine	95-103	insulin receptor	Homo sapiens	123-125
16839860-4	2006	Several mechanisms have been described as responsible for the inhibition of insulin-stimulated tyrosine phosphorylation of IR and the IR substrate (IRS) proteins, including proteasome-mediated degradation, phosphatase-mediated dephosphorylation, and kinase-mediated serine/threonine phosphorylation.	Serine	266-272	insulin receptor	Homo sapiens	123-125
16839860-4	2006	Several mechanisms have been described as responsible for the inhibition of insulin-stimulated tyrosine phosphorylation of IR and the IR substrate (IRS) proteins, including proteasome-mediated degradation, phosphatase-mediated dephosphorylation, and kinase-mediated serine/threonine phosphorylation.	Threonine	273-282	insulin receptor	Homo sapiens	123-125
16819546-2	2006	Using human colorectal cancer (CRC) cells, we evaluated the involvement of the insulin receptor isoform-A (InsR-A) in de novo resistance to gefitinib, an EGFR tyrosine kinase inhibitor.	Gefitinib	140-149	insulin receptor	Homo sapiens	107-111
16819546-5	2006	Insulin and IGF-II promoted cell growth and pEGFR Tyr845, Tyr1068 and Tyr1173 activity and conversely, the insulin-like growth factor-1 receptor (IGF-1R)/InsR inhibitor ABDP (1 muM) inhibited growth and reduced pEGFR activity at all three tyrosine residues.	Tyrosine	239-247	insulin receptor	Homo sapiens	154-158
16819546-10	2006	We concluded that InsR-A reduces sensitivity to gefitinib in LoVo CRC cells, thus its co-targeting alongside EGFR can improve the anti-tumour effect of gefitinib.	Gefitinib	48-57	insulin receptor	Homo sapiens	18-22
16819546-10	2006	We concluded that InsR-A reduces sensitivity to gefitinib in LoVo CRC cells, thus its co-targeting alongside EGFR can improve the anti-tumour effect of gefitinib.	Gefitinib	152-161	insulin receptor	Homo sapiens	18-22
16886086-0	2006	A cationic lanthanide complex binds selectively to phosphorylated tyrosine sites, aiding NMR analysis of the phosphorylated insulin receptor peptide fragment.	Tyrosine	66-74	insulin receptor	Homo sapiens	124-140
16524741-5	2006	Furthermore, VS-induced adiponectin accumulation occurred in the presence of AGL2263, an insulin receptor (IR) inhibitor.	AGL 2263	77-84	insulin receptor	Homo sapiens	89-105
16574792-5	2006	Reduced kinase activities of the insulin receptor (INSR) and several downstream INSR signaling intermediates (i.e. p70S6k, AMP-activated protein kinase, glycogen synthase kinase-3, and Fyn) were detected in adipocytes and T lymphocytes due to short-term treatment with dexamethasone (DEX), a synthetic fluorinated GC.	Dexamethasone	269-282	insulin receptor	Homo sapiens	33-49
16574792-5	2006	Reduced kinase activities of the insulin receptor (INSR) and several downstream INSR signaling intermediates (i.e. p70S6k, AMP-activated protein kinase, glycogen synthase kinase-3, and Fyn) were detected in adipocytes and T lymphocytes due to short-term treatment with dexamethasone (DEX), a synthetic fluorinated GC.	Dexamethasone	269-282	insulin receptor	Homo sapiens	51-55
16574792-5	2006	Reduced kinase activities of the insulin receptor (INSR) and several downstream INSR signaling intermediates (i.e. p70S6k, AMP-activated protein kinase, glycogen synthase kinase-3, and Fyn) were detected in adipocytes and T lymphocytes due to short-term treatment with dexamethasone (DEX), a synthetic fluorinated GC.	Dexamethasone	284-287	insulin receptor	Homo sapiens	33-49
16574792-5	2006	Reduced kinase activities of the insulin receptor (INSR) and several downstream INSR signaling intermediates (i.e. p70S6k, AMP-activated protein kinase, glycogen synthase kinase-3, and Fyn) were detected in adipocytes and T lymphocytes due to short-term treatment with dexamethasone (DEX), a synthetic fluorinated GC.	Dexamethasone	284-287	insulin receptor	Homo sapiens	51-55
16574792-6	2006	Western blot analysis confirmed suppressed phosphorylation of the INSR and a series of downstream INSR targets (i.e. INSR substrate-1, p70S6k, protein kinase B, phosphoinositide-dependent protein kinase, Fyn, and glycogen synthase kinase-3) after DEX treatment.	Dexamethasone	247-250	insulin receptor	Homo sapiens	66-70
16524741-5	2006	Furthermore, VS-induced adiponectin accumulation occurred in the presence of AGL2263, an insulin receptor (IR) inhibitor.	AGL 2263	77-84	insulin receptor	Homo sapiens	107-109
16789735-3	2006	The ortho substitution to the (S)-IZD on the aryl ring afforded low nanomolar enzyme inhibitors of PTP1B that also displayed low caco-2 permeability and cellular activity in an insulin receptor (IR) phosphorylation assay and an Akt phosphorylation assay.	(s)-izd	30-37	insulin receptor	Homo sapiens	177-193
16789735-3	2006	The ortho substitution to the (S)-IZD on the aryl ring afforded low nanomolar enzyme inhibitors of PTP1B that also displayed low caco-2 permeability and cellular activity in an insulin receptor (IR) phosphorylation assay and an Akt phosphorylation assay.	(s)-izd	30-37	insulin receptor	Homo sapiens	195-197
16611834-2	2006	A mechanism for impaired insulin signaling in peripheral tissues is the inhibition of insulin action through serine phosphorylation of insulin receptor substrate (Irs) proteins that abolish the coupling of Irs proteins to the activated insulin receptor.	Serine	109-115	insulin receptor	Homo sapiens	135-151
16434550-1	2006	Growth factor receptor-bound protein 10 (Grb10) is an adapter protein that interacts with a number of tyrosine-phosphorylated growth factor receptors, including the insulin receptor (IR).	Tyrosine	102-110	insulin receptor	Homo sapiens	165-181
16434550-1	2006	Growth factor receptor-bound protein 10 (Grb10) is an adapter protein that interacts with a number of tyrosine-phosphorylated growth factor receptors, including the insulin receptor (IR).	Tyrosine	102-110	insulin receptor	Homo sapiens	183-185
16702775-5	2006	This results from at least two independent insulin receptor signals, one leading to the activation of phosphatidylinositol (PI) 3-kinase and the other to the activation of the Rho family small GTP-binding protein TC10.	Phosphatidylinositols	102-122	insulin receptor	Homo sapiens	43-59
16702775-5	2006	This results from at least two independent insulin receptor signals, one leading to the activation of phosphatidylinositol (PI) 3-kinase and the other to the activation of the Rho family small GTP-binding protein TC10.	Guanosine Triphosphate	193-196	insulin receptor	Homo sapiens	43-59
16611834-2	2006	A mechanism for impaired insulin signaling in peripheral tissues is the inhibition of insulin action through serine phosphorylation of insulin receptor substrate (Irs) proteins that abolish the coupling of Irs proteins to the activated insulin receptor.	Serine	109-115	insulin receptor	Homo sapiens	236-252
16607115-7	2006	Another prominent case in point is insulin-independent "basal" insulin receptor kinase activity, which is strongly enhanced by hydrogen peroxide or by an oxidative shift in redox status.	Hydrogen Peroxide	127-144	insulin receptor	Homo sapiens	63-79
16733497-10	2006	Visfatin binds to the insulin receptor at a site distinct from insulin and exerts hypoglycemic effect by reducing glucose release from hepatocytes and stimulating glucose utilization in peripheral tissues.	Glucose	114-121	insulin receptor	Homo sapiens	22-38
16733497-10	2006	Visfatin binds to the insulin receptor at a site distinct from insulin and exerts hypoglycemic effect by reducing glucose release from hepatocytes and stimulating glucose utilization in peripheral tissues.	Glucose	163-170	insulin receptor	Homo sapiens	22-38
16607115-8	2006	The insulin receptor signaling cascade induces anabolic and anticatabolic effects, but its abnormal upregulation under starving conditions potentially compromises glucose and amino acid homeostasis.	Glucose	163-170	insulin receptor	Homo sapiens	4-20
16582879-0	2006	Interaction with Grb14 results in site-specific regulation of tyrosine phosphorylation of the insulin receptor.	Tyrosine	62-70	insulin receptor	Homo sapiens	94-110
16582879-4	2006	Using site-specific antibodies against phosphorylated tyrosines of the IR, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	54-63	insulin receptor	Homo sapiens	71-73
16582879-4	2006	Using site-specific antibodies against phosphorylated tyrosines of the IR, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	116-125	insulin receptor	Homo sapiens	71-73
16582879-4	2006	Using site-specific antibodies against phosphorylated tyrosines of the IR, we showed that Grb14 protected the three tyrosines of the kinase loop from dephosphorylation by PTP1B, while favouring dephosphorylation of tyrosine 972.	Tyrosine	54-62	insulin receptor	Homo sapiens	71-73
16582879-7	2006	Our work therefore suggests that Grb14 may regulate signalling through the IR by controlling its tyrosine dephosphorylation in a site-specific manner.	Tyrosine	97-105	insulin receptor	Homo sapiens	75-77
16457816-3	2006	Here, we show that insulin-receptor-mediated endocystosis and fluid phase insulin-stimulated endocytosis are enhanced in cells expressing the Rin1:wild type and the Rin1:C deletion mutant, which contain both the Rab5-GEF and GTP-bound Ras binding domains.	Guanosine Triphosphate	225-228	insulin receptor	Homo sapiens	19-35
16457816-6	2006	Furthermore, association of the Rin1 SH2 domain with the insulin receptor was dependent on tyrosine phosphorylation of the insulin receptor.	Tyrosine	91-99	insulin receptor	Homo sapiens	57-73
16457816-6	2006	Furthermore, association of the Rin1 SH2 domain with the insulin receptor was dependent on tyrosine phosphorylation of the insulin receptor.	Tyrosine	91-99	insulin receptor	Homo sapiens	123-139
16182514-7	2006	cAMP production is modulated by hormone receptors coupled to Gs/Gi family of GTP binding proteins, such as beta-adrenergic receptors, whereas cAMP degradation is controlled by modulation of phosphodiesterase activity, increased by insulin receptor signalling.	Cyclic AMP	142-146	insulin receptor	Homo sapiens	231-247
16598903-3	2005	The insulin receptor exhibits a tyrosine-kinase activity which leads, first, to receptor autophosphorylation and then to tyrosine phosphorylation of substrates proteins, IRS proteins in priority.	Tyrosine	32-40	insulin receptor	Homo sapiens	4-20
16244361-1	2006	Signal transduction from the insulin receptor to downstream effectors is attenuated by phosphorylation at a number of Ser/Thr residues of insulin receptor substrate-1 (IRS-1) resulting in resistance to insulin action, the hallmark of type II diabetes.	Threonine	122-125	insulin receptor	Homo sapiens	29-45
16884318-1	2006	BACKGROUND: ISIS 113715 is a 20-mer phosphorothioate antisense oligonucleotide (ASO) that is complementary to the protein tyrosine phosphatase 1B (PTP-1B) messenger RNA and subsequently reduces translation of the PTP-1B protein, a negative regulator of insulin receptor.	Parathion	36-52	insulin receptor	Homo sapiens	253-269
16884318-1	2006	BACKGROUND: ISIS 113715 is a 20-mer phosphorothioate antisense oligonucleotide (ASO) that is complementary to the protein tyrosine phosphatase 1B (PTP-1B) messenger RNA and subsequently reduces translation of the PTP-1B protein, a negative regulator of insulin receptor.	Oligonucleotides	63-78	insulin receptor	Homo sapiens	253-269
16510354-8	2006	Steady-state insulin receptor binding affinity was slightly lower for glulisine versus RHI (approximately 0.70).	glulisine	70-79	insulin receptor	Homo sapiens	13-29
16510354-10	2006	Glulisine, Asp(B10), and RHI showed similar insulin receptor-association kinetics; however, Asp(B10) revealed increased insulin receptor affinity.	glulisine	0-9	insulin receptor	Homo sapiens	44-60
16510354-11	2006	Glulisine and RHI showed similar insulin receptor-mediated phosphorylation and IRS-2 activation.	glulisine	0-9	insulin receptor	Homo sapiens	33-49
16309849-2	2006	This in turn triggers a kinase cascade which activates both IkappaB kinase-beta (IKK-beta) and c-Jun N-terminal kinase (JNK), each of which can phosphorylate a key serine residue in IRS-1, rendering it a poor substrate for the activated insulin receptor.	Serine	164-170	insulin receptor	Homo sapiens	237-253
16213197-7	2005	This bisubstrate compound proved to be a potent inhibitor against the insulin receptor kinase and occupied both peptide and nucleotide binding sites.	bisubstrate	5-16	insulin receptor	Homo sapiens	70-86
16235045-0	2005	The vanadyl (VO2+) chelate bis(acetylacetonato)oxovanadium(IV) potentiates tyrosine phosphorylation of the insulin receptor.	Vanadates	4-11	insulin receptor	Homo sapiens	107-123
16235045-0	2005	The vanadyl (VO2+) chelate bis(acetylacetonato)oxovanadium(IV) potentiates tyrosine phosphorylation of the insulin receptor.	vo2+	13-17	insulin receptor	Homo sapiens	107-123
16235045-0	2005	The vanadyl (VO2+) chelate bis(acetylacetonato)oxovanadium(IV) potentiates tyrosine phosphorylation of the insulin receptor.	Vanadium,4-pentanedionato)-	27-58	insulin receptor	Homo sapiens	107-123
16235045-0	2005	The vanadyl (VO2+) chelate bis(acetylacetonato)oxovanadium(IV) potentiates tyrosine phosphorylation of the insulin receptor.	Tyrosine	75-83	insulin receptor	Homo sapiens	107-123
16235045-4	2005	Each of the three VO2+ chelates increased the tyrosine phosphorylation of proteins in response to insulin, including the beta-subunit of the insulin receptor (IRbeta) and the insulin receptor substrate-1 (IRS1).	Tyrosine	46-54	insulin receptor	Homo sapiens	141-157
16235045-9	2005	Cumulatively, these results provide evidence that VO(acac)2 exerts its insulin-enhancing properties by directly potentiating the tyrosine phosphorylation of the insulin receptor, resulting in the initiation of insulin metabolic signaling cascades in 3T3-L1 adipocytes.	bis(acetylacetonato)oxovanadium(IV)	50-59	insulin receptor	Homo sapiens	161-177
16235045-9	2005	Cumulatively, these results provide evidence that VO(acac)2 exerts its insulin-enhancing properties by directly potentiating the tyrosine phosphorylation of the insulin receptor, resulting in the initiation of insulin metabolic signaling cascades in 3T3-L1 adipocytes.	Tyrosine	129-137	insulin receptor	Homo sapiens	161-177
16314505-0	2005	Tyrosine phosphorylation of phosphoinositide-dependent kinase 1 by the insulin receptor is necessary for insulin metabolic signaling.	Tyrosine	0-8	insulin receptor	Homo sapiens	71-87
16567414-3	2006	In contrast, the inhibition by tannic acid of p60(c-src) tyrosine kinase (IC50 = 14 microM) and insulin receptor tyrosine kinase (IC50 = 5 microM) was much weaker.	Tannins	31-42	insulin receptor	Homo sapiens	96-112
16567414-9	2006	The molecular modeling study suggested that tannic acid could be docked into the ATP binding pockets of either EGFr or insulin receptor.	Tannins	44-55	insulin receptor	Homo sapiens	119-135
16567414-9	2006	The molecular modeling study suggested that tannic acid could be docked into the ATP binding pockets of either EGFr or insulin receptor.	Adenosine Triphosphate	81-84	insulin receptor	Homo sapiens	119-135
16489046-5	2006	Twenty-four-hour pretreatment with EM164 also inhibited insulin-mediated phosphorylation of IR and insulin-stimulated proliferation of MCF-7 cells.	em164	35-40	insulin receptor	Homo sapiens	92-94
16244361-1	2006	Signal transduction from the insulin receptor to downstream effectors is attenuated by phosphorylation at a number of Ser/Thr residues of insulin receptor substrate-1 (IRS-1) resulting in resistance to insulin action, the hallmark of type II diabetes.	Serine	118-121	insulin receptor	Homo sapiens	29-45
16225476-5	2005	CONCLUSION: Iron status affects insulin sensitivity by modulating the transcription and membrane expression/affinity of insulin receptor expression in hepatocytes and influencing insulin-dependent gene expression suggesting that increased insulin clearance and decreased insulin resistance may contribute to the positive effect of iron depletion in patients with non-alcoholic fatty liver disease.	Iron	12-16	insulin receptor	Homo sapiens	120-136
16225476-5	2005	CONCLUSION: Iron status affects insulin sensitivity by modulating the transcription and membrane expression/affinity of insulin receptor expression in hepatocytes and influencing insulin-dependent gene expression suggesting that increased insulin clearance and decreased insulin resistance may contribute to the positive effect of iron depletion in patients with non-alcoholic fatty liver disease.	Iron	331-335	insulin receptor	Homo sapiens	120-136
16113094-5	2005	Moreover, combination strategies that additionally target the IGF-IR/InsR can enhance the antitumour effects of gefitinib.	Gefitinib	112-121	insulin receptor	Homo sapiens	69-73
16884318-1	2006	BACKGROUND: ISIS 113715 is a 20-mer phosphorothioate antisense oligonucleotide (ASO) that is complementary to the protein tyrosine phosphatase 1B (PTP-1B) messenger RNA and subsequently reduces translation of the PTP-1B protein, a negative regulator of insulin receptor.	Oligonucleotides, Antisense	80-83	insulin receptor	Homo sapiens	253-269
16260343-3	2005	OBJECTIVE: To determine the insulin receptor (IR) tyrosine kinase activity--phosphorylation of exogenous substrate poly(Glu 4: Tyr 1)--and insulin receptor substrate 1 expression in normal myometrium and leiomyoma.	poly(glu	115-123	insulin receptor	Homo sapiens	28-44
16260343-3	2005	OBJECTIVE: To determine the insulin receptor (IR) tyrosine kinase activity--phosphorylation of exogenous substrate poly(Glu 4: Tyr 1)--and insulin receptor substrate 1 expression in normal myometrium and leiomyoma.	poly(glu	115-123	insulin receptor	Homo sapiens	46-48
16260343-3	2005	OBJECTIVE: To determine the insulin receptor (IR) tyrosine kinase activity--phosphorylation of exogenous substrate poly(Glu 4: Tyr 1)--and insulin receptor substrate 1 expression in normal myometrium and leiomyoma.	Tyrosine	127-130	insulin receptor	Homo sapiens	46-48
16102994-3	2005	They contain an active insulin receptor and respond to insulin by increasing phosphorylation of tyrosine residues in several proteins.	Tyrosine	96-104	insulin receptor	Homo sapiens	23-39
16137651-0	2005	Natural anti-diabetic compound 1,2,3,4,6-penta-O-galloyl-D-glucopyranose binds to insulin receptor and activates insulin-mediated glucose transport signaling pathway.	[(2R,3R,4S,5R)-3,4,5,6-tetrakis[(2-deuterio-3,4,5-trihydroxybenzoyl)oxy]oxan-2-yl]methyl 2-deuterio-3,4,5-trihydroxybenzoate	31-72	insulin receptor	Homo sapiens	82-98
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	alphaPGG	39-48	insulin receptor	Homo sapiens	192-208
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	alphaPGG	39-48	insulin receptor	Homo sapiens	210-212
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	Glucose	141-148	insulin receptor	Homo sapiens	192-208
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	Glucose	243-250	insulin receptor	Homo sapiens	192-208
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	Glucose	243-250	insulin receptor	Homo sapiens	210-212
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	alphaPGG	274-283	insulin receptor	Homo sapiens	192-208
16137651-4	2005	Mechanistic studies in adipocytes with alpha-PGG, the more potent of the two anomers, reveal that inhibitors that block the insulin-mediated glucose transport, including one that inhibits the insulin receptor (IR), also completely abolish the glucose transport activated by alpha-PGG.	alphaPGG	274-283	insulin receptor	Homo sapiens	210-212
16137651-5	2005	In addition, alpha-PGG induces phosphorylation of the IR and Akt, activates PI 3-kinase, and stimulates membrane translocation of GLUT 4.	alphaPGG	13-22	insulin receptor	Homo sapiens	54-56
16137651-6	2005	Receptor binding studies indicate that alpha-PGG binds to the IR and affects the binding between insulin and IR by reducing the maximum binding of insulin to IR without significantly altering the binding affinity of insulin to IR.	alphaPGG	39-48	insulin receptor	Homo sapiens	62-64
16137651-6	2005	Receptor binding studies indicate that alpha-PGG binds to the IR and affects the binding between insulin and IR by reducing the maximum binding of insulin to IR without significantly altering the binding affinity of insulin to IR.	alphaPGG	39-48	insulin receptor	Homo sapiens	109-111
16137651-6	2005	Receptor binding studies indicate that alpha-PGG binds to the IR and affects the binding between insulin and IR by reducing the maximum binding of insulin to IR without significantly altering the binding affinity of insulin to IR.	alphaPGG	39-48	insulin receptor	Homo sapiens	109-111
16137651-7	2005	Western blotting analysis of the products of a cross-linking reaction suggests that alpha-PGG may bind to IR at a site located on the alpha-subunit of the receptor.	alphaPGG	84-93	insulin receptor	Homo sapiens	106-108
16020478-1	2005	Insulin receptor substrate 1 (IRS-1), an intracellular substrate of the insulin receptor tyrosine kinase, also is heavily phosphorylated on serine and threonine residues, and several serine phosphorylation sites alter the function of IRS-1.	Serine	140-146	insulin receptor	Homo sapiens	72-88
16020478-1	2005	Insulin receptor substrate 1 (IRS-1), an intracellular substrate of the insulin receptor tyrosine kinase, also is heavily phosphorylated on serine and threonine residues, and several serine phosphorylation sites alter the function of IRS-1.	Serine	183-189	insulin receptor	Homo sapiens	72-88
16099589-6	2005	Blocking endogenous autocrine insulin signaling in quiescent beta-cells with the insulin receptor inhibitor HMNPA led to a reduction in insulin synthesis, suggesting some degree of basal activity of this positive feed-forward loop.	hmnpa	108-113	insulin receptor	Homo sapiens	81-97
16045742-6	2005	Besides, tyrosine phosphorylation of Sam68 allows the formation of signalling complexes with other proteins containing SH2 and SH3 domains, suggesting a role in signal transduction of different systems in human lymphocytes, such as the T cell receptor, and leptin receptor, or the insulin receptor in other cell types.	Tyrosine	9-17	insulin receptor	Homo sapiens	281-297
15924436-3	2005	Different chromium(III) compounds were effective at enhancing insulin receptor phosphorylation in intact cells, but did not directly activate recombinant insulin receptor kinase.	tris(1,10-phenanthroline)chromium(III) chloride	10-23	insulin receptor	Homo sapiens	62-78
15737992-5	2005	APS is phosphorylated by the insulin receptor on a C-terminal tyrosine residue, which then serves as a binding site for the Cbl TKB domain.	Adenosine Phosphosulfate	0-3	insulin receptor	Homo sapiens	29-45
15737992-5	2005	APS is phosphorylated by the insulin receptor on a C-terminal tyrosine residue, which then serves as a binding site for the Cbl TKB domain.	Tyrosine	62-70	insulin receptor	Homo sapiens	29-45
15713122-1	2005	Serine and threonine phosphorylation of IRS-1 (insulin receptor substrate-1) has been reported to decrease its ability to be tyrosine-phosphorylated by the insulin receptor.	Serine	0-6	insulin receptor	Homo sapiens	47-63
15713122-1	2005	Serine and threonine phosphorylation of IRS-1 (insulin receptor substrate-1) has been reported to decrease its ability to be tyrosine-phosphorylated by the insulin receptor.	Threonine	11-20	insulin receptor	Homo sapiens	47-63
15713122-1	2005	Serine and threonine phosphorylation of IRS-1 (insulin receptor substrate-1) has been reported to decrease its ability to be tyrosine-phosphorylated by the insulin receptor.	Tyrosine	125-133	insulin receptor	Homo sapiens	47-63
15952059-2	2005	One mechanism recently identified to downregulate IGF-I or insulin receptor signaling in diabetic models is IRS-1 Ser(312) phosphorylation.	Serine	114-117	insulin receptor	Homo sapiens	59-75
15764603-0	2005	Differential contribution of insulin receptor substrates 1 versus 2 to insulin signaling and glucose uptake in l6 myotubes.	Glucose	93-100	insulin receptor	Homo sapiens	29-45
15611135-4	2005	Interestingly, a positively charged pocket is located near the PTPL1 catalytic site, reminiscent of the second phosphotyrosine binding site in PTP1B, which is required to dephosphorylate peptides containing two adjacent phosphotyrosine residues (as occurs for example in the activated insulin receptor).	Phosphotyrosine	111-126	insulin receptor	Homo sapiens	285-301
15694368-2	2005	We analyzed the effect of AICAR, an AMPK activator, on the expression of insulin receptor in a human hepatoma cell line, HepG2 cells.	AICA ribonucleotide	26-31	insulin receptor	Homo sapiens	73-89
15694368-6	2005	Dipyridamole, an adenosine transporter inhibitor, and 5"-amino-5"-deoxyadenosine, an adenosine kinase inhibitor, blocked the effect of AICAR on the down-regulation of the insulin receptor protein, mRNA, and promoter activity.	Dipyridamole	0-12	insulin receptor	Homo sapiens	171-187
15694368-6	2005	Dipyridamole, an adenosine transporter inhibitor, and 5"-amino-5"-deoxyadenosine, an adenosine kinase inhibitor, blocked the effect of AICAR on the down-regulation of the insulin receptor protein, mRNA, and promoter activity.	5'-amino-5'-deoxyadenosine	54-80	insulin receptor	Homo sapiens	171-187
15611135-5	2005	We demonstrate that PTPL1, like PTP1B, interacts with and dephosphorylates a bis-phosphorylated insulin receptor peptide more efficiently than monophosphorylated peptides, indicating that PTPL1 may down-regulate the phosphatidylinositol 3-kinase pathway, by dephosphorylating insulin or growth factor receptors that contain tandem phosphotyrosines.	Phosphotyrosine	331-347	insulin receptor	Homo sapiens	96-112
15677493-6	2005	The extent and time course of insulin receptor phosphorylation and activation of downstream signaling elements after insulin glulisine treatment was similar to that of human regular insulin in vivo.	glulisine	125-134	insulin receptor	Homo sapiens	30-46
15613682-1	2005	Insulin resistance in polycystic ovary syndrome (PCOS) is due to a postbinding defect in signaling that persists in cultured skin fibroblasts and is associated with constitutive serine phosphorylation of the insulin receptor (IR).	Serine	178-184	insulin receptor	Homo sapiens	208-224
15563471-2	2005	Using purified recombinant IRK fragments and the isolated intact insulin receptor, we show here that autophosphorylation is inhibited by ADP and that this effect is essentially reversed by hydrogen peroxide.	Adenosine Diphosphate	137-140	insulin receptor	Homo sapiens	65-81
15563471-2	2005	Using purified recombinant IRK fragments and the isolated intact insulin receptor, we show here that autophosphorylation is inhibited by ADP and that this effect is essentially reversed by hydrogen peroxide.	Hydrogen Peroxide	189-206	insulin receptor	Homo sapiens	65-81
15733745-10	2005	Moreover, inhibition of IR processing with tunicamycin indicated that the basal interaction of PTP1B with IR occurred during biosynthesis of the IR precursor in the endoplasmic reticulum.	Tunicamycin	43-54	insulin receptor	Homo sapiens	24-26
15733745-10	2005	Moreover, inhibition of IR processing with tunicamycin indicated that the basal interaction of PTP1B with IR occurred during biosynthesis of the IR precursor in the endoplasmic reticulum.	Tunicamycin	43-54	insulin receptor	Homo sapiens	106-108
15733745-10	2005	Moreover, inhibition of IR processing with tunicamycin indicated that the basal interaction of PTP1B with IR occurred during biosynthesis of the IR precursor in the endoplasmic reticulum.	Tunicamycin	43-54	insulin receptor	Homo sapiens	106-108
15494022-3	2004	This article focuses on the Ser/Thr protein kinases which phosphorylate insulin receptor substrates and the major Ser sites that are phosphorylated, as key elements in the uncoupling of insulin signalling and the induction of an insulin resistance state.	Serine	28-31	insulin receptor	Homo sapiens	72-88
15677487-6	2005	PTPs normally serve as negative regulators of insulin action via the dephosphorylation of the insulin receptor and its tyrosine-phosphorylated cellular substrates.	Tyrosine	119-127	insulin receptor	Homo sapiens	94-110
15581361-1	2004	Cbl is phosphorylated by the insulin receptor and reportedly functions within the flotillin/CAP/Cbl/Crk/C3G/TC10 complex during insulin-stimulated glucose transport in 3T3/L1 adipocytes.	Glucose	147-154	insulin receptor	Homo sapiens	29-45
15589136-1	2004	Recent studies show that hyperactivated mTOR, the "target of rapamycin" that senses nutrient availability in eukaryotic cells, inhibits signaling by insulin receptor substrates.	Sirolimus	61-70	insulin receptor	Homo sapiens	149-165
20704943-6	2004	One gene that is located in 20q is PTPN1, which encodes the PTP1B protein, a ubiquitously expressed phosphatase (protein tyrosine phosphatase 1B), which dephosphorylates phosphorylated tyrosine residues of the active insulin receptor protein thereby disrupting the insulin signaling pathway.	Tyrosine	121-129	insulin receptor	Homo sapiens	217-233
15541479-1	2005	In this study, we demonstrate that 17beta-estradiol (E(2)) inhibits human insulin receptor (IR) gene expression in a dose- and time-dependent manner in U-937 human promonocytic cells.	Estradiol	35-51	insulin receptor	Homo sapiens	74-95
15504985-2	2004	PTP-1B has been implicated in negatively regulating insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor.	Phosphotyrosine	95-110	insulin receptor	Homo sapiens	127-143
15610610-4	2004	As a potential tool to rescue glucose homeostasis at will in both insulin and insulin receptor deficiencies, we developed a recombinant chimeric insulin receptor (LFv2IRE) that can be homodimerized and activated by the small-molecule dimerizer AP20187.	Glucose	30-37	insulin receptor	Homo sapiens	145-161
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Chromium	53-55	insulin receptor	Homo sapiens	133-149
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Chromium	53-55	insulin receptor	Homo sapiens	151-153
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Zinc	60-62	insulin receptor	Homo sapiens	133-149
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Zinc	60-62	insulin receptor	Homo sapiens	151-153
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Tyrosine	105-113	insulin receptor	Homo sapiens	133-149
15516700-4	2004	In the present study, it has been observed that both Cr and Zn, upon prolonged exposure, could stimulate tyrosine phosphorylation of insulin receptor (IR) even in the absence of insulin.	Tyrosine	105-113	insulin receptor	Homo sapiens	151-153
15516700-5	2004	Insulin-mediated IR tyrosine phosphorylation was enhanced by the treatment with both of the metal ions.	Tyrosine	20-28	insulin receptor	Homo sapiens	17-19
15516700-5	2004	Insulin-mediated IR tyrosine phosphorylation was enhanced by the treatment with both of the metal ions.	Metals	92-97	insulin receptor	Homo sapiens	17-19
15476672-2	2004	This effect is associated with inhibition of insulin receptor (IR) and insulin-like growth factor-I receptor (IGF-IR) autophosphorylation, which implicates these receptors as direct targets for ethanol.	Ethanol	194-201	insulin receptor	Homo sapiens	45-66
15476672-3	2004	It was demonstrated previously that ethanol inhibits the autophosphorylation and kinase activity of the purified cytoplasmic tyrosine kinase domain of the IR.	Ethanol	36-43	insulin receptor	Homo sapiens	155-157
15476672-4	2004	We performed computer modeling of the ethanol interaction with the IR and IGF-IR kinases (IRK and IGF-IRK).	Ethanol	38-45	insulin receptor	Homo sapiens	67-69
15281015-9	2004	While binding of glargine to the insulin receptor was identical to insulin, degradation of glargine was reduced compared to insulin (16.3% +/- 0.3% v 21.6% +/- 0.4% degraded/h, P < .01).	Insulin Glargine	17-25	insulin receptor	Homo sapiens	33-49
15258906-9	2004	These results suggest, therefore, that IR activators such as TLK19781 may be useful in treating the insulin resistance associated with PIs.	Monothiopyrophosphoric acid	135-138	insulin receptor	Homo sapiens	39-41
15382121-3	2004	DCA and taurodeoxycholic acid (TDCA) (100 micromol/L) caused activation of ERBB1, insulin receptor, and the ERK1/2 and AKT pathways in primary rodent hepatocytes.	Deoxycholic Acid	0-3	insulin receptor	Homo sapiens	82-98
15382121-3	2004	DCA and taurodeoxycholic acid (TDCA) (100 micromol/L) caused activation of ERBB1, insulin receptor, and the ERK1/2 and AKT pathways in primary rodent hepatocytes.	Taurodeoxycholic Acid	8-29	insulin receptor	Homo sapiens	82-98
15069075-0	2004	Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1.	Tyrosine	157-165	insulin receptor	Homo sapiens	59-75
15025562-4	2004	The activation of IR autophosphorylation by insulin was blocked by G-protein inactivation through GDPbetaS (guanosine 5"-[beta-thio]disphosphate).	guanosine 5"-[beta-thio]disphosphate	108-144	insulin receptor	Homo sapiens	18-20
15075343-1	2004	The insulin receptor is a transmembrane protein dimer composed of two alphabeta monomers held together by inter-alpha-chain disulfide bonds.	Disulfides	124-133	insulin receptor	Homo sapiens	4-20
15075343-2	2004	In a previous report we described a monomeric insulin receptor obtained by replacing Cys-524, -682, -683, and -685 with serine.	Cysteine	85-88	insulin receptor	Homo sapiens	46-62
15075343-2	2004	In a previous report we described a monomeric insulin receptor obtained by replacing Cys-524, -682, -683, and -685 with serine.	Serine	120-126	insulin receptor	Homo sapiens	46-62
14722023-12	2004	IGF-I 10(-7) M stimulated incorporation of [(3)H]thymidine into DNA, and 10(-9)-10(-7) M also the incorporation of [(3)H]glucose in HMVEC, whereas glargine and insulin had no significant effects at 10(-9)-10(-7) M. Human micro- and macrovascular endothelial cells express more IGF-IR than IR.	[(3)h]glucose	115-128	insulin receptor	Homo sapiens	281-283
15169905-3	2004	In concordance with these increases by LPS, tyrosine phosphorylation of the insulin receptor (IR) is partially impaired and phosphorylation of the insulin receptor substrate (IRS) proteins is almost completely suppressed.	Tyrosine	44-52	insulin receptor	Homo sapiens	76-92
15169905-3	2004	In concordance with these increases by LPS, tyrosine phosphorylation of the insulin receptor (IR) is partially impaired and phosphorylation of the insulin receptor substrate (IRS) proteins is almost completely suppressed.	Tyrosine	44-52	insulin receptor	Homo sapiens	94-96
15135305-0	2004	Metformin (Glucophage) inhibits tyrosine phosphatase activity to stimulate the insulin receptor tyrosine kinase.	Metformin	0-9	insulin receptor	Homo sapiens	79-95
15135305-0	2004	Metformin (Glucophage) inhibits tyrosine phosphatase activity to stimulate the insulin receptor tyrosine kinase.	Metformin	11-21	insulin receptor	Homo sapiens	79-95
15135305-1	2004	Metformin is a commonly used anti-diabetic but whether its mechanism involves action on the insulin receptor or on downstream events is still controversial.	Metformin	0-9	insulin receptor	Homo sapiens	92-108
15135305-2	2004	With a time course that was slow compared with insulin action, metformin increased tyrosine phosphorylation of the regulatory domain of the insulin receptor (specifically, tyrosine residues 1150 and 1151).	Metformin	63-72	insulin receptor	Homo sapiens	140-156
15135305-2	2004	With a time course that was slow compared with insulin action, metformin increased tyrosine phosphorylation of the regulatory domain of the insulin receptor (specifically, tyrosine residues 1150 and 1151).	Tyrosine	83-91	insulin receptor	Homo sapiens	140-156
15135305-2	2004	With a time course that was slow compared with insulin action, metformin increased tyrosine phosphorylation of the regulatory domain of the insulin receptor (specifically, tyrosine residues 1150 and 1151).	Tyrosine	172-180	insulin receptor	Homo sapiens	140-156
15135305-3	2004	In a direct action, therapeutic levels of metformin stimulated the tyrosine kinase activity of the soluble intracellular portion of the beta subunit of the human insulin receptor toward a substrate derived from the insulin receptor regulatory domain.	Metformin	42-51	insulin receptor	Homo sapiens	162-178
15135305-3	2004	In a direct action, therapeutic levels of metformin stimulated the tyrosine kinase activity of the soluble intracellular portion of the beta subunit of the human insulin receptor toward a substrate derived from the insulin receptor regulatory domain.	Metformin	42-51	insulin receptor	Homo sapiens	215-231
15135305-5	2004	Using a Xenopus oocyte preparation, we simultaneously recorded tyrosine kinase and phosphatase activities that regulate the insulin receptor by measuring the tyrosine phosphorylation and dephosphorylation of peptides derived from the regulatory domain of the human insulin receptor.	Tyrosine	63-71	insulin receptor	Homo sapiens	124-140
15135305-6	2004	In an indirect stimulation of the insulin receptor, metformin inhibited endogenous tyrosine phosphatases and purified human protein tyrosine phosphatase 1B that dephosphorylate and inhibit the insulin receptor kinase.	Metformin	52-61	insulin receptor	Homo sapiens	34-50
15135305-6	2004	In an indirect stimulation of the insulin receptor, metformin inhibited endogenous tyrosine phosphatases and purified human protein tyrosine phosphatase 1B that dephosphorylate and inhibit the insulin receptor kinase.	Metformin	52-61	insulin receptor	Homo sapiens	193-209
15135305-7	2004	Thus, there was evidence that metformin acted directly upon the insulin receptor and indirectly through inhibition of tyrosine phosphatases.	Metformin	30-39	insulin receptor	Homo sapiens	64-80
15059979-5	2004	Glucosamine treatment resulted in inhibition of tyrosine-phosphorylation of the insulin receptor (IR), IRS-1, and IRS-2, which was associated with increased O-glycosylation.	Glucosamine	0-11	insulin receptor	Homo sapiens	80-96
15059979-5	2004	Glucosamine treatment resulted in inhibition of tyrosine-phosphorylation of the insulin receptor (IR), IRS-1, and IRS-2, which was associated with increased O-glycosylation.	Glucosamine	0-11	insulin receptor	Homo sapiens	98-100
15059979-5	2004	Glucosamine treatment resulted in inhibition of tyrosine-phosphorylation of the insulin receptor (IR), IRS-1, and IRS-2, which was associated with increased O-glycosylation.	Tyrosine	48-56	insulin receptor	Homo sapiens	80-96
15059979-5	2004	Glucosamine treatment resulted in inhibition of tyrosine-phosphorylation of the insulin receptor (IR), IRS-1, and IRS-2, which was associated with increased O-glycosylation.	Tyrosine	48-56	insulin receptor	Homo sapiens	98-100
15059979-7	2004	BADGP reversed the glucosamine-induced reduction in insulin-stimulated phosphorylation of IR, IRS-1, IRS-2, Akt, GSK-3, and FOXO1a.	Glucosamine	19-30	insulin receptor	Homo sapiens	90-92
15095290-0	2004	Na+/Mg2+ exchange is functionally coupled to the insulin receptor.	magnesium ion	4-8	insulin receptor	Homo sapiens	49-65
15037518-8	2004	Purified IR was phosphorylated in vitro with insulin in the presence of various synthetic peptides and lignocaine.	Peptides	90-98	insulin receptor	Homo sapiens	9-11
15037518-8	2004	Purified IR was phosphorylated in vitro with insulin in the presence of various synthetic peptides and lignocaine.	Lidocaine	103-113	insulin receptor	Homo sapiens	9-11
15037518-9	2004	The phosphorylation level of IR was then evaluated after SDS-PAGE separation, followed by Western blot analysis with antiphosphotyrosine antibody.	Sodium Dodecyl Sulfate	57-60	insulin receptor	Homo sapiens	29-31
15037518-16	2004	These results indicate that KIFMK, KIYEK, and lignocaine bind with the autophosphorylation sites of IR.	Lidocaine	46-56	insulin receptor	Homo sapiens	100-102
15135155-5	2004	Insulin-induced tyrosine phosphorylation of the insulin receptor was not affected by DMAP.	Tyrosine	16-24	insulin receptor	Homo sapiens	48-64
15094074-2	2004	In the central nervous system (CNS), insulin and the insulin receptor are found in specific brain regions where they show evidence of participation in a variety of region-specific functions through mechanisms that are different from its direct glucose regulation in the periphery.	Glucose	244-251	insulin receptor	Homo sapiens	53-69
15094078-7	2004	In late-onset sporadic Alzheimer disease, the neuronal insulin receptor may be desensitized by inhibition of receptor function at different sites by noradrenaline and/or cortisol, the levels of which both increase with increasing age.	Norepinephrine	149-162	insulin receptor	Homo sapiens	55-71
15094078-7	2004	In late-onset sporadic Alzheimer disease, the neuronal insulin receptor may be desensitized by inhibition of receptor function at different sites by noradrenaline and/or cortisol, the levels of which both increase with increasing age.	Hydrocortisone	170-178	insulin receptor	Homo sapiens	55-71
15118262-0	2004	K(ATP) channel knockout mice crossbred with transgenic mice expressing a dominant-negative form of human insulin receptor have glucose intolerance but not diabetes.	Glucose	127-134	insulin receptor	Homo sapiens	105-121
15072575-6	2004	Conversely, chemicals known to inhibit the mammalian insulin receptor or downstream elements of its signaling pathway, such as LY294002, an inhibitor of phosphatidylinositol 3-kinase (PI3K), were able to prevent the steroidogenic action of bovine insulin on fly ovaries.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	127-135	insulin receptor	Homo sapiens	53-69
15117549-4	2004	Insulin-induced DNA synthesis and c-Jun protein expression were also reduced by ethanol treatment in Rat-1 fibroblasts overexpressing normal human insulin receptor.	Ethanol	80-87	insulin receptor	Homo sapiens	147-163
14986111-3	2004	As nitric oxide is reported to be a systemic anticancer agent, studies were carried out to determine the role of insulin receptor binding that lead to the activation of tyrosine kinase and IANOS in erythrocytes in breast cancer.	Nitric Oxide	3-15	insulin receptor	Homo sapiens	113-129
14966267-1	2004	Insulin stimulation of target cells elicits a burst of H(2)O(2) that enhances tyrosine phosphorylation of the insulin receptor and its cellular substrate proteins as well as distal signaling events in the insulin action cascade.	Tyrosine	78-86	insulin receptor	Homo sapiens	110-126
14966267-6	2004	Overexpression of Nox4 also significantly reversed the inhibition of insulin-stimulated IR tyrosine phosphorylation induced by coexpression of PTP1B by inhibiting PTP1B catalytic activity.	Tyrosine	91-99	insulin receptor	Homo sapiens	88-90
14966267-7	2004	These data suggest that Nox4 provides a novel link between the IR and the generation of cellular reactive oxygen species that enhance insulin signal transduction, at least in part via the oxidative inhibition of cellular protein-tyrosine phosphatases (PTPases), including PTP1B, a PTPase that has been previously implicated in the regulation of insulin action.	Reactive Oxygen Species	97-120	insulin receptor	Homo sapiens	63-65
15117549-6	2004	However, association of the insulin receptor and IRS-1 with the Src homology 2 domain of the p85 subunit of phosphatidylinositol 3-kinase (PI3-kinase) was reduced by ethanol.	Ethanol	166-173	insulin receptor	Homo sapiens	28-44
15117549-8	2004	These results suggest that ethanol specifically inhibits the association of the insulin receptor and IRS-1 with the p85 subunit of PI3-kinase, which is required for increased glucose uptake, DNA synthesis, and c-Jun expression by insulin.	Ethanol	27-34	insulin receptor	Homo sapiens	80-96
15117549-8	2004	These results suggest that ethanol specifically inhibits the association of the insulin receptor and IRS-1 with the p85 subunit of PI3-kinase, which is required for increased glucose uptake, DNA synthesis, and c-Jun expression by insulin.	Glucose	175-182	insulin receptor	Homo sapiens	80-96
15070438-7	2004	Chromodulin may be the key to understanding the role of Cr at a molecular level, as the molecule has been found to bind to activated insulin receptor, stimulating its kinase activity.	Chromium	56-58	insulin receptor	Homo sapiens	133-149
14583092-8	2004	These results indicate that PKCdelta modulates the ability of the insulin receptor to tyrosine-phosphorylate IRS-1 by direct phosphorylation of the IRS-1 molecule.	Tyrosine	86-94	insulin receptor	Homo sapiens	66-82
14656737-2	2004	Structural changes in a long-acting insulin analog, insulin glargine, may change its binding properties to insulin receptor and structurally homologous receptors, such as the insulin-like growth factor-1 receptor, and thereby alter its vascular effects.	Insulin Glargine	60-68	insulin receptor	Homo sapiens	107-123
14767998-7	2004	Bile acids caused activation of GS to a similar level induced by insulin (50 nM); both were blocked by inhibition of insulin receptor function and the PI3 kinase/AKT/GSK3 pathway.	Bile Acids and Salts	0-10	insulin receptor	Homo sapiens	117-133
15289656-1	2004	Insulin receptor signal transduction plays a critical role in regulating pancreatic beta-cell function, notably the acute first-phase insulin release in response to glucose.	Glucose	165-172	insulin receptor	Homo sapiens	0-16
14583092-2	2004	In the present study, we have explored the possibility of a novel PKC, PKCdelta, to modulate directly the ability of the insulin receptor kinase to tyrosine-phosphorylate IRS-1.	Tyrosine	148-156	insulin receptor	Homo sapiens	121-137
14583092-4	2004	Activated PKCdelta was also found to inhibit the IRS-1 tyrosine phosphorylation in vitro by purified insulin receptor using recombinant full-length human IRS-1 and a partial IRS-1-glutathione S-transferase-fusion protein as substrates.	Tyrosine	55-63	insulin receptor	Homo sapiens	101-117
15289656-6	2004	Manipulations aimed at reducing expression of physiologically relevant PTPases acting at a step proximal to the insulin receptor are accompanied by normalization of blood glucose levels and improved insulin sensitivity in both normal and diabetic animals.	Glucose	171-178	insulin receptor	Homo sapiens	112-128
14641043-3	2003	Down-regulation of insulin receptor tyrosine phosphorylation and subsequent steps in the insulin signalling pathway, including insulin receptor substrate-1 (IRS-1)-associated phosphoinositide 3-kinase (PI3K), Akt kinase serine phosphorylation and activity and glucose transporter (GLUT-4) protein content, are evident in skeletal muscle after eccentric exercise.	Tyrosine	36-44	insulin receptor	Homo sapiens	19-35
14693696-4	2004	In 3T3-L1 adipocytes, DHEA increases tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and IRS-2 and stimulates IRS-1- and IRS-2-associated phosphatidylinositol (PI) 3-kinase activity with no effects on either insulin receptor or Akt phosphorylation.	Dehydroepiandrosterone	22-26	insulin receptor	Homo sapiens	65-81
14693696-4	2004	In 3T3-L1 adipocytes, DHEA increases tyrosine phosphorylation of insulin receptor substrate (IRS)-1 and IRS-2 and stimulates IRS-1- and IRS-2-associated phosphatidylinositol (PI) 3-kinase activity with no effects on either insulin receptor or Akt phosphorylation.	Tyrosine	37-45	insulin receptor	Homo sapiens	65-81
14641043-3	2003	Down-regulation of insulin receptor tyrosine phosphorylation and subsequent steps in the insulin signalling pathway, including insulin receptor substrate-1 (IRS-1)-associated phosphoinositide 3-kinase (PI3K), Akt kinase serine phosphorylation and activity and glucose transporter (GLUT-4) protein content, are evident in skeletal muscle after eccentric exercise.	Serine	220-226	insulin receptor	Homo sapiens	19-35
14690593-1	2003	The adaptor protein APS is a substrate of the insulin receptor and couples receptor activation with phosphorylation of Cbl to facilitate glucose uptake.	Glucose	137-144	insulin receptor	Homo sapiens	46-62
12925525-0	2003	The antidiabetic agent sodium tungstate activates glycogen synthesis through an insulin receptor-independent pathway.	sodium tungstate(VI)	23-39	insulin receptor	Homo sapiens	80-96
14641043-5	2003	Recent studies have shown that TNF-alpha can increase IRS-1 serine/threonine phosphorylation, which impairs IRS-1 docking to the insulin receptor, and this inhibits insulin signalling.	Serine	60-66	insulin receptor	Homo sapiens	129-145
14641043-5	2003	Recent studies have shown that TNF-alpha can increase IRS-1 serine/threonine phosphorylation, which impairs IRS-1 docking to the insulin receptor, and this inhibits insulin signalling.	Threonine	67-76	insulin receptor	Homo sapiens	129-145
12925525-0	2003	The antidiabetic agent sodium tungstate activates glycogen synthesis through an insulin receptor-independent pathway.	Glycogen	50-58	insulin receptor	Homo sapiens	80-96
14576451-3	2003	This article, describes recent studies that link the photobleaching of rhodopsin to tyrosine phosphorylation of the insulin receptor and subsequent activation of phosphoinositide 3- kinase (PI3K).	Tyrosine	84-92	insulin receptor	Homo sapiens	116-132
12948866-0	2003	Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes.	Thioctic Acid	0-17	insulin receptor	Homo sapiens	52-68
12948866-0	2003	Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes.	Sulfhydryl Compounds	28-33	insulin receptor	Homo sapiens	52-68
12948866-2	2003	In this study, alpha-lipoic acid was demonstrated to stimulate the autophosphorylation of insulin receptor and glucose uptake into 3T3-L1 adipocytes by reducing the thiol reactivity of intracellular proteins.	Thioctic Acid	15-32	insulin receptor	Homo sapiens	90-106
12948866-2	2003	In this study, alpha-lipoic acid was demonstrated to stimulate the autophosphorylation of insulin receptor and glucose uptake into 3T3-L1 adipocytes by reducing the thiol reactivity of intracellular proteins.	Sulfhydryl Compounds	165-170	insulin receptor	Homo sapiens	90-106
12948866-3	2003	To elucidate mechanism of this effect, role of protein thiol groups and H(2)O(2) in insulin receptor autophosphorylation and glucose uptake was investigated in 3T3-L1 adipocytes following stimulation with alpha-lipoic acid.	Thioctic Acid	205-222	insulin receptor	Homo sapiens	84-100
12948866-4	2003	Alpha-lipoic acid or insulin treatment of adipocytes increased intracellular level of oxidants, decreased thiol reactivity of the insulin receptor beta-subunit, increased tyrosine phosphorylation of the insulin receptor, and enhanced glucose uptake.	Thioctic Acid	0-17	insulin receptor	Homo sapiens	130-146
12948866-4	2003	Alpha-lipoic acid or insulin treatment of adipocytes increased intracellular level of oxidants, decreased thiol reactivity of the insulin receptor beta-subunit, increased tyrosine phosphorylation of the insulin receptor, and enhanced glucose uptake.	Thioctic Acid	0-17	insulin receptor	Homo sapiens	203-219
12948866-4	2003	Alpha-lipoic acid or insulin treatment of adipocytes increased intracellular level of oxidants, decreased thiol reactivity of the insulin receptor beta-subunit, increased tyrosine phosphorylation of the insulin receptor, and enhanced glucose uptake.	Sulfhydryl Compounds	106-111	insulin receptor	Homo sapiens	130-146
12948866-4	2003	Alpha-lipoic acid or insulin treatment of adipocytes increased intracellular level of oxidants, decreased thiol reactivity of the insulin receptor beta-subunit, increased tyrosine phosphorylation of the insulin receptor, and enhanced glucose uptake.	Tyrosine	171-179	insulin receptor	Homo sapiens	203-219
12948866-5	2003	Alpha-lipoic acid or insulin-stimulated glucose uptake was inhibited (i) by alkylation of intracellular, but not extracellular, thiol groups downstream of insulin receptor activation, and (ii) by diphenylene iodonium at the level of the insulin receptor autophosphorylation.	Thioctic Acid	0-17	insulin receptor	Homo sapiens	155-171
12948866-5	2003	Alpha-lipoic acid or insulin-stimulated glucose uptake was inhibited (i) by alkylation of intracellular, but not extracellular, thiol groups downstream of insulin receptor activation, and (ii) by diphenylene iodonium at the level of the insulin receptor autophosphorylation.	Thioctic Acid	0-17	insulin receptor	Homo sapiens	237-253
12948866-5	2003	Alpha-lipoic acid or insulin-stimulated glucose uptake was inhibited (i) by alkylation of intracellular, but not extracellular, thiol groups downstream of insulin receptor activation, and (ii) by diphenylene iodonium at the level of the insulin receptor autophosphorylation.	Glucose	40-47	insulin receptor	Homo sapiens	155-171
12948866-5	2003	Alpha-lipoic acid or insulin-stimulated glucose uptake was inhibited (i) by alkylation of intracellular, but not extracellular, thiol groups downstream of insulin receptor activation, and (ii) by diphenylene iodonium at the level of the insulin receptor autophosphorylation.	Glucose	40-47	insulin receptor	Homo sapiens	237-253
14520603-7	2003	This effect most likely results from tyrosine phosphorylation of insulin receptor substrates (IRSs) by PIG41.	Tyrosine	37-45	insulin receptor	Homo sapiens	65-81
12948866-5	2003	Alpha-lipoic acid or insulin-stimulated glucose uptake was inhibited (i) by alkylation of intracellular, but not extracellular, thiol groups downstream of insulin receptor activation, and (ii) by diphenylene iodonium at the level of the insulin receptor autophosphorylation.	diphenyleneiodonium	196-216	insulin receptor	Homo sapiens	237-253
12948866-7	2003	These findings indicate that oxidants produced by alpha-lipoic acid or insulin are involved in activation of insulin receptor and in inactivation of protein tyrosine phosphatases, which eventually result in elevated glucose uptake into 3T3-L1 adipocytes.	Thioctic Acid	50-67	insulin receptor	Homo sapiens	109-125
12948866-7	2003	These findings indicate that oxidants produced by alpha-lipoic acid or insulin are involved in activation of insulin receptor and in inactivation of protein tyrosine phosphatases, which eventually result in elevated glucose uptake into 3T3-L1 adipocytes.	Glucose	216-223	insulin receptor	Homo sapiens	109-125
12882906-1	2003	Stimulation of glucose transport by insulin involves tyrosine phosphorylation of the insulin receptor (IR) and IR substrates (IRSs).	Glucose	15-22	insulin receptor	Homo sapiens	85-101
12882906-1	2003	Stimulation of glucose transport by insulin involves tyrosine phosphorylation of the insulin receptor (IR) and IR substrates (IRSs).	Glucose	15-22	insulin receptor	Homo sapiens	103-105
12882906-1	2003	Stimulation of glucose transport by insulin involves tyrosine phosphorylation of the insulin receptor (IR) and IR substrates (IRSs).	Glucose	15-22	insulin receptor	Homo sapiens	111-113
12882906-1	2003	Stimulation of glucose transport by insulin involves tyrosine phosphorylation of the insulin receptor (IR) and IR substrates (IRSs).	Tyrosine	53-61	insulin receptor	Homo sapiens	85-101
12882906-1	2003	Stimulation of glucose transport by insulin involves tyrosine phosphorylation of the insulin receptor (IR) and IR substrates (IRSs).	Tyrosine	53-61	insulin receptor	Homo sapiens	103-105
12882909-2	2003	To determine whether the TZD-induced improvement in glycemic control is associated with enhanced insulin receptor signaling in skeletal muscle, 20 type 2 diabetic patients received a 75-g oral glucose tolerance test (OGTT) and euglycemic insulin (80 mU x m(-2) x min(-1)) clamp with [3-(3)H]glucose/indirect calorimetry/vastus lateralis muscle biopsies before and after 16 weeks of rosiglitazone treatment.	2,4-thiazolidinedione	25-28	insulin receptor	Homo sapiens	97-113
12882909-9	2003	In conclusion, in type 2 diabetic patients, rosiglitazone treatment enhances downstream insulin receptor signaling in muscle and decreases plasma FFA concentration while improving glycemic control.	Rosiglitazone	44-57	insulin receptor	Homo sapiens	88-104
14593614-3	2003	The insulin receptor exhibits a tyrosine-kinase activity which leads, first, to receptor autophosphorylation and then to tyrosine phosphorylation of substrates proteins, IRS proteins in priority.	Tyrosine	32-40	insulin receptor	Homo sapiens	4-20
12707268-0	2003	Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor.	Tyrosine	67-75	insulin receptor	Homo sapiens	115-131
12707268-1	2003	Tyrosine 984 in the juxtamembrane region of the insulin receptor, between the transmembrane helix and the cytoplasmic tyrosine kinase domain, is conserved among all insulin receptor-like proteins from hydra to humans.	Tyrosine	0-8	insulin receptor	Homo sapiens	48-64
12832322-2	2003	MyD is dominantly inherited and is due to heterozygosity for a trinucleotide repeat expansion mutation in a protein kinase gene able to induce derangement of RNA metabolism responsible of an aberrant insulin receptor expression.	trinucleotide	63-76	insulin receptor	Homo sapiens	200-216
12738810-4	2003	Furthermore, we find that alterations in insulin expression and secretion caused by chronic exposure to high glucose are paralleled by decreased insulin receptor expression and increased relative abundance of the Ex11+ isoform in both human islets and RIN beta-cells.	Glucose	109-116	insulin receptor	Homo sapiens	145-161
12876303-8	2003	In addition, H2O2 inhibited insulin receptor binding partially and inhibited insulin receptor autophosphorylation almost completely.	Hydrogen Peroxide	13-17	insulin receptor	Homo sapiens	28-44
12876303-8	2003	In addition, H2O2 inhibited insulin receptor binding partially and inhibited insulin receptor autophosphorylation almost completely.	Hydrogen Peroxide	13-17	insulin receptor	Homo sapiens	77-93
12802339-4	2003	Here we report the crystal structures of the regulatory sulphenic and irreversible sulphinic and sulphonic acids of protein tyrosine phosphatase 1B (PTP1B), an important enzyme in the negative regulation of the insulin receptor and a therapeutic target in type II diabetes and obesity.	sulphonic acids	97-112	insulin receptor	Homo sapiens	211-227
12707268-1	2003	Tyrosine 984 in the juxtamembrane region of the insulin receptor, between the transmembrane helix and the cytoplasmic tyrosine kinase domain, is conserved among all insulin receptor-like proteins from hydra to humans.	Tyrosine	0-8	insulin receptor	Homo sapiens	165-181
12707268-3	2003	Moreover, mutation of Tyr-984 in the full-length insulin receptor results in significantly elevated receptor phosphorylation levels in cells, both in the absence of insulin and following insulin stimulation.	Tyrosine	22-25	insulin receptor	Homo sapiens	49-65
12707268-4	2003	These data demonstrate that Tyr-984 plays an important structural role in maintaining the quiescent, basal state of the insulin receptor.	Tyrosine	28-31	insulin receptor	Homo sapiens	120-136
12888267-3	2003	In this study, bismaltolato oxovanadium (BMOV), a potent insulin sensitizer, was shown to be a reversible, competitive phosphatase inhibitor that inhibited phosphatase activity in cultured cells and enhanced insulin receptor activation in vivo.	bismaltolato oxovanadium	15-39	insulin receptor	Homo sapiens	208-224
12888267-3	2003	In this study, bismaltolato oxovanadium (BMOV), a potent insulin sensitizer, was shown to be a reversible, competitive phosphatase inhibitor that inhibited phosphatase activity in cultured cells and enhanced insulin receptor activation in vivo.	bis(maltolato)oxovanadium(IV)	41-45	insulin receptor	Homo sapiens	208-224
12654724-5	2003	Although lacking classical receptor-binding determinants, INS-6 binds to and activates the human insulin receptor.	ins-6	58-63	insulin receptor	Homo sapiens	97-113
12740809-0	2003	Signaling effects of demethylasterriquinone B1, a selective insulin receptor modulator.	L 783281	21-46	insulin receptor	Homo sapiens	60-76
12740809-7	2003	The action of DAQ B1 as a selective insulin receptor modulator can be accounted for by its ability to selectively activate one kinase among the many emanating from insulin receptor autophosphorylation and its reduced effects on gene expression.	L 783281	14-20	insulin receptor	Homo sapiens	36-52
12740809-7	2003	The action of DAQ B1 as a selective insulin receptor modulator can be accounted for by its ability to selectively activate one kinase among the many emanating from insulin receptor autophosphorylation and its reduced effects on gene expression.	L 783281	14-20	insulin receptor	Homo sapiens	164-180
12435730-8	2003	Courses of the activation loop that collide with STI-571 binding explain its inactivity at other kinases as the insulin receptor.	Imatinib Mesylate	49-56	insulin receptor	Homo sapiens	112-128
12767279-0	2003	Transcriptional inhibition of the human insulin receptor gene by aldosterone.	Aldosterone	65-76	insulin receptor	Homo sapiens	40-56
12767279-1	2003	In earlier studies, we reported reduced human insulin receptor (hIR) mRNA levels, insulin binding and insulin responsiveness in U-937 human promonocytic cells treated with aldosterone.	Aldosterone	172-183	insulin receptor	Homo sapiens	46-62
12510059-2	2003	One potential mechanism for this is that Ser/Thr phosphorylation decreases the ability of IRS-1 to be tyrosine-phosphorylated by the insulin receptor.	Serine	41-44	insulin receptor	Homo sapiens	133-149
12510059-2	2003	One potential mechanism for this is that Ser/Thr phosphorylation decreases the ability of IRS-1 to be tyrosine-phosphorylated by the insulin receptor.	Threonine	45-48	insulin receptor	Homo sapiens	133-149
12510059-2	2003	One potential mechanism for this is that Ser/Thr phosphorylation decreases the ability of IRS-1 to be tyrosine-phosphorylated by the insulin receptor.	Tyrosine	102-110	insulin receptor	Homo sapiens	133-149
12634852-5	2003	Inhibition of insulin-receptor processing using tunicamycin suggests that the basal interaction occurs during insulin-receptor biosynthesis in the ER.	Tunicamycin	48-59	insulin receptor	Homo sapiens	14-30
12634852-5	2003	Inhibition of insulin-receptor processing using tunicamycin suggests that the basal interaction occurs during insulin-receptor biosynthesis in the ER.	Tunicamycin	48-59	insulin receptor	Homo sapiens	110-126
12629126-0	2003	Metformin rapidly increases insulin receptor activation in human liver and signals preferentially through insulin-receptor substrate-2.	Metformin	0-9	insulin receptor	Homo sapiens	28-44
12629126-6	2003	Tyrphostin AG1024 was used to inhibit IR-KA and examine effects on deoxyglucose uptake.	Tyrphostins	0-10	insulin receptor	Homo sapiens	38-40
12629126-7	2003	Metformin (1 micro g/ml) increased IR tyrosine phosphorylation by 78% (P = 0.0007) in 30 min in human hepatocytes and Huh7 cells and increased IRS-2 but not IRS-1 activation, and the downstream increase in deoxyglucose uptake was mediated via increased translocation of GLUT-1 to the plasma membrane.	Metformin	0-9	insulin receptor	Homo sapiens	35-37
12629126-7	2003	Metformin (1 micro g/ml) increased IR tyrosine phosphorylation by 78% (P = 0.0007) in 30 min in human hepatocytes and Huh7 cells and increased IRS-2 but not IRS-1 activation, and the downstream increase in deoxyglucose uptake was mediated via increased translocation of GLUT-1 to the plasma membrane.	Tyrosine	38-46	insulin receptor	Homo sapiens	35-37
12629126-7	2003	Metformin (1 micro g/ml) increased IR tyrosine phosphorylation by 78% (P = 0.0007) in 30 min in human hepatocytes and Huh7 cells and increased IRS-2 but not IRS-1 activation, and the downstream increase in deoxyglucose uptake was mediated via increased translocation of GLUT-1 to the plasma membrane.	Deoxyglucose	206-218	insulin receptor	Homo sapiens	35-37
12629126-9	2003	Metformin increased basal IR-KA by 150% (P = 0.0001).	Metformin	0-9	insulin receptor	Homo sapiens	26-28
12629126-11	2003	This study demonstrates that the mechanism of action of metformin in liver involves IR activation, followed by selective IRS-2 activation, and increased glucose uptake via increased GLUT-1 translocation.	Metformin	56-65	insulin receptor	Homo sapiens	84-86
12629126-12	2003	The effect of metformin was completely blocked by an IR inhibitor.	Metformin	14-23	insulin receptor	Homo sapiens	53-55
12554784-3	2003	The MEK1 mutant, which activates ERK, markedly down-regulated expression of the insulin receptor (IR) and its major substrates, IRS-1 and IRS-2, mRNA and protein, and in turn reduced tyrosine phosphorylation of IR as well as IRS-1 and IRS-2 and their associated phosphatidyl inositol 3-kinase (PI3K) activity.	Tyrosine	183-191	insulin receptor	Homo sapiens	80-96
12554784-3	2003	The MEK1 mutant, which activates ERK, markedly down-regulated expression of the insulin receptor (IR) and its major substrates, IRS-1 and IRS-2, mRNA and protein, and in turn reduced tyrosine phosphorylation of IR as well as IRS-1 and IRS-2 and their associated phosphatidyl inositol 3-kinase (PI3K) activity.	Tyrosine	183-191	insulin receptor	Homo sapiens	98-100
12554784-3	2003	The MEK1 mutant, which activates ERK, markedly down-regulated expression of the insulin receptor (IR) and its major substrates, IRS-1 and IRS-2, mRNA and protein, and in turn reduced tyrosine phosphorylation of IR as well as IRS-1 and IRS-2 and their associated phosphatidyl inositol 3-kinase (PI3K) activity.	Tyrosine	183-191	insulin receptor	Homo sapiens	128-130
12554784-5	2003	Finally, the MKK7 mutant, which activates JNK, reduced tyrosine phosphorylation of IRS-1 and IRS-2 and IRS-associated PI3K activity without affecting expression of the IR, IRS-1, or IRS-2.	Tyrosine	55-63	insulin receptor	Homo sapiens	83-85
12647262-6	2003	However, captopril treatment caused an increase in insulin-induced insulin receptor substrate-1 (IRS-1) phosphorylation accompanied by an increased association of IRS-1 with phosphoinositide-3 kinase (PI-3 kinase), despite no change on insulin receptor (IR) autophosphorylation.	Captopril	9-18	insulin receptor	Homo sapiens	67-83
12647262-6	2003	However, captopril treatment caused an increase in insulin-induced insulin receptor substrate-1 (IRS-1) phosphorylation accompanied by an increased association of IRS-1 with phosphoinositide-3 kinase (PI-3 kinase), despite no change on insulin receptor (IR) autophosphorylation.	Captopril	9-18	insulin receptor	Homo sapiens	97-99
12711007-0	2003	Identification of a Vitamin D response element in the human insulin receptor gene promoter.	Vitamin D	20-29	insulin receptor	Homo sapiens	60-76
12537988-6	2003	A poor intracellular Mg concentration, as found in noninsulin-dependent diabetes mellitus (NIDDM) and in hypertensive patients, may result in a defective tyrosine-kinase activity at the insulin receptor level and exaggerated intracellular calcium concentration.	Magnesium	21-23	insulin receptor	Homo sapiens	186-202
12538626-1	2003	An infant with Donohue"s syndrome (leprechaunism) was found to be homozygous for an in-frame trinucleotide deletion within the insulin receptor gene resulting in the deletion of valine 335.	trinucleotide	93-106	insulin receptor	Homo sapiens	127-143
12538626-1	2003	An infant with Donohue"s syndrome (leprechaunism) was found to be homozygous for an in-frame trinucleotide deletion within the insulin receptor gene resulting in the deletion of valine 335.	Valine	178-184	insulin receptor	Homo sapiens	127-143
12734794-0	2003	Glucose-mannose-binding lectins isolated from Brazilian beans stimulate the autophosphorylation of the insulin receptor in vitro.	Glucose	0-7	insulin receptor	Homo sapiens	103-119
12734794-0	2003	Glucose-mannose-binding lectins isolated from Brazilian beans stimulate the autophosphorylation of the insulin receptor in vitro.	Mannose	8-15	insulin receptor	Homo sapiens	103-119
12711007-1	2003	The present study was designed to explore the possible presence and location of Vitamin D response elements (VDREs) in the human insulin receptor (hIR) gene promoter.	Vitamin D	80-89	insulin receptor	Homo sapiens	129-145
12504093-0	2003	Protection of insulin receptor substrate-3 from staurosporine-induced apoptosis.	Staurosporine	48-61	insulin receptor	Homo sapiens	14-30
14569873-3	2003	The comparative analysis of primary structures of the protein disulfide isomerase thioredoxine domains and C-terminal domain of the receptor suggests existence of the thioredoxine domain in the insulin receptor.	thioredoxine	82-94	insulin receptor	Homo sapiens	194-210
12237455-5	2002	On SPOT membranes, IR peptides with phosphotyrosine 1163 were efficiently bound by PTP1B D181A, and dephosphorylated by PTP-1B.	Phosphotyrosine	36-51	insulin receptor	Homo sapiens	19-21
12220227-2	2002	Here we show that stimulation by insulin of freshly isolated primary adipocytes resulted in the expected rapid tyrosine phosphorylation of the insulin receptor, IRS-1 and IRS-3.	Tyrosine	111-119	insulin receptor	Homo sapiens	143-159
12456798-2	2002	Stat5b and insulin receptor substrate 1 (IRS-1) interact with the same autophosphorylation site in the IR [phosphotyrosine (pY) 972] in yeast two-hybrid assays, and the IR phosphorylates Stat5b in vitro.	phosphotyrosine (py) 972	107-131	insulin receptor	Homo sapiens	41-43
12456798-2	2002	Stat5b and insulin receptor substrate 1 (IRS-1) interact with the same autophosphorylation site in the IR [phosphotyrosine (pY) 972] in yeast two-hybrid assays, and the IR phosphorylates Stat5b in vitro.	phosphotyrosine (py) 972	107-131	insulin receptor	Homo sapiens	103-105
12456798-9	2002	We also find that insulin stimulates tyrosine phosphorylation of JAKs that are constitutively associated with the IR.	Tyrosine	37-45	insulin receptor	Homo sapiens	114-116
12213804-3	2002	In HTC-IR cells, 20 microm TLK19780 enhanced maximal insulin-stimulated IR autophosphorylation 2-fold and increased insulin sensitivity 2-3-fold.	TLK 19780	27-35	insulin receptor	Homo sapiens	7-9
12213804-5	2002	The predominant effect of TLK19780 was to increase the number of IR that underwent autophosphorylation.	TLK 19780	26-34	insulin receptor	Homo sapiens	65-67
12213804-8	2002	These studies indicate that at low micromolar levels small IR activator molecules can enhance insulin action in various cultured cells and suggest that this effect is mediated by increasing the number of IR that are tyrosine-phosphorylated in response to insulin.	Tyrosine	216-224	insulin receptor	Homo sapiens	59-61
12436329-4	2002	This pathway begins with the phosphorylation of the adaptor protein Cbl by the insulin receptor, and results in the activation of a small GTP binding protein, TC10, a member of the Rho family.	Guanosine Triphosphate	138-141	insulin receptor	Homo sapiens	79-95
12472845-1	2003	Two phosphoserine tetradecapeptides corresponding to sequences 987-1000 (peptide pSer994) and 1017-1030 (peptide pSer1023/1025) from the human insulin receptor involved in the regulation of its activity were successfully synthesized using Fmoc-based chemistry.	Phosphoserine	4-17	insulin receptor	Homo sapiens	143-159
12213804-8	2002	These studies indicate that at low micromolar levels small IR activator molecules can enhance insulin action in various cultured cells and suggest that this effect is mediated by increasing the number of IR that are tyrosine-phosphorylated in response to insulin.	Tyrosine	216-224	insulin receptor	Homo sapiens	204-206
12169270-10	2002	In summary, these data indicate that PLCgamma, activated at least partially by PI3-kinase, is a link between insulin receptor and PKCzeta through the production of PA and could mediate insulin-induced glucose uptake and GLUT4 translocation.	Protactinium	164-166	insulin receptor	Homo sapiens	109-125
12125099-0	2002	Transcriptional activation of the human insulin receptor gene by 1,25-dihydroxyvitamin D(3).	1,25-dihydroxyvitamin D	65-88	insulin receptor	Homo sapiens	40-56
12125099-1	2002	Treatment with 10(-8) M 1,25-dihydroxyvitamin D(3) for 24 h causes transcriptional activation of the human insulin receptor gene in U-937 human promonocytic cells.	Calcitriol	24-50	insulin receptor	Homo sapiens	107-123
12125101-1	2002	In an earlier study, we have reported an inhibition of insulin receptor (IR) mRNA levels and insulin binding by aldosterone in U-937 human promonocytic cells.	Aldosterone	112-123	insulin receptor	Homo sapiens	55-71
12213853-3	2002	In this study, we have used a highly sensitive ELISA to measure IR tyrosine phosphorylation in fibroblasts from patients with PCOS and healthy control women.	Tyrosine	67-75	insulin receptor	Homo sapiens	64-66
12213853-4	2002	After the stimulation of intact fibroblasts with insulin, IR tyrosine phosphorylation in cells from the PCOS patients was decreased by approximately 40% when compared with controls.	Tyrosine	61-69	insulin receptor	Homo sapiens	58-60
12213853-7	2002	Pretreatment with H7, a nonspecific protein kinase inhibitor, completely reversed the decrease in insulin-stimulated IR autophosphorylation.	1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine	18-20	insulin receptor	Homo sapiens	117-119
12213853-13	2002	Moreover, the observation that TLK16998 and Merck L7 improved IR tyrosine phosphorylation in fibroblasts from patients with PCOS suggests that specific pharmacological therapies might be developed to treat the insulin resistance in PCOS.	Tyrosine	65-73	insulin receptor	Homo sapiens	62-64
12036959-0	2002	The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1.	Tyrosine	35-43	insulin receptor	Homo sapiens	4-20
12036959-10	2002	Taken together, these data indicate that the insulin receptor directly catalyzes the tyrosine phosphorylation of caveolin.	Tyrosine	85-93	insulin receptor	Homo sapiens	45-61
12169270-10	2002	In summary, these data indicate that PLCgamma, activated at least partially by PI3-kinase, is a link between insulin receptor and PKCzeta through the production of PA and could mediate insulin-induced glucose uptake and GLUT4 translocation.	Glucose	201-208	insulin receptor	Homo sapiens	109-125
12145261-0	2002	Obesity is a critical risk factor for worsening of glucose tolerance in a family with the mutant insulin receptor.	Glucose	51-58	insulin receptor	Homo sapiens	97-113
12006592-1	2002	Insulin receptor substrate p53/p58 (IRSp53) is involved in cytoskeletal dynamics and is a candidate disease sensor in polyglutamine expansion neurodegeneration.	polyglutamine	118-131	insulin receptor	Homo sapiens	0-16
12067836-1	2002	Considerable evidence suggests that atypical protein kinase C isoforms (aPKCs), serving downstream of insulin receptor substrates and phosphatidylinositol (PI) 3-kinase, are required for insulin-stimulated glucose transport in skeletal muscle and adipocytes.	Glucose	206-213	insulin receptor	Homo sapiens	102-118
12033942-2	2002	To determine whether basal Ser/Thr phosphorylation of IRS proteins influences insulin receptor catalyzed tyrosine phosphorylation, recombinant FLAG epitope-tagged IRS-1 (F-IRS-1) and IRS-2 (F-IRS-2) were expressed, purified, and subjected to both dephosphorylation and hyperphosphorylation prior to phosphorylation by the insulin receptor kinase.	Tyrosine	105-113	insulin receptor	Homo sapiens	78-94
11994298-7	2002	In vitro phosphorylation studies revealed that SYNCRIP, once extracted from low density microsomes, can be tyrosine phosphorylated using purified insulin receptor.	Tyrosine	107-115	insulin receptor	Homo sapiens	146-162
12033942-9	2002	Dephosphorylation of IRS-1 and IRS-2 immunoprecipitated from serum-deprived cells, however, resulted in inhibition of tyrosine phosphorylation by the insulin receptor.	Tyrosine	118-126	insulin receptor	Homo sapiens	150-166
12033942-3	2002	As expected, hyperphosphorylation of F-IRS-1 and F-IRS-2 by GSK3beta decreased their subsequent phosphorylation on tyrosine residues by the insulin receptor.	Tyrosine	115-123	insulin receptor	Homo sapiens	140-156
11551902-0	2001	Insulin receptor-mediated p62dok tyrosine phosphorylation at residues 362 and 398 plays distinct roles for binding GTPase-activating protein and Nck and is essential for inhibiting insulin-stimulated activation of Ras and Akt.	Tyrosine	33-41	insulin receptor	Homo sapiens	0-16
12031977-2	2002	Moreover, adiponectin administration to rodents has been shown to increase insulin-induced tyrosine phosphorylation of the insulin receptor (IR) and also increase whole-body insulin sensitivity.	Tyrosine	91-99	insulin receptor	Homo sapiens	123-144
12031977-5	2002	Group 1 (19 subjects) underwent skeletal muscle biopsies for the measurement of basal and insulin-stimulated tyrosine phosphorylation of the IR (stimulated by 100 nmol/l insulin).	Tyrosine	109-117	insulin receptor	Homo sapiens	141-143
12031977-9	2002	In group 1 plasma adiponectin was negatively associated with the basal (r = -0.65, P = 0.003) and positively associated with the fold increase in IR tyrosine phosphorylation (r = 0.69, P = 0.001) before and after the adjustment for percent body fat (r = -0.58, P = 0.01 and r = 0.54, P = 0.02, respectively).	Tyrosine	149-157	insulin receptor	Homo sapiens	146-148
12031977-11	2002	In conclusion, our cross-sectional data suggest a role of physiological concentration of fasting plasma adiponectin in the regulation of skeletal muscle IR tyrosine phosphorylation.	Tyrosine	156-164	insulin receptor	Homo sapiens	153-155
11897789-11	2002	2) PI 3-kinase-stimulated generation of membrane phospholipids can localize Shc to the plasma membrane through the Shc PTB domain facilitating phosphorylation by the insulin receptor.	Phospholipids	49-62	insulin receptor	Homo sapiens	166-182
11875066-2	2002	The fragments contained one or both cysteine residues (amino acids 524 and 682) that form disulfides between alpha-subunits in native IR.	Cysteine	36-44	insulin receptor	Homo sapiens	134-136
11875066-2	2002	The fragments contained one or both cysteine residues (amino acids 524 and 682) that form disulfides between alpha-subunits in native IR.	Disulfides	90-100	insulin receptor	Homo sapiens	134-136
12078019-5	2002	This subtype"s pathogenesis is determined by a cascade of events, among which age, a disturbance of neuronal insulin receptor function leading to a deficit in acetylcholine and available energy, and membrane instability are the most important factors.	Acetylcholine	159-172	insulin receptor	Homo sapiens	109-125
12032625-3	2002	This study aimed to examine the effects of insulin on glucose transport and changes in insulin receptor tyrosine phosphorylation, IRS-1 and PC-1.	Tyrosine	104-112	insulin receptor	Homo sapiens	87-103
11912559-7	2002	TNF-alpha also inhibited tyrosine autophosphorylation of the IR in HAEC induced by insulin and reduced IR beta-subunit protein expression in HAEC.	Tyrosine	25-33	insulin receptor	Homo sapiens	61-63
11779863-2	2002	Similar to TNF, cycloheximide and anisomycin stimulated serine phosphorylation of IRS-1 and IRS-2, reduced their ability to interact with the insulin receptor, inhibited the insulin-induced tyrosine phosphorylation of IRS proteins, and diminished their association with phosphatidylinositol 3-kinase (PI3K).	Cycloheximide	16-29	insulin receptor	Homo sapiens	142-158
11779863-2	2002	Similar to TNF, cycloheximide and anisomycin stimulated serine phosphorylation of IRS-1 and IRS-2, reduced their ability to interact with the insulin receptor, inhibited the insulin-induced tyrosine phosphorylation of IRS proteins, and diminished their association with phosphatidylinositol 3-kinase (PI3K).	Anisomycin	34-44	insulin receptor	Homo sapiens	142-158
11779863-2	2002	Similar to TNF, cycloheximide and anisomycin stimulated serine phosphorylation of IRS-1 and IRS-2, reduced their ability to interact with the insulin receptor, inhibited the insulin-induced tyrosine phosphorylation of IRS proteins, and diminished their association with phosphatidylinositol 3-kinase (PI3K).	Tyrosine	190-198	insulin receptor	Homo sapiens	142-158
11751579-4	2002	We report that, in liver-derived cells lacking caveolae, autophosphorylation of the endogenous IR is dependent on raft lipids, being compromised by acute cyclodextrin-mediated cholesterol depletion or by antibody clustering of glycosphingolipids.	Cyclodextrins	154-166	insulin receptor	Homo sapiens	95-97
11751579-4	2002	We report that, in liver-derived cells lacking caveolae, autophosphorylation of the endogenous IR is dependent on raft lipids, being compromised by acute cyclodextrin-mediated cholesterol depletion or by antibody clustering of glycosphingolipids.	Cholesterol	176-187	insulin receptor	Homo sapiens	95-97
11751579-4	2002	We report that, in liver-derived cells lacking caveolae, autophosphorylation of the endogenous IR is dependent on raft lipids, being compromised by acute cyclodextrin-mediated cholesterol depletion or by antibody clustering of glycosphingolipids.	Glycosphingolipids	227-245	insulin receptor	Homo sapiens	95-97
11751579-5	2002	Moreover, we provide evidence that IR becomes recruited to detergent-resistant domains upon ligand binding and that clustering of GM2 ganglioside inhibits IR signalling apparently by excluding the ligand-bound IR from these domains.	G(M2) Ganglioside	130-145	insulin receptor	Homo sapiens	155-157
12112020-2	2002	We have recently found that Sam68 is a substrate of the insulin receptor (IR) that translocates from the nucleus to the cytoplasm and that Tyr-phosphorylated Sam68 associates with the SH2 domains of p85 PI3K and GAP, in vivo and in vitro.	Tyrosine	139-142	insulin receptor	Homo sapiens	56-72
12112020-2	2002	We have recently found that Sam68 is a substrate of the insulin receptor (IR) that translocates from the nucleus to the cytoplasm and that Tyr-phosphorylated Sam68 associates with the SH2 domains of p85 PI3K and GAP, in vivo and in vitro.	Tyrosine	139-142	insulin receptor	Homo sapiens	74-76
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Aspartic Acid	41-44	insulin receptor	Homo sapiens	7-23
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Tyrosine	54-57	insulin receptor	Homo sapiens	7-23
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Lysine	204-207	insulin receptor	Homo sapiens	7-23
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Aspartic Acid	214-217	insulin receptor	Homo sapiens	7-23
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Arginine	224-227	insulin receptor	Homo sapiens	7-23
11598120-2	2001	In the insulin receptor"s kinase domain, Asp-1161 and Tyr-1162 in the peptide substrate-like sequence of the unphosphorylated activation loop can interact with four invariant residues in the active site: Lys-1085, Asp-1132, Arg-1136, and Gln-1208.	Glutamine	238-241	insulin receptor	Homo sapiens	7-23
12528542-0	2001	[The binding characteristics of insulin-MTX to insulin receptor].	Methotrexate	40-43	insulin receptor	Homo sapiens	47-63
12528542-7	2001	RESULTS: Insulin-MTX competed as effectively as insulin with 125I-insulin for insulin receptor.	Methotrexate	17-20	insulin receptor	Homo sapiens	78-94
12528542-9	2001	CONCLUSION: Insulin-MTX could bind with insulin receptor with high affinity.	Methotrexate	20-23	insulin receptor	Homo sapiens	40-56
11551902-9	2001	Taken together, our findings indicate that p62(dok) is a direct substrate for the IR tyrosine kinase and that phosphorylation at Tyr(362) and Tyr(398) plays an essential role for p62(dok) to interact with its effectors and negatively regulate the insulin signaling pathway.	Tyrosine	129-132	insulin receptor	Homo sapiens	82-84
11551902-9	2001	Taken together, our findings indicate that p62(dok) is a direct substrate for the IR tyrosine kinase and that phosphorylation at Tyr(362) and Tyr(398) plays an essential role for p62(dok) to interact with its effectors and negatively regulate the insulin signaling pathway.	Tyrosine	142-145	insulin receptor	Homo sapiens	82-84
11695899-3	2001	This approach identifies thymolphthalein, which is an apparent weak agonist that displaces insulin from its receptor, stimulates auto- and substrate phosphorylation of IR, and potentiates lipogenesis in adipocytes in the presence of submaximal concentrations of insulin.	Thymolphthalein	25-40	insulin receptor	Homo sapiens	168-170
11887975-0	2001	Rosiglitazone treatment of patients with extreme insulin resistance and diabetes mellitus due to insulin receptor mutations has no effects on glucose and lipid metabolism.	Rosiglitazone	0-13	insulin receptor	Homo sapiens	97-113
11887975-3	2001	OBJECTIVES: To evaluate whether hyperglycaemia in two lean patients with primary severe insulin resistance due to insulin receptor (IR) mutations and diabetes mellitus could be reduced by supplement of rosiglitazone for 180 days and secondary, to evaluate the effects on plasma NEFA, TG, Apo B, PAI-1 and serum insulin.	Rosiglitazone	202-215	insulin receptor	Homo sapiens	114-130
11887975-3	2001	OBJECTIVES: To evaluate whether hyperglycaemia in two lean patients with primary severe insulin resistance due to insulin receptor (IR) mutations and diabetes mellitus could be reduced by supplement of rosiglitazone for 180 days and secondary, to evaluate the effects on plasma NEFA, TG, Apo B, PAI-1 and serum insulin.	Rosiglitazone	202-215	insulin receptor	Homo sapiens	132-134
11887975-15	2001	These findings may suggest that the effect of rosiglitazone on glucose and lipid metabolism are dependent on the presence of intact IR protein.	Rosiglitazone	46-59	insulin receptor	Homo sapiens	132-134
11887975-15	2001	These findings may suggest that the effect of rosiglitazone on glucose and lipid metabolism are dependent on the presence of intact IR protein.	Glucose	63-70	insulin receptor	Homo sapiens	132-134
11604231-2	2001	We have recently found that Sam68 is a substrate of the insulin receptor (IR) and that Tyr-phosphorylated Sam68 associates with the SH2 domains of p85 PI3K.	Tyrosine	87-90	insulin receptor	Homo sapiens	56-77
11604231-6	2001	Moreover, we have found that Sam68 is a p120GAP associated protein after Tyr-phosphorylation by the IR.	Tyrosine	73-76	insulin receptor	Homo sapiens	100-102
11587538-3	2001	Since caveolae may be important sites for crosstalk between tyrosine kinase and sphingolipid signaling pathways, we examined the role of increased caveolar pools of ceramide in regulating tyrosine phosphorylation of the IR and its main substrate, insulin receptor substrate-1 (IRS-1).	Ceramides	165-173	insulin receptor	Homo sapiens	220-222
11574417-14	2001	Study of insulin signaling indicated that insulin-induced tyrosine phosphorylation of the insulin receptor (IR) was blunted in HiIMCL compared with LoIMCL (57 vs. 142% above basal, P < 0.05), while protein expression of the IR was unaltered.	Tyrosine	58-66	insulin receptor	Homo sapiens	90-111
11574417-14	2001	Study of insulin signaling indicated that insulin-induced tyrosine phosphorylation of the insulin receptor (IR) was blunted in HiIMCL compared with LoIMCL (57 vs. 142% above basal, P < 0.05), while protein expression of the IR was unaltered.	Tyrosine	58-66	insulin receptor	Homo sapiens	108-110
11574417-15	2001	IR substrate-1-associated phosphatidylinositol (PI) 3-kinase activation by insulin was also lower in the HiIMCL group than in the LoIMCL group (49 +/- 23 vs. 84 +/- 27% above basal, P < 0.05 between HiIMCL and LoIMCL).	Phosphatidylinositols	26-46	insulin receptor	Homo sapiens	0-2
11574417-15	2001	IR substrate-1-associated phosphatidylinositol (PI) 3-kinase activation by insulin was also lower in the HiIMCL group than in the LoIMCL group (49 +/- 23 vs. 84 +/- 27% above basal, P < 0.05 between HiIMCL and LoIMCL).	hiimcl	105-111	insulin receptor	Homo sapiens	0-2
11574417-15	2001	IR substrate-1-associated phosphatidylinositol (PI) 3-kinase activation by insulin was also lower in the HiIMCL group than in the LoIMCL group (49 +/- 23 vs. 84 +/- 27% above basal, P < 0.05 between HiIMCL and LoIMCL).	loimcl	130-136	insulin receptor	Homo sapiens	0-2
12096896-1	2002	A 480-kDa disulfide-linked heterodimer single-pass transmembrane protein, the insulin receptor, is autophosphorylated upon insulin binding to its extracellular domain.	Disulfides	10-19	insulin receptor	Homo sapiens	78-94
12096896-5	2002	Our preliminary studies confirm that (1) the intact receptor can be reconstituted constitutively within a lipid vesicle and (2) fusion of the receptor-containing vesicles to mica resulted in the formation of molecular flat 5.5-nm-thick supported planar bilayers populated by two populations of protrusions, the shape and size of which are consistent with those of the insulin receptor"s intra- and extracellular domains as modeled by the cryo-EM data of Ottensmeyer et al.	mica	174-178	insulin receptor	Homo sapiens	368-384
11820776-4	2002	The results showed: (i) significant alterations of RBC ultrastructure; (ii) relevant changes of spectrin cytoskeleton; (iii) altered insulin receptor distribution; and (iv) that treatment with the antioxidizing drug N-acetylcysteine was capable of significantly counteracting these changes.	Acetylcysteine	216-232	insulin receptor	Homo sapiens	133-149
11801259-4	2002	Perifusion experiments revealed that both glucose-stimulated and basal insulin secretion were significantly inhibited following human islet insulin receptor activation with L-783,281, and that signalling through phosphatidylinositol 3-kinase (PI 3-kinase) was responsible, at least in part, for this inhibitory effect.	Glucose	42-49	insulin receptor	Homo sapiens	140-156
11551902-2	2001	However, whether this protein is a direct in vivo substrate for the insulin receptor (IR) tyrosine kinase and whether the tyrosine phosphorylation plays a role in insulin signaling remain to be established.	Tyrosine	90-98	insulin receptor	Homo sapiens	86-88
11551902-3	2001	Here we show that the insulin-stimulated tyrosine phosphorylation of the GAP-associated protein, now identified as p62(dok), is inhibited by Grb10, an adaptor protein that binds directly to the kinase domain of the IR, both in vitro and in cells.	Tyrosine	41-49	insulin receptor	Homo sapiens	215-217
11551902-4	2001	Replacing Tyr(362) and Tyr(398) with phenylalanine greatly decreased the IR-catalyzed p62(dok) tyrosine phosphorylation in vitro, suggesting that these two residues are the major IR-mediated phosphorylation sites.	Tyrosine	95-103	insulin receptor	Homo sapiens	73-75
11579209-0	2001	Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor.	Serine	28-31	insulin receptor	Homo sapiens	86-102
11591170-3	2001	Whereas treatment adjuncts to insulin may address carbohydrate metabolism from glucose absorption to insulin receptor function, success may depend on the type of diabetes present in the patient.	Carbohydrates	50-62	insulin receptor	Homo sapiens	101-117
11423472-5	2001	By using inhibitors of the different signaling pathways evoked by insulin-receptor binding, it has been shown that the biosynthesis of PAI-1 is due to phosphatidylinositol (PI) 3-kinase activation, followed by protein kinase C and ultimately by mitogen-activated protein (MAP) kinase activation and extracellular signal-regulated kinase 2 phosphorylation.	Phosphatidylinositols	151-171	insulin receptor	Homo sapiens	66-82
11601679-1	2001	Metformin reduces blood glucose levels predominantly by inhibiting hepatic gluconeogenesis, although it also may enhance insulin receptor number or activity.	Metformin	0-9	insulin receptor	Homo sapiens	121-137
11513586-3	2001	A structural model of v-Fps, generated from the insulin receptor, indicates that pTyr-1073 chelates two arginines.	ptyr-1073	81-90	insulin receptor	Homo sapiens	48-64
11513586-3	2001	A structural model of v-Fps, generated from the insulin receptor, indicates that pTyr-1073 chelates two arginines.	Arginine	104-113	insulin receptor	Homo sapiens	48-64
11502760-1	2001	Recent studies indicate that insulin stimulation of glucose transporter (GLUT)4 translocation requires at least two distinct insulin receptor-mediated signals: one leading to the activation of phosphatidylinositol 3 (PI-3) kinase and the other to the activation of the small GTP binding protein TC10.	Guanosine Triphosphate	275-278	insulin receptor	Homo sapiens	125-141
11488908-3	2001	268, 25-34], epidermal growth factor (EGF) gave rise to transient tyrosine phosphorylation of insulin receptor substrates (IRS-1 and IRS-2), thereby activating the bound phosphatidylinositol 3-kinase in human epidermoid carcinoma A431 cells normally abundant in EGF receptors (EGFR) and Chinese hamster ovary (CHO) cells transfected with full-length EGFR.	Tyrosine	66-74	insulin receptor	Homo sapiens	94-110
11423485-10	2001	Interestingly, lack of IR expression in IR-null keratinocytes abolished insulin-induced glucose uptake and partially decreased insulin- and IGF-I-induced proliferation, demonstrating the direct involvement of the IR in these processes.	Glucose	88-95	insulin receptor	Homo sapiens	23-25
11423485-10	2001	Interestingly, lack of IR expression in IR-null keratinocytes abolished insulin-induced glucose uptake and partially decreased insulin- and IGF-I-induced proliferation, demonstrating the direct involvement of the IR in these processes.	Glucose	88-95	insulin receptor	Homo sapiens	40-42
11423485-10	2001	Interestingly, lack of IR expression in IR-null keratinocytes abolished insulin-induced glucose uptake and partially decreased insulin- and IGF-I-induced proliferation, demonstrating the direct involvement of the IR in these processes.	Glucose	88-95	insulin receptor	Homo sapiens	40-42
11390649-5	2001	The Asp1161Ala mutation increased the rate of in vitro autophosphorylation of the IRKD or IR at low ATP concentrations and in the absence of insulin.	Adenosine Triphosphate	100-103	insulin receptor	Homo sapiens	82-84
11390649-6	2001	However, saturation with ATP (for the IRKD) or the presence of insulin (for the IR) yielded equivalent rates of autophosphorylation for mutant versus wild-type kinases.	Adenosine Triphosphate	25-28	insulin receptor	Homo sapiens	38-40
11506178-5	2001	Tyrosine phosphorylation of PTP1B by the insulin receptor was absolutely dependent upon insulin-stimulated receptor autophosphorylation and required an intact kinase domain, containing insulin receptor tyrosines 1146, 1150 and 1151.	Tyrosine	0-8	insulin receptor	Homo sapiens	41-57
11506178-5	2001	Tyrosine phosphorylation of PTP1B by the insulin receptor was absolutely dependent upon insulin-stimulated receptor autophosphorylation and required an intact kinase domain, containing insulin receptor tyrosines 1146, 1150 and 1151.	Tyrosine	202-211	insulin receptor	Homo sapiens	41-57
11309621-4	2001	We previously described a pathway involving the insulin-stimulated tyrosine phosphorylation of Cbl, which is recruited to the insulin receptor by the adapter protein CAP.	Tyrosine	67-75	insulin receptor	Homo sapiens	126-142
11295155-9	2001	Vitamin D offers a protection from genotoxic effects of Vitamin D deficiency by increasing the insulin receptor gene expression and BSP (bone sialoprotein), bone-remodeling by decreasing the osteopontin (OPN) m-RNAs, maintaining the normal epidermal structure and enamel matrix.	Vitamin D	0-9	insulin receptor	Homo sapiens	95-111
11295155-9	2001	Vitamin D offers a protection from genotoxic effects of Vitamin D deficiency by increasing the insulin receptor gene expression and BSP (bone sialoprotein), bone-remodeling by decreasing the osteopontin (OPN) m-RNAs, maintaining the normal epidermal structure and enamel matrix.	Vitamin D	56-65	insulin receptor	Homo sapiens	95-111
11287630-1	2001	Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by the insulin receptor permits this docking protein to interact with signaling proteins that promote insulin action.	Tyrosine	0-8	insulin receptor	Homo sapiens	28-44
11287630-2	2001	Serine phosphorylation uncouples IRS-1 from the insulin receptor, thereby inhibiting its tyrosine phosphorylation and insulin signaling.	Serine	0-6	insulin receptor	Homo sapiens	48-64
11287630-2	2001	Serine phosphorylation uncouples IRS-1 from the insulin receptor, thereby inhibiting its tyrosine phosphorylation and insulin signaling.	Tyrosine	89-97	insulin receptor	Homo sapiens	48-64
11440359-4	2001	Activation of DAG-sensitive PKC isoforms, such as PKC-theta and PKC-epsilon, down-regulates insulin receptor signalling and could be an important biochemical mechanism linking dysregulated lipid metabolism and insulin resistance in muscle.	Diglycerides	14-17	insulin receptor	Homo sapiens	92-108
11295170-12	2001	An adaptive coregulation of Glut-4 and insulin receptor content appears to optimize the use of glucose during chronic hypobaric hypoxia within these tissues.	Glucose	95-102	insulin receptor	Homo sapiens	39-55
11342583-8	2001	In conclusion, chronic ET-1 treatment of 3T3-L1 adipocytes leads to heterologous desensitization of metabolic and mitogenic actions of insulin, most likely through the decreased tyrosine phosphorylation of the insulin receptor substrates IRS-1, SHC, and G alpha q/11.	Tyrosine	178-186	insulin receptor	Homo sapiens	210-226
11401470-0	2001	Identification of Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor in intact cells.	Serine	18-21	insulin receptor	Homo sapiens	84-100
11401470-0	2001	Identification of Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor in intact cells.	Serine	32-35	insulin receptor	Homo sapiens	84-100
11401470-1	2001	In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro.	Serine	34-37	insulin receptor	Homo sapiens	100-116
11401470-1	2001	In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro.	Serine	34-37	insulin receptor	Homo sapiens	118-120
11401470-1	2001	In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro.	Serine	48-51	insulin receptor	Homo sapiens	100-116
11401470-1	2001	In a previous report we described Ser(1275) and Ser(1309) as autophosphorylation sites of the human insulin receptor (IR) tyrosine kinase (TK) in vitro.	Serine	48-51	insulin receptor	Homo sapiens	118-120
11401470-3	2001	In this study, we determined the intrinsic activity of the IR to phosphorylate both serine residues in intact cells.	Serine	84-90	insulin receptor	Homo sapiens	59-61
11401470-4	2001	For this purpose CHO-09 and NIH-3T3 derived cell-lines expressing the human IR were metabolically labelled with [(32)P]orthophosphate, followed by hormone stimulation of the receptor.	[(32)p]orthophosphate	112-133	insulin receptor	Homo sapiens	76-78
11401470-5	2001	The IR was isolated by immunoprecipitation and SDS-PAGE and subsequently analysed for serine phosphorylation by phosphopeptide mapping of HPLC-purified tryptic phosphopeptides.	Sodium Dodecyl Sulfate	47-50	insulin receptor	Homo sapiens	4-6
11401470-5	2001	The IR was isolated by immunoprecipitation and SDS-PAGE and subsequently analysed for serine phosphorylation by phosphopeptide mapping of HPLC-purified tryptic phosphopeptides.	Serine	86-92	insulin receptor	Homo sapiens	4-6
11401470-6	2001	Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells.	Phosphates	62-71	insulin receptor	Homo sapiens	18-20
11401470-6	2001	Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells.	Serine	91-94	insulin receptor	Homo sapiens	18-20
11401470-6	2001	Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells.	Serine	105-108	insulin receptor	Homo sapiens	18-20
11401470-6	2001	Activation of the IR in the intact cell appeared to result in phosphate incorporation into Ser(1275) and Ser(1309), providing strong evidence that both serine residues are phosphorylation sites of the activated receptor in intact cells.	Serine	152-158	insulin receptor	Homo sapiens	18-20
11145958-1	2001	The pleckstrin homology (PH) domain of the insulin receptor substrate-1 (IRS-1) plays a role in directing this molecule to the insulin receptor, thereby regulating its tyrosine phosphorylation.	Tyrosine	168-176	insulin receptor	Homo sapiens	43-59
11145958-7	2001	Thus, compromising the function of the PH domain, e.g. in insulin-resistant states, could decrease both the ability of IRS-1 to be tyrosine phosphorylated by the insulin receptor and to link to subsequent downstream targets.	Tyrosine	131-139	insulin receptor	Homo sapiens	162-178
11084576-7	2000	In muscle tissues from pregnant control subjects vanadate increased tyrosine phosphorylation of the insulin receptor and insulin receptor substrate 1 to levels similar to those in muscle tissues from nonpregnant control subjects.	Vanadates	49-57	insulin receptor	Homo sapiens	100-116
11239554-1	2001	OBJECTIVE: To determine whether the tyrosine autophosphorylation of the insulin receptor (IR) in the ovary of a woman with polycystic ovary syndrome (PCOS) was reduced compared to normal.	Tyrosine	36-44	insulin receptor	Homo sapiens	72-88
11239554-1	2001	OBJECTIVE: To determine whether the tyrosine autophosphorylation of the insulin receptor (IR) in the ovary of a woman with polycystic ovary syndrome (PCOS) was reduced compared to normal.	Tyrosine	36-44	insulin receptor	Homo sapiens	90-92
11239554-7	2001	Colorimetric and chemiluminescent methods were used to detect the presence of the IR beta-subunit and IR tyrosine autophosphorylation, respectively.	Tyrosine	105-113	insulin receptor	Homo sapiens	102-104
11239554-10	2001	CONCLUSION(S): Tyrosine autophosphorylation of the IR may be decreased in the ovaries of women with PCOS, similar to the findings in other tissues.	Tyrosine	15-23	insulin receptor	Homo sapiens	51-53
11471071-1	2001	We determined the involvement of Tyr-1158 within the regulatory loop of the insulin receptor (IR) in the generation of insulin-specific responses in situ.	Tyrosine	33-36	insulin receptor	Homo sapiens	76-92
11471071-1	2001	We determined the involvement of Tyr-1158 within the regulatory loop of the insulin receptor (IR) in the generation of insulin-specific responses in situ.	Tyrosine	33-36	insulin receptor	Homo sapiens	94-96
11160869-0	2001	The sulfonylurea glimepiride regulates intracellular routing of the insulin-receptor complexes through their interaction with specific protein kinase C isoforms.	sulfonylurea glimepiride	4-28	insulin receptor	Homo sapiens	68-84
11235915-0	2001	Human growth factor receptor bound 14 binds the activated insulin receptor and alters the insulin-stimulated tyrosine phosphorylation levels of multiple proteins.	Tyrosine	109-117	insulin receptor	Homo sapiens	58-74
11217151-0	2001	Insulin receptor antibodies inhibit insulin uptake by the liver: in vivo 123I-insulin scintigraphic scanning and in vitro characterization in autoimmune hypoglycemia.	Iodine-123	73-77	insulin receptor	Homo sapiens	0-16
11135668-2	2001	Based on a phosphoryl transfer mechanism involving a dissociative transition state, a potent and selective bisubstrate inhibitor for the insulin receptor tyrosine kinase was synthesized by linking ATPgammaS to a peptide substrate analog via a two-carbon spacer.	Carbon	247-253	insulin receptor	Homo sapiens	137-153
11135668-4	2001	A crystal structure of this inhibitor bound to the tyrosine kinase domain of the insulin receptor confirmed the key design features inspired by a dissociative transition state, and revealed that the linker takes part in the octahedral coordination of an active site Mg2+.	magnesium ion	266-270	insulin receptor	Homo sapiens	81-97
11237218-6	2001	Excessive serine phosphorylation of the insulin receptor or downstream signaling proteins may be involved in the pathogenesis of insulin resistance in PCOS.	Serine	10-16	insulin receptor	Homo sapiens	40-56
11123895-5	2000	In computer modeling, AG 538 was placed in the kinase domain of the insulin receptor and was able to sit in place of tyrosines 1158 and 1162, which undergo autophosphorylation.	Tyrosine	117-126	insulin receptor	Homo sapiens	68-84
11118640-2	2000	To further explore the effect of aberrant (rather than absent) N-linked glycosylation of the insulin receptor, we examined the relationship of processing to function.	Nitrogen	63-64	insulin receptor	Homo sapiens	93-109
11078721-1	2000	Biotin regulation of asialoglycoprotein receptor expression and insulin receptor activity has been established in two human hepatoblastoma cell lines, Hep G2 and HuH-7.	Biotin	0-6	insulin receptor	Homo sapiens	64-80
11078721-3	2000	Metabolic labeling and subsequent immunoprecipitation indicate that the loss of insulin receptor activity during biotin deprivation was due to suppression of receptor synthesis.	Biotin	113-119	insulin receptor	Homo sapiens	80-96
11078721-4	2000	Evidence for posttranscriptional regulation of insulin receptor synthesis was provided by rapid biotin induction of receptor synthesis without an increase in gene transcript number.	Biotin	96-102	insulin receptor	Homo sapiens	47-63
11381801-10	2001	The insulin receptor is diminished on the cell surface membrane, tyrosine phosphorylation is decreased, serine and threonine phosphorylation is augmented.	Serine	104-110	insulin receptor	Homo sapiens	4-20
11381801-10	2001	The insulin receptor is diminished on the cell surface membrane, tyrosine phosphorylation is decreased, serine and threonine phosphorylation is augmented.	Threonine	115-124	insulin receptor	Homo sapiens	4-20
11158333-0	2001	Distinct functions of the two protein tyrosine phosphatase domains of LAR (leukocyte common antigen-related) on tyrosine dephosphorylation of insulin receptor.	Tyrosine	38-46	insulin receptor	Homo sapiens	142-158
11158333-4	2001	LAR associated with and preferentially dephosphorylated the insulin receptor that was tyrosine phosphorylated by insulin stimulation.	Tyrosine	86-94	insulin receptor	Homo sapiens	60-76
11158333-6	2001	The Cys-1522 to Ser mutant protein, which is defective in the LAR PTPase domain 1 catalytic site, was tightly associated with tyrosine-phosphorylated insulin receptor, but failed to dephosphorylate it, indicating that LAR PTPase domain 1 is critical for dephosphorylation of tyrosine-phosphorylated insulin receptor.	Tyrosine	126-134	insulin receptor	Homo sapiens	150-166
11084576-7	2000	In muscle tissues from pregnant control subjects vanadate increased tyrosine phosphorylation of the insulin receptor and insulin receptor substrate 1 to levels similar to those in muscle tissues from nonpregnant control subjects.	Vanadates	49-57	insulin receptor	Homo sapiens	121-137
11084576-7	2000	In muscle tissues from pregnant control subjects vanadate increased tyrosine phosphorylation of the insulin receptor and insulin receptor substrate 1 to levels similar to those in muscle tissues from nonpregnant control subjects.	Tyrosine	68-76	insulin receptor	Homo sapiens	100-116
11084576-8	2000	In patients with gestational diabetes mellitus vanadate increased insulin receptor and insulin receptor substrate 1 tyrosine phosphorylation, but these values remained less than in muscle tissues from nonpregnant control subjects (P<.05).	Vanadates	47-55	insulin receptor	Homo sapiens	66-82
11084576-8	2000	In patients with gestational diabetes mellitus vanadate increased insulin receptor and insulin receptor substrate 1 tyrosine phosphorylation, but these values remained less than in muscle tissues from nonpregnant control subjects (P<.05).	Vanadates	47-55	insulin receptor	Homo sapiens	87-103
11042115-6	2000	The PKC-specific inhibitors bisindolylmaleimide and Go 6976 abolish insulin-induced PLD2 activation in HEK-293 cells co-expressing the insulin receptor, PLC gamma and PLD2, confirming that not only PLD1, but PLD2 as well, is regulated in a PKC-dependent manner.	bisindolylmaleimide	28-47	insulin receptor	Homo sapiens	135-151
11042115-6	2000	The PKC-specific inhibitors bisindolylmaleimide and Go 6976 abolish insulin-induced PLD2 activation in HEK-293 cells co-expressing the insulin receptor, PLC gamma and PLD2, confirming that not only PLD1, but PLD2 as well, is regulated in a PKC-dependent manner.	Go 6976	52-59	insulin receptor	Homo sapiens	135-151
11154073-1	2000	It has been suggested that downstream signaling from the insulin receptor to the level of the protein kinases and protein phosphatases is accomplished by prosta-glandylinositol cyclic phosphate (cyclic PIP), a proposed second messenger of insulin.	prostaglandin-inositol cyclic phosphate	154-193	insulin receptor	Homo sapiens	57-73
11135668-2	2001	Based on a phosphoryl transfer mechanism involving a dissociative transition state, a potent and selective bisubstrate inhibitor for the insulin receptor tyrosine kinase was synthesized by linking ATPgammaS to a peptide substrate analog via a two-carbon spacer.	bisubstrate	107-118	insulin receptor	Homo sapiens	137-153
11135668-2	2001	Based on a phosphoryl transfer mechanism involving a dissociative transition state, a potent and selective bisubstrate inhibitor for the insulin receptor tyrosine kinase was synthesized by linking ATPgammaS to a peptide substrate analog via a two-carbon spacer.	adenosine 5'-O-(3-thiotriphosphate)	197-206	insulin receptor	Homo sapiens	137-153
10940390-0	2000	Autophosphorylation of the two C-terminal tyrosine residues Tyr1316 and Tyr1322 modulates the activity of the insulin receptor kinase in vitro.	Tyrosine	42-50	insulin receptor	Homo sapiens	110-126
10869355-0	2000	Probing the catalytic mechanism of the insulin receptor kinase with a tetrafluorotyrosine-containing peptide substrate.	tetrafluorotyrosine	70-89	insulin receptor	Homo sapiens	39-55
10923637-10	2000	Thus, we postulate that the decreased tyrosine kinase activity of the insulin receptor may be caused by serine/threonine phosphorylation by PKC.	Serine	104-110	insulin receptor	Homo sapiens	70-86
10923637-10	2000	Thus, we postulate that the decreased tyrosine kinase activity of the insulin receptor may be caused by serine/threonine phosphorylation by PKC.	Threonine	111-120	insulin receptor	Homo sapiens	70-86
11075717-9	2000	Sos is the predominant coupling pathway from the activated insulin receptor to p21ras.	sulfur monoxide	0-3	insulin receptor	Homo sapiens	59-75
11075718-0	2000	Stimulation by 1,25-dihydroxyvitamin D3 of insulin receptor expression and insulin responsiveness for glucose transport in U-937 human promonocytic cells.	Calcitriol	15-39	insulin receptor	Homo sapiens	43-59
11075718-1	2000	In the present work, we demonstrate that treatment with 1,25-dihydroxyvitamin D3 for 24 hours increased in a dose-dependent manner the levels of the two major insulin receptor (IR) mRNAs (11 and 8.5 Kb) present in U-937 human promonocytic cells.	Calcitriol	56-80	insulin receptor	Homo sapiens	159-180
11075718-3	2000	In these optimal conditions the stimulatory effect of 1,25-dihydroxyvitamin D3 was accompanied by increases in both IR capacity, and insulin responsiveness for glucose transport in these cells.	Calcitriol	54-78	insulin receptor	Homo sapiens	116-118
11225657-6	2000	RESULTS: Although insulin receptor number was similar in solubilized erythrocytes from the two groups, tyrosine kinase activity per insulin receptor was significantly (p < 0.02) greater in erythrocytes from glyburide-treated patients with type 2 diabetes.	Glyburide	210-219	insulin receptor	Homo sapiens	132-148
10927617-1	2000	Recent studies suggest that high glucose concentrations impair insulin receptor phosphorylation and kinase activation in certain cell models.	Glucose	33-40	insulin receptor	Homo sapiens	63-79
10764799-0	2000	Selective attenuation of metabolic branch of insulin receptor down-signaling by high glucose in a hepatoma cell line, HepG2 cells.	Glucose	85-92	insulin receptor	Homo sapiens	45-61
10764799-1	2000	The effects of a high concentration of glucose on the insulin receptor-down signaling were investigated in human hepatoma (HepG2) cells in vitro to delineate the molecular mechanism of insulin resistance under glucose toxicity.	Glucose	39-46	insulin receptor	Homo sapiens	54-70
10764780-9	2000	Failure to immunoprecipitate pp68 using antibodies directed against known 60-70-kDa tyrosine-phosphorylated proteins suggest that pp68 may be a novel cellular target that lies downstream of the insulin receptor.	Tyrosine	84-92	insulin receptor	Homo sapiens	194-210
10852715-1	2000	We examined the effects of mutations of tyrosine and serine autophosphorylation sites on the dual specificity of the insulin receptor kinase (IRKD) in vitro using autophosphorylation and substrate phosphorylation and phosphopeptide mapping.	Serine	53-59	insulin receptor	Homo sapiens	117-133
10852715-5	2000	Although the K(M) and V(MAX) values of this mutant were only slightly altered in substrate phosphorylation reactions using a recombinant C-terminal insulin receptor peptide (K(M): Y1151F, 9.9 +/- 0.4 microM; IRKD, 6.1 +/- 0.2 microM; V(MAX): Y1151F, 72 +/- 4 nmol min(-)(1) mg(-)(1); IRKD, 117 +/- 6 nmol min(-)(1) mg(-)(1)), diminished phosphate incorporation into serine residues of the peptide was observed.	Phosphates	337-346	insulin receptor	Homo sapiens	148-164
10852715-5	2000	Although the K(M) and V(MAX) values of this mutant were only slightly altered in substrate phosphorylation reactions using a recombinant C-terminal insulin receptor peptide (K(M): Y1151F, 9.9 +/- 0.4 microM; IRKD, 6.1 +/- 0.2 microM; V(MAX): Y1151F, 72 +/- 4 nmol min(-)(1) mg(-)(1); IRKD, 117 +/- 6 nmol min(-)(1) mg(-)(1)), diminished phosphate incorporation into serine residues of the peptide was observed.	Serine	366-372	insulin receptor	Homo sapiens	148-164
10852716-0	2000	Cysteine 981 of the human insulin receptor is required for covalent cross-linking between beta-subunit and a thiol-reactive membrane-associated protein.	Cysteine	0-8	insulin receptor	Homo sapiens	26-42
10852716-0	2000	Cysteine 981 of the human insulin receptor is required for covalent cross-linking between beta-subunit and a thiol-reactive membrane-associated protein.	Sulfhydryl Compounds	109-114	insulin receptor	Homo sapiens	26-42
10852716-2	2000	In this study, we examined the ability of the bifunctional cross-linking reagent 1,6-bismaleimidohexane (BMH) to covalently link IR with interacting proteins that possess reactive thiols.	1,6-bismaleimidohexane	81-103	insulin receptor	Homo sapiens	129-131
10852716-2	2000	In this study, we examined the ability of the bifunctional cross-linking reagent 1,6-bismaleimidohexane (BMH) to covalently link IR with interacting proteins that possess reactive thiols.	1,6-bismaleimidohexane	105-108	insulin receptor	Homo sapiens	129-131
10852716-2	2000	In this study, we examined the ability of the bifunctional cross-linking reagent 1,6-bismaleimidohexane (BMH) to covalently link IR with interacting proteins that possess reactive thiols.	Sulfhydryl Compounds	180-186	insulin receptor	Homo sapiens	129-131
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	Vanadates	84-92	insulin receptor	Homo sapiens	308-324
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	Vanadates	84-92	insulin receptor	Homo sapiens	326-328
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	pervanadate	97-108	insulin receptor	Homo sapiens	308-324
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	pervanadate	97-108	insulin receptor	Homo sapiens	326-328
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	Tyrosine	44-52	insulin receptor	Homo sapiens	308-324
10871840-1	2000	Treatment of cells with insulin and protein tyrosine phosphatase inhibitors such as vanadate and pervanadate resulted in the tyrosine phosphorylation of Grb10, a Src homology 2 (SH2) and pleckstrin homology domain-containing adaptor protein which binds to a number of receptor tyrosine kinases including the insulin receptor (IR).	Tyrosine	44-52	insulin receptor	Homo sapiens	326-328
10871840-6	2000	This mutant form of Grb10 bound with higher affinity to the IR in cells than that of the wild-type protein, suggesting that tyrosine phosphorylation of Grb10 may normally negatively regulate its binding to the IR.	Tyrosine	124-132	insulin receptor	Homo sapiens	60-62
10871840-6	2000	This mutant form of Grb10 bound with higher affinity to the IR in cells than that of the wild-type protein, suggesting that tyrosine phosphorylation of Grb10 may normally negatively regulate its binding to the IR.	Tyrosine	124-132	insulin receptor	Homo sapiens	210-212
10866039-0	2000	Serine residues 1177/78/82 of the insulin receptor are required for substrate phosphorylation but not autophosphorylation.	Serine	0-6	insulin receptor	Homo sapiens	34-50
10866039-1	2000	Serine residues of the human insulin receptor (HIR) may be phosphorylated and negatively regulate the insulin signal.	Serine	0-6	insulin receptor	Homo sapiens	29-45
10892730-1	2000	Our preliminary results are reported in the investigation of the tyrosine phosphorylation cascade triggered by the stimulation of the insulin receptor in the adipocyte cell line 3T3-L1 using a mini two-dimensional gel electrophoresis approach.	Tyrosine	65-73	insulin receptor	Homo sapiens	134-150
10984606-3	2000	Cellular subfractionation showed that the insulin receptor was associated with plasma membranes, from where it was not extractable with high salt or alkali, but a significant fraction was also localized in the nuclear fraction.	Salts	141-145	insulin receptor	Homo sapiens	42-58
10978177-0	2000	Identification of major tyrosine phosphorylation sites in the human insulin receptor substrate Gab-1 by insulin receptor kinase in vitro.	Tyrosine	24-32	insulin receptor	Homo sapiens	68-84
10978177-0	2000	Identification of major tyrosine phosphorylation sites in the human insulin receptor substrate Gab-1 by insulin receptor kinase in vitro.	Tyrosine	24-32	insulin receptor	Homo sapiens	104-120
10978177-7	2000	Our results demonstrate that hGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689).	Tyrosine	70-78	insulin receptor	Homo sapiens	58-60
11075717-3	2000	The NPXY motif around 960-Tyr residue of the insulin receptor binds to the N-terminal PTB domain of Shc.	Tyrosine	26-29	insulin receptor	Homo sapiens	45-61
10891367-6	2000	The reduced ATP level impaired insulin receptor (IR) autophosphorylation and tyrosine kinase activity toward substrates.	Adenosine Triphosphate	12-15	insulin receptor	Homo sapiens	31-47
10891367-6	2000	The reduced ATP level impaired insulin receptor (IR) autophosphorylation and tyrosine kinase activity toward substrates.	Adenosine Triphosphate	12-15	insulin receptor	Homo sapiens	49-51
10909978-1	2000	In patients harboring the IR1152 mutant insulin receptor, hepatic glucose production was normally suppressed by insulin.	Glucose	66-73	insulin receptor	Homo sapiens	40-56
10909978-9	2000	Thus, the mechanisms controlling insulin receptor internalization differ in liver and skeletal muscle cells and may enable IR1152 to control glucose metabolism selectively in liver.	Glucose	141-148	insulin receptor	Homo sapiens	33-49
10751417-7	2000	Compared with control cells, cells expressing high levels of PTP1B showed a 50-60% decrease in maximally insulin-stimulated tyrosyl phosphorylation of IR and insulin receptor substrate-1 (IRS-1) and phosphoinositide 3-kinase (PI3K) activity associated with IRS-1 or with phosphotyrosine.	cyclo(tyrosyl-tyrosyl)	124-131	insulin receptor	Homo sapiens	151-153
10751417-11	2000	Our results suggest that: 1) insulin stimulation of glucose transport in adipocytes requires </=45% of maximal tyrosyl phosphorylation of IR or IRS-1 and <50% of maximal activation of PI3K, 2) a novel PI3K-independent pathway may play a role in insulin-induced glucose transport in adipocytes, and 3) overexpression of PTP1B alone in adipocytes does not impair glucose transport.	Glucose	52-59	insulin receptor	Homo sapiens	141-143
10751417-11	2000	Our results suggest that: 1) insulin stimulation of glucose transport in adipocytes requires </=45% of maximal tyrosyl phosphorylation of IR or IRS-1 and <50% of maximal activation of PI3K, 2) a novel PI3K-independent pathway may play a role in insulin-induced glucose transport in adipocytes, and 3) overexpression of PTP1B alone in adipocytes does not impair glucose transport.	cyclo(tyrosyl-tyrosyl)	114-121	insulin receptor	Homo sapiens	141-143
10852715-0	2000	A single substitution of the insulin receptor kinase inhibits serine autophosphorylation in vitro: evidence for an interaction between the C-terminus and the activation loop.	Serine	62-68	insulin receptor	Homo sapiens	29-45
10852715-1	2000	We examined the effects of mutations of tyrosine and serine autophosphorylation sites on the dual specificity of the insulin receptor kinase (IRKD) in vitro using autophosphorylation and substrate phosphorylation and phosphopeptide mapping.	Tyrosine	40-48	insulin receptor	Homo sapiens	117-133
10940390-1	2000	Previously, several studies have demonstrated that autophosphorylation of the C-terminal tyrosine residues (Tyr1316 and Tyr1322) affects the signaling properties of the insulin receptor in vivo.	Tyrosine	89-97	insulin receptor	Homo sapiens	169-185
10777587-6	2000	Further, insulin-induced phosphorylation of downstream targets Akt and p70S6 kinase were also inhibited significantly by overexpression of PTEN, whereas tyrosine phosphorylation of the insulin receptor and IRS-1 or the phosphorylation of mitogen-activated protein kinase were not affected, suggesting that the Ras/mitogen-activated protein kinase pathway remains fully functional.	Tyrosine	153-161	insulin receptor	Homo sapiens	185-201
10769182-0	2000	Mutational analysis of the N-linked glycosylation sites of the human insulin receptor.	Nitrogen	27-28	insulin receptor	Homo sapiens	69-85
10804375-5	2000	The molecular grounds of insulin resistance could be an increased Serine phosphorylation of the insulin receptor.	Serine	66-72	insulin receptor	Homo sapiens	96-112
10747347-0	2000	Roles for insulin receptor, PI3-kinase, and Akt in insulin-signaling pathways related to production of nitric oxide in human vascular endothelial cells.	Nitric Oxide	103-115	insulin receptor	Homo sapiens	10-26
10744689-5	2000	These results show a novel pathway for intracellular signaling through the insulin receptor leading to the serine phosphorylation of key proteins involved in insulin action.	Serine	107-113	insulin receptor	Homo sapiens	75-91
10819237-0	2000	Serine residues 994 and 1023/25 are important for insulin receptor kinase inhibition by protein kinase C isoforms beta2 and theta.	Serine	0-6	insulin receptor	Homo sapiens	50-66
10871198-8	2000	Similarly, insulin receptor tyrosine phosphorylation was significantly decreased in subjects with GDM (P < 0.05) compared with pregnant and nonpregnant control subjects.	Tyrosine	28-36	insulin receptor	Homo sapiens	11-27
10819237-2	2000	It is speculated that serine residues in the insulin receptor beta-subunit are involved in receptor inhibition either as inhibitory phosphorylation sites or as part of receptor domains which bind inhibitory proteins or tyrosine phosphatases.	Serine	22-28	insulin receptor	Homo sapiens	45-61
10708756-0	2000	Properties of an insulin receptor with an IGF-1 receptor loop exchange in the cysteine-rich region.	Cysteine	78-86	insulin receptor	Homo sapiens	17-33
10708756-3	2000	In this report we have replaced residues 260-277 of human IR with residues 253-266 of the human IGF-1R to produce an IR-based, cysteine loop exchange chimaera, termed hIR-Cys loop exchange (CLX), in which all 14 amino acid residues in the exchanged loop differ from wild-type insulin receptor.	Cysteine	127-135	insulin receptor	Homo sapiens	117-119
10660532-8	2000	Okadaic acid, which rapidly induces insulin resistance in adipocytes independently of IR function, caused an almost quantitative release of IRS-1 into the cytosol commensurate with a significant reduction in tyrosyl-phosphorylated IRS proteins.	Okadaic Acid	0-12	insulin receptor	Homo sapiens	86-88
10694991-4	2000	There is also a modest but significant decrease in maximal insulin receptor tyrosine phosphorylation in muscle from obese GDM subjects.	Tyrosine	76-84	insulin receptor	Homo sapiens	59-75
10694991-5	2000	Results also suggest that increased insulin receptor serine/threonine phosphorylation and PC-1 could underlie the insulin resistance of pregnancy and pathogenesis of GDM.	Serine	53-59	insulin receptor	Homo sapiens	36-52
10694991-5	2000	Results also suggest that increased insulin receptor serine/threonine phosphorylation and PC-1 could underlie the insulin resistance of pregnancy and pathogenesis of GDM.	Threonine	60-69	insulin receptor	Homo sapiens	36-52
10720068-8	2000	The insulin resistance associated with pancreatic cancer is associated with a post-IR defect, which impairs skeletal muscle glycogen synthesis and glycogen storage.	Glycogen	124-132	insulin receptor	Homo sapiens	83-85
10720068-8	2000	The insulin resistance associated with pancreatic cancer is associated with a post-IR defect, which impairs skeletal muscle glycogen synthesis and glycogen storage.	Glycogen	147-155	insulin receptor	Homo sapiens	83-85
10726921-10	2000	Following vanadium, there was a consistent trend for increased basal levels of insulin receptor, Shc, and IRS-1 protein tyrosine phosphorylation and IRS-1-associated PI 3-kinase, but no further increase with insulin.	Vanadium	10-18	insulin receptor	Homo sapiens	79-95
10726921-15	2000	Vanadyl modifies proteins in human skeletal muscle involved in early insulin signaling, including basal insulin receptor and substrate tyrosine phosphorylation and activation of PI 3-kinase, and is not additive or synergistic with insulin at these steps.	Vanadates	0-7	insulin receptor	Homo sapiens	104-120
10793223-3	2000	Insulin-receptor conjugates were formed that carry a radioactive label as well as a biotin label.	Biotin	84-90	insulin receptor	Homo sapiens	0-16
10803466-8	2000	Two domains of Grb7 are implicated in the insulin receptor binding: the SH2 domain and the PIR (phosphotyrosine interacting region).	Phosphotyrosine	96-111	insulin receptor	Homo sapiens	42-58
10660596-2	2000	Regulation of the steady-state tyrosine phosphorylation of the insulin receptor and its postreceptor substrates are essential determinants of insulin signal transduction.	Tyrosine	31-39	insulin receptor	Homo sapiens	63-79
10705100-5	2000	Chromium increases insulin binding to cells, insulin receptor number and activates insulin receptor kinase leading to increased insulin sensitivity.	Chromium	0-8	insulin receptor	Homo sapiens	45-61
10650943-3	2000	Shp-2 becomes activated upon binding through one or both SH2 domains to tyrosine phosphorylated molecules such as Shc or insulin receptor substrates.	Tyrosine	72-80	insulin receptor	Homo sapiens	121-137
10650943-4	2000	We were interested in finding a new molecule(s), tyrosine phosphorylated by the insulin receptor (IR), that could interact with Shp-2.	Tyrosine	49-57	insulin receptor	Homo sapiens	80-96
10650943-4	2000	We were interested in finding a new molecule(s), tyrosine phosphorylated by the insulin receptor (IR), that could interact with Shp-2.	Tyrosine	49-57	insulin receptor	Homo sapiens	98-100
10868945-7	2000	In skeletal muscle from type 2 diabetic subjects, IRS-1 phosphorylation, PI 3-kinase activity, and glucose transport activity were impaired, whereas insulin receptor tyrosine phosphorylation, MAP kinase phosphorylation, and glycogen synthase activity were normal.	Tyrosine	166-174	insulin receptor	Homo sapiens	149-165
10655627-6	2000	The kinase activity of insulin receptor-agonist complexes increased in the order of IGF-II < IGF-I < insulin, and neither vanadium ions nor thiazolidine-type medicines for NIDDM, troglitazone and pioglitazone, directly acted on both the kinase reaction of insulin receptor or the binding of pY939 to SH2N.	Vanadium	128-136	insulin receptor	Homo sapiens	23-39
11450502-6	2000	Phosphotyrosine immunoblotting revealed that apparent insulin receptor autophosphorylation was visible only with IgG-NOV, not with the IgG-JAN or -FEB. Mutation of tyrosine-960 or lysine-1018 of the insulin receptor failed to transduce the IgG"s stimulatory effect.	Phosphotyrosine	0-15	insulin receptor	Homo sapiens	54-70
11450502-6	2000	Phosphotyrosine immunoblotting revealed that apparent insulin receptor autophosphorylation was visible only with IgG-NOV, not with the IgG-JAN or -FEB. Mutation of tyrosine-960 or lysine-1018 of the insulin receptor failed to transduce the IgG"s stimulatory effect.	Tyrosine	7-15	insulin receptor	Homo sapiens	54-70
11450502-6	2000	Phosphotyrosine immunoblotting revealed that apparent insulin receptor autophosphorylation was visible only with IgG-NOV, not with the IgG-JAN or -FEB. Mutation of tyrosine-960 or lysine-1018 of the insulin receptor failed to transduce the IgG"s stimulatory effect.	Lysine	180-186	insulin receptor	Homo sapiens	54-70
10655627-6	2000	The kinase activity of insulin receptor-agonist complexes increased in the order of IGF-II < IGF-I < insulin, and neither vanadium ions nor thiazolidine-type medicines for NIDDM, troglitazone and pioglitazone, directly acted on both the kinase reaction of insulin receptor or the binding of pY939 to SH2N.	Troglitazone	185-197	insulin receptor	Homo sapiens	23-39
10655627-6	2000	The kinase activity of insulin receptor-agonist complexes increased in the order of IGF-II < IGF-I < insulin, and neither vanadium ions nor thiazolidine-type medicines for NIDDM, troglitazone and pioglitazone, directly acted on both the kinase reaction of insulin receptor or the binding of pY939 to SH2N.	Pioglitazone	202-214	insulin receptor	Homo sapiens	23-39
10574975-6	1999	The beta-subunit of the insulin receptor was labeled with a maleimide-gold conjugate, which allowed orientation of the receptor complex in the membrane bilayer.	maleimide-gold	60-74	insulin receptor	Homo sapiens	24-40
10594015-1	2000	Insulin receptor substrate (IRS) proteins are tyrosine phosphorylated and mediate multiple signals during activation of the receptors for insulin, insulin-like growth factor 1 (IGF-1), and various cytokines.	Tyrosine	46-54	insulin receptor	Homo sapiens	0-16
10591140-4	1999	DMHV was more effective in increasing both the phosphotyrosine levels of various proteins in 3T3L1 fibroblasts and the level of insulin-receptor phosphorylation in CHO cells overexpressing the human insulin receptor.	bis(N,N-dimethylhydroxamido)hydroxooxovanadate	0-4	insulin receptor	Homo sapiens	199-215
10544179-5	1999	By extraction with beta-cyclodextrin or destruction with cholesterol oxidase, cholesterol reduction attenuated insulin receptor signaling to protein phosphorylation or glucose transport.	betadex	19-36	insulin receptor	Homo sapiens	111-127
10545192-2	1999	We have shown previously that vanadium salts activate mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase activities (PI3-K) via a pathway that does not involve the insulin receptor (IR) tyrosine kinase function [Pandey, S. K., Anand-Srivastava, M. B., and Srivastava, A. K. (1998) Biochemistry 37, 7006-7014].	vanadium salts	30-44	insulin receptor	Homo sapiens	205-207
10545192-4	1999	Treatment of IR-overexpressing cells with VS resulted in an increased level of tyrosine phosphorylation of p44(mapk) (ERK-1) and p42(mapk) (ERK-2) along with stimulation of MAPK, MAPK kinase (MEK), and C-raf-1 activities, and ras activation.	Tyrosine	79-87	insulin receptor	Homo sapiens	13-15
10544179-5	1999	By extraction with beta-cyclodextrin or destruction with cholesterol oxidase, cholesterol reduction attenuated insulin receptor signaling to protein phosphorylation or glucose transport.	Glucose	168-175	insulin receptor	Homo sapiens	111-127
10544179-9	1999	Insulin stimulation of cells prior to isolation of caveolae or insulin stimulation of the isolated caveolae fraction increased tyrosine phosphorylation of the insulin receptor in caveolae, demonstrating that insulin receptors in caveolae are functional.	Tyrosine	127-135	insulin receptor	Homo sapiens	159-175
10490615-9	1999	In summary, (i) Galphaq appears to play a necessary role in insulin-stimulated glucose transport, (ii) Galphaq action in the insulin signaling pathway is upstream of and dependent upon PI3-kinase, and (iii) Galphaq can transmit signals from the insulin receptor to the p110alpha subunit of PI3-kinase, which leads to GLUT4 translocation.	galphaq	103-110	insulin receptor	Homo sapiens	245-261
10521479-4	1999	The wild-type insulin receptor chimera mediated approximately 2-fold greater phosphorylation of insulin receptor substrate 1 (IRS-1), association of IRS-1 with phosphoinositide 3-kinase, stimulation of glucose uptake, and GLUT4 translocation, compared with the IGF-I receptor chimera.	Glucose	202-209	insulin receptor	Homo sapiens	14-30
10490615-9	1999	In summary, (i) Galphaq appears to play a necessary role in insulin-stimulated glucose transport, (ii) Galphaq action in the insulin signaling pathway is upstream of and dependent upon PI3-kinase, and (iii) Galphaq can transmit signals from the insulin receptor to the p110alpha subunit of PI3-kinase, which leads to GLUT4 translocation.	galphaq	103-110	insulin receptor	Homo sapiens	245-261
10488146-1	1999	Serine phosphorylation of insulin receptor substrate-1 (IRS-1) reduces its ability to act as an insulin receptor substrate and inhibits insulin receptor signal transduction.	Serine	0-6	insulin receptor	Homo sapiens	26-42
10488146-1	1999	Serine phosphorylation of insulin receptor substrate-1 (IRS-1) reduces its ability to act as an insulin receptor substrate and inhibits insulin receptor signal transduction.	Serine	0-6	insulin receptor	Homo sapiens	96-112
10480612-6	1999	The maximal effect of insulin on tyrosine phosphorylation of the insulin receptor was 37% lower (P < 0.05) in GDM subjects than in pregnant control subjects and was not related to changes in the abundance of the insulin receptor.	Tyrosine	33-41	insulin receptor	Homo sapiens	65-81
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Tyrosine	62-65	insulin receptor	Homo sapiens	85-101
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Tyrosine	62-65	insulin receptor	Homo sapiens	113-115
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Serine	162-165	insulin receptor	Homo sapiens	85-101
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Serine	162-165	insulin receptor	Homo sapiens	113-115
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Threonine	169-172	insulin receptor	Homo sapiens	85-101
10497255-1	1999	Incubation of cells with insulin leads to a transient rise in Tyr phosphorylation of insulin receptor substrate (IRS) proteins, accompanied by elevation in their Ser(P)/Thr(P) content and their dissociation from the insulin receptor (IR).	Threonine	169-172	insulin receptor	Homo sapiens	113-115
10497255-2	1999	Wortmannin, a phosphatidylinositol 3-kinase inhibitor, selectively prevented the increase in Ser(P)/Thr(P) content of IRS-1, its dissociation from IR, and the decrease in its Tyr(P) content following 60 min of insulin treatment.	Wortmannin	0-10	insulin receptor	Homo sapiens	118-120
10497255-2	1999	Wortmannin, a phosphatidylinositol 3-kinase inhibitor, selectively prevented the increase in Ser(P)/Thr(P) content of IRS-1, its dissociation from IR, and the decrease in its Tyr(P) content following 60 min of insulin treatment.	Serine	93-96	insulin receptor	Homo sapiens	118-120
10497255-2	1999	Wortmannin, a phosphatidylinositol 3-kinase inhibitor, selectively prevented the increase in Ser(P)/Thr(P) content of IRS-1, its dissociation from IR, and the decrease in its Tyr(P) content following 60 min of insulin treatment.	Threonine	100-103	insulin receptor	Homo sapiens	118-120
10497255-7	1999	These results implicate a wortmannin-sensitive Ser/Thr kinase, different from PKB, as the kinase that phosphorylates IRS-1 and acts as the feedback control regulator that turns off insulin signals by inducting the dissociation of IRS proteins from IR.	Wortmannin	26-36	insulin receptor	Homo sapiens	117-119
10622410-6	1999	Experiments with the RNA synthesis inhibitor actinomycin D indicated that the decrease in IR mRNA content in aldosterone-treated cells was not the result of transcript destabilisation.	Dactinomycin	45-58	insulin receptor	Homo sapiens	90-92
10446056-4	1999	The 3D reconstruction indicates that the two alpha subunits jointly participate in insulin binding and that the kinase domains in the two beta subunits are in a juxtaposition that permits autophosphorylation of tyrosine residues in the first step of insulin receptor activation.	Tyrosine	211-219	insulin receptor	Homo sapiens	250-266
10622410-7	1999	The inhibitory action of aldosterone was not prevented by the simultaneous presence of the protein synthesis inhibitor cycloheximide, suggesting that the reduction of IR gene expression occurs as a direct response to the action of aldosterone.	Aldosterone	25-36	insulin receptor	Homo sapiens	167-169
10622410-7	1999	The inhibitory action of aldosterone was not prevented by the simultaneous presence of the protein synthesis inhibitor cycloheximide, suggesting that the reduction of IR gene expression occurs as a direct response to the action of aldosterone.	Aldosterone	231-242	insulin receptor	Homo sapiens	167-169
10622410-10	1999	These results provide the first evidence for an in vitro modulation of human IR expression by aldosterone.	Aldosterone	94-105	insulin receptor	Homo sapiens	77-79
10433244-5	1999	This insulin-induced insulin receptor trafficking was not affected by treatment of the cells with PI3-kinase inhibitor (wortmannin), whereas treatment with MEK [mitogen-activated protein (MAP) kinase-Erk kinase] inhibitor (PD98059) partly inhibited the process in a dose-dependent manner.	Wortmannin	120-130	insulin receptor	Homo sapiens	21-37
10417330-0	1999	APS, an adapter protein with a PH and SH2 domain, is a substrate for the insulin receptor kinase.	aps	0-3	insulin receptor	Homo sapiens	73-89
10417330-4	1999	Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS.	aps	18-21	insulin receptor	Homo sapiens	41-57
10417330-4	1999	Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS.	Tyrosine	131-139	insulin receptor	Homo sapiens	41-57
10417330-4	1999	Here we show that APS interacts with the insulin receptor kinase activation loop through its SH2 domain and insulin stimulates the tyrosine-phosphorylation of APS.	aps	159-162	insulin receptor	Homo sapiens	41-57
10433244-5	1999	This insulin-induced insulin receptor trafficking was not affected by treatment of the cells with PI3-kinase inhibitor (wortmannin), whereas treatment with MEK [mitogen-activated protein (MAP) kinase-Erk kinase] inhibitor (PD98059) partly inhibited the process in a dose-dependent manner.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	223-230	insulin receptor	Homo sapiens	21-37
10437794-8	1999	In vitro studies demonstrate that Src associated in mitosis 68 associates with the Src homology 2 domains of p85 after tyrosine phosphorylation by the activated insulin receptor.	Tyrosine	119-127	insulin receptor	Homo sapiens	161-177
10433244-6	1999	Interestingly, treatment with both wortmannin and PD98059 almost completely inhibited insulin receptor trafficking.	Wortmannin	35-45	insulin receptor	Homo sapiens	86-102
10433244-6	1999	Interestingly, treatment with both wortmannin and PD98059 almost completely inhibited insulin receptor trafficking.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	50-57	insulin receptor	Homo sapiens	86-102
10433244-9	1999	Furthermore, to determine the crucial step for the requirement of PI3-kinase and MAP kinase pathways, the effect of wortmannin and PD98059 on insulin receptor endocytosis was studied.	Wortmannin	116-126	insulin receptor	Homo sapiens	142-158
10433244-9	1999	Furthermore, to determine the crucial step for the requirement of PI3-kinase and MAP kinase pathways, the effect of wortmannin and PD98059 on insulin receptor endocytosis was studied.	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	131-138	insulin receptor	Homo sapiens	142-158
10395191-6	1999	A reduction in tyrosine phosphorylation of both the insulin receptor (IR) and the insulin receptor substrate-1 (IRS-1) has been noted in both animal and human type 2 diabetes.	Tyrosine	15-23	insulin receptor	Homo sapiens	52-73
10456437-0	1999	Metformin modulates insulin receptor signaling in normal and cholesterol-treated human hepatoma cells (HepG2).	Metformin	0-9	insulin receptor	Homo sapiens	20-36
10456437-0	1999	Metformin modulates insulin receptor signaling in normal and cholesterol-treated human hepatoma cells (HepG2).	Cholesterol	61-72	insulin receptor	Homo sapiens	20-36
10416561-10	1999	The exercise-induced decreased insulin receptor tyrosine phosphorylation could explain the well-known effect of exercise to enhance the sensitivity of muscle to insulin.	Tyrosine	48-56	insulin receptor	Homo sapiens	31-47
10456437-9	1999	Overall, the results suggest that metformin may interact with the insulin receptor and/or a component involved in the early steps of insulin signal transduction.	Metformin	34-43	insulin receptor	Homo sapiens	66-82
10329994-0	1999	Insulin receptor autophosphorylation in cultured myoblasts correlates to glucose disposal in Pima Indians.	Glucose	73-80	insulin receptor	Homo sapiens	0-16
10350617-3	1999	Tyrosine phosphorylation of insulin receptor substrate (IRS) molecules is a specific IR post-receptor response.	Tyrosine	0-8	insulin receptor	Homo sapiens	28-44
10231542-1	1999	In this study, we used maleimidobutyrylbiocytin to examine possible alteration that may occur in the redox state of the insulin receptor (IR) sulfhydryl groups in response to reduced glutathione (GSH) or N-acetyl-L-cysteine (NAC).	Glutathione	183-194	insulin receptor	Homo sapiens	120-136
10231542-1	1999	In this study, we used maleimidobutyrylbiocytin to examine possible alteration that may occur in the redox state of the insulin receptor (IR) sulfhydryl groups in response to reduced glutathione (GSH) or N-acetyl-L-cysteine (NAC).	Glutathione	183-194	insulin receptor	Homo sapiens	138-140
10231542-1	1999	In this study, we used maleimidobutyrylbiocytin to examine possible alteration that may occur in the redox state of the insulin receptor (IR) sulfhydryl groups in response to reduced glutathione (GSH) or N-acetyl-L-cysteine (NAC).	Glutathione	196-199	insulin receptor	Homo sapiens	120-136
10231542-1	1999	In this study, we used maleimidobutyrylbiocytin to examine possible alteration that may occur in the redox state of the insulin receptor (IR) sulfhydryl groups in response to reduced glutathione (GSH) or N-acetyl-L-cysteine (NAC).	Glutathione	196-199	insulin receptor	Homo sapiens	138-140
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Glutathione	73-76	insulin receptor	Homo sapiens	65-67
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Glutathione	73-76	insulin receptor	Homo sapiens	127-129
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Disulfides	144-154	insulin receptor	Homo sapiens	65-67
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Disulfides	144-154	insulin receptor	Homo sapiens	127-129
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Sulfhydryl Compounds	200-205	insulin receptor	Homo sapiens	65-67
10231542-4	1999	Similar findings were obtained in cells transfected with IR mutants lacking cysteine524, one of the class I disulfides that link the two IR alpha-subunits.	cysteine524	76-87	insulin receptor	Homo sapiens	57-59
10231542-4	1999	Similar findings were obtained in cells transfected with IR mutants lacking cysteine524, one of the class I disulfides that link the two IR alpha-subunits.	Disulfides	108-118	insulin receptor	Homo sapiens	57-59
10231542-6	1999	No difference in insulin binding was observed in GSH-treated cells; however, ligand-mediated increases in IR autophosphorylation, tyrosine phosphorylation of cellular substrates, and dual phosphorylation of the downstream target mitogen-activated protein kinase were inhibited at concentrations of GSH (10 mM or greater) that yielded a significant increase in IR alpha-subunit thiol reactivity.	Glutathione	298-301	insulin receptor	Homo sapiens	106-108
10231542-6	1999	No difference in insulin binding was observed in GSH-treated cells; however, ligand-mediated increases in IR autophosphorylation, tyrosine phosphorylation of cellular substrates, and dual phosphorylation of the downstream target mitogen-activated protein kinase were inhibited at concentrations of GSH (10 mM or greater) that yielded a significant increase in IR alpha-subunit thiol reactivity.	Sulfhydryl Compounds	377-382	insulin receptor	Homo sapiens	106-108
10049496-8	1999	Because residues similar to Lys 782 in the sequences of mitogen-activated protein kinase and insulin receptor make contact with a ribose hydroxyl of ATP, it is proposed that Lys 782 may be one of the residues composing the ribose-binding site of epidermal growth factor receptor.	Lysine	28-31	insulin receptor	Homo sapiens	93-109
10210639-4	1999	IR mRNA was quantified by S1-nuclease assay using a 195-bp digoxigenin-labeled IR DNA probe and normalized to the level of expression of the glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene.	Digoxigenin	59-70	insulin receptor	Homo sapiens	0-2
10210639-4	1999	IR mRNA was quantified by S1-nuclease assay using a 195-bp digoxigenin-labeled IR DNA probe and normalized to the level of expression of the glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene.	Digoxigenin	59-70	insulin receptor	Homo sapiens	79-81
10338114-0	1999	The inhibitory effect of 2-deoxyglucose on insulin receptor autophosphorylation does not depend on known serine phosphorylation sites or other conserved serine residues of the receptor beta-subunit.	Deoxyglucose	25-39	insulin receptor	Homo sapiens	43-59
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Glucose	46-55	insulin receptor	Homo sapiens	86-102
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Glucose	46-55	insulin receptor	Homo sapiens	186-202
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Deoxyglucose	59-73	insulin receptor	Homo sapiens	86-102
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Deoxyglucose	59-73	insulin receptor	Homo sapiens	186-202
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Serine	156-162	insulin receptor	Homo sapiens	86-102
10338114-2	1999	It is known that supraphysiological levels of D-glucose or 2-deoxyglucose inhibit the insulin receptor and it is speculated that this effect is mediated by serine phosphorylation of the insulin receptor beta-subunit and other proteins of the insulin signaling chain.	Serine	156-162	insulin receptor	Homo sapiens	186-202
10338114-5	1999	2-Deoxyglucose consistently inhibits insulin stimulated autophosphorylation of all constructs to the same degree as observed in wild-type human insulin receptor.	Deoxyglucose	0-14	insulin receptor	Homo sapiens	144-160
10196204-4	1999	We show that APS associates with phosphotyrosines situated within the activation loop of the insulin receptor via the APS Src homology 2 domain.	Phosphotyrosine	33-49	insulin receptor	Homo sapiens	93-109
10230647-0	1999	Role of proline 193 in the insulin receptor post-translational processing.	Proline	8-15	insulin receptor	Homo sapiens	27-43
10049496-8	1999	Because residues similar to Lys 782 in the sequences of mitogen-activated protein kinase and insulin receptor make contact with a ribose hydroxyl of ATP, it is proposed that Lys 782 may be one of the residues composing the ribose-binding site of epidermal growth factor receptor.	ribose hydroxyl	130-145	insulin receptor	Homo sapiens	93-109
10049496-8	1999	Because residues similar to Lys 782 in the sequences of mitogen-activated protein kinase and insulin receptor make contact with a ribose hydroxyl of ATP, it is proposed that Lys 782 may be one of the residues composing the ribose-binding site of epidermal growth factor receptor.	Adenosine Triphosphate	149-152	insulin receptor	Homo sapiens	93-109
10049496-8	1999	Because residues similar to Lys 782 in the sequences of mitogen-activated protein kinase and insulin receptor make contact with a ribose hydroxyl of ATP, it is proposed that Lys 782 may be one of the residues composing the ribose-binding site of epidermal growth factor receptor.	Lysine	174-177	insulin receptor	Homo sapiens	93-109
10049496-8	1999	Because residues similar to Lys 782 in the sequences of mitogen-activated protein kinase and insulin receptor make contact with a ribose hydroxyl of ATP, it is proposed that Lys 782 may be one of the residues composing the ribose-binding site of epidermal growth factor receptor.	Ribose	130-136	insulin receptor	Homo sapiens	93-109
10196112-1	1999	The insulin receptor (IR) is a four-chain, transmembrane dimer held together by disulfide bonds.	Disulfides	80-89	insulin receptor	Homo sapiens	4-20
10196112-1	1999	The insulin receptor (IR) is a four-chain, transmembrane dimer held together by disulfide bonds.	Disulfides	80-89	insulin receptor	Homo sapiens	22-24
10196112-5	1999	Fab 83-7, which recognizes the cys-rich region of IR, bound halfway up one end of each side arm in a diametrically opposite manner, indicating a twofold axis of symmetry normal to the membrane surface.	Cysteine	31-34	insulin receptor	Homo sapiens	50-52
10196112-7	1999	These images, together with the data from the recently determined 3D structure of the first three domains of the insulin-like growth factor type I receptor, suggest that the IR dimer is organized into two layers with the L1/cys-rich/L2 domains occupying the upper (membrane distal) region of the U-shaped prism and the fibronectin type III domains and the insert domains located predominantly in the membrane-proximal region.	Cysteine	224-227	insulin receptor	Homo sapiens	174-176
9884156-2	1998	Previous studies demonstrated that the adverse effects of ethanol are mediated by inhibition of tyrosyl phosphorylation of the insulin receptor and the insulin receptor substrate-type 1 (IRS-1).	Ethanol	58-65	insulin receptor	Homo sapiens	127-143
9883910-2	1998	The three-dimensional structures of the tyrosine kinase domain of the IR and the first three extracellular domains (L1, Cys-rich and L2) of the IGF1R are known.	Cysteine	120-123	insulin receptor	Homo sapiens	70-72
9884156-2	1998	Previous studies demonstrated that the adverse effects of ethanol are mediated by inhibition of tyrosyl phosphorylation of the insulin receptor and the insulin receptor substrate-type 1 (IRS-1).	cyclo(tyrosyl-tyrosyl)	96-103	insulin receptor	Homo sapiens	127-143
10417854-2	1998	Insulin binds to the extracellular domain of the insulin receptor and induces conformational changes in the receptor, leading to autophosphorylation of the receptor on intracellular tyrosine residues.	Tyrosine	182-190	insulin receptor	Homo sapiens	49-65
10643053-2	1999	Various models simulating the interaction of regulatory subunits of PI-3-kinase and of their substrates (insulin receptor sustrate proteins phosphorylated on tyrosin residues) with molecules of receptors-tyrosinekinases have been considered.	Tyrosine	158-165	insulin receptor	Homo sapiens	105-121
9833943-8	1998	Insulin was four times more effective in stimulating tyrosine phosphorylation of the insulin receptor in subcutaneous fat cells (p < 0.001).	Tyrosine	53-61	insulin receptor	Homo sapiens	85-101
9922107-11	1998	An integrating link between insulin resistance and hyperandrogenemia may be serine phosphorylation, which inhibits activity of the insulin receptor and promotes the 17,20-lyase activity of P450c17.	Serine	76-82	insulin receptor	Homo sapiens	131-147
9801804-1	1998	Chromium (Cr), an essential element, mainly affects saccharide (potentiated insulin action via interaction with insulin receptor on the cell surface) and lipid metabolism (inhibition of hydroxymethylglutaryl-CoA reductase with a hypolipidemic effect).	Chromium	0-8	insulin receptor	Homo sapiens	112-128
9801804-1	1998	Chromium (Cr), an essential element, mainly affects saccharide (potentiated insulin action via interaction with insulin receptor on the cell surface) and lipid metabolism (inhibition of hydroxymethylglutaryl-CoA reductase with a hypolipidemic effect).	Chromium	10-12	insulin receptor	Homo sapiens	112-128
9801804-1	1998	Chromium (Cr), an essential element, mainly affects saccharide (potentiated insulin action via interaction with insulin receptor on the cell surface) and lipid metabolism (inhibition of hydroxymethylglutaryl-CoA reductase with a hypolipidemic effect).	Carbohydrates	52-62	insulin receptor	Homo sapiens	112-128
10417854-3	1998	These phosphorylated tyrosine residues act as binding sites for proteins which subsequently may be phosphorylated by the insulin receptor.	Tyrosine	21-29	insulin receptor	Homo sapiens	121-137
9760308-7	1998	The signal generated by the insulin receptor, as reflected in the extent of insulin receptor substrate-1 tyrosine phosphorylation, was unchanged after the exercise.	Tyrosine	105-113	insulin receptor	Homo sapiens	28-44
9738014-3	1998	Although the tyrosine phosphorylation of insulin receptor substrate-1 was slightly reduced, correlating with a 25% decrease in insulin receptor substrate-1-associated phosphatidylinositol 3-kinase activity, insulin-stimulated Akt kinase activation was unaffected.	Tyrosine	13-21	insulin receptor	Homo sapiens	41-57
9727002-11	1998	Insulin potentiated the effects of IGF-1, EGF, and PDGF on DNA synthesis in cells expressing the wild type insulin receptor, but this potentiation was inhibited in the presence of the FTase inhibitor, alpha-hydroxyfarnesylphosphonic acid.	(alpha-hydroxyfarnesyl)phosphonic acid	201-237	insulin receptor	Homo sapiens	107-123
9832615-7	1998	These results indicate that the opposite regulation of Cas phosphorylation by insulin and IGF-I may be mediated through different properties of their receptors, and that the interaction of the insulin receptor with SHP-2 may play an important role in determining the tyrosine-phosphorylation state of Cas.	Tyrosine	267-275	insulin receptor	Homo sapiens	193-209
9681494-3	1998	Bufo insulin was, however, more potent (4-fold) than human insulin in inhibiting the binding of [125I-Tyr-A14] insulin to the soluble full-length recombinant human insulin receptor, which is probably a consequence of the substitution (Thr --> His) at position A-8.	125i-tyr-a14	97-109	insulin receptor	Homo sapiens	164-180
9829343-1	1998	The aim of this study was to investigate the effect of sodium orthovanadate on the alterations of human erythrocytes insulin receptor autophosphorylation.	Sodium orthovanadate	55-75	insulin receptor	Homo sapiens	117-133
9829343-4	1998	When the erythrocytes were treated with insulin and then reincubated in insulin-free medium, vanadate completely inhibited insulin receptor dephosphorylation, although it had no effect on in vitro receptor autophosphorylation.	Vanadates	93-101	insulin receptor	Homo sapiens	123-139
9844992-6	1998	We would suggest that n-6 fatty acids, and in particular arachidonic acid, modify the membrane environment of the insulin receptor (or the glucose transporters) so that lower levels of insulin are required for glucose homeostasis.	Fatty Acids, Omega-6	22-37	insulin receptor	Homo sapiens	114-130
9844992-6	1998	We would suggest that n-6 fatty acids, and in particular arachidonic acid, modify the membrane environment of the insulin receptor (or the glucose transporters) so that lower levels of insulin are required for glucose homeostasis.	Arachidonic Acid	57-73	insulin receptor	Homo sapiens	114-130
9685425-7	1998	Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation.	Adenosine Triphosphate	27-30	insulin receptor	Homo sapiens	122-138
9685425-7	1998	Reduction of intracellular ATP using azide inhibited Glut 1 and Glut 4 translocation from the LDM to the plasma membrane, insulin receptor autophosphorylation, and IRS-1 tyrosine phosphorylation.	Azides	37-42	insulin receptor	Homo sapiens	122-138
9681494-3	1998	Bufo insulin was, however, more potent (4-fold) than human insulin in inhibiting the binding of [125I-Tyr-A14] insulin to the soluble full-length recombinant human insulin receptor, which is probably a consequence of the substitution (Thr --> His) at position A-8.	Threonine	235-238	insulin receptor	Homo sapiens	164-180
9681494-3	1998	Bufo insulin was, however, more potent (4-fold) than human insulin in inhibiting the binding of [125I-Tyr-A14] insulin to the soluble full-length recombinant human insulin receptor, which is probably a consequence of the substitution (Thr --> His) at position A-8.	Histidine	246-249	insulin receptor	Homo sapiens	164-180
9651339-1	1998	Insulin receptor substrates (IRSs) are tyrosine-phosphorylated following stimulation with insulin, insulin-like growth factors (IGFs), and interleukins.	Tyrosine	39-47	insulin receptor	Homo sapiens	0-16
9671232-8	1998	Next, we studied insulin receptor substrate-1 (IRS-1), a major endogenous substrate for the insulin receptor which, when tyrosine is phosphorylated by the insulin receptor, interacts with and activates PI3-K.	Tyrosine	121-129	insulin receptor	Homo sapiens	17-33
9671232-8	1998	Next, we studied insulin receptor substrate-1 (IRS-1), a major endogenous substrate for the insulin receptor which, when tyrosine is phosphorylated by the insulin receptor, interacts with and activates PI3-K.	Tyrosine	121-129	insulin receptor	Homo sapiens	92-108
9671232-10	1998	In these cells, both Shc tyrosine phosphorylation and mitogen-activated protein kinase (MAP-K) activity were increased by the insulin receptor (indicating that the p21ras pathway may account for insulin-stimulated cell growth in ZR-75-1 cells).	Tyrosine	25-33	insulin receptor	Homo sapiens	126-142
9668343-7	1998	GM3 inhibits both the epidermal growth factor receptor and basic fibroblast factor receptor; several gangliosides except GM3 inhibit the platelet-derived growth-factor receptor; GM1 enhances nerve growth-factor-stimulated activation of TrkA; insulin receptor is inhibited to varying degrees by several gangliosides, but 2-->3 sialosylparagloboside is most effective.	G(M1) Ganglioside	178-181	insulin receptor	Homo sapiens	242-258
9686926-2	1998	We have previously shown that phorbol ester stimulated PKC beta1 and beta2 as well as tumor necrosis factor-alpha (TNFalpha) stimulated PKC epsilon inhibit human insulin receptor (HIR) signalling.	Phorbol Esters	30-43	insulin receptor	Homo sapiens	162-178
9658397-1	1998	The newly identified insulin receptor (IR) substrate, Gab1 [growth factor receptor bound 2 (Grb2)-associated binder-1] is rapidly phosphorylated on several tyrosine residues by the activated IR.	Tyrosine	156-164	insulin receptor	Homo sapiens	21-37
9658397-1	1998	The newly identified insulin receptor (IR) substrate, Gab1 [growth factor receptor bound 2 (Grb2)-associated binder-1] is rapidly phosphorylated on several tyrosine residues by the activated IR.	Tyrosine	156-164	insulin receptor	Homo sapiens	39-41
9658397-1	1998	The newly identified insulin receptor (IR) substrate, Gab1 [growth factor receptor bound 2 (Grb2)-associated binder-1] is rapidly phosphorylated on several tyrosine residues by the activated IR.	Tyrosine	156-164	insulin receptor	Homo sapiens	191-193
9658397-5	1998	Our results demonstrate that to interact with p85 or SHP-2 SH2 domains, Gab1 must be tyrosine phosphorylated by IR.	Tyrosine	85-93	insulin receptor	Homo sapiens	112-114
9620279-2	1998	In the present paper, we show that exposure of these erythrocytes to the strong oxidizing agent menadione before addition of insulin blocks insulin receptor internalization as well as the decrease in electrical parameters associated with this process.	Vitamin K 3	96-105	insulin receptor	Homo sapiens	140-156
9564038-1	1998	Insulin stimulation of Chinese hamster ovary cells expressing the human insulin receptor resulted in a time-dependent decrease in the amount of GTP bound to Rap1.	Guanosine Triphosphate	144-147	insulin receptor	Homo sapiens	72-88
9607389-0	1998	Insulin receptor number in arterial hypertension: response to treatment with fosinopril or atenolol.	Fosinopril	77-87	insulin receptor	Homo sapiens	0-16
9607389-0	1998	Insulin receptor number in arterial hypertension: response to treatment with fosinopril or atenolol.	Atenolol	91-99	insulin receptor	Homo sapiens	0-16
9578588-3	1998	We have shown earlier that different vanadium salts stimulate the MAP kinase pathway and ribosomal-S-6-kinase (p70s6k) in chinese hamster ovary cells overexpressing human insulin receptor (CHO-HIR cells) [Pandey, S. K., Chiasson, J.-L., and Srivastava, A. K. (1995) Mol.	vanadium salts	37-51	insulin receptor	Homo sapiens	171-187
9514089-0	1998	Stimulation of the intracellular portion of the human insulin receptor by the antidiabetic drug metformin.	Metformin	96-105	insulin receptor	Homo sapiens	54-70
9528942-0	1998	Analysis of the juxtamembrane dileucine motif in the insulin receptor.	dileucine	30-39	insulin receptor	Homo sapiens	53-69
9528942-2	1998	Previously, we have shown that the dileucine motif (EKITLL, residues 982-987) in the juxtamembrane region of the insulin receptor is involved in receptor internalization.	dileucine	35-44	insulin receptor	Homo sapiens	113-129
9528942-9	1998	Thus, the dileucine motif (EKITLL) plays an important role in directing endocytosis of the intact insulin receptor and in mediating efficient endocytosis and lysosomal targeting as an isolated motif.	dileucine	10-19	insulin receptor	Homo sapiens	98-114
9506989-7	1998	Furthermore, interaction of the BPS domain requires the kinase domain of the IR, since mutation of the paired tyrosine residues (Y1150F/Y1151F) within the IR activation loop dramatically reduced the interaction.	Tyrosine	110-118	insulin receptor	Homo sapiens	77-79
9506989-7	1998	Furthermore, interaction of the BPS domain requires the kinase domain of the IR, since mutation of the paired tyrosine residues (Y1150F/Y1151F) within the IR activation loop dramatically reduced the interaction.	Tyrosine	110-118	insulin receptor	Homo sapiens	155-157
9514773-4	1998	Autophosphorylation of the insulin receptors is then measured by a two-site immunofluorometric assay using monoclonal anti-insulin receptor antibodies and europium-labeled anti-phosphotyrosine antibodies.	Phosphotyrosine	177-192	insulin receptor	Homo sapiens	27-43
9514089-2	1998	We now report that therapeutic concentrations (approximately 1 microg/mL) of metformin stimulated the tyrosine kinase activity of the intracellular portion of the beta-subunit of the human insulin receptor (IPbetaIRK), the intracellular portion of the epidermal growth factor receptor and pp60-src, but not cAMP-dependent protein kinase.	Metformin	77-86	insulin receptor	Homo sapiens	189-205
9383737-2	1997	The amino group of the first amino acid phenylalanine on the B chain (B1) of insulin was selected for conjugation with palmitic acid in anticipation that its binding to the insulin receptor would be preserved.	amino acid phenylalanine	29-53	insulin receptor	Homo sapiens	173-189
9566851-0	1998	Epinephrine-induced reduction in insulin receptor mRNA level and stability in U-937 human promonocytic cells.	Epinephrine	0-11	insulin receptor	Homo sapiens	33-49
9566851-1	1998	The administration of 10(-5) M epinephrine transiently decreased insulin receptor (IR) mRNA levels in U-937 human promonocytic cells, which reached their minimum value after 24 hours.	Epinephrine	31-42	insulin receptor	Homo sapiens	65-81
9566851-1	1998	The administration of 10(-5) M epinephrine transiently decreased insulin receptor (IR) mRNA levels in U-937 human promonocytic cells, which reached their minimum value after 24 hours.	Epinephrine	31-42	insulin receptor	Homo sapiens	83-85
9566851-2	1998	Such a decrease seems to be due, at least in part, to a reduction in transcript stability, since the IR mRNA half-life was observed to decline from approximately 4h in untreated cells to 3 h in epinephrine-treated cells.	Epinephrine	194-205	insulin receptor	Homo sapiens	101-103
9566851-4	1998	These domains could be targets for a RNA-binding protein induced by treatment with epinephrine producing a destabilization of IR mRNA in U-937 cells.	Epinephrine	83-94	insulin receptor	Homo sapiens	126-128
9566852-11	1998	In summary, the data show that the increased mitogenic activity of Asp(B10)insulin may be explained with a prolonged kinetics of tyrosine phosphorylation of the insulin receptor and of insulin signalling elements together with the preferential phosphorylation of an yet unidentified 60 kDa protein.	Tyrosine	129-137	insulin receptor	Homo sapiens	161-177
9421413-1	1998	The present study was conducted to examine the ability of insulin receptor to activate the calcium signaling system in Chinese hamster ovary (CHO) cells expressing human insulin receptor (CHO-IR cells).	Calcium	91-98	insulin receptor	Homo sapiens	170-186
9427627-8	1998	CONCLUSION: We have developed an approach using the small molecule FK1012 to conditionally activate chimeric proteins containing FKBP fused to the insulin receptor or to the PDGF beta receptor.	FK 1012	67-73	insulin receptor	Homo sapiens	147-163
10212828-1	1998	We have achieved significant progress in understanding the central role of the insulin receptor in an increasingly complicated web of intracellular signal transduction leading to the ultimate biological actions of insulin on glucose, lipid, and other metabolic pathways.	Glucose	225-232	insulin receptor	Homo sapiens	79-95
9395471-1	1997	Increased serine phosphorylation of insulin receptor substrate-1 (IRS-1) has been observed in several systems to correlate with a decreased ability of the insulin receptor to tyrosine-phosphorylate this endogenous substrate and to inhibit its subsequent association with phosphatidylinositol 3-kinase.	Serine	10-16	insulin receptor	Homo sapiens	36-52
9395471-1	1997	Increased serine phosphorylation of insulin receptor substrate-1 (IRS-1) has been observed in several systems to correlate with a decreased ability of the insulin receptor to tyrosine-phosphorylate this endogenous substrate and to inhibit its subsequent association with phosphatidylinositol 3-kinase.	Tyrosine	175-183	insulin receptor	Homo sapiens	36-52
9395471-3	1997	First, recombinantly produced kinase was shown to phosphorylate intact IRS-1 in a way that decreased the ability of isolated insulin receptor to phosphorylate the tyrosines recognized by the SH2 domains of the phosphatidylinositol 3-kinase.	Tyrosine	163-172	insulin receptor	Homo sapiens	125-141
9428692-4	1997	Further, we found that insulin promotes rapid tyrosine phosphorylation of endogenous Stat 5B in 293 EBNA cells overexpressing insulin receptor and in NHIR cells.	Tyrosine	46-54	insulin receptor	Homo sapiens	126-142
9368005-0	1997	The disulfide bonds in the C-terminal domains of the human insulin receptor ectodomain.	Disulfides	4-13	insulin receptor	Homo sapiens	59-75
9368005-1	1997	The human insulin receptor is a homodimer consisting of two monomers linked by disulfide bonds.	Disulfides	79-88	insulin receptor	Homo sapiens	10-26
9368005-4	1997	There are two classes of disulfide bonds in the insulin receptor, those that can be reduced under mild reducing conditions to give alpha-beta monomers (class I) and those that require stronger reducing conditions (class II).	Disulfides	25-34	insulin receptor	Homo sapiens	48-64
9399641-5	1997	This complex is induced rapidly after tyrosine autophosphorylation of the insulin receptor, and is sustained for several hours.	Tyrosine	38-46	insulin receptor	Homo sapiens	74-90
9360986-7	1997	The protein bound with high affinity to the insulin receptor in cells, and the interaction was dependent on the tyrosine phosphorylation of the receptor.	Tyrosine	112-120	insulin receptor	Homo sapiens	44-60
9383737-6	1997	NB1-palmitoyl insulin was found to interact with the insulin receptor on fat cells, thereby catalyzing the conversion of [14C]glucose into lipids, at reduced efficiency (30-40%).	[14c]glucose	121-133	insulin receptor	Homo sapiens	53-69
9361682-3	1997	Accordingly, to further investigate the mechanisms of the derangements observed in NIDDM cells, we examined the effects of the ionophore monensin, which inhibits endosomal acidification, on the cellular processing of insulin and insulin receptor in monocytes from control subjects (n = 12) and NIDDM patients (n = 14).	Monensin	137-145	insulin receptor	Homo sapiens	229-245
9346913-6	1997	Thus, tyrosine phosphorylation of IRS-1 by the insulin receptor specifically requires a PH domain derived from IRS proteins.	Tyrosine	6-14	insulin receptor	Homo sapiens	47-63
9335553-7	1997	Moreover, a synthetic peptide containing this phosphoserine and its nearby tyrosine was found to be phosphorylated by the insulin receptor to a much lower extent than the same peptide without the phosphoserine.	Phosphoserine	46-59	insulin receptor	Homo sapiens	122-138
9335553-7	1997	Moreover, a synthetic peptide containing this phosphoserine and its nearby tyrosine was found to be phosphorylated by the insulin receptor to a much lower extent than the same peptide without the phosphoserine.	Tyrosine	75-83	insulin receptor	Homo sapiens	122-138
9335553-7	1997	Moreover, a synthetic peptide containing this phosphoserine and its nearby tyrosine was found to be phosphorylated by the insulin receptor to a much lower extent than the same peptide without the phosphoserine.	Phosphoserine	196-209	insulin receptor	Homo sapiens	122-138
9335553-10	1997	These results indicate that activation of protein kinase C stimulates a kinase which can phosphorylate insulin receptor substrate-1 at serine 612, resulting in an inhibition of insulin signaling in the cell, posing a potential mechanism for insulin resistance in some models of obesity.	Serine	135-141	insulin receptor	Homo sapiens	103-119
9312016-0	1997	Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog.	Adenosine Triphosphate	106-109	insulin receptor	Homo sapiens	35-51
9369444-0	1997	Site-directed mutagenesis and yeast two-hybrid studies of the insulin and insulin-like growth factor-1 receptors: the Src homology-2 domain-containing protein hGrb10 binds to the autophosphorylated tyrosine residues in the kinase domain of the insulin receptor.	Tyrosine	198-206	insulin receptor	Homo sapiens	244-260
9369444-3	1997	To further identify the binding site for hGrb10, all conserved tyrosine residues in the kinase domain of the insulin receptor were replaced with either phenylalanine or alanine by site-directed mutagenesis.	Tyrosine	63-71	insulin receptor	Homo sapiens	109-125
9369444-6	1997	Our findings suggest that, unlike other Src homology 2 domain-containing proteins, hGrb10 binds to the autophosphorylated tyrosine residues in the kinase domain of the insulin receptor, and the pleckstrin homology domain plays an important role in hGrb10/receptor interaction.	Tyrosine	122-130	insulin receptor	Homo sapiens	168-184
9369444-7	1997	Because the autophosphorylated tyrosine residues are critical for the autophosphorylation and kinase activity of the receptor, the binding of hGrb10 at these sites may suggest a role for the protein in the transduction or regulation of insulin receptor signaling.	Tyrosine	31-39	insulin receptor	Homo sapiens	236-252
9345301-0	1997	Impact of mutations at different serine residues on the tyrosine kinase activity of the insulin receptor.	Serine	33-39	insulin receptor	Homo sapiens	88-104
9345301-2	1997	In addition to phosphorylation at tyrosine residues a serine phosphorylation of the insulin receptor is observed.	Serine	54-60	insulin receptor	Homo sapiens	84-100
9345301-4	1997	We studied potential functions of serine residues in human insulin receptor (HIR) with respect to its ability to undergo insulin stimulated autophosphorylation.	Serine	34-40	insulin receptor	Homo sapiens	59-75
9345301-9	1997	The data suggest that the serine residues at position 994 as well as 1023/25 might be part of inhibitory domains of the insulin receptor.	Serine	26-32	insulin receptor	Homo sapiens	120-136
9345317-1	1997	Two early events downstream of insulin receptor autophosphorylation that are necessary for activation of glucose transport in adipocytes appear to be: (1) The tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) which (2) recruits and activates phosphatidylinositol 3"-kinase (PI3"-K).	Glucose	105-112	insulin receptor	Homo sapiens	31-47
9345317-1	1997	Two early events downstream of insulin receptor autophosphorylation that are necessary for activation of glucose transport in adipocytes appear to be: (1) The tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) which (2) recruits and activates phosphatidylinositol 3"-kinase (PI3"-K).	Tyrosine	159-167	insulin receptor	Homo sapiens	31-47
9312143-7	1997	Among these three, the motif around Ser-270 is located in the phosphotyrosine binding domain of IRS-1, which is responsible for the interaction with the insulin receptor.	Serine	36-39	insulin receptor	Homo sapiens	153-169
9312143-7	1997	Among these three, the motif around Ser-270 is located in the phosphotyrosine binding domain of IRS-1, which is responsible for the interaction with the insulin receptor.	Phosphotyrosine	62-77	insulin receptor	Homo sapiens	153-169
9349593-1	1997	A population-based study in the Netherlands has recently demonstrated that a mutation of the human insulin receptor (HIR-973 valine to methionine) is associated with hyperglycaemia and an increased prevalence of non-insulin-dependent diabetes mellitus (NIDDM).	N(tau)-ribosylhistidine	117-120	insulin receptor	Homo sapiens	99-115
9312188-4	1997	Here we show that TZDs have powerful effects on the ability of TNF-alpha to alter the most proximal steps of insulin signaling, including tyrosine phosphorylation of the insulin receptor and its major substrate, IRS-1, and activation of PI3-kinase.	Thiazolidinediones	18-22	insulin receptor	Homo sapiens	170-186
9312188-4	1997	Here we show that TZDs have powerful effects on the ability of TNF-alpha to alter the most proximal steps of insulin signaling, including tyrosine phosphorylation of the insulin receptor and its major substrate, IRS-1, and activation of PI3-kinase.	Tyrosine	138-146	insulin receptor	Homo sapiens	170-186
9312016-1	1997	The crystal structure of the phosphorylated, activated form of the insulin receptor tyrosine kinase in complex with a peptide substrate and an ATP analog has been determined at 1.9 A resolution.	Adenosine Triphosphate	143-146	insulin receptor	Homo sapiens	67-83
9271396-1	1997	The ability of insulin to stimulate protein synthesis and cellular growth is mediated through the insulin receptor (IR), which phosphorylates Tyr residues in the insulin receptor substrate-signaling proteins (IRS-1 and IRS-2), Gab-1, and Shc.	Tyrosine	142-145	insulin receptor	Homo sapiens	98-114
9278451-2	1997	The cytoplasmic juxtamembrane domain of the human insulin receptor (hIR) contains a single copy of the tetrameric amino acid sequence Asn-Pro-Glu-Tyr (NPEY) (residues 969-972 in the exon 11-containing B-isoform), which exists in the context of NPXY.	asn-pro-glu-tyr	134-149	insulin receptor	Homo sapiens	50-66
9271396-1	1997	The ability of insulin to stimulate protein synthesis and cellular growth is mediated through the insulin receptor (IR), which phosphorylates Tyr residues in the insulin receptor substrate-signaling proteins (IRS-1 and IRS-2), Gab-1, and Shc.	Tyrosine	142-145	insulin receptor	Homo sapiens	116-118
9228034-5	1997	We have recently identified a major ligand binding site of the insulin receptor by alanine scannning mutagenesis.	Alanine	83-90	insulin receptor	Homo sapiens	63-79
9268295-0	1997	Dual role of a dileucine motif in insulin receptor endocytosis.	dileucine	15-24	insulin receptor	Homo sapiens	34-50
9228034-9	1997	Mutation of Phe701 resulted in a receptor with undetectable IGF-1 binding; alanine substitution of the corresponding amino acid of the insulin receptor, Phe714, produces a 140-fold reduction in affinity for insulin.	Alanine	75-82	insulin receptor	Homo sapiens	135-151
9228034-11	1997	In contrast, alanine mutation of the corresponding amino acids of the insulin receptor with the exception of Asp12 produces reductions in affinity that are 50-fold or greater.	Alanine	13-20	insulin receptor	Homo sapiens	70-86
9228034-13	1997	The Kd values for insulin of the corresponding alanine mutants of the insulin receptor, Arg14 and His710, are 2-3 orders of magnitude greater than for wild type receptor.	Alanine	47-54	insulin receptor	Homo sapiens	70-86
9112018-1	1997	We report a homozygous missense mutation at position 1092 (substitution of glutamine for arginine) in the tyrosine kinase domain of the insulin receptor in a patient with leprechaunism associated with severe insulin resistance and intrauterine growth retardation.	Glutamine	75-84	insulin receptor	Homo sapiens	136-152
9243110-3	1997	There is evidence that this effect on IRK activity might be mediated through phosphorylation of specific serine residues of the insulin receptor beta-subunit.	Serine	105-111	insulin receptor	Homo sapiens	128-144
9248702-3	1997	The XaaB28ProB29 HI series is approximately equipotent to HI in binding to the insulin receptor with the exception of when Xaa = Phe, Trp, Leu, Ile, and Gly (40-60% relative to HI).	hi	17-19	insulin receptor	Homo sapiens	79-95
9248702-3	1997	The XaaB28ProB29 HI series is approximately equipotent to HI in binding to the insulin receptor with the exception of when Xaa = Phe, Trp, Leu, Ile, and Gly (40-60% relative to HI).	xanthenone-4-acetic acid	4-7	insulin receptor	Homo sapiens	79-95
9195949-1	1997	In addition to the pleckstrin homology domain and the phosphotyrosine binding domain in insulin receptor substrate (IRS)-1 and IRS-2, a region between amino acids 591 and 786 in IRS-2 (IRS-2-(591-786)) binds to the insulin receptor.	Phosphotyrosine	54-69	insulin receptor	Homo sapiens	88-104
9195949-4	1997	Phosphorylation of tyrosine residues in the KRLB domain by the insulin receptor inhibits the binding to the receptor.	Tyrosine	19-27	insulin receptor	Homo sapiens	63-79
9207225-10	1997	These results are further evidence that LAR is a physiological regulator of the insulin receptor and is consistent with its direct interaction with the tyrosine phosphorylated insulin receptor.	Tyrosine	152-160	insulin receptor	Homo sapiens	80-96
9175764-3	1997	Most likely due to the IR affinity defect analyses of signal transduction pathways showed an impairment of insulin action on glucose uptake, total RNA synthesis and phosphorylation as well as activity of MAP-kinase.	Glucose	125-132	insulin receptor	Homo sapiens	23-25
9175790-0	1997	Identification of two novel insulin receptor mutations, Asp59Gly and Leu62Pro, in type A syndrome of extreme insulin resistance.	leu62pro	69-77	insulin receptor	Homo sapiens	28-44
9175790-2	1997	Two missense IR mutations (Asp59Gly and Leu62Pro) found in the proband, resulted in reduction by 90% of insulin binding to erythrocytes, decreased receptor autophosphorylation and a dramatic reduction of insulin sensitivity.	leu62pro	40-48	insulin receptor	Homo sapiens	13-15
9148904-1	1997	Alanine scanning mutagenesis has been used to identify specific side chains of insulin which strongly influence binding to the insulin receptor.	Alanine	0-7	insulin receptor	Homo sapiens	127-143
9148904-4	1997	In contrast, alanine substitutions at positions GlyB20, ArgB22, and SerA9 resulted in an increase in affinity for the insulin receptor.	Alanine	13-20	insulin receptor	Homo sapiens	118-134
9148904-7	1997	Thus, replacing GlyB20 with alanine most likely modifies the structure of the B-chain in this region, but this structural change appears to enhance binding to the insulin receptor.	glyb20	16-22	insulin receptor	Homo sapiens	163-179
9148904-7	1997	Thus, replacing GlyB20 with alanine most likely modifies the structure of the B-chain in this region, but this structural change appears to enhance binding to the insulin receptor.	Alanine	28-35	insulin receptor	Homo sapiens	163-179
9115260-2	1997	The addition of CSF-1 to cells transfected with the CSF1R/IR chimera cDNA stimulated the tyrosine phosphorylation of a protein that was immunoprecipitated by an antibody directed against the carboxyl terminus of the insulin receptor.	Tyrosine	89-97	insulin receptor	Homo sapiens	216-232
9115260-3	1997	Phosphopeptide maps of the 32P-labeled CSF1R/IR protein revealed the same pattern of phosphorylation observed in 32P-labeled insulin receptor beta subunits.	Phosphorus-32	27-30	insulin receptor	Homo sapiens	125-141
9115260-3	1997	Phosphopeptide maps of the 32P-labeled CSF1R/IR protein revealed the same pattern of phosphorylation observed in 32P-labeled insulin receptor beta subunits.	Phosphorus-32	113-116	insulin receptor	Homo sapiens	125-141
9112018-1	1997	We report a homozygous missense mutation at position 1092 (substitution of glutamine for arginine) in the tyrosine kinase domain of the insulin receptor in a patient with leprechaunism associated with severe insulin resistance and intrauterine growth retardation.	Arginine	89-97	insulin receptor	Homo sapiens	136-152
9112018-2	1997	Site-directed mutagenesis as well as analyses of the patient"s lymphocytes revealed that this mutation causes a marked decrease in tyrosine kinase activity of the insulin receptor without any defect in insulin binding, which causes severe defects in insulin-stimulated glucose transport, glycogen synthesis and DNA synthesis.	Glucose	269-276	insulin receptor	Homo sapiens	163-179
9112018-2	1997	Site-directed mutagenesis as well as analyses of the patient"s lymphocytes revealed that this mutation causes a marked decrease in tyrosine kinase activity of the insulin receptor without any defect in insulin binding, which causes severe defects in insulin-stimulated glucose transport, glycogen synthesis and DNA synthesis.	Glycogen	288-296	insulin receptor	Homo sapiens	163-179
8940353-0	1996	Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates.	Tyrosine	26-34	insulin receptor	Homo sapiens	38-54
9111084-0	1997	14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner.	Phosphoserine	112-125	insulin receptor	Homo sapiens	78-94
9137903-5	1997	Since both body weight and plasma glucose concentrations were similar before and after treatment, the effect of metformin on insulin-receptor binding and tyrosine kinase activity appeared to be independent of either of these variables.	Metformin	112-121	insulin receptor	Homo sapiens	125-141
9054426-1	1997	L6 myotubes expressing the constitutively active Arg1152-->Gln insulin receptor (L6(1152)) featured a 31% increased glucose consumption as compared with L6 cells expressing wild-type receptors (L6(WT)).	Glucose	119-126	insulin receptor	Homo sapiens	66-82
9054578-8	1997	Our observation that ATP binds to the insulin receptor in the presence and absence of insulin supports the idea that the conformational change produced by insulin binding increases the rate of autophosphorylation rather than increases ATP affinity.	Adenosine Triphosphate	21-24	insulin receptor	Homo sapiens	38-54
9056694-6	1997	A poor intracellular magnesium concentration, as found in non-insulin-dependent diabetes mellitus (NIDDM) and in hypertensive (HP) patients, may result in a defective tyrosine-kinase activity at the insulin receptor level and exaggerated intracellular calcium concentration.	Magnesium	21-30	insulin receptor	Homo sapiens	199-215
9006905-3	1997	Through its SH2 domain, Nck recognizes a specific phosphotyrosine residue on RTKs or on protein substrates of RTKs like insulin receptor substrate-1, the major substrate of the insulin receptor, and through its SH3 domains it interacts with poorly characterized effector molecules.	Phosphotyrosine	50-65	insulin receptor	Homo sapiens	120-136
8999905-2	1997	Recent studies utilizing alanine scanning mutagenesis have identified a major ligand binding domain of the secreted recombinant insulin receptor composed of two subdomains, one between amino acids 1 and 120 and the other between amino acids 704 and 716.	Alanine	25-32	insulin receptor	Homo sapiens	128-144
8999839-0	1997	Protein-tyrosine phosphatase 1B complexes with the insulin receptor in vivo and is tyrosine-phosphorylated in the presence of insulin.	Tyrosine	8-16	insulin receptor	Homo sapiens	51-67
9000514-0	1997	Identification of Ser-1275 and Ser-1309 as autophosphorylation sites of the insulin receptor.	Serine	18-21	insulin receptor	Homo sapiens	76-92
9000514-0	1997	Identification of Ser-1275 and Ser-1309 as autophosphorylation sites of the insulin receptor.	Serine	31-34	insulin receptor	Homo sapiens	76-92
9000514-1	1997	We have identified Ser-1275 and Ser-1309 as novel serine autophosphorylation sites by direct sequencing of HPLC-purified tryptic phosphopeptides of the histidine-tagged insulin receptor kinase IRKD-HIS.	Serine	19-22	insulin receptor	Homo sapiens	169-185
9000514-1	1997	We have identified Ser-1275 and Ser-1309 as novel serine autophosphorylation sites by direct sequencing of HPLC-purified tryptic phosphopeptides of the histidine-tagged insulin receptor kinase IRKD-HIS.	Serine	32-35	insulin receptor	Homo sapiens	169-185
9000514-1	1997	We have identified Ser-1275 and Ser-1309 as novel serine autophosphorylation sites by direct sequencing of HPLC-purified tryptic phosphopeptides of the histidine-tagged insulin receptor kinase IRKD-HIS.	Serine	50-56	insulin receptor	Homo sapiens	169-185
9000514-2	1997	The corresponding peptides (Ser-1275, amino acids 1272-1292; Ser-1309, amino acids 1305-1313) have been detected in the HPLC profiles of both the soluble kinase IRKD, which contains the entire cytoplasmic domain of the insulin receptor beta-subunit, and the insulin receptor purified from human placenta.	Serine	28-31	insulin receptor	Homo sapiens	219-235
9000514-2	1997	The corresponding peptides (Ser-1275, amino acids 1272-1292; Ser-1309, amino acids 1305-1313) have been detected in the HPLC profiles of both the soluble kinase IRKD, which contains the entire cytoplasmic domain of the insulin receptor beta-subunit, and the insulin receptor purified from human placenta.	Serine	28-31	insulin receptor	Homo sapiens	258-274
9000514-3	1997	In contrast, a kinase negative mutant, IRKD-K1018A, did not undergo phosphorylation at either the tyrosine or serine residues, strongly suggesting that insulin receptor kinase has an intrinsic activity to autophosphorylate serine residues.	Serine	223-229	insulin receptor	Homo sapiens	152-168
9354853-1	1997	Post-receptor signalling molecules that convey the signal from the activated insulin receptor to the actual process of Glut4 translocation and hexose uptake are poorly understood.	Hexoses	143-149	insulin receptor	Homo sapiens	77-93
8940353-0	1996	Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates.	Tyrosine	64-72	insulin receptor	Homo sapiens	38-54
8940353-1	1996	Prior studies have demonstrated that a juxtamembrane tyrosine (tyrosine 972) in the insulin receptor is required for the receptor to elicit various biological responses and to stimulate the tyrosine phosphorylation of two endogenous substrates, the insulin receptor substrate-1 and the adaptor protein called Shc.	Tyrosine	53-61	insulin receptor	Homo sapiens	84-100
8940353-1	1996	Prior studies have demonstrated that a juxtamembrane tyrosine (tyrosine 972) in the insulin receptor is required for the receptor to elicit various biological responses and to stimulate the tyrosine phosphorylation of two endogenous substrates, the insulin receptor substrate-1 and the adaptor protein called Shc.	Tyrosine	63-71	insulin receptor	Homo sapiens	84-100
8940353-1	1996	Prior studies have demonstrated that a juxtamembrane tyrosine (tyrosine 972) in the insulin receptor is required for the receptor to elicit various biological responses and to stimulate the tyrosine phosphorylation of two endogenous substrates, the insulin receptor substrate-1 and the adaptor protein called Shc.	Tyrosine	63-71	insulin receptor	Homo sapiens	84-100
8940353-5	1996	These results further demonstrate the critical role that the juxtamembrane tyrosine 972 plays in downstream signaling by the insulin receptor.	Tyrosine	75-83	insulin receptor	Homo sapiens	125-141
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	vo(o2)2(bipy)	56-69	insulin receptor	Homo sapiens	129-145
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	vo(o2)2(bipy)	56-69	insulin receptor	Homo sapiens	242-258
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	2,2'-Dipyridyl	64-68	insulin receptor	Homo sapiens	129-145
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	2,2'-Dipyridyl	64-68	insulin receptor	Homo sapiens	242-258
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	vo(o2)2	56-63	insulin receptor	Homo sapiens	129-145
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	ethylenediamine	183-186	insulin receptor	Homo sapiens	129-145
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	ethylenediamine	205-220	insulin receptor	Homo sapiens	129-145
8893518-4	1996	Scatchard analysis of the binding data indicates that the observed effect of the [VO(O2)2(bipy)]- ion on insulin receptor binding is exerted mainly at the high-capacity low-affinity sites.	(o2)2	84-89	insulin receptor	Homo sapiens	105-121
8893518-4	1996	Scatchard analysis of the binding data indicates that the observed effect of the [VO(O2)2(bipy)]- ion on insulin receptor binding is exerted mainly at the high-capacity low-affinity sites.	bipy)	90-95	insulin receptor	Homo sapiens	105-121
8893518-7	1996	The observed modulation of insulin receptor binding by peroxovanadates is interpreted in terms of a ternary complex model in which the peroxovanadate acts as an allosteric effector modulating the binding equilibrium between insulin and its receptor.	peroxovanadate	55-70	insulin receptor	Homo sapiens	27-43
8893518-7	1996	The observed modulation of insulin receptor binding by peroxovanadates is interpreted in terms of a ternary complex model in which the peroxovanadate acts as an allosteric effector modulating the binding equilibrium between insulin and its receptor.	peroxovanadate	55-69	insulin receptor	Homo sapiens	27-43
8916921-1	1996	In cells, insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Tyrosine	76-84	insulin receptor	Homo sapiens	56-72
8916921-1	1996	In cells, insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Serine	112-118	insulin receptor	Homo sapiens	56-72
8916921-1	1996	In cells, insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Threonine	123-132	insulin receptor	Homo sapiens	56-72
8916921-5	1996	The kinase could be reconstituted back to the insulin receptor stripped of the kinase to yield a high stoichiometry of serine phosphorylation of the insulin receptor in the presence of insulin (0.75 +/- 0.15 mol/mol of beta-subunit, mean +/- SEM, n = 3).	Serine	119-125	insulin receptor	Homo sapiens	46-62
8916921-5	1996	The kinase could be reconstituted back to the insulin receptor stripped of the kinase to yield a high stoichiometry of serine phosphorylation of the insulin receptor in the presence of insulin (0.75 +/- 0.15 mol/mol of beta-subunit, mean +/- SEM, n = 3).	Serine	119-125	insulin receptor	Homo sapiens	149-165
8916921-8	1996	The purified kinase specifically phosphorylated serine 1078 of the insulin receptor, a major site of insulin-stimulated serine phosphorylation in vivo, showing that the purified kinase phosphorylated a physiologically relevant site on the insulin receptor.	Serine	48-54	insulin receptor	Homo sapiens	67-83
8916921-8	1996	The purified kinase specifically phosphorylated serine 1078 of the insulin receptor, a major site of insulin-stimulated serine phosphorylation in vivo, showing that the purified kinase phosphorylated a physiologically relevant site on the insulin receptor.	Serine	48-54	insulin receptor	Homo sapiens	239-255
8916921-8	1996	The purified kinase specifically phosphorylated serine 1078 of the insulin receptor, a major site of insulin-stimulated serine phosphorylation in vivo, showing that the purified kinase phosphorylated a physiologically relevant site on the insulin receptor.	Serine	120-126	insulin receptor	Homo sapiens	67-83
8916921-8	1996	The purified kinase specifically phosphorylated serine 1078 of the insulin receptor, a major site of insulin-stimulated serine phosphorylation in vivo, showing that the purified kinase phosphorylated a physiologically relevant site on the insulin receptor.	Serine	120-126	insulin receptor	Homo sapiens	239-255
8916921-9	1996	Phosphorylation of serine 1078 of the insulin receptor to high stoichiometry by the kinase did not affect insulin-stimulated exogenous protein tyrosine kinase activity of the insulin receptor.	Serine	19-25	insulin receptor	Homo sapiens	38-54
8916921-10	1996	Similarly, insulin receptor phosphorylated with or without the purified kinase exhibited the same levels of tyrosine autophosphorylation and of the tyrosine kinase-activating tris-phosphorylated kinase domain species.	Tyrosine	108-116	insulin receptor	Homo sapiens	11-27
8916921-12	1996	The serine kinase underwent autophosphorylation on serine and immunoprecipitated with the insulin receptor.	Serine	4-10	insulin receptor	Homo sapiens	90-106
8912638-6	1996	The results suggest that this specific cellular phospholipid modification will be useful in dissecting the specific functions of the two forms of the mammalian insulin receptor.	Phospholipids	48-60	insulin receptor	Homo sapiens	160-176
8903330-3	1996	Expression of a carboxy-terminal truncated IRS-1 molecule containing the pleckstrin homology and phosphotyrosine-binding domains associates with the insulin receptor and prevents tyrosyl phosphorylation of endogenous IRS-1 and Shc proteins.	Phosphotyrosine	97-112	insulin receptor	Homo sapiens	149-165
8824290-3	1996	In the present study, we demonstrate that gastrin stimulates tyrosine phosphorylation of insulin receptor substrate 1 (IRS-1), the major cytoplasmic substrate of the insulin receptor.	Tyrosine	61-69	insulin receptor	Homo sapiens	89-105
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	vanadium(v)-peroxo	13-31	insulin receptor	Homo sapiens	129-145
8893518-3	1996	Among the 16 vanadium(V)-peroxo complexes studied, the [VO(O2)2(bipy)]- ion, where bipy = 2,2"-bipyridine, was found to increase insulin receptor binding by 24%, whereas the [VO(O2)2(en)]- ion, where en = ethylenediamine, was found to reduce insulin receptor binding by about the same amount under steady-state conditions.	vanadium(v)-peroxo	13-31	insulin receptor	Homo sapiens	242-258
8826975-6	1996	A catalytically inactive [35S]PTP1B-fusion protein bound directly to immobilized insulin receptor kinase domains and was displaced in a concentration-dependent manner.	Sulfur-35	26-29	insulin receptor	Homo sapiens	81-97
8858098-1	1996	The binding of insulin to the plasma membrane insulin receptor initiates two dynamic processes: (i) autophosphorylation of the receptor on tyrosine residues, activating the intrinsic tyrosine kinase activity required for insulin signaling, and (ii) endocytosis of the receptor.	Tyrosine	139-147	insulin receptor	Homo sapiens	46-62
8826966-9	1996	Insulin stimulation of muscle glucose transport was negatively related to muscle PC-1 content (r = -0.68, P = 0.001) and positively related to insulin receptor content (r = 0.60, P = 0.005).	Glucose	30-37	insulin receptor	Homo sapiens	143-159
8826975-7	1996	Finally, tyrosine-phosphorylated PTP1B was precipitated from whole-cell lysates by an anti-insulin receptor antibody after insulin stimulation.	Tyrosine	9-17	insulin receptor	Homo sapiens	91-107
8826975-11	1996	We conclude that PTP1B can associate directly with the activated insulin receptor at multiple different phosphotyrosine sites and that dephosphorylation by PTP1B may play a significant role in insulin receptor signal transduction.	Phosphotyrosine	104-119	insulin receptor	Homo sapiens	65-81
8826975-11	1996	We conclude that PTP1B can associate directly with the activated insulin receptor at multiple different phosphotyrosine sites and that dephosphorylation by PTP1B may play a significant role in insulin receptor signal transduction.	Phosphotyrosine	104-119	insulin receptor	Homo sapiens	193-209
8898905-1	1996	Basic polymers such as polylysine have been found to activate insulin receptor autophosphorylation and kinase activity toward substrates.	Polymers	6-14	insulin receptor	Homo sapiens	62-78
8898905-1	1996	Basic polymers such as polylysine have been found to activate insulin receptor autophosphorylation and kinase activity toward substrates.	Polylysine	23-33	insulin receptor	Homo sapiens	62-78
8898905-11	1996	Our data indicate that the insulin receptor C-terminal acidic domain including residues 1270-1280 is involved in the interaction of polylysine and other polybasic molecules with the receptor.	Polylysine	132-142	insulin receptor	Homo sapiens	27-43
8902843-4	1996	Our data support the idea that tyrosine phosphorylation of the insulin receptor juxtamembrane domain is necessary for receptor association with IRS-1.	Tyrosine	31-39	insulin receptor	Homo sapiens	63-79
8905476-1	1996	The administration of 5 x 10(-6) mol/l dexamethasone transiently increased insulin receptor (IR) mRNA levels in U-937 human promonocytic cells, which reached the maximum level at 15 h of treatment.	Dexamethasone	39-52	insulin receptor	Homo sapiens	75-91
8891897-1	1996	The lipid second messenger, phosphatidic acid, inhibits the intrinsic tyrosine kinase activity of the insulin receptor in detergent-lipid mixed micelles or in reconstituted membranes.	Phosphatidic Acids	28-45	insulin receptor	Homo sapiens	102-118
8891897-5	1996	Thus, both a high affinity interaction of the insulin receptor with the phosphate headgroup and a stabilizing hydrophobic interaction with the acyl chains contribute to the inhibitory protein-lipid interaction.	Phosphates	72-81	insulin receptor	Homo sapiens	46-62
8891897-6	1996	The selective sensitivity of the insulin receptor to phosphatidic acid suggests that the receptor-mediated generation of this lipid in the plasma membrane could negatively modulate insulin receptor function.	Phosphatidic Acids	53-70	insulin receptor	Homo sapiens	33-49
8891897-6	1996	The selective sensitivity of the insulin receptor to phosphatidic acid suggests that the receptor-mediated generation of this lipid in the plasma membrane could negatively modulate insulin receptor function.	Phosphatidic Acids	53-70	insulin receptor	Homo sapiens	181-197
8905476-4	1996	Finally, the A isoform (lacking exon 11) was found to be the only IR isoform present in both untreated and dexamethasone treated-U-937 cells.	Dexamethasone	107-120	insulin receptor	Homo sapiens	66-68
8772194-2	1996	In resting Chinese hamster ovary cells overexpressing the human insulin receptor (CHO-IR cells), GSK-3 was tyrosine-phosphorylated and active.	Tyrosine	107-115	insulin receptor	Homo sapiens	64-80
8702527-0	1996	An insulin receptor mutant (Asp707 --> Ala), involved in leprechaunism, is processed and transported to the cell surface but unable to bind insulin.	Alanine	42-45	insulin receptor	Homo sapiens	3-19
8702527-6	1996	On solubilization of the mutant insulin receptor in Triton X-100-containing buffers, 125I-insulin was efficiently cross-linked to the receptor alpha subunit by disuccinimidyl suberate.	Octoxynol	52-64	insulin receptor	Homo sapiens	32-48
8702527-6	1996	On solubilization of the mutant insulin receptor in Triton X-100-containing buffers, 125I-insulin was efficiently cross-linked to the receptor alpha subunit by disuccinimidyl suberate.	disuccinimidyl	160-174	insulin receptor	Homo sapiens	32-48
8899294-6	1996	TNF has been shown to inhibit insulin-simulated tyrosine phosphorylation of both the insulin receptor (IR) and insulin receptor substrate (IRS)-1 and to stimulate downregulation of the insulin-sensitive glucose transporter, GLUT4, in adipocytes.	Tyrosine	48-56	insulin receptor	Homo sapiens	85-106
8663233-6	1996	Interaction of two random peptide libraries with glutathione S-transferase-LIM3 of Enigma indicated specific binding to Gly-Pro-Hyd-Gly-Pro-Hyd-Tyr-Ala corresponding to the major endocytic code of InsR.	Glutathione	49-60	insulin receptor	Homo sapiens	197-201
8663233-6	1996	Interaction of two random peptide libraries with glutathione S-transferase-LIM3 of Enigma indicated specific binding to Gly-Pro-Hyd-Gly-Pro-Hyd-Tyr-Ala corresponding to the major endocytic code of InsR.	gly-pro-hyd-gly-pro-hyd-tyr-ala	120-151	insulin receptor	Homo sapiens	197-201
8663233-7	1996	Peptide competition demonstrated that both Pro and Tyr residues were required for specific interaction of InsR with Enigma.	Proline	43-46	insulin receptor	Homo sapiens	106-110
8663233-7	1996	Peptide competition demonstrated that both Pro and Tyr residues were required for specific interaction of InsR with Enigma.	Tyrosine	51-54	insulin receptor	Homo sapiens	106-110
8666152-0	1996	The inhibition of the insulin receptor by the receptor protein PC-1 is not specific and results from the hydrolysis of ATP.	Adenosine Triphosphate	119-122	insulin receptor	Homo sapiens	22-38
8964871-2	1996	The aim of this study was to investigate whether intensified treatment with either LP or RI influences insulin receptor status.	Insulin Lispro	83-85	insulin receptor	Homo sapiens	103-119
8658525-5	1996	TCDD induced IR mRNA levels and inhibited several other insulin-induced responses including c-fos protooncogene expression, phosphorylation of the insulin receptor, and a 185-kDa protein in MCF-7 cells.	Polychlorinated Dibenzodioxins	0-4	insulin receptor	Homo sapiens	13-15
8658525-5	1996	TCDD induced IR mRNA levels and inhibited several other insulin-induced responses including c-fos protooncogene expression, phosphorylation of the insulin receptor, and a 185-kDa protein in MCF-7 cells.	Polychlorinated Dibenzodioxins	0-4	insulin receptor	Homo sapiens	147-163
8647800-1	1996	Insulin stimulation of Chinese hamster ovary cells expressing the human insulin receptor and differentiated 3T3L1 adipocytes resulted in a time-dependent reduction in the SDS-polyacrylamide gel electrophoretic mobility of STAT3.	Sodium Dodecyl Sulfate	171-174	insulin receptor	Homo sapiens	72-88
8647800-1	1996	Insulin stimulation of Chinese hamster ovary cells expressing the human insulin receptor and differentiated 3T3L1 adipocytes resulted in a time-dependent reduction in the SDS-polyacrylamide gel electrophoretic mobility of STAT3.	polyacrylamide	175-189	insulin receptor	Homo sapiens	72-88
8662806-9	1996	We conclude that IRS-2, unlike IRS-1, can interact with tyrosine-phosphorylated receptors such as the IR and insulin-like growth factor I receptor via multiple independent binding motifs.	Tyrosine	56-64	insulin receptor	Homo sapiens	17-19
8628319-2	1996	This extension is absent from the human insulin receptor but resembles a region in insulin receptor substrate (IRS) proteins which binds to the phosphatidylinositol (PI) 3-kinase and mediates mitogenesis.	Phosphatidylinositols	144-164	insulin receptor	Homo sapiens	40-56
8628319-4	1996	Insulin stimulated tyrosine autophosphorylation of the human insulin receptor and hDIR, and both receptors mediated tyrosine phosphorylation of Shc and activated mitogen-activated protein kinase.	Tyrosine	19-27	insulin receptor	Homo sapiens	61-77
8628319-4	1996	Insulin stimulated tyrosine autophosphorylation of the human insulin receptor and hDIR, and both receptors mediated tyrosine phosphorylation of Shc and activated mitogen-activated protein kinase.	Tyrosine	116-124	insulin receptor	Homo sapiens	61-77
8732688-1	1996	Protein-tyrosine phosphatases (PTPases) regulate insulin signaling by catalyzing the tyrosine dephosphorylation of the insulin receptor and its substrate proteins.	Tyrosine	8-16	insulin receptor	Homo sapiens	119-135
8732688-6	1996	After stimulation with 100 nM insulin, tyrosine phosphorylation of the insulin receptor was decreased by 31% at 1 min (P < 0.01) and by 42% at 10 min (P < 0.01), and that of IRS-1 was decreased by 34% (P < 0.01) at 1 min and by 56% (P < 0.01) at 10 min in the LAR-overexpressing cells compared with empty vector transfectants.	Tyrosine	39-47	insulin receptor	Homo sapiens	71-87
8744943-0	1996	Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers.	Cysteine	22-30	insulin receptor	Homo sapiens	93-109
8744943-0	1996	Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers.	Cysteine	22-30	insulin receptor	Homo sapiens	125-141
8744943-0	1996	Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers.	Disulfides	64-73	insulin receptor	Homo sapiens	93-109
8744943-1	1996	The cysteine residues involved in the class I disulfide bonds between the alpha subunits in the (alpha beta)2 dimer of the human insulin receptor have been identified by labeling with N-ethylmaleimide and by site-directed mutagenesis.	Cysteine	4-12	insulin receptor	Homo sapiens	129-145
8744943-1	1996	The cysteine residues involved in the class I disulfide bonds between the alpha subunits in the (alpha beta)2 dimer of the human insulin receptor have been identified by labeling with N-ethylmaleimide and by site-directed mutagenesis.	Disulfides	46-55	insulin receptor	Homo sapiens	129-145
8744943-1	1996	The cysteine residues involved in the class I disulfide bonds between the alpha subunits in the (alpha beta)2 dimer of the human insulin receptor have been identified by labeling with N-ethylmaleimide and by site-directed mutagenesis.	Ethylmaleimide	184-200	insulin receptor	Homo sapiens	129-145
8905476-1	1996	The administration of 5 x 10(-6) mol/l dexamethasone transiently increased insulin receptor (IR) mRNA levels in U-937 human promonocytic cells, which reached the maximum level at 15 h of treatment.	Dexamethasone	39-52	insulin receptor	Homo sapiens	93-95
8905476-3	1996	The stimulatory action of dexamethasone was not prevented by the simultaneous presence of the protein synthesis inhibitor cycloheximide, indicating that the induction of IR gene transcription occurs as a direct response to the action of the synthetic glucocorticoid.	Dexamethasone	26-39	insulin receptor	Homo sapiens	170-172
8620937-2	1996	Recent experiments have shown that purified rat liver ACP, corresponding to human ACP1, is able to hydrolyze a phosphotyrosine-containing synthetic peptide corresponding to the 1146-1158 sequence of the human insulin receptor, and shows a high affinity for it.	Phosphotyrosine	111-126	insulin receptor	Homo sapiens	209-225
8620937-6	1996	The data suggest that quantitative variations of ACP1 may influence the clinical manifestations of diabetic disorders, and call for further studies on the role of this enzyme in the modulation of insulin-receptor phosphotyrosine pathways.	Phosphotyrosine	213-228	insulin receptor	Homo sapiens	196-212
8636129-8	1996	These results suggest that the IR interacts with its downstream effectors through distinct receptor regions, and that autophosphorylation of Tyr residues located at the CT domain of the IR can modulate these interactions.	Tyrosine	141-144	insulin receptor	Homo sapiens	31-33
8617880-2	1996	Inhibition of insulin receptor signaling by high glucose levels and by TNF-alpha was recently observed in different cell systems.	Glucose	49-56	insulin receptor	Homo sapiens	14-30
8617880-4	1996	TNF-alpha (0.5-10 nM) and high glucose (25 mM) showed similar rapid kinetics of inhibition (5-10 min, > 50%) of insulin receptor autophosphorylation in NIH3T3 cells overexpressing the human insulin receptor.	Glucose	31-38	insulin receptor	Homo sapiens	193-209
8617880-10	1996	In summary, the data suggest that TNF-alpha and high glucose modulate insulin receptor-signaling through different mechanisms: (a) TNF-alpha modulates insulin receptor signals by PTPase activation, whereas glucose acts through activation of PKC.	Glucose	53-60	insulin receptor	Homo sapiens	70-86
8617880-10	1996	In summary, the data suggest that TNF-alpha and high glucose modulate insulin receptor-signaling through different mechanisms: (a) TNF-alpha modulates insulin receptor signals by PTPase activation, whereas glucose acts through activation of PKC.	Glucose	53-60	insulin receptor	Homo sapiens	151-167
8617880-10	1996	In summary, the data suggest that TNF-alpha and high glucose modulate insulin receptor-signaling through different mechanisms: (a) TNF-alpha modulates insulin receptor signals by PTPase activation, whereas glucose acts through activation of PKC.	Glucose	206-213	insulin receptor	Homo sapiens	70-86
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Glucose	106-113	insulin receptor	Homo sapiens	37-53
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Glucose	106-113	insulin receptor	Homo sapiens	137-153
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Glucose	106-113	insulin receptor	Homo sapiens	137-153
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Tyrosine	204-212	insulin receptor	Homo sapiens	37-53
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Tyrosine	204-212	insulin receptor	Homo sapiens	137-153
8617880-11	1996	(b) Differences in modulation of the insulin receptor signaling cascade are found with TNF-alpha and high glucose: Hyperglycemia-induced insulin receptor inhibition blocks both insulin receptor-dependent tyrosine phosphorylation and dephosphorylation of insulin receptor substrate proteins.	Tyrosine	204-212	insulin receptor	Homo sapiens	137-153
8626379-0	1996	Insulin receptor substrate-2 binds to the insulin receptor through its phosphotyrosine-binding domain and through a newly identified domain comprising amino acids 591-786.	Phosphotyrosine	71-86	insulin receptor	Homo sapiens	42-58
8626379-4	1996	The IH2PTB binds to the phosphorylated NPXY motif (Tyr-960) in the activated insulin receptor, providing a specific mechanism for the interaction between the receptor and IRS-1.	Tyrosine	51-54	insulin receptor	Homo sapiens	77-93
8626379-7	1996	This IRS-2-specific domain is independent of the IH2PTB and does not require the NPEY motif; however, it requires a functional insulin receptor kinase and the presence of three tyrosine phosphorylation sites in the regulatory loop (Tyr-1146, Tyr-1150, and Tyr-1151).	Tyrosine	177-185	insulin receptor	Homo sapiens	127-143
8626379-7	1996	This IRS-2-specific domain is independent of the IH2PTB and does not require the NPEY motif; however, it requires a functional insulin receptor kinase and the presence of three tyrosine phosphorylation sites in the regulatory loop (Tyr-1146, Tyr-1150, and Tyr-1151).	Tyrosine	232-235	insulin receptor	Homo sapiens	127-143
8626379-7	1996	This IRS-2-specific domain is independent of the IH2PTB and does not require the NPEY motif; however, it requires a functional insulin receptor kinase and the presence of three tyrosine phosphorylation sites in the regulatory loop (Tyr-1146, Tyr-1150, and Tyr-1151).	Tyrosine	242-245	insulin receptor	Homo sapiens	127-143
8626379-7	1996	This IRS-2-specific domain is independent of the IH2PTB and does not require the NPEY motif; however, it requires a functional insulin receptor kinase and the presence of three tyrosine phosphorylation sites in the regulatory loop (Tyr-1146, Tyr-1150, and Tyr-1151).	Tyrosine	242-245	insulin receptor	Homo sapiens	127-143
8621421-3	1996	The data revealed new potential Grb2 binding sites at Tyr-1114 (epidermal growth factor receptor (EGFR) C-tail); Tyr-743 (platelet-derived growth factor receptor (PDGFR) insert region), Tyr-1110 from the E-helix of the catalytic domain of insulin receptor (IR), and Tyr-47, Tyr-939, and Tyr-727 in IRS-1.	Tyrosine	54-57	insulin receptor	Homo sapiens	239-255
8621421-3	1996	The data revealed new potential Grb2 binding sites at Tyr-1114 (epidermal growth factor receptor (EGFR) C-tail); Tyr-743 (platelet-derived growth factor receptor (PDGFR) insert region), Tyr-1110 from the E-helix of the catalytic domain of insulin receptor (IR), and Tyr-47, Tyr-939, and Tyr-727 in IRS-1.	Tyrosine	54-57	insulin receptor	Homo sapiens	257-259
8638681-4	1996	Although the insulin receptor itself is a tyrosine kinase that is activated upon hormone binding, the ensuing changes in phosphorylation occur predominantly on serine and threonine residues.	Serine	160-166	insulin receptor	Homo sapiens	13-29
8638681-4	1996	Although the insulin receptor itself is a tyrosine kinase that is activated upon hormone binding, the ensuing changes in phosphorylation occur predominantly on serine and threonine residues.	Threonine	171-180	insulin receptor	Homo sapiens	13-29
8721774-9	1996	The t1/2 of intracellular dissociation of insulin-receptor complexes measured by a polyethylene glycol assay was lower in normal (6 +/- 1 min) than in obese (12 +/- 2 min, p < 0.03) and NIDDM subjects (14 +/- 3 min, p < 0.02).	Polyethylene Glycols	83-102	insulin receptor	Homo sapiens	42-58
8626723-0	1996	Interaction between the phosphotyrosine binding domain of Shc and the insulin receptor is required for Shc phosphorylation by insulin in vivo.	Phosphotyrosine	24-39	insulin receptor	Homo sapiens	70-86
8603380-3	1996	Addition of exogenous P-Tyr inhibited the insulin triggered insulin receptor (IR) tyrosine phosphorylation in the HEPG2 cell line and the tyrosine phosphorylation of a variety of cellular proteins in src-transformed NIH3T3 cells.	O-phospho-L-tyrosine	22-27	insulin receptor	Homo sapiens	60-76
8603380-3	1996	Addition of exogenous P-Tyr inhibited the insulin triggered insulin receptor (IR) tyrosine phosphorylation in the HEPG2 cell line and the tyrosine phosphorylation of a variety of cellular proteins in src-transformed NIH3T3 cells.	O-phospho-L-tyrosine	22-27	insulin receptor	Homo sapiens	78-80
8603380-3	1996	Addition of exogenous P-Tyr inhibited the insulin triggered insulin receptor (IR) tyrosine phosphorylation in the HEPG2 cell line and the tyrosine phosphorylation of a variety of cellular proteins in src-transformed NIH3T3 cells.	Tyrosine	82-90	insulin receptor	Homo sapiens	60-76
8603380-3	1996	Addition of exogenous P-Tyr inhibited the insulin triggered insulin receptor (IR) tyrosine phosphorylation in the HEPG2 cell line and the tyrosine phosphorylation of a variety of cellular proteins in src-transformed NIH3T3 cells.	Tyrosine	82-90	insulin receptor	Homo sapiens	78-80
8626723-1	1996	Stimulation of the insulin receptor (IR) results in tyrosine phosphorylation of the intermediate molecules insulin receptor substrate-1 (IRS-1), IRS-2, and Shc, which then couple the IR to downstream signaling pathways by serving as binding sites for signaling molecules with SH2 domains.	Tyrosine	52-60	insulin receptor	Homo sapiens	19-35
8626723-1	1996	Stimulation of the insulin receptor (IR) results in tyrosine phosphorylation of the intermediate molecules insulin receptor substrate-1 (IRS-1), IRS-2, and Shc, which then couple the IR to downstream signaling pathways by serving as binding sites for signaling molecules with SH2 domains.	Tyrosine	52-60	insulin receptor	Homo sapiens	37-39
8626723-1	1996	Stimulation of the insulin receptor (IR) results in tyrosine phosphorylation of the intermediate molecules insulin receptor substrate-1 (IRS-1), IRS-2, and Shc, which then couple the IR to downstream signaling pathways by serving as binding sites for signaling molecules with SH2 domains.	Tyrosine	52-60	insulin receptor	Homo sapiens	137-139
8626723-2	1996	It has been proposed that direct binding of IRS-1, IRS-2, and Shc to an NPX-Tyr(P) motif in the juxtamembrane region of the IR is required for tyrosine phosphorylation of these molecules by the IR.	Tyrosine	76-79	insulin receptor	Homo sapiens	44-46
8626723-2	1996	It has been proposed that direct binding of IRS-1, IRS-2, and Shc to an NPX-Tyr(P) motif in the juxtamembrane region of the IR is required for tyrosine phosphorylation of these molecules by the IR.	Tyrosine	76-79	insulin receptor	Homo sapiens	51-53
8626723-2	1996	It has been proposed that direct binding of IRS-1, IRS-2, and Shc to an NPX-Tyr(P) motif in the juxtamembrane region of the IR is required for tyrosine phosphorylation of these molecules by the IR.	Tyrosine	143-151	insulin receptor	Homo sapiens	44-46
8626723-2	1996	It has been proposed that direct binding of IRS-1, IRS-2, and Shc to an NPX-Tyr(P) motif in the juxtamembrane region of the IR is required for tyrosine phosphorylation of these molecules by the IR.	Tyrosine	143-151	insulin receptor	Homo sapiens	51-53
8626723-8	1996	These findings support a model in which binding of the PTB/PI domain of Shc directly to the NPX-Tyr(P) motif on the IR mediates Shc phosphorylation by insulin.	Tyrosine	96-99	insulin receptor	Homo sapiens	116-118
8621681-2	1996	These proteins can also be tyrosine phosphorylated in vitro by the isolated human insulin receptor.	Tyrosine	27-35	insulin receptor	Homo sapiens	82-98
8621681-3	1996	Increased tyrosine phosphorylation of these proteins is also observed in cells expressing a transforming chicken c-Src (mutant Phe-527) and in cells with the activated tyrosine kinase domains of the Drosophila insulin receptor, human insulin-like growth factor I receptor, and human insulin receptor-related receptor.	Tyrosine	10-18	insulin receptor	Homo sapiens	210-226
8621681-6	1996	This sequence was utilized to isolate a cDNA clone that encodes a previously uncharacterized 53-kDa protein which, when expressed in mammalian cells, is tyrosine phosphorylated by the insulin receptor.	Tyrosine	153-161	insulin receptor	Homo sapiens	184-200
8609215-0	1996	Glucose-induced phosphorylation of the insulin receptor.	Glucose	0-7	insulin receptor	Homo sapiens	39-55
8603747-1	1996	Studies with detergent:lipid mixed micelles reveal that diacylglycerol directly stimulates the intrinsic tyrosine kinase activity of the insulin receptor.	Diglycerides	56-70	insulin receptor	Homo sapiens	137-153
8603747-6	1996	Second, the activation by diacylglycerol is not stereospecific, in marked contrast to the specificity for 1,2-diacyl-sn-glycerol in the activation of protein kinase C. Because circulating levels of insulin are below the Kd of the insulin receptor for insulin, the ability of diacylglycerol to modulate the affinity of the receptor for ligand suggests that increases in cellular levels of diacylglycerol directly sensitize the receptor to insulin.	1,2-diacyl-sn-glycerol	106-128	insulin receptor	Homo sapiens	230-246
8593783-4	1996	Of these, only the tyrosine at position 1316 is conserved in the homologous position of the insulin receptor.	Tyrosine	19-27	insulin receptor	Homo sapiens	92-108
8609215-2	1996	Elevated glucose concentrations have been reported to inhibit insulin receptor kinase activity.	Glucose	9-16	insulin receptor	Homo sapiens	62-78
8609215-11	1996	Proportionately, the impairment of insulin receptor substrate-1 tyrosine phosphorylation is greater than that of the insulin receptor resulting in attenuated phosphatidylinositol 3-kinase activation and mitogenic signaling.	Tyrosine	64-72	insulin receptor	Homo sapiens	35-51
8561776-3	1996	A mutant insulin receptor, which lacked 47 amino acid residues (delta Ex13 IR) corresponding to exon 13 of insulin receptor gene, accumulated in the endoplasmic reticulum as uncleaved proreceptor with immature oligosaccharide chains.	Oligosaccharides	210-225	insulin receptor	Homo sapiens	9-25
8561776-3	1996	A mutant insulin receptor, which lacked 47 amino acid residues (delta Ex13 IR) corresponding to exon 13 of insulin receptor gene, accumulated in the endoplasmic reticulum as uncleaved proreceptor with immature oligosaccharide chains.	Oligosaccharides	210-225	insulin receptor	Homo sapiens	107-123
8557631-9	1996	Phosphoamino acid analysis establishes that insulin receptor-catalyzed phosphorylation of the beta 2-adrenergic receptor in vitro is confined to phosphotyrosine.	Phosphoamino Acids	0-17	insulin receptor	Homo sapiens	44-60
8624116-0	1996	Brain glucose metabolism is controlled by amplification and desensitization of the neuronal insulin receptor.	Glucose	6-13	insulin receptor	Homo sapiens	92-108
8557631-9	1996	Phosphoamino acid analysis establishes that insulin receptor-catalyzed phosphorylation of the beta 2-adrenergic receptor in vitro is confined to phosphotyrosine.	Phosphotyrosine	145-160	insulin receptor	Homo sapiens	44-60
8550573-0	1996	The type I interferon receptor mediates tyrosine phosphorylation of insulin receptor substrate 2.	Tyrosine	40-48	insulin receptor	Homo sapiens	68-84
8550573-2	1996	IFN alpha also induces tyrosine phosphorylation of IRS-1, the principle substrate of the insulin receptor.	Tyrosine	23-31	insulin receptor	Homo sapiens	89-105
8550582-12	1996	Receptor-catalyzed autophosphorylation of serine may play an important role in modulating insulin receptor signaling.	Serine	42-48	insulin receptor	Homo sapiens	90-106
8546696-4	1996	5-fold) than porcine insulin in inhibiting the binding of [125I-TyrA14]insulin to the soluble human insulin receptor from transfected 293EBNA cells (an adenovirus-transformed human kidney cell line).	Iodine-125	59-63	insulin receptor	Homo sapiens	100-116
8546696-4	1996	5-fold) than porcine insulin in inhibiting the binding of [125I-TyrA14]insulin to the soluble human insulin receptor from transfected 293EBNA cells (an adenovirus-transformed human kidney cell line).	tyra14	64-70	insulin receptor	Homo sapiens	100-116
8529791-15	1996	These data suggest that signals from the insulin receptor modify signaling from the bradykinin receptor to tyrosine phosphorylation of different cellular proteins.	Tyrosine	107-115	insulin receptor	Homo sapiens	41-57
9082618-3	1996	It is shown that AAS of juxtamembrane, ATP-binding and C-terminal domains of IR include long regions, homologous to the regions of RRR CD3, which are functionally important for coupling with G-proteins.	Adenosine Triphosphate	39-42	insulin receptor	Homo sapiens	77-79
8855443-2	1996	It is generally accepted that reversible phosphorylation of protein tyrosine residues by polypeptide growth factor receptor protein tyrosine kinases (e.g., epidermal growth factor receptor, platelet derived growth factor receptor, insulin receptor) is a signalling mechanism implicated in cell proliferation, adhesion, differentiation, transformation, and apoptosis.	Tyrosine	68-76	insulin receptor	Homo sapiens	231-247
9082618-5	1996	It is found that the clusters of basic amino acids (e.g. forming BBXXB-motifs) and serine residues, located in RRR, coincide with similar amino acids present in IR primary structure.	Amino Acids, Basic	33-50	insulin receptor	Homo sapiens	161-163
9082618-5	1996	It is found that the clusters of basic amino acids (e.g. forming BBXXB-motifs) and serine residues, located in RRR, coincide with similar amino acids present in IR primary structure.	Serine	83-89	insulin receptor	Homo sapiens	161-163
7588273-1	1995	The insulin receptor substrate-1 (IRS-1) is rapidly phosphorylated on several tyrosine residues by the activated insulin receptor.	Tyrosine	78-86	insulin receptor	Homo sapiens	4-20
15157524-1	1996	The insulin receptor is a transmembrane tyrosine kinase that is essential for mediating multiple intracellular signalling cascades that lead ultimately to the biological actions of insulin Tyrosine phosphorylation o f the cytosolic proteins insulin receptor substrate 1 and 2 (IRS1 and IRS2) produces protein "scaffolding" for the assembly of effector proteins containing Src homology 2 (SH2) domains, thereby generating multisubunit signalling complexes.	Tyrosine	189-197	insulin receptor	Homo sapiens	4-20
15157524-1	1996	The insulin receptor is a transmembrane tyrosine kinase that is essential for mediating multiple intracellular signalling cascades that lead ultimately to the biological actions of insulin Tyrosine phosphorylation o f the cytosolic proteins insulin receptor substrate 1 and 2 (IRS1 and IRS2) produces protein "scaffolding" for the assembly of effector proteins containing Src homology 2 (SH2) domains, thereby generating multisubunit signalling complexes.	Tyrosine	189-197	insulin receptor	Homo sapiens	241-257
8964871-15	1996	We conclude that the improved insulin receptor status observed during LP treatment is caused by its more physiological pharmacokinetic profile.	Insulin Lispro	70-72	insulin receptor	Homo sapiens	30-46
7589842-2	1995	The Co(3+)-insulin hexamer is an extraordinary stable insulin hexamer that has no affinity for the insulin receptor per se but is converted into active insulin in vivo.	cobalt adenosine diphosphate complex	4-10	insulin receptor	Homo sapiens	99-115
8822314-10	1995	These results indicate that octreotide improves insulin resistance at the insulin receptor site by lowering plasma levels of GH and insulin in acromegalic patients with glucose intolerance.	Octreotide	28-38	insulin receptor	Homo sapiens	74-90
8530637-3	1995	Insulin-stimulated estradiol and progesterone production was inhibited by an anti-insulin receptor antibody.	Estradiol	19-28	insulin receptor	Homo sapiens	82-98
8530637-3	1995	Insulin-stimulated estradiol and progesterone production was inhibited by an anti-insulin receptor antibody.	Progesterone	33-45	insulin receptor	Homo sapiens	82-98
8529629-0	1995	Isoproterenol inhibits insulin-stimulated tyrosine phosphorylation of the insulin receptor without increasing its serine/threonine phosphorylation.	Isoproterenol	0-13	insulin receptor	Homo sapiens	74-90
8529629-0	1995	Isoproterenol inhibits insulin-stimulated tyrosine phosphorylation of the insulin receptor without increasing its serine/threonine phosphorylation.	Tyrosine	42-50	insulin receptor	Homo sapiens	74-90
8529629-1	1995	The effect of a beta-adrenergic agonist (isoproterenol) on the tyrosine kinase activity of the insulin receptor was studied in intact adipocytes.	Isoproterenol	41-54	insulin receptor	Homo sapiens	95-111
7487933-12	1995	Thus chloroquine appears to have the opposite effect to excess insulin, and evidence was found for the induction of positive co-operativity in the insulin-receptor interaction at high chloroquine concentrations.	Chloroquine	184-195	insulin receptor	Homo sapiens	147-163
8567177-1	1995	The insulin receptor, as a consequence of ligand binding, undergoes autophosphorylation of critical tyrosyl residues within the cytoplasmic portion of its beta-subunit.	cyclo(tyrosyl-tyrosyl)	100-107	insulin receptor	Homo sapiens	4-20
8567177-6	1995	The association of p85 N + C SH2 domains with the autophosphorylated receptor was competed efficiently by a 15-residue tyrosine-phosphorylated peptide corresponding to the carboxyl-terminal region of the insulin receptor, but not by phosphopeptides of similar length derived from the juxtamembrane or regulatory regions.	Tyrosine	119-127	insulin receptor	Homo sapiens	204-220
8575665-6	1995	In contrast to the reduced binding affinity of other fish insulins, lamprey insulin was equipotent with porcine insulin in inhibiting the binding of [3-[125I]iodotyrosine-A14] human insulin to the human insulin receptor.	3-[125i]iodotyrosine	150-170	insulin receptor	Homo sapiens	203-219
7559478-1	1995	Insulin receptor substrate 1 (IRS-1) and src homology and collagen protein (SHC) are signaling proteins which are rapidly phosphorylated on tyrosines after insulin receptor (IR) activation.	Tyrosine	140-149	insulin receptor	Homo sapiens	156-172
7559478-1	1995	Insulin receptor substrate 1 (IRS-1) and src homology and collagen protein (SHC) are signaling proteins which are rapidly phosphorylated on tyrosines after insulin receptor (IR) activation.	Tyrosine	140-149	insulin receptor	Homo sapiens	30-32
7559478-15	1995	We confirm that Tyr-960 within the NPEY motif of the IR is essential for both IRS-1 and SHC interaction and that Asn-957 and Pro-958 are essential for IRS-1 interaction and important but not critical for SHC interaction.	Tyrosine	16-19	insulin receptor	Homo sapiens	53-55
8575665-6	1995	In contrast to the reduced binding affinity of other fish insulins, lamprey insulin was equipotent with porcine insulin in inhibiting the binding of [3-[125I]iodotyrosine-A14] human insulin to the human insulin receptor.	(1s,4s,5s,7r)-7-{[(5s)-5-Amino-5-Carboxypentanoyl]amino}-3,3-Dimethyl-6-Oxo-2-Thiabicyclo[3.2.0]heptane-4-Carboxylic Acid	171-174	insulin receptor	Homo sapiens	203-219
7665623-0	1995	Replacements of leucine 87 in human insulin receptor alter affinity for insulin.	Leucine	16-23	insulin receptor	Homo sapiens	36-52
7673181-1	1995	Individuals with insulin resistance show increased levels of PC-1 expression in skeletal muscle and fibroblasts, and in transfected cell lines that overexpress PC-1 there is a reduction in the insulin-stimulated insulin receptor tyrosine phosphorylation.	Tyrosine	229-237	insulin receptor	Homo sapiens	212-228
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Proline	72-75	insulin receptor	Homo sapiens	141-157
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Proline	72-75	insulin receptor	Homo sapiens	159-161
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Leucine	86-89	insulin receptor	Homo sapiens	141-157
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	Leucine	86-89	insulin receptor	Homo sapiens	159-161
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	ctg	91-94	insulin receptor	Homo sapiens	141-157
7665623-1	1995	In a previous analysis, we identified a point mutation that substituted Pro (CCG) for Leu (CTG) at amino acid 87 in the alpha-subunit of the insulin receptor (IR) in a Japanese patient with leprechaunism.	ctg	91-94	insulin receptor	Homo sapiens	159-161
7665623-5	1995	The Pro-87 IR reduced the insulin binding affinity to about 15% of Leu-87 IR, and the dissociation of insulin in Pro-87 IR was more rapid than in Leu-87 IR.	Leucine	67-70	insulin receptor	Homo sapiens	11-13
7665623-5	1995	The Pro-87 IR reduced the insulin binding affinity to about 15% of Leu-87 IR, and the dissociation of insulin in Pro-87 IR was more rapid than in Leu-87 IR.	Leucine	67-70	insulin receptor	Homo sapiens	74-76
7665623-9	1995	The Ile-87 IR enhanced the insulin binding affinity about 4-fold.	Isoleucine	4-7	insulin receptor	Homo sapiens	11-13
7665623-11	1995	In addition, the dissociation of insulin in Ile-87 IR was slower than in Leu-87 IR, but in Ala-87 IR it was more rapid.	Isoleucine	44-47	insulin receptor	Homo sapiens	51-53
7657664-4	1995	Insulin receptor autophosphorylation on tyrosine residues and activation of phosphatidylinositol 3"-kinase were unaffected.	Tyrosine	40-48	insulin receptor	Homo sapiens	0-16
7557427-3	1995	This cDNA was isolated from Ls via PCR with degenerate oligodeoxynucleotides corresponding to conserved parts of the tyrosine kinase domain of the human insulin receptor and its Drosophila homologue.	Oligodeoxyribonucleotides	55-76	insulin receptor	Homo sapiens	153-169
7657666-7	1995	Dexamethasone treatment caused an increase in in vivo IR autophosphorylation and insulin receptor substrate-1 (IRS-1) phosphorylation both early events in the insulin signaling pathway.	Dexamethasone	0-13	insulin receptor	Homo sapiens	54-56
7657666-9	1995	Total cellular tyrosine phosphatase activity was unaltered when assayed with 32P-labeled IR and IRS-1.	Phosphorus-32	77-80	insulin receptor	Homo sapiens	89-91
7629070-1	1995	Immunoprecipitation of the cytosolic Src homology 2 domain-containing protein-tyrosine phosphatase, SHPTP2, from insulin-stimulated 3T3L1 adipocytes or Chinese hamster ovary cells expressing the human insulin receptor resulted in the coimmunoprecipitation of a diffuse tyrosine-phosphorylated band in the 115-kDa protein region on SDS-polyacrylamide gels.	Tyrosine	78-86	insulin receptor	Homo sapiens	201-217
7542920-2	1995	The identity of the sites of insulin-stimulated serine phosphorylation in the human insulin receptor was examined by synthesizing peptides that together encompassed all the serine residues of the cytosolic portion of the beta-subunit and testing them as substrates for phosphorylation by a preparation of human insulin receptor copurified with insulin-stimulated insulin receptor serine kinase activity.	Serine	48-54	insulin receptor	Homo sapiens	84-100
7542920-14	1995	It is concluded that serine 1078 of the insulin receptor is a major site of insulin-stimulated phosphorylation in vivo and in vitro.	Serine	21-27	insulin receptor	Homo sapiens	40-56
7542920-15	1995	The peptide sequences provide a range of substrates to facilitate the study, purification, and characterization of the insulin-stimulated insulin receptor serine kinase or kinases, and the identification of a major site of insulin-stimulated serine phosphorylation will help elucidate the function of the insulin receptor serine phosphorylation.	Serine	155-161	insulin receptor	Homo sapiens	138-154
8948451-1	1995	In cells insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Tyrosine	75-83	insulin receptor	Homo sapiens	55-71
7626065-5	1995	The methods employed, DEAE and affinity chromatography, were published previously for the mammalian insulin receptor.	2-diethylaminoethanol	22-26	insulin receptor	Homo sapiens	100-116
7782332-2	1995	In the present study, GH is shown to stimulate tyrosyl phosphorylation of insulin receptor substrate 1 (IRS-1), the principle substrate of the insulin receptor.	cyclo(tyrosyl-tyrosyl)	47-54	insulin receptor	Homo sapiens	74-90
7635975-0	1995	Excessive insulin receptor serine phosphorylation in cultured fibroblasts and in skeletal muscle.	Serine	27-33	insulin receptor	Homo sapiens	10-26
7615833-3	1995	Phosphorylation of receptor serine/threonine residues has been proposed to exert an inhibitory influence on receptor tyrosine kinase activity and Ser 1327 and Thr 1348 have been identified as specific sites of phosphorylation in the insulin receptor COOH terminal domain.	Serine	28-34	insulin receptor	Homo sapiens	233-249
7615833-3	1995	Phosphorylation of receptor serine/threonine residues has been proposed to exert an inhibitory influence on receptor tyrosine kinase activity and Ser 1327 and Thr 1348 have been identified as specific sites of phosphorylation in the insulin receptor COOH terminal domain.	Threonine	35-44	insulin receptor	Homo sapiens	233-249
7615833-3	1995	Phosphorylation of receptor serine/threonine residues has been proposed to exert an inhibitory influence on receptor tyrosine kinase activity and Ser 1327 and Thr 1348 have been identified as specific sites of phosphorylation in the insulin receptor COOH terminal domain.	Serine	146-149	insulin receptor	Homo sapiens	233-249
7615833-3	1995	Phosphorylation of receptor serine/threonine residues has been proposed to exert an inhibitory influence on receptor tyrosine kinase activity and Ser 1327 and Thr 1348 have been identified as specific sites of phosphorylation in the insulin receptor COOH terminal domain.	Threonine	159-162	insulin receptor	Homo sapiens	233-249
7615833-10	1995	It is concluded that the stoichiometry of serine/threonine phosphorylation of insulin receptor in vivo is low, and that increased phosphorylation of Ser 1327 or Thr 1348 is not responsible for the decreased insulin receptor tyrosine kinase activity observed in the skeletal muscle of NIDDM patients.	Serine	42-48	insulin receptor	Homo sapiens	78-94
7615833-10	1995	It is concluded that the stoichiometry of serine/threonine phosphorylation of insulin receptor in vivo is low, and that increased phosphorylation of Ser 1327 or Thr 1348 is not responsible for the decreased insulin receptor tyrosine kinase activity observed in the skeletal muscle of NIDDM patients.	Threonine	49-58	insulin receptor	Homo sapiens	78-94
7539611-1	1995	Activation of the tyrosine kinase activity of the insulin receptor by autophosphorylation leads to phosphorylation of cellular substrates on tyrosine.	Tyrosine	18-26	insulin receptor	Homo sapiens	50-66
7539611-12	1995	The presence of this 60 kDa tyrosine-phosphorylated protein in adipocytes and hepatoma cells suggests that it represents another important intermediate in the insulin-receptor signal-transduction pathway.	Tyrosine	28-36	insulin receptor	Homo sapiens	159-175
7540611-4	1995	The insulin-dose responses for the tyrosine phosphorylation of caveolin and the 29-kD caveolin-associated protein paralleled those for the phosphorylation of the insulin receptor.	Tyrosine	35-43	insulin receptor	Homo sapiens	162-178
7540611-9	1995	Thus, the insulin-dependent tyrosine phosphorylation of caveolin represents a novel, insulin-specific signal transduction pathway that may involve activation of a tyrosine kinase downstream of the insulin receptor.	Tyrosine	28-36	insulin receptor	Homo sapiens	197-213
7567962-2	1995	Using the Wisconsin GCG sequence analysis programs, we have demonstrated that the cysteine-rich regions of INSR and EGFR conform to the structural motif found in the tumor necrosis factor receptor (TNFR) family.	Cysteine	82-90	insulin receptor	Homo sapiens	107-111
7567962-4	1995	The sequence alignments identified two cysteine residues in INSR that could be responsible for the additional disulfide bonds known to be involved in dimer formation.	Cysteine	39-47	insulin receptor	Homo sapiens	60-64
7567962-4	1995	The sequence alignments identified two cysteine residues in INSR that could be responsible for the additional disulfide bonds known to be involved in dimer formation.	Disulfides	110-119	insulin receptor	Homo sapiens	60-64
7567962-5	1995	The published data on the alignments for the fibronectin type III repeat region of the INSR together with previous cysteine mutagenesis studies indicated that there were two disulfide bonds linking the alpha and beta chains of the INSR, but only one alpha-beta linkage in the insulin-like growth factor 1 receptor (IG1R).	Disulfides	174-183	insulin receptor	Homo sapiens	87-91
7786302-2	1995	Nanomolar concentrations of hypericin inhibit the protein tyrosine kinase activities (PTK) of the epidermal growth factor receptor and the insulin receptor, while being ineffective towards the cytosolic protein tyrosine kinases Lyn, Fgr, TPK-IIB and CSK.	hypericin	28-37	insulin receptor	Homo sapiens	139-155
7741749-4	1995	Insulin stimulated a rapid and transient tyrosine phosphorylation of receptor beta subunits (95 kDa) and of IRS-1 in intact Y79 cells, whereas in vitro studies with enriched membrane glycoproteins resulted in the autophosphorylation of both InsR (95 kDa) and IGF-1-R (98k Da) beta subunits.	Tyrosine	41-49	insulin receptor	Homo sapiens	241-245
8948451-1	1995	In cells insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Serine	111-117	insulin receptor	Homo sapiens	55-71
8948451-1	1995	In cells insulin stimulates autophosphorylation of the insulin receptor on tyrosine and its phosphorylation on serine and threonine by poorly characterized kinases.	Threonine	122-131	insulin receptor	Homo sapiens	55-71
7537758-9	1995	We conclude that impaired insulin-stimulated glucose uptake in skeletal muscle from severely obese subjects is accompanied by a deficiency in insulin receptor signaling, which may contribute to decreased insulin action.	Glucose	45-52	insulin receptor	Homo sapiens	142-158
7730324-1	1995	Insulin treatment of Chinese hamster ovary cells expressing high levels of the human insulin receptor resulted in the tyrosine dephosphorylation of the 125-kDa focal adhesion kinase (pp125FAK).	Tyrosine	118-126	insulin receptor	Homo sapiens	85-101
7662110-1	1995	Use of insulin"s intrinsic tyrosine absorption and fluorescence to monitor its interaction with the insulin receptor is limited because the spectral properties of the receptor tryptophan residues mask the spectral properties of the hormone tyrosine residues.	Tyrosine	27-35	insulin receptor	Homo sapiens	100-116
7537496-1	1995	The human insulin receptor (hIR) cytoplasmic juxtamembrane domain contains two tyrosine (Y) residues which exist in GPLY and NPEY motifs that have been implicated in endocytic function.	Tyrosine	79-87	insulin receptor	Homo sapiens	10-26
7698218-3	1995	RNA blot assays indicated that 1,25-(OH)2D3 increased the levels of the two major insulin receptor mRNAs (11 and 8.5 kb) present in these cells.	Calcitriol	31-43	insulin receptor	Homo sapiens	82-98
7698218-6	1995	Finally, polymerase chain reaction assays revealed that the insulin receptor mRNA isotype lacking the exon 11 (A isotype) was the only one present in both untreated and 1,25-(OH)2D3-treated U-937 cells.	Calcitriol	169-181	insulin receptor	Homo sapiens	60-76
7535776-12	1995	In conclusion, exposing cells to high glucose levels desensitizes insulin receptor function, and thiazolidine derivatives can reverse the process via the normalization of cytosolic PTPase, but not of protein kinase C.	Glucose	38-45	insulin receptor	Homo sapiens	66-82
7702578-1	1995	Native human insulin receptor (hIR) has been reported to contain only one free thiol group proposed to lie near the ATP-binding.	Sulfhydryl Compounds	79-84	insulin receptor	Homo sapiens	13-29
7613486-1	1995	Asparagine-linked glycosylation of the insulin receptor is required for complete biosynthesis and acquisition of function.	Asparagine	0-10	insulin receptor	Homo sapiens	39-55
7702578-1	1995	Native human insulin receptor (hIR) has been reported to contain only one free thiol group proposed to lie near the ATP-binding.	Adenosine Triphosphate	116-119	insulin receptor	Homo sapiens	13-29
7737184-2	1995	In a previous study, we showed that a chimeric insulin-like-growth-factor-1 (IGF-1) receptor, with the beta subunit C-terminal part of the insulin receptor was more efficient in stimulating glycogen synthesis and p44mapk activity compared to the wild-type IFG-1 receptor [Tartare, S., Mothe, I., Kowalski-Chauvel, A., Breittmayer, J.-P., Ballotti, R. & Van Obberghen, E. (1994) J. Biol.	Glycogen	190-198	insulin receptor	Homo sapiens	139-155
7876259-10	1995	Moreover, we show that only tyrosine-phosphorylated hIRS-p30 is able to bind to the insulin receptor.	Tyrosine	28-36	insulin receptor	Homo sapiens	84-100
7720193-0	1995	Vanadate enhances insulin-receptor binding in gestational diabetic human placenta.	Vanadates	0-8	insulin receptor	Homo sapiens	18-34
7849042-3	1995	Compounds which raise the bilayer to hexagonal phase transition temperature in model membranes, including carbobenzoxydipeptides, apolipoprotein A-I, acyl carnitines, and lysophosphatidylcholine, inhibited insulin stimulation of insulin receptor tyrosine phosphorylation of isolated receptors as well as in cells overexpressing human insulin receptor.	acylcarnitine	150-165	insulin receptor	Homo sapiens	229-245
7849042-3	1995	Compounds which raise the bilayer to hexagonal phase transition temperature in model membranes, including carbobenzoxydipeptides, apolipoprotein A-I, acyl carnitines, and lysophosphatidylcholine, inhibited insulin stimulation of insulin receptor tyrosine phosphorylation of isolated receptors as well as in cells overexpressing human insulin receptor.	Lysophosphatidylcholines	171-194	insulin receptor	Homo sapiens	229-245
7849042-3	1995	Compounds which raise the bilayer to hexagonal phase transition temperature in model membranes, including carbobenzoxydipeptides, apolipoprotein A-I, acyl carnitines, and lysophosphatidylcholine, inhibited insulin stimulation of insulin receptor tyrosine phosphorylation of isolated receptors as well as in cells overexpressing human insulin receptor.	Tyrosine	246-254	insulin receptor	Homo sapiens	229-245
7849042-4	1995	For compounds of similar structure, the inhibition of insulin receptor tyrosine phosphorylation correlates well with their bilayer-stabilizing potency.	Tyrosine	71-79	insulin receptor	Homo sapiens	54-70
7849042-5	1995	Most of the compounds which inhibit tyrosine phosphorylation of the insulin receptor also inhibited glucose uptake in the same cells.	Tyrosine	36-44	insulin receptor	Homo sapiens	68-84
7849042-5	1995	Most of the compounds which inhibit tyrosine phosphorylation of the insulin receptor also inhibited glucose uptake in the same cells.	Glucose	100-107	insulin receptor	Homo sapiens	68-84
7835273-1	1995	Insulin-stimulated glucose transport in adipocytes is mediated by the insulin receptor.	Glucose	19-26	insulin receptor	Homo sapiens	70-86
7835273-12	1995	These data suggest that the insulin and EGF signaling pathways that lead to glucose transport converge in these adipocytes down-stream of the insulin receptor, and that activation of this pathway requires signaling motifs in the carboxy-terminus of the EGFR.	Glucose	76-83	insulin receptor	Homo sapiens	142-158
7867639-1	1995	We have previously shown, in rat-1 fibroblasts which stably overexpress high levels of human insulin receptor (HIR), that high glucose levels induce an inhibition of insulin receptor tyrosine kinase (IRK) activity [Berti, L., Mosthaf, L., Kellerer, M., Tippmer, S., Mushack, J., Seffer, E., Seedorf, K., Haring, H. (1994) J. Biol.	Glucose	127-134	insulin receptor	Homo sapiens	93-109
7867639-1	1995	We have previously shown, in rat-1 fibroblasts which stably overexpress high levels of human insulin receptor (HIR), that high glucose levels induce an inhibition of insulin receptor tyrosine kinase (IRK) activity [Berti, L., Mosthaf, L., Kellerer, M., Tippmer, S., Mushack, J., Seffer, E., Seedorf, K., Haring, H. (1994) J. Biol.	Glucose	127-134	insulin receptor	Homo sapiens	166-182
7867639-13	1995	To test whether serine residues 955/956 and 962/964 in the juxtamembrane region of the insulin receptor are involved in the inhibitory effect of glucose, 293 cells transiently transfected either with wild-type HIR or HIR with a juxtamembrane deletion spanning amino acids 954-965 [des-(954-965)-HIR] were studied in parallel.	Serine	16-22	insulin receptor	Homo sapiens	87-103
7867639-13	1995	To test whether serine residues 955/956 and 962/964 in the juxtamembrane region of the insulin receptor are involved in the inhibitory effect of glucose, 293 cells transiently transfected either with wild-type HIR or HIR with a juxtamembrane deletion spanning amino acids 954-965 [des-(954-965)-HIR] were studied in parallel.	Glucose	145-152	insulin receptor	Homo sapiens	87-103
7867639-16	1995	Together, the data suggest that the regulatory serine or threonine phosphorylation site(s) involved in the inhibitory effect of hyperglycemia are neither located in the C-terminus nor in the juxtamembrane region of the insulin receptor beta subunit.	Serine	47-53	insulin receptor	Homo sapiens	219-235
7836419-5	1995	We conclude that: 1) in contrast to other growth factors, insulin stimulates the dephosphorylation of pp125fak; 2) the presence of the insulin receptor C-terminal tyrosines 1328 and 1334 is required for the insulin-stimulated tyrosine dephosphorylation of pp125fak, suggesting a possible SH2 domain-dependent interaction; 3) insulin may modulate integrin-mediated signaling through pp125fak by altering the phosphorylation state of pp125fak.	Tyrosine	163-172	insulin receptor	Homo sapiens	135-151
7836419-5	1995	We conclude that: 1) in contrast to other growth factors, insulin stimulates the dephosphorylation of pp125fak; 2) the presence of the insulin receptor C-terminal tyrosines 1328 and 1334 is required for the insulin-stimulated tyrosine dephosphorylation of pp125fak, suggesting a possible SH2 domain-dependent interaction; 3) insulin may modulate integrin-mediated signaling through pp125fak by altering the phosphorylation state of pp125fak.	Tyrosine	163-171	insulin receptor	Homo sapiens	135-151
7814414-0	1995	Deletion of lysine 121 creates a temperature-sensitive alteration in insulin binding by the insulin receptor.	Lysine	12-18	insulin receptor	Homo sapiens	92-108
7814414-1	1995	Recently we reported the deletion of Lys-121 in one allele of the insulin receptor gene from a child with severe insulin resistance.	Lysine	37-40	insulin receptor	Homo sapiens	66-82
7814414-8	1995	The results of these and other studies argue that Lys-121 occupies an important position for the regulation of insulin receptor conformation.	Lysine	50-53	insulin receptor	Homo sapiens	111-127
7826318-0	1995	Glucose-induced stimulation of human insulin-receptor mRNA and tyrosine kinase activity in cultured cells.	Glucose	0-7	insulin receptor	Homo sapiens	37-53
7852381-0	1995	Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis.	Alanine	74-81	insulin receptor	Homo sapiens	54-70
7852381-3	1995	Alanine mutant cDNAs encoding a secreted recombinant insulin receptor extracellular domain were expressed transiently in adenovirus transformed human embryonic kidney cells and the affinity of the expressed receptor for insulin was determined.	Alanine	0-7	insulin receptor	Homo sapiens	53-69
7588528-1	1995	The addition of sodium dodecyl sulfate (SDS) micelles in the running buffer can be used to resolve mono- and diphosphorylated isomers of the insulin receptor peptide by capillary electrophoresis.	Sodium Dodecyl Sulfate	16-38	insulin receptor	Homo sapiens	141-157
7588528-1	1995	The addition of sodium dodecyl sulfate (SDS) micelles in the running buffer can be used to resolve mono- and diphosphorylated isomers of the insulin receptor peptide by capillary electrophoresis.	Sodium Dodecyl Sulfate	40-43	insulin receptor	Homo sapiens	141-157
7829633-7	1995	The relative levels of expression of the 2 alleles of the IR gene were evaluated by allele-specific oligonucleotide hybridization in cells from most of these patients, and no gross alteration was detected.	Oligonucleotides	100-115	insulin receptor	Homo sapiens	58-60
7826318-1	1995	The effects of high glucose on insulin-receptor tyrosine kinase activity and gene expression were investigated in 3T3-HIR cells.	Glucose	20-27	insulin receptor	Homo sapiens	31-47
7826318-8	1995	In cells challenged with high glucose plus inhibitor, insulin-receptor mRNA half-life was increased from 1 to 3 h, indicating that posttranscriptional mechanisms are involved in these processes of glucose regulation.	Glucose	30-37	insulin receptor	Homo sapiens	54-70
7826318-8	1995	In cells challenged with high glucose plus inhibitor, insulin-receptor mRNA half-life was increased from 1 to 3 h, indicating that posttranscriptional mechanisms are involved in these processes of glucose regulation.	Glucose	197-204	insulin receptor	Homo sapiens	54-70
7826318-9	1995	Inhibition of protein synthesis by cycloheximide induced an overexpression of insulin-receptor mRNA levels in the presence of glucose, suggesting that labile repressor protein(s) could be implicated in the effects of glucose.	Cycloheximide	35-48	insulin receptor	Homo sapiens	78-94
7826318-9	1995	Inhibition of protein synthesis by cycloheximide induced an overexpression of insulin-receptor mRNA levels in the presence of glucose, suggesting that labile repressor protein(s) could be implicated in the effects of glucose.	Glucose	126-133	insulin receptor	Homo sapiens	78-94
7826318-9	1995	Inhibition of protein synthesis by cycloheximide induced an overexpression of insulin-receptor mRNA levels in the presence of glucose, suggesting that labile repressor protein(s) could be implicated in the effects of glucose.	Glucose	217-224	insulin receptor	Homo sapiens	78-94
7826318-10	1995	We conclude that (1) long-term culture with high glucose increases the amount of insulin receptors and their tyrosine kinase activity and (2) the glucose-induced increase in insulin-receptor mRNA levels can be accounted for, at least in part, by posttranscriptional events.	Glucose	49-56	insulin receptor	Homo sapiens	174-190
7826318-10	1995	We conclude that (1) long-term culture with high glucose increases the amount of insulin receptors and their tyrosine kinase activity and (2) the glucose-induced increase in insulin-receptor mRNA levels can be accounted for, at least in part, by posttranscriptional events.	Glucose	146-153	insulin receptor	Homo sapiens	174-190
7806523-8	1994	Furthermore, replacement of the insulin receptor amino acid phenylalanine 39 with the corresponding IGF-I receptor amino acid, serine 35, decreased insulin affinity 8-fold.	Serine	127-133	insulin receptor	Homo sapiens	32-48
7811279-0	1994	Unusual insulin binding to cells expressing an insulin receptor mutated at cysteine 524.	Cysteine	75-83	insulin receptor	Homo sapiens	47-63
7811279-1	1994	The involvement of cysteine 524 of the insulin receptor in an intermolecular (class I) disulfide bond between the two alpha-subunits was investigated using site-directed mutagenesis.	Cysteine	19-27	insulin receptor	Homo sapiens	39-55
7811279-1	1994	The involvement of cysteine 524 of the insulin receptor in an intermolecular (class I) disulfide bond between the two alpha-subunits was investigated using site-directed mutagenesis.	Disulfides	87-96	insulin receptor	Homo sapiens	39-55
7806523-0	1994	Chimeric receptors indicate that phenylalanine 39 is a major contributor to insulin specificity of the insulin receptor.	Phenylalanine	33-46	insulin receptor	Homo sapiens	103-119
7806523-7	1994	Using chimeric insulin/IGF-I receptors to elucidate how the insulin receptor interacts with the insulin molecule we identified phenylalanine 39 of the insulin receptor as a major contributor in determining the receptor specificity for insulin, increasing insulin affinity 15-fold when replacing the corresponding amino acid in the insulin-like growth factor I receptor.	Phenylalanine	127-140	insulin receptor	Homo sapiens	60-76
7806523-7	1994	Using chimeric insulin/IGF-I receptors to elucidate how the insulin receptor interacts with the insulin molecule we identified phenylalanine 39 of the insulin receptor as a major contributor in determining the receptor specificity for insulin, increasing insulin affinity 15-fold when replacing the corresponding amino acid in the insulin-like growth factor I receptor.	Phenylalanine	127-140	insulin receptor	Homo sapiens	151-167
7806523-8	1994	Furthermore, replacement of the insulin receptor amino acid phenylalanine 39 with the corresponding IGF-I receptor amino acid, serine 35, decreased insulin affinity 8-fold.	amino acid phenylalanine	49-73	insulin receptor	Homo sapiens	32-48
7535732-3	1994	Recently, we described a leprechaun patient having an Arg for Gly substitution in one allele of the insulin receptor whereas the other allele has the normal sequence.	Arginine	54-57	insulin receptor	Homo sapiens	100-116
7535732-3	1994	Recently, we described a leprechaun patient having an Arg for Gly substitution in one allele of the insulin receptor whereas the other allele has the normal sequence.	Glycine	62-65	insulin receptor	Homo sapiens	100-116
7893993-9	1994	In contrast, the insulin receptor does not bind Grb2 directly but rather induces the tyrosine phosphorylation of two proteins, insulin receptor substrate-1 and Shc, that bind the Grb2/Sos complex.	Tyrosine	85-93	insulin receptor	Homo sapiens	17-33
7893993-9	1994	In contrast, the insulin receptor does not bind Grb2 directly but rather induces the tyrosine phosphorylation of two proteins, insulin receptor substrate-1 and Shc, that bind the Grb2/Sos complex.	sulfur monoxide	184-187	insulin receptor	Homo sapiens	17-33
7947843-2	1994	To investigate the structural determinants underlying the enhanced internalization rate observed for the insulin receptor transmembrane mutant Gly933-Pro934-->Ala-Ala (GP-->AA), we have designed and chemically synthesized two peptides, IR(TM)-GP and IR-(TM)-AA, corresponding respectively to the N-terminal portion of the wild-type and the mutant insulin receptor TM segment containing these sites.	alanylalanine	162-169	insulin receptor	Homo sapiens	105-121
7525547-9	1994	Therefore, we conclude that p85 and Syp bind to the insulin receptor C terminus at tyrosine 1322 and GAP binds to the insulin receptor NPXY domain at tyrosine 960.	Tyrosine	83-91	insulin receptor	Homo sapiens	52-68
7525547-9	1994	Therefore, we conclude that p85 and Syp bind to the insulin receptor C terminus at tyrosine 1322 and GAP binds to the insulin receptor NPXY domain at tyrosine 960.	Tyrosine	150-158	insulin receptor	Homo sapiens	118-134
7989492-3	1994	The nucleotide sequence analysis of the patient"s genomic DNA revealed a 3-basepair in-frame deletion in one allele, resulting in the loss of leucine at position 999 of the insulin receptor (delta Leu999).	Leucine	142-149	insulin receptor	Homo sapiens	173-189
7526800-1	1994	Calmodulin is phosphorylated by the purified insulin receptor on tyrosine residues with a maximum stoichiometry of 1 mol phosphate/mol of calmodulin.	Tyrosine	65-73	insulin receptor	Homo sapiens	45-61
7526800-1	1994	Calmodulin is phosphorylated by the purified insulin receptor on tyrosine residues with a maximum stoichiometry of 1 mol phosphate/mol of calmodulin.	Phosphates	121-130	insulin receptor	Homo sapiens	45-61
7926300-4	1994	On a cellular level, TNF-alpha is a potent inhibitor of the insulin-stimulated tyrosine phosphorylations on the beta-chain of the insulin receptor and insulin receptor substrate-1, suggesting a defect at or near the tyrosine kinase activity of the insulin receptor.	Tyrosine	79-87	insulin receptor	Homo sapiens	130-146
7806540-0	1994	A mutant insulin receptor induces formation of a Shc-growth factor receptor bound protein 2 (Grb2) complex and p21ras-GTP without detectable interaction of insulin receptor substrate 1 (IRS1) with Grb2.	Guanosine Triphosphate	118-121	insulin receptor	Homo sapiens	9-25
7806540-4	1994	We investigated the contribution of the major tyrosine autophosphorylation sites Tyr1158, Tyr1162, and Tyr1163 of the insulin receptor to IRS1.Grb2 and Shc.Grb2 association and the formation of p21ras-GTP.	Tyrosine	46-54	insulin receptor	Homo sapiens	118-134
7980500-0	1994	Role of phosphatidylinositol-3-kinase in insulin receptor signaling: studies with inhibitor, LY294002.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	93-101	insulin receptor	Homo sapiens	41-57
7929343-0	1994	Phorbol ester stimulates phosphorylation on serine 1327 of the human insulin receptor.	Phorbol Esters	0-13	insulin receptor	Homo sapiens	69-85
7524496-3	1994	Herein we find using the hexameric peptide sequence Ac-D-A-D-E-X-L-amide, where X = (D/L)-Pmp or L-F2Pmp, that the half maximal inhibition values of these two peptides against PTP 1B-mediated dephosphorylation of autophosphorylated insulin receptor to be 200 microM and 100 nM, respectively.	Actinium	52-54	insulin receptor	Homo sapiens	232-248
7524496-3	1994	Herein we find using the hexameric peptide sequence Ac-D-A-D-E-X-L-amide, where X = (D/L)-Pmp or L-F2Pmp, that the half maximal inhibition values of these two peptides against PTP 1B-mediated dephosphorylation of autophosphorylated insulin receptor to be 200 microM and 100 nM, respectively.	Deuterium	55-57	insulin receptor	Homo sapiens	232-248
7524496-3	1994	Herein we find using the hexameric peptide sequence Ac-D-A-D-E-X-L-amide, where X = (D/L)-Pmp or L-F2Pmp, that the half maximal inhibition values of these two peptides against PTP 1B-mediated dephosphorylation of autophosphorylated insulin receptor to be 200 microM and 100 nM, respectively.	d-e-x-l-amide	59-72	insulin receptor	Homo sapiens	232-248
7524496-3	1994	Herein we find using the hexameric peptide sequence Ac-D-A-D-E-X-L-amide, where X = (D/L)-Pmp or L-F2Pmp, that the half maximal inhibition values of these two peptides against PTP 1B-mediated dephosphorylation of autophosphorylated insulin receptor to be 200 microM and 100 nM, respectively.	pmp	90-93	insulin receptor	Homo sapiens	232-248
7945263-0	1994	Characterization of phorbol ester-stimulated serine phosphorylation of the human insulin receptor.	Phorbol Esters	20-33	insulin receptor	Homo sapiens	81-97
7945263-0	1994	Characterization of phorbol ester-stimulated serine phosphorylation of the human insulin receptor.	Serine	45-51	insulin receptor	Homo sapiens	81-97
7945263-1	1994	Phorbol 12-myristate 13-acetate (PMA)-stimulated phosphorylation of the human insulin receptor (IR) was characterized and compared in two cell types of different lineage: normal rat kidney epithelial (NRK) cells and Chinese hamster ovary (CHO) fibroblasts.	Tetradecanoylphorbol Acetate	0-31	insulin receptor	Homo sapiens	78-99
7945263-1	1994	Phorbol 12-myristate 13-acetate (PMA)-stimulated phosphorylation of the human insulin receptor (IR) was characterized and compared in two cell types of different lineage: normal rat kidney epithelial (NRK) cells and Chinese hamster ovary (CHO) fibroblasts.	Tetradecanoylphorbol Acetate	33-36	insulin receptor	Homo sapiens	78-99
7945263-4	1994	Tryptic phosphopeptide analysis by Tricine/SDS/PAGE revealed significant differences in the PMA-stimulated phosphorylation of the IR in these two cell types.	tricine	35-42	insulin receptor	Homo sapiens	130-132
7945263-4	1994	Tryptic phosphopeptide analysis by Tricine/SDS/PAGE revealed significant differences in the PMA-stimulated phosphorylation of the IR in these two cell types.	Sodium Dodecyl Sulfate	43-46	insulin receptor	Homo sapiens	130-132
7945263-4	1994	Tryptic phosphopeptide analysis by Tricine/SDS/PAGE revealed significant differences in the PMA-stimulated phosphorylation of the IR in these two cell types.	Tetradecanoylphorbol Acetate	92-95	insulin receptor	Homo sapiens	130-132
7945263-9	1994	These results demonstrate that PMA-stimulated phosphorylation of the IR can exhibit significant differences when expressed in different cell types, and that Ser1315 is a major PMA-stimulated phosphorylation site on the human IR.	Tetradecanoylphorbol Acetate	31-34	insulin receptor	Homo sapiens	69-71
7945263-9	1994	These results demonstrate that PMA-stimulated phosphorylation of the IR can exhibit significant differences when expressed in different cell types, and that Ser1315 is a major PMA-stimulated phosphorylation site on the human IR.	Tetradecanoylphorbol Acetate	31-34	insulin receptor	Homo sapiens	225-227
7945263-9	1994	These results demonstrate that PMA-stimulated phosphorylation of the IR can exhibit significant differences when expressed in different cell types, and that Ser1315 is a major PMA-stimulated phosphorylation site on the human IR.	Tetradecanoylphorbol Acetate	176-179	insulin receptor	Homo sapiens	225-227
7925113-2	1994	A 50-kilodalton protein (p50) was found to be greatly phosphorylated on threonine residues upon insulin stimulation in intact rat hepatoma cells (Fao) and Chinese hamster ovary cells overexpressing human insulin receptor (CHO-HIR).	Threonine	72-81	insulin receptor	Homo sapiens	204-220
7926368-3	1994	Although the insulin receptor itself is a tyrosine kinase that is activated upon hormone binding, the ensuing changes in phosphorylation occur predominantly on serine and threonine residues.	Serine	160-166	insulin receptor	Homo sapiens	13-29
7926368-3	1994	Although the insulin receptor itself is a tyrosine kinase that is activated upon hormone binding, the ensuing changes in phosphorylation occur predominantly on serine and threonine residues.	Threonine	171-180	insulin receptor	Homo sapiens	13-29
7983787-2	1994	The basic structure of the insulin receptor is a disulfide-linked tetramer, composed of the alpha subunit (135 kDa), which is extracellular and provides the binding site for insulin, and the beta subunit (95 kDa), contains the transmembrane domain, tyrosine kinase domain and C-terminal domain.	Disulfides	49-58	insulin receptor	Homo sapiens	27-43
7983788-5	1994	Possible regulation of the expression of the insulin receptor gene by hormones such as insulin and dexamethasone and some transcription factors including Sp1 and C/EBP have been shown at the mRNA and transcription levels.	Dexamethasone	99-112	insulin receptor	Homo sapiens	45-61
7983789-4	1994	The same mutation in the insulin receptor does not always necessarily show the same phenotypes of skin lesion or the same glucose intolerance.	Glucose	122-129	insulin receptor	Homo sapiens	25-41
7983803-5	1994	In these cases, despite having a same mutation in the insulin receptor gene, some individuals exhibited significant clinical differences (e.g. insulin resistance or glucose tolerance).	Glucose	165-172	insulin receptor	Homo sapiens	54-70
7712917-0	1994	[The effect of hydrocortisone or dexamethasone on human erythrocyte membrane insulin receptor].	Hydrocortisone	15-29	insulin receptor	Homo sapiens	77-93
7712917-0	1994	[The effect of hydrocortisone or dexamethasone on human erythrocyte membrane insulin receptor].	Dexamethasone	33-46	insulin receptor	Homo sapiens	77-93
8093061-1	1994	Insulin receptor (IR) purified from human placenta by wheat germ agglutinin affinity chromatography was incubated in the presence of insulin, [gamma-32P]ATP and annexin I.	[gamma-32p	142-152	insulin receptor	Homo sapiens	18-20
8093061-1	1994	Insulin receptor (IR) purified from human placenta by wheat germ agglutinin affinity chromatography was incubated in the presence of insulin, [gamma-32P]ATP and annexin I.	Adenosine Triphosphate	153-156	insulin receptor	Homo sapiens	0-16
20692961-0	1994	Effect of alkylating and redox cycling quinones on insulin receptor autophosphorylation.	Quinones	39-47	insulin receptor	Homo sapiens	51-67
20692961-3	1994	Since the toxicity of quinones can be related to two mechanisms-redox cycling resulting in oxidative stress, and arylation of cellular nucleophilic groups-the effects of 1,4-naphthoquinone and menadione on insulin receptor autophosphorylation were investigated.	Quinones	22-30	insulin receptor	Homo sapiens	206-222
20692961-3	1994	Since the toxicity of quinones can be related to two mechanisms-redox cycling resulting in oxidative stress, and arylation of cellular nucleophilic groups-the effects of 1,4-naphthoquinone and menadione on insulin receptor autophosphorylation were investigated.	1,4-naphthoquinone	170-188	insulin receptor	Homo sapiens	206-222
20692961-3	1994	Since the toxicity of quinones can be related to two mechanisms-redox cycling resulting in oxidative stress, and arylation of cellular nucleophilic groups-the effects of 1,4-naphthoquinone and menadione on insulin receptor autophosphorylation were investigated.	Vitamin K 3	193-202	insulin receptor	Homo sapiens	206-222
20692961-4	1994	The results show that these two quinones have a dual effect: lower concentrations leading to oxidative stress increase insulin receptor autophosphorylation, whereas higher concentrations cause a thiol depletion and inhibit the normal insulin receptor autophosphorylation.	Quinones	32-40	insulin receptor	Homo sapiens	119-135
20692961-4	1994	The results show that these two quinones have a dual effect: lower concentrations leading to oxidative stress increase insulin receptor autophosphorylation, whereas higher concentrations cause a thiol depletion and inhibit the normal insulin receptor autophosphorylation.	Quinones	32-40	insulin receptor	Homo sapiens	234-250
8027066-0	1994	The functions of the human insulin receptor are affected in different ways by mutation of each of the four N-glycosylation sites in the beta subunit.	Nitrogen	107-108	insulin receptor	Homo sapiens	27-43
8027066-1	1994	The functional role of the oligosaccharide chains linked to the insulin receptor (IR) beta subunit was investigated by site-directed mutagenesis of each of the 4 acceptor asparagines (N1 to N4 from the amino to the carboxyl terminus) and stable expression of the receptors in CHO cells.	Oligosaccharides	27-42	insulin receptor	Homo sapiens	64-80
7980420-10	1994	It was still a disulphide-linked dimer as judged by SDS/PAGE, indicating that there are alpha-alpha-chain disulphide bonds additional to the Cys-524 linkage in the insulin receptor dimer.	disulphide	15-25	insulin receptor	Homo sapiens	164-180
7980420-10	1994	It was still a disulphide-linked dimer as judged by SDS/PAGE, indicating that there are alpha-alpha-chain disulphide bonds additional to the Cys-524 linkage in the insulin receptor dimer.	Cysteine	141-144	insulin receptor	Homo sapiens	164-180
7865816-0	1994	[Insulin receptor interactions and metabolic effects of "essential" phospholipids in diabetes mellitus].	Phospholipids	68-81	insulin receptor	Homo sapiens	1-17
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Leucine	0-3	insulin receptor	Homo sapiens	52-68
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Leucine	0-3	insulin receptor	Homo sapiens	98-114
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Cysteine	24-32	insulin receptor	Homo sapiens	52-68
8093054-0	1994	Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding.	Cysteine	24-32	insulin receptor	Homo sapiens	98-114
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	Homo sapiens	35-51
8093061-1	1994	Insulin receptor (IR) purified from human placenta by wheat germ agglutinin affinity chromatography was incubated in the presence of insulin, [gamma-32P]ATP and annexin I.	[gamma-32p	142-152	insulin receptor	Homo sapiens	0-16
8082780-0	1994	Functional properties of a heterozygous mutation (Arg1174-->Gln) in the tyrosine kinase domain of the insulin receptor from a type A insulin resistant patient.	Glutamine	63-66	insulin receptor	Homo sapiens	105-121
8048939-1	1994	Specific insulin binding by the fetal lung insulin receptor is reduced in vitro by a combination of high glucose and insulin.	Glucose	105-112	insulin receptor	Homo sapiens	43-59
8048939-4	1994	Insulin-receptor mRNA abundance was reduced by high glucose + insulin to 37 +/- 6% of control values (p < .05).	Glucose	52-59	insulin receptor	Homo sapiens	0-16
7929343-0	1994	Phorbol ester stimulates phosphorylation on serine 1327 of the human insulin receptor.	Serine	44-50	insulin receptor	Homo sapiens	69-85
7929343-1	1994	Phorbol esters stimulate the phosphorylation of the insulin receptor on discrete serine and threonine residues in intact cells.	Phorbol Esters	0-14	insulin receptor	Homo sapiens	52-68
7929343-1	1994	Phorbol esters stimulate the phosphorylation of the insulin receptor on discrete serine and threonine residues in intact cells.	Serine	81-87	insulin receptor	Homo sapiens	52-68
7929343-1	1994	Phorbol esters stimulate the phosphorylation of the insulin receptor on discrete serine and threonine residues in intact cells.	Threonine	92-101	insulin receptor	Homo sapiens	52-68
7929343-2	1994	Phosphorylation of the insulin receptor cytoplasmic domain on serine, threonine, and tyrosine residues regulates receptor tyrosine kinase activity and signaling.	Serine	62-68	insulin receptor	Homo sapiens	23-39
7929343-2	1994	Phosphorylation of the insulin receptor cytoplasmic domain on serine, threonine, and tyrosine residues regulates receptor tyrosine kinase activity and signaling.	Threonine	70-79	insulin receptor	Homo sapiens	23-39
7929343-2	1994	Phosphorylation of the insulin receptor cytoplasmic domain on serine, threonine, and tyrosine residues regulates receptor tyrosine kinase activity and signaling.	Tyrosine	85-93	insulin receptor	Homo sapiens	23-39
7929343-3	1994	In these studies, we demonstrate that phorbol ester treatment of intact COS-1 cells transiently expressing the human insulin receptor stimulates phosphorylation of serine 1327 within the carboxyl-terminal tail of the insulin receptor beta subunit.	Phorbol Esters	38-51	insulin receptor	Homo sapiens	117-133
7929343-3	1994	In these studies, we demonstrate that phorbol ester treatment of intact COS-1 cells transiently expressing the human insulin receptor stimulates phosphorylation of serine 1327 within the carboxyl-terminal tail of the insulin receptor beta subunit.	carbonyl sulfide	72-75	insulin receptor	Homo sapiens	117-133
7929343-3	1994	In these studies, we demonstrate that phorbol ester treatment of intact COS-1 cells transiently expressing the human insulin receptor stimulates phosphorylation of serine 1327 within the carboxyl-terminal tail of the insulin receptor beta subunit.	Serine	164-170	insulin receptor	Homo sapiens	117-133
7929343-6	1994	The synthetic peptide 1327S (KRSYEEHIPYTHMNGGKK) corresponding to amino acids 1325-1342 of the human insulin receptor is phosphorylated on serine by protein kinase C. After digestion with trypsin, the phosphorylated synthetic peptide comigrated with the serine-phosphorylated peptide isolated from wild-type insulin receptors that was absent from the Ala1327 mutant.	Serine	139-145	insulin receptor	Homo sapiens	101-117
7929343-6	1994	The synthetic peptide 1327S (KRSYEEHIPYTHMNGGKK) corresponding to amino acids 1325-1342 of the human insulin receptor is phosphorylated on serine by protein kinase C. After digestion with trypsin, the phosphorylated synthetic peptide comigrated with the serine-phosphorylated peptide isolated from wild-type insulin receptors that was absent from the Ala1327 mutant.	Serine	254-260	insulin receptor	Homo sapiens	101-117
7929343-9	1994	The chemically modified peptide 1327S(P) was synthesized with the stoichiometric addition of phosphate to the side chain hydroxyl of a serine corresponding to position 1327 of the insulin receptor.	Phosphates	93-102	insulin receptor	Homo sapiens	180-196
7929343-9	1994	The chemically modified peptide 1327S(P) was synthesized with the stoichiometric addition of phosphate to the side chain hydroxyl of a serine corresponding to position 1327 of the insulin receptor.	Serine	135-141	insulin receptor	Homo sapiens	180-196
7929343-13	1994	Radiosequence analysis revealed that the chemical addition of phosphate to the serine in peptide 1327S(P) inhibited insulin receptor-catalyzed phosphorylation of the tyrosine on 1327S(P) corresponding to Tyr1334 but not of the tyrosine corresponding to Tyr1328.	Phosphates	62-71	insulin receptor	Homo sapiens	116-132
7929343-13	1994	Radiosequence analysis revealed that the chemical addition of phosphate to the serine in peptide 1327S(P) inhibited insulin receptor-catalyzed phosphorylation of the tyrosine on 1327S(P) corresponding to Tyr1334 but not of the tyrosine corresponding to Tyr1328.	Serine	79-85	insulin receptor	Homo sapiens	116-132
7929343-13	1994	Radiosequence analysis revealed that the chemical addition of phosphate to the serine in peptide 1327S(P) inhibited insulin receptor-catalyzed phosphorylation of the tyrosine on 1327S(P) corresponding to Tyr1334 but not of the tyrosine corresponding to Tyr1328.	Tyrosine	166-174	insulin receptor	Homo sapiens	116-132
7929343-13	1994	Radiosequence analysis revealed that the chemical addition of phosphate to the serine in peptide 1327S(P) inhibited insulin receptor-catalyzed phosphorylation of the tyrosine on 1327S(P) corresponding to Tyr1334 but not of the tyrosine corresponding to Tyr1328.	Tyrosine	227-235	insulin receptor	Homo sapiens	116-132
7929343-14	1994	These data suggest that the juxtaposition of a serine phosphorylation site adjacent to receptor tyrosine phosphorylation sites provides the potential for regulation of insulin receptor autophosphorylation and signaling through its carboxyl-terminal tail.	Serine	47-53	insulin receptor	Homo sapiens	168-184
7929343-14	1994	These data suggest that the juxtaposition of a serine phosphorylation site adjacent to receptor tyrosine phosphorylation sites provides the potential for regulation of insulin receptor autophosphorylation and signaling through its carboxyl-terminal tail.	Tyrosine	96-104	insulin receptor	Homo sapiens	168-184
8206928-0	1994	Internalization of the constitutively active arginine 1152-->glutamine insulin receptor occurs independently of insulin at an accelerated rate.	Arginine	45-53	insulin receptor	Homo sapiens	74-90
8024589-0	1994	Dithiothreitol stimulates insulin receptor autophosphorylation at the juxtamembrane domain.	Dithiothreitol	0-14	insulin receptor	Homo sapiens	26-42
8024589-6	1994	These observations suggest that a thiol(s) may be involved in insulin receptor autophosphorylation in the juxtamembrane domain.	Sulfhydryl Compounds	34-39	insulin receptor	Homo sapiens	62-78
8206928-5	1994	Cell preincubation with 35 mM Tris, which inhibits the insulin receptor degradative route, elicited no effect on M receptor recycling but inhibited that of WT by 40%.	Tromethamine	30-34	insulin receptor	Homo sapiens	55-71
8206928-6	1994	In contrast, the energy depleter 2,4-dinitrophenol, which inhibits normal insulin receptor retroendocytosis, impaired M receptor recycling 4-fold more effectively than that of WT.	2,4-Dinitrophenol	33-50	insulin receptor	Homo sapiens	74-90
7515062-4	1994	Tyr(P) IRS-1 was prepared by phosphorylation of recombinant IRS-1 with recombinant cytoplasmic insulin receptor kinase (CIRK).	Tyrosine	0-3	insulin receptor	Homo sapiens	95-111
8024702-0	1994	Effects of tyrosine-->phenylalanine mutations on auto- and trans-phosphorylation reactions catalyzed by the insulin receptor beta-subunit cytoplasmic domain.	Tyrosine	11-19	insulin receptor	Homo sapiens	111-127
8195229-2	1994	Here we show that the maximal hyperphosphorylation of Raf-1 and MAPKK (10 min) was substantially achieved after the maximal activation of MAPKKK of Raf-1, MAPKK (2-5 min), and MAPK in Chinese hamster ovary cells overexpressing human insulin receptor (CHO-HIR cells) treated with insulin or 12-O-tetradecanoylphorbol-13-acetate (TPA).	Tetradecanoylphorbol Acetate	290-326	insulin receptor	Homo sapiens	233-249
8195229-2	1994	Here we show that the maximal hyperphosphorylation of Raf-1 and MAPKK (10 min) was substantially achieved after the maximal activation of MAPKKK of Raf-1, MAPKK (2-5 min), and MAPK in Chinese hamster ovary cells overexpressing human insulin receptor (CHO-HIR cells) treated with insulin or 12-O-tetradecanoylphorbol-13-acetate (TPA).	Tetradecanoylphorbol Acetate	328-331	insulin receptor	Homo sapiens	233-249
8024702-0	1994	Effects of tyrosine-->phenylalanine mutations on auto- and trans-phosphorylation reactions catalyzed by the insulin receptor beta-subunit cytoplasmic domain.	Phenylalanine	25-38	insulin receptor	Homo sapiens	111-127
8024702-1	1994	Activation of the insulin receptor kinase is closely associated with autophosphorylation of several tyrosine residues in the cytoplasmic domain of the receptor"s two beta-subunits.	Tyrosine	100-108	insulin receptor	Homo sapiens	18-34
8024702-2	1994	To determine the contribution of these tyrosine phosphorylations to autoactivation of the receptor kinase, we have blocked phosphorylation at specific tyrosine by replacing these tyrosine residues, individually and in combination, with phenylalanine in a soluble 45-kD analog of the cytoplasmic insulin receptor kinase domain (CIRK).	Phenylalanine	236-249	insulin receptor	Homo sapiens	295-311
8179619-0	1994	Effect of dexamethasone on the carbohydrate chains of the insulin receptor.	Dexamethasone	10-23	insulin receptor	Homo sapiens	58-74
7927191-2	1994	Insulin receptor activity, as assessed by [125I Tyr A14] insulin binding, was significantly lower in erythrocyte preparations from the obese group when compared with similar preparations from non-obese subjects, with either normal glucose tolerance or NIDDM.	Tyrosine	48-51	insulin receptor	Homo sapiens	0-16
7927191-2	1994	Insulin receptor activity, as assessed by [125I Tyr A14] insulin binding, was significantly lower in erythrocyte preparations from the obese group when compared with similar preparations from non-obese subjects, with either normal glucose tolerance or NIDDM.	Glucose	231-238	insulin receptor	Homo sapiens	0-16
7927191-4	1994	Insulin receptor tyrosine kinase activity, measured in the absence (basal) and presence of insulin (0.3-3000 nM), was decreased in obese and NIDDM subjects with normal glucose tolerance and in patients with NIDDM.	Glucose	168-175	insulin receptor	Homo sapiens	0-16
8179619-0	1994	Effect of dexamethasone on the carbohydrate chains of the insulin receptor.	Carbohydrates	31-43	insulin receptor	Homo sapiens	58-74
8179619-3	1994	The carbohydrate side chains of the insulin receptor were less branched on the dexamethasone-treated cells; i.e., the ratio of saccharides with three and four branches to those bearing only two branches was decreased.	Carbohydrates	4-16	insulin receptor	Homo sapiens	36-52
8179619-3	1994	The carbohydrate side chains of the insulin receptor were less branched on the dexamethasone-treated cells; i.e., the ratio of saccharides with three and four branches to those bearing only two branches was decreased.	Dexamethasone	79-92	insulin receptor	Homo sapiens	36-52
7512567-6	1994	These studies indicate that insulin stimulates the tyrosine phosphorylation of at least two distinct 60-kDa proteins, one that becomes associated with GAP and appears to be a direct substrate of the insulin receptor kinase and another that associates with the phosphatidylinositol 3-kinase.	Tyrosine	51-59	insulin receptor	Homo sapiens	199-215
8069230-0	1994	Association of GIR, a novel 66kDa GTP-binding placental protein, with insulin receptor.	Guanosine Triphosphate	34-37	insulin receptor	Homo sapiens	70-86
8069230-5	1994	IR and Gir from human placental membrane bound to insulin-Sepharose column.	Sepharose	58-67	insulin receptor	Homo sapiens	0-2
8069230-6	1994	GTP as well as GDP (1 mM) eluted Gir from the column and acetate buffer (pH 5.0) eluted both IR and Gir.	Acetates	57-64	insulin receptor	Homo sapiens	93-95
8069230-7	1994	Both IR and Gir, thus eluted, absorbed on the anti-IR-Sepharose column and GTP eluted Gir.	Sepharose	54-63	insulin receptor	Homo sapiens	5-7
8166629-6	1994	When tested on purified enzymes, Itu did not affect the activities of the major Ser/Thr-specific protein phosphatases (PP-1, PP-2A, PP-2B and PP-2C), but it inhibited various Ser/Thr-specific protein kinases as well as the tyrosine kinase activity of the insulin receptor (IC50 between 0.4 and 28 microM at 10-15 microM ATP).	5-iodotubercidin	33-36	insulin receptor	Homo sapiens	255-271
7510639-0	1994	Src homology 2 domains of protein tyrosine phosphatase are associated in vitro with both the insulin receptor and insulin receptor substrate-1 via different phosphotyrosine motifs.	Phosphotyrosine	157-172	insulin receptor	Homo sapiens	93-109
8131857-1	1994	Treatment of Chinese hamster ovary (CHO) cells over-expressing the human insulin receptor (CHO-HIRc) with the insulin mimetic agent, vanadate, resulted in a dose- and time-dependent tyrosine phosphorylation of two proteins with apparent molecular sizes of 42 kDa (p42) and 44 kDa (p44).	Vanadates	133-141	insulin receptor	Homo sapiens	73-89
8131857-1	1994	Treatment of Chinese hamster ovary (CHO) cells over-expressing the human insulin receptor (CHO-HIRc) with the insulin mimetic agent, vanadate, resulted in a dose- and time-dependent tyrosine phosphorylation of two proteins with apparent molecular sizes of 42 kDa (p42) and 44 kDa (p44).	Tyrosine	182-190	insulin receptor	Homo sapiens	73-89
8135757-0	1994	Identification of serines-967/968 in the juxtamembrane region of the insulin receptor as insulin-stimulated phosphorylation sites.	Serine	18-25	insulin receptor	Homo sapiens	69-85
8200911-9	1994	However, a monoclonal antibody to the insulin receptor (MA-20) at equimolar concentrations with insulin equally inhibits pertussis toxin-catalyzed ADP ribosylation of Gi without activating tyrosine kinase or insulin receptor autophosphorylation.	Adenosine Diphosphate	147-150	insulin receptor	Homo sapiens	38-54
8179619-3	1994	The carbohydrate side chains of the insulin receptor were less branched on the dexamethasone-treated cells; i.e., the ratio of saccharides with three and four branches to those bearing only two branches was decreased.	Carbohydrates	127-138	insulin receptor	Homo sapiens	36-52
8119395-0	1994	Guanosine 5"-(gamma-thio) triphosphate (GTP gamma S) inhibits phosphorylation of insulin receptor and a novel GTP-binding protein, Gir, from human placenta.	Guanosine 5'-O-(3-Thiotriphosphate)	0-38	insulin receptor	Homo sapiens	81-97
8119395-0	1994	Guanosine 5"-(gamma-thio) triphosphate (GTP gamma S) inhibits phosphorylation of insulin receptor and a novel GTP-binding protein, Gir, from human placenta.	Guanosine Triphosphate	40-43	insulin receptor	Homo sapiens	81-97
8119395-2	1994	This protein binds 8-azido-GTP, is ADP-ribosylated by pertussis toxin, phosphorylated by IR tyrosine kinase and cross-reacts with antibodies against synthetic peptides from the GTP-binding domain of Gz alpha(P960).	8-azidoguanosine triphosphate	19-30	insulin receptor	Homo sapiens	89-91
8119395-2	1994	This protein binds 8-azido-GTP, is ADP-ribosylated by pertussis toxin, phosphorylated by IR tyrosine kinase and cross-reacts with antibodies against synthetic peptides from the GTP-binding domain of Gz alpha(P960).	Peptides	159-167	insulin receptor	Homo sapiens	89-91
8119395-2	1994	This protein binds 8-azido-GTP, is ADP-ribosylated by pertussis toxin, phosphorylated by IR tyrosine kinase and cross-reacts with antibodies against synthetic peptides from the GTP-binding domain of Gz alpha(P960).	Guanosine Triphosphate	27-30	insulin receptor	Homo sapiens	89-91
8119950-0	1994	Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling.	Serine	0-6	insulin receptor	Homo sapiens	36-52
8119950-0	1994	Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling.	Threonine	7-16	insulin receptor	Homo sapiens	36-52
7509599-6	1994	Thiol redox reactions are known to play a role in regulating conformational changes in the insulin receptor and possibly also in the IGF-I receptor.	Sulfhydryl Compounds	0-5	insulin receptor	Homo sapiens	91-107
8192864-3	1994	Independent of the purification state the analysis of the phosphoamino acids of the insulin receptor beta-subunit showed tyrosine and serine phosphorylation in an insulin dependent manner.	Phosphoamino Acids	58-76	insulin receptor	Homo sapiens	84-100
8192864-3	1994	Independent of the purification state the analysis of the phosphoamino acids of the insulin receptor beta-subunit showed tyrosine and serine phosphorylation in an insulin dependent manner.	Tyrosine	121-129	insulin receptor	Homo sapiens	84-100
8192864-3	1994	Independent of the purification state the analysis of the phosphoamino acids of the insulin receptor beta-subunit showed tyrosine and serine phosphorylation in an insulin dependent manner.	Serine	134-140	insulin receptor	Homo sapiens	84-100
8288048-1	1994	The insulin receptor is synthesized as a single chain of 190 kiloDaltons, which is processed to disulfide-linked mature alpha- and beta- subunits, containing N- and O-linked oligosaccharides and fatty acids.	Disulfides	96-105	insulin receptor	Homo sapiens	4-20
8288048-1	1994	The insulin receptor is synthesized as a single chain of 190 kiloDaltons, which is processed to disulfide-linked mature alpha- and beta- subunits, containing N- and O-linked oligosaccharides and fatty acids.	n- and o-linked oligosaccharides	158-190	insulin receptor	Homo sapiens	4-20
8288048-1	1994	The insulin receptor is synthesized as a single chain of 190 kiloDaltons, which is processed to disulfide-linked mature alpha- and beta- subunits, containing N- and O-linked oligosaccharides and fatty acids.	Fatty Acids	195-206	insulin receptor	Homo sapiens	4-20
8200732-4	1994	Thus, the free tyrosyl side-chain containing-peptide IR (1142-1153) on support was phosphinylated with the above phosphoramidite reagent followed by oxidation with either S8/CS2 or tetraethylthiuram disulfide/CH3CN solutions.	phosphoramidite	113-128	insulin receptor	Homo sapiens	53-55
8200732-4	1994	Thus, the free tyrosyl side-chain containing-peptide IR (1142-1153) on support was phosphinylated with the above phosphoramidite reagent followed by oxidation with either S8/CS2 or tetraethylthiuram disulfide/CH3CN solutions.	Disulfiram	181-208	insulin receptor	Homo sapiens	53-55
8200732-4	1994	Thus, the free tyrosyl side-chain containing-peptide IR (1142-1153) on support was phosphinylated with the above phosphoramidite reagent followed by oxidation with either S8/CS2 or tetraethylthiuram disulfide/CH3CN solutions.	acetonitrile	209-214	insulin receptor	Homo sapiens	53-55
8276809-8	1994	These data support the hypothesis that binding of tyrosyl-phosphorylated receptors to p85 SH2 domains is a general mechanism for PtdIns 3"-kinase activation, and they suggest that direct interactions between the insulin receptor and PtdIns 3"-kinase may provide an alternative pathway for the activation of this enzyme by insulin.	cyclo(tyrosyl-tyrosyl)	50-57	insulin receptor	Homo sapiens	212-228
8278385-0	1994	Ala-->Gly mutation in the putative catalytic loop confers temperature sensitivity on Ros, insulin receptor, and insulin-like growth factor I receptor protein-tyrosine kinases.	Alanine	0-3	insulin receptor	Homo sapiens	93-152
8278385-0	1994	Ala-->Gly mutation in the putative catalytic loop confers temperature sensitivity on Ros, insulin receptor, and insulin-like growth factor I receptor protein-tyrosine kinases.	Glycine	9-12	insulin receptor	Homo sapiens	93-152
8190022-2	1994	Insulin receptor kinase activity was evaluated using the synthetic polypeptide poly(Glu-Tyr)(4:1) as substrate.	poly(glu-tyr)	79-92	insulin receptor	Homo sapiens	0-16
8088708-5	1994	The insulin receptor binds insulin with high affinity, and this specificity is determined by domains lying to the N-terminal and C-terminal sides of the cysteine-rich region in the alpha-subunit.	Cysteine	153-161	insulin receptor	Homo sapiens	4-20
8088709-11	1994	In a rat-1 fibroblast cell line overexpressing human insulin receptor, inhibition of the tyrosine kinase activity of the receptor can be induced by high glucose levels.	Glucose	153-160	insulin receptor	Homo sapiens	53-69
8088709-12	1994	This effect appears to be mediated through activation of certain protein kinase C isoforms, which are able to form stable complexes with the insulin receptor and modulate its tyrosine kinase activity through serine phosphorylation of the receptor beta-subunit.	Serine	208-214	insulin receptor	Homo sapiens	141-157
7997056-3	1994	As a possible primary abnormal event in sporadic Alzheimer"s disease, a desensitization of the neuronal insulin receptor and the subsequent deficits in ATP and acetylcholine are discussed with its impact on protein processing in general and beta-amyloid formation in particular, and neurotoxicity of the latter.	Acetylcholine	160-173	insulin receptor	Homo sapiens	104-120
8190022-4	1994	The levels of poly(Glu-Tyr)(4:1) phosphorylation were significantly higher in the insulin receptor preparations incubated in the presence of the Asu11-hGH 6-13 peptide.	poly(glu-tyr)	14-27	insulin receptor	Homo sapiens	82-98
8190022-7	1994	From these data, it is concluded that the increase of poly (Glu-Tyr) (4:1) phosphorylation is the result of the interaction between the Asu11-hGH 6-13 and the hepatic insulin receptor.	poly (glu-tyr)	54-68	insulin receptor	Homo sapiens	167-183
7504175-2	1993	It contains over 20 potential tyrosine phosphorylation sites, and we suspect that multiple insulin signals are enabled when the activated insulin receptor kinase phosphorylates several of them.	Tyrosine	30-38	insulin receptor	Homo sapiens	138-154
8267569-0	1993	Importance of Asp1191 for tyrosine kinase activity of the insulin receptor: functional difference of universally conserved Asp between tyrosine kinase and c-AMP dependent serine/threonine protein kinase.	Aspartic Acid	14-17	insulin receptor	Homo sapiens	58-74
8267569-1	1993	Asp1191 of the tyrosine kinase domain in the insulin receptor is located in the almost perfectly conserved Ser-Asp-X-Trp motif of all tyrosine kinases, and the function of the motif has not been clarified.	Serine	107-110	insulin receptor	Homo sapiens	45-61
8267569-1	1993	Asp1191 of the tyrosine kinase domain in the insulin receptor is located in the almost perfectly conserved Ser-Asp-X-Trp motif of all tyrosine kinases, and the function of the motif has not been clarified.	Aspartic Acid	0-3	insulin receptor	Homo sapiens	45-61
8267569-1	1993	Asp1191 of the tyrosine kinase domain in the insulin receptor is located in the almost perfectly conserved Ser-Asp-X-Trp motif of all tyrosine kinases, and the function of the motif has not been clarified.	x-trp	115-120	insulin receptor	Homo sapiens	45-61
7815387-0	1994	Dexamethasone mediated stabilization of insulin receptor mRNA.	Dexamethasone	0-13	insulin receptor	Homo sapiens	40-56
7815387-3	1994	In the glucocorticoid responsive breast cancer cell line, MCF-7, Dex increased IR mRNA by 60%, and increased the IR mRNA half-life from approximately 6hrs to > 24 hrs.	Dexamethasone	65-68	insulin receptor	Homo sapiens	79-81
7815387-3	1994	In the glucocorticoid responsive breast cancer cell line, MCF-7, Dex increased IR mRNA by 60%, and increased the IR mRNA half-life from approximately 6hrs to > 24 hrs.	Dexamethasone	65-68	insulin receptor	Homo sapiens	113-115
7524845-5	1994	The existence of the common epitope leads to competition of insulin and apoprotein B for an insulin receptor and reduces tissue glucose uptake.	Glucose	128-135	insulin receptor	Homo sapiens	92-108
8243830-0	1993	Ala1048-->Asp mutation in the kinase domain of insulin receptor causes defective kinase activity and insulin resistance.	Aspartic Acid	13-16	insulin receptor	Homo sapiens	50-66
8243830-1	1993	We identified a heterozygous missense mutation that substituted aspartic acid (GAC) for alanine (GCC) at codon 1048 of the insulin receptor gene in a patient who displayed typical symptoms of Type A syndrome of insulin resistance.	Aspartic Acid	64-77	insulin receptor	Homo sapiens	123-139
8243830-1	1993	We identified a heterozygous missense mutation that substituted aspartic acid (GAC) for alanine (GCC) at codon 1048 of the insulin receptor gene in a patient who displayed typical symptoms of Type A syndrome of insulin resistance.	DIHYDRO-ACARBOSE	79-82	insulin receptor	Homo sapiens	123-139
8243830-1	1993	We identified a heterozygous missense mutation that substituted aspartic acid (GAC) for alanine (GCC) at codon 1048 of the insulin receptor gene in a patient who displayed typical symptoms of Type A syndrome of insulin resistance.	Alanine	88-95	insulin receptor	Homo sapiens	123-139
8243830-6	1993	Photoaffinity labeling of the mutant insulin receptor with ATP analogue, 8-azido (alpha-32P)ATP was not influenced by the mutation, suggesting that the mutation did not inhibit ATP binding but possibly interfered with subsequent phosphoryl transfer.	Adenosine Triphosphate	59-62	insulin receptor	Homo sapiens	37-53
8243830-6	1993	Photoaffinity labeling of the mutant insulin receptor with ATP analogue, 8-azido (alpha-32P)ATP was not influenced by the mutation, suggesting that the mutation did not inhibit ATP binding but possibly interfered with subsequent phosphoryl transfer.	8-Azido-[alpha-32P]ATP	73-95	insulin receptor	Homo sapiens	37-53
8243830-6	1993	Photoaffinity labeling of the mutant insulin receptor with ATP analogue, 8-azido (alpha-32P)ATP was not influenced by the mutation, suggesting that the mutation did not inhibit ATP binding but possibly interfered with subsequent phosphoryl transfer.	Adenosine Triphosphate	92-95	insulin receptor	Homo sapiens	37-53
7504303-3	1993	By this method we have found multiple proteins (including the p85 subunit of phosphatidylinositol 3"-kinase and the ras GTPase-activating protein) that specifically associate with the activated (phosphorylated) insulin receptor (insulin receptor complex proteins) but are released from the complex after they are phosphorylated on tyrosine residues.	Tyrosine	331-339	insulin receptor	Homo sapiens	211-227
7504303-3	1993	By this method we have found multiple proteins (including the p85 subunit of phosphatidylinositol 3"-kinase and the ras GTPase-activating protein) that specifically associate with the activated (phosphorylated) insulin receptor (insulin receptor complex proteins) but are released from the complex after they are phosphorylated on tyrosine residues.	Tyrosine	331-339	insulin receptor	Homo sapiens	229-245
7504303-4	1993	We have also shown that tyrosine phosphorylation of p85 by the activated insulin receptor blocks binding to the activated receptor.	Tyrosine	24-32	insulin receptor	Homo sapiens	73-89
7504175-4	1993	We identified some of the tyrosine residues of IRS-1 that undergo insulin-stimulated phosphorylation by the purified insulin receptor and in intact cells during insulin stimulation.	Tyrosine	26-34	insulin receptor	Homo sapiens	117-133
8252754-3	1993	These findings provide the first evidence that insulin receptor mRNA levels may be modulated in vivo by high levels of catecholamines.	Catecholamines	119-133	insulin receptor	Homo sapiens	47-63
8227078-1	1993	Several tyrosine phosphorylation sites in the insulin receptor kinase substrate IRS-1 are predicted to be within Tyr-Met-X-Met (YMXM) motifs, and synthetic peptides corresponding to these sequences are excellent substrates for the insulin receptor kinase in vitro (Shoelson, S. E., Chatterjee, S., Chaudhuri, M., and White, M. F. (1992) Proc.	Tyrosine	8-16	insulin receptor	Homo sapiens	46-62
8227078-1	1993	Several tyrosine phosphorylation sites in the insulin receptor kinase substrate IRS-1 are predicted to be within Tyr-Met-X-Met (YMXM) motifs, and synthetic peptides corresponding to these sequences are excellent substrates for the insulin receptor kinase in vitro (Shoelson, S. E., Chatterjee, S., Chaudhuri, M., and White, M. F. (1992) Proc.	Tyrosine	8-16	insulin receptor	Homo sapiens	231-247
8227078-1	1993	Several tyrosine phosphorylation sites in the insulin receptor kinase substrate IRS-1 are predicted to be within Tyr-Met-X-Met (YMXM) motifs, and synthetic peptides corresponding to these sequences are excellent substrates for the insulin receptor kinase in vitro (Shoelson, S. E., Chatterjee, S., Chaudhuri, M., and White, M. F. (1992) Proc.	Tyrosine	113-116	insulin receptor	Homo sapiens	46-62
8227078-1	1993	Several tyrosine phosphorylation sites in the insulin receptor kinase substrate IRS-1 are predicted to be within Tyr-Met-X-Met (YMXM) motifs, and synthetic peptides corresponding to these sequences are excellent substrates for the insulin receptor kinase in vitro (Shoelson, S. E., Chatterjee, S., Chaudhuri, M., and White, M. F. (1992) Proc.	Tyrosine	113-116	insulin receptor	Homo sapiens	231-247
8224218-6	1993	ISRP2 and ISRP3 contained five of six autophosphorylated tyrosine residues in insR.	Tyrosine	57-65	insulin receptor	Homo sapiens	78-82
8130075-0	1993	The role of polybasic compounds in determining the tyrosyl phosphorylation of calmodulin by the human insulin receptor.	cyclo(tyrosyl-tyrosyl)	51-58	insulin receptor	Homo sapiens	102-118
8130075-4	1993	Polybasic substances such as poly-L-arginine, histone H1 and protamine sulphate all promoted calmodulin phosphorylation by the insulin receptor in a similar biphasic dose-dependent fashion.	polyarginine	29-44	insulin receptor	Homo sapiens	127-143
7906861-7	1993	alpha 2HSG, purified from human serum, specifically inhibits insulin-stimulated IR autophosphorylation in vitro and in vivo as well as exogenous substrate tyrosine phosphorylation.	alpha 2hsg	0-10	insulin receptor	Homo sapiens	80-82
8270132-5	1993	One allele contains in-frame 12 additional base pairs in exon 3 coding for the amino acids Leu-His-Leu-Val located between Asp-261 and Leu-262 in the receptor"s extracellular domain, being the first report of an insertion mutation of the insulin receptor gene.	leu-his-	91-99	insulin receptor	Homo sapiens	238-254
8270132-5	1993	One allele contains in-frame 12 additional base pairs in exon 3 coding for the amino acids Leu-His-Leu-Val located between Asp-261 and Leu-262 in the receptor"s extracellular domain, being the first report of an insertion mutation of the insulin receptor gene.	H-LEU-VAL-OH	99-106	insulin receptor	Homo sapiens	238-254
8270132-5	1993	One allele contains in-frame 12 additional base pairs in exon 3 coding for the amino acids Leu-His-Leu-Val located between Asp-261 and Leu-262 in the receptor"s extracellular domain, being the first report of an insertion mutation of the insulin receptor gene.	Aspartic Acid	123-126	insulin receptor	Homo sapiens	238-254
8270132-5	1993	One allele contains in-frame 12 additional base pairs in exon 3 coding for the amino acids Leu-His-Leu-Val located between Asp-261 and Leu-262 in the receptor"s extracellular domain, being the first report of an insertion mutation of the insulin receptor gene.	Leucine	91-94	insulin receptor	Homo sapiens	238-254
7692086-7	1993	We conclude that deletion of the carboxyl region of the Gag-IGFR inactivates, instead of activating as in the case with Gag-IR, its transforming activity and the amino acid sequence 1250 to 1310 is essential for PTK and transforming activities.	Glycosaminoglycans	56-59	insulin receptor	Homo sapiens	124-126
8216295-1	1993	We examined the effect of anti-phosphothreonine and anti-phosphoserine antibodies on insulin receptor autophosphorylation.	Phosphoserine	57-70	insulin receptor	Homo sapiens	85-101
8216295-5	1993	These data suggest that phosphoserine and phosphothreonine on insulin receptor play an important role in insulin-induced conformational change of the receptor.	Phosphoserine	24-37	insulin receptor	Homo sapiens	62-78
8216295-5	1993	These data suggest that phosphoserine and phosphothreonine on insulin receptor play an important role in insulin-induced conformational change of the receptor.	Phosphothreonine	42-58	insulin receptor	Homo sapiens	62-78
8408055-0	1993	Effect of dexamethasone on the alternative splicing of the insulin receptor mRNA and insulin action in HepG2 hepatoma cells.	Dexamethasone	10-23	insulin receptor	Homo sapiens	59-75
8408055-4	1993	Dexamethasone alone could cause both a switch in expression from the A to the B isoform of the insulin receptor and also an increase in insulin sensitivity for both glucose incorporation into glycogen and 2-deoxyglucose transport.	Dexamethasone	0-13	insulin receptor	Homo sapiens	95-111
8408055-4	1993	Dexamethasone alone could cause both a switch in expression from the A to the B isoform of the insulin receptor and also an increase in insulin sensitivity for both glucose incorporation into glycogen and 2-deoxyglucose transport.	Glycogen	192-200	insulin receptor	Homo sapiens	95-111
8409897-1	1993	The insulin receptor, purified from the hepatopancreas of the shrimp Penaeus monodon, is a hydrophobic heterodimer of subunits with relative masses (Mr) of 70,000 and 58,000, as estimated by FPLC on Superose 12 and SDS-PAGE.	superose	199-207	insulin receptor	Homo sapiens	4-20
8409897-1	1993	The insulin receptor, purified from the hepatopancreas of the shrimp Penaeus monodon, is a hydrophobic heterodimer of subunits with relative masses (Mr) of 70,000 and 58,000, as estimated by FPLC on Superose 12 and SDS-PAGE.	Sodium Dodecyl Sulfate	215-218	insulin receptor	Homo sapiens	4-20
7504175-1	1993	IRS-1 (insulin receptor substrate 1) is a principal insulin receptor substrate that undergoes tyrosine phosphorylation during insulin stimulation.	Tyrosine	94-102	insulin receptor	Homo sapiens	7-23
7906861-11	1993	Finally, the action of alpha 2HSG is specific toward the IR-TK; its effect does not extend to insulin-like growth factor-I-stimulated TKA.	alpha 2hsg	23-33	insulin receptor	Homo sapiens	57-59
8356081-0	1993	Insulin stimulates the biosynthesis of chiro-inositol-containing phospholipids in a rat fibroblast line expressing the human insulin receptor.	Inositol	39-53	insulin receptor	Homo sapiens	125-141
8356081-0	1993	Insulin stimulates the biosynthesis of chiro-inositol-containing phospholipids in a rat fibroblast line expressing the human insulin receptor.	Phospholipids	65-78	insulin receptor	Homo sapiens	125-141
8390680-2	1993	However, a Gly-Pro sequence within the TM domain of the insulin receptor is predicted to act as a helix breaker.	glycylproline	11-18	insulin receptor	Homo sapiens	56-72
8393875-1	1993	Phosphorylation of threonine 1336 of the human insulin receptor (HIR) is stimulated by insulin or 4 beta-phorbol 12-myristate 13-acetate in Chinese hamster ovary (CHO) transfectant cells expressing the wild type receptor (CHO/HIR).	Threonine	19-28	insulin receptor	Homo sapiens	47-63
8393875-1	1993	Phosphorylation of threonine 1336 of the human insulin receptor (HIR) is stimulated by insulin or 4 beta-phorbol 12-myristate 13-acetate in Chinese hamster ovary (CHO) transfectant cells expressing the wild type receptor (CHO/HIR).	Tetradecanoylphorbol Acetate	98-136	insulin receptor	Homo sapiens	47-63
7686158-6	1993	Insulin, guanosine 5"-O-(3-thiotriphosphate), guanylyl imidodiphosphate, NaF, and phorbol 12-myristate 13-acetate also induced the translocation of GLUT4myc in Chinese hamster ovary cells coexpressing the human insulin receptor.	Guanylyl Imidodiphosphate	46-71	insulin receptor	Homo sapiens	211-227
7686158-6	1993	Insulin, guanosine 5"-O-(3-thiotriphosphate), guanylyl imidodiphosphate, NaF, and phorbol 12-myristate 13-acetate also induced the translocation of GLUT4myc in Chinese hamster ovary cells coexpressing the human insulin receptor.	Tetradecanoylphorbol Acetate	82-113	insulin receptor	Homo sapiens	211-227
8401310-1	1993	A 66 kDa GTP-binding protein, Gir, and insulin receptor (IR) were copurified from human placental membrane by DEAE-Sephacel and Wheat Germ Agglutinin (WGA)-Sepharose affinity chromatography.	2-diethylaminoethanol	110-114	insulin receptor	Homo sapiens	57-59
8401310-1	1993	A 66 kDa GTP-binding protein, Gir, and insulin receptor (IR) were copurified from human placental membrane by DEAE-Sephacel and Wheat Germ Agglutinin (WGA)-Sepharose affinity chromatography.	Sepharose	156-165	insulin receptor	Homo sapiens	57-59
8401310-2	1993	The WGA-fraction containing IR and Gir (IR-Gir-fraction) was phosphorylated (95 kDa IR-beta and 66 kDa Gir) by IR-tyrosine kinase using [32P]ATP or photolabeled with [32P]8-azido-GTP (mainly 66 kDa), and was cross-linked with a bifunctional reagent, bis-[sulfosuccinimidyl] suberate (BS3).	Phosphorus-32	137-140	insulin receptor	Homo sapiens	28-30
8401310-2	1993	The WGA-fraction containing IR and Gir (IR-Gir-fraction) was phosphorylated (95 kDa IR-beta and 66 kDa Gir) by IR-tyrosine kinase using [32P]ATP or photolabeled with [32P]8-azido-GTP (mainly 66 kDa), and was cross-linked with a bifunctional reagent, bis-[sulfosuccinimidyl] suberate (BS3).	Adenosine Triphosphate	141-144	insulin receptor	Homo sapiens	28-30
8401310-2	1993	The WGA-fraction containing IR and Gir (IR-Gir-fraction) was phosphorylated (95 kDa IR-beta and 66 kDa Gir) by IR-tyrosine kinase using [32P]ATP or photolabeled with [32P]8-azido-GTP (mainly 66 kDa), and was cross-linked with a bifunctional reagent, bis-[sulfosuccinimidyl] suberate (BS3).	Phosphorus-32	167-170	insulin receptor	Homo sapiens	28-30
8401310-2	1993	The WGA-fraction containing IR and Gir (IR-Gir-fraction) was phosphorylated (95 kDa IR-beta and 66 kDa Gir) by IR-tyrosine kinase using [32P]ATP or photolabeled with [32P]8-azido-GTP (mainly 66 kDa), and was cross-linked with a bifunctional reagent, bis-[sulfosuccinimidyl] suberate (BS3).	8-azidoguanosine triphosphate	171-182	insulin receptor	Homo sapiens	28-30
8401310-2	1993	The WGA-fraction containing IR and Gir (IR-Gir-fraction) was phosphorylated (95 kDa IR-beta and 66 kDa Gir) by IR-tyrosine kinase using [32P]ATP or photolabeled with [32P]8-azido-GTP (mainly 66 kDa), and was cross-linked with a bifunctional reagent, bis-[sulfosuccinimidyl] suberate (BS3).	bis-[sulfosuccinimidyl	250-272	insulin receptor	Homo sapiens	28-30
8513978-1	1993	Two N-linked sites of glycosylation in the insulin receptor were examined for their contribution to insulin binding, tyrosine kinase activity, and receptor biosynthesis.	Nitrogen	4-5	insulin receptor	Homo sapiens	43-59
8504095-10	1993	These observations demonstrate that: (1) both ATP and insulin regulate reaction in each autophosphorylation subdomain, (2) insulin stimulation occurs predominantly in the central and carboxy-terminal regions, and (3) autophosphorylation observed with the cytoplasmic kinase domain was similar to native insulin receptor in the absence of insulin.	Adenosine Triphosphate	46-49	insulin receptor	Homo sapiens	303-319
8390680-4	1993	On this basis, Gly933 and Pro934 within the TM domain of the intact human insulin receptor were mutated to Ala (G-->A, P-->A, GP-->AA) to assess effects of altered helicity on receptor functions.	Alanine	107-110	insulin receptor	Homo sapiens	74-90
8388799-0	1993	Human erythrocyte insulin receptor processing is affected by the oxidizing agent menadione.	Vitamin K 3	81-90	insulin receptor	Homo sapiens	18-34
8505282-1	1993	The insulin receptor substrate 1 (IRS1) is a protein that is rapidly phosphorylated on tyrosine by the activated insulin receptor.	Tyrosine	87-95	insulin receptor	Homo sapiens	4-20
8496180-0	1993	Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor.	Serine	19-25	insulin receptor	Homo sapiens	90-106
8503928-1	1993	The effects of phorbol ester induced activation of protein kinase C on insulin receptor phosphorylation and tyrosine kinase activity have been investigated in transfected fibroblasts expressing high levels of the human insulin receptor.	Phorbol Esters	15-28	insulin receptor	Homo sapiens	71-87
8496180-1	1993	Insulin-stimulated autophosphorylation of the cytoplasmic juxtamembrane region of the human insulin receptor was examined by Tricine/SDS-PAGE.	Sodium Dodecyl Sulfate	133-136	insulin receptor	Homo sapiens	92-108
8496180-0	1993	Insulin stimulates serine and tyrosine phosphorylation in the juxtamembrane region of the insulin receptor.	Tyrosine	30-38	insulin receptor	Homo sapiens	90-106
8496180-9	1993	The insulin receptor also undergoes serine phosphorylation outside of the juxtamembrane region which depends on the presence of Tyr1151.	Serine	36-42	insulin receptor	Homo sapiens	4-20
8496180-1	1993	Insulin-stimulated autophosphorylation of the cytoplasmic juxtamembrane region of the human insulin receptor was examined by Tricine/SDS-PAGE.	tricine	125-132	insulin receptor	Homo sapiens	92-108
8491186-5	1993	The interactions between GRB2 and these two proteins require ligand activation of the insulin receptor and are mediated by the binding of the SH2 domain of GRB2 to phosphotyrosines on both IRS-1 and Shc.	Phosphotyrosine	164-180	insulin receptor	Homo sapiens	86-102
8389126-1	1993	Sulphydryl reagents have been shown to produce a variety of effects on insulin-receptor structure and function.	sulphydryl reagents	0-19	insulin receptor	Homo sapiens	71-87
8389126-6	1993	These results contrast with those obtained with dithiothreitol which appears to activate phosphorylation in association with reduction of the extracellular insulin-receptor disulphides, but is without effect on the EGF receptor or the IRK protein.	Dithiothreitol	48-62	insulin receptor	Homo sapiens	156-172
8389126-6	1993	These results contrast with those obtained with dithiothreitol which appears to activate phosphorylation in association with reduction of the extracellular insulin-receptor disulphides, but is without effect on the EGF receptor or the IRK protein.	disulphides	173-184	insulin receptor	Homo sapiens	156-172
7683457-0	1993	Inhibitory effect of fluoride on insulin receptor autophosphorylation and tyrosine kinase activity.	Fluorides	21-29	insulin receptor	Homo sapiens	33-49
8481401-0	1993	Rapid screening method of abnormal insulin-receptor gene expression: allele-specific oligonucleotide hybridization by using silent polymorphisms.	Oligonucleotides	85-100	insulin receptor	Homo sapiens	35-51
8481401-2	1993	To detect this abnormality, we designed the less laborious method; Allele-specific oligonucleotide hybridization of the amplified mRNA (cDNA) by using silent polymorphisms in the insulin receptor gene (nucleotide positions at 1686 and 1698).	Oligonucleotides	83-98	insulin receptor	Homo sapiens	179-195
8481401-6	1993	Nineteen (64%) out of 30 cases are heterozygous at one or two position(s), suggesting that it is possible to distinguish the mRNA transcribed from each of two alleles of the insulin receptor gene with using allele-specific oligonucleotide hybridization.	Oligonucleotides	223-238	insulin receptor	Homo sapiens	174-190
8481401-8	1993	We showed that allele-specific oligonucleotide hybridization method is useful for the screening of abnormal insulin-receptor gene expression.	Oligonucleotides	31-46	insulin receptor	Homo sapiens	108-124
7683457-7	1993	Addition of fluoride to the pre-phosphorylated insulin receptor produced a slow (time range of minutes) inhibition of receptor kinase activity.	Fluorides	12-20	insulin receptor	Homo sapiens	47-63
8463287-7	1993	CHO cells transfected with the wild type (CHO/HIR) or a mutant human insulin receptor (CHO/HIRT1336N), in which threonine 1336 was substituted with asparagine, were 32P labeled and then stimulated with insulin or phorbol 12-myristate 13-acetate (PMA).	Phosphorus-32	165-168	insulin receptor	Homo sapiens	69-85
8394171-0	1993	Regulation of insulin receptor signaling by protein-tyrosine dephosphorylation.	Tyrosine	52-60	insulin receptor	Homo sapiens	14-30
8394171-2	1993	PTPases also modulate signaling through postreceptor pathways by catalyzing the dephosphorylation of cellular substrates of the insulin receptor kinase, such as IRS-1, or other tyrosine-phosphorylated proteins along the cellular cascade of insulin action.	Tyrosine	177-185	insulin receptor	Homo sapiens	128-144
8454604-4	1993	However, in response to phorbol esters, cells overexpressing isoenzymes alpha, beta I, and gamma, but not epsilon or inactive alpha, exhibited 3-4-fold higher levels of insulin receptor phosphorylation.	Phorbol Esters	24-38	insulin receptor	Homo sapiens	169-185
8440700-1	1993	The unoccupied insulin receptor is a structurally symmetric, disulfide-linked dimer, comprising two alpha beta halves, each with a potential insulin binding alpha subunit and a kinase active beta subunit.	Disulfides	61-70	insulin receptor	Homo sapiens	15-31
8363571-0	1993	An insulin receptor peptide (1135-1156) stimulates guanosine 5"-[gamma-thio]triphosphate binding to the 67 kDa G-protein associated with the insulin receptor.	Guanosine 5'-O-(3-Thiotriphosphate)	51-88	insulin receptor	Homo sapiens	3-19
8363571-0	1993	An insulin receptor peptide (1135-1156) stimulates guanosine 5"-[gamma-thio]triphosphate binding to the 67 kDa G-protein associated with the insulin receptor.	Guanosine 5'-O-(3-Thiotriphosphate)	51-88	insulin receptor	Homo sapiens	141-157
8383132-1	1993	We have recently reported two non-insulin-dependent diabetic patients exhibiting a heterozygous point mutation (R1152-Q) next to the key tyrosine autophosphorylation sites (Y1146, Y1150, Y1151) of the insulin receptor.	Tyrosine	137-145	insulin receptor	Homo sapiens	201-217
8432414-0	1993	Methionine for valine substitution in exon 17 of the insulin receptor gene in a pedigree with familial NIDDM.	Methionine	0-10	insulin receptor	Homo sapiens	53-69
8432414-0	1993	Methionine for valine substitution in exon 17 of the insulin receptor gene in a pedigree with familial NIDDM.	Valine	15-21	insulin receptor	Homo sapiens	53-69
8382690-3	1993	BpaB25 insulin binds specifically to the insulin receptor with an affinity approximately 40% that of native insulin.	bpab25	0-6	insulin receptor	Homo sapiens	41-57
8382690-6	1993	Photolysis of a complex of the insulin receptor and either BpaB25 insulin or [125I]iodo-TyrA14,BpaB25 insulin yields a covalent insulin-receptor complex.	bpab25	59-65	insulin receptor	Homo sapiens	31-47
8382690-6	1993	Photolysis of a complex of the insulin receptor and either BpaB25 insulin or [125I]iodo-TyrA14,BpaB25 insulin yields a covalent insulin-receptor complex.	iodo-tyra14	83-94	insulin receptor	Homo sapiens	31-47
8382690-6	1993	Photolysis of a complex of the insulin receptor and either BpaB25 insulin or [125I]iodo-TyrA14,BpaB25 insulin yields a covalent insulin-receptor complex.	bpab25	95-101	insulin receptor	Homo sapiens	31-47
8382476-0	1993	Phorbol esters inhibit insulin-induced receptor down-regulation in cultured human lymphocytes: association with diminished insulin receptor autophosphorylation.	Phorbol Esters	0-14	insulin receptor	Homo sapiens	123-139
8382493-1	1993	One of the first steps that follows insulin receptor activation is the tyrosine phosphorylation of the 160-185 kDa insulin receptor substrate IRS-1.	Tyrosine	71-79	insulin receptor	Homo sapiens	36-52
8425534-0	1993	Differential insertion of insulin receptor complexes into Triton X-114 bilayer membranes.	Nonidet P-40	58-70	insulin receptor	Homo sapiens	26-42
8421104-4	1993	In this study we investigated the ability of the monocyte insulin receptor to acutely alter its affinity in response to oral glucose.	Glucose	125-132	insulin receptor	Homo sapiens	58-74
16353347-0	1993	Mechanism of free fatty acid effects on hepatocyte insulin receptor binding and processing.	Fatty Acids, Nonesterified	13-28	insulin receptor	Homo sapiens	51-67
1334490-2	1992	Immunoprecipitation studies of Chinese hamster ovary cells, which overexpress the human insulin receptor when treated with insulin, showed increased amounts of p85 and PI 3-kinase activity immunoprecipitable with monoclonal anti-p85 antibody and no increase in the tyrosine phosphorylation of p85.	Tyrosine	265-273	insulin receptor	Homo sapiens	88-104
8419945-0	1993	Activation of glucose transport by a natural mutation in the human insulin receptor.	Glucose	14-21	insulin receptor	Homo sapiens	67-83
8419945-3	1993	However, fibroblasts cultured from a patient with intrauterine growth restriction and severe insulin resistance (leprechaun Atl-1) had normal amounts of insulin receptor protein and defective insulin binding but constitutive activation of insulin-receptor autophosphorylation and kinase activity and of glucose transport.	Glucose	303-310	insulin receptor	Homo sapiens	239-255
8419945-17	1993	These results suggest that the R86P mutation in the insulin receptor activates glucose transport without promoting cell growth and that distinct cell types process this mutant insulin receptor differently.	Glucose	79-86	insulin receptor	Homo sapiens	52-68
1472036-0	1992	Identification of a disulfide bridge connecting the alpha-subunits of the extracellular domain of the insulin receptor.	Disulfides	20-29	insulin receptor	Homo sapiens	102-118
1472036-1	1992	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.	Disulfides	94-103	insulin receptor	Homo sapiens	36-52
1472036-4	1992	Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.	Disulfides	209-218	insulin receptor	Homo sapiens	61-77
1334088-13	1992	Insulin receptor mRNA levels were reduced to 56% of their base line within 6 h when growth-arrested cells were stimulated to proliferate; protein inhibition with cycloheximide completely inhibited the decline in insulin receptor mRNA.	Cycloheximide	162-175	insulin receptor	Homo sapiens	212-228
1334490-3	1992	Insulin also induced an association of p85 with the tyrosine-phosphorylated insulin receptor substrate 1 (IRS-1) and other phosphorylated proteins ranging in size from 100 to 170 kDa but not with the activated insulin receptor.	Tyrosine	52-60	insulin receptor	Homo sapiens	76-92
1478248-0	1992	Effect of intravenous polyunsaturated phosphatidylcholine infusion on insulin receptor processing and lipid composition of erythrocytes in patients with liver cirrhosis.	polyene phosphatidylcholine	22-57	insulin receptor	Homo sapiens	70-86
1478248-1	1992	The aim of this study was to determine whether insulin receptor processing capabilities of human erythrocytes could be improved by changing the cell membrane lipid composition using an intravenous infusion of polyunsaturated phosphatidylcholine.	polyene phosphatidylcholine	209-244	insulin receptor	Homo sapiens	47-63
1385401-1	1992	After adding insulin to cells overexpressing the insulin receptor, the activity of phosphatidylinositol (PI) 3-kinase in the anti-phosphotyrosine immunoprecipitates was rapidly and greatly increased.	Phosphatidylinositols	83-103	insulin receptor	Homo sapiens	49-65
1337116-2	1992	Insulin receptor is a heterotetrameric glycoprotein, consisting of two alpha-subunits and two beta-subunits linked by disulfide bonds.	Disulfides	118-127	insulin receptor	Homo sapiens	0-16
1331107-3	1992	However, after insulin treatment in the presence of the phosphotyrosine phosphatase inhibitor phenylarsine oxide (PAO), 5-10% of GAP was found to be associated with the insulin receptor, and, in addition, a fraction of total GAP was phosphorylated on tyrosine.	oxophenylarsine	94-112	insulin receptor	Homo sapiens	169-185
1331107-3	1992	However, after insulin treatment in the presence of the phosphotyrosine phosphatase inhibitor phenylarsine oxide (PAO), 5-10% of GAP was found to be associated with the insulin receptor, and, in addition, a fraction of total GAP was phosphorylated on tyrosine.	oxophenylarsine	114-117	insulin receptor	Homo sapiens	169-185
1331107-3	1992	However, after insulin treatment in the presence of the phosphotyrosine phosphatase inhibitor phenylarsine oxide (PAO), 5-10% of GAP was found to be associated with the insulin receptor, and, in addition, a fraction of total GAP was phosphorylated on tyrosine.	Tyrosine	63-71	insulin receptor	Homo sapiens	169-185
1331107-6	1992	These results suggest that GAP can transiently interact with the insulin receptor after insulin treatment, and this interaction is arrested after PAO pretreatment.	oxophenylarsine	146-149	insulin receptor	Homo sapiens	65-81
1280110-13	1992	Phosphorylation of the threonine residue within this sequence (corresponding to the known phosphorylation site Thr-1348 in the insulin receptor) decreased the affinity of antibody binding approx.	Threonine	23-32	insulin receptor	Homo sapiens	127-143
1280110-13	1992	Phosphorylation of the threonine residue within this sequence (corresponding to the known phosphorylation site Thr-1348 in the insulin receptor) decreased the affinity of antibody binding approx.	Threonine	111-114	insulin receptor	Homo sapiens	127-143
1385393-1	1992	When the catalytically active, tyrosyl-phosphorylated form of insulin receptor was isolated from human placenta and treated with ADP, only partial dephosphorylation was observed.	cyclo(tyrosyl-tyrosyl)	31-38	insulin receptor	Homo sapiens	62-78
1385393-1	1992	When the catalytically active, tyrosyl-phosphorylated form of insulin receptor was isolated from human placenta and treated with ADP, only partial dephosphorylation was observed.	Adenosine Diphosphate	129-132	insulin receptor	Homo sapiens	62-78
1385393-2	1992	This observation suggests the existence of two distinct classes of phosphotyrosyl residues of the phosphorylated insulin receptor: one in which the phosphoryl groups undergo reversible transfer to ADP and one in which they do not.	Adenosine Diphosphate	197-200	insulin receptor	Homo sapiens	113-129
1385401-1	1992	After adding insulin to cells overexpressing the insulin receptor, the activity of phosphatidylinositol (PI) 3-kinase in the anti-phosphotyrosine immunoprecipitates was rapidly and greatly increased.	Phosphotyrosine	130-145	insulin receptor	Homo sapiens	49-65
1385393-7	1992	Phosphorylation of the irreversible phosphorylation sites then renders the insulin receptor relatively insensitive to the continued presence of insulin and facilitates rapid reversible phosphorylation of a second group of tyrosyl residues.	cyclo(tyrosyl-tyrosyl)	222-229	insulin receptor	Homo sapiens	75-91
1385393-8	1992	The dependence of the degree of phosphorylation of insulin receptor on the ATP:ADP ratio may provide a mechanism for modulating the cellular response to insulin.	Adenosine Triphosphate	75-78	insulin receptor	Homo sapiens	51-67
1385401-4	1992	We reported previously that the 85-kDa subunit of purified PI 3-kinase was phosphorylated at tyrosine residue(s) by the insulin receptor in vitro.	Tyrosine	93-101	insulin receptor	Homo sapiens	120-136
1385393-8	1992	The dependence of the degree of phosphorylation of insulin receptor on the ATP:ADP ratio may provide a mechanism for modulating the cellular response to insulin.	Adenosine Diphosphate	79-82	insulin receptor	Homo sapiens	51-67
1385403-7	1992	Expression of the human insulin receptor and rat IRS-1 together in CHO/IR/IRS-1 cells increased the basal serine phosphorylation of IRS-1 and strongly increased tyrosine phosphorylation during insulin stimulation.	Serine	106-112	insulin receptor	Homo sapiens	24-40
1385403-7	1992	Expression of the human insulin receptor and rat IRS-1 together in CHO/IR/IRS-1 cells increased the basal serine phosphorylation of IRS-1 and strongly increased tyrosine phosphorylation during insulin stimulation.	Tyrosine	161-169	insulin receptor	Homo sapiens	24-40
1332046-1	1992	IRS-1 is an insulin receptor substrate that undergoes tyrosine phosphorylation and associates with the phosphatidylinositol (PtdIns) 3"-kinase immediately after insulin stimulation.	Tyrosine	54-62	insulin receptor	Homo sapiens	12-28
1426762-7	1992	Insulin receptor antibodies, however, have been reported to increase glucose transport without increasing kinase activity.	Glucose	69-76	insulin receptor	Homo sapiens	0-16
1332046-1	1992	IRS-1 is an insulin receptor substrate that undergoes tyrosine phosphorylation and associates with the phosphatidylinositol (PtdIns) 3"-kinase immediately after insulin stimulation.	Phosphatidylinositols	103-123	insulin receptor	Homo sapiens	12-28
1332046-2	1992	Recombinant IRS-1 protein was tyrosine phosphorylated by the insulin receptor in vitro and associated with the PtdIns 3"-kinase from lysates of quiescent 3T3 fibroblasts.	Tyrosine	30-38	insulin receptor	Homo sapiens	61-77
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Asparagine	106-109	insulin receptor	Homo sapiens	88-104
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Histidine	122-125	insulin receptor	Homo sapiens	88-104
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Phenylalanine	139-142	insulin receptor	Homo sapiens	88-104
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Lysine	115-118	insulin receptor	Homo sapiens	88-104
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Asparagine	177-180	insulin receptor	Homo sapiens	88-104
1390778-2	1992	We previously identified five such mutations located in the extracellular domain of the insulin receptor (Asn-->Lys15, His-->Arg209, Phe-->Val382, Lys-->Glu460, and Asn-->Ser462) and studied the effects of these mutations upon posttranslational processing, insulin binding, and tyrosine autophosphorylation.	Tyrosine	293-301	insulin receptor	Homo sapiens	88-104
1303753-1	1992	An autophosphorylation site in the activated insulin receptor tyrosine kinase domain has three tyrosines phosphorylated when fully activated.	Tyrosine	95-104	insulin receptor	Homo sapiens	45-61
1466789-1	1992	The insulin derivative 4-azidosalicyloyl-[B1-biocytin-B2-lysine]insulin was used to photo-affinity-label the highly purified insulin receptor from human placenta.	4-azidosalicyloyl-[b1-biocytin-b2-lysine]	23-64	insulin receptor	Homo sapiens	125-141
1476159-8	1992	For example, the immediate submembranous domain of the insulin receptor has been found to contain sequences (Gly-Pro-Leu-Tyr and, to a lesser extent, Asn-Pro-Gln-Tyr) that are necessary for normal endocytosis.	gly-pro-leu-tyr	109-124	insulin receptor	Homo sapiens	55-71
1476159-8	1992	For example, the immediate submembranous domain of the insulin receptor has been found to contain sequences (Gly-Pro-Leu-Tyr and, to a lesser extent, Asn-Pro-Gln-Tyr) that are necessary for normal endocytosis.	asn-pro-gln-tyr	150-165	insulin receptor	Homo sapiens	55-71
1321605-0	1992	Analysis of the order of autophosphorylation of human insulin receptor tyrosines 1158, 1162 and 1163.	Tyrosine	71-80	insulin receptor	Homo sapiens	54-70
1381676-1	1992	We studied the inhibitory effect of non-phosphorylated and triphosphorylated synthetic peptides, corresponding to amino acids 1143-1155 of the insulin proreceptor (domain 1151) on autophosphorylation and kinase of the insulin receptor.	Peptides	87-95	insulin receptor	Homo sapiens	218-234
1381676-13	1992	These data may provide a basis for further understanding the role of tyrosine phosphorylation in insulin receptor kinase activation or regulation.	Tyrosine	69-77	insulin receptor	Homo sapiens	97-113
1381504-0	1992	Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor.	Serine	13-19	insulin receptor	Homo sapiens	66-82
1381504-0	1992	Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor.	Tyrosine	24-32	insulin receptor	Homo sapiens	66-82
1381504-5	1992	(ii) Phosphorylation of a synthetic peptide substrate composed of insulin receptor residues 1290-1319 on serines-1305/1306 by partially purified insulin receptors was also inhibited by HNMPA.	Serine	105-112	insulin receptor	Homo sapiens	66-82
1381504-7	1992	These results suggest that the catalytic site of the insulin receptor tyrosine kinase also recognizes receptor serine residues as substrates for the phosphotransfer reaction.	Serine	111-117	insulin receptor	Homo sapiens	53-69
1381504-8	1992	Furthermore, insulin-stimulated receptor serine phosphorylation in intact cells may occur in part by an autophosphorylation mechanism subsequent to tyrosine phosphorylation of the insulin receptor.	Serine	41-47	insulin receptor	Homo sapiens	180-196
1381504-8	1992	Furthermore, insulin-stimulated receptor serine phosphorylation in intact cells may occur in part by an autophosphorylation mechanism subsequent to tyrosine phosphorylation of the insulin receptor.	Tyrosine	148-156	insulin receptor	Homo sapiens	180-196
1321605-1	1992	Insulin receptor tyrosines 1158, 1162 and 1163 are the most rapidly autophosphorylated residues following insulin binding.	Tyrosine	17-26	insulin receptor	Homo sapiens	0-16
1321605-3	1992	In the present study we demonstrate that autophosphorylation of the insulin receptor probably initiates on either of tyrosines 1158 and 1162 while autophosphorylation of tyrosine 1163 occurs predominantly late in the autophosphorylation cascade.	Tyrosine	117-126	insulin receptor	Homo sapiens	68-84
1321605-3	1992	In the present study we demonstrate that autophosphorylation of the insulin receptor probably initiates on either of tyrosines 1158 and 1162 while autophosphorylation of tyrosine 1163 occurs predominantly late in the autophosphorylation cascade.	Tyrosine	117-125	insulin receptor	Homo sapiens	68-84
1618850-0	1992	Differential role of insulin receptor autophosphorylation sites 1162 and 1163 in the long-term insulin stimulation of glucose transport, glycogenesis, and protein synthesis.	Glucose	118-125	insulin receptor	Homo sapiens	21-37
1617668-16	1992	In the breast cancer cells, MA-5, an agonist monoclonal antibody to the insulin receptor, stimulated [3H]thymidine incorporation.	Tritium	102-104	insulin receptor	Homo sapiens	72-88
1617668-16	1992	In the breast cancer cells, MA-5, an agonist monoclonal antibody to the insulin receptor, stimulated [3H]thymidine incorporation.	Thymidine	105-114	insulin receptor	Homo sapiens	72-88
1322128-8	1992	The sensitivity of the activated human IGF-I receptor to dephosphorylation on tyrosine leads to the speculation that IGF-I receptor activity might be regulated by mechanisms such as those described for the insulin receptor.	Tyrosine	78-86	insulin receptor	Homo sapiens	206-222
1644241-4	1992	The deletion shifted the reading frame, resulting in a termination codon after amino acid 867 (Glu), thereby producing a truncated insulin receptor without a transmembrane region and cytoplasmic domain.	Glutamic Acid	95-98	insulin receptor	Homo sapiens	131-147
1511777-3	1992	Aim of this work was to investigate the effects of two androgens (testosterone and dihydrotestosterone) on insulin receptor mRNA levels and insulin binding activity as well as on either metabolic or growth-promoting actions of insulin in a human larynx carcinoma cell line (HEp-2).	Testosterone	66-78	insulin receptor	Homo sapiens	107-123
1511777-3	1992	Aim of this work was to investigate the effects of two androgens (testosterone and dihydrotestosterone) on insulin receptor mRNA levels and insulin binding activity as well as on either metabolic or growth-promoting actions of insulin in a human larynx carcinoma cell line (HEp-2).	Dihydrotestosterone	83-102	insulin receptor	Homo sapiens	107-123
1320025-6	1992	We demonstrate that these 68 N-terminal amino acids of the IR also confer insulin affinity on the intact IGFI holoreceptor both in the membrane-bound state and when solubilized by Triton X-100.	Octoxynol	180-192	insulin receptor	Homo sapiens	59-61
1320027-6	1992	The level of biological function approximately paralleled the insulin-stimulated tyrosine kinase activity in the intact cell as estimated by tyrosine phosphorylation of the insulin receptor and its endogenous substrate pp 185/IRS-1.	Tyrosine	81-89	insulin receptor	Homo sapiens	173-189
1619013-9	1992	We conclude that in vivo activation of the insulin receptor tyrosine kinase in human skeletal muscle is a rapid process, related to insulin action on glucose disposal, and that circulating insulin primes inactive insulin receptor molecules for subsequent tyrosine kinase activation by a mechanism that remains to be elucidated.	Glucose	150-157	insulin receptor	Homo sapiens	43-59
1618780-1	1992	We have studied the function of a mutant human insulin receptor in which two COOH-terminal autophosphorylation sites (Tyr-1316 and -1322) were replaced by phenylalanine (F/Y COOH-terminal 2 tyrosines (CT2)).	Tyrosine	118-121	insulin receptor	Homo sapiens	47-63
1618780-1	1992	We have studied the function of a mutant human insulin receptor in which two COOH-terminal autophosphorylation sites (Tyr-1316 and -1322) were replaced by phenylalanine (F/Y COOH-terminal 2 tyrosines (CT2)).	Phenylalanine	155-168	insulin receptor	Homo sapiens	47-63
1618780-1	1992	We have studied the function of a mutant human insulin receptor in which two COOH-terminal autophosphorylation sites (Tyr-1316 and -1322) were replaced by phenylalanine (F/Y COOH-terminal 2 tyrosines (CT2)).	Tyrosine	190-199	insulin receptor	Homo sapiens	47-63
1374400-0	1992	Regulation of the expression of pp160, a putative insulin receptor signal protein, by insulin, dexamethasone, and 1-methyl-3-isobutylxanthine in 3T3-L1 adipocytes.	Dexamethasone	95-108	insulin receptor	Homo sapiens	50-66
1374400-0	1992	Regulation of the expression of pp160, a putative insulin receptor signal protein, by insulin, dexamethasone, and 1-methyl-3-isobutylxanthine in 3T3-L1 adipocytes.	1-Methyl-3-isobutylxanthine	114-141	insulin receptor	Homo sapiens	50-66
1374400-1	1992	pp160, a cytosolic protein with Mr of approximately 160,000, is phosphorylated on tyrosine in response to insulin and is considered to be involved in signaling from the insulin receptor.	Tyrosine	82-90	insulin receptor	Homo sapiens	169-185
1577744-0	1992	Intracellular signaling by a mutant human insulin receptor lacking the carboxyl-terminal tyrosine autophosphorylation sites.	Tyrosine	89-97	insulin receptor	Homo sapiens	42-58
1577744-1	1992	We have recently characterized a mutant insulin receptor (Y/F2) in which the two tyrosines in the carboxyl terminus (Tyr1316, Tyr1322) were mutated to phenylalanine.	Tyrosine	81-90	insulin receptor	Homo sapiens	40-56
1577744-1	1992	We have recently characterized a mutant insulin receptor (Y/F2) in which the two tyrosines in the carboxyl terminus (Tyr1316, Tyr1322) were mutated to phenylalanine.	Phenylalanine	151-164	insulin receptor	Homo sapiens	40-56
1577744-12	1992	In summary: 1) Y/F2 receptors exhibit normal metabolic and enhanced mitogenic signaling; 2) the enhanced mitogenic signaling is specific for the insulin receptor in the Y/F2 cells, since IGF-I-stimulated mitogenesis is normal; 3) Y/F2 cells display increased endogenous substrate phosphorylation and augmented insulin-stimulated S6 kinase activity placing these responses among insulin"s mitogenic effects; and 4) these results are consistent with the concept that the COOH-terminal tyrosine residues of the insulin receptor are normally inhibitory to mitogenic signaling.	Tyrosine	483-491	insulin receptor	Homo sapiens	145-161
1516485-0	1992	In vivo demonstration of insulin-receptor defect with 123I-labeled insulin and scintigraphic scanning in severe insulin resistance.	Iodine-123	54-58	insulin receptor	Homo sapiens	25-41
1521731-2	1992	The variant sequences Val-Met985 and Lys-Glu1068 of the insulin receptor and Val-Ile383 of GLUT 4 were each separately found in three different diabetic subjects.	Valine	22-25	insulin receptor	Homo sapiens	56-72
1521731-2	1992	The variant sequences Val-Met985 and Lys-Glu1068 of the insulin receptor and Val-Ile383 of GLUT 4 were each separately found in three different diabetic subjects.	Lysine	37-40	insulin receptor	Homo sapiens	56-72
1619960-12	1992	When insulin receptor protein is confined to small areas of the cell membrane through aggregation, any potential inhibitory function is negated and glucose entry increases dramatically.	Glucose	148-155	insulin receptor	Homo sapiens	5-21
1312805-4	1992	The detergents tested, Triton X-100, octyl-beta-D-glucopyranoside, octyl-beta-D-thioglucopyranoside, 3[(3-cholamidopropyl)dimethylammonio]propanesulfonic acid (Chaps), and Na deoxycholate affected the insulin receptor properties differently when compared with the control receptor in the absence of detergent.	3[(3-cholamidopropyl)dimethylammonio]propanesulfonic acid	101-158	insulin receptor	Homo sapiens	201-217
1312805-5	1992	On the partially purified insulin receptor, Na deoxycholate inhibited both insulin receptor activities; octyl-beta-D-glucopyranoside and octyl-beta-D-thioglucopyranoside decreased insulin binding and kinase activation as their concentration increased, particularly above their respective critical micellar concentration (CMC).	na deoxycholate	44-59	insulin receptor	Homo sapiens	26-42
1312805-13	1992	These alterations in the oligomerization status of the insulin receptor may explain the deleterious effects observed with both Chaps and octylglucoside at higher concentrations.	3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate	127-132	insulin receptor	Homo sapiens	55-71
1312805-13	1992	These alterations in the oligomerization status of the insulin receptor may explain the deleterious effects observed with both Chaps and octylglucoside at higher concentrations.	octyl-beta-D-glucoside	137-151	insulin receptor	Homo sapiens	55-71
1543016-0	1992	Metformin ameliorates extreme insulin resistance in a patient with anti-insulin receptor antibodies: description of insulin receptor and postreceptor effects in vivo and in vitro.	Metformin	0-9	insulin receptor	Homo sapiens	72-88
1328257-0	1992	Monoclonal antibody to the human insulin receptor, but not insulin, stimulates S6 kinase via human insulin receptors mutated at three major tyrosine autophosphorylation sites.	Tyrosine	140-148	insulin receptor	Homo sapiens	33-49
1328257-1	1992	Studies were carried out to examine the role of the major insulin receptor tyrosine autophosphorylation sites in stimulation of S6 kinase activity.	Tyrosine	75-83	insulin receptor	Homo sapiens	58-74
1543016-0	1992	Metformin ameliorates extreme insulin resistance in a patient with anti-insulin receptor antibodies: description of insulin receptor and postreceptor effects in vivo and in vitro.	Metformin	0-9	insulin receptor	Homo sapiens	116-132
1543016-9	1992	It is suggested that metformin increases, possibly through a change in the spatial conformation of insulin receptor within the plasma membrane, the availability of pre-existing receptors to insulin binding and/or decreases the availability of specific epitopes to antibody anchoring.	Metformin	21-30	insulin receptor	Homo sapiens	99-115
1370250-3	1992	Direct evidence is presented for the phosphorylation of myelin basic protein and microtubule-associated protein 2 on tyrosine residues by the insulin receptor.	Tyrosine	117-125	insulin receptor	Homo sapiens	142-158
1547686-1	1992	OBJECTIVE: To evaluate insulin receptor binding characteristics of urbanized South African black women with normal glucose tolerance and of patients with newly diagnosed untreated non-insulin-dependent diabetes mellitus (NIDDM).	Glucose	115-122	insulin receptor	Homo sapiens	23-39
1547686-6	1992	CONCLUSIONS: Our study of urban South African black women showed decreasing insulin-receptor activity with obesity and glucose intolerance.	Glucose	119-126	insulin receptor	Homo sapiens	76-92
1576365-7	1992	In particular, an increase in the cholesterol to phospholipid molar ratio and a decrease in polyunsaturated fatty acid content of phospholipids in erythrocyte membranes of cirrhotic patients was associated with impairments in insulin receptor processing.	Fatty Acids, Unsaturated	92-118	insulin receptor	Homo sapiens	226-242
1576365-7	1992	In particular, an increase in the cholesterol to phospholipid molar ratio and a decrease in polyunsaturated fatty acid content of phospholipids in erythrocyte membranes of cirrhotic patients was associated with impairments in insulin receptor processing.	Phospholipids	130-143	insulin receptor	Homo sapiens	226-242
1576365-8	1992	Similar changes in insulin receptor processing were observed when the molar ratio of cholesterol to phospholipid in normal erythrocytes was modified in vitro by incubation with cholesterol-rich liposomes.	Cholesterol	85-96	insulin receptor	Homo sapiens	19-35
1576365-8	1992	Similar changes in insulin receptor processing were observed when the molar ratio of cholesterol to phospholipid in normal erythrocytes was modified in vitro by incubation with cholesterol-rich liposomes.	Phospholipids	100-112	insulin receptor	Homo sapiens	19-35
1576365-8	1992	Similar changes in insulin receptor processing were observed when the molar ratio of cholesterol to phospholipid in normal erythrocytes was modified in vitro by incubation with cholesterol-rich liposomes.	Cholesterol	177-188	insulin receptor	Homo sapiens	19-35
1730683-4	1992	Long term treatment of cultured cells with insulin or the glucocorticoid dexamethasone increases or decreases, respectively, the rate constant for insulin receptor inactivation (Knutson, V. P., Ronnett, G. V., and Lane, M. D. (1982) Proc.	Dexamethasone	73-86	insulin receptor	Homo sapiens	147-163
1290322-4	1992	Idiopathic insulin resistance in type 2 diabetes is additionally characterized by reduced glucose storage, the basis of which may reside in an insulin receptor defect, in the presence of insulin receptor antibodies, in a postreceptor defect or in the synthesis of abnormal insulin molecules.	Glucose	90-97	insulin receptor	Homo sapiens	143-159
1314199-6	1992	Using this system we found that stimulation of the cells with EGF induced tyrosine autophosphorylation of the EGF-insulin receptor chimera (150 kd) and tyrosine phosphorylation of the beta-subunit of the kinase-deficient insulin receptor (95 kd).	Tyrosine	74-82	insulin receptor	Homo sapiens	114-130
1375946-2	1992	The Tyr(P) forms of the insulin receptor and its 160-kDa substrate protein (pp160) associated with fusion proteins containing either or both the SH2 domains of PI3K, but not with fusion proteins containing the two SH2 domains of GAP or phospholipase C gamma.	Tyrosine	4-7	insulin receptor	Homo sapiens	24-40
1375946-3	1992	These results demonstrate a specificity for the association of the Tyr(P) form of the insulin receptor and pp160 with SH2 domains that parallels the reported effects of insulin on PI3K, GAP, and phospholipase C gamma in vivo.	Tyrosine	67-70	insulin receptor	Homo sapiens	86-102
1314199-8	1992	When immunoaffinity purified EGF-insulin receptor hybrids and kinase-deficient insulin receptors were used in a cell lysate phosphorylation assay, it was found that addition of EGF produced [32P]-labeling of both receptor species.	Phosphorus-32	191-194	insulin receptor	Homo sapiens	33-49
1316358-4	1992	Non-tyrosine kinase pathways that could signal insulin effects through the insulin receptor include non-covalent activation of G proteins, phospholipase Cs, or docking proteins such as IRS-1.	Cesium	153-155	insulin receptor	Homo sapiens	75-91
1939203-0	1991	Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor.	Serine	19-25	insulin receptor	Homo sapiens	69-85
1308998-0	1992	Mutations in the insulin receptor and their effect on glucose transport.	Glucose	54-61	insulin receptor	Homo sapiens	17-33
1661148-9	1991	When effects of polylysine and polyarginine on both receptor TPKs were closely compared, subtle qualitative differences were found: Polylysine stimulated autophosphorylation and exogenous substrate phosphorylation activities of both insulin receptor TPK and IGF-I receptor TPK similarly.	Polylysine	132-142	insulin receptor	Homo sapiens	233-249
1661148-10	1991	In contrast, another polycation, polyarginine, affected both TPKs in a manner quite different from polylysine: Polyarginine stimulated insulin receptor autophosphorylation to a greater extent than polylysine did while it had a very small effect on the IGF-I receptor autophosphorylation as well as the exogenous substrate phosphorylation activities of the two receptor TPKs.	polyarginine	33-45	insulin receptor	Homo sapiens	135-151
1661148-10	1991	In contrast, another polycation, polyarginine, affected both TPKs in a manner quite different from polylysine: Polyarginine stimulated insulin receptor autophosphorylation to a greater extent than polylysine did while it had a very small effect on the IGF-I receptor autophosphorylation as well as the exogenous substrate phosphorylation activities of the two receptor TPKs.	polyarginine	111-123	insulin receptor	Homo sapiens	135-151
1722393-1	1991	Insulin causes a dramatic and rapid increase in phosphatidylinositol 3-kinase activity in the anti-phosphotyrosine immunoprecipitates of cells overexpressing the human insulin receptor.	Phosphotyrosine	99-114	insulin receptor	Homo sapiens	168-184
1722393-12	1991	We report here evidence that the 85 kDa subunit of highly purified phosphatidylinositol 3-kinase is phosphorylated on the tyrosine residue by the activated normal insulin receptor in vitro, but not by a mutant insulin receptor which lacks tyrosine kinase activity.	Tyrosine	122-130	insulin receptor	Homo sapiens	163-179
1744103-0	1991	Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembranous domain of the insulin receptor are required for normal endocytosis.	gly-pro-leu-tyr	21-36	insulin receptor	Homo sapiens	92-108
1744103-0	1991	Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the submembranous domain of the insulin receptor are required for normal endocytosis.	asn-pro-glu-tyr	41-56	insulin receptor	Homo sapiens	92-108
1838051-5	1991	In vitro studies of phenytoin in a primary culture system of adipocytes that allowed assessment of both insulin receptor binding and post-binding function showed a 57% reduction in maximum [14C]3-0-methylglucose transport in the presence of phenytoin while having no effect on maximum insulin binding.	Phenytoin	20-29	insulin receptor	Homo sapiens	104-120
1663881-1	1991	The insulin receptor is a heterotetrameric structure consisting of two alpha-subunits of Mr 135 kilodalton on the outside of the plasma membrane connected by disulphide bonds to beta-subunits of Mr 95 kilodalton which are transmembrane proteins.	disulphide	158-168	insulin receptor	Homo sapiens	4-20
1658624-4	1991	The expression of the uncleaved Met protein is due to defective posttranslational processing, since in this cell line (i) the proteolytic cleavage site Lys-303-Arg-Lys-Lys-Arg-Ser-308 is present in the precursor, (ii) p190NC is sensitive to mild trypsin digestion of the cell surface, generating alpha and beta chains of the correct size, and (iii) the 205-kDa insulin receptor precursor is not cleaved as well.	Lysine	164-167	insulin receptor	Homo sapiens	361-377
1658624-4	1991	The expression of the uncleaved Met protein is due to defective posttranslational processing, since in this cell line (i) the proteolytic cleavage site Lys-303-Arg-Lys-Lys-Arg-Ser-308 is present in the precursor, (ii) p190NC is sensitive to mild trypsin digestion of the cell surface, generating alpha and beta chains of the correct size, and (iii) the 205-kDa insulin receptor precursor is not cleaved as well.	Lysine	164-167	insulin receptor	Homo sapiens	361-377
1309253-1	1992	The human insulinlike growth factor 1 (hIGF-1) receptor (hIGFR) is a transmembrane protein tyrosine kinase (PTK) molecule which shares high sequence homology in the PTK domain with the insulin receptor and, to a lesser degree, the ros transforming protein of avian sarcoma virus UR2.	ros	93-96	insulin receptor	Homo sapiens	185-201
1939203-0	1991	Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor.	Threonine	30-39	insulin receptor	Homo sapiens	69-85
1657981-2	1991	TPA increased total phosphorylation of the wild-type insulin receptor and inhibited insulin-stimulated autophosphorylation by 32 +/- 10% in HIRc cells.	Tetradecanoylphorbol Acetate	0-3	insulin receptor	Homo sapiens	53-69
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Tetradecanoylphorbol Acetate	18-21	insulin receptor	Homo sapiens	44-60
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Tetradecanoylphorbol Acetate	18-21	insulin receptor	Homo sapiens	228-244
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Tyrosine	61-69	insulin receptor	Homo sapiens	44-60
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Tetradecanoylphorbol Acetate	280-283	insulin receptor	Homo sapiens	44-60
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Serine	436-442	insulin receptor	Homo sapiens	44-60
1657981-6	1991	In conclusion, 1) TPA-induced inhibition of insulin receptor tyrosine autophosphorylation was linked to concomitant inhibition of the biological effects of insulin in cells expressing either wild-type or COOH-terminal truncated insulin receptors; and 2) the inhibitory effects of TPA were not dependent upon phosphorylation of COOH-terminal residues and furthermore appeared to be independent of phosphorylation of any insulin receptor serine/threonine residues.	Threonine	443-452	insulin receptor	Homo sapiens	44-60
1939160-1	1991	Insulin treatment of fibroblasts overexpressing the insulin receptor causes a rapid accumulation of the GTP-bound form of p21ras.	Guanosine Triphosphate	104-107	insulin receptor	Homo sapiens	52-68
1898412-0	1991	Transmembrane signalling by insulin via an insulin receptor mutated at tyrosines 1158, 1162, and 1163.	Tyrosine	71-80	insulin receptor	Homo sapiens	43-59
1898412-1	1991	In order to study the role of tyrosine autophosphorylation in insulin receptor signalling, we investigated a mutant human insulin receptor whereby the three major tyrosine autophosphorylation sites at positions 1158, 1162, and 1163 in the receptor beta-subunit were mutated to phenylalanines.	Tyrosine	163-171	insulin receptor	Homo sapiens	122-138
1894624-0	1991	Polylysine increases the number of insulin binding sites in soluble insulin receptor preparations.	Polylysine	0-10	insulin receptor	Homo sapiens	68-84
1717334-4	1991	3) A phosphotyrosine-containing protein of 38 kDa, pI 7.0-7.2, reacted by both immunoblotting and immunoprecipitation with antiserum to P2, a peptide from the human insulin receptor that contains an autophosphorylated tyrosine residue.	Phosphotyrosine	5-20	insulin receptor	Homo sapiens	165-181
1658004-1	1991	We have examined the role of autophosphorylation in insulin signal transmission by oligonucleotide directed mutagenesis of seven potential tyrosine autophosphorylation sites in the human insulin receptor.	Oligonucleotides	83-98	insulin receptor	Homo sapiens	187-203
1658004-1	1991	We have examined the role of autophosphorylation in insulin signal transmission by oligonucleotide directed mutagenesis of seven potential tyrosine autophosphorylation sites in the human insulin receptor.	Tyrosine	139-147	insulin receptor	Homo sapiens	187-203
1652474-2	1991	PMA stimulated the phosphorylation of 5 distinct insulin receptor phosphopeptides: a single major phosphothreonine peptide containing Thr-1348, one major and 3 minor phosphoserine peptides.	phosphothreonine peptide	98-122	insulin receptor	Homo sapiens	49-65
1652474-2	1991	PMA stimulated the phosphorylation of 5 distinct insulin receptor phosphopeptides: a single major phosphothreonine peptide containing Thr-1348, one major and 3 minor phosphoserine peptides.	Threonine	134-137	insulin receptor	Homo sapiens	49-65
1652474-2	1991	PMA stimulated the phosphorylation of 5 distinct insulin receptor phosphopeptides: a single major phosphothreonine peptide containing Thr-1348, one major and 3 minor phosphoserine peptides.	phosphoserine peptides	166-188	insulin receptor	Homo sapiens	49-65
1717334-4	1991	3) A phosphotyrosine-containing protein of 38 kDa, pI 7.0-7.2, reacted by both immunoblotting and immunoprecipitation with antiserum to P2, a peptide from the human insulin receptor that contains an autophosphorylated tyrosine residue.	Tyrosine	12-20	insulin receptor	Homo sapiens	165-181
1651108-2	1991	This lysosphingolipid has been shown previously to inhibit the Ca2+/lipid-dependent protein kinase C. Here we show that insulin-dependent autophosphorylation of partially purified insulin receptor is half-maximally inhibited by 145 microM sphingosine (9 mol %) in Triton X-100 micelles.	Sphingolipids	5-21	insulin receptor	Homo sapiens	180-196
1651108-2	1991	This lysosphingolipid has been shown previously to inhibit the Ca2+/lipid-dependent protein kinase C. Here we show that insulin-dependent autophosphorylation of partially purified insulin receptor is half-maximally inhibited by 145 microM sphingosine (9 mol %) in Triton X-100 micelles.	Sphingosine	239-250	insulin receptor	Homo sapiens	180-196
1651108-2	1991	This lysosphingolipid has been shown previously to inhibit the Ca2+/lipid-dependent protein kinase C. Here we show that insulin-dependent autophosphorylation of partially purified insulin receptor is half-maximally inhibited by 145 microM sphingosine (9 mol %) in Triton X-100 micelles.	Octoxynol	264-276	insulin receptor	Homo sapiens	180-196
1651108-5	1991	Similar to the effects observed for protein kinase C, inhibition of the insulin receptor kinase by sphingosine is reduced in the presence of other lipids.	Sphingosine	99-110	insulin receptor	Homo sapiens	72-88
1651108-7	1991	The inhibition occurs at the level of the protein/membrane interaction: a soluble form of the insulin receptor comprising the cytoplasmic kinase domain is resistant to sphingosine inhibition.	Sphingosine	168-179	insulin receptor	Homo sapiens	94-110
1651108-8	1991	Lastly, sphingosine inhibits the insulin-stimulated rate of tyrosine phosphorylation of the insulin receptor in NIH 3T3 cells expressing the human insulin receptor.	Sphingosine	8-19	insulin receptor	Homo sapiens	147-163
1651108-8	1991	Lastly, sphingosine inhibits the insulin-stimulated rate of tyrosine phosphorylation of the insulin receptor in NIH 3T3 cells expressing the human insulin receptor.	Tyrosine	60-68	insulin receptor	Homo sapiens	147-163
2028355-4	1991	Receptor-mediated insulin resistance may be a consequence of various factors including increased serine/threonine phosphorylation of the receptor with decreased tyrosine phosphorylation, receptor desensitization, auto-antibodies to the receptor and inherited structural defects in the insulin receptor.	Serine	97-103	insulin receptor	Homo sapiens	285-301
1715686-1	1991	The identity of protein-tyrosine-phosphatases (PTPases) active against autophosphorylated insulin receptor was probed by using an insulin-receptor-related peptide phosphorylated on tyrosine (peptide 1142-1153).	Tyrosine	24-32	insulin receptor	Homo sapiens	90-106
1715686-1	1991	The identity of protein-tyrosine-phosphatases (PTPases) active against autophosphorylated insulin receptor was probed by using an insulin-receptor-related peptide phosphorylated on tyrosine (peptide 1142-1153).	Tyrosine	24-32	insulin receptor	Homo sapiens	130-146
1715686-1	1991	The identity of protein-tyrosine-phosphatases (PTPases) active against autophosphorylated insulin receptor was probed by using an insulin-receptor-related peptide phosphorylated on tyrosine (peptide 1142-1153).	Peptides	155-162	insulin receptor	Homo sapiens	90-106
1715686-1	1991	The identity of protein-tyrosine-phosphatases (PTPases) active against autophosphorylated insulin receptor was probed by using an insulin-receptor-related peptide phosphorylated on tyrosine (peptide 1142-1153).	Peptides	155-162	insulin receptor	Homo sapiens	130-146
1715686-6	1991	The tyrosine-1150 domain of the insulin receptor in triply phosphorylated form was found to be highly sensitive to the action of both PTPases, and was dephosphorylated at least 4 times faster than the doubly and singly phosphorylated forms of the tyrosine-1150 domain or phosphorylation sites in other domains by either PTPase.	Tyrosine	4-12	insulin receptor	Homo sapiens	32-48
1715686-6	1991	The tyrosine-1150 domain of the insulin receptor in triply phosphorylated form was found to be highly sensitive to the action of both PTPases, and was dephosphorylated at least 4 times faster than the doubly and singly phosphorylated forms of the tyrosine-1150 domain or phosphorylation sites in other domains by either PTPase.	Tyrosine	247-255	insulin receptor	Homo sapiens	32-48
1769008-0	1991	Effect of insulin receptor down regulation on insulin-stimulated thymidine incorporation in cultured human fibroblasts and tumor cell lines.	Thymidine	65-74	insulin receptor	Homo sapiens	10-26
1648089-11	1991	Inhibition of insulin receptor kinase activity by unbound fatty acids suggests that the end products of the lipogenic pathway may feedback inhibit the tyrosyl kinase and that fatty acid-binding proteins have the potential to modulate such interaction.	Fatty Acids	58-69	insulin receptor	Homo sapiens	14-30
1648089-11	1991	Inhibition of insulin receptor kinase activity by unbound fatty acids suggests that the end products of the lipogenic pathway may feedback inhibit the tyrosyl kinase and that fatty acid-binding proteins have the potential to modulate such interaction.	Fatty Acids	58-68	insulin receptor	Homo sapiens	14-30
1653112-0	1991	High levels of cytosolic free calcium inhibit dephosphorylation of insulin receptor and glycogen synthase.	Calcium	30-37	insulin receptor	Homo sapiens	67-83
1656240-1	1991	CHO/IRF960/T962 cells express a mutant human insulin receptor in which Tyr960 and Ser962 in the juxtamembrane region of the receptor"s beta-subunit are replaced by Phe and Thr, respectively.	Phenylalanine	164-167	insulin receptor	Homo sapiens	45-61
1656240-1	1991	CHO/IRF960/T962 cells express a mutant human insulin receptor in which Tyr960 and Ser962 in the juxtamembrane region of the receptor"s beta-subunit are replaced by Phe and Thr, respectively.	Threonine	172-175	insulin receptor	Homo sapiens	45-61
1860561-0	1991	Inducement of antibody that mimics insulin action on insulin receptor by insulin autoantibody directed at determinant at asparagine site on human insulin B chain.	Asparagine	121-131	insulin receptor	Homo sapiens	53-69
1860561-8	1991	These findings indicate that the conformation of TH-IAA idiotope is a mirror image of the determinant on the insulin B chain, the binding site for TH-IAA on anti-TH is also related to the insulin binding site on the insulin receptor, and anti-TH mimics insulin action on the insulin receptor.	th-iaa	49-55	insulin receptor	Homo sapiens	216-232
1680759-1	1991	In searching for a genetic marker of type 2 diabetes we estimated the frequency of alleles of the Bgl II restriction fragment length polymorphism (RFLP) of the insulin receptor gene in a group of type II diabetic patients (n = 50), characterized by OGTT (glucose, insulin, C-peptide) and insulin receptor binding parameters.	Glucose	255-262	insulin receptor	Homo sapiens	160-176
1680759-3	1991	Insulin receptor numbers and receptor affinity were estimated by 125I-(Tyr-A-14)- insulin binding to red blood cells.	Tyrosine	71-74	insulin receptor	Homo sapiens	0-16
1910463-9	1991	If this is the case, [B21 D-Glu]insulin may exhibit a stabilized geometry similar to that of natural insulin when bound to the insulin receptor.	Glutamic Acid	28-31	insulin receptor	Homo sapiens	127-143
1645524-6	1991	Furthermore, binding of GTP to these plasma membranes inhibited both the binding of 125I-insulin to the insulin receptor and the stimulation of the insulin receptor kinase, suggesting a feedback interaction between the insulin-stimulated GTP-binding site and the insulin receptor.	Guanosine Triphosphate	24-27	insulin receptor	Homo sapiens	104-120
1645524-6	1991	Furthermore, binding of GTP to these plasma membranes inhibited both the binding of 125I-insulin to the insulin receptor and the stimulation of the insulin receptor kinase, suggesting a feedback interaction between the insulin-stimulated GTP-binding site and the insulin receptor.	Guanosine Triphosphate	238-241	insulin receptor	Homo sapiens	104-120
1645524-9	1991	In conclusion, in plasma membranes of fat cells and skeletal muscle, the insulin receptor interacts with a 40 kDa GTP-binding site.	Guanosine Triphosphate	114-117	insulin receptor	Homo sapiens	73-89
2028355-4	1991	Receptor-mediated insulin resistance may be a consequence of various factors including increased serine/threonine phosphorylation of the receptor with decreased tyrosine phosphorylation, receptor desensitization, auto-antibodies to the receptor and inherited structural defects in the insulin receptor.	Threonine	104-113	insulin receptor	Homo sapiens	285-301
2019259-8	1991	Insulin receptor down-regulation (18%) was observed after 24 h (but not 5 h) in insulin-treated cells; however, the major portion of the decrease in insulin sensitivity was due to uncoupling of occupied insulin receptors from stimulation of the glucose transport system.	Glucose	245-252	insulin receptor	Homo sapiens	0-16
2039503-0	1991	Quantitation of the class I disulfides of the insulin receptor.	Disulfides	28-38	insulin receptor	Homo sapiens	46-62
2039503-1	1991	The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues.	Disulfides	4-13	insulin receptor	Homo sapiens	31-47
2039503-1	1991	The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues.	Dithiothreitol	65-79	insulin receptor	Homo sapiens	31-47
2039503-1	1991	The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues.	[3h]-n-ethylmaleimide	84-105	insulin receptor	Homo sapiens	31-47
2039503-1	1991	The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues.	Cysteine	164-172	insulin receptor	Homo sapiens	31-47
2022184-3	1991	In cells expressing elevated levels of insulin receptor, this process involves a rapid increase in p21rasGTP levels (from 20% to 70% GTP as a percentage of total guanine nucleotides).	p21rasgtp	99-108	insulin receptor	Homo sapiens	39-55
2022184-3	1991	In cells expressing elevated levels of insulin receptor, this process involves a rapid increase in p21rasGTP levels (from 20% to 70% GTP as a percentage of total guanine nucleotides).	Guanosine Triphosphate	105-108	insulin receptor	Homo sapiens	39-55
2022184-3	1991	In cells expressing elevated levels of insulin receptor, this process involves a rapid increase in p21rasGTP levels (from 20% to 70% GTP as a percentage of total guanine nucleotides).	Guanine Nucleotides	162-181	insulin receptor	Homo sapiens	39-55
1676686-0	1991	Screening for insulin receptor gene DNA polymorphisms associated with glucose intolerance in a Scandinavian population.	Glucose	70-77	insulin receptor	Homo sapiens	14-30
2022311-2	1991	This review addresses the processes involved in the synthetic assembly of the insulin receptor; the interaction of insulin with the receptor protein; the receptor-mediated endocytosis of insulin; and the role of receptor tyrosine and serine phosphorylation in both endocytosis and recycling.	Tyrosine	221-229	insulin receptor	Homo sapiens	78-94
2022311-2	1991	This review addresses the processes involved in the synthetic assembly of the insulin receptor; the interaction of insulin with the receptor protein; the receptor-mediated endocytosis of insulin; and the role of receptor tyrosine and serine phosphorylation in both endocytosis and recycling.	Serine	234-240	insulin receptor	Homo sapiens	78-94
1848075-6	1991	(3) Replacement of tyrosine-1162 with phenylalanine blocked insulin-stimulated threonine phosphorylation of the insulin receptor in intact cells.	Threonine	79-88	insulin receptor	Homo sapiens	112-128
1999434-1	1991	Possible association of ganglioside-induced inhibition of insulin receptor function and monocytic differentiation induction in HL-60 cells.	Gangliosides	24-35	insulin receptor	Homo sapiens	58-74
1716863-1	1991	An assay which permitted a comparison of insulin receptor tyrosine phosphorylation induced under in vivo and in situ conditions was developed.	Tyrosine	58-66	insulin receptor	Homo sapiens	41-57
1716863-3	1991	In addition, chronically treated, down-regulated cells demonstrated a significant decrease in the level of insulin receptor tyrosine phosphorylation compared to cells acutely treated with insulin.	Tyrosine	124-132	insulin receptor	Homo sapiens	107-123
1716863-4	1991	The procedure utilized an antibody specific for the insulin receptor which allowed separation of the receptor from other cellular proteins which are potential substrates for tyrosine phosphorylation.	Tyrosine	174-182	insulin receptor	Homo sapiens	52-68
1848075-0	1991	Changes in insulin-receptor tyrosine, serine and threonine phosphorylation as a result of substitution of tyrosine-1162 with phenylalanine.	Tyrosine	28-36	insulin receptor	Homo sapiens	11-27
1848075-0	1991	Changes in insulin-receptor tyrosine, serine and threonine phosphorylation as a result of substitution of tyrosine-1162 with phenylalanine.	Threonine	49-58	insulin receptor	Homo sapiens	11-27
1848075-1	1991	Previous studies, by ourselves and others, have shown that tyrosine residues 1158, 1162 and 1163 are very rapidly autophosphorylated on the human insulin receptor after insulin binding and that this is followed by the autophosphorylation of tyrosine residues 1328 and 1334.	Tyrosine	59-67	insulin receptor	Homo sapiens	146-162
1848075-1	1991	Previous studies, by ourselves and others, have shown that tyrosine residues 1158, 1162 and 1163 are very rapidly autophosphorylated on the human insulin receptor after insulin binding and that this is followed by the autophosphorylation of tyrosine residues 1328 and 1334.	Tyrosine	241-249	insulin receptor	Homo sapiens	146-162
1847054-0	1991	Phosphorylation of tyrosines 1158, 1162 and 1163 on a synthetic dodecapeptide by the insulin receptor protein-tyrosine kinase.	Tyrosine	19-28	insulin receptor	Homo sapiens	85-101
1847054-1	1991	To investigate the mechanism of tyrosine phosphorylation by the insulin receptor protein-tyrosine kinase, we utilized a synthetic dodecapeptide substrate (RRDIYETDYYRK; amino acids 1155-1165) containing the three major insulin receptor autophosphorylation sites.	Tyrosine	32-40	insulin receptor	Homo sapiens	64-80
1847054-1	1991	To investigate the mechanism of tyrosine phosphorylation by the insulin receptor protein-tyrosine kinase, we utilized a synthetic dodecapeptide substrate (RRDIYETDYYRK; amino acids 1155-1165) containing the three major insulin receptor autophosphorylation sites.	Tyrosine	32-40	insulin receptor	Homo sapiens	219-235
1846000-0	1991	The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain.	Tyrosine	29-37	insulin receptor	Homo sapiens	71-87
1845969-0	1991	Expression of inducible membrane-anchored insulin receptor kinase enhances deoxyglucose uptake.	Deoxyglucose	75-87	insulin receptor	Homo sapiens	42-58
1845969-4	1991	Transfected cells which are exposed to dexamethasone express two proteins of approximate Mr = 54,000 which (a) react with anti-peptide antisera raised to human insulin receptor sequences, (b) localize to the membrane fraction, and (c) possess ligand (insulin)-independent tyrosine kinase activity.	Dexamethasone	39-52	insulin receptor	Homo sapiens	160-176
1845969-5	1991	In extracts of steroid-treated MARK cells, a phosphotyrosine-containing protein of Mr = 185,000 is detected, which corresponds in size to a known endogenous substrate for the insulin receptor.	Steroids	15-22	insulin receptor	Homo sapiens	175-191
1845969-10	1991	These studies demonstrate that a membrane-anchored insulin receptor kinase, devoid of virtually the entire extracellular domain of the insulin receptor, is sufficient to induce enhanced deoxyglucose uptake.	Deoxyglucose	186-198	insulin receptor	Homo sapiens	51-67
1845969-10	1991	These studies demonstrate that a membrane-anchored insulin receptor kinase, devoid of virtually the entire extracellular domain of the insulin receptor, is sufficient to induce enhanced deoxyglucose uptake.	Deoxyglucose	186-198	insulin receptor	Homo sapiens	135-151
2039477-4	1991	14-fold less potent than pig insulin in inhibiting the binding of [125I-Tyr-A14](human insulin) to transfected mouse NIH 3T3 cells expressing the human insulin receptor.	Tyrosine	72-75	insulin receptor	Homo sapiens	152-168
2039477-4	1991	14-fold less potent than pig insulin in inhibiting the binding of [125I-Tyr-A14](human insulin) to transfected mouse NIH 3T3 cells expressing the human insulin receptor.	(1s,4s,5s,7r)-7-{[(5s)-5-Amino-5-Carboxypentanoyl]amino}-3,3-Dimethyl-6-Oxo-2-Thiabicyclo[3.2.0]heptane-4-Carboxylic Acid	76-79	insulin receptor	Homo sapiens	152-168
1991570-1	1991	The insulin receptor, an integral membrane glycoprotein, is synthesized as a single-chain precursor that is cleaved to produce two mature subunits, both of which contain N-linked oligosaccharide chains and covalently linked fatty acids.	n-linked oligosaccharide	170-194	insulin receptor	Homo sapiens	4-20
1991570-1	1991	The insulin receptor, an integral membrane glycoprotein, is synthesized as a single-chain precursor that is cleaved to produce two mature subunits, both of which contain N-linked oligosaccharide chains and covalently linked fatty acids.	Fatty Acids	224-235	insulin receptor	Homo sapiens	4-20
1991570-10	1991	Therefore, the insulin receptor contains O-linked oligosaccharides on the NH2-terminal tryptic peptide of the beta-subunit, and these O-linked oligosaccharides are not necessary to the binding or autophosphorylation function of the receptor.	o-linked oligosaccharides	41-66	insulin receptor	Homo sapiens	15-31
1991570-10	1991	Therefore, the insulin receptor contains O-linked oligosaccharides on the NH2-terminal tryptic peptide of the beta-subunit, and these O-linked oligosaccharides are not necessary to the binding or autophosphorylation function of the receptor.	Peptides	95-102	insulin receptor	Homo sapiens	15-31
1991570-10	1991	Therefore, the insulin receptor contains O-linked oligosaccharides on the NH2-terminal tryptic peptide of the beta-subunit, and these O-linked oligosaccharides are not necessary to the binding or autophosphorylation function of the receptor.	o-linked oligosaccharides	134-159	insulin receptor	Homo sapiens	15-31
1993068-0	1991	Mapping of carbohydrate sites on the human insulin receptor.	Carbohydrates	11-23	insulin receptor	Homo sapiens	43-59
1993068-7	1991	Using this technique we have shown the insulin receptor to be glycosylated at Asn 397 and Asn 881.	Asparagine	78-81	insulin receptor	Homo sapiens	39-55
1993068-7	1991	Using this technique we have shown the insulin receptor to be glycosylated at Asn 397 and Asn 881.	Asparagine	90-93	insulin receptor	Homo sapiens	39-55
1716452-7	1991	We conclude from these studies that (a) insulin inhibition of glycerol release can not be mediated directly by intracellular cAMP modulation, (b) as in the case of hexose transport activation, the signalling mechanism by the occupied insulin receptor appears to be relatively independent of the membrane lipid environment.	Glycerol	62-70	insulin receptor	Homo sapiens	234-250
1716452-7	1991	We conclude from these studies that (a) insulin inhibition of glycerol release can not be mediated directly by intracellular cAMP modulation, (b) as in the case of hexose transport activation, the signalling mechanism by the occupied insulin receptor appears to be relatively independent of the membrane lipid environment.	Hexoses	164-170	insulin receptor	Homo sapiens	234-250
1849849-0	1991	Effects of media conditions, insulin, and dexamethasone on insulin-receptor mRNA and promoter activity in HepG2 cells.	Dexamethasone	42-55	insulin receptor	Homo sapiens	59-75
1786203-1	1991	Insulin receptor mutation studies indicate that the receptor tyrosine kinase activity is necessary for receptor endocytosis, and several insulin receptor-containing tissues have a plasma membrane-associated protein (Mr congruent to 180,000, p180) whose tyrosine phosphorylation is receptor catalysed.	Tyrosine	61-69	insulin receptor	Homo sapiens	0-16
1786203-10	1991	Addition of glycerol gradient fractions to a prephosphorylated insulin receptor preparation, however, gave a tyrosine-phosphorylated 180,000 molecular weight protein when cytoplasmic and coated vesicle fractions were added.	Glycerol	12-20	insulin receptor	Homo sapiens	63-79
1786203-10	1991	Addition of glycerol gradient fractions to a prephosphorylated insulin receptor preparation, however, gave a tyrosine-phosphorylated 180,000 molecular weight protein when cytoplasmic and coated vesicle fractions were added.	Tyrosine	109-117	insulin receptor	Homo sapiens	63-79
1849849-8	1991	The effect of conditioned media, insulin, and dexamethasone on insulin-receptor promoter activity was also examined.	Dexamethasone	46-59	insulin receptor	Homo sapiens	63-79
1905936-5	1991	The predominant abnormality in brain glucose utilization in incipient late-onset DAT may be associated with an impairment of its control mechanism(s), which are assumed to be either an influence of brain insulin action, or brain insulin receptor function, or both.	Glucose	37-44	insulin receptor	Homo sapiens	229-245
1920277-0	1991	Insulin receptor sub-types in a human lymphoid-derived cell line (IM-9): differential regulation by insulin, dexamethasone and monensin.	Dexamethasone	109-122	insulin receptor	Homo sapiens	0-16
1719349-0	1991	Preparation and use of anti-phosphotyrosine antibodies to study structure and function of insulin receptor.	Phosphotyrosine	28-43	insulin receptor	Homo sapiens	90-106
2253226-8	1990	In order to study the functional significance of the increased insulin receptor levels, we incubated T47D cells with progesterone and then treated them with insulin.	Progesterone	117-129	insulin receptor	Homo sapiens	63-79
1843205-5	1991	When measured at 15 degrees C, insulin receptor number rose from 9000 to 22,000 per cell with increased fatty acid unsaturation.	Fatty Acids	104-114	insulin receptor	Homo sapiens	31-47
2124484-1	1990	A novel GTP-binding protein, GIR, along with insulin receptor (IR), has been partially purified from human placenta.	Guanosine Triphosphate	8-11	insulin receptor	Homo sapiens	30-32
2123490-0	1990	Mutagenesis of lysine 460 in the human insulin receptor.	Lysine	15-21	insulin receptor	Homo sapiens	39-55
2250023-0	1990	Insulin receptor tyrosine residues 1162 and 1163 control insulin stimulation of myristoyl-diacylglycerol generation and subsequent activation of glucose transport.	Tyrosine	17-25	insulin receptor	Homo sapiens	0-16
2250023-0	1990	Insulin receptor tyrosine residues 1162 and 1163 control insulin stimulation of myristoyl-diacylglycerol generation and subsequent activation of glucose transport.	myristoyl-diacylglycerol	80-104	insulin receptor	Homo sapiens	0-16
2250023-0	1990	Insulin receptor tyrosine residues 1162 and 1163 control insulin stimulation of myristoyl-diacylglycerol generation and subsequent activation of glucose transport.	Glucose	145-152	insulin receptor	Homo sapiens	0-16
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Arginine	93-96	insulin receptor	Homo sapiens	3-19
2229049-0	1990	Glucose regulation of insulin receptor affinity in primary cultured adipocytes.	Glucose	0-7	insulin receptor	Homo sapiens	22-38
2229049-1	1990	Treatment of primary cultured adipocytes with 20 mM glucose resulted in a progressive increase in specific 125I-insulin binding that began almost immediately (no lag period) and culminated in a 60% increase by 24 h. This effect was dose-dependent (glucose ED50 of 4.6 mM) and mediated by an increase in insulin receptor affinity.	Glucose	52-59	insulin receptor	Homo sapiens	303-319
2229049-1	1990	Treatment of primary cultured adipocytes with 20 mM glucose resulted in a progressive increase in specific 125I-insulin binding that began almost immediately (no lag period) and culminated in a 60% increase by 24 h. This effect was dose-dependent (glucose ED50 of 4.6 mM) and mediated by an increase in insulin receptor affinity.	Glucose	248-255	insulin receptor	Homo sapiens	303-319
2229049-2	1990	Moreover, it appears that glucose modulates insulin receptor affinity through de novo protein synthesis rather than through covalent modification of receptors, since cycloheximide selectively inhibited the glucose-induced increase in insulin binding capacity (ED50 of 360 ng/ml) and restored receptor affinity to control values.	Glucose	26-33	insulin receptor	Homo sapiens	44-60
2229049-2	1990	Moreover, it appears that glucose modulates insulin receptor affinity through de novo protein synthesis rather than through covalent modification of receptors, since cycloheximide selectively inhibited the glucose-induced increase in insulin binding capacity (ED50 of 360 ng/ml) and restored receptor affinity to control values.	Cycloheximide	166-179	insulin receptor	Homo sapiens	44-60
2229049-2	1990	Moreover, it appears that glucose modulates insulin receptor affinity through de novo protein synthesis rather than through covalent modification of receptors, since cycloheximide selectively inhibited the glucose-induced increase in insulin binding capacity (ED50 of 360 ng/ml) and restored receptor affinity to control values.	Glucose	206-213	insulin receptor	Homo sapiens	44-60
2229049-5	1990	On the basis of these studies, we conclude that 1) insulin binding is subject to dual regulation (glucose controls insulin action by enhancing receptor affinity, whereas insulin controls the number of cell surface receptors); and 2) glucose appears to modulate insulin receptor affinity through the rapid biosynthesis of an affinity regulatory protein.	Glucose	233-240	insulin receptor	Homo sapiens	261-277
2211730-0	1990	Substructural analysis of the insulin receptor by microsequence analyses of limited tryptic fragments isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence or presence of dithiothreitol.	Sodium Dodecyl Sulfate	114-136	insulin receptor	Homo sapiens	30-46
2211730-0	1990	Substructural analysis of the insulin receptor by microsequence analyses of limited tryptic fragments isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence or presence of dithiothreitol.	polyacrylamide	137-151	insulin receptor	Homo sapiens	30-46
2211730-1	1990	Human placental insulin receptor contains 47 Cys per an alpha beta dimer.	Cysteine	45-48	insulin receptor	Homo sapiens	16-32
2211730-3	1990	In order to gain more insight into the three-dimensional organization of the insulin receptor, we have used limited trypsin digestion, SDS-PAGE, and protein microsequencing.	Sodium Dodecyl Sulfate	135-138	insulin receptor	Homo sapiens	77-93
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Dexamethasone	106-119	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Glucose	185-192	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Glucose	185-192	insulin receptor	Homo sapiens	123-139
1697749-6	1990	When the phosphorylation of both receptors was examined individually by using specific monoclonal antibodies to immunoprecipitate the receptors, phosphorylation of the insulin receptor was found to increase on both serine and tyrosine residues in cells treated with 100 ng of IGF-I/ml.	Serine	215-221	insulin receptor	Homo sapiens	168-184
1697749-6	1990	When the phosphorylation of both receptors was examined individually by using specific monoclonal antibodies to immunoprecipitate the receptors, phosphorylation of the insulin receptor was found to increase on both serine and tyrosine residues in cells treated with 100 ng of IGF-I/ml.	Tyrosine	226-234	insulin receptor	Homo sapiens	168-184
2164929-1	1990	We have recently described an insulin-resistant patient with leprechaunism (leprechaun G.) having a homozygous leucine----proline mutation at amino acid position 233 in the alpha-chain of the insulin receptor.	Proline	122-129	insulin receptor	Homo sapiens	192-208
2193799-11	1990	Thus, the insulin receptor contains several sites of serine/threonine phosphorylation, some of which are substrates for more than one protein kinase.	Serine	53-59	insulin receptor	Homo sapiens	10-26
2193799-11	1990	Thus, the insulin receptor contains several sites of serine/threonine phosphorylation, some of which are substrates for more than one protein kinase.	Threonine	60-69	insulin receptor	Homo sapiens	10-26
1694071-2	1990	In this work (i) we stably cultured three human cell lines in media containing different glucose concentrations (from 0 to 25 mM), (ii) we characterized glucose effects on insulin receptor gene expression, (iii) we investigated the mechanism by which glucose produces these effects.	Glucose	153-160	insulin receptor	Homo sapiens	172-188
1694071-2	1990	In this work (i) we stably cultured three human cell lines in media containing different glucose concentrations (from 0 to 25 mM), (ii) we characterized glucose effects on insulin receptor gene expression, (iii) we investigated the mechanism by which glucose produces these effects.	Glucose	153-160	insulin receptor	Homo sapiens	172-188
1694071-4	1990	Our data indicate that glucose affects insulin receptor gene expression in human cells and that protein glycosylation plays a role in this regulatory mechanism.	Glucose	23-30	insulin receptor	Homo sapiens	39-55
1694662-0	1990	Anti-(insulin receptor) monoclonal antibody-stimulated tyrosine phosphorylation in cells transfected with human insulin receptor cDNA.	Tyrosine	55-63	insulin receptor	Homo sapiens	6-22
1694662-0	1990	Anti-(insulin receptor) monoclonal antibody-stimulated tyrosine phosphorylation in cells transfected with human insulin receptor cDNA.	Tyrosine	55-63	insulin receptor	Homo sapiens	112-128
2373247-0	1990	Phorbol ester-induced downregulation of protein kinase C potentiates insulin receptor tyrosine autophosphorylation: evidence for a major constitutive role in insulin receptor regulation.	Phorbol Esters	0-13	insulin receptor	Homo sapiens	69-85
2373247-0	1990	Phorbol ester-induced downregulation of protein kinase C potentiates insulin receptor tyrosine autophosphorylation: evidence for a major constitutive role in insulin receptor regulation.	Phorbol Esters	0-13	insulin receptor	Homo sapiens	158-174
2373247-0	1990	Phorbol ester-induced downregulation of protein kinase C potentiates insulin receptor tyrosine autophosphorylation: evidence for a major constitutive role in insulin receptor regulation.	Tyrosine	86-94	insulin receptor	Homo sapiens	69-85
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Leucine	22-25	insulin receptor	Homo sapiens	152-168
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Phenylalanine	31-34	insulin receptor	Homo sapiens	152-168
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Serine	40-43	insulin receptor	Homo sapiens	152-168
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Phenylalanine	52-55	insulin receptor	Homo sapiens	152-168
2192846-4	1990	Replacing A3-Val with Leu, B24-Phe with Ser, or B25-Phe with Leu results in molecules that have essentially normal immunoreactivity but greatly reduced insulin-receptor-binding potency.	Leucine	61-64	insulin receptor	Homo sapiens	152-168
2159709-7	1990	By covalently labeling the insulin receptor with the photoactive insulin derivative, 125I-NAPA-DP-insulin, it was demonstrated that the rates of receptor degradation of down-regulated and control receptors were similar.	125i-napa-dp	85-97	insulin receptor	Homo sapiens	27-43
1703148-1	1991	The tyrosines phosphorylated are typical of those observed following phosphorylation of the heterotetrameric insulin receptor in intact cells.	Tyrosine	4-13	insulin receptor	Homo sapiens	109-125
1703148-4	1991	Two-dimensional thin layer phosphopeptide mapping reveals that the 48-kDa enzyme undergoes a rapid autophosphorylation on the same tyrosines (residues 1158, 1162, 1163, 1328, and 1334) that have previously been shown to be major autophosphorylation sites on the native insulin receptor beta-subunit in intact cells.	Tyrosine	131-140	insulin receptor	Homo sapiens	269-285
1703148-8	1991	Phosphorylation of these tyrosine residues occurs in a cascade manner analogous to that found in the intact insulin receptor beta-subunit.	Tyrosine	25-33	insulin receptor	Homo sapiens	108-124
2119296-0	1990	Insulin receptor carbohydrate units contain poly-N-acetyllactosamine chains.	poly-N-acetyllactosamine	44-68	insulin receptor	Homo sapiens	0-16
2119296-1	1990	The insulin receptor was immunoprecipitated from cultured human lymphocytes (IM-9) and rat hepatocytes (Fao) after biosynthetic labeling with [3H]glucosamine or [3H]mannose, and the nature of the carbohydrate units was investigated.	Tritium	143-145	insulin receptor	Homo sapiens	4-20
2119296-1	1990	The insulin receptor was immunoprecipitated from cultured human lymphocytes (IM-9) and rat hepatocytes (Fao) after biosynthetic labeling with [3H]glucosamine or [3H]mannose, and the nature of the carbohydrate units was investigated.	Glucosamine	146-157	insulin receptor	Homo sapiens	4-20
2119296-1	1990	The insulin receptor was immunoprecipitated from cultured human lymphocytes (IM-9) and rat hepatocytes (Fao) after biosynthetic labeling with [3H]glucosamine or [3H]mannose, and the nature of the carbohydrate units was investigated.	Tritium	162-164	insulin receptor	Homo sapiens	4-20
2119296-1	1990	The insulin receptor was immunoprecipitated from cultured human lymphocytes (IM-9) and rat hepatocytes (Fao) after biosynthetic labeling with [3H]glucosamine or [3H]mannose, and the nature of the carbohydrate units was investigated.	Mannose	165-172	insulin receptor	Homo sapiens	4-20
2119296-1	1990	The insulin receptor was immunoprecipitated from cultured human lymphocytes (IM-9) and rat hepatocytes (Fao) after biosynthetic labeling with [3H]glucosamine or [3H]mannose, and the nature of the carbohydrate units was investigated.	Carbohydrates	196-208	insulin receptor	Homo sapiens	4-20
2119296-3	1990	The susceptibility of the insulin receptor to this enzyme indicates that its carbohydrate units contain poly-N-acetyllactosamine sequences.	Carbohydrates	77-89	insulin receptor	Homo sapiens	26-42
2119296-3	1990	The susceptibility of the insulin receptor to this enzyme indicates that its carbohydrate units contain poly-N-acetyllactosamine sequences.	poly-N-acetyllactosamine	104-128	insulin receptor	Homo sapiens	26-42
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Colforsin	18-27	insulin receptor	Homo sapiens	36-52
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Colforsin	18-27	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Colforsin	18-27	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Colforsin	93-102	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Colforsin	93-102	insulin receptor	Homo sapiens	123-139
1697168-3	1990	We found that (i) forskolin reduces insulin receptor mRNA levels; (ii) the effects of either forskolin or dexamethasone on insulin receptor mRNA levels are near completely abolished in glucose-starved cells; (iii) 2-mercaptoethanol and heat shock, besides previously described stress conditions (glycosylatyon inhibitors), reduce insulin receptor mRNA levels.	Dexamethasone	106-119	insulin receptor	Homo sapiens	123-139
1696549-2	1990	The insulin stimulated tyrosine phosphorylation of the insulin receptor was not affected.	Tyrosine	23-31	insulin receptor	Homo sapiens	55-71
2200525-1	1990	Expression of the cDNA encoding a human insulin receptor with replacement of alanine for lysine at residue 1018 in the ATP binding domain of the beta subunit results in a receptor that is not only kinase-defective, but also biologically inactive.	Adenosine Triphosphate	119-122	insulin receptor	Homo sapiens	40-56
2077476-3	1990	In erythrocytes from 8 children with high reticulocyte count and 9 healthy age-matched subjects we studied insulin receptor binding in correlation with pyruvate kinase (PK) activity and creatine levels.	Creatine	186-194	insulin receptor	Homo sapiens	107-123
2077476-7	1990	Our results indicate that creatine content is the best marker of red cell age for insulin receptor studies.	Creatine	26-34	insulin receptor	Homo sapiens	82-98
2188977-0	1990	Replacement of the human insulin receptor transmembrane and cytoplasmic domains by corresponding domains of the oncogene product v-ros leads to accelerated internalization, degradation, and down-regulation.	ros	131-134	insulin receptor	Homo sapiens	25-41
2339989-1	1990	Concanavalin A (ConA) stimulated the phosphorylation of the beta-subunit of the insulin receptor and an Mr-185,000 protein on serine and tyrosine residues in intact H-35 rat hepatoma cells.	Serine	126-132	insulin receptor	Homo sapiens	80-96
2339989-1	1990	Concanavalin A (ConA) stimulated the phosphorylation of the beta-subunit of the insulin receptor and an Mr-185,000 protein on serine and tyrosine residues in intact H-35 rat hepatoma cells.	Tyrosine	137-145	insulin receptor	Homo sapiens	80-96
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Lysine	97-100	insulin receptor	Homo sapiens	3-19
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Arginine	101-104	insulin receptor	Homo sapiens	3-19
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Arginine	101-104	insulin receptor	Homo sapiens	3-19
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Amino Acids, Basic	109-125	insulin receptor	Homo sapiens	3-19
15539203-1	1990	The substitution of trans- for half of the cis-monounsaturated fatty acids in the diet of Macaca fasicularis monkeys resulted in alterations in erythrocyte fatty acid composition and insulin receptor properties but not in membrane fluidity.	cis-monounsaturated fatty acids	43-74	insulin receptor	Homo sapiens	183-199
2318937-5	1990	Polymorphisms in the nucleotide sequences for codons 523 (Ala), 1058 (His), and 1062 (Leu) provided useful markers to differentiate the patient"s two alleles of the insulin receptor gene.	Alanine	58-61	insulin receptor	Homo sapiens	165-181
2318937-5	1990	Polymorphisms in the nucleotide sequences for codons 523 (Ala), 1058 (His), and 1062 (Leu) provided useful markers to differentiate the patient"s two alleles of the insulin receptor gene.	Histidine	70-73	insulin receptor	Homo sapiens	165-181
2318937-5	1990	Polymorphisms in the nucleotide sequences for codons 523 (Ala), 1058 (His), and 1062 (Leu) provided useful markers to differentiate the patient"s two alleles of the insulin receptor gene.	Leucine	86-89	insulin receptor	Homo sapiens	165-181
15539203-6	1990	In the absence of an effect on overall membrane fluidity, altered receptor activity suggests that insulin receptor activity is dynamic, requiring specific fluid membrane subdomains or highly specific fatty acid-protein interactions.	Fatty Acids	200-210	insulin receptor	Homo sapiens	98-114
2156441-2	1990	In both species, IGF-II has been reported to stimulate glucose transport by interacting with the insulin receptor.	Glucose	55-62	insulin receptor	Homo sapiens	97-113
2157215-0	1990	Mn2(+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor.	mn2(+)	0-6	insulin receptor	Homo sapiens	90-106
2157215-10	1990	We conclude that Mn2+ ions, although they bind weakly, induce an activating conformational change in the secondary structure of the human insulin receptor cytoplasmic domain.	Manganese(2+)	17-21	insulin receptor	Homo sapiens	138-154
2155093-2	1990	The autophosphorylation of the insulin receptor on tyrosyl residues activates the intrinsic tyrosine kinase of the receptor, rendering its ligand independent.	cyclo(tyrosyl-tyrosyl)	51-58	insulin receptor	Homo sapiens	31-47
2110001-0	1990	Threonine 1336 of the human insulin receptor is a major target for phosphorylation by protein kinase C. The ability of tumor-promoting phorbol diesters to inhibit both insulin receptor tyrosine kinase activity and its intracellular signaling correlates with the phosphorylation of the insulin receptor beta subunit on serine and threonine residues.	Threonine	0-9	insulin receptor	Homo sapiens	28-44
2110001-0	1990	Threonine 1336 of the human insulin receptor is a major target for phosphorylation by protein kinase C. The ability of tumor-promoting phorbol diesters to inhibit both insulin receptor tyrosine kinase activity and its intracellular signaling correlates with the phosphorylation of the insulin receptor beta subunit on serine and threonine residues.	Phorbol Esters	135-151	insulin receptor	Homo sapiens	28-44
2153593-2	1990	In the present study, insulin treatment of Chinese hamster ovary cells overexpressing the human insulin receptor was found to stimulate the ability of their membrane extracts to phosphorylate poly (Glu, Tyr) 1:1.	poly (glu	192-201	insulin receptor	Homo sapiens	96-112
2110001-0	1990	Threonine 1336 of the human insulin receptor is a major target for phosphorylation by protein kinase C. The ability of tumor-promoting phorbol diesters to inhibit both insulin receptor tyrosine kinase activity and its intracellular signaling correlates with the phosphorylation of the insulin receptor beta subunit on serine and threonine residues.	Serine	318-324	insulin receptor	Homo sapiens	28-44
2110001-0	1990	Threonine 1336 of the human insulin receptor is a major target for phosphorylation by protein kinase C. The ability of tumor-promoting phorbol diesters to inhibit both insulin receptor tyrosine kinase activity and its intracellular signaling correlates with the phosphorylation of the insulin receptor beta subunit on serine and threonine residues.	Threonine	329-338	insulin receptor	Homo sapiens	28-44
2110001-5	1990	Partial hydrolysis and radiosequence analysis of the phosphopeptide derived from insulin receptor phosphorylated by protein kinase C indicated that the phosphorylation of this tryptic peptide occurred specifically on a threonine, three amino acids from the amino terminus of the tryptic fragment.	Threonine	219-228	insulin receptor	Homo sapiens	81-97
1689998-1	1990	Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain.	Tyrosine	75-84	insulin receptor	Homo sapiens	46-62
1689998-1	1990	Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain.	Tyrosine	103-112	insulin receptor	Homo sapiens	46-62
1689998-1	1990	Insulin stimulates autophosphorylation of the insulin receptor on multiple tyrosines in three domains: tyrosines 1316 and 1322 in the C-terminal tail, 1146, 1150 and 1151 in the tyrosine-1150 domain, and possibly 953, 960 or 972 in the juxtamembrane domain.	Tyrosine	75-83	insulin receptor	Homo sapiens	46-62
1689998-7	1990	Dephosphorylation of the diphosphorylated C-terminal domain yielded insulin receptor in which the domain was singly phosphorylated at tyrosine 1322.	Tyrosine	134-142	insulin receptor	Homo sapiens	68-84
1689998-8	1990	Triphosphorylation of the insulin receptor in the tyrosine-1150 domain appears important in activating the receptor tyrosine kinase to phosphorylate other proteins.	Tyrosine	50-58	insulin receptor	Homo sapiens	26-42
1689998-9	1990	The extreme sensitivity of the triphosphorylated form of the tyrosine-1150 domain to dephosphorylation may thus be important in terminating or regulating insulin-receptor tyrosine kinase action and insulin signalling.	Tyrosine	61-69	insulin receptor	Homo sapiens	154-170
2153593-2	1990	In the present study, insulin treatment of Chinese hamster ovary cells overexpressing the human insulin receptor was found to stimulate the ability of their membrane extracts to phosphorylate poly (Glu, Tyr) 1:1.	Tyrosine	203-207	insulin receptor	Homo sapiens	96-112
2153593-3	1990	It was concluded that this activity was due to the receptor itself because: 1) it was precipitated with a monoclonal antibody to the receptor; 2) the addition of various membrane extracts to purified insulin receptor preparations stimulated the ability of these preparations to phosphorylate poly (Glu, Tyr) 1:1; and 3) certain purified proteins, including bovine serum albumin and casein, were also capable of stimulating the purified receptor to phosphorylate poly (Glu, Tyr) 1:1.	poly (glu, tyr)	292-307	insulin receptor	Homo sapiens	200-216
2153593-3	1990	It was concluded that this activity was due to the receptor itself because: 1) it was precipitated with a monoclonal antibody to the receptor; 2) the addition of various membrane extracts to purified insulin receptor preparations stimulated the ability of these preparations to phosphorylate poly (Glu, Tyr) 1:1; and 3) certain purified proteins, including bovine serum albumin and casein, were also capable of stimulating the purified receptor to phosphorylate poly (Glu, Tyr) 1:1.	poly (glu, tyr)	462-477	insulin receptor	Homo sapiens	200-216
1688999-6	1990	In the presence of the coexpressed human insulin receptor, insulin induced a two- to threefold increase in hexose transport.	Hexoses	107-113	insulin receptor	Homo sapiens	41-57
1688999-9	1990	We conclude that the expressed human insulin receptor is able to couple efficiently with preexisting postreceptor regulatory pathways in oocytes and that the regulation of hexose transport in these cells can be mediated through the combined actions of the expressed human insulin receptor and the endogenous oocyte insulin-like growth factor I receptor.	Hexoses	172-178	insulin receptor	Homo sapiens	37-53
2404758-0	1990	Diacylglycerols modulate phosphorylation of the insulin receptor from human mononuclear cells.	Diglycerides	0-15	insulin receptor	Homo sapiens	48-64
2227134-3	1990	The time course of pp185 phosphorylation at 37 degrees C was rapid and corresponded closely to insulin-receptor autophosphorylation but preceded insulin-stimulated glucose transport.	pp185	19-24	insulin receptor	Homo sapiens	95-111
1688432-2	1990	Treatment of Chinese hamster ovary (CHO) cells overexpressing the human insulin receptor (CHO.T) with insulin results in a 38 +/- 11 (mean +/- S.E., n = 9)-fold increase in a phosphatidylinositol (PtdIns) kinase activity in anti-phosphotyrosine immunoprecipitates of whole cell lysates.	Phosphotyrosine	229-244	insulin receptor	Homo sapiens	72-88
2184349-0	1990	Mutation of tyrosine residues 1162 and 1163 of the insulin receptor affects hormone and receptor internalization.	Tyrosine	12-20	insulin receptor	Homo sapiens	51-67
2136851-0	1990	Insulin-sensitive phosphorylation of serine 1293/1294 on the human insulin receptor by a tightly associated serine kinase.	Serine	37-43	insulin receptor	Homo sapiens	67-83
2136851-2	1990	Analysis of the serine phosphate incorporated into partially purified or highly purified insulin receptor suggests that an insulin-sensitive serine kinase (IRSK) copurifies with the insulin receptor.	Phosphoserine	16-32	insulin receptor	Homo sapiens	89-105
2136851-2	1990	Analysis of the serine phosphate incorporated into partially purified or highly purified insulin receptor suggests that an insulin-sensitive serine kinase (IRSK) copurifies with the insulin receptor.	Phosphoserine	16-32	insulin receptor	Homo sapiens	182-198
2136851-3	1990	Following trypsin digestion, reversed-phase high pressure liquid chromatography (HPLC) analysis of the phosphorylated, affinity-purified insulin receptor preparation reveals phosphopeptide profiles similar to those of trypsin-digested receptors immunoprecipitated from 32P-labeled fibroblasts overexpressing the human insulin receptor.	Phosphorus-32	269-272	insulin receptor	Homo sapiens	137-153
2136851-6	1990	The serine containing tryptic peptide within the cytoplasmic domain of the human insulin receptor predicted to elute most rapidly upon HPLC had the sequence SSHCQR corresponding to residues 1293-1298.	Serine	4-10	insulin receptor	Homo sapiens	81-97
2136851-6	1990	The serine containing tryptic peptide within the cytoplasmic domain of the human insulin receptor predicted to elute most rapidly upon HPLC had the sequence SSHCQR corresponding to residues 1293-1298.	Peptides	30-37	insulin receptor	Homo sapiens	81-97
2136851-9	1990	We propose that serine 1293 or 1294 of the human insulin receptor is a major site(s) phosphorylated on the insulin receptor in intact cells and is phosphorylated by IRSK.	Serine	16-22	insulin receptor	Homo sapiens	49-65
2136851-9	1990	We propose that serine 1293 or 1294 of the human insulin receptor is a major site(s) phosphorylated on the insulin receptor in intact cells and is phosphorylated by IRSK.	Serine	16-22	insulin receptor	Homo sapiens	107-123
2210055-5	1990	The sequences of the gene and oligonucleotide primers will facilitate studies of genetic variation in the hINSR gene and thereby increase our understanding of the role of this gene in the development of insulin-resistant states and glucose intolerance.	Glucose	232-239	insulin receptor	Homo sapiens	106-111
2153301-0	1990	Labile disulfide bonds in human placental insulin receptor.	Disulfides	7-16	insulin receptor	Homo sapiens	42-58
1964389-8	1990	The occurrence of pp180, an insulin receptor substrate, in plasma membranes of several insulin responsive tissues suggests that it has a role in insulin signalling.	pp180	18-23	insulin receptor	Homo sapiens	28-44
2153301-1	1990	The disulfide crosslinking pattern of human placental insulin receptor was investigated using selective reduction with tributylphosphine followed by alkylation with N-[3H]ethylmaleimide.	Disulfides	4-13	insulin receptor	Homo sapiens	54-70
2153301-1	1990	The disulfide crosslinking pattern of human placental insulin receptor was investigated using selective reduction with tributylphosphine followed by alkylation with N-[3H]ethylmaleimide.	tri-n-butylphosphine	119-136	insulin receptor	Homo sapiens	54-70
2153301-1	1990	The disulfide crosslinking pattern of human placental insulin receptor was investigated using selective reduction with tributylphosphine followed by alkylation with N-[3H]ethylmaleimide.	n-[3h]ethylmaleimide	165-185	insulin receptor	Homo sapiens	54-70
2236159-0	1990	Does taurine bind to the insulin binding site of the insulin receptor?	Taurine	5-12	insulin receptor	Homo sapiens	53-69
2153301-2	1990	Insulin receptor contains a single sulfhydryl group in each beta subunit whose alkylation with N-[3H]ethylmaleimide inhibits receptor autophosphorylation.	n-[3h]ethylmaleimide	95-115	insulin receptor	Homo sapiens	0-16
33777737-3	2021	The aim of this study is to explore the association of triglyceride glucose (TyG) index, a simple surrogate marker of IR, with NSCLC risk.	Glucose	68-75	insulin receptor	Homo sapiens	118-120
33805872-11	2021	CONCLUSIONS: An increase of fasting glucose and more frequent incidence of metabolic syndrome, diabetes, and cardiovascular diseases in subjects with IR are associated with the prevalence of cardiovascular risk factors.	Glucose	36-43	insulin receptor	Homo sapiens	150-152
33810179-5	2021	This review aims to discuss causes behind the diminished activation of IR in neurons, with a focus on the functional relationship between mitochondria and IR during early insulin signaling and the related roles of oxidative stress, mitochondrial hypometabolism, and glutamate excitotoxicity in the development of IR insensitivity to insulin.	Glutamic Acid	266-275	insulin receptor	Homo sapiens	71-73
33777737-3	2021	The aim of this study is to explore the association of triglyceride glucose (TyG) index, a simple surrogate marker of IR, with NSCLC risk.	8-methyl-2-{[(pyridin-4-yl)sulfanyl]methyl}quinazolin-4(3H)-one	77-80	insulin receptor	Homo sapiens	118-120
33033446-12	2020	Several parameter values were affected by the INSR genotype, particularly W/H ratio, lipid, insulin and glucose levels and insulin resistance in PCOS patients.	Glucose	104-111	insulin receptor	Homo sapiens	46-50
33776919-5	2021	The aim of the present study was to measure the content of IR and IGF-1R and their phosphorylation in the placenta of women with type 1 diabetes mellitus (T1D) or with gestational diabetes mellitus (GDM) compared to women with normal glucose tolerance (NGT) during pregnancy.	Glucose	234-241	insulin receptor	Homo sapiens	59-61
33776919-13	2021	A positive correlation was observed between phosphorylation of placental IR and the glucose levels during the third trimester of GDM and T1D pregnancy (R-squared 0.21, p=0.003).	Glucose	84-91	insulin receptor	Homo sapiens	73-75
33032225-9	2021	Finally, the mechanism study by XPS, XRD, and IR demonstrated that the ligand exchange played an important role in the electro-assisted phosphate uptake process.	Phosphates	136-145	insulin receptor	Homo sapiens	46-48
33034331-0	2020	Salt-inclusion chalcogenides: an emerging class of IR nonlinear optical materials.	chalcogenides	15-28	insulin receptor	Homo sapiens	51-53
33034331-1	2020	Non-centrosymmetric metal chalcogenides such as AgGaS2 and AgGaSe2 are two of the commercial nonlinear optical (NLO) crystals widely used in the infrared (IR) region.	metal chalcogenides	20-39	insulin receptor	Homo sapiens	155-157
33034331-1	2020	Non-centrosymmetric metal chalcogenides such as AgGaS2 and AgGaSe2 are two of the commercial nonlinear optical (NLO) crystals widely used in the infrared (IR) region.	aggas2	48-54	insulin receptor	Homo sapiens	155-157
33034331-1	2020	Non-centrosymmetric metal chalcogenides such as AgGaS2 and AgGaSe2 are two of the commercial nonlinear optical (NLO) crystals widely used in the infrared (IR) region.	aggase2	59-66	insulin receptor	Homo sapiens	155-157
33034331-3	2020	Recently, the development of salt-inclusion chalcogenides with non-centrosymmetric structures has attracted more and more attention and interest owing to their intensive potential applications originating from their wide Eg, strong dij, ultrahigh laser-induced damage thresholds (LIDTs) and large IR transmission range.	Salts	29-33	insulin receptor	Homo sapiens	297-299
33034331-3	2020	Recently, the development of salt-inclusion chalcogenides with non-centrosymmetric structures has attracted more and more attention and interest owing to their intensive potential applications originating from their wide Eg, strong dij, ultrahigh laser-induced damage thresholds (LIDTs) and large IR transmission range.	chalcogenides	44-57	insulin receptor	Homo sapiens	297-299
33034331-4	2020	In this frontier paper, we review the recent progress of salt-inclusion chalcogenides (including 28 related compounds) as favourable candidates for IR-NLO materials, which can be divided into 3 types according to their chemical compositions and structural characteristics: (i) the [RaXb][GanQ2n] type and its derivatives, (ii) [NaBa4Cl][Ge3S10] and its derivatives, and (iii) the [A3X][MB12(MQ4)3] type.	Salts	57-61	insulin receptor	Homo sapiens	148-150
33034331-4	2020	In this frontier paper, we review the recent progress of salt-inclusion chalcogenides (including 28 related compounds) as favourable candidates for IR-NLO materials, which can be divided into 3 types according to their chemical compositions and structural characteristics: (i) the [RaXb][GanQ2n] type and its derivatives, (ii) [NaBa4Cl][Ge3S10] and its derivatives, and (iii) the [A3X][MB12(MQ4)3] type.	chalcogenides	72-85	insulin receptor	Homo sapiens	148-150
33034331-6	2020	In addition, the present challenges of creating new IR-NLO salt-inclusion chalcogenides and future perspectives in this field are discussed.	Salts	59-63	insulin receptor	Homo sapiens	52-54
33034331-6	2020	In addition, the present challenges of creating new IR-NLO salt-inclusion chalcogenides and future perspectives in this field are discussed.	chalcogenides	74-87	insulin receptor	Homo sapiens	52-54
34931736-8	2022	Histological examination indicated that treatment of ovarian I/R injury with GOS led to the improvement of ovarian tissue, which was accompanied by an increase in SOD activity and GSH level and a decrease in MDA level, NF-kappaB, TNF-alpha, IL-1beta, and IL-6 expressions.	Glutathione	180-183	insulin receptor	Homo sapiens	61-64
25676548-2	2015	Signalling pathways appear to converge on glycogen regulatory enzymes via insulin (glycogen synthase kinase 3beta, protein phosphatase 1, allosteric action of glucose-6-phosphate), beta-adrenergic (phosphorylase kinase protein phosphatase 1 inhibitor), and 5" adenosine monophosphate-activated protein kinase (allosteric action of glucose-6-phosphate, direct glycogen binding, insulin receptor).	Glycogen	42-50	insulin receptor	Homo sapiens	377-393
7821730-11	1994	We have found that in rat-1 fibroblasts which overexpressing human insulin receptor an inhibition of the tyrosine kinase activity of the receptor may be induced by high glucose levels.	Glucose	169-176	insulin receptor	Homo sapiens	67-83
7821730-12	1994	This appears to be mediated through activation of certain protein kinase C isoforms which form stable complexes with the insulin receptor and modulate the tyrosine kinase activity of the insulin receptor through serine phosphorylation of the receptor beta subunit.	Serine	212-218	insulin receptor	Homo sapiens	121-137
34965699-13	2021	Leprechaunism was confirmed by genetic analysis of the insulin receptor (INSR) gene, in which a novel c.320C>G; p. Thr107Arg homozygous missense mutation in exon 2 was found.	thr107arg	115-124	insulin receptor	Homo sapiens	55-71
34965699-13	2021	Leprechaunism was confirmed by genetic analysis of the insulin receptor (INSR) gene, in which a novel c.320C>G; p. Thr107Arg homozygous missense mutation in exon 2 was found.	thr107arg	115-124	insulin receptor	Homo sapiens	73-77
34964902-8	2021	We identified dual IGF1R/IR antagonists, BMS-754807 and linsitinib, able to inhibit tumor cell viability at concentrations that do not affect CAR T-cells.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	56-66	insulin receptor	Homo sapiens	25-27
34882427-3	2022	In this report, a mechanistic study of a prototypical tandem photoredox/HAT reaction coupling cyclohexene and 1,4-dicyanobenzene (DCB) using an Ir(ppy)3 photocatalyst and thiol HAT catalyst is reported.	cyclohexene	94-105	insulin receptor	Homo sapiens	144-152
34882427-3	2022	In this report, a mechanistic study of a prototypical tandem photoredox/HAT reaction coupling cyclohexene and 1,4-dicyanobenzene (DCB) using an Ir(ppy)3 photocatalyst and thiol HAT catalyst is reported.	1,4-dicyanobenzene	110-128	insulin receptor	Homo sapiens	144-152
34882427-3	2022	In this report, a mechanistic study of a prototypical tandem photoredox/HAT reaction coupling cyclohexene and 1,4-dicyanobenzene (DCB) using an Ir(ppy)3 photocatalyst and thiol HAT catalyst is reported.	1,4-dicyanobenzene	130-133	insulin receptor	Homo sapiens	144-152
34882427-8	2022	Kinetic modeling of the reaction, using rate constants derived from TAS, demonstrates that the efficiency of the reaction is limited by parasitic absorption and unproductive quenching between excited Ir(ppy)3 and the cyanohydrin photoproduct.	cyanohydrin	217-228	insulin receptor	Homo sapiens	200-208
34944530-3	2021	Insulin receptor stimulation is correlated with multiple physiological and biochemical functions, including glucose transport, glucose homeostasis, food intake, proliferation, glycolysis, and lipogenesis.	Glucose	108-115	insulin receptor	Homo sapiens	0-16
34944530-5	2021	Signal transducers such as protein kinases or the GLUT4-induced influx of glucose connect insulin receptor stimulation with transcription.	Glucose	74-81	insulin receptor	Homo sapiens	90-106
34944037-10	2021	Treatment with miR-497-5p inhibitors did not change the diameter of the myotubes but increased the expression of its target genes Insr and Igf1r.	CHEMBL3740941	23-25	insulin receptor	Homo sapiens	130-134
34551248-3	2021	The strategy relies on the of use visible-light-mediated photocatalysis with readily available Ir(III) complexes to bring about single-electron reduction of an all-alkyl ketimine species to an alpha-amino radical intermediate; the alpha-amino radical undergoes Giese-type addition with a variety of alkenes to forge the alpha-trialkyl-alpha-tertiary amine center.	alkyl ketimine	164-178	insulin receptor	Homo sapiens	95-102
34877528-3	2021	Infrared (IR) spectroscopy is a well-established technique which has been widely applied in polysaccharide structural analysis.	Polysaccharides	92-106	insulin receptor	Homo sapiens	10-12
34877528-4	2021	In this paper, the principle of IR and interpretation of polysaccharide IR spectrum are briefly introduced.	Polysaccharides	57-71	insulin receptor	Homo sapiens	32-34
34877528-4	2021	In this paper, the principle of IR and interpretation of polysaccharide IR spectrum are briefly introduced.	Polysaccharides	57-71	insulin receptor	Homo sapiens	72-74
34877528-5	2021	Classical applications of IR spectroscopy in polysaccharide structural elucidation are reviewed from qualitative and quantitative aspects.	Polysaccharides	45-59	insulin receptor	Homo sapiens	26-28
34877528-7	2021	These emerging techniques can considerably expand application scope of IR, thus exert a more important effect on carbohydrate characterization.	Carbohydrates	113-125	insulin receptor	Homo sapiens	71-73
34877528-8	2021	Overall, this review seeks to provide a comprehensive insight to applications of IR spectroscopy in polysaccharide structural analysis and highlights the importance of advanced IR-integrating techniques.	Polysaccharides	100-114	insulin receptor	Homo sapiens	81-83
34732796-3	2021	Using Si would bring EOT and its many applications to the silicon photonics realm and the mid-IR range.	Silicon	6-8	insulin receptor	Homo sapiens	94-96
34732796-4	2021	Since Si thin film is a semi-transparent film in mid-IR, a generalization was proposed of the normalized transmission metric used in literature for EOT studies in opaque films.	Silicon	6-8	insulin receptor	Homo sapiens	53-55
34931736-3	2022	This study aimed to investigate whether the gossypin (GOS) with antioxidant properties, a flavonoid, has beneficial effects on the biochemical, molecular, and histopathological aspects of ovarian I/R injury.	gossypin	44-52	insulin receptor	Homo sapiens	196-199
34931736-3	2022	This study aimed to investigate whether the gossypin (GOS) with antioxidant properties, a flavonoid, has beneficial effects on the biochemical, molecular, and histopathological aspects of ovarian I/R injury.	gossypin	54-57	insulin receptor	Homo sapiens	196-199
34931736-3	2022	This study aimed to investigate whether the gossypin (GOS) with antioxidant properties, a flavonoid, has beneficial effects on the biochemical, molecular, and histopathological aspects of ovarian I/R injury.	Flavonoids	90-99	insulin receptor	Homo sapiens	196-199
34959365-0	2021	Hepatocyte-Specific Co-Delivery of Zinc Ions and Plasmid DNA by Lactosylated Poly(1-vinylimidazole) for Suppression of Insulin Receptor Internalization.	poly(1-vinylimidazole)	77-98	insulin receptor	Homo sapiens	119-135
34969688-3	2021	An in vitro model of IR cleavage shows that extracellular calpain 2 directly cleaves IR, which generates sIR, and sequential cleavage of the IRbeta subunit by gamma-secretase impairs insulin signaling in a glucose concentration-dependent manner.	Glucose	206-213	insulin receptor	Homo sapiens	21-23
34089144-2	2021	Objective To compare patients receiving tapentadol IR versus oxycodone IR following orthopaedic surgery during hospitalisation with regard to the changing of opioids at hospital discharge.	Tapentadol	40-50	insulin receptor	Homo sapiens	51-53
34089144-2	2021	Objective To compare patients receiving tapentadol IR versus oxycodone IR following orthopaedic surgery during hospitalisation with regard to the changing of opioids at hospital discharge.	Oxycodone	61-70	insulin receptor	Homo sapiens	71-73
34089144-5	2021	Participants included adult orthopaedic surgery patients receiving postoperative tapentadol IR or oxycodone IR during hospitalisation between 1 January 2018 and 30 June 2019.	Tapentadol	81-91	insulin receptor	Homo sapiens	92-94
34089144-5	2021	Participants included adult orthopaedic surgery patients receiving postoperative tapentadol IR or oxycodone IR during hospitalisation between 1 January 2018 and 30 June 2019.	Oxycodone	98-107	insulin receptor	Homo sapiens	108-110
34089144-13	2021	Conclusions The post-operative use of tapentadol IR during hospitalisation was associated with an increased likelihood of opioid changing at hospital discharge.	Tapentadol	38-48	insulin receptor	Homo sapiens	49-51
34884763-4	2021	Adipogenesis was unaffected in Nrg4 KD adipocytes, but there was a complete impairment of the insulin-induced 2-deoxyglucose uptake, which was likely the result of reduced insulin receptor and Glut4 protein.	Deoxyglucose	110-124	insulin receptor	Homo sapiens	172-188
34755745-0	2021	An ab initio anharmonic approach to IR, Raman and SFG spectra of the solvated methylammonium ion.	methylamine	78-96	insulin receptor	Homo sapiens	36-38
34755745-3	2021	In the present work, we have applied the ab initio anharmonic algorithm at the CCSD/aug-cc-pVDZ level to simulate the IR and Raman spectra of the solvated methylammonium ion, MA-H+ X3, where X denotes the solvent molecules, to understand the Fermi resonance mechanism in which the overtones of NH bending modes are coupled with the fundamentals of NH stretching modes.	methylamine	155-173	insulin receptor	Homo sapiens	118-120
34551248-3	2021	The strategy relies on the of use visible-light-mediated photocatalysis with readily available Ir(III) complexes to bring about single-electron reduction of an all-alkyl ketimine species to an alpha-amino radical intermediate; the alpha-amino radical undergoes Giese-type addition with a variety of alkenes to forge the alpha-trialkyl-alpha-tertiary amine center.	alpha-amino radical	193-212	insulin receptor	Homo sapiens	95-102
34290045-7	2021	Rather these findings are better explained as a direct consequence of postmenopausal women with features of insulin resistance (IR) eating a low-fat high-carbohydrate diet for 13 years.	Carbohydrates	154-166	insulin receptor	Homo sapiens	128-130
34087222-8	2021	More importantly, it is for the first time to show that the anti-neuroinflammatory effects of tangeretin through VEGFA, EGFR, IGF-1 receptor, InsR, and mTOR signaling pathway.	tangeretin	94-104	insulin receptor	Homo sapiens	142-146
34539566-8	2021	Computational docking analysis disclosed the possible stabilizing effect of PFOA on the complex between InsR and GM3 ganglioside, previously shown to be associated with the low grade chronic inflammation-related insulin resistance.	perfluorooctanoic acid	76-80	insulin receptor	Homo sapiens	104-108
34539566-8	2021	Computational docking analysis disclosed the possible stabilizing effect of PFOA on the complex between InsR and GM3 ganglioside, previously shown to be associated with the low grade chronic inflammation-related insulin resistance.	G(M3) Ganglioside	113-128	insulin receptor	Homo sapiens	104-108
34196088-3	2021	We have characterized the adducts formed between a series of isostructural N -heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry.	n -heterocyclic carbene	75-98	insulin receptor	Homo sapiens	136-138
34196088-3	2021	We have characterized the adducts formed between a series of isostructural N -heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry.	nhc	100-103	insulin receptor	Homo sapiens	136-138
34196088-3	2021	We have characterized the adducts formed between a series of isostructural N -heterocyclic carbene (NHC) complexes with Ru, Os, Rh, and Ir centers and the model protein hen egg white lysozyme by X-ray crystallography and mass spectrometry.	Ruthenium	120-122	insulin receptor	Homo sapiens	136-138
34196088-5	2021	In contrast, the more inert Os and Ir derivatives were detected in an electronegative binding pocket after undergoing ligand exchange of a chlorido ligand for an amino acid side chain.	chlorido	139-147	insulin receptor	Homo sapiens	35-37
34324831-0	2021	Phospholipid exchange shows insulin receptor activity is supported by both the propensity to form wide bilayers and ordered raft domains.	Phospholipids	0-12	insulin receptor	Homo sapiens	28-44
34324831-3	2021	Here, using efficient methyl-alpha-cyclodextrin mediated lipid exchange, we studied the effect of altering plasma membrane outer leaflet phospholipid composition upon the activity of IR in mammalian cells.	methyl-alpha-cyclodextrin	22-47	insulin receptor	Homo sapiens	183-185
34324831-3	2021	Here, using efficient methyl-alpha-cyclodextrin mediated lipid exchange, we studied the effect of altering plasma membrane outer leaflet phospholipid composition upon the activity of IR in mammalian cells.	Phospholipids	137-149	insulin receptor	Homo sapiens	183-185
34324831-4	2021	After substitution of endogenous lipids with lipids having an ability to form liquid ordered (Lo) domains (sphingomyelins) or liquid disordered (Ld) domains (unsaturated phosphatidylcholines (PCs)), we found that the propensity of lipids to form ordered domains is required for high IR activity.	Sphingomyelins	107-121	insulin receptor	Homo sapiens	283-285
34390422-0	2021	Correction to: Switch-on effect on conformation-specific arylamine-DNA adduct by cyclometalated Ir(III) complexes.	aniline	57-66	insulin receptor	Homo sapiens	96-103
34438601-7	2021	IR was calculated by using the homeostasis model assessment for IR in patients with obesity and the estimated glucose disposal rate in T1D.	Glucose	110-117	insulin receptor	Homo sapiens	0-2
34484117-11	2021	The results of this study could be used as a theoretical basis in support of using metformin in the treatment of PCOS-IR patients.	Metformin	83-92	insulin receptor	Homo sapiens	118-120
34531946-4	2021	The Ir(III) complex nanoparticles have relatively strong photodynamic activity upon irradiation, which includes type I and type II reactive oxygen species.	Reactive Oxygen Species	131-154	insulin receptor	Homo sapiens	4-11
34408667-3	2021	We found that urate-associated variants in the human insulin (INS), insulin receptor (INSR), and insulin receptor substrate-1 (IRS1) loci associate with the expression of the insulin-like growth factor 2, IRS1, INSR, and ZNF358 genes; additionally, we found genetic interaction between SLC2A9 and the three loci, most evident in women.	Uric Acid	14-19	insulin receptor	Homo sapiens	68-84
34408667-3	2021	We found that urate-associated variants in the human insulin (INS), insulin receptor (INSR), and insulin receptor substrate-1 (IRS1) loci associate with the expression of the insulin-like growth factor 2, IRS1, INSR, and ZNF358 genes; additionally, we found genetic interaction between SLC2A9 and the three loci, most evident in women.	Uric Acid	14-19	insulin receptor	Homo sapiens	86-90
34408667-3	2021	We found that urate-associated variants in the human insulin (INS), insulin receptor (INSR), and insulin receptor substrate-1 (IRS1) loci associate with the expression of the insulin-like growth factor 2, IRS1, INSR, and ZNF358 genes; additionally, we found genetic interaction between SLC2A9 and the three loci, most evident in women.	Uric Acid	14-19	insulin receptor	Homo sapiens	211-215
34111424-7	2021	Simvastatin impaired the phosphorylation of the insulin receptor (IR beta), Akt ser473 and S6rp, and increased phosphorylation of AMPK thr172 in both myotubes and myoblasts, which was prevented by insulin and mevalonate.	Simvastatin	0-11	insulin receptor	Homo sapiens	48-64
34111424-7	2021	Simvastatin impaired the phosphorylation of the insulin receptor (IR beta), Akt ser473 and S6rp, and increased phosphorylation of AMPK thr172 in both myotubes and myoblasts, which was prevented by insulin and mevalonate.	Mevalonic Acid	209-219	insulin receptor	Homo sapiens	48-64
34413118-6	2021	Addition of a C20 fatty diacid-containing side chain imparts strong, reversible albumin binding, while three amino acid substitutions (A14E, B16H and B25H) provide molecular stability and contribute to attenuating insulin receptor (IR) binding and clearance, further prolonging the half-life.	c20 fatty diacid	14-30	insulin receptor	Homo sapiens	232-234
34283407-3	2021	The examples evaluated make use of different photocatalysts, such as polypyridyl complexes of Ir or Ru transition metals, organic dyes such as Rose Bengal, phthalocyanine-metal organocatalysts, or visible-light activated complexes.	polypyridyl complexes	69-90	insulin receptor	Homo sapiens	94-96
34361768-5	2021	The most efficient green PhOLED with 10 wt% of Ir(ppy)3 {tris(2-phenylpyridine)iridium(III)} in the H2 host showed a power efficiency of 34.1 lm/W, current efficiency of 33.9 cd/A, and a high value of 9.4% for external quantum efficiency at a high brightness of 1000 cd/m2, which is required for lighting applications.	Tris(2-phenylpyridine)iridium	57-86	insulin receptor	Homo sapiens	47-55
34361768-5	2021	The most efficient green PhOLED with 10 wt% of Ir(ppy)3 {tris(2-phenylpyridine)iridium(III)} in the H2 host showed a power efficiency of 34.1 lm/W, current efficiency of 33.9 cd/A, and a high value of 9.4% for external quantum efficiency at a high brightness of 1000 cd/m2, which is required for lighting applications.	Deuterium	100-102	insulin receptor	Homo sapiens	47-55
34232631-6	2021	Pearson"s correlation coefficient test showed that elemental carbon (EC), polycyclic aromatic hydrocarbons (PAHs), and metals (Ca, Co, and V) were negatively correlated to the dysregulated proteins (INSR, IRS-1, AKT, FOXO1, GLUT2, and GLUT4).	Carbon	61-67	insulin receptor	Homo sapiens	199-203
34232631-6	2021	Pearson"s correlation coefficient test showed that elemental carbon (EC), polycyclic aromatic hydrocarbons (PAHs), and metals (Ca, Co, and V) were negatively correlated to the dysregulated proteins (INSR, IRS-1, AKT, FOXO1, GLUT2, and GLUT4).	Carbon	69-71	insulin receptor	Homo sapiens	199-203
34358111-0	2021	Interaction between DNA, Albumin and Apo-Transferrin and Iridium(III) Complexes with Phosphines Derived from Fluoroquinolones as a Potent Anticancer Drug.	Phosphines	85-95	insulin receptor	Homo sapiens	65-68
34358111-0	2021	Interaction between DNA, Albumin and Apo-Transferrin and Iridium(III) Complexes with Phosphines Derived from Fluoroquinolones as a Potent Anticancer Drug.	Fluoroquinolones	109-125	insulin receptor	Homo sapiens	65-68
34358111-1	2021	A group of cytotoxic half-sandwich iridium(III) complexes with aminomethyl(diphenyl)phosphine derived from fluoroquinolone antibiotics exhibit the ability to (i) accumulate in the nucleus, (ii) induce apoptosis, (iii) activate caspase-3/7 activity, (iv) induce the changes in cell cycle leading to G2/M phase arrest, and (v) radicals generation.	aminomethyl(diphenyl)phosphine	63-93	insulin receptor	Homo sapiens	43-46
34358111-1	2021	A group of cytotoxic half-sandwich iridium(III) complexes with aminomethyl(diphenyl)phosphine derived from fluoroquinolone antibiotics exhibit the ability to (i) accumulate in the nucleus, (ii) induce apoptosis, (iii) activate caspase-3/7 activity, (iv) induce the changes in cell cycle leading to G2/M phase arrest, and (v) radicals generation.	aminomethyl(diphenyl)phosphine	63-93	insulin receptor	Homo sapiens	213-216
34358111-1	2021	A group of cytotoxic half-sandwich iridium(III) complexes with aminomethyl(diphenyl)phosphine derived from fluoroquinolone antibiotics exhibit the ability to (i) accumulate in the nucleus, (ii) induce apoptosis, (iii) activate caspase-3/7 activity, (iv) induce the changes in cell cycle leading to G2/M phase arrest, and (v) radicals generation.	Fluoroquinolones	107-122	insulin receptor	Homo sapiens	43-46
34358111-1	2021	A group of cytotoxic half-sandwich iridium(III) complexes with aminomethyl(diphenyl)phosphine derived from fluoroquinolone antibiotics exhibit the ability to (i) accumulate in the nucleus, (ii) induce apoptosis, (iii) activate caspase-3/7 activity, (iv) induce the changes in cell cycle leading to G2/M phase arrest, and (v) radicals generation.	Fluoroquinolones	107-122	insulin receptor	Homo sapiens	213-216
34358111-7	2021	Furthermore, Ir(III) complexes were found to dock within the apo-Tf binding site, including nearby tyrosine residues.	Tyrosine	99-107	insulin receptor	Homo sapiens	13-20
34343291-0	2021	Effects of changes in glycan composition on glycoprotein dynamics: example of N-glycans on insulin receptor.	Polysaccharides	22-28	insulin receptor	Homo sapiens	91-107
34343291-0	2021	Effects of changes in glycan composition on glycoprotein dynamics: example of N-glycans on insulin receptor.	n-glycans	78-87	insulin receptor	Homo sapiens	91-107
34343291-3	2021	One such example is the development of insulin resistance, which has been attributed to the removal of sialic acid residues from N-glycans of insulin receptor (IR) from various experimental studies.	N-Acetylneuraminic Acid	103-114	insulin receptor	Homo sapiens	142-158
34343291-3	2021	One such example is the development of insulin resistance, which has been attributed to the removal of sialic acid residues from N-glycans of insulin receptor (IR) from various experimental studies.	N-Acetylneuraminic Acid	103-114	insulin receptor	Homo sapiens	160-162
34343291-3	2021	One such example is the development of insulin resistance, which has been attributed to the removal of sialic acid residues from N-glycans of insulin receptor (IR) from various experimental studies.	n-glycans	129-138	insulin receptor	Homo sapiens	142-158
34343291-3	2021	One such example is the development of insulin resistance, which has been attributed to the removal of sialic acid residues from N-glycans of insulin receptor (IR) from various experimental studies.	n-glycans	129-138	insulin receptor	Homo sapiens	160-162
34087222-7	2021	Taken together, we assumed that tangeretin could exert protective effects on neuroinflammation by decreasing the expression of VEGFA, EGFR, InsR, and IGF-1 receptor in the PI3K-AKT, MAPK, mTOR signaling pathway.	tangeretin	32-42	insulin receptor	Homo sapiens	140-144
34324831-4	2021	After substitution of endogenous lipids with lipids having an ability to form liquid ordered (Lo) domains (sphingomyelins) or liquid disordered (Ld) domains (unsaturated phosphatidylcholines (PCs)), we found that the propensity of lipids to form ordered domains is required for high IR activity.	unsaturated phosphatidylcholines	158-190	insulin receptor	Homo sapiens	283-285
34324831-4	2021	After substitution of endogenous lipids with lipids having an ability to form liquid ordered (Lo) domains (sphingomyelins) or liquid disordered (Ld) domains (unsaturated phosphatidylcholines (PCs)), we found that the propensity of lipids to form ordered domains is required for high IR activity.	Phosphatidylcholines	192-195	insulin receptor	Homo sapiens	283-285
34324831-6	2021	Incorporating purified IR into alkyl maltoside micelles with increasing hydrocarbon lengths also increased IR activity, but more modestly than by increasing lipid acyl chain length in cells.	alkyl maltoside	31-46	insulin receptor	Homo sapiens	23-25
34324831-6	2021	Incorporating purified IR into alkyl maltoside micelles with increasing hydrocarbon lengths also increased IR activity, but more modestly than by increasing lipid acyl chain length in cells.	alkyl maltoside	31-46	insulin receptor	Homo sapiens	107-109
34324831-6	2021	Incorporating purified IR into alkyl maltoside micelles with increasing hydrocarbon lengths also increased IR activity, but more modestly than by increasing lipid acyl chain length in cells.	Hydrocarbons	72-83	insulin receptor	Homo sapiens	23-25
34324831-6	2021	Incorporating purified IR into alkyl maltoside micelles with increasing hydrocarbon lengths also increased IR activity, but more modestly than by increasing lipid acyl chain length in cells.	Hydrocarbons	72-83	insulin receptor	Homo sapiens	107-109
34443576-7	2021	Results showed that the new ncAA, bulky-isonitrile-carbamate-lysine (BICK) is efficiently and specifically incorporated into proteins by genetic code expansion, and despite the slow (4 + 1) cycloaddition, enables the labeling of outer membrane receptors such as insulin receptor (IR) with a membrane-impermeable dye.	ncaa	28-32	insulin receptor	Homo sapiens	262-278
34443576-7	2021	Results showed that the new ncAA, bulky-isonitrile-carbamate-lysine (BICK) is efficiently and specifically incorporated into proteins by genetic code expansion, and despite the slow (4 + 1) cycloaddition, enables the labeling of outer membrane receptors such as insulin receptor (IR) with a membrane-impermeable dye.	bick	69-73	insulin receptor	Homo sapiens	262-278
34160136-0	2021	Ir(III)-Catalyzed Diarylation/Annulation of Benzoic Acids: Facile Access to Multi-Aryl Spirobifluorenes as Pure Hydrocarbon Hosts for High-Performance OLEDs.	Benzoates	44-57	insulin receptor	Homo sapiens	0-7
34160136-0	2021	Ir(III)-Catalyzed Diarylation/Annulation of Benzoic Acids: Facile Access to Multi-Aryl Spirobifluorenes as Pure Hydrocarbon Hosts for High-Performance OLEDs.	-aryl spirobifluorenes	81-103	insulin receptor	Homo sapiens	0-7
34160136-0	2021	Ir(III)-Catalyzed Diarylation/Annulation of Benzoic Acids: Facile Access to Multi-Aryl Spirobifluorenes as Pure Hydrocarbon Hosts for High-Performance OLEDs.	Hydrocarbons	112-123	insulin receptor	Homo sapiens	0-7
34160136-0	2021	Ir(III)-Catalyzed Diarylation/Annulation of Benzoic Acids: Facile Access to Multi-Aryl Spirobifluorenes as Pure Hydrocarbon Hosts for High-Performance OLEDs.	oleds	151-156	insulin receptor	Homo sapiens	0-7
34340727-1	2021	BACKGROUND & AIMS: Branched-chain amino acids (BCAAs) are considered markers of insulin resistance (IR) in subjects with obesity.	Amino Acids, Branched-Chain	19-45	insulin receptor	Homo sapiens	100-102
34340727-1	2021	BACKGROUND & AIMS: Branched-chain amino acids (BCAAs) are considered markers of insulin resistance (IR) in subjects with obesity.	Amino Acids, Branched-Chain	47-52	insulin receptor	Homo sapiens	100-102
34165135-6	2021	However, clinical trials and systematic reviews show statistical differences on glucose, insulin, and glycated hemoglobin levels of patients with T2DM, associated with activation mechanisms of transcription factors related to genes of the glucide metabolism and the insulin receptor, and the regulation of intracellular Ca2+ insulin concentrations.	Glucose	80-87	insulin receptor	Homo sapiens	266-282
34275275-0	2021	Evidence of IR-Induced Chemistry in a Neat Solid: Tautomerization of Thiotropolone by Thermal, Electronic, and Vibrational Excitations.	thiotropolone	69-82	insulin receptor	Homo sapiens	12-14
34275275-2	2021	Visible light irradiation (lambda >= 400 nm) leads to thione-enol   thiol-keto tautomerization in matrices and under neat solid conditions at 15 K. The assignment of the IR spectra of the two thiotropolone tautomers (thione-enol and thiol-keto) was carried out with the support of B3LYP/6-311+G(2d,p) computations.	thiotropolone	192-205	insulin receptor	Homo sapiens	170-172
34275275-2	2021	Visible light irradiation (lambda >= 400 nm) leads to thione-enol   thiol-keto tautomerization in matrices and under neat solid conditions at 15 K. The assignment of the IR spectra of the two thiotropolone tautomers (thione-enol and thiol-keto) was carried out with the support of B3LYP/6-311+G(2d,p) computations.	thione-enol	217-228	insulin receptor	Homo sapiens	170-172
34275275-4	2021	Moreover, it was found that narrowband IR irradiation of the thiol-keto form in a neat solid, at the frequency of its CH stretching overtones/combination modes, also induces tautomerization to the thione-enol form.	Sulfhydryl Compounds	61-66	insulin receptor	Homo sapiens	39-41
34275275-4	2021	Moreover, it was found that narrowband IR irradiation of the thiol-keto form in a neat solid, at the frequency of its CH stretching overtones/combination modes, also induces tautomerization to the thione-enol form.	overtones	132-141	insulin receptor	Homo sapiens	39-41
34275275-4	2021	Moreover, it was found that narrowband IR irradiation of the thiol-keto form in a neat solid, at the frequency of its CH stretching overtones/combination modes, also induces tautomerization to the thione-enol form.	thione-enol	197-208	insulin receptor	Homo sapiens	39-41
34249083-15	2021	Conclusion: Homozygous G/G genotype at the INSR locus (rs4804416) is associated with an increased risk of AF in patients on L-thyroxine, independent of serum of free thyroxine and thyroid-stimulating hormone serum concentrations.	Thyroxine	124-135	insulin receptor	Homo sapiens	43-47
34290045-8	2021	All the worst clinical features of IR, including type 2 diabetes mellitus (T2DM) in some, can be "reversed" by the prescription of a high-fat low-carbohydrate diet.	Carbohydrates	146-158	insulin receptor	Homo sapiens	35-37
34207541-1	2021	Insulin acts by binding with a specific receptor called an insulin receptor (INSR), ending up with glucose transporter activation and glucose uptake.	Glucose	99-106	insulin receptor	Homo sapiens	77-81
34207541-1	2021	Insulin acts by binding with a specific receptor called an insulin receptor (INSR), ending up with glucose transporter activation and glucose uptake.	Glucose	134-141	insulin receptor	Homo sapiens	59-75
34203120-2	2021	LRP1 is a scaffold protein for insulin receptor involved in the insulin-induced glucose transporter type 4 (GLUT4) translocation to plasma membrane and glucose uptake in different types of cells.	Glucose	152-159	insulin receptor	Homo sapiens	31-47
34207541-1	2021	Insulin acts by binding with a specific receptor called an insulin receptor (INSR), ending up with glucose transporter activation and glucose uptake.	Glucose	134-141	insulin receptor	Homo sapiens	77-81
34503438-9	2021	INS too showed similar results.INSR, INS and TRIB3 were found to have the maximum change in their binding free energy due to rSNP variation.	rsnp	125-129	insulin receptor	Homo sapiens	31-35
34207541-1	2021	Insulin acts by binding with a specific receptor called an insulin receptor (INSR), ending up with glucose transporter activation and glucose uptake.	Glucose	99-106	insulin receptor	Homo sapiens	59-75
35065520-0	2022	Detection of siloxane thin films on glass substrate using IR ratio-reflectance spectrum.	Siloxanes	13-21	insulin receptor	Homo sapiens	58-60
35066640-11	2022	Finally, in vitro assays confirmed that EGCG acts as an insulin-sensitizing agent and that the chronic treatment of liver cells with tea extracts results in an enhancement of the insulin receptor levels and insulin sensitivity.	epigallocatechin gallate	40-44	insulin receptor	Homo sapiens	179-195
35587699-11	2022	In contrast with other Ir(ppz)2(LX) complexes, Ir(ppz)2(picOH) produced long-lived TA species, attributed to excited-state intramolecular proton transfer of the picOH ligand in the excited singlet state.	lx	32-34	insulin receptor	Homo sapiens	47-55
35587699-11	2022	In contrast with other Ir(ppz)2(LX) complexes, Ir(ppz)2(picOH) produced long-lived TA species, attributed to excited-state intramolecular proton transfer of the picOH ligand in the excited singlet state.	picoh	56-61	insulin receptor	Homo sapiens	47-55
35587699-11	2022	In contrast with other Ir(ppz)2(LX) complexes, Ir(ppz)2(picOH) produced long-lived TA species, attributed to excited-state intramolecular proton transfer of the picOH ligand in the excited singlet state.	Tantalum	83-85	insulin receptor	Homo sapiens	47-55
35587699-11	2022	In contrast with other Ir(ppz)2(LX) complexes, Ir(ppz)2(picOH) produced long-lived TA species, attributed to excited-state intramolecular proton transfer of the picOH ligand in the excited singlet state.	picoh	161-166	insulin receptor	Homo sapiens	47-55
34740281-0	2022	Differentiation of Disaccharide Isomers via a Combination of IR and UV Photodissociation Mass Spectrometry.	Disaccharides	19-31	insulin receptor	Homo sapiens	61-63
34740281-2	2022	For photodissociation MS, infrared (IR) and ultraviolet (UV) lasers can generate complementary fragment ions, so an effective combination of the two methods may provide rich and valuable fragment patterns for glycan analysis.	Polysaccharides	209-215	insulin receptor	Homo sapiens	36-38
34740281-8	2022	CONCLUSIONS: This study demonstrates the capabilities of the combination of IR and UV photodissociation MS in the identification of diverse glycan isomers.	Polysaccharides	140-146	insulin receptor	Homo sapiens	76-78
35441186-4	2022	Our results showed that the existence of the galloyl moiety in the structure of polyphenols was necessary for their inhibition of adipogenic differentiation, which could help to delay cells from entering the G2/M phase as well as to hinder the MCE process in the early stage of differentiation and the downstream PPARgamma and C/EBPalpha related MAPK signaling pathway, probably via binding to IR and disturbing the alpha-helix in its conformation.	galloyl	45-52	insulin receptor	Homo sapiens	394-396
35441186-4	2022	Our results showed that the existence of the galloyl moiety in the structure of polyphenols was necessary for their inhibition of adipogenic differentiation, which could help to delay cells from entering the G2/M phase as well as to hinder the MCE process in the early stage of differentiation and the downstream PPARgamma and C/EBPalpha related MAPK signaling pathway, probably via binding to IR and disturbing the alpha-helix in its conformation.	Polyphenols	80-91	insulin receptor	Homo sapiens	394-396
35149128-0	2022	Tyrphostin AG1024 downregulates aryl hydrocarbon receptor (AhR) expression in an IGF1R and IR-independent manner.	Tyrphostins	0-10	insulin receptor	Homo sapiens	91-93
35149128-0	2022	Tyrphostin AG1024 downregulates aryl hydrocarbon receptor (AhR) expression in an IGF1R and IR-independent manner.	tyrphostin AG 1024	11-17	insulin receptor	Homo sapiens	91-93
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	Tyrphostins	50-60	insulin receptor	Homo sapiens	150-166
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	Tyrphostins	50-60	insulin receptor	Homo sapiens	168-170
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	tyrphostin AG 1024	61-67	insulin receptor	Homo sapiens	150-166
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	tyrphostin AG 1024	61-67	insulin receptor	Homo sapiens	168-170
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	Methylcholanthrene	213-233	insulin receptor	Homo sapiens	150-166
35149128-4	2022	Among 164 kinase inhibitors listed in these kits, tyrphostin AG1024, commonly used as an inhibitor of insulin-like growth factor receptor (IGF1R) and insulin receptor (IR), was identified as a potent inhibitor of 3-methylcholanthrene (MC)-mediated AhR activation.	Methylcholanthrene	213-233	insulin receptor	Homo sapiens	168-170
35587699-0	2022	Influence of picolinate ancillary ligands on unique photophysical properties of Ir(ppz)2(LX).	picolinic acid	13-23	insulin receptor	Homo sapiens	80-88
35587699-1	2022	Homoleptic fac-Ir(ppz)3 (ppz = phenylpyrazole) and a series of heteroleptic Ir(ppz)2(LX) complexes consisting of picolinic acid (pic), 3-hydroxypicolinic acid (picOH), and isoquinolinecarboxylic acid (iq) as ancillary ligands (LX) were synthesised to investigate the influence of the ancillary ligands on the photophysical properties of the complexes.	lx	85-87	insulin receptor	Homo sapiens	76-84
35587699-1	2022	Homoleptic fac-Ir(ppz)3 (ppz = phenylpyrazole) and a series of heteroleptic Ir(ppz)2(LX) complexes consisting of picolinic acid (pic), 3-hydroxypicolinic acid (picOH), and isoquinolinecarboxylic acid (iq) as ancillary ligands (LX) were synthesised to investigate the influence of the ancillary ligands on the photophysical properties of the complexes.	picolinic acid	113-127	insulin receptor	Homo sapiens	76-84
35587699-1	2022	Homoleptic fac-Ir(ppz)3 (ppz = phenylpyrazole) and a series of heteroleptic Ir(ppz)2(LX) complexes consisting of picolinic acid (pic), 3-hydroxypicolinic acid (picOH), and isoquinolinecarboxylic acid (iq) as ancillary ligands (LX) were synthesised to investigate the influence of the ancillary ligands on the photophysical properties of the complexes.	3-hydroxypicolinic acid	135-158	insulin receptor	Homo sapiens	76-84
35609831-6	2022	The chemical stability of milled bosentan was evaluated using ATR-IR and 1 H NMR as well.	Bosentan	33-41	insulin receptor	Homo sapiens	66-74
35579256-4	2022	Notably, the formation of QDI derivatives can actively scavenge the reactive oxygen species generated by fac -Ir(ppy) 3 , thus avoiding oxygen quenching of the photocatalyst.	Reactive Oxygen Species	68-91	insulin receptor	Homo sapiens	110-119
35182540-4	2022	Our findings indicate the importance of insulin receptor-mediated activation of the MAPK signalling pathway in the proliferation and growth of the bladder wall of the racemose cyst and its susceptibility to metformin action.	Metformin	207-216	insulin receptor	Homo sapiens	40-56
35557695-3	2022	Here, different heterocyclic compounds with indole and pyrimidine moieties have been synthesized effectively, and their structures have been validated using NMR, IR, and mass spectroscopy.	indole	44-50	insulin receptor	Homo sapiens	162-164
35557695-3	2022	Here, different heterocyclic compounds with indole and pyrimidine moieties have been synthesized effectively, and their structures have been validated using NMR, IR, and mass spectroscopy.	pyrimidine	55-65	insulin receptor	Homo sapiens	162-164
35564095-0	2022	Octagonal Quasicrystal Defect Mode Laser-Based PVK: Ir(ppy)3 Polymer Driven by Optical Pumping.	Polymers	61-68	insulin receptor	Homo sapiens	52-60
35065520-1	2022	In case of thin films of siloxane obtained from different organo-silane derivatives (alkoxy and chloro) on soda lime silica glass substrates, IR-ATR and IR-SR could not detect the organic functional groups of the coating.	Siloxanes	25-33	insulin receptor	Homo sapiens	142-144
35457152-3	2022	Insulin resistance in this group of patients results from defects at the molecular level, including impaired insulin receptor-related signaling pathways enhanced by obesity and its features: Excess visceral fat, chronic inflammation, and reactive oxygen species.	Oxygen	247-253	insulin receptor	Homo sapiens	109-125
35065520-1	2022	In case of thin films of siloxane obtained from different organo-silane derivatives (alkoxy and chloro) on soda lime silica glass substrates, IR-ATR and IR-SR could not detect the organic functional groups of the coating.	Siloxanes	25-33	insulin receptor	Homo sapiens	153-155
35014128-4	2022	Spironolactone therapy was triggered by the detection of subclinical LVD (GLS <=16% or diastolic abnormalities (at least one of E/e">15, E/e" >10 with left atrial enlargement (LAE) or impaired relaxation (E/A <0.8, IR), LAE with IR), or borderline GLS (17%) with IR or borderline GLS with LAE.	Spironolactone	0-14	insulin receptor	Homo sapiens	215-217
35450409-3	2022	In addition to the direct association between I-R and the release of reactive oxygen species and reactive nitrogen species, it is involved in developing mitochondrial oxidative damage.	oxygen species	78-92	insulin receptor	Homo sapiens	46-49
35450409-3	2022	In addition to the direct association between I-R and the release of reactive oxygen species and reactive nitrogen species, it is involved in developing mitochondrial oxidative damage.	Nitrogen	106-114	insulin receptor	Homo sapiens	46-49
35456670-5	2022	Our main goal, however, is to intensively investigate whether this relatively simple polymer may find applications in protecting against ionizing radiation (IR) or for therapy in cases of radiation-induced damage.	Polymers	85-92	insulin receptor	Homo sapiens	157-159
35014128-4	2022	Spironolactone therapy was triggered by the detection of subclinical LVD (GLS <=16% or diastolic abnormalities (at least one of E/e">15, E/e" >10 with left atrial enlargement (LAE) or impaired relaxation (E/A <0.8, IR), LAE with IR), or borderline GLS (17%) with IR or borderline GLS with LAE.	Spironolactone	0-14	insulin receptor	Homo sapiens	229-231
35014128-4	2022	Spironolactone therapy was triggered by the detection of subclinical LVD (GLS <=16% or diastolic abnormalities (at least one of E/e">15, E/e" >10 with left atrial enlargement (LAE) or impaired relaxation (E/A <0.8, IR), LAE with IR), or borderline GLS (17%) with IR or borderline GLS with LAE.	Spironolactone	0-14	insulin receptor	Homo sapiens	263-265
35346008-10	2022	Several heterogeneous conditions that share the occurrence of insulin resistance, such as aging, obesity, acromegaly, lipodystrophy, cystic fibrosis, insulin receptor dysfunction, and Alstrom syndrome, also share both clinical and structural manifestations of kidney disease, including glomerulomegaly and other features of DKD, focal segmental glomerulosclerosis, and C3 glomerulopathy, which might be ascribed to reduction in the synthesis of factor H binding sites (such as heparan sulfate) that leads to uncontrolled complement activation.	Heparitin Sulfate	477-492	insulin receptor	Homo sapiens	150-166
35073186-10	2022	Conclusions: We developed a simple and affordable method of identifying IR in children with overweight or OB based on anthropometric variables and routine blood tests for metabolic indicators, such as glucose and triglycerides, which can be implemented in underserved sites.	Glucose	201-208	insulin receptor	Homo sapiens	72-74
35073186-10	2022	Conclusions: We developed a simple and affordable method of identifying IR in children with overweight or OB based on anthropometric variables and routine blood tests for metabolic indicators, such as glucose and triglycerides, which can be implemented in underserved sites.	Triglycerides	213-226	insulin receptor	Homo sapiens	72-74
35193378-3	2022	Methods: To define the mechanisms by which insulin controls plasma cholesterol levels, we knocked down the insulin receptor, FoxO1, and the key bile acid synthesis enzyme, CYP8B1.	Cholesterol	67-78	insulin receptor	Homo sapiens	107-123
35228371-5	2022	It has been shown that GM3 regulates the signal transduction of insulin receptor in adipose tissue as a component of membrane microdomains, and elevation in GM3 level causes insulin resistance.	gm3	23-26	insulin receptor	Homo sapiens	64-80
35434067-4	2022	CASE SUMMARY: We present the rare case of a female patient aged 11 years and 9 mo with type A insulin resistance and an INSR heterozygous mutation (c.3614C>T), who was treated with a combination of pioglitazone and flutamide.	Pioglitazone	198-210	insulin receptor	Homo sapiens	120-124
35434067-4	2022	CASE SUMMARY: We present the rare case of a female patient aged 11 years and 9 mo with type A insulin resistance and an INSR heterozygous mutation (c.3614C>T), who was treated with a combination of pioglitazone and flutamide.	Flutamide	215-224	insulin receptor	Homo sapiens	120-124
35241773-0	2022	Membrane extraction with styrene-maleic acid copolymer results in insulin receptor autophosphorylation in the absence of ligand.	Styrene	25-32	insulin receptor	Homo sapiens	66-82
35241773-0	2022	Membrane extraction with styrene-maleic acid copolymer results in insulin receptor autophosphorylation in the absence of ligand.	maleic acid copolymer	33-54	insulin receptor	Homo sapiens	66-82
35241773-3	2022	Here we report the first functional investigation of the mammalian insulin receptor which was extracted from cell membranes using poly(styrene-co-maleic acid).	styrene-maleic acid polymer	130-158	insulin receptor	Homo sapiens	67-83
35241773-5	2022	Surprisingly, activation of the insulin receptor and proximal downstream signalling was detected upon copolymer extraction even in the absence of insulin stimulation.	copolymer	102-111	insulin receptor	Homo sapiens	32-48
35217681-7	2022	We validate putative targets for therapy ex vivo and identify potential combination treatments, such as the inhibition of the INSR/IGF-1R axis to increase the sensitivity to dasatinib treatment.	Dasatinib	174-183	insulin receptor	Homo sapiens	126-130
35147164-2	2022	Signals from the occupied insulin receptor are translated into downstream signalling changes in serine/threonine kinases within timescales of seconds, and this is followed by delivery and accumulation of the glucose transporter GLUT4 at the plasma membrane.	Serine	96-102	insulin receptor	Homo sapiens	26-42
35000900-6	2022	Metformin may have a role in the treatment of type A insulin resistance syndrome due to heterozygous mutation of the INSR gene.	Metformin	0-9	insulin receptor	Homo sapiens	117-121
35074429-0	2022	The P300 acetyltransferase inhibitor C646 promotes membrane translocation of insulin receptor protein substrate and interaction with the insulin receptor.	C646	37-41	insulin receptor	Homo sapiens	77-93
35074429-0	2022	The P300 acetyltransferase inhibitor C646 promotes membrane translocation of insulin receptor protein substrate and interaction with the insulin receptor.	C646	37-41	insulin receptor	Homo sapiens	137-153
35074429-5	2022	Inhibition of P300 acetyltransferase activity by C646 drastically increased tyrosine phosphorylation of the insulin receptor protein substrates (IRS1/2) without affecting the tyrosine phosphorylation of the beta subunit of the insulin receptor (IRbeta) in hepatocytes in the absence of insulin.	C646	49-53	insulin receptor	Homo sapiens	108-124
35074429-5	2022	Inhibition of P300 acetyltransferase activity by C646 drastically increased tyrosine phosphorylation of the insulin receptor protein substrates (IRS1/2) without affecting the tyrosine phosphorylation of the beta subunit of the insulin receptor (IRbeta) in hepatocytes in the absence of insulin.	Tyrosine	76-84	insulin receptor	Homo sapiens	108-124
35476887-1	2022	OBJECTIVE: Evaluate the pupillary-constricting effects following administration of buprenorphine buccal film (BBF) and immediate-release (IR) oxycodone.	Oxycodone	142-151	insulin receptor	Homo sapiens	138-140
35157107-5	2022	RESULTS: Oleic acid (OA, 100 microM) was shown to down regulate expression of the insulin receptor, PTEN and a PI3K catalytic (p110beta) and regulatory (p85alpha) subunit compared to palmitic, linoleic and stearic acids (P < 0.04), and promote greater eNOS phosphorylation at Ser1177.	Oleic Acid	9-19	insulin receptor	Homo sapiens	82-98
35223937-7	2021	In addition, we illustrated our cellular and molecular model consisting of studying the functional activity of CM fractions on IR and its downstream signaling pathways in the hepatocarcinoma (HepG2) and the human embryonic kidney (HEK293) cells using the bioluminescence resonance energy transfer (BRET), phosphorylation, and glucose uptake assays.	Glucose	326-333	insulin receptor	Homo sapiens	127-129
35223937-8	2021	Overall, our work demonstrated for the first time that CM lactoferrin and CM-derived bioactive peptides positively modulate IR and its related signaling pathways in HepG2 and HEK293 cells.	Cm	74-76	insulin receptor	Homo sapiens	124-126
35223937-9	2021	As a conclusion, the pharmacological targeting of IR by CM sheds more light on the antidiabetic properties of CM by providing its molecular basis that may constitute a solid rationale for the development of new generation of antidiabetic tools from CM-derived proteins and peptides and the utilization of CM in the management of diabetes.	Cm	56-58	insulin receptor	Homo sapiens	50-52
35223937-9	2021	As a conclusion, the pharmacological targeting of IR by CM sheds more light on the antidiabetic properties of CM by providing its molecular basis that may constitute a solid rationale for the development of new generation of antidiabetic tools from CM-derived proteins and peptides and the utilization of CM in the management of diabetes.	Cm	110-112	insulin receptor	Homo sapiens	50-52
35223937-9	2021	As a conclusion, the pharmacological targeting of IR by CM sheds more light on the antidiabetic properties of CM by providing its molecular basis that may constitute a solid rationale for the development of new generation of antidiabetic tools from CM-derived proteins and peptides and the utilization of CM in the management of diabetes.	Cm	305-307	insulin receptor	Homo sapiens	50-52
35095765-13	2021	Conclusions: There were several independent factors associated with IR in patients with chronic HCV infection, including obesity, treatment experience, high serum ALT and triglyceride levels, as well as advanced hepatic fibrosis.	Triglycerides	171-183	insulin receptor	Homo sapiens	68-70
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Prednisolone	15-27	insulin receptor	Homo sapiens	170-186
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Prednisolone	29-32	insulin receptor	Homo sapiens	170-186
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Mycophenolic Acid	35-56	insulin receptor	Homo sapiens	170-186
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Mycophenolic Acid	58-61	insulin receptor	Homo sapiens	170-186
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Tacrolimus	68-78	insulin receptor	Homo sapiens	170-186
34651654-4	2022	Treatment with prednisolone (PSL), mycophenolate mofetil (MMF), and tacrolimus (TAC) resulted in improved SLE activity and glucose intolerance with the reduction of anti-insulin receptor autoantibodies.	Tacrolimus	80-83	insulin receptor	Homo sapiens	170-186
35228371-5	2022	It has been shown that GM3 regulates the signal transduction of insulin receptor in adipose tissue as a component of membrane microdomains, and elevation in GM3 level causes insulin resistance.	gm3	157-160	insulin receptor	Homo sapiens	64-80
35355907-9	2021	Significant results were observed in rs1799817 single nucleotide polymorphisms (SNP) of INSR with elevated levels of triglycerides and rs10818854 of DENND1A, rs13429458 of THADA, rs2349415 of FSHR with the high levels of DHEAS.	Triglycerides	117-130	insulin receptor	Homo sapiens	88-92
35355907-9	2021	Significant results were observed in rs1799817 single nucleotide polymorphisms (SNP) of INSR with elevated levels of triglycerides and rs10818854 of DENND1A, rs13429458 of THADA, rs2349415 of FSHR with the high levels of DHEAS.	Dehydroepiandrosterone Sulfate	221-226	insulin receptor	Homo sapiens	88-92
35230100-4	2022	QD-shuttle complexes photocatalyze homo- and heterointermolecular (2 + 2) photocycloadditions of benzalacetone, chalcone and its derivatives with up to 94% yield; the yields for all reactions are comparable to those achieved by Ir(ppy)3 but with the advantages of a factor of 2.5 lower catalyst loading, superior stability, and the ability to recover the catalyst by simple centrifugation and reuse it for multiple reaction cycles.	benzylideneacetone	97-110	insulin receptor	Homo sapiens	228-236
35230100-4	2022	QD-shuttle complexes photocatalyze homo- and heterointermolecular (2 + 2) photocycloadditions of benzalacetone, chalcone and its derivatives with up to 94% yield; the yields for all reactions are comparable to those achieved by Ir(ppy)3 but with the advantages of a factor of 2.5 lower catalyst loading, superior stability, and the ability to recover the catalyst by simple centrifugation and reuse it for multiple reaction cycles.	Chalcone	112-120	insulin receptor	Homo sapiens	228-236
2558650-5	1989	We previously demonstrated that insulin receptor gene expression in human cell lines in enhanced by glucose.	Glucose	100-107	insulin receptor	Homo sapiens	32-48
35225010-8	2022	High glucose can influence on GBM progression through the promotion of the following parameters: cell viability, dispersal, InsR expression and cell proliferation (Ki-67).	Glucose	5-12	insulin receptor	Homo sapiens	124-128
2557012-12	1989	Poly(L-lysine) activates the insulin receptor kinase by increasing the Vmax.	poly(l-lysine	0-13	insulin receptor	Homo sapiens	29-45
2557012-14	1989	Poly(L-lysine) markedly stimulates the kinase activity of insulin receptor preparations that have lost both basal kinase activity and the ability to be stimulated by insulin.	poly(l-lysine	0-13	insulin receptor	Homo sapiens	58-74
2583100-3	1989	Stimulation of these cells with EGF induced tyrosine autophosphorylation of the EGF-insulin receptor chimera (150 kd) and tyrosine phosphorylation of the beta-subunit of the kinase-deficient insulin receptor (95 kd).	Tyrosine	44-52	insulin receptor	Homo sapiens	84-100
2583100-5	1989	When immunoaffinity purified EGF-insulin receptor hybrids and kinase-deficient insulin receptors were used in a cell lysate phosphorylation assay, it was found that addition of EGF produced 32P-labeling of both receptor species.	Phosphorus-32	190-193	insulin receptor	Homo sapiens	33-49
2551760-9	1989	However, IGF-I stimulates glucose transport predominantly by interacting with the insulin receptor.	Glucose	26-33	insulin receptor	Homo sapiens	82-98
2552437-0	1989	In vitro tyrosine phosphorylation studies on RAS proteins and calmodulin suggest that polylysine-like basic peptides or domains may be involved in interactions between insulin receptor kinase and its substrate.	Tyrosine	9-17	insulin receptor	Homo sapiens	168-184
2676896-4	1989	Cells enriched with docosahexaenoic acid show an increase in insulin binding at 15 degrees C that is due to an increase in the number of available insulin receptor sites on the plasma membrane.	Docosahexaenoic Acids	20-40	insulin receptor	Homo sapiens	147-163
2552266-3	1989	Affinity cross-linking study revealed that molecular weight of the insulin receptor was 210 kDa and that it could not be dissociated to alpha- and beta-subunit with dithiothreitol treatment.	Dithiothreitol	165-179	insulin receptor	Homo sapiens	67-83
2552437-1	1989	We have investigated the in vitro tyrosine phosphorylation of the HRAS and KRAS proteins by human placental insulin receptor kinase.	Tyrosine	34-42	insulin receptor	Homo sapiens	108-124
2552437-3	1989	Since the tyrosine phosphorylation of calmodulin by the insulin receptor kinase in vitro requires cofactors such as protamine and poly(L-lysine), we examined the possibility that poly(L-lysine) may also potentiate the interaction between RAS proteins and the insulin receptor.	Tyrosine	10-18	insulin receptor	Homo sapiens	56-72
2552437-3	1989	Since the tyrosine phosphorylation of calmodulin by the insulin receptor kinase in vitro requires cofactors such as protamine and poly(L-lysine), we examined the possibility that poly(L-lysine) may also potentiate the interaction between RAS proteins and the insulin receptor.	poly(l-lysine	130-143	insulin receptor	Homo sapiens	56-72
2552437-3	1989	Since the tyrosine phosphorylation of calmodulin by the insulin receptor kinase in vitro requires cofactors such as protamine and poly(L-lysine), we examined the possibility that poly(L-lysine) may also potentiate the interaction between RAS proteins and the insulin receptor.	poly(l-lysine)	130-144	insulin receptor	Homo sapiens	56-72
2552437-4	1989	We found that purified HRAS proteins are indeed phosphorylated by purified insulin receptor kinase in the presence of poly(L-lysine).	poly(l-lysine)	118-132	insulin receptor	Homo sapiens	75-91
2552437-7	1989	Further examination of the role of poly(L-lysine) in potentiating tyrosine phosphorylation of the HRAS protein and calmodulin by purified insulin receptor kinase indicates that poly(L-lysine) affects the conformation of these protein substrates as well as that of the receptor kinase domain.	poly(l-lysine)	35-49	insulin receptor	Homo sapiens	138-154
2552437-7	1989	Further examination of the role of poly(L-lysine) in potentiating tyrosine phosphorylation of the HRAS protein and calmodulin by purified insulin receptor kinase indicates that poly(L-lysine) affects the conformation of these protein substrates as well as that of the receptor kinase domain.	Tyrosine	66-74	insulin receptor	Homo sapiens	138-154
2552437-7	1989	Further examination of the role of poly(L-lysine) in potentiating tyrosine phosphorylation of the HRAS protein and calmodulin by purified insulin receptor kinase indicates that poly(L-lysine) affects the conformation of these protein substrates as well as that of the receptor kinase domain.	poly(l-lysine)	177-191	insulin receptor	Homo sapiens	138-154
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Threonine	107-110	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Cysteine	111-114	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Tyrosine	127-130	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Tyrosine	131-134	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Histidine	135-138	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Phenylalanine	139-142	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Glutamine	143-146	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Aspartic Acid	147-150	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Threonine	154-157	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Cysteine	158-161	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Tyrosine	131-134	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Tyrosine	131-134	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Aspartic Acid	182-185	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Phenylalanine	186-189	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Glutamine	190-193	insulin receptor	Homo sapiens	32-48
2550426-7	1989	We have now constructed a human insulin receptor mutant in which 3 residues in this sequence were altered (Thr-Cys-Pro-Pro-Pro-Tyr-Tyr-His-Phe-Gln-Asp to Thr-Cys-Pro-Arg-Arg-Tyr-Tyr-Asp-Phe-Gln-Asp) and have expressed this mutant in rat hepatoma (HTC) cells.	Aspartic Acid	182-185	insulin receptor	Homo sapiens	32-48
2569023-4	1989	In contrast, insulin receptor autophosphorylation in 1% Triton X-100 cell lysates was reduced in both patients and parents.	Octoxynol	56-68	insulin receptor	Homo sapiens	13-29
2504716-8	1989	Surprisingly, the insulin-independent activated (1 min in vivo insulin-treated) and uncoupled (24 h in vivo insulin-treated) insulin receptors displayed similar stoichiometries of 32P incorporation into the beta subunit by in vitro autophosphorylation when compared with the control insulin receptors, ranging from 1.5 to 1.8 mol of phosphate incorporated/mol of insulin receptor.	Phosphates	333-342	insulin receptor	Homo sapiens	125-141
2479553-0	1989	A leucine-to-proline mutation in the insulin receptor in a family with insulin resistance.	Leucine	2-9	insulin receptor	Homo sapiens	37-53
2479553-0	1989	A leucine-to-proline mutation in the insulin receptor in a family with insulin resistance.	Proline	13-20	insulin receptor	Homo sapiens	37-53
2697986-8	1989	The mature insulin receptor is inserted into the plasma membrane as an alpha 2-beta 2 disulfide-linked heterodimer.	Disulfides	86-95	insulin receptor	Homo sapiens	11-27
2753889-1	1989	Recently, we have described a COOH-terminal deletion mutation of the human insulin receptor (HIR delta CT) that exhibits normal insulin-mediated kinase activity and endocytosis, but is inefficient in stimulating glucose transport and glycogen synthase (McClain, D. A., Maegawa, H., Levy, J., Huecksteadt, T., Dull, T. J., Lee, J., Ullrich, A., and Olefsky, J.M.	Glucose	212-219	insulin receptor	Homo sapiens	75-91
2546561-5	1989	Similarly, insulin receptor tyrosine kinase as assessed by receptor autophosphorylation and phosphorylation of the substrate poly-(Glu/Tyr) was not fully activated by treatment of cells with the insulin dimer (31 and 42% of the effect of insulin, respectively) in concentrations which maximally activate glucose transport and give rise to full insulin receptor occupancy (5 X 10(-7) M).	poly-	125-130	insulin receptor	Homo sapiens	11-27
2546561-5	1989	Similarly, insulin receptor tyrosine kinase as assessed by receptor autophosphorylation and phosphorylation of the substrate poly-(Glu/Tyr) was not fully activated by treatment of cells with the insulin dimer (31 and 42% of the effect of insulin, respectively) in concentrations which maximally activate glucose transport and give rise to full insulin receptor occupancy (5 X 10(-7) M).	Glutamic Acid	131-134	insulin receptor	Homo sapiens	11-27
2546561-5	1989	Similarly, insulin receptor tyrosine kinase as assessed by receptor autophosphorylation and phosphorylation of the substrate poly-(Glu/Tyr) was not fully activated by treatment of cells with the insulin dimer (31 and 42% of the effect of insulin, respectively) in concentrations which maximally activate glucose transport and give rise to full insulin receptor occupancy (5 X 10(-7) M).	Tyrosine	135-138	insulin receptor	Homo sapiens	11-27
2546561-5	1989	Similarly, insulin receptor tyrosine kinase as assessed by receptor autophosphorylation and phosphorylation of the substrate poly-(Glu/Tyr) was not fully activated by treatment of cells with the insulin dimer (31 and 42% of the effect of insulin, respectively) in concentrations which maximally activate glucose transport and give rise to full insulin receptor occupancy (5 X 10(-7) M).	Glucose	304-311	insulin receptor	Homo sapiens	11-27
2472386-8	1989	As predicted from the single deletion analogs [1-27,Gly4,38-62]hIGF-I has reduced affinity for the type 1 IGF receptor (approximately 40-fold) and increased affinity for the insulin receptor (5-fold).	glycyl-glycyl-glycyl-glycine	52-56	insulin receptor	Homo sapiens	174-190
2736256-2	1989	The two PTKs phosphorylated poly(Glu: Tyr; 4:1) very effectively with apparent Km values of 0.3 mg/ml for insulin receptor PTK and 0.8 mg/ml for lung PTK.	poly	28-32	insulin receptor	Homo sapiens	106-122
2786417-0	1989	Induction of the insulin receptor and other differentiation markers by sodium butyrate in the Burkitt lymphoma cell, Raji.	Butyric Acid	71-86	insulin receptor	Homo sapiens	17-33
2653318-1	1989	The insulin receptor is synthesized as a single chain, 190 kDa glycoprotein precursor, which undergoes proteolytic cleavage, carbohydrate processing, and fatty acylation to generate the mature receptor on the plasma membrane.	Carbohydrates	125-137	insulin receptor	Homo sapiens	4-20
2472754-5	1989	To determine the usefulness of thin-layer chromatography in phosphoamino acid analysis, the propionic acid/ammonium hydroxide/isopropyl alcohol solution was used to characterize phosphorylated residues in a plasma membrane protein which is a substrate for the insulin receptor kinase, in insulin receptor phosphorylated histone H2B, and in an in vivo phosphorylated 90000-Da protein from IM9 cells.	propionic acid	92-106	insulin receptor	Homo sapiens	260-276
2472754-5	1989	To determine the usefulness of thin-layer chromatography in phosphoamino acid analysis, the propionic acid/ammonium hydroxide/isopropyl alcohol solution was used to characterize phosphorylated residues in a plasma membrane protein which is a substrate for the insulin receptor kinase, in insulin receptor phosphorylated histone H2B, and in an in vivo phosphorylated 90000-Da protein from IM9 cells.	propionic acid	92-106	insulin receptor	Homo sapiens	288-304
2472754-6	1989	32P-labeled proteins were separated by dodecyl sulfate-gel electrophoresis, digested with trypsin, and then hydrolyzed with 6 N HCl, 2 h, 110 degrees C. Following thin-layer chromatography of the hydrolyzates and autoradiography, phosphotyrosine was detected in insulin receptor substrates, and phosphoserine and phosphothreonine were found in the in vivo-phosphorylated protein.	Phosphorus-32	0-3	insulin receptor	Homo sapiens	262-278
2465763-0	1989	Binding to GDP-agarose identifies a novel 60kDa substrate for the insulin receptor tyrosyl kinase in mouse NIH-3T3 cells expressing high concentrations of the human insulin receptor.	gdp-agarose	11-22	insulin receptor	Homo sapiens	165-181
2465763-1	1989	Insulin increased dramatically the tyrosyl phosphorylation of the insulin receptor beta-subunit in mouse NIH-3T3 fibroblasts transfected with the human insulin receptor.	cyclo(tyrosyl-tyrosyl)	35-42	insulin receptor	Homo sapiens	152-168
2644147-5	1989	Regardless of whether the enzyme enters the cell via the insulin receptor or via the low-density lipoprotein (ApoB) receptor, it can be found associated with a lysosomal fraction and is effective in lowering levels of accumulated substrate, cholesteryl ester.	Cholesterol Esters	241-258	insulin receptor	Homo sapiens	57-73
2732294-2	1989	Uniformly labeled [32P]antisense RNA probes complementary to insulin receptor mRNA were prepared by an SP6 or T7 RNA polymerase transcription reaction.	Phosphorus-32	19-22	insulin receptor	Homo sapiens	61-77
2669959-10	1989	Mild reduction of the insulin receptor preparation with dithiothreitol (DTT) activated the total kinase activity by 3.5-fold.	Dithiothreitol	56-70	insulin receptor	Homo sapiens	22-38
2669959-10	1989	Mild reduction of the insulin receptor preparation with dithiothreitol (DTT) activated the total kinase activity by 3.5-fold.	Dithiothreitol	72-75	insulin receptor	Homo sapiens	22-38
2543399-0	1989	Effect of two different glucose concentrations on insulin receptor mRNA levels in human hepatoma HepG2 cells.	Glucose	24-31	insulin receptor	Homo sapiens	50-66
2543399-3	1989	Insulin receptor mRNA levels and insulin binding activity were reduced in HepG2 cultured at lower glucose concentrations.	Glucose	98-105	insulin receptor	Homo sapiens	0-16
2543399-4	1989	These data suggest that glucose affects insulin receptor gene expression.	Glucose	24-31	insulin receptor	Homo sapiens	40-56
2719663-12	1989	Furthermore, treatment with trypsin of intact Chinese hamster ovary cells that overexpress the human insulin receptor stimulates both autophosphorylation of the receptor and 2-deoxyglucose uptake into the cells, but does not enhance receptor internalization.	Deoxyglucose	174-188	insulin receptor	Homo sapiens	101-117
2649887-5	1989	Microinjection of a monoclonal antibody directed against the tyrosine kinase domain of the human insulin receptor blocks activation of hexose uptake by insulin-like growth factor I and insulin but has no effect on basal uptake.	Hexoses	135-141	insulin receptor	Homo sapiens	97-113
2658681-8	1989	Definitive identification of labeled phosphoserine residues in histone, phosphoserine and phosphothreonine residues in myelin basic protein and insulin receptor, and phosphotyrosine residues in autophosphorylated insulin receptor was accomplished with as little as 0.2 nCi in about 50 ng of phosphorylated protein.	Phosphoserine	37-50	insulin receptor	Homo sapiens	144-160
2658681-8	1989	Definitive identification of labeled phosphoserine residues in histone, phosphoserine and phosphothreonine residues in myelin basic protein and insulin receptor, and phosphotyrosine residues in autophosphorylated insulin receptor was accomplished with as little as 0.2 nCi in about 50 ng of phosphorylated protein.	Phosphothreonine	90-106	insulin receptor	Homo sapiens	144-160
2658681-8	1989	Definitive identification of labeled phosphoserine residues in histone, phosphoserine and phosphothreonine residues in myelin basic protein and insulin receptor, and phosphotyrosine residues in autophosphorylated insulin receptor was accomplished with as little as 0.2 nCi in about 50 ng of phosphorylated protein.	Phosphotyrosine	166-181	insulin receptor	Homo sapiens	213-229
2546845-5	1989	After corticoids and immunosuppressive therapy by azathioprine, the patient hypoglycaemic episodes disappeared, and concomitantly, the antibodies to insulin receptor were no longer detected, as judged by both immunoprecipitation of insulin receptor and stimulation of glucose transport.	Glucose	268-275	insulin receptor	Homo sapiens	149-165
2645866-6	1989	In conclusion, the substitution of the specificity of tyrosine kinase of the insulin receptor with that of the v-ros oncogene product results in defective internalization and degradation of insulin, and loss of ligand-induced receptor internalization.	ros	56-59	insulin receptor	Homo sapiens	77-93
2653432-1	1989	Properties of oligomeric states of the insulin receptor were analyzed by polyacrylamide gel electrophoresis in nondenaturing buffer conditions (ND-PAGE).	polyacrylamide	73-87	insulin receptor	Homo sapiens	39-55
2736256-2	1989	The two PTKs phosphorylated poly(Glu: Tyr; 4:1) very effectively with apparent Km values of 0.3 mg/ml for insulin receptor PTK and 0.8 mg/ml for lung PTK.	Glutamic Acid	33-36	insulin receptor	Homo sapiens	106-122
2736256-2	1989	The two PTKs phosphorylated poly(Glu: Tyr; 4:1) very effectively with apparent Km values of 0.3 mg/ml for insulin receptor PTK and 0.8 mg/ml for lung PTK.	Tyrosine	38-41	insulin receptor	Homo sapiens	106-122
2695195-4	1989	In the latter patient, the dissociation observed between glucose and potassium transport suggests several manners of differential impairment of insulin action and/or steps distal to the insulin receptor as being responsible for insulin resistance.	Potassium	69-78	insulin receptor	Homo sapiens	186-202
2722129-6	1989	MC-51, a highly specific monoclonal antibody for the insulin receptor, inhibited the stimulation of [3H]thymidine incorporation by 25 ng/ml of insulin.	mc-51	0-5	insulin receptor	Homo sapiens	53-69
2722129-6	1989	MC-51, a highly specific monoclonal antibody for the insulin receptor, inhibited the stimulation of [3H]thymidine incorporation by 25 ng/ml of insulin.	Tritium	101-103	insulin receptor	Homo sapiens	53-69
2722129-6	1989	MC-51, a highly specific monoclonal antibody for the insulin receptor, inhibited the stimulation of [3H]thymidine incorporation by 25 ng/ml of insulin.	Thymidine	104-113	insulin receptor	Homo sapiens	53-69
2650737-8	1989	Here, we provide evidence that a polyclonal antibody, raised against the human insulin receptor, can restore the receptor-mediated stimulation of glycogen synthesis that was abolished by the mutation.	Glycogen	146-154	insulin receptor	Homo sapiens	79-95
2464505-0	1989	Characterization of sites of serine phosphorylation in human placental insulin receptor copurified with insulin-stimulated serine kinase activity by two-dimensional thin-layer peptide mapping.	Serine	29-35	insulin receptor	Homo sapiens	71-87
2464505-1	1989	Insulin receptor was copurified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues.	Serine	145-151	insulin receptor	Homo sapiens	0-16
2464505-1	1989	Insulin receptor was copurified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues.	Serine	145-151	insulin receptor	Homo sapiens	125-141
2464505-2	1989	Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin.	Peptides	71-78	insulin receptor	Homo sapiens	27-43
2464505-2	1989	Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin.	Peptides	71-78	insulin receptor	Homo sapiens	157-173
2464505-2	1989	Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin.	Serine	127-133	insulin receptor	Homo sapiens	27-43
2464505-2	1989	Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin.	Serine	127-133	insulin receptor	Homo sapiens	157-173
2464505-2	1989	Analysis of phosphorylated insulin receptor by two-dimensional tryptic peptide mapping showed that sites of insulin stimulated serine phosphorylation in the insulin receptor were recovered in the same peptides as those known to be phosphorylated on serine in vivo in response to insulin.	Serine	249-255	insulin receptor	Homo sapiens	157-173
2464505-3	1989	This indicates that the serine kinase copurified with the insulin receptor represents a physiologically important enzyme involved in the insulin triggered serine phosphorylation of the insulin receptor in vivo.	Serine	24-30	insulin receptor	Homo sapiens	58-74
2464505-3	1989	This indicates that the serine kinase copurified with the insulin receptor represents a physiologically important enzyme involved in the insulin triggered serine phosphorylation of the insulin receptor in vivo.	Serine	24-30	insulin receptor	Homo sapiens	185-201
2911561-8	1989	Comparison of the exon structure of the tyrosine kinase domain of the INSR with the corresponding regions of the human SRC, ROS, and ERBB2 (NGL) protooncogenes indicates that the exon-intron organization of this region has not been well conserved.	ros	124-127	insulin receptor	Homo sapiens	70-74
2534941-0	1989	Serine phosphorylations triggered by the insulin receptor.	Serine	0-6	insulin receptor	Homo sapiens	41-57
2701772-0	1989	[Metal ions in the insulin-receptor interaction in human erythrocytes].	Metals	1-6	insulin receptor	Homo sapiens	19-35
3066348-1	1988	UNLABELLED: Recently it was speculated that activation of GTP-binding proteins and of phospholipase is involved in the transmission of a signal from the insulin-receptor kinase to effector systems in the cell.	Guanosine Triphosphate	58-61	insulin receptor	Homo sapiens	153-169
2537240-1	1989	The regulation of the insulin receptor by cAMP has been examined in glial C6 cells.	Cyclic AMP	42-46	insulin receptor	Homo sapiens	22-38
2701772-7	1989	These results suggest the possible involvement of a metal ion associated to the receptor in the formation of the insulin-receptor complex.	Metals	52-57	insulin receptor	Homo sapiens	113-129
2972576-8	1988	These results indicate that 1) the defect is specific to the insulin-receptor binding in these patients, 2) insulin and IGF-I activate glucose incorporation and alpha-aminoisobutyric acid uptake mainly through their own specific receptors, but 3) the IGF-I receptor appears to have a more important role in stimulating thymidine incorporation than the insulin receptor in physiological condition or, alternatively, an unknown postreceptor process with cascade signal transmission may overcome the decreased insulin-receptor binding to produce a normal dose-response curve.	Glucose	135-142	insulin receptor	Homo sapiens	61-77
2849108-0	1988	ATP sensitizes the insulin receptor to insulin.	Adenosine Triphosphate	0-3	insulin receptor	Homo sapiens	19-35
2972576-8	1988	These results indicate that 1) the defect is specific to the insulin-receptor binding in these patients, 2) insulin and IGF-I activate glucose incorporation and alpha-aminoisobutyric acid uptake mainly through their own specific receptors, but 3) the IGF-I receptor appears to have a more important role in stimulating thymidine incorporation than the insulin receptor in physiological condition or, alternatively, an unknown postreceptor process with cascade signal transmission may overcome the decreased insulin-receptor binding to produce a normal dose-response curve.	Glucose	135-142	insulin receptor	Homo sapiens	352-368
2972576-8	1988	These results indicate that 1) the defect is specific to the insulin-receptor binding in these patients, 2) insulin and IGF-I activate glucose incorporation and alpha-aminoisobutyric acid uptake mainly through their own specific receptors, but 3) the IGF-I receptor appears to have a more important role in stimulating thymidine incorporation than the insulin receptor in physiological condition or, alternatively, an unknown postreceptor process with cascade signal transmission may overcome the decreased insulin-receptor binding to produce a normal dose-response curve.	Glucose	135-142	insulin receptor	Homo sapiens	507-523
2972576-8	1988	These results indicate that 1) the defect is specific to the insulin-receptor binding in these patients, 2) insulin and IGF-I activate glucose incorporation and alpha-aminoisobutyric acid uptake mainly through their own specific receptors, but 3) the IGF-I receptor appears to have a more important role in stimulating thymidine incorporation than the insulin receptor in physiological condition or, alternatively, an unknown postreceptor process with cascade signal transmission may overcome the decreased insulin-receptor binding to produce a normal dose-response curve.	2-aminoisobutyric acid	161-187	insulin receptor	Homo sapiens	61-77
2972576-8	1988	These results indicate that 1) the defect is specific to the insulin-receptor binding in these patients, 2) insulin and IGF-I activate glucose incorporation and alpha-aminoisobutyric acid uptake mainly through their own specific receptors, but 3) the IGF-I receptor appears to have a more important role in stimulating thymidine incorporation than the insulin receptor in physiological condition or, alternatively, an unknown postreceptor process with cascade signal transmission may overcome the decreased insulin-receptor binding to produce a normal dose-response curve.	Thymidine	319-328	insulin receptor	Homo sapiens	61-77
3255363-2	1988	Changes in insulin receptor number, affinity and mRNA levels were observed when HL60 cells were induced to differentiate with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) or dimethylsulphoxide (DMSO).	Tetradecanoylphorbol Acetate	126-163	insulin receptor	Homo sapiens	11-27
2975946-1	1988	Insulin receptor was co-purified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues.	Serine	146-152	insulin receptor	Homo sapiens	0-16
2975946-1	1988	Insulin receptor was co-purified from human placenta together with insulin-stimulated kinase activity that phosphorylates the insulin receptor on serine residues.	Serine	146-152	insulin receptor	Homo sapiens	126-142
2975946-4	1988	Additionally, direct stimulation of the receptor tyrosine kinase by vanadate increased serine phosphorylation of the insulin receptor.	Vanadates	68-76	insulin receptor	Homo sapiens	117-133
2975946-4	1988	Additionally, direct stimulation of the receptor tyrosine kinase by vanadate increased serine phosphorylation of the insulin receptor.	Serine	87-93	insulin receptor	Homo sapiens	117-133
2975946-5	1988	Insulin-stimulated tyrosine phosphorylation preceded insulin-stimulated serine phosphorylation of the insulin receptor.	Tyrosine	19-27	insulin receptor	Homo sapiens	102-118
2975946-5	1988	Insulin-stimulated tyrosine phosphorylation preceded insulin-stimulated serine phosphorylation of the insulin receptor.	Serine	72-78	insulin receptor	Homo sapiens	102-118
3255363-2	1988	Changes in insulin receptor number, affinity and mRNA levels were observed when HL60 cells were induced to differentiate with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) or dimethylsulphoxide (DMSO).	Tetradecanoylphorbol Acetate	165-168	insulin receptor	Homo sapiens	11-27
3255363-2	1988	Changes in insulin receptor number, affinity and mRNA levels were observed when HL60 cells were induced to differentiate with 12-O-tetradecanoyl-phorbol-13-acetate (TPA) or dimethylsulphoxide (DMSO).	Dimethyl Sulfoxide	173-191	insulin receptor	Homo sapiens	11-27
3255363-3	1988	Total and high-affinity insulin receptor numbers decreased following treatment of HL60 cells with DMSO, whereas total insulin receptor number increased and high-affinity receptor number decreased in cells treated with TPA.	Dimethyl Sulfoxide	98-102	insulin receptor	Homo sapiens	24-40
3255363-3	1988	Total and high-affinity insulin receptor numbers decreased following treatment of HL60 cells with DMSO, whereas total insulin receptor number increased and high-affinity receptor number decreased in cells treated with TPA.	Tetradecanoylphorbol Acetate	218-221	insulin receptor	Homo sapiens	118-134
3245391-0	1988	Erythrocyte insulin receptor: normalization of binding data for the average cell age by the red cell creatine determination in obese, diabetic and acromegalic patients.	Creatine	101-109	insulin receptor	Homo sapiens	12-28
3052459-0	1988	Taurine binding to the purified insulin receptor.	Taurine	0-7	insulin receptor	Homo sapiens	32-48
2458350-6	1988	Second, in situ phosphorylation experiments showed that vanadate activated tyrosine phosphorylation of the insulin receptor"s beta-subunit.	Vanadates	56-64	insulin receptor	Homo sapiens	107-124
2458350-6	1988	Second, in situ phosphorylation experiments showed that vanadate activated tyrosine phosphorylation of the insulin receptor"s beta-subunit.	Tyrosine	75-83	insulin receptor	Homo sapiens	107-124
3052459-1	1988	Taurine (2-aminoethanesulfonic acid) was shown to bind specifically and reversibly to the purified human insulin receptor.	Taurine	0-7	insulin receptor	Homo sapiens	105-121
3052459-1	1988	Taurine (2-aminoethanesulfonic acid) was shown to bind specifically and reversibly to the purified human insulin receptor.	Taurine	9-35	insulin receptor	Homo sapiens	105-121
3052459-3	1988	The apparent Kd for taurine binding to the purified insulin receptor was calculated to be 130 X 10(-9) M and the maximum number of binding sites (Bmax) was 1.6 nmol/mg receptor protein.	Taurine	20-27	insulin receptor	Homo sapiens	52-68
3052459-7	1988	Taurine binding to the protein was pH dependent, and sulfur-containing taurine analogues were able to displace taurine from the insulin receptor.	Taurine	0-7	insulin receptor	Homo sapiens	128-144
3052459-7	1988	Taurine binding to the protein was pH dependent, and sulfur-containing taurine analogues were able to displace taurine from the insulin receptor.	Sulfur	53-59	insulin receptor	Homo sapiens	128-144
3052459-7	1988	Taurine binding to the protein was pH dependent, and sulfur-containing taurine analogues were able to displace taurine from the insulin receptor.	Taurine	71-78	insulin receptor	Homo sapiens	128-144
3052459-7	1988	Taurine binding to the protein was pH dependent, and sulfur-containing taurine analogues were able to displace taurine from the insulin receptor.	Taurine	111-118	insulin receptor	Homo sapiens	128-144
3052459-8	1988	These data supported our previous in vivo and in vitro observations that the hypoglycemic properties of taurine appear to be mediated through an interaction of taurine with the insulin receptor.	Taurine	104-111	insulin receptor	Homo sapiens	177-193
3052459-8	1988	These data supported our previous in vivo and in vitro observations that the hypoglycemic properties of taurine appear to be mediated through an interaction of taurine with the insulin receptor.	Taurine	160-167	insulin receptor	Homo sapiens	177-193
3047118-5	1988	To further delineate the mechanisms of insulin receptor regulation, we have measured insulin receptor mRNA levels in hydrocortisone-treated and insulin-treated IM-9 lymphocytes.	Hydrocortisone	117-131	insulin receptor	Homo sapiens	85-101
3047118-6	1988	An increase in insulin receptor mRNA could be detected after 2 h of incubation with hydrocortisone and a plateau was reached by 4-6 h. The response was dose-dependent, being detectable with 50 nM hydrocortisone and reaching a maximal 3.7-fold increase at 200 nM.	Hydrocortisone	84-98	insulin receptor	Homo sapiens	15-31
3047118-6	1988	An increase in insulin receptor mRNA could be detected after 2 h of incubation with hydrocortisone and a plateau was reached by 4-6 h. The response was dose-dependent, being detectable with 50 nM hydrocortisone and reaching a maximal 3.7-fold increase at 200 nM.	Hydrocortisone	196-210	insulin receptor	Homo sapiens	15-31
3047118-10	1988	The present study demonstrates that hydrocortisone, but not insulin, stimulates insulin receptor biosynthesis by increasing the rate of transcription and that de novo protein synthesis is probably required for a maximal effect.	Hydrocortisone	36-50	insulin receptor	Homo sapiens	80-96
3045261-8	1988	We conclude that (1) cultured neurons from fetal chicken brain express the same subtype of insulin receptor previously identified in adult rat and human brain, (2) the neuronal subtype of insulin receptor undergoes internalization and down-regulation in response to insulin, and (3) neuronal insulin receptors do not acutely regulate glucose metabolism but mediate growth in neurons.	Glucose	334-341	insulin receptor	Homo sapiens	188-204
3164998-2	1988	The phosphotransferase activity of an oncogene product, pp130fps, and a growth factor receptor, insulin receptor, were inhibited by myricetin, a derivative of quercetin.	myricetin	132-141	insulin receptor	Homo sapiens	96-112
3234633-3	1988	The digested DNA was subjected to agarose gel electrophoresis, Southern blotted, and hybridised to 32P-labelled human insulin receptor gene cDNA.	Phosphorus-32	99-102	insulin receptor	Homo sapiens	118-134
3164998-2	1988	The phosphotransferase activity of an oncogene product, pp130fps, and a growth factor receptor, insulin receptor, were inhibited by myricetin, a derivative of quercetin.	Quercetin	159-168	insulin receptor	Homo sapiens	96-112
3164998-4	1988	Apparent Ki values of myricetin for tyrosine protein kinases of pp130fps and insulin receptor were 1.8 and 2.6 microM, respectively.	myricetin	22-31	insulin receptor	Homo sapiens	77-93
3164998-8	1988	Structure activity studies exhibited that the inhibitory potencies of the flavonoids for tyrosine kinases of pp130fps and insulin receptor correlated with the number of hydroxy residues on the flavone rings (gamma = 0.974 and 0.926, respectively), whereas the hydroxylation influenced to a lesser extent the inhibitory potencies for serine/threonine protein kinase.	Flavonoids	74-84	insulin receptor	Homo sapiens	122-138
3164998-8	1988	Structure activity studies exhibited that the inhibitory potencies of the flavonoids for tyrosine kinases of pp130fps and insulin receptor correlated with the number of hydroxy residues on the flavone rings (gamma = 0.974 and 0.926, respectively), whereas the hydroxylation influenced to a lesser extent the inhibitory potencies for serine/threonine protein kinase.	flavone	193-200	insulin receptor	Homo sapiens	122-138
3052583-1	1988	Partially purified human placental insulin receptor preparations give rise to three distinct insulin-binding peaks when eluted from a Mono Q high-performance liquid chromatography anion-exchange column.	Mono Q	134-140	insulin receptor	Homo sapiens	35-51
2843552-5	1988	Acylation of the insulin receptor was an early event as judged by fatty acid incorporation into the alpha beta-precursor and prevention by protein synthesis inhibitors.	Fatty Acids	66-76	insulin receptor	Homo sapiens	17-33
3052583-4	1988	This analysis of subunit composition was confirmed by silver staining of affinity-purified insulin receptor following resolution of the forms on a Mono Q column as described previously.	Silver	54-60	insulin receptor	Homo sapiens	91-107
3044777-6	1988	This unusual and unexpected observation in carbohydrate-sensitive subjects suggests an altered response of the insulin receptor, namely the failure of plasma insulin to down-regulate the number of receptors.	Carbohydrates	43-55	insulin receptor	Homo sapiens	111-127
3288633-0	1988	Vanadate down-regulates cell surface insulin and growth hormone receptors and inhibits insulin receptor degradation in cultured human lymphocytes.	Vanadates	0-8	insulin receptor	Homo sapiens	87-103
3372510-2	1988	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cross-linked, affinity-labeled stingray insulin receptor shows an apparent molecular mass of 210 kDa for the intact receptor.	Sodium Dodecyl Sulfate	0-22	insulin receptor	Homo sapiens	101-117
3372510-2	1988	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cross-linked, affinity-labeled stingray insulin receptor shows an apparent molecular mass of 210 kDa for the intact receptor.	polyacrylamide	23-37	insulin receptor	Homo sapiens	101-117
3372510-4	1988	Gel filtration studies of Triton X-100 solubilized stingray insulin receptor demonstrated an apparent Stokes radius of 7.6 nm.	Octoxynol	26-38	insulin receptor	Homo sapiens	60-76
3283119-3	1988	Biochemical assays based on the selective precipitation by polyethylene glycol of intact insulin-receptor complexes but not of free intracellular insulin were developed to study the time course of intracellular insulin-receptor dissociation.	Polyethylene Glycols	59-78	insulin receptor	Homo sapiens	89-105
2837189-0	1988	Direct modulation of insulin receptor protein tyrosine kinase by vanadate and anti-insulin receptor monoclonal antibodies.	Vanadates	65-73	insulin receptor	Homo sapiens	21-37
2837189-1	1988	Sodium vanadate activates "in vitro" insulin receptor autophosphorylation and protein tyrosine kinase in a dose-dependent manner.	Vanadates	0-15	insulin receptor	Homo sapiens	37-53
2837189-4	1988	In this report we show that insulin receptor protein tyrosine kinase, activated by sodium vanadate or by monoclonal antibody 18-44, is inhibited by MA-10 antibody.	Vanadates	83-98	insulin receptor	Homo sapiens	28-44
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Arginine	198-201	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Lysine	202-205	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Arginine	206-209	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Arginine	206-209	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Arginine	206-209	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Lysine	221-224	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Arginine	206-209	insulin receptor	Homo sapiens	30-46
3283938-1	1988	A point mutation in the human insulin receptor gene in a patient with type A insulin resistance alters the amino acid sequence within the tetrabasic processing site of the proreceptor molecule from Arg-Lys-Arg-Arg to Arg-Lys-Arg-Ser.	Serine	229-232	insulin receptor	Homo sapiens	30-46
3075902-4	1988	Although metformin may increase insulin-receptor binding, its main effect appears to be directed at the postreceptor level of insulin action.	Metformin	9-18	insulin receptor	Homo sapiens	32-48
2834414-0	1988	Alterations in insulin receptor autophosphorylation in insulin resistance: correlation with altered sensitivity to glucose transport and antilipolysis to insulin.	Glucose	115-122	insulin receptor	Homo sapiens	15-31
2834414-5	1988	These data indicate a significant correlation between changes in sensitivity of glucose transport and antilipolysis to insulin and receptor kinase activity in those patients and suggest that defective coupling of insulin binding to insulin action at the level of phosphorylation of the insulin receptor may cause the insulin resistance in this group of patients.	Glucose	80-87	insulin receptor	Homo sapiens	286-302
2844286-3	1988	Quantitatively, the fraction of phosphatidylinositol kinase that was bound to WGA sepharose and eluted together with the insulin receptor amounted to 2% of the Triton X-100 soluble phosphatidylinositol kinase.	Octoxynol	160-172	insulin receptor	Homo sapiens	121-137
3446556-0	1987	Effect of dexamethasone on the synthesis and degradation of insulin receptor mRNA in cultured IM-9 cells.	Dexamethasone	10-23	insulin receptor	Homo sapiens	60-76
3358780-2	1988	We evaluated the ability of NO2 to alter the surface membrane fluidity, lipid composition, and insulin receptor binding of porcine pulmonary artery endothelial cells in culture.	Nitrogen Dioxide	28-31	insulin receptor	Homo sapiens	95-111
3358780-10	1988	Scatchard analysis of the binding data indicated that NO2 exposure caused a 5-fold reduction in insulin receptor binding sites in endothelial cells.	Nitrogen Dioxide	54-57	insulin receptor	Homo sapiens	96-112
3293865-13	1988	These results suggest that insulin action at the receptor may be affected by the administration of cyclosporine.	Cyclosporine	99-111	insulin receptor	Homo sapiens	49-57
3359262-0	1988	Characterization of the altered oligosaccharide composition of the insulin receptor on neural-derived cells.	Oligosaccharides	32-47	insulin receptor	Homo sapiens	67-83
3129526-0	1988	Influence of a small molecular weight proteinase inhibitor, gabexate mesilate (FOY), on insulin receptor function in vitro.	Gabexate	60-77	insulin receptor	Homo sapiens	88-104
3339130-3	1988	Incubation of IM-9 cells with 100 nM dexamethasone for 4 h stimulated a parallel increase in both polysomal and nuclear insulin receptor RNAs indicating that glucocorticoids did not alter the nuclear transport of insulin receptor RNA.	Dexamethasone	37-50	insulin receptor	Homo sapiens	120-136
3339130-5	1988	Furthermore, the dexamethasone-induced increase in insulin receptor mRNA levels was not blocked by pretreatment of cells with cycloheximide indicating that the glucocorticoid effect was independent of new protein synthesis.	Dexamethasone	17-30	insulin receptor	Homo sapiens	51-67
2973824-0	1988	[Preparation of 125I-labelled monoclonal antibodies of the insulin receptor].	Iodine-125	16-20	insulin receptor	Homo sapiens	59-76
2973824-3	1988	Cloramine T method produced labelled antibody with constant specific activity; however, some preparations were unstable and showed reduced capacity to recognize the insulin receptor.	chloramine-T	0-11	insulin receptor	Homo sapiens	165-181
2973824-5	1988	The IODO-GEN method produced antibodies with constant specific activity, stable, high capacity to interact with the insulin receptor, and, moreover, maintaining in full the capacity to inhibit the insulin-stimulated auto-phosphorylation of the insulin receptor, since it does not induce antibody alterations which in turn affect antibody-receptor interaction biological action.	1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril	4-12	insulin receptor	Homo sapiens	116-132
2973824-5	1988	The IODO-GEN method produced antibodies with constant specific activity, stable, high capacity to interact with the insulin receptor, and, moreover, maintaining in full the capacity to inhibit the insulin-stimulated auto-phosphorylation of the insulin receptor, since it does not induce antibody alterations which in turn affect antibody-receptor interaction biological action.	1,3,4,6-tetrachloro-3 alpha,6 alpha-diphenylglycoluril	4-12	insulin receptor	Homo sapiens	244-260
3126223-3	1987	Glibenclamide (2 microM) and metformin (1-10 microM) induced a 13-28% reduction in insulin receptor down regulation in fibroblasts exposed to 1.7 x 10(-8)M-insulin, the loss of binding on exposure to insulin decreasing from 55% to 40-48%.	Glyburide	0-13	insulin receptor	Homo sapiens	83-99
3126223-3	1987	Glibenclamide (2 microM) and metformin (1-10 microM) induced a 13-28% reduction in insulin receptor down regulation in fibroblasts exposed to 1.7 x 10(-8)M-insulin, the loss of binding on exposure to insulin decreasing from 55% to 40-48%.	Metformin	29-38	insulin receptor	Homo sapiens	83-99
3676333-3	1987	In the human insulin receptor, the second series of cystine domains is replaced by a different sequence.	Cystine	52-59	insulin receptor	Homo sapiens	13-29
3680248-8	1987	A comparison between the promoter sequence of the human insulin receptor and those of other "housekeeping" genes revealed the presence of homologous sequences among these genes, in addition to the potential Sp 1 binding sites.	boron nitride	207-211	insulin receptor	Homo sapiens	56-72
3313056-2	1987	At one end of the signalling chain, the structure of the insulin receptor is known in detail, and at the other end, insulin controls cellular metabolism by regulating the phosphorylation of serine and threonine residues in key target enzymes.	Serine	190-196	insulin receptor	Homo sapiens	57-73
3313056-2	1987	At one end of the signalling chain, the structure of the insulin receptor is known in detail, and at the other end, insulin controls cellular metabolism by regulating the phosphorylation of serine and threonine residues in key target enzymes.	Threonine	201-210	insulin receptor	Homo sapiens	57-73
3360145-0	1988	Polylysine activates and alters the divalent cation requirements of the insulin receptor protein tyrosine kinase.	Polylysine	0-10	insulin receptor	Homo sapiens	72-88
3360145-1	1988	Protamine and poly(Lys) activate the protein tyrosine kinase of both the human placental insulin receptor and its purified recombinant cytoplasmic domain.	poly(lys)	14-23	insulin receptor	Homo sapiens	89-105
2902666-5	1988	The results suggest that sulfonylureas exert in part their hypoglucemic effect by modificating the insulin receptor binding through the inhibition of transglutaminase activity.	Sulfonylurea Compounds	25-38	insulin receptor	Homo sapiens	99-115
3281654-2	1988	Cortisol and cortexolone, but not oestrogen, increased both the binding of insulin and the amount of insulin-receptor mRNA in a time- and dose-dependent manner.	Hydrocortisone	0-8	insulin receptor	Homo sapiens	101-117
3281654-2	1988	Cortisol and cortexolone, but not oestrogen, increased both the binding of insulin and the amount of insulin-receptor mRNA in a time- and dose-dependent manner.	Cortodoxone	13-24	insulin receptor	Homo sapiens	101-117
3275643-9	1988	These tyrosines are clustered in several domains in a distribution virtually identical to that previously found for partially purified human insulin receptor autophosphorylated in vitro in the presence of insulin.	Tyrosine	6-15	insulin receptor	Homo sapiens	141-157
3144155-6	1988	Adipocyte insulin receptor binding was comparable before and after therapy, both in the fasting state and following glucose intake.	Glucose	116-123	insulin receptor	Homo sapiens	10-26
2893587-8	1988	(iv) While (E4,Y1)n and (E6,A3,Y1)n are good substrates for both receptor kinases, the ratio of phosphate incorporation into the former to the latter is characteristically high (approximately 4) for the IGF-I receptor and low (approximately 1) for the insulin receptor.	Phosphates	96-105	insulin receptor	Homo sapiens	252-268
2835273-4	1988	The insulin receptor phosphorylates a guanine nucleotide-binding protein, which activates a particular phospholipase C. This in turn stimulates the production of two lipid-derived messengers: inositol-phospho-glucosamine and diacylglycerol.	inositol-phospho-glucosamine	192-220	insulin receptor	Homo sapiens	4-20
2835273-4	1988	The insulin receptor phosphorylates a guanine nucleotide-binding protein, which activates a particular phospholipase C. This in turn stimulates the production of two lipid-derived messengers: inositol-phospho-glucosamine and diacylglycerol.	Diglycerides	225-239	insulin receptor	Homo sapiens	4-20
3446556-1	1987	The effect of glucocorticoid (dexamethasone) on insulin receptor mRNA was examined in the IM-9 cell line by dot hybridization analysis using insulin receptor c-DNA probe (<protein-id="3643">phINSR 13-1).	Dexamethasone	30-43	insulin receptor	Homo sapiens	48-64
3320694-6	1987	These changes in the membrane phospholipids would then theoretically increase both insulin receptor binding affinity and sensitivity, thus enhancing glucose transport across their membranes.	Phospholipids	30-43	insulin receptor	Homo sapiens	83-99
3320694-6	1987	These changes in the membrane phospholipids would then theoretically increase both insulin receptor binding affinity and sensitivity, thus enhancing glucose transport across their membranes.	Glucose	149-156	insulin receptor	Homo sapiens	83-99
2959436-5	1987	The intrinsic tyrosine kinase activity of the insulin receptor was demonstrated by autophosphorylation of receptors purified by immunoprecipitation, and by phosphorylation of a synthetic substrate: poly(Glu, Tyr (4:1].	poly(glu, tyr	198-211	insulin receptor	Homo sapiens	46-62
3307773-5	1987	Furthermore, it showed that adrenaline also increased insulin receptor affinity.	Epinephrine	28-38	insulin receptor	Homo sapiens	54-70
3307773-6	1987	The negative co-operativity affinity profile demonstrated that adrenaline caused a rise in only the upper limit average affinity, Ki, of the insulin receptor.	Epinephrine	63-73	insulin receptor	Homo sapiens	141-157
2957374-1	1987	We have previously demonstrated that the human insulin receptor, mutated in the ATP-binding domain of the beta-subunit, is kinase-defective and fails to mediate multiple post-receptor actions of insulin in stably transfected Chinese hamster ovary cells (Chou, C.-K., Dull, T. J., Russell, D. S., Gherzi, R., Lebwohl, D., Ullrich, A., and Rosen, O. M. (1987) J. Biol.	Adenosine Triphosphate	80-83	insulin receptor	Homo sapiens	47-63
2957375-0	1987	Effects of castanospermine and 1-deoxynojirimycin on insulin receptor biogenesis.	castanospermine	11-26	insulin receptor	Homo sapiens	53-69
2957375-0	1987	Effects of castanospermine and 1-deoxynojirimycin on insulin receptor biogenesis.	1-DEOXYNOJIRIMYCIN	31-49	insulin receptor	Homo sapiens	53-69
3304429-0	1987	The effect of insulin, serum and dexamethasone on mRNA levels for the insulin receptor in the human lymphoblastoic cell line IM-9.	Dexamethasone	33-46	insulin receptor	Homo sapiens	70-86
3304429-1	1987	The effect of insulin, serum and dexamethasone on mRNA levels in the insulin receptor in the human lymphoblastoic cell line IM-9 was examined.	Dexamethasone	33-46	insulin receptor	Homo sapiens	69-85
3304429-3	1987	The presence of 0.1 microM dexamethasone in the medium had a strong stimulatory effect on mRNA levels in insulin receptor, suggesting the presence of a glucocorticoid inducible enhancer element near the insulin receptor gene.	Dexamethasone	27-40	insulin receptor	Homo sapiens	105-121
3304429-3	1987	The presence of 0.1 microM dexamethasone in the medium had a strong stimulatory effect on mRNA levels in insulin receptor, suggesting the presence of a glucocorticoid inducible enhancer element near the insulin receptor gene.	Dexamethasone	27-40	insulin receptor	Homo sapiens	203-219
3680872-3	1987	The results obtained clearly demonstrate that dexamethasone increases insulin receptor concentration while glucose ingestion increases both insulin receptor affinity and concentration on young RBCs.	Dexamethasone	46-59	insulin receptor	Homo sapiens	70-86
3680872-3	1987	The results obtained clearly demonstrate that dexamethasone increases insulin receptor concentration while glucose ingestion increases both insulin receptor affinity and concentration on young RBCs.	Glucose	107-114	insulin receptor	Homo sapiens	140-156
3039503-1	1987	A retrovirus containing part of the human insulin receptor (hIR) gene was constructed by replacing ros sequences in the avian sarcoma virus UR2 with hIR cDNA sequences coding for 46 amino acids of the extracellular domain and the entire transmembrane and cytoplasmic domains of the beta subunit of hIR.	ros	99-102	insulin receptor	Homo sapiens	42-58
3038872-0	1987	Identification of insulin receptor tyrosine residues autophosphorylated in vitro.	Tyrosine	35-43	insulin receptor	Homo sapiens	18-34
3038872-1	1987	To identify the autophosphorylation sites on the human insulin receptor (IR), partially purified human IR was incubated in vitro in the presence of insulin and manganese [gamma-32P]ATP so as to achieve near-maximal activation of the histone 2b kinase activity.	Manganese	160-169	insulin receptor	Homo sapiens	55-71
3038872-1	1987	To identify the autophosphorylation sites on the human insulin receptor (IR), partially purified human IR was incubated in vitro in the presence of insulin and manganese [gamma-32P]ATP so as to achieve near-maximal activation of the histone 2b kinase activity.	Manganese	160-169	insulin receptor	Homo sapiens	73-75
3038872-1	1987	To identify the autophosphorylation sites on the human insulin receptor (IR), partially purified human IR was incubated in vitro in the presence of insulin and manganese [gamma-32P]ATP so as to achieve near-maximal activation of the histone 2b kinase activity.	gamma-32p	171-180	insulin receptor	Homo sapiens	55-71
3038872-1	1987	To identify the autophosphorylation sites on the human insulin receptor (IR), partially purified human IR was incubated in vitro in the presence of insulin and manganese [gamma-32P]ATP so as to achieve near-maximal activation of the histone 2b kinase activity.	gamma-32p	171-180	insulin receptor	Homo sapiens	73-75
3038872-1	1987	To identify the autophosphorylation sites on the human insulin receptor (IR), partially purified human IR was incubated in vitro in the presence of insulin and manganese [gamma-32P]ATP so as to achieve near-maximal activation of the histone 2b kinase activity.	Adenosine Triphosphate	181-184	insulin receptor	Homo sapiens	55-71
3038872-10	1987	We conclude that autophosphorylation of human IR in vitro leads to the phosphorylation of at least 6 of the 13 tyrosine residues on the beta subunit intracellular extension.	Tyrosine	111-119	insulin receptor	Homo sapiens	46-48
2822020-2	1987	The insulin-receptor kinase was observed to be more sensitive to inhibition by N-ethylmaleimide in the presence [IC50 (concn, giving 50% inhibition) = 25 +/- 3 microM] than in the absence (IC50 = 73 +/- 6 microM) of insulin.	Ethylmaleimide	79-95	insulin receptor	Homo sapiens	4-20
2439512-2	1987	In Fao cells, besides the beta-subunit of the insulin receptor, a protein with a molecular mass between 170 and 210 kDa designated pp185, undergoes tyrosine phosphorylation immediately after insulin stimulation reaching a maximum level within 30 s. After 4 h of continuous insulin stimulation, the labeling of pp185 decreased to less than half of its original intensity, whereas the insulin receptor was unchanged.	Tyrosine	148-156	insulin receptor	Homo sapiens	46-62
3316225-1	1987	The dissociation of the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex into an alpha beta heterodimeric state was found to occur in a pH- and dithiothreitol (DTT)-dependent manner.	Dithiothreitol	177-191	insulin receptor	Homo sapiens	81-97
3316225-1	1987	The dissociation of the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex into an alpha beta heterodimeric state was found to occur in a pH- and dithiothreitol (DTT)-dependent manner.	Dithiothreitol	193-196	insulin receptor	Homo sapiens	81-97
3316225-5	1987	Kinetic analyses of the insulin receptor protein kinase activity demonstrated that the insulin stimulation of glutamic acid:tyrosine (4:1) synthetic polymer phosphorylation for both the alpha 2 beta 2 heterotetrameric and alpha beta heterodimeric complexes occurred via an increase in Vmax without any significant change in Km.	Glutamic Acid	110-123	insulin receptor	Homo sapiens	24-40
3316225-5	1987	Kinetic analyses of the insulin receptor protein kinase activity demonstrated that the insulin stimulation of glutamic acid:tyrosine (4:1) synthetic polymer phosphorylation for both the alpha 2 beta 2 heterotetrameric and alpha beta heterodimeric complexes occurred via an increase in Vmax without any significant change in Km.	Tyrosine	124-132	insulin receptor	Homo sapiens	24-40
3316225-5	1987	Kinetic analyses of the insulin receptor protein kinase activity demonstrated that the insulin stimulation of glutamic acid:tyrosine (4:1) synthetic polymer phosphorylation for both the alpha 2 beta 2 heterotetrameric and alpha beta heterodimeric complexes occurred via an increase in Vmax without any significant change in Km.	Polymers	149-156	insulin receptor	Homo sapiens	24-40
3038645-0	1987	Phospholipid activation of the insulin receptor kinase: regulation by phosphatidylinositol.	Phospholipids	0-12	insulin receptor	Homo sapiens	31-47
3038645-0	1987	Phospholipid activation of the insulin receptor kinase: regulation by phosphatidylinositol.	Phosphatidylinositols	70-90	insulin receptor	Homo sapiens	31-47
3038645-1	1987	A soybean phospholipid mixture produced a concentration-dependent enhancement of beta subunit autophosphorylation of the detergent-soluble, purified human placental insulin receptor.	Phospholipids	10-22	insulin receptor	Homo sapiens	165-181
3038645-2	1987	Although phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine also increased insulin receptor autophosphorylation, only phosphatidylinositol (PtdIns) stimulated to a similar extent as the phospholipid mixture.	Phosphatidylcholines	9-28	insulin receptor	Homo sapiens	93-109
3038645-2	1987	Although phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine also increased insulin receptor autophosphorylation, only phosphatidylinositol (PtdIns) stimulated to a similar extent as the phospholipid mixture.	phosphatidylethanolamine	30-54	insulin receptor	Homo sapiens	93-109
3038645-2	1987	Although phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine also increased insulin receptor autophosphorylation, only phosphatidylinositol (PtdIns) stimulated to a similar extent as the phospholipid mixture.	Phosphatidylserines	59-77	insulin receptor	Homo sapiens	93-109
3038645-4	1987	Phospholipids also stimulated the exogenous protein kinase activity of the insulin receptor toward histone H2B.	Phospholipids	0-13	insulin receptor	Homo sapiens	75-91
3038645-5	1987	Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity.	Phosphatidylinositols	19-25	insulin receptor	Homo sapiens	55-71
3038645-5	1987	Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity.	Phosphatidylinositols	157-163	insulin receptor	Homo sapiens	55-71
3038645-5	1987	Phosphorylation of PtdIns occurred with these purified insulin receptor preparations, but this activity was insulin-independent, and the turnover number for PtdIns phosphorylation in the presence of soybean phospholipid was 1/220th as small as the turnover number for the autophosphorylating activity.	Phospholipids	207-219	insulin receptor	Homo sapiens	55-71
3038645-6	1987	These results suggest that although PtdIns can modulate the activity of the insulin receptor kinase, PtdIns phosphorylation itself is not directly involved in this regulation.	Phosphatidylinositols	36-42	insulin receptor	Homo sapiens	76-92
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Dithiothreitol	75-89	insulin receptor	Homo sapiens	25-41
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Tromethamine	100-104	insulin receptor	Homo sapiens	25-41
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Disulfides	158-167	insulin receptor	Homo sapiens	25-41
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Disulfides	183-193	insulin receptor	Homo sapiens	25-41
3033648-0	1987	Monoclonal antibodies to the human insulin receptor that activate glucose transport but not insulin receptor kinase activity.	Glucose	66-73	insulin receptor	Homo sapiens	35-51
3549468-2	1987	A reduction in the biologic action of insulin, at a point beyond the insulin receptor (postbinding site), is primarily responsible for the reduced rate of glucose utilization.	Glucose	155-162	insulin receptor	Homo sapiens	69-85
3569675-1	1987	We found with IM-9 human cultured lymphocytes, that the glucocorticoid dexamethasone increased insulin-receptor mRNA levels.	Dexamethasone	71-84	insulin receptor	Homo sapiens	95-111
3621802-4	1987	Monocyte insulin-receptor binding was decreased in all the subjects from 30 to 60% after ethanol infusion.	Ethanol	89-96	insulin receptor	Homo sapiens	9-25
3550798-2	1987	It has been shown previously that phenylarsine oxide, an agent that complexes vicinal dithiols, interrupts signal transmission from the insulin receptor to the glucose transport system.	oxophenylarsine	34-52	insulin receptor	Homo sapiens	136-152
3550798-2	1987	It has been shown previously that phenylarsine oxide, an agent that complexes vicinal dithiols, interrupts signal transmission from the insulin receptor to the glucose transport system.	vicinal dithiols	78-94	insulin receptor	Homo sapiens	136-152
3550798-2	1987	It has been shown previously that phenylarsine oxide, an agent that complexes vicinal dithiols, interrupts signal transmission from the insulin receptor to the glucose transport system.	Glucose	160-167	insulin receptor	Homo sapiens	136-152
3550798-3	1987	Several lines of evidence presented here indicate the involvement of pp15 in insulin receptor-initiated signal transduction to the glucose transport system.	Glucose	131-138	insulin receptor	Homo sapiens	77-93
2439512-5	1987	The pp185 and the beta-subunit of the insulin receptor were strongly labeled with [32P]orthophosphate, but in contrast to the insulin receptor, the pp185 was not labeled by cross-linking with 125I-insulin or surface 125I iodination.	32p]orthophosphate	83-101	insulin receptor	Homo sapiens	38-54
2439512-10	1987	Increasing the concentration of the human insulin receptor in the Chinese hamster ovary cells by transfection with a plasmid containing the human insulin receptor cDNA caused a higher level of tyrosine phosphorylation of the beta-subunit and the pp185.	Tyrosine	193-201	insulin receptor	Homo sapiens	42-58
2439512-10	1987	Increasing the concentration of the human insulin receptor in the Chinese hamster ovary cells by transfection with a plasmid containing the human insulin receptor cDNA caused a higher level of tyrosine phosphorylation of the beta-subunit and the pp185.	Tyrosine	193-201	insulin receptor	Homo sapiens	146-162
3567178-4	1987	These peptides, along with a phenylalanine-containing analogue, did serve as competitive inhibitors of the insulin receptor/kinase with apparent Ki values in the range of 2-4 mM.	Phenylalanine	29-42	insulin receptor	Homo sapiens	107-123
3567178-1	1987	The insulin receptor has been shown to be a protein kinase which phosphorylates its substrates on tyrosine residues.	Tyrosine	98-106	insulin receptor	Homo sapiens	4-20
3297047-6	1987	The increased accumulation of the 90 kDa tryptic peptide from cells preincubated at 37 degrees C, but not at 16 degrees C, indicated that trypsin cleavage sites within the 90 kDa segment of the insulin-receptor alpha-subunit that were exposed at 16 degrees C were made inaccessible by incubation at 37 degrees C, a finding that is consistent with generation of a cryptic domain of the receptor subunit.	Peptides	49-56	insulin receptor	Homo sapiens	194-210
3542655-3	1987	It was found that the insulin-receptor complex was fully stable at this ethanol concentration, regardless of the source of the receptor employed.	Ethanol	72-79	insulin receptor	Homo sapiens	22-38
3546299-5	1987	Comparisons between the time courses of beta subunit autophosphorylation with those of Glu:Tyr phosphorylation both in the presence and absence of insulin confirmed that insulin can stimulate the exogenous protein kinase activity of the insulin receptor in the complete absence of beta subunit autophosphorylation.	Glutamic Acid	87-90	insulin receptor	Homo sapiens	237-253
3546299-5	1987	Comparisons between the time courses of beta subunit autophosphorylation with those of Glu:Tyr phosphorylation both in the presence and absence of insulin confirmed that insulin can stimulate the exogenous protein kinase activity of the insulin receptor in the complete absence of beta subunit autophosphorylation.	Tyrosine	91-94	insulin receptor	Homo sapiens	237-253
3546299-6	1987	Prephosphorylation of the insulin receptor (from 0 to 1.3 mol of phosphate/mol of insulin receptor) in the absence of insulin was found to have no significant effect on the exogenous protein kinase activity when assayed both in the presence and absence of insulin.	Phosphates	65-74	insulin receptor	Homo sapiens	26-42
3546299-8	1987	In contrast, prephosphorylation of the insulin receptors in the presence of insulin was observed to enhance the exogenous protein kinase activity dependent on the extent of autophosphorylation, such that by 1.4 mol of phosphate incorporated per mol of insulin receptor, insulin was found to maximally stimulate the initial rate of Glu:Tyr phosphorylation (approximately 9-fold).	Phosphates	218-227	insulin receptor	Homo sapiens	39-55
3546299-8	1987	In contrast, prephosphorylation of the insulin receptors in the presence of insulin was observed to enhance the exogenous protein kinase activity dependent on the extent of autophosphorylation, such that by 1.4 mol of phosphate incorporated per mol of insulin receptor, insulin was found to maximally stimulate the initial rate of Glu:Tyr phosphorylation (approximately 9-fold).	Glutamic Acid	331-334	insulin receptor	Homo sapiens	39-55
3546299-8	1987	In contrast, prephosphorylation of the insulin receptors in the presence of insulin was observed to enhance the exogenous protein kinase activity dependent on the extent of autophosphorylation, such that by 1.4 mol of phosphate incorporated per mol of insulin receptor, insulin was found to maximally stimulate the initial rate of Glu:Tyr phosphorylation (approximately 9-fold).	Tyrosine	335-338	insulin receptor	Homo sapiens	39-55
3026782-2	1987	The labeling of this protein was greatly increased by concurrent treatment of the cells with N-ethylmaleimide, to the extent that the amount of [125I]-insulin cross-linked to the enzyme in these cells was approximately 20 to 50% that cross-linked to the insulin receptor.	Ethylmaleimide	93-109	insulin receptor	Homo sapiens	254-270
3552593-2	1987	Two covalent receptor modifications possibly involved in producing pharmacodynamic effects as a result of insulin receptor binding are autophosphorylation and disulphide insulin binding.	disulphide	159-169	insulin receptor	Homo sapiens	106-122
3552772-3	1987	We suggest that metformin can correct down regulation of the insulin receptor.	Metformin	16-25	insulin receptor	Homo sapiens	61-77
3101064-0	1987	Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.	Lysine	15-21	insulin receptor	Homo sapiens	77-93
3101064-0	1987	Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.	Adenosine Triphosphate	51-54	insulin receptor	Homo sapiens	77-93
3101064-0	1987	Replacement of lysine residue 1030 in the putative ATP-binding region of the insulin receptor abolishes insulin- and antibody-stimulated glucose uptake and receptor kinase activity.	Glucose	137-144	insulin receptor	Homo sapiens	77-93
3101064-1	1987	To test whether the tyrosine kinase activity of the insulin receptor is crucial for insulin action, we have constructed mutations of the human insulin receptor at Lys-1030, which is in the presumed ATP-binding region.	Lysine	163-166	insulin receptor	Homo sapiens	52-68
3101064-1	1987	To test whether the tyrosine kinase activity of the insulin receptor is crucial for insulin action, we have constructed mutations of the human insulin receptor at Lys-1030, which is in the presumed ATP-binding region.	Lysine	163-166	insulin receptor	Homo sapiens	143-159
3101064-1	1987	To test whether the tyrosine kinase activity of the insulin receptor is crucial for insulin action, we have constructed mutations of the human insulin receptor at Lys-1030, which is in the presumed ATP-binding region.	Adenosine Triphosphate	198-201	insulin receptor	Homo sapiens	52-68
3101064-1	1987	To test whether the tyrosine kinase activity of the insulin receptor is crucial for insulin action, we have constructed mutations of the human insulin receptor at Lys-1030, which is in the presumed ATP-binding region.	Adenosine Triphosphate	198-201	insulin receptor	Homo sapiens	143-159
3803233-0	1987	[At the start of the path to stroke: insulin receptor damage by alcohol and fatty liver-hyperinsulinism in young men].	Alcohols	64-71	insulin receptor	Homo sapiens	37-53
3440445-11	1987	Thus, this inborn error of the insulin receptor offers unique insight into a regulatory signal by its alpha subunit which, when altered, results in constitutively increased glucose transport.	Glucose	173-180	insulin receptor	Homo sapiens	31-47
3543511-0	1987	Induction of insulin receptor expression of human leukemic cells by 1 alpha, 25 dihydroxyvitamin D3.	Calcitriol	68-99	insulin receptor	Homo sapiens	13-29
2842659-0	1987	A membrane-anchored cytoplasmic domain of the human insulin receptor mediates a constitutively elevated insulin-independent uptake of 2-deoxyglucose.	Deoxyglucose	134-148	insulin receptor	Homo sapiens	52-68
3550373-3	1987	Insulin binding to red blood cells and insulin receptor number also improved significantly during Cr supplementation.	Chromium	98-100	insulin receptor	Homo sapiens	39-55
3805028-1	1987	The presence of covalently bound fatty acids in the insulin receptor has been explored in cultured human (IM-9) lymphocytes.	Fatty Acids	33-44	insulin receptor	Homo sapiens	52-68
3805028-7	1987	The incorporation of fatty acids into the insulin receptor is dependent on protein synthesis and is also detectable in the Mr = 190,000 proreceptor form.	Fatty Acids	21-32	insulin receptor	Homo sapiens	42-58
3567178-5	1987	These data suggest that the insulin receptor/kinase is specific for tyrosine residues in its acceptor substrate and imply that serine phosphate or threonine phosphate present in receptor is due to phosphorylation by other protein kinases.	Tyrosine	68-76	insulin receptor	Homo sapiens	28-44
3567178-5	1987	These data suggest that the insulin receptor/kinase is specific for tyrosine residues in its acceptor substrate and imply that serine phosphate or threonine phosphate present in receptor is due to phosphorylation by other protein kinases.	Phosphoserine	127-143	insulin receptor	Homo sapiens	28-44
3567178-5	1987	These data suggest that the insulin receptor/kinase is specific for tyrosine residues in its acceptor substrate and imply that serine phosphate or threonine phosphate present in receptor is due to phosphorylation by other protein kinases.	Phosphothreonine	147-166	insulin receptor	Homo sapiens	28-44
3567178-6	1987	The kinetics of the phosphorylation of the L-tyrosine-containing peptide were examined by using prephosphorylated insulin receptor/kinase.	Tyrosine	43-53	insulin receptor	Homo sapiens	114-130
3567178-10	1987	Thus, the insulin receptor/kinase catalyzes the reaction via a mechanism that does not involve transfer of phosphate from a phosphotyrosine-containing enzyme intermediate.	Phosphotyrosine	124-139	insulin receptor	Homo sapiens	10-26
3036692-0	1986	Effect of cAMP on down-regulation of erythrocyte insulin receptor.	Cyclic AMP	10-14	insulin receptor	Homo sapiens	49-65
3447155-1	1987	Tryptic peptides were isolated from human insulin receptor (1.8 nmol) by sequential reverse-phase HPLC on SynChropak RP-C8 and Vydac C-18.	Peptides	8-16	insulin receptor	Homo sapiens	42-58
3533683-0	1986	Diacylglycerol modulation of insulin receptor from cultured human mononuclear cells.	Diglycerides	0-14	insulin receptor	Homo sapiens	29-45
3533683-5	1986	Inhibition of insulin binding by diacylglycerols, analyzed by Scatchard plot, seems to be due to altered binding affinity of the insulin receptor.	Diglycerides	33-48	insulin receptor	Homo sapiens	129-145
3533683-11	1986	The ability of diacylglycerol to mimic the effects of TPA on the insulin receptor supports the concept of diacylglycerols as endogenous phorbol diester analogues even though the sole role of protein kinase C in our system is doubtful.	Diglycerides	15-29	insulin receptor	Homo sapiens	65-81
3533683-11	1986	The ability of diacylglycerol to mimic the effects of TPA on the insulin receptor supports the concept of diacylglycerols as endogenous phorbol diester analogues even though the sole role of protein kinase C in our system is doubtful.	Tetradecanoylphorbol Acetate	54-57	insulin receptor	Homo sapiens	65-81
3533683-11	1986	The ability of diacylglycerol to mimic the effects of TPA on the insulin receptor supports the concept of diacylglycerols as endogenous phorbol diester analogues even though the sole role of protein kinase C in our system is doubtful.	Diglycerides	106-121	insulin receptor	Homo sapiens	65-81
3533683-11	1986	The ability of diacylglycerol to mimic the effects of TPA on the insulin receptor supports the concept of diacylglycerols as endogenous phorbol diester analogues even though the sole role of protein kinase C in our system is doubtful.	Phorbol Esters	136-151	insulin receptor	Homo sapiens	65-81
3026445-0	1986	Dithiothreitol activation of the insulin receptor/kinase does not involve subunit dissociation of the native alpha 2 beta 2 insulin receptor subunit complex.	Dithiothreitol	0-14	insulin receptor	Homo sapiens	33-49
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Dithiothreitol	31-45	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Dithiothreitol	48-51	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Sodium Dodecyl Sulfate	103-125	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Sodium Dodecyl Sulfate	127-130	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	polyacrylamide	132-146	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Sodium Dodecyl Sulfate	224-227	insulin receptor	Homo sapiens	63-79
3026445-1	1986	The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions.	Octoxynol	252-264	insulin receptor	Homo sapiens	63-79
3026445-2	1986	Pretreatment of 32P-labeled insulin receptors with 50 mM DTT followed by gel filtration chromatography in 0.1% SDS demonstrated the dissociation of the alpha 2 beta 2 insulin receptor complex (Mr 400,000) into the monomeric 95,000 beta subunit.	Phosphorus-32	16-19	insulin receptor	Homo sapiens	28-44
3026445-2	1986	Pretreatment of 32P-labeled insulin receptors with 50 mM DTT followed by gel filtration chromatography in 0.1% SDS demonstrated the dissociation of the alpha 2 beta 2 insulin receptor complex (Mr 400,000) into the monomeric 95,000 beta subunit.	Dithiothreitol	57-60	insulin receptor	Homo sapiens	28-44
3026445-2	1986	Pretreatment of 32P-labeled insulin receptors with 50 mM DTT followed by gel filtration chromatography in 0.1% SDS demonstrated the dissociation of the alpha 2 beta 2 insulin receptor complex (Mr 400,000) into the monomeric 95,000 beta subunit.	Sodium Dodecyl Sulfate	111-114	insulin receptor	Homo sapiens	28-44
3026445-5	1986	This suggests that the insulin receptor can reoxidize into the Mr 400,000 complex after the removal of DTT by gel filtration chromatography.	Dithiothreitol	103-106	insulin receptor	Homo sapiens	23-39
3766633-1	1986	The effect of a low-dose triphasic oral contraceptive (ethinyl estradiol and levonorgestrel) on glucose tolerance, plasma insulin response to a glucose challenge, and insulin receptor binding to monocytes and erythrocytes was investigated in seven women with previous gestational diabetes and seven nondiabetic control subjects.	triphasic	25-34	insulin receptor	Homo sapiens	167-183
3026365-2	1986	Analysis of the samples by SDS/polyacrylamide-gel electrophoresis and autoradiography revealed the insulin receptor as a predominant band of 450 kDa.	polyacrylamide	31-45	insulin receptor	Homo sapiens	99-115
2877871-4	1986	In analogy with the 152,784 Mr insulin receptor precursor, cleavage of the Arg-Lys-Arg-Arg sequence at position 707 of the IGF-I receptor precursor will generate alpha (80,423 Mr) and beta (70,866 Mr) subunits, which compare with approximately 135,000 Mr (alpha) and 90,000 Mr (beta) fully glycosylated subunits.	Arginine	75-78	insulin receptor	Homo sapiens	31-47
2877871-4	1986	In analogy with the 152,784 Mr insulin receptor precursor, cleavage of the Arg-Lys-Arg-Arg sequence at position 707 of the IGF-I receptor precursor will generate alpha (80,423 Mr) and beta (70,866 Mr) subunits, which compare with approximately 135,000 Mr (alpha) and 90,000 Mr (beta) fully glycosylated subunits.	Lysine	79-82	insulin receptor	Homo sapiens	31-47
2877871-4	1986	In analogy with the 152,784 Mr insulin receptor precursor, cleavage of the Arg-Lys-Arg-Arg sequence at position 707 of the IGF-I receptor precursor will generate alpha (80,423 Mr) and beta (70,866 Mr) subunits, which compare with approximately 135,000 Mr (alpha) and 90,000 Mr (beta) fully glycosylated subunits.	Arginine	83-86	insulin receptor	Homo sapiens	31-47
2877871-4	1986	In analogy with the 152,784 Mr insulin receptor precursor, cleavage of the Arg-Lys-Arg-Arg sequence at position 707 of the IGF-I receptor precursor will generate alpha (80,423 Mr) and beta (70,866 Mr) subunits, which compare with approximately 135,000 Mr (alpha) and 90,000 Mr (beta) fully glycosylated subunits.	Arginine	83-86	insulin receptor	Homo sapiens	31-47
3528154-3	1986	The insulin receptor, isolated by lectin adsorption and two-dimensional nonreducing/reducing polyacrylamide gel electrophoresis, occurred as a single oligomeric species with an apparent alpha 2 beta 2 subunit composition.	polyacrylamide gels	93-111	insulin receptor	Homo sapiens	4-20
3541915-13	1986	The findings demonstrate that vanadate stimulates glucose transport by an effect at a level distal to the insulin receptor.	Vanadates	30-38	insulin receptor	Homo sapiens	106-122
3541915-13	1986	The findings demonstrate that vanadate stimulates glucose transport by an effect at a level distal to the insulin receptor.	Glucose	50-57	insulin receptor	Homo sapiens	106-122
3023061-6	1986	Significant homology, especially with respect to the topography of cysteine residues, was found between the cysteine-rich regions of the human insulin receptor, the human epidermal growth factor receptor and furin.	Cysteine	67-75	insulin receptor	Homo sapiens	143-159
3023061-6	1986	Significant homology, especially with respect to the topography of cysteine residues, was found between the cysteine-rich regions of the human insulin receptor, the human epidermal growth factor receptor and furin.	Cysteine	108-116	insulin receptor	Homo sapiens	143-159
3017998-6	1986	The insulin receptor was found to behave differently in response to phorbol myristate acetate, however, in that only the occupied receptors were stimulated to internalize.	Tetradecanoylphorbol Acetate	68-93	insulin receptor	Homo sapiens	4-20
3827820-0	1986	Characterization of the N-linked high-mannose oligosaccharides of the insulin pro-receptor and mature insulin receptor subunits.	n-linked high-mannose oligosaccharides	24-62	insulin receptor	Homo sapiens	102-118
3827820-1	1986	The insulin receptor is synthesized as a 190,000-Mr single-chain precursor that contains exclusively asparagine-N-linked high-mannose-type carbohydrate chains.	asparagine-n-linked high-	101-126	insulin receptor	Homo sapiens	4-20
3827820-1	1986	The insulin receptor is synthesized as a 190,000-Mr single-chain precursor that contains exclusively asparagine-N-linked high-mannose-type carbohydrate chains.	Mannose	126-133	insulin receptor	Homo sapiens	4-20
3827820-1	1986	The insulin receptor is synthesized as a 190,000-Mr single-chain precursor that contains exclusively asparagine-N-linked high-mannose-type carbohydrate chains.	Carbohydrates	139-151	insulin receptor	Homo sapiens	4-20
3827820-9	1986	The mature alpha- and beta-subunits of the insulin receptor are known to contain both high-mannose-type and complex-type oligosaccharides.	Mannose	91-98	insulin receptor	Homo sapiens	43-59
3827820-9	1986	The mature alpha- and beta-subunits of the insulin receptor are known to contain both high-mannose-type and complex-type oligosaccharides.	Oligosaccharides	121-137	insulin receptor	Homo sapiens	43-59
3539101-4	1986	The phorbol-ester-induced enhancement of internalized insulin in HepG2 cells was additive with the potentiation of endocytosed insulin induced by both the lysosomotropic reagent chloroquine and the ionophore monensin; this indicates that TPA affects the intracellular processing of the insulin receptor at a point other than those disrupted by either of these two reagents.	Phorbol Esters	4-17	insulin receptor	Homo sapiens	286-302
3534894-6	1986	The presence of fructose in the diet prevented any increase in insulin receptor number.	Fructose	16-24	insulin receptor	Homo sapiens	63-79
3526339-4	1986	These results indicate that activators of protein kinase C, such as phorbol esters, desensitize cells to insulin by direct protein kinase C action on the insulin receptor.	Phorbol Esters	68-82	insulin receptor	Homo sapiens	154-170
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Disulfides	29-39	insulin receptor	Homo sapiens	43-59
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Dithiothreitol	82-96	insulin receptor	Homo sapiens	43-59
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Dithiothreitol	131-145	insulin receptor	Homo sapiens	43-59
3019388-1	1986	Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin.	Dithiothreitol	0-14	insulin receptor	Homo sapiens	131-147
3019388-1	1986	Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin.	Dithiothreitol	16-19	insulin receptor	Homo sapiens	131-147
3019388-3	1986	The activation of the insulin receptor/kinase by both DTT and thioredoxin was found to be additive with that of insulin.	Dithiothreitol	54-57	insulin receptor	Homo sapiens	22-38
3019388-6	1986	In the presence of relatively low concentrations of DTT, insulin was found to potentiate the apparent insulin receptor subunit reduction of the native alpha 2 beta 2 heterotetrameric complex into alpha beta heterodimers, when observed by silver staining of sodium dodecyl sulfate-polyacrylamide gels.	Dithiothreitol	52-55	insulin receptor	Homo sapiens	102-118
3019388-6	1986	In the presence of relatively low concentrations of DTT, insulin was found to potentiate the apparent insulin receptor subunit reduction of the native alpha 2 beta 2 heterotetrameric complex into alpha beta heterodimers, when observed by silver staining of sodium dodecyl sulfate-polyacrylamide gels.	Sodium Dodecyl Sulfate	257-279	insulin receptor	Homo sapiens	102-118
3019388-6	1986	In the presence of relatively low concentrations of DTT, insulin was found to potentiate the apparent insulin receptor subunit reduction of the native alpha 2 beta 2 heterotetrameric complex into alpha beta heterodimers, when observed by silver staining of sodium dodecyl sulfate-polyacrylamide gels.	polyacrylamide	280-294	insulin receptor	Homo sapiens	102-118
3733682-5	1986	The insulin receptor was then isolated from 32P-labeled IM-9 cells that had been exposed to insulin.	Phosphorus-32	44-47	insulin receptor	Homo sapiens	4-20
3098013-0	1986	Changes in insulin receptor functions of the erythrocyte by treatment of non-insulin-dependent diabetes mellitus (NIDDM) patients with glibenclamide and diet control.	Glyburide	135-148	insulin receptor	Homo sapiens	11-27
3518947-0	1986	Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose.	Tyrosine	32-40	insulin receptor	Homo sapiens	15-31
3518947-0	1986	Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose.	Deoxyglucose	125-139	insulin receptor	Homo sapiens	15-31
3518947-1	1986	Insulin stimulates the autophosphorylation of tyrosine residues of the beta subunit of the insulin receptor (IR); this modified insulin-independent kinase has increased activity toward exogenous substrates in vitro.	Tyrosine	46-54	insulin receptor	Homo sapiens	109-111
3518947-3	1986	In vivo, these mutations not only result in a substantial decrease in insulin-stimulated IR autophosphorylation but also in a parallel decrease in the insulin-activated uptake of 2-deoxyglucose.	Deoxyglucose	179-193	insulin receptor	Homo sapiens	89-91
3518947-5	1986	IR autophosphorylation is thus implicated in the regulation of IR activities, with tyrosines 1162 and 1163 as major sites of this regulation.	Tyrosine	83-92	insulin receptor	Homo sapiens	0-2
3084215-12	1986	The immunoprecipitation of human insulin receptor is not dependent on the method used for labeling the cells ([125I]insulin cross-linking), inasmuch as the receptor labeled by autophosphorylation with [gamma-32P]ATP could also be immunoprecipitated by TBR serum.	[gamma-32p]atp	201-215	insulin receptor	Homo sapiens	33-49
3084215-12	1986	The immunoprecipitation of human insulin receptor is not dependent on the method used for labeling the cells ([125I]insulin cross-linking), inasmuch as the receptor labeled by autophosphorylation with [gamma-32P]ATP could also be immunoprecipitated by TBR serum.	tbr	252-255	insulin receptor	Homo sapiens	33-49
3539101-5	1986	The potentiation of insulin receptor internalization by tumour-promoting phorbol esters could be completely mimicked by treatment with phospholipase C, but not with phospholipase A, and partially mimicked by treatment with the synthetic diacylglycerol 1-oleoyl-2-acetylglycerol.	Phorbol Esters	73-87	insulin receptor	Homo sapiens	20-36
3539101-5	1986	The potentiation of insulin receptor internalization by tumour-promoting phorbol esters could be completely mimicked by treatment with phospholipase C, but not with phospholipase A, and partially mimicked by treatment with the synthetic diacylglycerol 1-oleoyl-2-acetylglycerol.	Diglycerides	237-251	insulin receptor	Homo sapiens	20-36
3539101-5	1986	The potentiation of insulin receptor internalization by tumour-promoting phorbol esters could be completely mimicked by treatment with phospholipase C, but not with phospholipase A, and partially mimicked by treatment with the synthetic diacylglycerol 1-oleoyl-2-acetylglycerol.	1-oleoyl-2-acetylglycerol	252-277	insulin receptor	Homo sapiens	20-36
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	34-48	insulin receptor	Homo sapiens	56-72
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	34-48	insulin receptor	Homo sapiens	272-288
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	228-242	insulin receptor	Homo sapiens	56-72
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	228-242	insulin receptor	Homo sapiens	272-288
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	421-434	insulin receptor	Homo sapiens	56-72
3539101-6	1986	By these criteria, the effects of phorbol esters on the insulin receptor in HepG2 cells appear to be mediated through protein kinase C. These results support the concept that the activation of protein kinase C by treatment with phorbol esters causes a perturbation of the insulin-receptor-mediated endocytotic pathway in HepG2 cells, reflected in a long-term decreased rate of dissociation of internalized insulin by the phorbol-ester-treated cells.	Phorbol Esters	421-434	insulin receptor	Homo sapiens	272-288
3518798-1	1986	The insulin receptor of liver, adipose, and placental plasma membranes was photoaffinity labeled with radioiodinated N epsilon B29-(monoazidobenzoyl)insulin.	n epsilon b29-(monoazidobenzoyl)insulin	117-156	insulin receptor	Homo sapiens	4-20
3518798-4	1986	The distribution of radioactivity between the three insulin receptor bands was dependent on the tissue, the purity of the receptor preparation, and the conditions of solubilization in SDS.	Sodium Dodecyl Sulfate	184-187	insulin receptor	Homo sapiens	52-68
3513838-1	1986	Processing of the insulin receptor by hepatocytes was studied using a 125I-labelled photoreactive insulin derivative which could be covalently attached to the receptor and facilitate the analysis of receptor structure in isolated subcellular fractions by SDS-polyacrylamide gel electrophoresis.	Iodine-125	70-74	insulin receptor	Homo sapiens	18-34
3513838-1	1986	Processing of the insulin receptor by hepatocytes was studied using a 125I-labelled photoreactive insulin derivative which could be covalently attached to the receptor and facilitate the analysis of receptor structure in isolated subcellular fractions by SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	255-258	insulin receptor	Homo sapiens	18-34
3513838-1	1986	Processing of the insulin receptor by hepatocytes was studied using a 125I-labelled photoreactive insulin derivative which could be covalently attached to the receptor and facilitate the analysis of receptor structure in isolated subcellular fractions by SDS-polyacrylamide gel electrophoresis.	polyacrylamide	259-273	insulin receptor	Homo sapiens	18-34
3017297-1	1986	The insulin receptor is an integral membrane glycoprotein (Mr approximately 300,000) composed of two alpha-subunits (Mr approximately 130,000) and two beta-subunits (Mr approximately 95,000) linked by disulphide bonds.	disulphide	201-211	insulin receptor	Homo sapiens	4-20
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	Homo sapiens	89-105
3017297-12	1986	The purified insulin receptor phosphorylates its own beta-subunit and exogenous protein and peptide substrates on tyrosine residues, a reaction which is insulin-sensitive, Mn2+-dependent and specific for ATP.	Tyrosine	114-122	insulin receptor	Homo sapiens	13-29
3017297-12	1986	The purified insulin receptor phosphorylates its own beta-subunit and exogenous protein and peptide substrates on tyrosine residues, a reaction which is insulin-sensitive, Mn2+-dependent and specific for ATP.	Manganese(2+)	172-176	insulin receptor	Homo sapiens	13-29
3017297-12	1986	The purified insulin receptor phosphorylates its own beta-subunit and exogenous protein and peptide substrates on tyrosine residues, a reaction which is insulin-sensitive, Mn2+-dependent and specific for ATP.	Adenosine Triphosphate	204-207	insulin receptor	Homo sapiens	13-29
3005298-6	1986	The purified brain insulin receptor was found to be identical with the placental insulin receptor in the amount of neuraminidase-sensitive sialic acid and reaction with three monoclonal antibodies to the beta subunit of the placental receptor.	N-Acetylneuraminic Acid	139-150	insulin receptor	Homo sapiens	19-35
3005298-6	1986	The purified brain insulin receptor was found to be identical with the placental insulin receptor in the amount of neuraminidase-sensitive sialic acid and reaction with three monoclonal antibodies to the beta subunit of the placental receptor.	N-Acetylneuraminic Acid	139-150	insulin receptor	Homo sapiens	81-97
3005298-8	1986	These results indicate that the brain insulin receptor differs from the receptor in other tissues and suggests that this difference is not simply due to the amount of sialic acid on the receptor.	N-Acetylneuraminic Acid	167-178	insulin receptor	Homo sapiens	38-54
3007126-1	1986	Various lipids were tested as substrates for the insulin receptor kinase using either receptor partially purified from rat hepatoma cells by wheat-germ-agglutinin-Sepharose chromatography or receptor purified from human placenta by insulin-Sepharose affinity chromatography.	Sepharose	163-172	insulin receptor	Homo sapiens	49-65
2419331-0	1986	Increasing the cAMP content of IM-9 cells alters the phosphorylation state and protein kinase activity of the insulin receptor.	Cyclic AMP	15-19	insulin receptor	Homo sapiens	110-126
3007126-1	1986	Various lipids were tested as substrates for the insulin receptor kinase using either receptor partially purified from rat hepatoma cells by wheat-germ-agglutinin-Sepharose chromatography or receptor purified from human placenta by insulin-Sepharose affinity chromatography.	Sepharose	240-249	insulin receptor	Homo sapiens	49-65
2419331-10	1986	These results suggest that agents that raise intracellular cAMP increase phosphorylation of the insulin receptor on serine and threonine residues, reduce insulin-mediated receptor phosphorylation on tyrosine, serine, and threonine residues, and inhibit the insulin-dependent tyrosine protein kinase activity of the receptor.	Cyclic AMP	59-63	insulin receptor	Homo sapiens	96-112
2419331-10	1986	These results suggest that agents that raise intracellular cAMP increase phosphorylation of the insulin receptor on serine and threonine residues, reduce insulin-mediated receptor phosphorylation on tyrosine, serine, and threonine residues, and inhibit the insulin-dependent tyrosine protein kinase activity of the receptor.	Serine	116-122	insulin receptor	Homo sapiens	96-112
2419331-10	1986	These results suggest that agents that raise intracellular cAMP increase phosphorylation of the insulin receptor on serine and threonine residues, reduce insulin-mediated receptor phosphorylation on tyrosine, serine, and threonine residues, and inhibit the insulin-dependent tyrosine protein kinase activity of the receptor.	Threonine	127-136	insulin receptor	Homo sapiens	96-112
3007126-2	1986	Phosphatidylinositol was phosphorylated to phosphatidylinositol 4-phosphate by the partially purified insulin receptor.	Phosphatidylinositols	0-20	insulin receptor	Homo sapiens	102-118
3007126-2	1986	Phosphatidylinositol was phosphorylated to phosphatidylinositol 4-phosphate by the partially purified insulin receptor.	phosphatidylinositol 4-phosphate	43-75	insulin receptor	Homo sapiens	102-118
3007126-9	1986	These characteristics of the phosphatidylinositol kinase activity of the purified insulin receptor and its metal ion preference paralleled those of the receptor tyrosine kinase activity and differed from bulk phosphatidylinositol kinase activity in cell extracts, which was not significantly inhibited by (Glu80Tyr20)n, stimulated by dithiothreitol or depleted by immunoprecipitation with anti-(insulin receptor) antibody.	Metals	107-112	insulin receptor	Homo sapiens	82-98
3007126-9	1986	These characteristics of the phosphatidylinositol kinase activity of the purified insulin receptor and its metal ion preference paralleled those of the receptor tyrosine kinase activity and differed from bulk phosphatidylinositol kinase activity in cell extracts, which was not significantly inhibited by (Glu80Tyr20)n, stimulated by dithiothreitol or depleted by immunoprecipitation with anti-(insulin receptor) antibody.	Dithiothreitol	334-348	insulin receptor	Homo sapiens	82-98
3002611-7	1986	Commitment to increased insulin receptor expression was demonstrated after 1-h exposure to 1 microM 1 alpha, 25-dihydroxyvitamin D3.	alpha, 25-dihydroxyvitamin d3	102-131	insulin receptor	Homo sapiens	24-40
3002611-8	1986	Agents which induced granulocytic differentiation, such as 160 mM dimethyl sulfoxide and 100 nM retinoic acid, significantly decreased insulin receptor expression compared to monocytic inducing agents.	Dimethyl Sulfoxide	66-84	insulin receptor	Homo sapiens	135-151
3002611-8	1986	Agents which induced granulocytic differentiation, such as 160 mM dimethyl sulfoxide and 100 nM retinoic acid, significantly decreased insulin receptor expression compared to monocytic inducing agents.	Tretinoin	96-109	insulin receptor	Homo sapiens	135-151
2419331-10	1986	These results suggest that agents that raise intracellular cAMP increase phosphorylation of the insulin receptor on serine and threonine residues, reduce insulin-mediated receptor phosphorylation on tyrosine, serine, and threonine residues, and inhibit the insulin-dependent tyrosine protein kinase activity of the receptor.	Threonine	221-230	insulin receptor	Homo sapiens	96-112
3005370-4	1986	The functions of the insulin receptor were examined by measuring specific 125I-insulin binding (receptor concentration, affinity, specificity, pH-, time-, and temperature dependence), insulin-induced down-regulation of the receptor, insulin-stimulated autophosphorylation of the beta-subunit, and phosphorylation of exogenous substrates as well as insulin-stimulated glucose uptake in glioblastoma cells.	Glucose	367-374	insulin receptor	Homo sapiens	21-37
2419331-11	1986	Thus cAMP may attenuate insulin action by altering the state of phosphorylation of the insulin receptor.	Cyclic AMP	5-9	insulin receptor	Homo sapiens	87-103
3512585-3	1986	In the present study the insulin receptor was tagged with a 125I-photoreactive insulin analogue that can be covalently coupled to the insulin receptor by ultraviolet irradiation.	Iodine-125	60-64	insulin receptor	Homo sapiens	25-41
3512585-3	1986	In the present study the insulin receptor was tagged with a 125I-photoreactive insulin analogue that can be covalently coupled to the insulin receptor by ultraviolet irradiation.	Iodine-125	60-64	insulin receptor	Homo sapiens	134-150
3005370-8	1986	Since the glial elements compose a majority of the brain cells, the "normal" structure and function of their insulin receptor might provide a key to understanding the role of insulin in the carbohydrate metabolism of the human central nervous system.	Carbohydrates	190-202	insulin receptor	Homo sapiens	109-125
3001088-5	1986	In unstimulated cells, phosphorylation of the insulin receptor occurred on seryl and to a lesser extent on threonyl residues.	seryl	75-80	insulin receptor	Homo sapiens	46-62
3512542-0	1986	The role of cell surface sialic acid in insulin receptor function and insulin action.	N-Acetylneuraminic Acid	25-36	insulin receptor	Homo sapiens	40-56
3518702-5	1986	Insulin receptor autophosphorylation as stimulated by ATP and insulin failed to affect significantly 125I-insulin binding to partially purified insulin receptor from human placenta.	Adenosine Triphosphate	54-57	insulin receptor	Homo sapiens	0-16
3510210-2	1986	Phosphorylation of the insulin receptor is detected readily in the plasma membrane of these cells by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	117-139	insulin receptor	Homo sapiens	23-39
3510210-2	1986	Phosphorylation of the insulin receptor is detected readily in the plasma membrane of these cells by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	140-154	insulin receptor	Homo sapiens	23-39
3510210-3	1986	In the presence of sodium dodecyl sulfate and under nonreducing conditions, the predominant species of phosphorylated insulin receptor has an apparent molecular mass of 350,000 daltons with the beta-subunit (92,000 daltons) being phosphorylated.	Sodium Dodecyl Sulfate	19-41	insulin receptor	Homo sapiens	118-134
3510210-4	1986	The phosphorylation of the insulin receptor in the isolated plasma membrane is absolutely dependent on insulin; tyrosine residues and, to a lesser extent, serine residues of the receptor are phosphorylated.	Tyrosine	112-120	insulin receptor	Homo sapiens	27-43
3510210-4	1986	The phosphorylation of the insulin receptor in the isolated plasma membrane is absolutely dependent on insulin; tyrosine residues and, to a lesser extent, serine residues of the receptor are phosphorylated.	Serine	155-161	insulin receptor	Homo sapiens	27-43
3510210-5	1986	Treatment of the plasma membrane with N-ethylmaleimide (NEM) has two effects; 1) NEM prevents the formation of a larger form (greater than 350,000 daltons) of the phosphorylated insulin receptor.	Ethylmaleimide	38-54	insulin receptor	Homo sapiens	178-194
3510210-5	1986	Treatment of the plasma membrane with N-ethylmaleimide (NEM) has two effects; 1) NEM prevents the formation of a larger form (greater than 350,000 daltons) of the phosphorylated insulin receptor.	Ethylmaleimide	56-59	insulin receptor	Homo sapiens	178-194
3555257-0	1986	The role of calcium and calmodulin in insulin receptor function in the adipocyte.	Calcium	12-19	insulin receptor	Homo sapiens	38-54
3004334-0	1986	Kinetic properties of the insulin receptor tyrosine protein kinase: activation through an insulin-stimulated tyrosine-specific, intramolecular autophosphorylation.	Tyrosine	43-51	insulin receptor	Homo sapiens	26-42
3004334-3	1986	We have employed the highly purified insulin receptor, immobilized on insulin-Sepharose or eluted in an active form, to define the metal/ATP requirements for kinase activation, the relationship of receptor autophosphorylation to activation, and the kinetic properties of the autophosphorylated, activated receptor kinase.	Sepharose	78-87	insulin receptor	Homo sapiens	37-53
3510133-1	1986	The structure of the insulin receptor in intact human erythrocytes was defined using the techniques of disuccinimidyl suberate (DSS) cross-linking of 125I-insulin and surface [125I]iodination followed by receptor immunoprecipitation.	disuccinimidyl	103-117	insulin receptor	Homo sapiens	21-37
3510133-1	1986	The structure of the insulin receptor in intact human erythrocytes was defined using the techniques of disuccinimidyl suberate (DSS) cross-linking of 125I-insulin and surface [125I]iodination followed by receptor immunoprecipitation.	disuccinimidyl suberate	128-131	insulin receptor	Homo sapiens	21-37
3510133-2	1986	In contrast to a recent report, we found the erythrocyte insulin receptor to be similar in structure to that in classic target tissues for insulin, consisting of at least three species of molecular weight approximately 295,000, 265,000, and 245,000, containing disulfide-linked subunits of molecular weight approximately 130,000 and 95,000.	Disulfides	261-270	insulin receptor	Homo sapiens	57-73
3510136-3	1986	Insulin receptor turnover was estimated by measurement of insulin binding after inhibition of synthesis of functional receptors with tunicamycin (0.5 micrograms/ml).	Tunicamycin	133-144	insulin receptor	Homo sapiens	0-16
2945975-4	1986	Insulin stimulated glycogen synthesis in the insulin receptor bearing cell lines.	Glycogen	19-27	insulin receptor	Homo sapiens	45-61
3020828-0	1986	[Role of the ATP-Mg generated by plasma membranes in mediating signal transmission from the insulin receptor and other regulators to membrane kinase].	atp-mg	13-19	insulin receptor	Homo sapiens	92-108
3001088-5	1986	In unstimulated cells, phosphorylation of the insulin receptor occurred on seryl and to a lesser extent on threonyl residues.	threonyl	107-115	insulin receptor	Homo sapiens	46-62
3001089-7	1986	The insulin receptor made in the presence of the inhibitor can be affinity labeled at the cell surface using 125I-insulin and disuccinimidyl suberate cross-linking; there is also no significant difference in its affinity for insulin.	disuccinimidyl	126-140	insulin receptor	Homo sapiens	4-20
4074360-1	1985	A radioactive photoaffinity probe for the insulin receptor was prepared by derivatizing insulin at its B29 lysine with a novel crosslinking reagent having a cleavable azo linkage.	anthrone	167-170	insulin receptor	Homo sapiens	42-58
4074360-1	1985	A radioactive photoaffinity probe for the insulin receptor was prepared by derivatizing insulin at its B29 lysine with a novel crosslinking reagent having a cleavable azo linkage.	Lysine	107-113	insulin receptor	Homo sapiens	42-58
3902825-0	1985	The effects of cycloheximide and chloroquine on insulin receptor metabolism.	Cycloheximide	15-28	insulin receptor	Homo sapiens	48-64
3902825-0	1985	The effects of cycloheximide and chloroquine on insulin receptor metabolism.	Chloroquine	33-44	insulin receptor	Homo sapiens	48-64
3902825-2	1985	The effects of protein synthesis inhibitors and the lysosomotropic agent chloroquine on the metabolism of the insulin receptor were examined.	Chloroquine	73-84	insulin receptor	Homo sapiens	110-126
3902825-3	1985	Through the use of the heavy-isotope density shift technique, cycloheximide was found to inhibit both the synthesis of new insulin receptor and the inactivation of old cellular insulin receptor.	Cycloheximide	62-75	insulin receptor	Homo sapiens	123-139
3902825-3	1985	Through the use of the heavy-isotope density shift technique, cycloheximide was found to inhibit both the synthesis of new insulin receptor and the inactivation of old cellular insulin receptor.	Cycloheximide	62-75	insulin receptor	Homo sapiens	177-193
3902825-5	1985	Cycloheximide did, however, rapidly and completely inhibit the inactivation of the insulin receptor.	Cycloheximide	0-13	insulin receptor	Homo sapiens	83-99
3902825-7	1985	Puromycin and pactamycin, protein synthesis inhibitors with mechanisms of action which differ from cycloheximide, produced the same effects on insulin receptor metabolism as cycloheximide, indicating that this effect on receptor metabolism is due to the inhibition of protein synthesis and not a secondary effect of cycloheximide.	Puromycin	0-9	insulin receptor	Homo sapiens	143-159
3902825-7	1985	Puromycin and pactamycin, protein synthesis inhibitors with mechanisms of action which differ from cycloheximide, produced the same effects on insulin receptor metabolism as cycloheximide, indicating that this effect on receptor metabolism is due to the inhibition of protein synthesis and not a secondary effect of cycloheximide.	Pactamycin	14-24	insulin receptor	Homo sapiens	143-159
4074346-0	1985	Homogeneous bivalent insulin receptor: purification using insulin coupled to 1,1"-carbonyldiimidazole activated-agarose.	1,1"-carbonyldiimidazole activated-agarose	77-119	insulin receptor	Homo sapiens	21-37
4084284-0	1985	Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor.	Urea	0-4	insulin receptor	Homo sapiens	75-91
4084284-0	1985	Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor.	Urea	0-4	insulin receptor	Homo sapiens	168-184
4084284-0	1985	Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor.	Dithiothreitol	22-36	insulin receptor	Homo sapiens	75-91
4084284-0	1985	Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor.	Dithiothreitol	22-36	insulin receptor	Homo sapiens	168-184
3906655-3	1985	The human insulin receptor expressed in CHO cells specifically binds 125I-labeled insulin but not insulin-like growth factor I, displays insulin-stimulated autophosphorylation of the beta subunit, and mediates insulin-stimulated 2-deoxyglucose uptake.	Iodine-125	69-73	insulin receptor	Homo sapiens	10-26
3906655-3	1985	The human insulin receptor expressed in CHO cells specifically binds 125I-labeled insulin but not insulin-like growth factor I, displays insulin-stimulated autophosphorylation of the beta subunit, and mediates insulin-stimulated 2-deoxyglucose uptake.	Deoxyglucose	229-243	insulin receptor	Homo sapiens	10-26
4084539-6	1985	Addition of [gamma-32P]ATP to the insulin receptor containing vesicles was relatively ineffective in promoting the autophosphorylation of the beta subunit in the absence or presence of insulin.	[gamma-32p]atp	12-26	insulin receptor	Homo sapiens	34-50
3893431-0	1985	Removal of sialic acids from the purified insulin receptor results in enhanced insulin-binding and kinase activities.	Sialic Acids	11-23	insulin receptor	Homo sapiens	42-58
4043557-2	1985	In the present study, we found a subpopulation of antibodies (eluted from a protein A-Sepharose affinity column at pH 4.3) directed at the human fibroblast insulin receptor.	Sepharose	86-95	insulin receptor	Homo sapiens	156-172
2416352-2	1985	The results show that the insulin receptor exists under different free and disulfide-linked combinations of alpha and beta subunits.	Disulfides	75-84	insulin receptor	Homo sapiens	26-42
2415418-4	1985	Semisynthetic human insulin was conjugated to FITC, which resulted in at least four types of FITC-insulin molecules with different affinities to the insulin receptor.	Fluorescein-5-isothiocyanate	46-50	insulin receptor	Homo sapiens	149-165
2415418-4	1985	Semisynthetic human insulin was conjugated to FITC, which resulted in at least four types of FITC-insulin molecules with different affinities to the insulin receptor.	Fluorescein-5-isothiocyanate	93-97	insulin receptor	Homo sapiens	149-165
4043927-1	1985	Previous investigations have demonstrated an increase in monocyte insulin receptor affinity two and five hours following oral carbohydrate loading.	Carbohydrates	126-138	insulin receptor	Homo sapiens	66-82
3907813-1	1985	In previous work, we identified two insulin receptor species, RI (KAV = 0.31) and RII (KAV = 0.53), that could be separated by gel filtration on Sepharose 6B.	Sepharose	145-154	insulin receptor	Homo sapiens	36-52
3927905-0	1985	Inhibition of insulin receptor binding by A23187: synergy with phorbol esters.	Calcimycin	42-48	insulin receptor	Homo sapiens	14-30
3927905-0	1985	Inhibition of insulin receptor binding by A23187: synergy with phorbol esters.	Phorbol Esters	63-77	insulin receptor	Homo sapiens	14-30
3931471-4	1985	After the addition of cyclophosphamide for one week, the anti-insulin receptor autoantibody titer dropped from greater than 1:1,000 to 1:1.	Cyclophosphamide	22-38	insulin receptor	Homo sapiens	62-78
2413806-2	1985	Purification of tyrosyl-phosphorylated insulin receptor was effected by adsorption on and elution (with a hapten) from a column of O-phosphotyrosyl-binding antibody immobilized on protein A-Sepharose (Ab-protein A).	cyclo(tyrosyl-tyrosyl)	16-23	insulin receptor	Homo sapiens	39-55
2413806-2	1985	Purification of tyrosyl-phosphorylated insulin receptor was effected by adsorption on and elution (with a hapten) from a column of O-phosphotyrosyl-binding antibody immobilized on protein A-Sepharose (Ab-protein A).	Sepharose	190-199	insulin receptor	Homo sapiens	39-55
3000460-1	1985	The insulin receptor appears as a tetrameric glycoprotein consisting of two Mr 130,000 subunits (alpha), and two Mr 95,000 subunits (beta) in a disulfide-linked complex.	Disulfides	144-153	insulin receptor	Homo sapiens	4-20
2864925-3	1985	The tumor promoting phorbol esters have been reported to stimulate phosphorylation of the insulin receptor and thereby decrease the ability of insulin to induce tyrosine aminotransferase.	Phorbol Esters	20-34	insulin receptor	Homo sapiens	90-106
3901745-5	1985	Because 125I-labeled insulin transport was demonstrated to be receptor-mediated, factors regulating insulin-receptor binding may also affect the insulin transport rate across the vascular barrier.	Iodine-125	8-12	insulin receptor	Homo sapiens	100-116
2412229-1	1985	The relationship between the structure of the insulin receptor and its kinase activity was studied on the purified receptor treated with different concentrations of dithiothreitol.	Dithiothreitol	165-179	insulin receptor	Homo sapiens	46-62
3891757-3	1985	The subunit stoichiometry of these different high molecular weight forms of the insulin receptor were determined by comparisons of silver-stained gel profiles with the autoradiograms of 125I-insulin specifically cross-linked to the alpha subunit and [gamma-32P]ATP specifically autophosphorylated beta subunit gel profiles.	Silver	131-137	insulin receptor	Homo sapiens	80-96
3891757-3	1985	The subunit stoichiometry of these different high molecular weight forms of the insulin receptor were determined by comparisons of silver-stained gel profiles with the autoradiograms of 125I-insulin specifically cross-linked to the alpha subunit and [gamma-32P]ATP specifically autophosphorylated beta subunit gel profiles.	gamma-32p	251-260	insulin receptor	Homo sapiens	80-96
3891757-3	1985	The subunit stoichiometry of these different high molecular weight forms of the insulin receptor were determined by comparisons of silver-stained gel profiles with the autoradiograms of 125I-insulin specifically cross-linked to the alpha subunit and [gamma-32P]ATP specifically autophosphorylated beta subunit gel profiles.	Adenosine Triphosphate	261-264	insulin receptor	Homo sapiens	80-96
3891757-5	1985	Treatment of the insulin receptor preparations with oxidized glutathione or N-ethylmaleimide prior to SDS-polyacrylamide gel electrophoresis increased the relative amount of the alpha 2 beta 2 complex concomitant with a total disappearance of the alpha 2 beta, alpha 2 beta 1, alpha 2, and free beta forms.	Glutathione	61-72	insulin receptor	Homo sapiens	17-33
3891757-5	1985	Treatment of the insulin receptor preparations with oxidized glutathione or N-ethylmaleimide prior to SDS-polyacrylamide gel electrophoresis increased the relative amount of the alpha 2 beta 2 complex concomitant with a total disappearance of the alpha 2 beta, alpha 2 beta 1, alpha 2, and free beta forms.	Ethylmaleimide	76-92	insulin receptor	Homo sapiens	17-33
3891757-5	1985	Treatment of the insulin receptor preparations with oxidized glutathione or N-ethylmaleimide prior to SDS-polyacrylamide gel electrophoresis increased the relative amount of the alpha 2 beta 2 complex concomitant with a total disappearance of the alpha 2 beta, alpha 2 beta 1, alpha 2, and free beta forms.	Sodium Dodecyl Sulfate	102-105	insulin receptor	Homo sapiens	17-33
3891757-5	1985	Treatment of the insulin receptor preparations with oxidized glutathione or N-ethylmaleimide prior to SDS-polyacrylamide gel electrophoresis increased the relative amount of the alpha 2 beta 2 complex concomitant with a total disappearance of the alpha 2 beta, alpha 2 beta 1, alpha 2, and free beta forms.	polyacrylamide	106-120	insulin receptor	Homo sapiens	17-33
3891757-8	1985	The formation of these lower molecular weight insulin receptor subunit complexes was further demonstrated to be due to SDS/heat-dependent intramolecular sulfhydryl-disulfide exchange occurring within the alpha 2 beta 2 complex.	Sodium Dodecyl Sulfate	119-122	insulin receptor	Homo sapiens	46-62
3891757-8	1985	The formation of these lower molecular weight insulin receptor subunit complexes was further demonstrated to be due to SDS/heat-dependent intramolecular sulfhydryl-disulfide exchange occurring within the alpha 2 beta 2 complex.	sulfhydryl-disulfide	153-173	insulin receptor	Homo sapiens	46-62
3891757-9	1985	These studies demonstrate that the largest disulfide-linked complex (alpha 2 beta 2) is the predominant insulin receptor form purified from the human placenta with the other complexes being generated by proteolysis and by internal subunit dissociation.	Disulfides	43-52	insulin receptor	Homo sapiens	104-120
2990467-1	1985	To characterize the carbohydrate moieties of the insulin receptor on IM-9 lymphocytes, the cells were surface iodinated and solubilized, and the insulin receptors were precipitated with anti-receptor antibody.	Carbohydrates	20-32	insulin receptor	Homo sapiens	49-65
2985615-1	1985	When a partially purified insulin receptor preparation immobilized on insulin-agarose is incubated with [gamma-32P]ATP, Mn2+, and Mg2+ ions, the receptor beta subunit becomes 32P-labeled.	Sepharose	78-85	insulin receptor	Homo sapiens	26-42
2985615-1	1985	When a partially purified insulin receptor preparation immobilized on insulin-agarose is incubated with [gamma-32P]ATP, Mn2+, and Mg2+ ions, the receptor beta subunit becomes 32P-labeled.	[gamma-32p]atp	104-118	insulin receptor	Homo sapiens	26-42
2985615-1	1985	When a partially purified insulin receptor preparation immobilized on insulin-agarose is incubated with [gamma-32P]ATP, Mn2+, and Mg2+ ions, the receptor beta subunit becomes 32P-labeled.	Manganese(2+)	120-124	insulin receptor	Homo sapiens	26-42
2985615-1	1985	When a partially purified insulin receptor preparation immobilized on insulin-agarose is incubated with [gamma-32P]ATP, Mn2+, and Mg2+ ions, the receptor beta subunit becomes 32P-labeled.	magnesium ion	130-134	insulin receptor	Homo sapiens	26-42
2985615-1	1985	When a partially purified insulin receptor preparation immobilized on insulin-agarose is incubated with [gamma-32P]ATP, Mn2+, and Mg2+ ions, the receptor beta subunit becomes 32P-labeled.	Phosphorus-32	111-114	insulin receptor	Homo sapiens	26-42
2985615-2	1985	The 32P-labeling of the insulin receptor beta subunit is increased by 2-3-fold when src kinase is included in the phosphorylation reaction.	Phosphorus-32	4-7	insulin receptor	Homo sapiens	24-40
2985615-4	1985	The Mr = 93,000 receptor beta subunit and the Mr = 125,000 32P-labeled bands are absent when an insulin receptor-deficient sample, prepared by the inclusion of excess free insulin to inhibit the adsorption of the receptor to the insulin-agarose, is phosphorylated in the presence of the src kinase.	Phosphorus-32	59-62	insulin receptor	Homo sapiens	96-112
2985615-6	1985	The src kinase-catalyzed phosphorylation of the insulin receptor is not due to the activation of receptor autophosphorylation because a N-ethylmaleimide-treated receptor preparation devoid of receptor kinase activity is also phosphorylated by the src kinase.	Ethylmaleimide	136-152	insulin receptor	Homo sapiens	48-64
2985615-8	1985	Subsequent to src kinase-mediated tyrosine phosphorylation, the insulin receptor, either immobilized on insulin-agarose or in detergent extracts, exhibits a 2-fold increase in associated kinase activity using histone as substrate.	Tyrosine	34-42	insulin receptor	Homo sapiens	64-80
2985615-8	1985	Subsequent to src kinase-mediated tyrosine phosphorylation, the insulin receptor, either immobilized on insulin-agarose or in detergent extracts, exhibits a 2-fold increase in associated kinase activity using histone as substrate.	Sepharose	112-119	insulin receptor	Homo sapiens	64-80
2985615-9	1985	src kinase mediates phosphorylation of predominantly tyrosine residues on both alpha and beta subunits of the insulin receptor.	Tyrosine	53-61	insulin receptor	Homo sapiens	110-126
2985615-12	1985	These results indicate that: the src kinase catalyzes tyrosine phosphorylation of the insulin receptor alpha and beta subunits; and src kinase-catalyzed phosphorylation of insulin receptor can mimic the action of autophosphorylation to activate the insulin receptor kinase in vitro, although whether this occurs in intact cells remains to be determined.	Tyrosine	54-62	insulin receptor	Homo sapiens	86-102
2985615-12	1985	These results indicate that: the src kinase catalyzes tyrosine phosphorylation of the insulin receptor alpha and beta subunits; and src kinase-catalyzed phosphorylation of insulin receptor can mimic the action of autophosphorylation to activate the insulin receptor kinase in vitro, although whether this occurs in intact cells remains to be determined.	Tyrosine	54-62	insulin receptor	Homo sapiens	172-188
2985615-12	1985	These results indicate that: the src kinase catalyzes tyrosine phosphorylation of the insulin receptor alpha and beta subunits; and src kinase-catalyzed phosphorylation of insulin receptor can mimic the action of autophosphorylation to activate the insulin receptor kinase in vitro, although whether this occurs in intact cells remains to be determined.	Tyrosine	54-62	insulin receptor	Homo sapiens	172-188
2986534-13	1985	The insulin receptor kinase is also inhibited in intact cells by phorbol esters that mediate serine/threonine phosphorylation of the insulin receptor, presumably via the Ca++-phospholipid-dependent protein kinase.	Serine	93-99	insulin receptor	Homo sapiens	4-20
4039320-1	1985	The autophosphorylation reaction responsible for conversion of insulin receptor (from human placenta) to an active tyrosyl-protein kinase was shown to be inhibited by Zn2+ and other divalent metal ions.	Zinc	167-171	insulin receptor	Homo sapiens	63-79
4039320-1	1985	The autophosphorylation reaction responsible for conversion of insulin receptor (from human placenta) to an active tyrosyl-protein kinase was shown to be inhibited by Zn2+ and other divalent metal ions.	Metals	191-196	insulin receptor	Homo sapiens	63-79
4039320-3	1985	Autophosphorylation of insulin receptor was almost completely blocked by 10 microM Zn2+.	Zinc	83-87	insulin receptor	Homo sapiens	23-39
4039320-8	1985	Zn2+ was also observed to inhibit phosphotyrosyl-protein phosphatase activity present in preparations of partially purified insulin receptor.	Zinc	0-4	insulin receptor	Homo sapiens	124-140
4039320-9	1985	These inhibitory effects of Zn2+ should be considered in the design of protocols for the isolation and handling of insulin receptor and possibly other tyrosine kinases.	Zinc	28-32	insulin receptor	Homo sapiens	115-131
2982824-5	1985	Amiloride similarly inhibited the tyrosine phosphorylation of the human placental insulin receptor and the platelet-derived growth factor receptor of Swiss 3T3 cells.	Amiloride	0-9	insulin receptor	Homo sapiens	82-98
2982824-5	1985	Amiloride similarly inhibited the tyrosine phosphorylation of the human placental insulin receptor and the platelet-derived growth factor receptor of Swiss 3T3 cells.	Tyrosine	34-42	insulin receptor	Homo sapiens	82-98
2986534-3	1985	The predominant subunit configuration in the native insulin receptor is a disulfide-linked heterotetrameric structure containing two alpha and two beta subunits.	Disulfides	74-83	insulin receptor	Homo sapiens	52-68
2986534-10	1985	The insulin receptor kinase is regulated by beta-adrenergic agonists and other agents that elevate cAMP in adipocytes, presumably via the cAMP-dependent protein kinase.	Cyclic AMP	99-103	insulin receptor	Homo sapiens	4-20
2986534-13	1985	The insulin receptor kinase is also inhibited in intact cells by phorbol esters that mediate serine/threonine phosphorylation of the insulin receptor, presumably via the Ca++-phospholipid-dependent protein kinase.	Phorbol Esters	65-79	insulin receptor	Homo sapiens	4-20
6090205-1	1984	Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin-stimulated phosphate incorporation from [gamma-32P]ATP into endogenous (membrane) and exogenous phosphatidylinositol.	Phosphates	120-129	insulin receptor	Homo sapiens	0-16
6090205-1	1984	Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin-stimulated phosphate incorporation from [gamma-32P]ATP into endogenous (membrane) and exogenous phosphatidylinositol.	[gamma-32p]atp	149-163	insulin receptor	Homo sapiens	0-16
6090205-1	1984	Insulin receptor preparations from human placenta at various states of purity were shown to catalyze insulin-stimulated phosphate incorporation from [gamma-32P]ATP into endogenous (membrane) and exogenous phosphatidylinositol.	Phosphatidylinositols	205-225	insulin receptor	Homo sapiens	0-16
6378700-2	1984	After covalent cross-linking of 125I-insulin to the insulin receptor on cultured human lymphocytes (IM-9 cells) using disuccinimidyl suberate, we inquired whether the insulin-receptor complex could be immunoprecipitated with anti-insulin antibodies.	disuccinimidyl	118-132	insulin receptor	Homo sapiens	52-68
4041242-0	1985	Insulin receptor protein rendered visible in triton X-114 membranes.	Nonidet P-40	45-57	insulin receptor	Homo sapiens	0-16
3001106-4	1985	Under appropriate conditions, insulin can promote the reaction of the insulin receptor with the organomercurial-agarose derivative.	organomercurial-agarose	96-119	insulin receptor	Homo sapiens	70-86
3001107-4	1985	In an attempt to find a protein that might link the receptor tyrosine kinase to these serine/threonine phosphorylation reactions, we have studied the interaction of a partially purified preparation of insulin receptor with purified preparations of serine/threonine kinases known to phosphorylate glycogen synthase.	Threonine	93-102	insulin receptor	Homo sapiens	201-217
6599719-4	1984	In non-diabetics, low affinity insulin receptor concentration increased after bendrofluazide but high affinity receptor concentration remained unchanged.	Bendroflumethiazide	78-92	insulin receptor	Homo sapiens	31-47
6599719-7	1984	In the long term, non-diabetics may maintain normal glucose tolerance on thiazide diuretics by increasing insulin receptor numbers.	Glucose	52-59	insulin receptor	Homo sapiens	106-122
6599719-7	1984	In the long term, non-diabetics may maintain normal glucose tolerance on thiazide diuretics by increasing insulin receptor numbers.	Thiazides	73-81	insulin receptor	Homo sapiens	106-122
6390435-0	1984	Avidin-biotin affinity chromatography: application to the isolation of human placental insulin receptor.	avidin-biotin	0-13	insulin receptor	Homo sapiens	87-103
6389533-0	1984	Effects of insulin receptor down-regulation on hexose transport in human erythrocytes.	Hexoses	47-53	insulin receptor	Homo sapiens	11-27
6389223-8	1984	beta-Hydroxybutyrate also potentiated the effect of hydrogen peroxide (which acts at a level distal to the insulin receptor) even in cells that had been depleted of insulin receptors by trypsin treatment.	3-Hydroxybutyric Acid	0-20	insulin receptor	Homo sapiens	107-123
6389223-8	1984	beta-Hydroxybutyrate also potentiated the effect of hydrogen peroxide (which acts at a level distal to the insulin receptor) even in cells that had been depleted of insulin receptors by trypsin treatment.	Hydrogen Peroxide	52-69	insulin receptor	Homo sapiens	107-123
6389223-9	1984	Therefore, beta-hydroxybutyrate acts, at least partly, at a post-insulin receptor level.	3-Hydroxybutyric Acid	11-31	insulin receptor	Homo sapiens	65-81
6389227-2	1984	Terbium (Tb3+), an ion of the lanthanide series that has been used as a fluorescent probe for calcium (Ca2+) binding sites in proteins, binds to the proteins in both solubilized and purified human placental insulin receptor preparations.	Terbium	0-7	insulin receptor	Homo sapiens	207-223
6389227-2	1984	Terbium (Tb3+), an ion of the lanthanide series that has been used as a fluorescent probe for calcium (Ca2+) binding sites in proteins, binds to the proteins in both solubilized and purified human placental insulin receptor preparations.	tb3+	9-13	insulin receptor	Homo sapiens	207-223
6389227-7	1984	In addition, Tb3+ could be displaced from insulin-sensitive sites by Ca2+, indicating that there were Ca2+ (and Tb3+) binding sites on or near the insulin receptor.	tb3+	13-17	insulin receptor	Homo sapiens	147-163
6389227-7	1984	In addition, Tb3+ could be displaced from insulin-sensitive sites by Ca2+, indicating that there were Ca2+ (and Tb3+) binding sites on or near the insulin receptor.	tb3+	112-116	insulin receptor	Homo sapiens	147-163
6389227-9	1984	The decrease in Tb3+ fluorescence after insulin binding may be indicative of a conformational change in the insulin receptor precipitated by the binding of insulin.	tb3+	16-20	insulin receptor	Homo sapiens	108-124
6386444-2	1984	We have used dithiotheitol, which has major effects on the oligomeric structure of the insulin receptor, to determine if this decreased antibody recognition is due to alteration in the conformation of insulin itself or to steric factors.	dithiotheitol	13-26	insulin receptor	Homo sapiens	87-103
6479460-2	1984	The insulin receptor preparations were subjected to sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis under reducing or nonreducing conditions.	Sodium Dodecyl Sulfate	52-74	insulin receptor	Homo sapiens	4-20
6479460-2	1984	The insulin receptor preparations were subjected to sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis under reducing or nonreducing conditions.	Sodium Dodecyl Sulfate	76-79	insulin receptor	Homo sapiens	4-20
6479460-2	1984	The insulin receptor preparations were subjected to sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis under reducing or nonreducing conditions.	polyacrylamide	81-95	insulin receptor	Homo sapiens	4-20
6090502-12	1984	Moreover, this regulation of glycogen metabolism is mediated by both the insulin receptor and the IGF receptors.	Glycogen	29-37	insulin receptor	Homo sapiens	73-89
6384270-4	1984	In these studies, the glucose clamp technique was employed to isolate perturbations in plasma glucose and plasma insulin as potential mediators of the regulation of the mitogen-induced T lymphocyte insulin receptor.	Glucose	22-29	insulin receptor	Homo sapiens	198-214
6384270-4	1984	In these studies, the glucose clamp technique was employed to isolate perturbations in plasma glucose and plasma insulin as potential mediators of the regulation of the mitogen-induced T lymphocyte insulin receptor.	Glucose	94-101	insulin receptor	Homo sapiens	198-214
2986534-13	1985	The insulin receptor kinase is also inhibited in intact cells by phorbol esters that mediate serine/threonine phosphorylation of the insulin receptor, presumably via the Ca++-phospholipid-dependent protein kinase.	Threonine	100-109	insulin receptor	Homo sapiens	4-20
2986534-14	1985	These data suggest the hypothesis that a complex network of tyrosine and serine/threonine phosphorylations on the insulin receptor modulate its binding and kinase activities in an antagonistic manner.	Tyrosine	60-68	insulin receptor	Homo sapiens	114-130
2986534-14	1985	These data suggest the hypothesis that a complex network of tyrosine and serine/threonine phosphorylations on the insulin receptor modulate its binding and kinase activities in an antagonistic manner.	Serine	73-79	insulin receptor	Homo sapiens	114-130
2986534-14	1985	These data suggest the hypothesis that a complex network of tyrosine and serine/threonine phosphorylations on the insulin receptor modulate its binding and kinase activities in an antagonistic manner.	Threonine	80-89	insulin receptor	Homo sapiens	114-130
6732235-7	1984	These results indicate that the subcellular distribution of internalized insulin and of intracellular glucose transport activity are different, suggesting that the pathways of intracellular processing of the insulin receptor and the glucose transport mechanism are different.	Glucose	102-109	insulin receptor	Homo sapiens	208-224
6732235-7	1984	These results indicate that the subcellular distribution of internalized insulin and of intracellular glucose transport activity are different, suggesting that the pathways of intracellular processing of the insulin receptor and the glucose transport mechanism are different.	Glucose	233-240	insulin receptor	Homo sapiens	208-224
6389294-1	1984	We have examined insulin binding to the erythrocyte insulin receptor in normal males following a short fast and a test meal or glucose load.	Glucose	127-134	insulin receptor	Homo sapiens	52-68
6374370-4	1984	Scatchard analysis indicated that ATP was acting primarily to change the binding affinity of the insulin receptor.	Adenosine Triphosphate	34-37	insulin receptor	Homo sapiens	97-113
6426651-0	1984	Insulin receptor antibodies causing steroid responsive diabetes mellitus in a patient with myositis.	Steroids	36-43	insulin receptor	Homo sapiens	0-16
6427220-6	1984	Vanadate also stimulated the phosphorylation of the 95,000-dalton subunit of a highly purified insulin receptor from human placenta.	Vanadates	0-8	insulin receptor	Homo sapiens	95-111
6371815-2	1984	As previously seen with antibodies against the insulin receptor from patients with the type B syndrome of insulin resistance and acanthosis nigricans, RAR acutely mimicked the action of insulin by stimulating deoxyglucose uptake.	Deoxyglucose	209-221	insulin receptor	Homo sapiens	47-63
6419784-1	1984	Calcium (Ca2+) increased insulin-receptor binding in both membrane and solubilised receptor preparations.	Calcium	0-7	insulin receptor	Homo sapiens	25-41
6331454-0	1984	Effect of glucose on beta-adrenergic induced downregulation of insulin receptor binding in human fat cells.	Glucose	10-17	insulin receptor	Homo sapiens	63-79
6693383-3	1984	From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1).	Sodium Dodecyl Sulfate	21-43	insulin receptor	Homo sapiens	139-155
6693383-3	1984	From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1).	polyacrylamide	44-58	insulin receptor	Homo sapiens	139-155
6392057-5	1984	After a 24-hour preliminary incubation of cells with glipizide, we found a 44% increase of insulin receptor binding apparently due to an increase of insulin binding sites.	Glipizide	53-62	insulin receptor	Homo sapiens	91-107
6360756-0	1983	Insulin receptor binding to monocytes, insulin secretion, and glucose tolerance following metformin treatment.	Metformin	90-99	insulin receptor	Homo sapiens	0-16
6415086-2	1983	To further elucidate the mechanisms of this action, we studied the effect of glibenclamide on in vivo and in vitro cellular insulin receptor binding in normal subjects.	Glyburide	77-90	insulin receptor	Homo sapiens	124-140
6357090-6	1983	These effects appeared to be mediated via inhibitory actions on the hexose transport system with the preservation of a functional insulin-receptor interaction resulting in insulin stimulation of deoxy-D-glucose transport at physiological insulin concentrations, 250 microU/ml (10 ng/ml).	Hexoses	68-74	insulin receptor	Homo sapiens	130-146
6357090-6	1983	These effects appeared to be mediated via inhibitory actions on the hexose transport system with the preservation of a functional insulin-receptor interaction resulting in insulin stimulation of deoxy-D-glucose transport at physiological insulin concentrations, 250 microU/ml (10 ng/ml).	deoxy-d-glucose	195-210	insulin receptor	Homo sapiens	130-146
6833291-1	1983	Insulin receptor was purified 2400-fold with an overall yield of 40% from human placental membranes by affinity chromatography on wheat germ agglutinin-Sepharose and insulin-Sepharose.	Sepharose	152-161	insulin receptor	Homo sapiens	0-16
6833291-1	1983	Insulin receptor was purified 2400-fold with an overall yield of 40% from human placental membranes by affinity chromatography on wheat germ agglutinin-Sepharose and insulin-Sepharose.	Sepharose	174-183	insulin receptor	Homo sapiens	0-16
6331454-6	1984	In conclusion, low amounts of glucose prevent catecholamine induced down-regulation of insulin receptor binding in human fat cells at physiological temperature.	Glucose	30-37	insulin receptor	Homo sapiens	87-103
6331454-6	1984	In conclusion, low amounts of glucose prevent catecholamine induced down-regulation of insulin receptor binding in human fat cells at physiological temperature.	Catecholamines	46-59	insulin receptor	Homo sapiens	87-103
6693383-3	1984	From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1).	Dithiothreitol	110-124	insulin receptor	Homo sapiens	139-155
6693383-3	1984	From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1).	Disulfides	198-207	insulin receptor	Homo sapiens	139-155
6693383-4	1984	The largest disulfide-linked complex (alpha 2, 2 beta) appears to be the minimum unit of the intact insulin receptor whereas the other complexes appear to be generated from (alpha 2, 2 beta) by proteolytic degradation and/or reduction.	Disulfides	12-21	insulin receptor	Homo sapiens	100-116
6382903-0	1984	[Insulin receptor and postreceptor disorders: significance for the development and therapy of carbohydrate metabolic disorders].	Carbohydrates	94-106	insulin receptor	Homo sapiens	1-17
6582851-9	1983	IGF-I shows cross-reactivity with the insulin receptor, with a potency of 12 and 100 times less than insulin in Krebs-Ringer phosphate buffer and G-buffer respectively.	krebs	112-117	insulin receptor	Homo sapiens	38-54
6582851-9	1983	IGF-I shows cross-reactivity with the insulin receptor, with a potency of 12 and 100 times less than insulin in Krebs-Ringer phosphate buffer and G-buffer respectively.	Phosphates	125-134	insulin receptor	Homo sapiens	38-54
6363065-1	1983	Insulin stimulates a kinase that phosphorylates tyrosines in the insulin receptor; this kinase is tightly associated with the insulin receptor itself.	Tyrosine	48-57	insulin receptor	Homo sapiens	65-81
6363065-1	1983	Insulin stimulates a kinase that phosphorylates tyrosines in the insulin receptor; this kinase is tightly associated with the insulin receptor itself.	Tyrosine	48-57	insulin receptor	Homo sapiens	126-142
6363065-3	1983	As with phosphorylation of the insulin receptor, insulin selectively enhanced by 2-3-fold the phosphorylation of tyrosines in casein.	Tyrosine	113-122	insulin receptor	Homo sapiens	31-47
6195925-10	1983	These results indicate that MIX may counteract insulin receptor downregulation by a cAMP-independent process.	Cyclic AMP	84-88	insulin receptor	Homo sapiens	47-63
6355082-15	1983	Internalization of insulin receptor and its bound ligand were, however, rapidly (less than 10 min) blocked by phenylarsine oxide.	oxophenylarsine	110-128	insulin receptor	Homo sapiens	19-35
6194153-6	1983	The half-time of disappearance of disulfide linked insulin-receptor complexes (I-(S-S)-R) was rapid (4.5 min), consistent with their hypothesized role.	Disulfides	34-43	insulin receptor	Homo sapiens	51-67
6350337-7	1983	It is suggested, therefore, that the action of metformin on the insulin receptor may be one of the mechanisms of the antidiabetic effect of this drug.	Metformin	47-56	insulin receptor	Homo sapiens	64-80
6309826-1	1983	The insulin receptor purified from human placenta by sequential affinity chromatography on wheat germ agglutinin- and insulin-Sepharose to near homogeneity retained tyrosine-specific protein kinase activity.	Sepharose	126-135	insulin receptor	Homo sapiens	4-20
6411700-2	1983	The biosynthesis and carbohydrate processing of the insulin receptor were studied in cultured human lymphocytes by means of metabolic and cell surface labeling, immunoprecipitation with anti-receptor autoantibodies, and analysis on sodium dodecyl sulfate-polyacrylamide gels under reducing conditions.	Carbohydrates	21-33	insulin receptor	Homo sapiens	52-68
6411700-2	1983	The biosynthesis and carbohydrate processing of the insulin receptor were studied in cultured human lymphocytes by means of metabolic and cell surface labeling, immunoprecipitation with anti-receptor autoantibodies, and analysis on sodium dodecyl sulfate-polyacrylamide gels under reducing conditions.	Sodium Dodecyl Sulfate	232-254	insulin receptor	Homo sapiens	52-68
6411700-2	1983	The biosynthesis and carbohydrate processing of the insulin receptor were studied in cultured human lymphocytes by means of metabolic and cell surface labeling, immunoprecipitation with anti-receptor autoantibodies, and analysis on sodium dodecyl sulfate-polyacrylamide gels under reducing conditions.	polyacrylamide	255-269	insulin receptor	Homo sapiens	52-68
6411700-12	1983	In conclusion, the Mr = 190,000 component appears to represent the high mannose precursor form of the insulin receptor that undergoes carbohydrate processing and proteolytic cleavage to generate the two major subunits.	Mannose	72-79	insulin receptor	Homo sapiens	102-118
6411700-12	1983	In conclusion, the Mr = 190,000 component appears to represent the high mannose precursor form of the insulin receptor that undergoes carbohydrate processing and proteolytic cleavage to generate the two major subunits.	Carbohydrates	134-146	insulin receptor	Homo sapiens	102-118
6574482-1	1983	Preparations of insulin receptor from cultured 3T3-L1 adipocytes and human placenta previously was found to catalyze the phosphorylation of the 90,000-dalton component of the insulin receptor on tyrosine residues.	Tyrosine	195-203	insulin receptor	Homo sapiens	16-32
6574482-1	1983	Preparations of insulin receptor from cultured 3T3-L1 adipocytes and human placenta previously was found to catalyze the phosphorylation of the 90,000-dalton component of the insulin receptor on tyrosine residues.	Tyrosine	195-203	insulin receptor	Homo sapiens	175-191
6344921-0	1983	Insulin receptor: insulin-modulated interconversion between distinct molecular forms involving disulfide-sulfhydryl exchange.	Disulfides	95-104	insulin receptor	Homo sapiens	0-16
6344921-0	1983	Insulin receptor: insulin-modulated interconversion between distinct molecular forms involving disulfide-sulfhydryl exchange.	Sulfhydryl Compounds	105-115	insulin receptor	Homo sapiens	0-16
6405894-0	1983	Effect of metformin on insulin receptor binding and diabetic control.	Metformin	10-19	insulin receptor	Homo sapiens	23-39
6337399-4	1983	After previous saturation of the insulin receptor compartment, [123I]insulin was concentrated by the kidneys only and the rate of appearance of free iodide was markedly decreased.	Iodides	149-155	insulin receptor	Homo sapiens	33-49
6340724-5	1983	The photoincorporation of 8-azido[alpha-32P]ATP into placental insulin receptor preparations was carried out to identify the ATP binding site responsible for the protein kinase activity.	8-azido[alpha-32p]atp	26-47	insulin receptor	Homo sapiens	63-79
6340724-5	1983	The photoincorporation of 8-azido[alpha-32P]ATP into placental insulin receptor preparations was carried out to identify the ATP binding site responsible for the protein kinase activity.	Adenosine Triphosphate	44-47	insulin receptor	Homo sapiens	63-79
6340724-9	1983	Phosphotyrosine formation is the primary result of this activity in placental insulin receptor preparations.	Phosphotyrosine	0-15	insulin receptor	Homo sapiens	78-94
6336749-3	1983	The identity of the surface-labeled product as insulin receptor was established by immunoprecipitation with antireceptor antibody and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	134-156	insulin receptor	Homo sapiens	47-63
6849137-2	1983	This subunit of the insulin receptor was also labeled with [alpha-32P]8-azidoadenosine 5"-triphosphate, a photoaffinity label for adenosine triphosphate binding sites.	[alpha-32p]8-azidoadenosine 5"-triphosphate	59-102	insulin receptor	Homo sapiens	20-36
6849137-2	1983	This subunit of the insulin receptor was also labeled with [alpha-32P]8-azidoadenosine 5"-triphosphate, a photoaffinity label for adenosine triphosphate binding sites.	Adenosine Triphosphate	130-152	insulin receptor	Homo sapiens	20-36
6336749-3	1983	The identity of the surface-labeled product as insulin receptor was established by immunoprecipitation with antireceptor antibody and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	157-171	insulin receptor	Homo sapiens	47-63
6343940-5	1983	Dissociation of insulin receptor protein or lipid with Triton X-100 or phospholipase results in significant decreases in 125I insulin binding by retinal blood vessels.	Octoxynol	55-67	insulin receptor	Homo sapiens	16-32
6346428-3	1983	Our data and observations from other laboratories have led to the suggestion that the insulin receptor is a heterodimer of the 134,000 and 95,000 subunits and, in fact, has an immunoglobulin-like structure with heavy and light chains held together by disulfide bonds.	Disulfides	251-260	insulin receptor	Homo sapiens	86-102
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Monosaccharides	67-82	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Fucose	84-90	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Mannose	92-99	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Galactose	101-110	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Glucosamine	115-126	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Carbohydrates	232-244	insulin receptor	Homo sapiens	163-179
6346428-4	1983	Biosynthetic studies showing the incorporation of all four labeled monosaccharides (fucose, mannose, galactose and glucosamine) into the two major subunits of the insulin receptor suggested that both subunits were likely to contain carbohydrate chains of the complex, N-linked type.	Nitrogen	268-269	insulin receptor	Homo sapiens	163-179
6353801-0	1983	[Linking of the insulin-receptor complex with the membrane transport system through ATP generation by plasma membranes].	Adenosine Triphosphate	84-87	insulin receptor	Homo sapiens	16-32
6757253-0	1982	Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes.	Tyrosine	19-27	insulin receptor	Homo sapiens	51-67
6757253-2	1982	Addition of insulin to Triton-solubilized extracts of human placental membranes selectively stimulates the incorporation of 32P from [gamma-32P]ATP into an endogenous 95,000-dalton protein, which is identified as a component of the insulin receptor by immunoprecipitation.	Phosphorus-32	124-127	insulin receptor	Homo sapiens	232-248
6757253-2	1982	Addition of insulin to Triton-solubilized extracts of human placental membranes selectively stimulates the incorporation of 32P from [gamma-32P]ATP into an endogenous 95,000-dalton protein, which is identified as a component of the insulin receptor by immunoprecipitation.	[gamma-32p]atp	133-147	insulin receptor	Homo sapiens	232-248
6891320-0	1982	Inhibition of insulin receptor binding by phorbol esters.	Phorbol Esters	42-56	insulin receptor	Homo sapiens	14-30
7149493-3	1982	A woman with type B extreme insulin resistance developed clinical evidence of masculinization in association with a markedly elevated level of plasma testosterone (1000 ng/dL).	Testosterone	150-162	insulin receptor	Homo sapiens	13-46
7149493-4	1982	In nine women with autoantibodies to the insulin receptor, excessive ovarian production of testosterone was a common feature among the premenopausal patients.	Testosterone	91-103	insulin receptor	Homo sapiens	41-57
6757032-5	1982	This photoprobe was used to specifically label the insulin receptor in the three tissues: after ultra-violet irradiation, sodium dodecyl sulphate-polyacrylamide gel analysis of extracts under reducing conditions revealed that most of the radioactivity was associated with a 130,000 dalton band.	Sodium Dodecyl Sulfate	122-145	insulin receptor	Homo sapiens	51-67
6757032-5	1982	This photoprobe was used to specifically label the insulin receptor in the three tissues: after ultra-violet irradiation, sodium dodecyl sulphate-polyacrylamide gel analysis of extracts under reducing conditions revealed that most of the radioactivity was associated with a 130,000 dalton band.	polyacrylamide	146-160	insulin receptor	Homo sapiens	51-67
6294652-3	1982	It catalyzes the phosphorylation of the 92,000-dalton component of the insulin receptor, histone, and casein; in each case, tyrosine is the principal amino acid modified.	Tyrosine	124-132	insulin receptor	Homo sapiens	71-87
6294652-5	1982	The insulin-activated kinase is copurified with the human placental insulin receptor until the final elution from insulin-Sepharose.	Sepharose	122-131	insulin receptor	Homo sapiens	68-84
6751097-0	1982	Affinity alteration of insulin receptor induced by a phorbol ester.	Phorbol Esters	53-66	insulin receptor	Homo sapiens	23-39
6751097-8	1982	TPA perturbs the insulin receptor of cultured human lymphocytes in a fashion similar to its effect on the epidermal growth factor receptor of several other cell types.	Tetradecanoylphorbol Acetate	0-3	insulin receptor	Homo sapiens	17-33
6178977-0	1982	Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system.	Tyrosine	19-27	insulin receptor	Homo sapiens	51-67
6761204-3	1982	To confirm directly that the insulin receptor is internalized with the ligand, we covalently linked photoreactive 125I-N sigma B29 (azidobenzoyl) insulin to its specific hepatocyte receptor and followed its fate by quantitative electron microscopic autoradiography.	azidobenzoyl	132-144	insulin receptor	Homo sapiens	29-45
6749630-0	1982	Effect of L-dopa administration on insulin binding: possible role of growth hormone in regulation of insulin receptor affinity.	Levodopa	10-16	insulin receptor	Homo sapiens	101-117
6293791-0	1982	Increased insulin receptor binding to monocytes from insulin-dependent diabetic patients after a low-fat, high-starch, high-fiber diet.	Starch	111-117	insulin receptor	Homo sapiens	10-26
6293791-0	1982	Increased insulin receptor binding to monocytes from insulin-dependent diabetic patients after a low-fat, high-starch, high-fiber diet.	Dietary Fiber	124-129	insulin receptor	Homo sapiens	10-26
6807693-0	1982	Insulin receptor binding increased by high carbohydrate low fat diet in non-insulin-dependent diabetics.	Carbohydrates	43-55	insulin receptor	Homo sapiens	0-16
6807693-5	1982	In contrast to the usual low carbohydrate diet, a high carbohydrate diet tends to correct the lowered insulin receptor status observed in maturity-onset diabetics.	Carbohydrates	55-67	insulin receptor	Homo sapiens	102-118
7040416-3	1982	The insulin receptor was labeled with a 125I-photoreactive insulin analogue (B2[2-nitro,4-azidophenylacetyl]des-PheB1-insulin).	b2[2-nitro,4-azidophenylacetyl]des-pheb1	77-117	insulin receptor	Homo sapiens	4-20
7039318-3	1982	The 19-norprogestins can produce these carbohydrate changes and seen to act at the insulin receptor level.	Carbohydrates	39-51	insulin receptor	Homo sapiens	83-99
7026563-0	1981	Affinity of the hepatic insulin receptor is influenced by membrane phospholipids.	Phospholipids	67-80	insulin receptor	Homo sapiens	24-40
7029441-7	1981	Furthermore, Diazoxide therapy in two patients caused a mild but consistent decrease in the number of insulin receptor sites, and the institution of continuous nocturnal nasogastric feedings in a patient with glycogen storage disease type I was followed by amelioration of the hypoglycemia and a marked increase in 125I-insulin specific binding from 5.2 to 9.5%.	Diazoxide	13-22	insulin receptor	Homo sapiens	102-118
7019705-0	1981	Biguanide treatment increases the number of insulin-receptor sites on human erythrocytes.	Biguanides	0-9	insulin receptor	Homo sapiens	44-60
7021559-1	1981	Human placenta insulin receptor was purified 11,000-fold to near homogeneity using DEAE-cellulose chromatography and affinity chromatography on insulin-Sepharose.	DEAE-Cellulose	83-97	insulin receptor	Homo sapiens	15-31
7021559-1	1981	Human placenta insulin receptor was purified 11,000-fold to near homogeneity using DEAE-cellulose chromatography and affinity chromatography on insulin-Sepharose.	Sepharose	152-161	insulin receptor	Homo sapiens	15-31
7020769-1	1981	Insulin and its analogues displaced membrane-bound calcium within a physiological range of insulin concentration, in proportion to both biological potency and ability to displace porcine 125 I-labelled insulin from the insulin receptor.	Calcium	51-58	insulin receptor	Homo sapiens	219-235
6946427-8	1981	These data demonstrate that the major subunits of the insulin receptor are complex glycoproteins that have differences in the nonreducing ends of the carbohydrate chains.	Carbohydrates	150-162	insulin receptor	Homo sapiens	54-70
6946427-10	1981	These labeling techniques provide new tools to examine the role of the carbohydrate moiety in insulin receptor function and turnover.	Carbohydrates	71-83	insulin receptor	Homo sapiens	94-110
6270667-6	1981	Upon gel electrophoresis in the presence of 2-mercaptoethanol, the photolabeled constituent, like the insulin receptor, migrates as a species with an apparent molecular weight of about 140,000; in the absence of reducing agent, a molecular weight greater than 240,000 is observed.	Mercaptoethanol	44-61	insulin receptor	Homo sapiens	102-118
6403102-0	1983	Effect of metformin on insulin receptor binding and glycaemic control in type II diabetes.	Metformin	10-19	insulin receptor	Homo sapiens	23-39
7045574-2	1982	Solubilized, partially purified insulin receptor from human placenta binds to affinity resins in which N alpha,B1-biotinylinsulin is noncovalently attached to AH Sepharose 4B-immobilized-succinolylavidin.	Sepharose	162-174	insulin receptor	Homo sapiens	32-48
7045574-2	1982	Solubilized, partially purified insulin receptor from human placenta binds to affinity resins in which N alpha,B1-biotinylinsulin is noncovalently attached to AH Sepharose 4B-immobilized-succinolylavidin.	succinolylavidin	187-203	insulin receptor	Homo sapiens	32-48
7045574-3	1982	Exposure of the receptor loaded resin to 20 mM biotin results in liberation of a high molecular weight material containing bound 125I-biotinylinsulin, which precipitates with polyethyleneglycol and cross reacts with human insulin receptor antibodies.	Biotin	47-53	insulin receptor	Homo sapiens	222-238
7045574-5	1982	Crude solubilized insulin receptor from human placenta is contaminated with "insulinase" which is inhibited by N-ethylmaleimide.	Ethylmaleimide	111-127	insulin receptor	Homo sapiens	18-34
7045094-6	1982	In the present studies, dithiothreitol added directly to intact rat fat cells or to membranes prepared from rat fat cell, rat liver, or human placenta, reduced the class I disulfides, but not the class II disulfides, of the insulin receptor.	Dithiothreitol	24-38	insulin receptor	Homo sapiens	224-240
7041848-2	1982	Unlike most previously reported cases of islet cell hyperplasia, where the islet cell hyperactivity produced disturbed glucose metabolism (hypoglycemia, this case illustrates compensatory islet cell hyperplasia in response to a perturbation in glucose metabolism by insulin-receptor blockade with resultant hyperglycemia.	Glucose	244-251	insulin receptor	Homo sapiens	266-282
6801160-1	1982	Characteristic of insulin receptor in human placental villi with relation to glucose uptake and glycogenesis was studied in vitro.	Glucose	77-84	insulin receptor	Homo sapiens	18-34
6801160-6	1982	Collectively, the data suggest the presence of insulin receptor in placental villi varying its concentration with gestational age, where insulin plays a role in adjusting glucose uptake and glycogenesis.	Glucose	171-178	insulin receptor	Homo sapiens	47-63
6760709-1	1982	We tested retinyl palmitate for in vivo effects in man and in vitro effects on the IM-9 lymphocyte insulin receptor.	retinol palmitate	10-27	insulin receptor	Homo sapiens	99-115
6756616-2	1982	Further, we have developed conditions under which the basic SM receptor, in the presence of equivalent amounts of insulin receptor, can be selectively and specifically affinity-labeled with 125I-labeled basic SM, using the cross-linking reagent disuccinimidyl suberate (DSS).	disuccinimidyl	245-259	insulin receptor	Homo sapiens	114-130
6756616-9	1982	In comparison, selective DSS labeling of the insulin receptor in the presence of excess basic SM revealed components which, upon electrophoresis under reducing conditions, exhibited apparent molecular weights of 300 000, 140 000, 90 000--100 000, 43 000 and 35 000.	disuccinimidyl suberate	25-28	insulin receptor	Homo sapiens	45-61
6756618-3	1982	Two cross-linkers, which possess succinimide ester residues (disuccinimidyl suberate and dithiobis(succinimidyl propionate)) and react selectively with amino groups, appeared to react relatively specifically with the insulin receptor.	succinimide ester	33-50	insulin receptor	Homo sapiens	217-233
6756618-3	1982	Two cross-linkers, which possess succinimide ester residues (disuccinimidyl suberate and dithiobis(succinimidyl propionate)) and react selectively with amino groups, appeared to react relatively specifically with the insulin receptor.	disuccinimidyl suberate	61-84	insulin receptor	Homo sapiens	217-233
6756618-3	1982	Two cross-linkers, which possess succinimide ester residues (disuccinimidyl suberate and dithiobis(succinimidyl propionate)) and react selectively with amino groups, appeared to react relatively specifically with the insulin receptor.	dithiobis(succinimidylpropionate)	89-123	insulin receptor	Homo sapiens	217-233
7033271-5	1982	Scatchard plots indicated that phenformin increased the insulin receptor"s affinity rather than the number of insulin-binding sites on IM-9 cells.	Phenformin	31-41	insulin receptor	Homo sapiens	56-72
7033271-9	1982	Therefore, these studies suggest that: 1) in vitro, biguanides enhance insulin binding to its receptors in a variety of cell types; 2) this effect of biguanides doesn"t depend on new receptor synthesis; it is a result of changes in the affinity of the insulin receptor; and 3) in contrast to the biguanides, the sulfonylureas do not have a major direct effect on insulin binding to its receptors in most cell types.	Biguanides	52-62	insulin receptor	Homo sapiens	252-275
7033271-9	1982	Therefore, these studies suggest that: 1) in vitro, biguanides enhance insulin binding to its receptors in a variety of cell types; 2) this effect of biguanides doesn"t depend on new receptor synthesis; it is a result of changes in the affinity of the insulin receptor; and 3) in contrast to the biguanides, the sulfonylureas do not have a major direct effect on insulin binding to its receptors in most cell types.	Biguanides	150-160	insulin receptor	Homo sapiens	252-275
7033271-9	1982	Therefore, these studies suggest that: 1) in vitro, biguanides enhance insulin binding to its receptors in a variety of cell types; 2) this effect of biguanides doesn"t depend on new receptor synthesis; it is a result of changes in the affinity of the insulin receptor; and 3) in contrast to the biguanides, the sulfonylureas do not have a major direct effect on insulin binding to its receptors in most cell types.	Biguanides	150-160	insulin receptor	Homo sapiens	252-275
7033271-9	1982	Therefore, these studies suggest that: 1) in vitro, biguanides enhance insulin binding to its receptors in a variety of cell types; 2) this effect of biguanides doesn"t depend on new receptor synthesis; it is a result of changes in the affinity of the insulin receptor; and 3) in contrast to the biguanides, the sulfonylureas do not have a major direct effect on insulin binding to its receptors in most cell types.	Sulfonylurea Compounds	312-325	insulin receptor	Homo sapiens	252-275
7319476-3	1981	After AcA 34 gel chromatography, affinity chromatography and DEAE-Sephacel chromatography an insulin receptor preparation was obtained which was 2500-fold purified over crude homogenate and which had a specific binding activity of up to 1 x 10(-9) mol insulin/mg protein.	deae-sephacel	61-74	insulin receptor	Homo sapiens	93-109
7319476-6	1981	Dodecyl sulfate gradient gel electrophoresis of the purified insulin receptor protein showed up to eight protein bands in the range from 38 to 175 kDa.	dodecyl sulfate	0-15	insulin receptor	Homo sapiens	61-77
7028773-9	1981	Finally, the enhanced neonatal glucose tolerance of these babies may be related not only to the hyperinsulinemia but also to increased insulin sensitivity mediated, in part, by the increased insulin receptor binding.	Glucose	31-38	insulin receptor	Homo sapiens	191-207
7018254-6	1981	Maximal effects of insulin on glucose production and utilization occurred at plasma insulin concentrations causing 11 and 49% insulin receptor occupancy, respectively.	Glucose	30-37	insulin receptor	Homo sapiens	126-142
7228853-7	1981	This strongly suggests that inactive aglycoinsulin receptor accumulated post-translationally during chronic treatment with tunicamycin and then re-entered the glycosylation pathway when the inhibitor was removed giving rise to a functional insulin receptor.	Tunicamycin	123-134	insulin receptor	Homo sapiens	43-59
7021139-5	1981	From these data it appears that buffers induce variations in binding properties of the human placenta insulin receptor, thus, at ths present state of our knowledge, no definite conclusions can be drawn on the effect of procedures, such as solubilization, on human placenta insulin receptor affinity and/or concentration.	Thorium	129-132	insulin receptor	Homo sapiens	102-118
6940121-1	1981	We have identified the subunits of the insulin receptor in cultured human lymphocytes (IM-9 line) by biosynthetic labeling with [35S]methionine and specific precipitation with autoantibodies against the insulin receptor.	Sulfur-35	129-132	insulin receptor	Homo sapiens	39-55
6450778-5	1981	In 68 studies from seven families that provide examples of two haplotype identical matches, haplo-identical matches and total haplo mismatches, the presence of an insulin receptor correlated in every case with a positive MLC as estimated by [3H]thymidine incorporation.	Tritium	242-244	insulin receptor	Homo sapiens	163-179
6450778-5	1981	In 68 studies from seven families that provide examples of two haplotype identical matches, haplo-identical matches and total haplo mismatches, the presence of an insulin receptor correlated in every case with a positive MLC as estimated by [3H]thymidine incorporation.	Thymidine	245-254	insulin receptor	Homo sapiens	163-179
6940121-1	1981	We have identified the subunits of the insulin receptor in cultured human lymphocytes (IM-9 line) by biosynthetic labeling with [35S]methionine and specific precipitation with autoantibodies against the insulin receptor.	Methionine	133-143	insulin receptor	Homo sapiens	39-55
6940121-9	1981	In conclusion, we have biosynthetically labeled the insulin receptor with [35S]methionine and showed that the receptor consists of two major glycoprotein subunits with apparent molecular weights of 130,000 and 90,000.	Sulfur-35	75-78	insulin receptor	Homo sapiens	52-68
6940121-9	1981	In conclusion, we have biosynthetically labeled the insulin receptor with [35S]methionine and showed that the receptor consists of two major glycoprotein subunits with apparent molecular weights of 130,000 and 90,000.	Methionine	79-89	insulin receptor	Homo sapiens	52-68
7002662-6	1980	These data suggest that acute alteration of insulin receptor function could occur in erythrocytes by small amounts of dexamethasone or prednisone through a mechanism consistent with a decrease in receptor affinity rather than a decrease in the number of receptors.	Dexamethasone	118-131	insulin receptor	Homo sapiens	44-60
7451643-1	1981	Combined estrogen/progestagen oral contraceptives (OC) have been reported to be associated with a deterioration of glucose tolerance and a decrease in insulin sensitivity; thus, since it has been suggested that steroids affect insulin receptor properties, the influence of OC on insulin receptors was investigated.	Steroids	211-219	insulin receptor	Homo sapiens	227-243
7451643-8	1981	The present data appear to confirm that sex steroids affect the insulin receptor and lend further support to the concept that caution must be used in clinical studies of insulin receptors when women are included.	Steroids	44-52	insulin receptor	Homo sapiens	64-80
7429030-1	1980	Three forms of disulfide-linked insulin receptor complexes are labeled by covalent cross-linking to receptor-bound 125I-insulin in native adipocyte or liver membranes.	Disulfides	15-24	insulin receptor	Homo sapiens	32-48
7002662-6	1980	These data suggest that acute alteration of insulin receptor function could occur in erythrocytes by small amounts of dexamethasone or prednisone through a mechanism consistent with a decrease in receptor affinity rather than a decrease in the number of receptors.	Prednisone	135-145	insulin receptor	Homo sapiens	44-60
6997328-1	1980	Results of a recent study suggested that depending upon the glucocorticoid or the model used, opposite changes occur in insulin binding; in fact, the increase in insulin receptor number on monocytes after prednisone ingestion in man appears to contrast with previous reports in animals in which a decrease was shown after dexamethasone.	Prednisone	205-215	insulin receptor	Homo sapiens	162-178
6997328-1	1980	Results of a recent study suggested that depending upon the glucocorticoid or the model used, opposite changes occur in insulin binding; in fact, the increase in insulin receptor number on monocytes after prednisone ingestion in man appears to contrast with previous reports in animals in which a decrease was shown after dexamethasone.	Dexamethasone	322-335	insulin receptor	Homo sapiens	162-178
6995104-3	1980	To investigate the role of pancreatic glucagon we have studied the effect of arginine infusion on monocyte insulin receptor in five normal subjects.	Arginine	77-85	insulin receptor	Homo sapiens	107-123
6986378-9	1980	These data indicate that the labeled monomer with an apparent molecular weight of 125,00 represents a high affinity insulin receptor subunit which exists in the native adipocyte plasma membrane in a disulfide-linked complex.	Disulfides	199-208	insulin receptor	Homo sapiens	116-132
6989367-0	1980	Effect of vinblastine on the insulin-receptor interaction in mammalian heart muscle.	Vinblastine	10-21	insulin receptor	Homo sapiens	29-45
567493-8	1978	Anti-insulin receptor serum from a patient with Acanthosis Nigricans Type B competed with 125I-labeled insulin for binding to cell surface sites.	Iodine-125	90-94	insulin receptor	Homo sapiens	5-21
6928620-1	1980	A density-shift method is described for analyzing insulin receptor synthesis and turnover in cultured cells labeled with "heavy" amino acids (2H, 13C, and 15N).	Deuterium	142-144	insulin receptor	Homo sapiens	50-66
6928620-1	1980	A density-shift method is described for analyzing insulin receptor synthesis and turnover in cultured cells labeled with "heavy" amino acids (2H, 13C, and 15N).	13c	146-149	insulin receptor	Homo sapiens	50-66
6928620-1	1980	A density-shift method is described for analyzing insulin receptor synthesis and turnover in cultured cells labeled with "heavy" amino acids (2H, 13C, and 15N).	15n	155-158	insulin receptor	Homo sapiens	50-66
472708-1	1979	By using the chelate EDTA at low concentration to remove the bivalent cations in the plasma membranes and followed by n-butanol to extract the membrane lipids, we have obtained a water-soluble insulin receptor without detergent from the liver-cell plasma membranes.	Edetic Acid	21-25	insulin receptor	Homo sapiens	193-209
472708-1	1979	By using the chelate EDTA at low concentration to remove the bivalent cations in the plasma membranes and followed by n-butanol to extract the membrane lipids, we have obtained a water-soluble insulin receptor without detergent from the liver-cell plasma membranes.	1-Butanol	118-127	insulin receptor	Homo sapiens	193-209
472708-4	1979	It is thus proved that the insulin-receptor protein obtained by this method is completely soluble in water.	Water	101-106	insulin receptor	Homo sapiens	27-43
420863-0	1979	Inhibition of insulin receptor binding by dimethyl sulfoxide.	Dimethyl Sulfoxide	42-60	insulin receptor	Homo sapiens	14-30
420863-6	1979	Analysis of the data of binding at steady state indicated that the decrease in binding of 125I-labeled insulin was due to a reduced affinity of the insulin receptor without noticeable change in the concentration of receptor sites.	Iodine-125	90-94	insulin receptor	Homo sapiens	148-164
279910-1	1978	Exposure of adipocytes to antibodies to the insulin receptor results in a blockade of (125)I-labeled insulin binding, stimulation of glucose oxidation, and many more insulin-like effects.	Glucose	133-140	insulin receptor	Homo sapiens	44-60
27236-2	1978	In the present study, the insulin receptor of the avian erythrocyte has been solubilized in Triton X-100, extensively characterized and partially purified, and its properties compared to those of the membrane-bound receptor.	Octoxynol	92-104	insulin receptor	Homo sapiens	26-42
33798-1	1978	The insulin receptor for human placental membranes has been solubilized in Triton X-100 and its properties have been examined in detail.	Octoxynol	75-87	insulin receptor	Homo sapiens	4-20
4375575-0	1974	[Proceedings: Carbohydrate and lipid metabolism: specificity of the insulin receptor in obese animals].	Carbohydrates	14-26	insulin receptor	Homo sapiens	68-84
1069300-0	1976	Direct method for detection and characterization of cell surface receptors for insulin by means of 125I-labeled autoantibodies against the insulin receptor.	Iodine-125	99-103	insulin receptor	Homo sapiens	139-155
5434-9	1976	Divalent cations (calcium and magnesium) appear to stabilize the insulin-receptor interaction, since higher degrees of receptor occupancy were required to achieve a given rate of dissociation of 125I-insulin.	Calcium	18-25	insulin receptor	Homo sapiens	65-81
5434-9	1976	Divalent cations (calcium and magnesium) appear to stabilize the insulin-receptor interaction, since higher degrees of receptor occupancy were required to achieve a given rate of dissociation of 125I-insulin.	Magnesium	30-39	insulin receptor	Homo sapiens	65-81
1165235-4	1975	Termination of the glucose transport action of insulin (which includes insulin-receptor disassociation and all other steps leading to decelerated glucose entry) began within 2 min and was complete within 30 min.	Glucose	19-26	insulin receptor	Homo sapiens	71-87
607397-3	1977	After passing the membrane protein dissolved in 1% DOC over a Sepharose 4B column, a peak with insulin receptor binding activity has been shown in the void volumn.	Desoxycorticosterone	51-54	insulin receptor	Homo sapiens	95-111
607397-3	1977	After passing the membrane protein dissolved in 1% DOC over a Sepharose 4B column, a peak with insulin receptor binding activity has been shown in the void volumn.	Sepharose	62-71	insulin receptor	Homo sapiens	95-111
4351804-2	1973	Various lines of evidence indicate that the insulin receptor on the plasma membrane, in addition to the insulin coupled to the agarose, was responsible for the observed binding.	Sepharose	127-134	insulin receptor	Homo sapiens	44-60
4501116-0	1972	Isolation of the insulin receptor of liver and fat-cell membranes (detergent-solubilized-( 125 I)insulin-polyethylene glycol precipitation-sephadex).	Polyethylene Glycols	105-124	insulin receptor	Homo sapiens	17-33
4501116-0	1972	Isolation of the insulin receptor of liver and fat-cell membranes (detergent-solubilized-( 125 I)insulin-polyethylene glycol precipitation-sephadex).	sephadex	139-147	insulin receptor	Homo sapiens	17-33
6034871-0	1967	Tryptophan residues may be at the insulin receptor site in muscle.	Tryptophan	0-10	insulin receptor	Homo sapiens	34-50
34001235-5	2021	The involvement of CAV1 in glucose/lipid homeostasis is revealed and could modify the signaling of the insulin receptor.	Glucose	27-34	insulin receptor	Homo sapiens	103-119
34052843-1	2021	In this study, we report the emissive properties of a heteroleptic cyclometalated Ir(iii) complex, [Ir(bzq)2(PBO)] (bzqH = benzo[h]quinoline; PBOH = 2-(2-hydroxyphenyl)benzoxazole).	[ir(bzq)2(pbo)] (bzqh	99-120	insulin receptor	Homo sapiens	85-88
34052843-1	2021	In this study, we report the emissive properties of a heteroleptic cyclometalated Ir(iii) complex, [Ir(bzq)2(PBO)] (bzqH = benzo[h]quinoline; PBOH = 2-(2-hydroxyphenyl)benzoxazole).	benzo(h)quinoline	123-140	insulin receptor	Homo sapiens	85-88
34052843-1	2021	In this study, we report the emissive properties of a heteroleptic cyclometalated Ir(iii) complex, [Ir(bzq)2(PBO)] (bzqH = benzo[h]quinoline; PBOH = 2-(2-hydroxyphenyl)benzoxazole).	pboh	142-146	insulin receptor	Homo sapiens	85-88
34052843-1	2021	In this study, we report the emissive properties of a heteroleptic cyclometalated Ir(iii) complex, [Ir(bzq)2(PBO)] (bzqH = benzo[h]quinoline; PBOH = 2-(2-hydroxyphenyl)benzoxazole).	2-(2'-hydroxyphenyl)benzoxazole	149-179	insulin receptor	Homo sapiens	85-88
33609563-3	2021	Metformin is an established insulin receptor sensitizing antihyperglycemic agent, is highly affordable, and has superior safety and efficacy profiles.	Metformin	0-9	insulin receptor	Homo sapiens	28-44
33736254-9	2021	Several differentially expressed genes (such as OXR1, OXSR1, INSR, and PPARA) and changed metabolites (such as pyruvate, acetate, and L-phenylalanine) were involved in the combined toxicity of As and PA.	Pyruvic Acid	111-119	insulin receptor	Homo sapiens	61-65
33736254-9	2021	Several differentially expressed genes (such as OXR1, OXSR1, INSR, and PPARA) and changed metabolites (such as pyruvate, acetate, and L-phenylalanine) were involved in the combined toxicity of As and PA.	Acetates	121-128	insulin receptor	Homo sapiens	61-65
33569729-7	2021	RESULTS: In the longitudinal study, significant relationships were found between remission of IR and changes in visceral adiposity index (VAI) (r = 0.452, P < 0.05) and triglyceride-glucose index (TyG) (r = 0.650, P < 0.01).	Triglycerides	169-181	insulin receptor	Homo sapiens	94-96
33711432-5	2021	This review summarizes the pathogenesis of depression from six of the most related receptors and their associated genes, including N-methyl-D-aspartate receptor, alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor, glucocoricoid receptor, 5-hydroxytryptamine receptor, GABAA receptor alpha2, and dopamine receptor; and several "non-classic" receptors, such as metabotropic glutamate receptor, opioid receptor, and insulin receptor.	Dopamine	310-318	insulin receptor	Homo sapiens	407-444
33879610-3	2021	We show that IR preferentially stimulates phosphorylations associated with mammalian target of rapamycin complex 1 (mTORC1) and Akt pathways, whereas IGF1R preferentially stimulates phosphorylations on proteins associated with the Ras homolog family of guanosine triphosphate hydrolases (Rho GTPases), and cell cycle progression.	Sirolimus	95-104	insulin receptor	Homo sapiens	13-15
33900852-10	2021	At the protein level, virilizing testosterone concentrations were associated with increased PI3K 110alpha in liver and increased INSR and phospho(Ser256)-FOXO1 in visceral (v) WAT but decreased phospho(Ser473)-AKT in vWAT and scWAT.	Testosterone	33-45	insulin receptor	Homo sapiens	129-133
33591957-6	2021	The absence of LPCAT3 reduced phospholipid packing of cellular membranes and increased plasma membrane lipid clustering, suggesting that LPCAT3 affects insulin receptor phosphorylation by modulating plasma membrane lipid organization.	Phospholipids	30-42	insulin receptor	Homo sapiens	152-168
33089594-11	2021	CONCLUSION: in subjects with AO and MO, postprandial triglycerides values are higher than healthy individuals and independently predicted by fasting IR parameters.	Triglycerides	53-66	insulin receptor	Homo sapiens	149-151
33729232-0	2021	Recent progress in oxychalcogenides as IR nonlinear optical materials.	oxychalcogenides	19-35	insulin receptor	Homo sapiens	39-41
33729232-1	2021	Currently, non-centrosymmetric oxychalcogenides, a class of newly developed heteroanionic compounds, have emerged as promising candidates for IR nonlinear optical (NLO) materials due to the fact that they can combine the impressive second-harmonic generation (SHG) responses of chalcogenides with the wide energy gaps of oxides.	oxychalcogenides	31-47	insulin receptor	Homo sapiens	142-144
33729232-1	2021	Currently, non-centrosymmetric oxychalcogenides, a class of newly developed heteroanionic compounds, have emerged as promising candidates for IR nonlinear optical (NLO) materials due to the fact that they can combine the impressive second-harmonic generation (SHG) responses of chalcogenides with the wide energy gaps of oxides.	chalcogenides	34-47	insulin receptor	Homo sapiens	142-144
33729232-3	2021	In this Frontiers article, the recent developments of oxychalcogenides as IR-NLO candidates are summarized.	oxychalcogenides	54-70	insulin receptor	Homo sapiens	74-76
33569729-7	2021	RESULTS: In the longitudinal study, significant relationships were found between remission of IR and changes in visceral adiposity index (VAI) (r = 0.452, P < 0.05) and triglyceride-glucose index (TyG) (r = 0.650, P < 0.01).	Glucose	182-189	insulin receptor	Homo sapiens	94-96
33569729-10	2021	TyG showed better ability to predict IR in normal weight females (best cutoff value: 8.39 AUC = 0.813, P < 0.001).	8-methyl-2-{[(pyridin-4-yl)sulfanyl]methyl}quinazolin-4(3H)-one	0-3	insulin receptor	Homo sapiens	37-39
33663226-16	2021	Pioglitazone significantly reduced myocardial IR, restored glucose metabolism, and improved cardiac function in pubertal CH animals.	Pioglitazone	0-12	insulin receptor	Homo sapiens	46-48
33464083-2	2021	In the presence of 1 mol % fac-Ir(ppy)3, a variety of spiro[4.5]deca-1,7,9-trien-6-ones were obtained in moderate to excellent yields under mild conditions.	-1,7,9-trien-6-ones	68-87	insulin receptor	Homo sapiens	31-39
33091325-2	2021	The synthesized polymers were characterized through IR, 1H NMR, and UV-visible spectroscopy techniques.	Polymers	16-24	insulin receptor	Homo sapiens	52-54
33634518-5	2021	We present the current literature on the importance of the insulin receptor with respect to regulating glucose and energy homeostasis and mood-related behaviours.	Glucose	103-110	insulin receptor	Homo sapiens	59-75
33670803-0	2021	Effect of Modification of Amorphous Silica with Ammonium Agents on the Physicochemical Properties and Hydrogenation Activity of Ir/SiO2 Catalysts.	Silicon Dioxide	36-42	insulin receptor	Homo sapiens	128-130
33670803-0	2021	Effect of Modification of Amorphous Silica with Ammonium Agents on the Physicochemical Properties and Hydrogenation Activity of Ir/SiO2 Catalysts.	Ammonium Compounds	48-56	insulin receptor	Homo sapiens	128-130
33670803-0	2021	Effect of Modification of Amorphous Silica with Ammonium Agents on the Physicochemical Properties and Hydrogenation Activity of Ir/SiO2 Catalysts.	Silicon Dioxide	131-135	insulin receptor	Homo sapiens	128-130
33670803-6	2021	As modified amorphous SiO2 materials used as a support for iridium (1 wt %, Ir(acac)3) nanoparticles permitted to obtain highly active catalysts for toluene hydrogenation under atmospheric pressure.	Silicon Dioxide	22-26	insulin receptor	Homo sapiens	76-78
33670803-6	2021	As modified amorphous SiO2 materials used as a support for iridium (1 wt %, Ir(acac)3) nanoparticles permitted to obtain highly active catalysts for toluene hydrogenation under atmospheric pressure.	Iridium	59-66	insulin receptor	Homo sapiens	76-78
33670803-6	2021	As modified amorphous SiO2 materials used as a support for iridium (1 wt %, Ir(acac)3) nanoparticles permitted to obtain highly active catalysts for toluene hydrogenation under atmospheric pressure.	Toluene	149-156	insulin receptor	Homo sapiens	76-78
33600899-11	2021	The improvement of IR after RSA is improved greater by patient questionnaires compared to physical exam.	rabbit sperm membrane autoantigen	28-31	insulin receptor	Homo sapiens	19-21
33242225-0	2021	Iridium(III) Sensitizers and Energy Upconversion: The Influence of Ligand Structure Upon TTA-UC Performance.	1-(carboxymethylthio)tetradecane	89-92	insulin receptor	Homo sapiens	8-11
33242225-2	2021	These species are demonstrated to be effective cyclometalating ligands for Ir(III) yielding complexes of the form [Ir(C^N)2(bipy)]PF6 (where C^N = cyclometalating ligand; bipy = 2,2"-bipyridine).	[ir(c	114-119	insulin receptor	Homo sapiens	75-82
33242225-2	2021	These species are demonstrated to be effective cyclometalating ligands for Ir(III) yielding complexes of the form [Ir(C^N)2(bipy)]PF6 (where C^N = cyclometalating ligand; bipy = 2,2"-bipyridine).	2,2'-Dipyridyl	124-128	insulin receptor	Homo sapiens	75-82
33242225-2	2021	These species are demonstrated to be effective cyclometalating ligands for Ir(III) yielding complexes of the form [Ir(C^N)2(bipy)]PF6 (where C^N = cyclometalating ligand; bipy = 2,2"-bipyridine).	2,2'-Dipyridyl	178-193	insulin receptor	Homo sapiens	75-82
33358613-4	2021	We found that adamantane-derived compounds bind to the insulin receptor more effectively (Kd value of 0.5 muM) than proline-derived compounds (Kd values of 15-38 muM) bearing the same peptides.	Adamantane	14-24	insulin receptor	Homo sapiens	55-71
33583602-3	2021	In this study, we desired to elucidate the mechanisms of miR-103 in IR of PCOS.	mir-103	57-64	insulin receptor	Homo sapiens	68-70
33358613-4	2021	We found that adamantane-derived compounds bind to the insulin receptor more effectively (Kd value of 0.5 muM) than proline-derived compounds (Kd values of 15-38 muM) bearing the same peptides.	Proline	116-123	insulin receptor	Homo sapiens	55-71
33293347-7	2021	Hepatocellular insulin signaling, assessed for the first time in humans, exhibited a proximal block in insulin-resistant subjects: Signaling was attenuated from the level of the insulin receptor through both glucose and lipogenesis pathways.	Glucose	208-215	insulin receptor	Homo sapiens	178-194
33347268-1	2021	An intriguing aggregation-induced electrochemiluminescence (AIECL) bioconjugate was fabricated by encapsulating fac-tris(2-phenylpyridine)iridium(III) complexes [Ir(ppy)3] in the apoferritin (apoFt) cavity for biosensing application.	Ir(ppy)3	112-150	insulin receptor	Homo sapiens	162-170
33347268-2	2021	Based on the unique pH-dependent disassembly/reassembly characteristic of apoFt, approximately 44.3 molecules of Ir(ppy)3 aggregated in the single cavity through both intermolecular pi-pi-stacking interactions and hydrogen bonds that efficiently restricted the intramolecular motions to trigger the AIECL effect.	Hydrogen	214-222	insulin receptor	Homo sapiens	113-121
33347268-3	2021	Compared to monomers, Ir(ppy)3 aggregates performed 5.3-fold-enhanced ECL emission using tri-n-propylamine (TPrA) as a coreactant.	tripropylamine	89-106	insulin receptor	Homo sapiens	22-30
33347268-3	2021	Compared to monomers, Ir(ppy)3 aggregates performed 5.3-fold-enhanced ECL emission using tri-n-propylamine (TPrA) as a coreactant.	tripropylamine	108-112	insulin receptor	Homo sapiens	22-30
33347268-5	2021	To further catalyze the ECL reaction between the reductive TPrA  and the oxidative Ir(ppy)3+  radicals, a conductive and electroactive substrate of Fe2N and gold nanoparticle-codecorated reduced graphene oxide (Fe2N/rGO/Au) was established to incubate the capture antibody.	fe2n	148-152	insulin receptor	Homo sapiens	83-91
33347268-5	2021	To further catalyze the ECL reaction between the reductive TPrA  and the oxidative Ir(ppy)3+  radicals, a conductive and electroactive substrate of Fe2N and gold nanoparticle-codecorated reduced graphene oxide (Fe2N/rGO/Au) was established to incubate the capture antibody.	graphene oxide	195-209	insulin receptor	Homo sapiens	83-91
33347268-5	2021	To further catalyze the ECL reaction between the reductive TPrA  and the oxidative Ir(ppy)3+  radicals, a conductive and electroactive substrate of Fe2N and gold nanoparticle-codecorated reduced graphene oxide (Fe2N/rGO/Au) was established to incubate the capture antibody.	fe2n	211-215	insulin receptor	Homo sapiens	83-91
33347268-5	2021	To further catalyze the ECL reaction between the reductive TPrA  and the oxidative Ir(ppy)3+  radicals, a conductive and electroactive substrate of Fe2N and gold nanoparticle-codecorated reduced graphene oxide (Fe2N/rGO/Au) was established to incubate the capture antibody.	rgo	216-219	insulin receptor	Homo sapiens	83-91
33347268-5	2021	To further catalyze the ECL reaction between the reductive TPrA  and the oxidative Ir(ppy)3+  radicals, a conductive and electroactive substrate of Fe2N and gold nanoparticle-codecorated reduced graphene oxide (Fe2N/rGO/Au) was established to incubate the capture antibody.	Gold	220-222	insulin receptor	Homo sapiens	83-91
33410883-5	2021	IR-A43 alone is inactive, but, in the presence of insulin, it potentiates autophosphorylation and downstream signaling of the insulin receptor.	ir-a43	0-6	insulin receptor	Homo sapiens	126-142
33410883-6	2021	By using the species-specific activity of IR-A43 at the human insulin receptor, we demonstrate that residue Q272 in the cysteine-rich domain is directly involved in the insulin-enhancing activity of IR-A43.	q272	108-112	insulin receptor	Homo sapiens	62-78
33410883-6	2021	By using the species-specific activity of IR-A43 at the human insulin receptor, we demonstrate that residue Q272 in the cysteine-rich domain is directly involved in the insulin-enhancing activity of IR-A43.	Cysteine	120-128	insulin receptor	Homo sapiens	62-78
33410883-7	2021	Therefore, we propose that the region containing residue Q272 is a hotspot that can be used to enhance insulin receptor activation.	q272	57-61	insulin receptor	Homo sapiens	103-119
32936988-2	2021	Triglyceride-glucose index (TyG), a simple, inexpensive and easily accessible IR marker, is calculated by fasting serum glucose and triglyceride values.	Triglycerides	0-12	insulin receptor	Homo sapiens	78-80
32936988-2	2021	Triglyceride-glucose index (TyG), a simple, inexpensive and easily accessible IR marker, is calculated by fasting serum glucose and triglyceride values.	Glucose	13-20	insulin receptor	Homo sapiens	78-80
32936988-2	2021	Triglyceride-glucose index (TyG), a simple, inexpensive and easily accessible IR marker, is calculated by fasting serum glucose and triglyceride values.	Glucose	120-127	insulin receptor	Homo sapiens	78-80
32936988-2	2021	Triglyceride-glucose index (TyG), a simple, inexpensive and easily accessible IR marker, is calculated by fasting serum glucose and triglyceride values.	Triglycerides	132-144	insulin receptor	Homo sapiens	78-80
33384765-8	2020	Such studies revealed that all three parameters (insulin receptor, insulin receptor substrate 1, and protein kinase B) were inactivated by high glucose, indicating a disruption of the signal pathway.	Glucose	144-151	insulin receptor	Homo sapiens	49-65
33029835-9	2021	This study suggests that acteoside can ameliorate the ICV-STZ-induced learning and memory impairment caused due to insulin receptor, insulin receptor substrate 1, Glu T1, Glu T3, and Glu T4 pathways by triggering intracerebral metabolism.	acteoside	25-34	insulin receptor	Homo sapiens	115-131
33029835-9	2021	This study suggests that acteoside can ameliorate the ICV-STZ-induced learning and memory impairment caused due to insulin receptor, insulin receptor substrate 1, Glu T1, Glu T3, and Glu T4 pathways by triggering intracerebral metabolism.	Streptozocin	58-61	insulin receptor	Homo sapiens	115-131
33316063-10	2021	Besides, INSR protein as an insulin receptor precursor showed a high potential site for posttranslation modifications, including phosphorylation and N-glycosylation.	Nitrogen	10-11	insulin receptor	Homo sapiens	28-44
33045613-0	2020	Novel idebenone analogs block Shc"s access to insulin receptor to improve insulin sensitivity.	idebenone	6-15	insulin receptor	Homo sapiens	46-62
33045613-5	2020	Idebenone blocks p52Shc"s access to Insulin Receptor to increase insulin sensitivity.	idebenone	0-9	insulin receptor	Homo sapiens	36-52
33045613-6	2020	In this work the avidity of 34 novel idebenone analogs and 3 metabolites to bind p52Shc, and to block the interaction of p52Shc with the Insulin receptor was tested.	idebenone	37-46	insulin receptor	Homo sapiens	137-153
33045613-7	2020	Our hypothesis was that if an idebenone analog bound and blocked p52Shc"s access to insulin receptor better than idebenone, it should be a more effective insulin sensitizing agent than idebenone itself.	idebenone	30-39	insulin receptor	Homo sapiens	84-100
32877816-7	2020	Moreover, K1079 residue in IR is seen to be sitting in a pocket which is different than the allosteric inhibitor binding pocket present in its homologue (IGF1R).	k1079	10-15	insulin receptor	Homo sapiens	27-29
32964344-6	2020	For instance, hyperglycaemia impairs insulin signalling through the generation of reactive oxygen species, which abrogate insulin-induced tyrosine autophosphorylation of the insulin receptor.	Reactive Oxygen Species	82-105	insulin receptor	Homo sapiens	174-190
33364490-0	2020	Effect of the interaction between ribosomal protein L10a and insulin receptor on carbohydrate metabolism.	Carbohydrates	81-93	insulin receptor	Homo sapiens	61-77
33125153-7	2020	Statistically significant associations were found between HER2 expression and response to treatment with the ALK/IGF-IR/InsR inhibitor ceritinib and fibroblast growth factor receptor (FGFR)1/2/3 inhibitor AZD4547, HER3 and IGF-IR expression and their response to treatment with TKIs targeting HER family members (erlotinib and afatinib), and c-MET and ALK7 expression and their response to treatment with stattic.	ceritinib	135-144	insulin receptor	Homo sapiens	120-124
31989990-12	2020	We report, for the first time, an association of INSR mutation with neonatal HH responsive to diazoxide therapy that resolved subsequently.	Diazoxide	94-103	insulin receptor	Homo sapiens	49-53
32896381-4	2020	Insulin induced insulin receptor (IR) tyrosine kinase-catalyzed Tyr-19 phosphorylation of N-myristoylable M14A Cav-2 and triggered activation of IR signaling cascade.	Tyrosine	64-67	insulin receptor	Homo sapiens	16-32
32896381-4	2020	Insulin induced insulin receptor (IR) tyrosine kinase-catalyzed Tyr-19 phosphorylation of N-myristoylable M14A Cav-2 and triggered activation of IR signaling cascade.	Tyrosine	64-67	insulin receptor	Homo sapiens	34-36
32964344-6	2020	For instance, hyperglycaemia impairs insulin signalling through the generation of reactive oxygen species, which abrogate insulin-induced tyrosine autophosphorylation of the insulin receptor.	Tyrosine	138-146	insulin receptor	Homo sapiens	174-190
32898742-3	2020	METHOD: A study was carried out using molecular modeling, where cysteines of the insulin-receptor are replaced by selenocysteines.	Cysteine	64-73	insulin receptor	Homo sapiens	81-97
32898742-3	2020	METHOD: A study was carried out using molecular modeling, where cysteines of the insulin-receptor are replaced by selenocysteines.	Selenocysteine	114-129	insulin receptor	Homo sapiens	81-97
32898742-6	2020	RESULTS: The results show that the substitution of cysteine by selenocysteine in the insulin receptor does not lead to stabilization of the complex receptor/insulin, but to its disruption.In addition, the types and the number of bonds between insulin and its receptor in the two cases are different, where 7 strong bonds between insulin and its receptor were found in the case of the cysteine complex compared to 6 weak bonds in the second case.	Cysteine	51-59	insulin receptor	Homo sapiens	85-101
32898742-6	2020	RESULTS: The results show that the substitution of cysteine by selenocysteine in the insulin receptor does not lead to stabilization of the complex receptor/insulin, but to its disruption.In addition, the types and the number of bonds between insulin and its receptor in the two cases are different, where 7 strong bonds between insulin and its receptor were found in the case of the cysteine complex compared to 6 weak bonds in the second case.	Selenocysteine	63-77	insulin receptor	Homo sapiens	85-101
32898742-6	2020	RESULTS: The results show that the substitution of cysteine by selenocysteine in the insulin receptor does not lead to stabilization of the complex receptor/insulin, but to its disruption.In addition, the types and the number of bonds between insulin and its receptor in the two cases are different, where 7 strong bonds between insulin and its receptor were found in the case of the cysteine complex compared to 6 weak bonds in the second case.	Cysteine	69-77	insulin receptor	Homo sapiens	85-101
32898742-7	2020	CONCLUSION: Findings of this study suggest that misincorporation of selenocysteines in insulin receptor could lead to destabilization of the insulin-receptor complex and therefore may possibly cause an insulin resistance.	Selenocysteine	68-83	insulin receptor	Homo sapiens	87-103
32898742-7	2020	CONCLUSION: Findings of this study suggest that misincorporation of selenocysteines in insulin receptor could lead to destabilization of the insulin-receptor complex and therefore may possibly cause an insulin resistance.	Selenocysteine	68-83	insulin receptor	Homo sapiens	141-157
33096618-5	2020	Insulin is a protein hormone secreted from pancreatic beta-cells that stimulates glucose uptake and metabolism via insulin receptor signaling.	Glucose	81-88	insulin receptor	Homo sapiens	115-131
32814161-0	2020	Defective insulin receptor signaling in patients with gestational diabetes is related to dysregulated miR-140 which can be improved by naringenin.	naringenin	135-145	insulin receptor	Homo sapiens	10-26
32814161-11	2020	In conclusion, miR-140-3p overexpression contributes to the defective placental IR signaling in patients with GDM.	mir-140-3p	15-25	insulin receptor	Homo sapiens	80-82
32909759-2	2020	The reaction was enabled by visible-light-mediated regioselective radical addition of sulfonyl chlorides to 2-arylstyrenes using fac[Ir(ppy)3] as a photocatalyst, demonstrating its unique role in a photocascade process to execute atom transfer radical addition (ATRA) followed by photocyclization.	2-arylstyrenes	108-122	insulin receptor	Homo sapiens	133-141
32909759-0	2020	The Different Faces of [Ru(bpy)3Cl2] and fac[Ir(ppy)3] Photocatalysts: Redox Potential Controlled Synthesis of Sulfonylated Fluorenes and Pyrroloindoles from Unactivated Olefins and Sulfonyl Chlorides.	Fluorenes	124-133	insulin receptor	Homo sapiens	45-53
32909759-0	2020	The Different Faces of [Ru(bpy)3Cl2] and fac[Ir(ppy)3] Photocatalysts: Redox Potential Controlled Synthesis of Sulfonylated Fluorenes and Pyrroloindoles from Unactivated Olefins and Sulfonyl Chlorides.	pyrroloindoles	138-152	insulin receptor	Homo sapiens	45-53
32909759-0	2020	The Different Faces of [Ru(bpy)3Cl2] and fac[Ir(ppy)3] Photocatalysts: Redox Potential Controlled Synthesis of Sulfonylated Fluorenes and Pyrroloindoles from Unactivated Olefins and Sulfonyl Chlorides.	Alkenes	170-177	insulin receptor	Homo sapiens	45-53
33434167-4	2020	Detection of anti-insulin receptor antibodies confirmed TBIR.	tbir	56-60	insulin receptor	Homo sapiens	18-34
32998286-3	2020	p70 S6 kinase 1 (S6K1) is a serine/threonine kinase that phosphorylates insulin receptor substrate 1 (IRS-1)S1101 and desensitizes the insulin receptor (IR).	Serine	28-34	insulin receptor	Homo sapiens	72-88
32909759-0	2020	The Different Faces of [Ru(bpy)3Cl2] and fac[Ir(ppy)3] Photocatalysts: Redox Potential Controlled Synthesis of Sulfonylated Fluorenes and Pyrroloindoles from Unactivated Olefins and Sulfonyl Chlorides.	sulfonyl chloride	182-200	insulin receptor	Homo sapiens	45-53
32909759-2	2020	The reaction was enabled by visible-light-mediated regioselective radical addition of sulfonyl chlorides to 2-arylstyrenes using fac[Ir(ppy)3] as a photocatalyst, demonstrating its unique role in a photocascade process to execute atom transfer radical addition (ATRA) followed by photocyclization.	sulfonyl chloride	86-104	insulin receptor	Homo sapiens	133-141
32583238-2	2020	A time delay was considered to represent the time required for performing various cellular mechanisms between activation of insulin receptor and subsequent glucose entry from extracellular region into intracellular region of a cardiac cell.	Glucose	156-163	insulin receptor	Homo sapiens	124-140
32100949-4	2020	We report a case of type A IR syndrome with an in-frame INSR heterozygous deletion (DeltaLeu999) that was treated with a combination of conventional therapy and ipragliflozin, a sodium-glucose cotransporter 2 (SGLT2) inhibitor.	ipragliflozin	161-174	insulin receptor	Homo sapiens	56-60
32969484-3	2020	On suspicion of TBIRS the patient was started on tapering glucocorticoids to overcome the autoimmune insulin receptor blockade, resulting in an immediate and dramatic effect.	tbirs	16-21	insulin receptor	Homo sapiens	101-117
32867022-7	2020	There is evidence that Cd exposure results in the perturbation of the enzymes and modulatory proteins involved in insulin signal transduction at the target tissue and mutations of the insulin receptor.	Cadmium	23-25	insulin receptor	Homo sapiens	184-200
32409919-6	2020	Insulin-resistant Huh7 (Huh7-IR) showed a reduction in Glut2, glycogen levels, and glucose uptake stimulated by insulin or tyrosine phosphorylation from the beta-fraction of insulin receptor post-insulin stimulation, with an increase of glucose production and lipid intracellular content.	Glucose	83-90	insulin receptor	Homo sapiens	174-190
32409919-6	2020	Insulin-resistant Huh7 (Huh7-IR) showed a reduction in Glut2, glycogen levels, and glucose uptake stimulated by insulin or tyrosine phosphorylation from the beta-fraction of insulin receptor post-insulin stimulation, with an increase of glucose production and lipid intracellular content.	Tyrosine	123-131	insulin receptor	Homo sapiens	174-190
32409919-6	2020	Insulin-resistant Huh7 (Huh7-IR) showed a reduction in Glut2, glycogen levels, and glucose uptake stimulated by insulin or tyrosine phosphorylation from the beta-fraction of insulin receptor post-insulin stimulation, with an increase of glucose production and lipid intracellular content.	Glucose	237-244	insulin receptor	Homo sapiens	174-190
32191645-8	2020	Despite high lipolysis, INSR subjects had low hepatic triglycerides (0.5 [0.1-0.5]), in contrast to lipodystrophy (10.6 [2.8-17.1], p<0.0001).	Triglycerides	54-67	insulin receptor	Homo sapiens	24-28
32739259-0	2020	Obesity-related hypoxia via miR-128 decreases insulin-receptor expression in human and mouse adipose tissue promoting systemic insulin resistance.	mir-128	28-35	insulin receptor	Homo sapiens	46-62
32651463-9	2020	Compared with non-DCI cases, patients with DCI exhibited an increased degree of methylation in the replication study: INSR, 0.855 (0.779-0.913) in DCI vs. 0.582 (0.565-0.689) in non-DCI; CDHR5, 0.786 (0.708-0.904) in DCI vs. 0.632 (0.610-0.679) in non-DCI.	dci	43-46	insulin receptor	Homo sapiens	118-122
32651463-9	2020	Compared with non-DCI cases, patients with DCI exhibited an increased degree of methylation in the replication study: INSR, 0.855 (0.779-0.913) in DCI vs. 0.582 (0.565-0.689) in non-DCI; CDHR5, 0.786 (0.708-0.904) in DCI vs. 0.632 (0.610-0.679) in non-DCI.	dci	43-46	insulin receptor	Homo sapiens	118-122
32651463-9	2020	Compared with non-DCI cases, patients with DCI exhibited an increased degree of methylation in the replication study: INSR, 0.855 (0.779-0.913) in DCI vs. 0.582 (0.565-0.689) in non-DCI; CDHR5, 0.786 (0.708-0.904) in DCI vs. 0.632 (0.610-0.679) in non-DCI.	dci	43-46	insulin receptor	Homo sapiens	118-122
32651463-9	2020	Compared with non-DCI cases, patients with DCI exhibited an increased degree of methylation in the replication study: INSR, 0.855 (0.779-0.913) in DCI vs. 0.582 (0.565-0.689) in non-DCI; CDHR5, 0.786 (0.708-0.904) in DCI vs. 0.632 (0.610-0.679) in non-DCI.	dci	43-46	insulin receptor	Homo sapiens	118-122
32651463-9	2020	Compared with non-DCI cases, patients with DCI exhibited an increased degree of methylation in the replication study: INSR, 0.855 (0.779-0.913) in DCI vs. 0.582 (0.565-0.689) in non-DCI; CDHR5, 0.786 (0.708-0.904) in DCI vs. 0.632 (0.610-0.679) in non-DCI.	dci	43-46	insulin receptor	Homo sapiens	118-122
32733189-4	2020	Here, we explore the relationship between insulin receptor signaling and glucose metabolism using similar methods.	Glucose	73-80	insulin receptor	Homo sapiens	42-58
32191645-9	2020	beta-hydroxybutyrate was 2-7-fold higher in INSR versus all other groups (p<0.0001) consistent with higher hepatic fat oxidation.	3-Hydroxybutyric Acid	0-20	insulin receptor	Homo sapiens	44-48
32191645-10	2020	CONCLUSION: These data support a key pathogenic role of adipose tissue IR to increase glycerol and FFA availability to the liver in both receptor and post-receptor IR.	Glycerol	86-94	insulin receptor	Homo sapiens	71-73
31899992-0	2020	Arg1201Gln mutation of insulin receptor impairs tyrosine kinase activity and causes insulin resistance: a case report.	Tyrosine	48-56	insulin receptor	Homo sapiens	23-39
32487991-8	2020	In addition, we experimentally validated predicted synergy of the BRAF/insulin receptor combination (Dabrafenib/BMS-754807) in 48 colorectal cancer cell lines.	dabrafenib	101-111	insulin receptor	Homo sapiens	71-87
32297376-5	2020	Despite sharing this conserved ligand-binding module, IR and EGFR family members are considered mechanistically distinct-in part because IR is a disulfide-linked (alphabeta)2 dimer regardless of ligand binding, whereas EGFR is a monomer that undergoes ligand-induced dimerization.	Disulfides	145-154	insulin receptor	Homo sapiens	137-139
32427889-6	2020	We also found that the effects of N6-adenine methylation on lipid production involved the regulation of INSR signaling pathway, which promotes glucose up-taking and lipid production in the terminal differentiation stage.	n6-adenine	34-44	insulin receptor	Homo sapiens	104-108
32427889-6	2020	We also found that the effects of N6-adenine methylation on lipid production involved the regulation of INSR signaling pathway, which promotes glucose up-taking and lipid production in the terminal differentiation stage.	Glucose	143-150	insulin receptor	Homo sapiens	104-108
32001311-3	2020	At a cellular level, the inhibitory effect of BBR on mitochondrial enzymes is probably responsible for many of its biological activities, including the activation of low-density lipoprotein receptor (LDLR), AMP-activated protein kinase (AMPK) and insulin receptor (InsR); these biological activities contribute to ameliorate peripheral blood metabolic profiles, e.g. by reducing plasma lipids and glucose levels, thus improving signs and symptoms of metabolic disorders.	Berberine	46-49	insulin receptor	Homo sapiens	247-263
32001311-3	2020	At a cellular level, the inhibitory effect of BBR on mitochondrial enzymes is probably responsible for many of its biological activities, including the activation of low-density lipoprotein receptor (LDLR), AMP-activated protein kinase (AMPK) and insulin receptor (InsR); these biological activities contribute to ameliorate peripheral blood metabolic profiles, e.g. by reducing plasma lipids and glucose levels, thus improving signs and symptoms of metabolic disorders.	Berberine	46-49	insulin receptor	Homo sapiens	265-269
32332780-4	2020	In muscle, LRP2 is necessary for insulin-dependent IR internalization, an initial trigger for insulin signaling, that is crucial in regulating downstream signaling and glucose uptake.	Glucose	168-175	insulin receptor	Homo sapiens	51-53
32478674-12	2020	On suspicion of TBIRS, the patient was started on tapering glucocorticoids to overcome the autoimmune insulin receptor blockade, resulting in an immediate and pronounced effect; within days insulin requirements decreased by 80-90% and plasma glucose stabilized around 7-8 mmol/L.	tbirs	16-21	insulin receptor	Homo sapiens	102-118
32373071-10	2020	Furthermore, we tested palbociclib in combination with insulin-like growth factor 1/insulin receptor inhibitor linsitinib showing an additive effect.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	111-121	insulin receptor	Homo sapiens	84-100
32252239-6	2020	D-chiro-inositol (DCI), which is a naturally occurring stereoisomer of inositol, has been classified as an insulin-sensitizer and seems to mitigate multiple InsR-related metabolic alterations in PCOS with a safe profile.	Inositol	8-16	insulin receptor	Homo sapiens	157-161
31490549-8	2020	Patients with ER+, IGF-1R-positive breast cancer without p-IGF-1R/InsR staining (n=242) had tamoxifen benefit (HR 0.41, p = 0.0038), while the results for p-IGF-1R/InsR-positive patients (n = 125) were not significant (HR 0.95, p = 0.3).	Tamoxifen	92-101	insulin receptor	Homo sapiens	66-70
31490549-11	2020	This could be abrogated by the dual IGF-1R/InsR inhibitor linsitinib, but not by the IGF-IR-selective antibody 1H7.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	58-68	insulin receptor	Homo sapiens	43-47
31490549-14	2020	In conclusion, p-IGF-1R/InsR positivity in ER+ breast cancer is associated with reduced benefit from adjuvant tamoxifen in postmenopausal patients.	Tamoxifen	110-119	insulin receptor	Homo sapiens	24-28
32252239-6	2020	D-chiro-inositol (DCI), which is a naturally occurring stereoisomer of inositol, has been classified as an insulin-sensitizer and seems to mitigate multiple InsR-related metabolic alterations in PCOS with a safe profile.	Inositol	0-16	insulin receptor	Homo sapiens	157-161
32252239-6	2020	D-chiro-inositol (DCI), which is a naturally occurring stereoisomer of inositol, has been classified as an insulin-sensitizer and seems to mitigate multiple InsR-related metabolic alterations in PCOS with a safe profile.	dci	18-21	insulin receptor	Homo sapiens	157-161
32273886-6	2020	Meanwhile, functional terms of programmed cell death involved in cell development and regulation of insulin receptor signaling pathway were mostly enriched with 42 candidate genes, which also included reproduction related terms of steroid metabolic process and cellular response to hormone stimulus.	Steroids	231-238	insulin receptor	Homo sapiens	100-116
32114435-3	2020	TLG supplementation enhanced mRNA levels for fatty acid synthase (FASN) and SLC27A2 in white adipose tissue; insulin receptor in duodenum; aquaporin-8 in ileum, jejunum and colon; aquaporin-10 in duodenum and ileum; nuclear factor like-2 in jejunum and colon; glutathione S-transferase and phosphoenolpyruvate carboxykinase-1 in intestines; and abundances of claudin-1 and occludin proteins.	(5r)-3-Acetyl-4-Hydroxy-5-Methyl-5-[(1z)-2-Methylbuta-1,3-Dien-1-Yl]thiophen-2(5h)-One	0-3	insulin receptor	Homo sapiens	109-125
31588494-0	2020	Thyroid Hormone Effects on Glucose Disposal in Patients With Insulin Receptor Mutations.	Glucose	27-34	insulin receptor	Homo sapiens	61-77
31979418-8	2020	Exposure of the thyroid to NaI modulates 15 cellular pathways, most of which are also affected by ICM treatment (including the elF4 and P706SK cell signaling pathway and INSR identified as an upstream activator in both treatments).	Sodium	27-30	insulin receptor	Homo sapiens	170-174
31759099-3	2020	We found that treatment of the normal human liver cell LO2 with 1000 nM insulin for 48 h reduced glucose uptake and increased serine phosphorylation of insulin receptor substrate-1, indicating a reduction in insulin receptor signaling.	Serine	126-132	insulin receptor	Homo sapiens	152-168
31794259-8	2020	Chronic rapamycin treatment reduced Grb10 protein abundance in conjunction with increased insulin receptor protein levels.	Sirolimus	8-17	insulin receptor	Homo sapiens	90-106
31979110-7	2020	In addition, we disclose a potential compensatory pathway via activation of the Insulin Receptor upon crizotinib treatment.	crizotinib	102-112	insulin receptor	Homo sapiens	80-96
31882596-0	2019	Chronic heavy alcohol consumption influences the association between genetic variants of GCK or INSR and the development of diabetes in men: A 12-year follow-up study.	Alcohols	14-21	insulin receptor	Homo sapiens	96-100
31825461-1	2020	The surfacing of the glucose transporter GLUT4 driven by insulin receptor activation provides the prototypic example of a homeostasis response dependent on mobilization of an intracellular storage compartment.	Glucose	21-28	insulin receptor	Homo sapiens	57-73
32468825-0	2020	Intra-Pancreatic Insulin Nourishes Cancer Cells: Do Insulin-Receptor Antagonists such as PGG and EGCG Play a Role?	pgg	89-92	insulin receptor	Homo sapiens	52-68
32468825-0	2020	Intra-Pancreatic Insulin Nourishes Cancer Cells: Do Insulin-Receptor Antagonists such as PGG and EGCG Play a Role?	epigallocatechin gallate	97-101	insulin receptor	Homo sapiens	52-68
32888269-5	2020	OBJECTIVES: Insulin receptor sensitization is done by signal transduction mechanism via selective protein tyrosine phospha-tase (PTP1B).	Tyrosine	106-114	insulin receptor	Homo sapiens	12-28
31748790-4	2020	IRS2 is an adapter protein that functionally links receptor tyrosine kinases, such as insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R), and their downstream effectors.	Tyrosine	60-68	insulin receptor	Homo sapiens	86-107
31882596-2	2019	We aimed to determine whether the longitudinal associations between genetic variants of glucokinase (GCK) and insulin receptor (INSR) and the risk of developing diabetes were influenced by chronic heavy alcohol consumption.	Alcohols	203-210	insulin receptor	Homo sapiens	110-126
31882596-2	2019	We aimed to determine whether the longitudinal associations between genetic variants of glucokinase (GCK) and insulin receptor (INSR) and the risk of developing diabetes were influenced by chronic heavy alcohol consumption.	Alcohols	203-210	insulin receptor	Homo sapiens	128-132
31882596-7	2019	We identified that these GCK and INSR polymorphisms are affected by chronic heavy alcohol consumption and have an effect on the incidence of diabetes.	Alcohols	82-89	insulin receptor	Homo sapiens	33-37
31882596-11	2019	These results potentially suggest that chronic heavy alcohol consumption induce beta-cell dysfunction partially mediated by decreased GCK expression or decline of insulin sensitivity via inhibition of INSR, thereby contributing to the development of diabetes.	Alcohols	53-60	insulin receptor	Homo sapiens	201-205
31856878-3	2019	To explore this issue, the present study aimed to investigate the effects of glutamate-evoked increases in intracellular free Ca2+ concentrations [Ca2+]i and mitochondrial depolarisations, two key factors associated with excitotoxicity, on the insulin-induced activation of the insulin receptor (IR) and components of the Akt/ mammalian target of rapamycin (mTOR) pathway in primary cultures of rat cortical neurons.	Glutamic Acid	77-86	insulin receptor	Homo sapiens	278-294
31856878-3	2019	To explore this issue, the present study aimed to investigate the effects of glutamate-evoked increases in intracellular free Ca2+ concentrations [Ca2+]i and mitochondrial depolarisations, two key factors associated with excitotoxicity, on the insulin-induced activation of the insulin receptor (IR) and components of the Akt/ mammalian target of rapamycin (mTOR) pathway in primary cultures of rat cortical neurons.	Glutamic Acid	77-86	insulin receptor	Homo sapiens	296-298
31856878-3	2019	To explore this issue, the present study aimed to investigate the effects of glutamate-evoked increases in intracellular free Ca2+ concentrations [Ca2+]i and mitochondrial depolarisations, two key factors associated with excitotoxicity, on the insulin-induced activation of the insulin receptor (IR) and components of the Akt/ mammalian target of rapamycin (mTOR) pathway in primary cultures of rat cortical neurons.	Calcium	126-130	insulin receptor	Homo sapiens	278-294
31856878-3	2019	To explore this issue, the present study aimed to investigate the effects of glutamate-evoked increases in intracellular free Ca2+ concentrations [Ca2+]i and mitochondrial depolarisations, two key factors associated with excitotoxicity, on the insulin-induced activation of the insulin receptor (IR) and components of the Akt/ mammalian target of rapamycin (mTOR) pathway in primary cultures of rat cortical neurons.	Calcium	126-130	insulin receptor	Homo sapiens	296-298
31969308-1	2019	Sesamin (SES) has the ameliorating effect on L02 hepatocyte model of insulin resistance induced by high glucose and high insulin, based on insulin receptor signaling pathway IRS/PI3K/Akt.	sesamin	0-7	insulin receptor	Homo sapiens	139-155
31546230-11	2019	Moreover, in alphaTC1-6 cells atorvastatin treatment affected insulin-mediated glucagon suppression, insulin receptor phosphorylation and IRS-1-AKT pathway signaling.	Atorvastatin	30-42	insulin receptor	Homo sapiens	101-117
31721020-0	2019	1-Deoxynojirimycin modulates glucose homeostasis by regulating the combination of IR-GlUT4 and ADIPO-GLUT4 pathways in 3T3-L1 adipocytes.	1-Deoxynojirimycin	0-18	insulin receptor	Homo sapiens	82-84
31721020-4	2019	The results demonstrated that the genes/proteins expression of insulin receptor (IR), phosphatidylinositol-3-kinase (PI3K), protein kinase B (AKt/PkB), and adiponectin (ADIPO) increased with the increasing of DNJ concentration from 0.1-10 mumol/L.	1-Deoxynojirimycin	209-212	insulin receptor	Homo sapiens	63-79
31721020-6	2019	Both IR and ADIPO signaling pathways simultaneously affect the glucose homeostasis regulation effect of DNJ, whereas the key response target located in AMPK and its effect on subsequent GLUT4 mRNA expression.	Glucose	63-70	insulin receptor	Homo sapiens	5-7
31721020-6	2019	Both IR and ADIPO signaling pathways simultaneously affect the glucose homeostasis regulation effect of DNJ, whereas the key response target located in AMPK and its effect on subsequent GLUT4 mRNA expression.	1-Deoxynojirimycin	104-107	insulin receptor	Homo sapiens	5-7
31211453-7	2019	We found that TCF7L2 rs290481 (T > C) and INSR rs1799817 (G > A) polymorphisms were associated with the increased susceptibility of AEG (P = .007 and 0.004 for TCF7L2 rs290481 in TC vs TT and TC/CC vs TT models, and P = .040 for INSR rs1799817 in GA/AA vs GG model).	Technetium	14-16	insulin receptor	Homo sapiens	229-233
31211453-9	2019	We identified that TCF7L2 rs290481, INS rs689, and INSR rs1799817 SNPs increased the susceptibility of AEG in different cancer stage subgroups.	N-(2-aminoethyl)glycine	103-106	insulin receptor	Homo sapiens	51-55
31211453-11	2019	However, the association of INSR rs1799817 SNP with a decreased risk of lymph node metastasis in smoking patients with AEG was found.	N-(2-aminoethyl)glycine	119-122	insulin receptor	Homo sapiens	28-32
31211453-13	2019	In addition, TCF7L2 rs290481 and INSR rs1799817 SNPs may influence the lymph node metastasis in patients with AEG.	N-(2-aminoethyl)glycine	110-113	insulin receptor	Homo sapiens	33-37
31505460-5	2019	Dexamethasone enhanced insulin receptor abundance, activated mTOR complex 1 and 2 signaling and stimulated System A activity, measured by Na+-dependent 14C-methylaminoisobutyric acid uptake.	Dexamethasone	0-13	insulin receptor	Homo sapiens	23-39
31969308-1	2019	Sesamin (SES) has the ameliorating effect on L02 hepatocyte model of insulin resistance induced by high glucose and high insulin, based on insulin receptor signaling pathway IRS/PI3K/Akt.	sesamin	9-12	insulin receptor	Homo sapiens	139-155
31969308-3	2019	Moreover, treatment with SES promoted the gene and protein expression levels of insulin receptor (InsR) and the post-receptor associated proteins, such as insulin receptor substrate 1 (IRS1), insulin receptor substrate 2 (IRS2), PI3K (phosphatidylinositol 3-kinase), GLUT4 (glucose transporter 4) significantly, which were determined by RT-PCR and immunoblot analysis.	sesamin	25-28	insulin receptor	Homo sapiens	80-96
31969308-3	2019	Moreover, treatment with SES promoted the gene and protein expression levels of insulin receptor (InsR) and the post-receptor associated proteins, such as insulin receptor substrate 1 (IRS1), insulin receptor substrate 2 (IRS2), PI3K (phosphatidylinositol 3-kinase), GLUT4 (glucose transporter 4) significantly, which were determined by RT-PCR and immunoblot analysis.	sesamin	25-28	insulin receptor	Homo sapiens	98-102
31969308-3	2019	Moreover, treatment with SES promoted the gene and protein expression levels of insulin receptor (InsR) and the post-receptor associated proteins, such as insulin receptor substrate 1 (IRS1), insulin receptor substrate 2 (IRS2), PI3K (phosphatidylinositol 3-kinase), GLUT4 (glucose transporter 4) significantly, which were determined by RT-PCR and immunoblot analysis.	Phosphatidylinositols	235-255	insulin receptor	Homo sapiens	80-96
31969308-4	2019	In conclusion, SES has the ameliorating effect on L02 hepatocyte model of insulin resistance induced by high glucose/high insulin, which might be related to its effect on promoting expression of insulin receptor and its associated proteins of IRS-PI3K-Akt passway, and thus promoting insulin sensitivity.	sesamin	15-18	insulin receptor	Homo sapiens	195-211
31969308-4	2019	In conclusion, SES has the ameliorating effect on L02 hepatocyte model of insulin resistance induced by high glucose/high insulin, which might be related to its effect on promoting expression of insulin receptor and its associated proteins of IRS-PI3K-Akt passway, and thus promoting insulin sensitivity.	Glucose	109-116	insulin receptor	Homo sapiens	195-211
31480400-3	2019	Here, we targeted the IGF pathway using ceritinib, an off-target inhibitor of the IGF1 receptor (IGF1R) and insulin receptor (INSR), in a pediatric patient with an unclassified brain tumor and a notch receptor 1 (NOTCH1) germline mutation.	ceritinib	40-49	insulin receptor	Homo sapiens	126-130
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Tyrosine	97-105	insulin receptor	Homo sapiens	54-70
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Phosphatidylinositols	205-225	insulin receptor	Homo sapiens	54-70
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Phosphatidylinositols	276-294	insulin receptor	Homo sapiens	54-70
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Glucose	387-394	insulin receptor	Homo sapiens	54-70
31872693-2	2019	Insulin stimulation causes autophosphorylation of the insulin receptor( IR),which then activates tyrosine phosphorylation of insulin receptor substrate( IRS).Phosphorylation of IRS can induce and activate phosphatidylinositol 3-kinase( PI3 K),subsequently activate downstream 3-phosphoinositide-dependent protease 1( PDK1) and Akt/PKB,and finally promote expression and translocation of glucose transporter 4 to increase glucose uptake of insulin-sensitive tissues and alleviate insulin resistance.	Glucose	421-428	insulin receptor	Homo sapiens	54-70
31477741-9	2019	In conclusion, among IR parameters, TyG index was independently associated with the presence of CAD and obstructive CAD in non-diabetic patients.	8-methyl-2-{[(pyridin-4-yl)sulfanyl]methyl}quinazolin-4(3H)-one	36-39	insulin receptor	Homo sapiens	21-23
31265936-9	2019	Consequently, essential hydrophobic residues for binding to insulin receptor exposed to surface in the presence of vitamin E.	Vitamin E	115-124	insulin receptor	Homo sapiens	60-76
31480400-5	2019	The proliferation of the patient tumor cells (225ZL) was inhibited by arsenic trioxide (ATO), which is an inhibitor of the SHH pathway, by linsitinib, which is an inhibitor of IGF1R and INSR, and by ceritinib.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	139-149	insulin receptor	Homo sapiens	186-190
31480400-6	2019	225ZL expressed INSR but not IGF1R at the protein level, and ceritinib blocked the phosphorylation of INSR.	ceritinib	61-70	insulin receptor	Homo sapiens	102-106
31382738-0	2019	Extracellular Glutamate-Induced mTORC1 Activation via the IR/IRS/PI3K/Akt Pathway Enhances the Expansion of Porcine Intestinal Stem Cells.	Glutamic Acid	14-23	insulin receptor	Homo sapiens	58-60
31382738-8	2019	In addition, Glu increased the phosphorylation levels of IR and IRS, and inhibiting IR downregulated the IRS/PI3K/Akt pathway.	Glutamic Acid	13-16	insulin receptor	Homo sapiens	57-59
31382738-8	2019	In addition, Glu increased the phosphorylation levels of IR and IRS, and inhibiting IR downregulated the IRS/PI3K/Akt pathway.	Glutamic Acid	13-16	insulin receptor	Homo sapiens	64-66
30909453-4	2019	In the CME-1 cell line, overactivation of IGF1 and Insulin receptors (IGF1R/InsR) sustained AKT activation and pazopanib resistance, which was overcome by a combination treatment with the double IGF1R/InsR inhibitor BMS754807.	pazopanib	111-120	insulin receptor	Homo sapiens	76-80
30970232-8	2019	The results confirmed that baicalein (10-6 and 10-5 mol/L) promotes glucose uptake and glycolysis, inhibits gluconeogenesis of hepatocytes to improve glucose metabolism, and may be as a result from regulation of InsR/IRS-1/PI3K/AKT pathway.	baicalein	27-36	insulin receptor	Homo sapiens	212-216
31341684-12	2019	Parallel evolution of glucose levels and serum anti-insulin receptor antibodies seemed to be the consequence of immune suppressive properties of cladribine.	Cladribine	145-155	insulin receptor	Homo sapiens	52-68
31309101-8	2019	In multivariate analysis, IR was significantly associated with higher odds of low high-density lipoprotein cholesterol, high triglyceride, and impaired fasting glucose in groups of normal weight, overweight/obese, nondiabetes, diabetes, and overall sample.	Cholesterol	107-118	insulin receptor	Homo sapiens	26-28
31309101-8	2019	In multivariate analysis, IR was significantly associated with higher odds of low high-density lipoprotein cholesterol, high triglyceride, and impaired fasting glucose in groups of normal weight, overweight/obese, nondiabetes, diabetes, and overall sample.	Triglycerides	125-137	insulin receptor	Homo sapiens	26-28
30946565-3	2019	Subsequently, the azido-insulin analogs were used in azide-alkyne [3 + 2] cycloaddition reactions to synthesize a diverse array of triazole-based RHI bioconjugates that were found to be potent human insulin receptor binders.	azide-alkyne	53-65	insulin receptor	Homo sapiens	199-215
30946565-3	2019	Subsequently, the azido-insulin analogs were used in azide-alkyne [3 + 2] cycloaddition reactions to synthesize a diverse array of triazole-based RHI bioconjugates that were found to be potent human insulin receptor binders.	Triazoles	131-139	insulin receptor	Homo sapiens	199-215
30661991-4	2019	Using CHIP-RIP, we demonstrate that GAS5 binds to promoter of insulin receptor to regulate its expression, and its depletion inhibits glucose uptake and insulin signaling.	Glucose	134-141	insulin receptor	Homo sapiens	62-78
30739791-7	2019	GW501516 treatment increased the expression of insulin receptor and inhibited TNFalpha-mediated repression of insulin receptor.	GW 501516	0-8	insulin receptor	Homo sapiens	110-126
30739791-9	2019	In summary, our study demonstrated that the PPARbeta/delta agonist, GW501516 reversed TNFalpha-induced decreases in adipocyte differentiation and adiponectin expression, and improved insulin sensitivity by increasing the expression of insulin receptor.	GW 501516	68-76	insulin receptor	Homo sapiens	235-251
30707913-1	2019	This study aimed to functionally characterize beta2-adrenergic (beta2AR) and insulin receptor (IR) heteromers in regard to beta-arrestin 2 (betaarr2) recruitment and cAMP signaling and to examine the involvement of the cytoplasmic portion of the IR beta chain in heteromerization with beta2AR.	Cyclic AMP	166-170	insulin receptor	Homo sapiens	77-93
30833584-7	2019	DNA methylation level of INSR was positively associated with triglyceride (beta = 0.011, P = 0.021), and negatively associated with high-density lipoprotein cholesterol (beta = -0.039, P = 0.021).	Triglycerides	61-73	insulin receptor	Homo sapiens	25-29
30889804-4	2019	Intracellular Mg2+ concentrations are critical for the phosphorylation of the insulin receptor and other downstream signal kinases of the target cells.	magnesium ion	14-18	insulin receptor	Homo sapiens	78-94
30449809-4	2019	Ceritinib can aggravate hyperglycemia in patients with diabetes who lack compensatory insulin secretion, due to its inhibitory effects on the insulin receptor.	ceritinib	0-9	insulin receptor	Homo sapiens	142-158
30422809-0	2019	Antitumor effects of beta-elemene via targeting the phosphorylation of insulin receptor.	beta-elemene	21-33	insulin receptor	Homo sapiens	71-87
30576640-7	2019	Here, we provide a review of contemporary literature on brain insulin resistance, highlight the rationale for improving memory function using intranasal insulin, and describe initial results from experiments using a molecular approach to more directly measure the impact of insulin receptor activation and signaling on glucose uptake in neurons.	Glucose	319-326	insulin receptor	Homo sapiens	274-290
30718702-4	2019	The increased glucose uptake was accompanied by enhanced phosphorylation of the insulin receptor (IR), insulin receptor substrate-1 (IRS-1), the serine/threonine kinase Akt and Akt substrate of 160 kDa (AS160).	Glucose	14-21	insulin receptor	Homo sapiens	80-96
30718702-4	2019	The increased glucose uptake was accompanied by enhanced phosphorylation of the insulin receptor (IR), insulin receptor substrate-1 (IRS-1), the serine/threonine kinase Akt and Akt substrate of 160 kDa (AS160).	Glucose	14-21	insulin receptor	Homo sapiens	98-100
30718702-7	2019	Taken together, these results establish that apoA-I increases glucose disposal in skeletal muscle by activating the IR/IRS-1/PI3K/Akt/AS160 signal transduction pathway.	Glucose	62-69	insulin receptor	Homo sapiens	116-118
30422809-6	2019	To investigate the mechanisms, we focused on the effects of beta-elemene on IR signaling pathway.	beta-elemene	60-72	insulin receptor	Homo sapiens	76-78
30422809-8	2019	Further, the phosphorylation of IR was found to be suppressed notably by beta-elemene specifically in tumor cells but not normal hepatocytes.	beta-elemene	73-85	insulin receptor	Homo sapiens	32-34
30422809-9	2019	In addition, beta-elemene inhibited the growth of ESFT xenografts in vivo, and the phosphorylation of IR and S6 ribosomal protein was significantly repressed in the beta-elemene-treated xenografts.	beta-elemene	165-177	insulin receptor	Homo sapiens	102-104
30422809-10	2019	These data suggest that beta-elemene targets IR phosphorylation to inhibit the proliferation of tumor cells specifically and enhace the effects of IGF1R inhibitors.	beta-elemene	24-36	insulin receptor	Homo sapiens	45-47
30739791-7	2019	GW501516 treatment increased the expression of insulin receptor and inhibited TNFalpha-mediated repression of insulin receptor.	GW 501516	0-8	insulin receptor	Homo sapiens	47-63
30966770-7	2019	We also investigated whether a phytochemical, penta-O-galloyl- beta -D-glucose ( beta -PGG), antagonizes IR/IGF1R, sabotages pancreatic cancer cells and alleviates cancer cachexia.	penta-o-galloyl- beta -d-glucose	46-78	insulin receptor	Homo sapiens	105-107
30966770-7	2019	We also investigated whether a phytochemical, penta-O-galloyl- beta -D-glucose ( beta -PGG), antagonizes IR/IGF1R, sabotages pancreatic cancer cells and alleviates cancer cachexia.	beta -pgg	81-90	insulin receptor	Homo sapiens	105-107
30966770-10	2019	beta -PGG inhibited IR/IGF1R activity and decreased glycolytic enzymes in MiaPaCa2 and Panc-1 pancreatic cancer cells.	beta -pgg	0-9	insulin receptor	Homo sapiens	20-22
30559346-5	2019	We additionally show, using preclinical mouse as well as patient data, that treatment with the inhibitor sunitinib significantly reduces the expression of INSR-A.	Sunitinib	105-114	insulin receptor	Homo sapiens	155-159
30532646-8	2018	In humans, reduced representation bisulfite sequencing (RRBS) was performed on peripheral samples that were obtained from individuals who were prenatally exposed to the "Dutch Hunger Winter", resulting in two Differentially Methylated Regions (DMRs) in INSR and CPTIA genes that were functionally, biologically and technically validated, and significantly associated with birth weights and LDL cholesterol levels in offspring.	hydrogen sulfite	34-43	insulin receptor	Homo sapiens	253-257
31148068-1	2019	During exposure of cells to acute high dose-rate ionizing radiation (IR), oxidants from the radiolysis of water can overwhelm antioxidant systems.	Water	106-111	insulin receptor	Homo sapiens	69-71
31827016-2	2019	Incubation of a highly purified insulin receptor preparation with [gamma-32P]ATP also resulted in tyrosine phosphorylation of the beta subunit in an insulin-dependent manner, suggesting that the receptor itself is a tyrosine-specific protein kinase.	adenosine 5'-O-(3-thiotriphosphate)	66-80	insulin receptor	Homo sapiens	32-48
31827016-2	2019	Incubation of a highly purified insulin receptor preparation with [gamma-32P]ATP also resulted in tyrosine phosphorylation of the beta subunit in an insulin-dependent manner, suggesting that the receptor itself is a tyrosine-specific protein kinase.	Tyrosine	98-106	insulin receptor	Homo sapiens	32-48
31827016-2	2019	Incubation of a highly purified insulin receptor preparation with [gamma-32P]ATP also resulted in tyrosine phosphorylation of the beta subunit in an insulin-dependent manner, suggesting that the receptor itself is a tyrosine-specific protein kinase.	Tyrosine	216-224	insulin receptor	Homo sapiens	32-48
31827016-3	2019	Furthermore, a Japanese boy with insulin resistance and acanthosis nigricans was found to be heterozygous for a mutation of the insulin receptor gene that resulted in the replacement of glycine-996 with valine in the ATP binding site of the receptor.	Adenosine Triphosphate	217-220	insulin receptor	Homo sapiens	128-144
31827016-4	2019	Expression of the mutant receptor in cultured cells revealed it to be deficient in tyrosine kinase activity and mediation of insulin action, suggesting that the tyrosine kinase activity of the insulin receptor is essential for insulin action in vivo.	Tyrosine	83-91	insulin receptor	Homo sapiens	193-209
31827016-4	2019	Expression of the mutant receptor in cultured cells revealed it to be deficient in tyrosine kinase activity and mediation of insulin action, suggesting that the tyrosine kinase activity of the insulin receptor is essential for insulin action in vivo.	Tyrosine	161-169	insulin receptor	Homo sapiens	193-209
30040480-11	2018	Additionally, IGF-II reduced mRNA expression of the insulin receptor in adipocytes and downregulated insulin receptor isoform A and glucose transporter 4 abundance and corresponding glucose uptake in visceral adipocytes.	Glucose	132-139	insulin receptor	Homo sapiens	52-68
30391805-2	2018	We hypothesize that changes in the expression of insulin receptor-related genes in the post-mortem brain tissue of patients with mood and psychotic disorders mediate the expression of dopamine regulation-related genes.	Dopamine	184-192	insulin receptor	Homo sapiens	49-65
30391805-7	2018	Illnesses by BMI effects on expression of dopamine genes were fully mediated by expression of insulin receptor gene (INSR).	Dopamine	42-50	insulin receptor	Homo sapiens	94-110
30391805-7	2018	Illnesses by BMI effects on expression of dopamine genes were fully mediated by expression of insulin receptor gene (INSR).	Dopamine	42-50	insulin receptor	Homo sapiens	117-121
32422022-3	2019	Upon binding of the insulin and insulin-like growth factor-1 (IGF-1), IR is activated by increasing the levels of tyrosine-phosphorylated (pY) IRP on tyrosine 960, 1150, and 1151 residues as well as IRS-1 recruitment to IRbeta.	Tyrosine	114-122	insulin receptor	Homo sapiens	70-72
32422022-3	2019	Upon binding of the insulin and insulin-like growth factor-1 (IGF-1), IR is activated by increasing the levels of tyrosine-phosphorylated (pY) IRP on tyrosine 960, 1150, and 1151 residues as well as IRS-1 recruitment to IRbeta.	Tyrosine	150-158	insulin receptor	Homo sapiens	70-72
31333090-9	2019	Protein tyrosine phosphatase-1B (PTP1B) works as a negative governor for the insulin signalling pathways, as it dephosphorylates the tyrosine of the insulin receptor and suppresses the insulin signalling cascade.	Tyrosine	8-16	insulin receptor	Homo sapiens	149-165
29721854-3	2019	Potential mechanisms underlying insulin resistance include serine phosphorylation of the insulin receptor substrate (IRS) or insulin receptor (IR) misallocation.	Serine	59-65	insulin receptor	Homo sapiens	89-105
29721854-3	2019	Potential mechanisms underlying insulin resistance include serine phosphorylation of the insulin receptor substrate (IRS) or insulin receptor (IR) misallocation.	Serine	59-65	insulin receptor	Homo sapiens	117-119
30532646-8	2018	In humans, reduced representation bisulfite sequencing (RRBS) was performed on peripheral samples that were obtained from individuals who were prenatally exposed to the "Dutch Hunger Winter", resulting in two Differentially Methylated Regions (DMRs) in INSR and CPTIA genes that were functionally, biologically and technically validated, and significantly associated with birth weights and LDL cholesterol levels in offspring.	Cholesterol	394-405	insulin receptor	Homo sapiens	253-257
29469970-0	2018	Glimepiride treatment in a patient with type A insulin resistance syndrome due to a novel heterozygous missense mutation in the insulin receptor gene.	glimepiride	0-11	insulin receptor	Homo sapiens	128-144
30001602-2	2018	Recently, 2,4-Diarylaminopyrimidines with high inhibitory activity over InsR/IGF1R were reported as ALK inhibitors, which harboring phosphine oxide moiety.	2,4-diarylaminopyrimidines	10-36	insulin receptor	Homo sapiens	72-76
30001602-2	2018	Recently, 2,4-Diarylaminopyrimidines with high inhibitory activity over InsR/IGF1R were reported as ALK inhibitors, which harboring phosphine oxide moiety.	Phosphine oxide	132-147	insulin receptor	Homo sapiens	72-76
30001602-3	2018	In this work, it is the first time to reveal that the incorporation of dimethylphosphine oxide moiety and the smaller active pocket of ALK is key factor in the selectivity of inhibitor 11q toward ALK over IGF1R/InsR.	Dimethylphosphine oxide	71-94	insulin receptor	Homo sapiens	211-215
30206202-5	2018	In this study, we described that treatment of breast cancer cell lines (T47D, BT474, and MDA-MB-468) with BEZ235 significantly triggered PI3K/mTOR signaling inactivation and increased multiple RTK expression, including EGFR, HER2, HER3, IGF-1 receptor, insulin receptor, and their phosphorylation levels.	dactolisib	106-112	insulin receptor	Homo sapiens	253-269
30033101-7	2018	Furthermore, the overexpression of miR-424-5p suppressed INSR expression significantly, leading to impaired insulin signaling and glycogen synthesis in hepatocytes.	Glycogen	130-138	insulin receptor	Homo sapiens	57-61
29274299-9	2018	Our data indicate that rosiglitazone has an anti-proliferative effect in Jurkat cells, which may be at least partly mediated via downregulating IR and IGF-1R expression.	Rosiglitazone	23-36	insulin receptor	Homo sapiens	144-146
29874257-3	2018	METHODS: An endothelial/dendritic cell-based innate immune model was used to study antigen-presenting cell activation, cytokine secretion, and insulin receptor signalling pathways induced by originator and non-originator insulin glargine products.	Insulin Glargine	229-237	insulin receptor	Homo sapiens	143-159
29874257-6	2018	In studies aimed at addressing the mechanisms leading to differential cytokine production by these products, we found (1) the inflammatory response was not mediated by bacterial contaminants, (2) the innate response was driven by the native insulin receptor through the MAPK pathway, and (3) the removal of insulin glargine significantly reduced their capacity to induce innate activity.	Insulin Glargine	315-323	insulin receptor	Homo sapiens	241-257
29168473-9	2018	Before treatment, the fasting and postprandial levels of the insulin receptor were significantly lower in patients with impaired glucose tolerance compared with those in patients with normal glucose tolerance and healthy children.	Glucose	129-136	insulin receptor	Homo sapiens	61-77
29168473-10	2018	After YTF treatment, both the fasting and the postprandial circulating insulin receptor levels were upregulated, and close to those in healthy children.	ytf	6-9	insulin receptor	Homo sapiens	71-87
30168485-0	2018	S961, a biosynthetic insulin receptor antagonist, downregulates insulin receptor expression &amp; suppresses the growth of breast cancer cells.	Adenosine Monophosphate	93-96	insulin receptor	Homo sapiens	21-37
30017861-4	2018	Our results demonstrate that chronic high insulin exposure increases glutamate-induced excitotoxity, which was blocked by insulin receptor antagonist (S961) and GSK-3beta inhibitor (SB216763).	Glutamic Acid	69-78	insulin receptor	Homo sapiens	122-138
29543533-3	2018	The inhibition of the transcriptional activity of Egr-1 enhanced the phosphorylation of the insulin receptor (InsR) and Akt, thus increasing glucose uptake in L6 myotubes after insulin stimulation, whereas overexpression of Egr-1 decreased insulin sensitivity.	Glucose	141-148	insulin receptor	Homo sapiens	92-108
29543533-3	2018	The inhibition of the transcriptional activity of Egr-1 enhanced the phosphorylation of the insulin receptor (InsR) and Akt, thus increasing glucose uptake in L6 myotubes after insulin stimulation, whereas overexpression of Egr-1 decreased insulin sensitivity.	Glucose	141-148	insulin receptor	Homo sapiens	110-114
29726999-3	2018	Whereas glycogen synthesis is attributed to progesterone, we previously found that the metabolic B isoform of the insulin receptor is maximally expressed in secretory-phase endometrium, indicating a potential role of insulin in glucose metabolism.	Glycogen	8-16	insulin receptor	Homo sapiens	114-130
29726999-3	2018	Whereas glycogen synthesis is attributed to progesterone, we previously found that the metabolic B isoform of the insulin receptor is maximally expressed in secretory-phase endometrium, indicating a potential role of insulin in glucose metabolism.	Progesterone	44-56	insulin receptor	Homo sapiens	114-130
29633446-10	2018	Structural analysis of this variant suggested disruption of a critical hydrogen bond between insulin and the insulin receptor; however, the clinical picture in some individuals also suggested abnormal insulin processing and insulin deficiency.	Hydrogen	71-79	insulin receptor	Homo sapiens	109-125
29899115-4	2018	A cis-alkene permitted the conformational flexibility of the A-chain N-terminal helix necessary for high-affinity IR binding, resulting in surprisingly rapid activity in vivo Here, we show that, unlike the rapidly acting LysB28ProB29 insulin analogue (KP insulin), cis-dicarba insulin is not inherently monomeric.	cis-alkene	2-12	insulin receptor	Homo sapiens	114-116
29274299-8	2018	Moreover, rosiglitazone significantly upregulated the level of PPARgamma, and downregulated the expression of insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF-1R) in a dose-dependent manner.	Rosiglitazone	10-23	insulin receptor	Homo sapiens	110-131
29731242-4	2018	In human hepatoma-derived cells (HepG2), KY-226 (0.3-10 muM) increased the phosphorylated insulin receptor (pIR) produced by insulin.	KY-226	41-47	insulin receptor	Homo sapiens	90-106
29731738-8	2018	These findings have therapeutic implications because cells with a decreased expression of IGF2BP3/IGF1R axis but an increased expression of the IR/IGF2 loop display higher sensitivity to the dual inhibitor OSI-906 than do control cells.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	206-213	insulin receptor	Homo sapiens	144-146
29512653-1	2018	The insulin receptor is a dimeric protein that has a crucial role in controlling glucose homeostasis, regulating lipid, protein and carbohydrate metabolism, and modulating brain neurotransmitter levels.	Carbohydrates	132-144	insulin receptor	Homo sapiens	4-20
29610518-2	2018	Here we show that the amount of biologically active IR is regulated by the cleavage of its ectodomain, by the beta-site amyloid precursor protein cleaving enzyme 1 (BACE1), in a glucose concentration-dependent manner.	Glucose	178-185	insulin receptor	Homo sapiens	52-54
29507903-9	2018	While exposure to insulin stimulated the cytotoxic activity of healthy NK cells, rapamycin prevented this effect and reduced NK insulin receptor expressions.	Sirolimus	81-90	insulin receptor	Homo sapiens	128-144
29262294-1	2018	The insulin receptor is an important regulator of metabolic processes in the body, and in particular of glucose homeostasis, including glucose uptake into peripheral tissues.	Glucose	104-111	insulin receptor	Homo sapiens	4-20
29619007-0	2018	Uric Acid Impairs Insulin Signaling by Promoting Enpp1 Binding to Insulin Receptor in Human Umbilical Vein Endothelial Cells.	Uric Acid	0-9	insulin receptor	Homo sapiens	66-82
29619007-10	2018	Moreover, UA induced ENPP1 binding to IR that resulted in an impairment of insulin signaling cascade.	Uric Acid	10-12	insulin receptor	Homo sapiens	38-40
29330302-7	2018	Holo-IGF1R and HybR both promoted cell proliferation and glucose uptake, whereas holo-InsR only promoted glucose uptake, and only holo-IGF1R showed anti-apoptotic effects.	Glucose	105-112	insulin receptor	Homo sapiens	86-90
29500363-4	2018	We find that by improving insulin sensitivity at the level of the insulin receptor (IR), either by IR over-expression or by knocking down the negative regulator of IR activity, protein tyrosine-phosphatase 1B (PTP1B), podocytes are protected from ER stress caused by fatty acids or diabetic media containing high glucose, high insulin and inflammatory cytokines TNFalpha and IL-6.	Fatty Acids	267-278	insulin receptor	Homo sapiens	66-82
29500363-4	2018	We find that by improving insulin sensitivity at the level of the insulin receptor (IR), either by IR over-expression or by knocking down the negative regulator of IR activity, protein tyrosine-phosphatase 1B (PTP1B), podocytes are protected from ER stress caused by fatty acids or diabetic media containing high glucose, high insulin and inflammatory cytokines TNFalpha and IL-6.	Fatty Acids	267-278	insulin receptor	Homo sapiens	84-86
29500363-4	2018	We find that by improving insulin sensitivity at the level of the insulin receptor (IR), either by IR over-expression or by knocking down the negative regulator of IR activity, protein tyrosine-phosphatase 1B (PTP1B), podocytes are protected from ER stress caused by fatty acids or diabetic media containing high glucose, high insulin and inflammatory cytokines TNFalpha and IL-6.	Glucose	313-320	insulin receptor	Homo sapiens	66-82
29500363-4	2018	We find that by improving insulin sensitivity at the level of the insulin receptor (IR), either by IR over-expression or by knocking down the negative regulator of IR activity, protein tyrosine-phosphatase 1B (PTP1B), podocytes are protected from ER stress caused by fatty acids or diabetic media containing high glucose, high insulin and inflammatory cytokines TNFalpha and IL-6.	Glucose	313-320	insulin receptor	Homo sapiens	84-86
28990588-9	2018	CONCLUSIONS: Triglycerides cross the blood-brain barrier rapidly, are found in human cerebrospinal fluid, and induce central leptin and insulin receptor resistance, decreasing satiety and cognition.	Triglycerides	13-26	insulin receptor	Homo sapiens	136-152
29321379-5	2018	When the blood glucose level is elevated, as in individuals with diabetes mellitus, MR binding diminishes due to glucose competition, leading to reduced MR-mediated clearance and increased partitioning for IR binding and consequent glucose lowering.	Glucose	15-22	insulin receptor	Homo sapiens	206-208
29321379-5	2018	When the blood glucose level is elevated, as in individuals with diabetes mellitus, MR binding diminishes due to glucose competition, leading to reduced MR-mediated clearance and increased partitioning for IR binding and consequent glucose lowering.	Glucose	113-120	insulin receptor	Homo sapiens	206-208
29321379-5	2018	When the blood glucose level is elevated, as in individuals with diabetes mellitus, MR binding diminishes due to glucose competition, leading to reduced MR-mediated clearance and increased partitioning for IR binding and consequent glucose lowering.	Glucose	113-120	insulin receptor	Homo sapiens	206-208
29321379-6	2018	These studies demonstrate that a glucose-dependent locus of insulin clearance and, hence, insulin action can be achieved by targeting MR and IR concurrently.	Glucose	33-40	insulin receptor	Homo sapiens	141-143
29435137-6	2018	We also show that silencing of HER2 and the insulin receptor can partially resensitize AZD0530 resistant cells, which was associated with decreased phosphorylation of MEK and ERK.	saracatinib	87-94	insulin receptor	Homo sapiens	44-60
30205369-8	2018	These biguanide actions are likely mediated through modulation of: 1) common (mTOR/PI3K/intracellular-Ca2+mobilization) and distinct (MAPK) signaling pathways; and 2) gene expression of key receptors regulating somatotrope/corticotrope/gonadotrope function (i.e. upregulation of SSTR2/SSTR5/INSR/IGF1R/LEPR).	Biguanides	6-15	insulin receptor	Homo sapiens	291-295
29264467-7	2017	We tried high-dose steroids, azathioprine, and intravenous immunoglobulins, which resulted in improvement and barely detectable insulin receptor antibody.	Steroids	19-27	insulin receptor	Homo sapiens	128-144
29264467-7	2017	We tried high-dose steroids, azathioprine, and intravenous immunoglobulins, which resulted in improvement and barely detectable insulin receptor antibody.	Azathioprine	29-41	insulin receptor	Homo sapiens	128-144
28852804-9	2017	These podocytes lose expression of the IR as a direct consequence of prolonged exposure to high insulin concentrations, which causes an increase in IR protein degradation via a proteasome-dependent and bafilomycin-sensitive pathway.	bafilomycin	202-213	insulin receptor	Homo sapiens	39-41
28852804-9	2017	These podocytes lose expression of the IR as a direct consequence of prolonged exposure to high insulin concentrations, which causes an increase in IR protein degradation via a proteasome-dependent and bafilomycin-sensitive pathway.	bafilomycin	202-213	insulin receptor	Homo sapiens	148-150
29159216-7	2017	The data is related to a research article entitled "MiR-1271 upregulated by saturated fatty acid palmitate provokes impaired insulin signaling by repressing INSR and IRS-1 expression in HepG2 cells" (Yang et al., 2016) [1].	saturated fatty acid palmitate	76-106	insulin receptor	Homo sapiens	157-161
30151293-9	2017	Irisin is found to improve insulin resistance and type 2 diabetes by increasing sensitization of the insulin receptor in skeletal muscle and heart by improving hepatic glucose and lipid metabolism, promoting pancreatic beta cell functions, and transforming white adipose tissue to brown adipose tissue.	Glucose	168-175	insulin receptor	Homo sapiens	101-117
29124099-6	2017	More detailed analysis and understanding of the roles of miR-96 in diet-induced insulin resistance can be found in "Induction of miR-96 by dietary saturated fatty acids exacerbates hepatic insulin resistance through the suppression of INSR and IRS-1" (Yang et al., 2016) [1].	Fatty Acids	147-168	insulin receptor	Homo sapiens	235-239
28576743-5	2017	We assessed the effects of BIL on internalization of the insulin receptor (IR) and studied cellular clearance of BIL.	basal insulin peglispro	27-30	insulin receptor	Homo sapiens	57-78
28760855-0	2017	Dual Targeting of Insulin Receptor and KIT in Imatinib-Resistant Gastrointestinal Stromal Tumors.	Imatinib Mesylate	46-54	insulin receptor	Homo sapiens	18-34
28576743-9	2017	BIL and human insulin both induced rapid phosphorylation and internalization of human IR.	basal insulin peglispro	0-3	insulin receptor	Homo sapiens	86-88
28576743-10	2017	CONCLUSIONS: Our findings show that treatment of cells with BIL stimulates internalization and localization of IR to early endosomes.	basal insulin peglispro	60-63	insulin receptor	Homo sapiens	111-113
28760855-5	2017	Additive effects showing increased apoptosis, antiproliferative effects, cell-cycle arrest, and decreased pAKT and pS6 expression, tumor growth, migration, and invasiveness were observed in imatinib-resistant GIST cells with IR activation after coordinated inhibition of IR and KIT by linsitinib (or IR shRNA) and imatinib, respectively, compared with either intervention alone.	Imatinib Mesylate	314-322	insulin receptor	Homo sapiens	225-227
28760855-7	2017	Our findings suggest that combinatorial inhibition of IR and KIT warrants clinical evaluation as a novel therapeutic strategy in imatinib-resistant GISTs.	Imatinib Mesylate	129-137	insulin receptor	Homo sapiens	54-56
28729397-0	2017	The IGF1R/INSR Inhibitor BI 885578 Selectively Inhibits Growth of IGF2-Overexpressing Colorectal Cancer Tumors and Potentiates the Efficacy of Anti-VEGF Therapy.	BI 885578	25-34	insulin receptor	Homo sapiens	10-14
28729397-6	2017	An in vitro screen of 34 colorectal cancer cell lines revealed IGF2 expression to significantly correlate with sensitivity to the IGF1R/INSR inhibitor BI 885578.	BI 885578	151-160	insulin receptor	Homo sapiens	136-140
28877477-4	2017	Our results support a model whereby heparin competes with insulin for insulin receptor binding on AgRP neurons, and by doing so it inhibits FoxO1 activity to promote AgRP release and feeding.	Heparin	36-43	insulin receptor	Homo sapiens	70-86
28760855-3	2017	Using phospho-RTK and immunoblot assays, we demonstrate activation of KIT and insulin receptor (IR) in imatinib-resistant GIST cell lines (GIST430 and GIST48) and biopsies with acquisition of KIT secondary mutations, but not in imatinib-sensitive GIST cells (GIST882 and GIST-T1).	Imatinib Mesylate	103-111	insulin receptor	Homo sapiens	78-94
28760855-3	2017	Using phospho-RTK and immunoblot assays, we demonstrate activation of KIT and insulin receptor (IR) in imatinib-resistant GIST cell lines (GIST430 and GIST48) and biopsies with acquisition of KIT secondary mutations, but not in imatinib-sensitive GIST cells (GIST882 and GIST-T1).	Imatinib Mesylate	103-111	insulin receptor	Homo sapiens	96-98
28760855-3	2017	Using phospho-RTK and immunoblot assays, we demonstrate activation of KIT and insulin receptor (IR) in imatinib-resistant GIST cell lines (GIST430 and GIST48) and biopsies with acquisition of KIT secondary mutations, but not in imatinib-sensitive GIST cells (GIST882 and GIST-T1).	Imatinib Mesylate	228-236	insulin receptor	Homo sapiens	78-94
28760855-3	2017	Using phospho-RTK and immunoblot assays, we demonstrate activation of KIT and insulin receptor (IR) in imatinib-resistant GIST cell lines (GIST430 and GIST48) and biopsies with acquisition of KIT secondary mutations, but not in imatinib-sensitive GIST cells (GIST882 and GIST-T1).	Imatinib Mesylate	228-236	insulin receptor	Homo sapiens	96-98
28760855-4	2017	Treatment with linsitinib, a specific IR inhibitor, inhibited IR and downstream intermediates AKT, MAPK, and S6 in GIST430 and GIST48, but not in GIST882, exerting minimal effect on KIT phosphorylation in these cell lines.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	15-25	insulin receptor	Homo sapiens	38-40
28760855-4	2017	Treatment with linsitinib, a specific IR inhibitor, inhibited IR and downstream intermediates AKT, MAPK, and S6 in GIST430 and GIST48, but not in GIST882, exerting minimal effect on KIT phosphorylation in these cell lines.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	15-25	insulin receptor	Homo sapiens	62-64
28760855-5	2017	Additive effects showing increased apoptosis, antiproliferative effects, cell-cycle arrest, and decreased pAKT and pS6 expression, tumor growth, migration, and invasiveness were observed in imatinib-resistant GIST cells with IR activation after coordinated inhibition of IR and KIT by linsitinib (or IR shRNA) and imatinib, respectively, compared with either intervention alone.	Imatinib Mesylate	190-198	insulin receptor	Homo sapiens	225-227
28760855-5	2017	Additive effects showing increased apoptosis, antiproliferative effects, cell-cycle arrest, and decreased pAKT and pS6 expression, tumor growth, migration, and invasiveness were observed in imatinib-resistant GIST cells with IR activation after coordinated inhibition of IR and KIT by linsitinib (or IR shRNA) and imatinib, respectively, compared with either intervention alone.	Imatinib Mesylate	190-198	insulin receptor	Homo sapiens	271-273
28760855-5	2017	Additive effects showing increased apoptosis, antiproliferative effects, cell-cycle arrest, and decreased pAKT and pS6 expression, tumor growth, migration, and invasiveness were observed in imatinib-resistant GIST cells with IR activation after coordinated inhibition of IR and KIT by linsitinib (or IR shRNA) and imatinib, respectively, compared with either intervention alone.	Imatinib Mesylate	190-198	insulin receptor	Homo sapiens	271-273
28760855-5	2017	Additive effects showing increased apoptosis, antiproliferative effects, cell-cycle arrest, and decreased pAKT and pS6 expression, tumor growth, migration, and invasiveness were observed in imatinib-resistant GIST cells with IR activation after coordinated inhibition of IR and KIT by linsitinib (or IR shRNA) and imatinib, respectively, compared with either intervention alone.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	285-295	insulin receptor	Homo sapiens	225-227
28442548-7	2017	In K8-null hepatocytes, IR trafficking vesicles that are labeled by Rab5/EEA1/phosphatidylinositol 3-phosphate accumulate at a juxtanuclear region via a microtubule-dependent process.	phosphatidylinositol 3-phosphate	78-110	insulin receptor	Homo sapiens	24-26
28442548-8	2017	Moreover, interference with phosphatidylinositol 4,5-biphosphate signaling aggravates IR/Rab5 accumulation.	Phosphatidylinositol 4,5-Diphosphate	28-64	insulin receptor	Homo sapiens	86-88
28130417-0	2017	Phosphorylation of clustered serine residues in the N-terminus of BPS domain negatively regulates formation of the complex between human Grb14 and insulin receptor.	Serine	29-35	insulin receptor	Homo sapiens	147-163
28703075-5	2017	Thus, insulin released from the AuNP@Dextran-insulin conjugates to maintain kinetic equilibrium and prefers to bind to the insulin receptor.	Dextrans	37-44	insulin receptor	Homo sapiens	123-139
28436941-0	2017	INSR gene polymorphisms correlate with sensitivity to platinum-based chemotherapy and prognosis in patients with epithelial ovarian cancer.	Platinum	54-62	insulin receptor	Homo sapiens	0-4
28436941-1	2017	This study aimed to investigate the correlation between INSR gene polymorphisms on platinum-based chemotherapy sensitivity and prognosis in epithelial ovarian cancer (EOC).	Platinum	83-91	insulin receptor	Homo sapiens	56-60
28436941-9	2017	These findings indicate that INSR rs2252673 and rs3745546 polymorphisms were associated with sensitivity to platinum-based chemotherapy in EOC patients and rs2252673 polymorphism may be an independent risk factor for EOC prognosis.	Platinum	108-116	insulin receptor	Homo sapiens	29-33
28560459-5	2017	The phosphorylation of extracellular signal-regulated kinase (ERK), an important downstream protein of the InsR-mitogen-activated protein kinases (MAPK) signaling pathway, was also detected by western blot analysis when (+)-PTZ and BD-1063 were added to the 80 mmHg-treated cells.	Pentazocine	220-227	insulin receptor	Homo sapiens	107-111
28468775-3	2017	Our previous work showed that in tamoxifen-resistant cells, IGF1R expression was lacking, but InsR inhibition effectively blocked growth.	Tamoxifen	33-42	insulin receptor	Homo sapiens	94-98
28560459-9	2017	(+)-PTZ decreased the apoptosis and death of hTMCs and increased the expression of Sig-1R and InsR, and the phosphorylation of ERK.	Pentazocine	0-7	insulin receptor	Homo sapiens	94-98
28560459-11	2017	The present study suggested that Sig-1R agonist (+)-PTZ can protect hTMCs from pressure-induced apoptosis and death by activating InsR and the MAPK signal pathway.	Pentazocine	48-55	insulin receptor	Homo sapiens	130-134
28507217-1	2017	Regulation of Glucose Uptake and Enteroendocrine Function by the Intestinal Epithelial Insulin Receptor.	Glucose	14-21	insulin receptor	Homo sapiens	87-103
28507218-1	2017	Regulation of Glucose Uptake and Enteroendocrine Function by the Intestinal Epithelial Insulin Receptor.	Glucose	14-21	insulin receptor	Homo sapiens	87-103
28117222-5	2017	In the Sinhalese cohort, maternal INSR rs2059806 AA genotype was greater among pre-eclamptic women who delivered small for gestational age infants compared with the uncomplicated pregnancies (10.8% versus 4.2%, OR[95%CI] = 2.8[1.0-7.4], P = 0.03).	sinhalese	7-16	insulin receptor	Homo sapiens	34-38
28345670-5	2017	Strikingly, replacement of leucine973 in the juxtamembrane region of IR to phenylalanine, which is present in IGF1R, mimics many of these signalling and gene expression responses.	leucine973	27-37	insulin receptor	Homo sapiens	69-71
28345670-5	2017	Strikingly, replacement of leucine973 in the juxtamembrane region of IR to phenylalanine, which is present in IGF1R, mimics many of these signalling and gene expression responses.	Phenylalanine	75-88	insulin receptor	Homo sapiens	69-71
26950281-8	2017	The surface area around position A3 was increased when valine was substituted by leucine, while at positions B24 and B25 aromatic amino acid phenylalanine replaced by non-aromatic serine and leucine might be responsible for fewer binding interactions at the binding site of IR that leads to instability of the complex.	aromatic amino acid phenylalanine	121-154	insulin receptor	Homo sapiens	274-276
26950281-8	2017	The surface area around position A3 was increased when valine was substituted by leucine, while at positions B24 and B25 aromatic amino acid phenylalanine replaced by non-aromatic serine and leucine might be responsible for fewer binding interactions at the binding site of IR that leads to instability of the complex.	Leucine	191-198	insulin receptor	Homo sapiens	274-276
28677502-4	2017	Its binding to insulin receptor on the surface of diverse cells allows glucose entry into cells, and activates a variety of cellular actions.	Glucose	71-78	insulin receptor	Homo sapiens	15-31
27868170-5	2017	The phosphorylation of serine residues in the insulin receptor and IRS-1 molecule results in diminished enzymatic activity in the phosphatidylinositol 3-kinase (PI3K)/Akt pathway.	Serine	23-29	insulin receptor	Homo sapiens	46-62
28025108-8	2017	The results of in vitro experiments could determine that the DEHP-induced activation of peroxisome proliferator activated receptor gamma (PPARgamma) played a key role in the production of oxidative stress and down-regulated expression of insulin receptor and GLUT4 proteins in L02 cells.	Diethylhexyl Phthalate	61-65	insulin receptor	Homo sapiens	238-254
26660109-6	2016	Treatment with memantine (1-10 muM) improved STZ-induced neurotrophic factor decline (BDNF, GDNF) along with IR dysfunction as evidenced by a significant increase in IR protein expression, phosphorylation of IRS-1, Akt, and GSK-3 alpha/beta in astrocytes.	Streptozocin	45-48	insulin receptor	Homo sapiens	166-168
28122381-6	2017	In addition, this review highlights insulin transport into the brain, signaling pathways associated with hypothalamic insulin receptor expression in the regulation of hepatic glucose production, and finally the perturbation of systemic glucose homeostasis as a consequence of central insulin resistance.	Glucose	175-182	insulin receptor	Homo sapiens	118-134
28239181-1	2017	BACKGROUND: Magnesium acts as a cofactor in many intracellular reactions including phosphorylation of the insulin receptor; therefore, its imbalance can potentially cause insulin resistance.	Magnesium	12-21	insulin receptor	Homo sapiens	106-122
27983572-7	2016	Selenium supplementation was associated with a significantly decreased level of HbA1c but not fasting plasma glucose (FPG) and significant down-regulation of seven genes: INSR, ADIPOR1, LDHA, PDHA, PDHB, MYC, and HIF1AN.	Selenium	0-8	insulin receptor	Homo sapiens	171-175
27695899-1	2016	AIMS/HYPOTHESIS: Soluble insulin receptor (sIR), the ectodomain of the insulin receptor (IR), has been detected in human plasma and its concentration paralleled that of blood glucose.	Glucose	175-182	insulin receptor	Homo sapiens	25-41
27695899-1	2016	AIMS/HYPOTHESIS: Soluble insulin receptor (sIR), the ectodomain of the insulin receptor (IR), has been detected in human plasma and its concentration paralleled that of blood glucose.	Glucose	175-182	insulin receptor	Homo sapiens	71-87
27695899-1	2016	AIMS/HYPOTHESIS: Soluble insulin receptor (sIR), the ectodomain of the insulin receptor (IR), has been detected in human plasma and its concentration paralleled that of blood glucose.	Glucose	175-182	insulin receptor	Homo sapiens	44-46
27695899-2	2016	We have previously developed an in vitro model using HepG2 liver-derived cells, which mimics changes in sIR levels in plasma from diabetic patients and shows that calcium-dependent proteases cleave IR extracellularly (a process known as shedding).	Calcium	163-170	insulin receptor	Homo sapiens	105-107
27695899-4	2016	METHODS: Using the in vitro model, we investigated the molecular mechanisms of IR cleavage, which is accelerated by high-glucose treatment.	Glucose	121-128	insulin receptor	Homo sapiens	79-81
27695899-10	2016	CONCLUSIONS/INTERPRETATION: Sequential cleavage of IR by calpain 2 and gamma-secretase may contribute to insulin signalling in cells and its inhibition may be partly responsible for the glucose-lowering effects of metformin.	Glucose	186-193	insulin receptor	Homo sapiens	51-53
27695899-10	2016	CONCLUSIONS/INTERPRETATION: Sequential cleavage of IR by calpain 2 and gamma-secretase may contribute to insulin signalling in cells and its inhibition may be partly responsible for the glucose-lowering effects of metformin.	Metformin	214-223	insulin receptor	Homo sapiens	51-53
26660109-0	2016	Inhibitory Effect of Memantine on Streptozotocin-Induced Insulin Receptor Dysfunction, Neuroinflammation, Amyloidogenesis, and Neurotrophic Factor Decline in Astrocytes.	Memantine	21-30	insulin receptor	Homo sapiens	57-73
26660109-0	2016	Inhibitory Effect of Memantine on Streptozotocin-Induced Insulin Receptor Dysfunction, Neuroinflammation, Amyloidogenesis, and Neurotrophic Factor Decline in Astrocytes.	Streptozocin	34-48	insulin receptor	Homo sapiens	57-73
26660109-1	2016	Our earlier studies showed that insulin receptor (IR) dysfunction along with neuroinflammation and amyloidogenesis played a major role in streptozotocin (STZ)-induced toxicity in astrocytes.	Streptozocin	138-152	insulin receptor	Homo sapiens	32-48
26660109-1	2016	Our earlier studies showed that insulin receptor (IR) dysfunction along with neuroinflammation and amyloidogenesis played a major role in streptozotocin (STZ)-induced toxicity in astrocytes.	Streptozocin	138-152	insulin receptor	Homo sapiens	50-52
26660109-1	2016	Our earlier studies showed that insulin receptor (IR) dysfunction along with neuroinflammation and amyloidogenesis played a major role in streptozotocin (STZ)-induced toxicity in astrocytes.	Streptozocin	154-157	insulin receptor	Homo sapiens	32-48
26660109-1	2016	Our earlier studies showed that insulin receptor (IR) dysfunction along with neuroinflammation and amyloidogenesis played a major role in streptozotocin (STZ)-induced toxicity in astrocytes.	Streptozocin	154-157	insulin receptor	Homo sapiens	50-52
26660109-6	2016	Treatment with memantine (1-10 muM) improved STZ-induced neurotrophic factor decline (BDNF, GDNF) along with IR dysfunction as evidenced by a significant increase in IR protein expression, phosphorylation of IRS-1, Akt, and GSK-3 alpha/beta in astrocytes.	Memantine	15-24	insulin receptor	Homo sapiens	109-111
26660109-6	2016	Treatment with memantine (1-10 muM) improved STZ-induced neurotrophic factor decline (BDNF, GDNF) along with IR dysfunction as evidenced by a significant increase in IR protein expression, phosphorylation of IRS-1, Akt, and GSK-3 alpha/beta in astrocytes.	Memantine	15-24	insulin receptor	Homo sapiens	166-168
27729247-10	2016	Together, high fructose dysregulates IRS-1 phosphorylation state and proximal insulin receptor signaling in VSMCs, but does not affect PDGF-induced proliferative signaling.	Fructose	15-23	insulin receptor	Homo sapiens	78-94
27729247-11	2016	These findings suggest that systemic insulin resistance rather than VSMC-specific dysregulation of insulin receptor signaling by high fructose may play a major role in enhancing atherosclerosis and neointimal hyperplasia.	Fructose	134-142	insulin receptor	Homo sapiens	99-115
27743890-9	2016	Simvastatin also decreased phosphorylation of insulin receptor (IR), insulin receptor substrate 1 (IRS-1), AKT and glycogen synthase kinase 3beta (GSK-3beta), and downregulated GLUT4.	Simvastatin	0-11	insulin receptor	Homo sapiens	46-62
27743890-9	2016	Simvastatin also decreased phosphorylation of insulin receptor (IR), insulin receptor substrate 1 (IRS-1), AKT and glycogen synthase kinase 3beta (GSK-3beta), and downregulated GLUT4.	Simvastatin	0-11	insulin receptor	Homo sapiens	64-66
27514532-2	2016	When tyrosine is phosphorylated by the activated insulin receptor, IRS proteins recruit downstream effectors, such as phosphoinositide 3-kinase and mitogen-activated protein kinase, in order to elicit cellular responses such as glucose uptake, lipid metabolism and cell proliferation.	Tyrosine	5-13	insulin receptor	Homo sapiens	49-65
27729247-0	2016	High fructose-mediated attenuation of insulin receptor signaling does not affect PDGF-induced proliferative signaling in vascular smooth muscle cells.	Fructose	5-13	insulin receptor	Homo sapiens	38-54
27514532-2	2016	When tyrosine is phosphorylated by the activated insulin receptor, IRS proteins recruit downstream effectors, such as phosphoinositide 3-kinase and mitogen-activated protein kinase, in order to elicit cellular responses such as glucose uptake, lipid metabolism and cell proliferation.	Glucose	228-235	insulin receptor	Homo sapiens	49-65
27729247-6	2016	Concentration-dependent studies with high fructose (5-25mM) showed marked increases in IRS-1 serine phosphorylation, a key adapter protein in insulin receptor signaling.	Fructose	42-50	insulin receptor	Homo sapiens	142-158
27729247-6	2016	Concentration-dependent studies with high fructose (5-25mM) showed marked increases in IRS-1 serine phosphorylation, a key adapter protein in insulin receptor signaling.	Serine	93-99	insulin receptor	Homo sapiens	142-158
27296149-8	2016	In vitro, we found that INSR was degraded by MMP-8 and this was inhibited by doxycycline and Ilomastat/GM6001.	Doxycycline	77-88	insulin receptor	Homo sapiens	24-28
27470565-5	2016	Mechanistically, the inhibition of glucose uptake and GLUT4 translocation elicited by simvastatin were associated with the suppression of the insulin receptor (IR)/IR substrate (IRS)/Akt signaling cascade.	Glucose	35-42	insulin receptor	Homo sapiens	142-158
27470565-5	2016	Mechanistically, the inhibition of glucose uptake and GLUT4 translocation elicited by simvastatin were associated with the suppression of the insulin receptor (IR)/IR substrate (IRS)/Akt signaling cascade.	Glucose	35-42	insulin receptor	Homo sapiens	160-162
27470565-5	2016	Mechanistically, the inhibition of glucose uptake and GLUT4 translocation elicited by simvastatin were associated with the suppression of the insulin receptor (IR)/IR substrate (IRS)/Akt signaling cascade.	Simvastatin	86-97	insulin receptor	Homo sapiens	142-158
27470565-5	2016	Mechanistically, the inhibition of glucose uptake and GLUT4 translocation elicited by simvastatin were associated with the suppression of the insulin receptor (IR)/IR substrate (IRS)/Akt signaling cascade.	Simvastatin	86-97	insulin receptor	Homo sapiens	160-162
27470565-6	2016	Simvastatin suppressed the phosphorylation of IR, IRS-1 and Akt, and total expression of IR or IRS-1, but did not affect Akt.	Simvastatin	0-11	insulin receptor	Homo sapiens	46-48
27470565-6	2016	Simvastatin suppressed the phosphorylation of IR, IRS-1 and Akt, and total expression of IR or IRS-1, but did not affect Akt.	Simvastatin	0-11	insulin receptor	Homo sapiens	50-52
27470565-8	2016	In conclusion, our findings indicate that simvastatin suppresses glucose uptake activity and GLUT4 translocation via IR-dependent IRS-1/PI3K/Akt pathway.	Simvastatin	42-53	insulin receptor	Homo sapiens	117-119
27470565-8	2016	In conclusion, our findings indicate that simvastatin suppresses glucose uptake activity and GLUT4 translocation via IR-dependent IRS-1/PI3K/Akt pathway.	Glucose	65-72	insulin receptor	Homo sapiens	117-119
27490779-6	2016	We observed that swertiamarin significantly increased the expressions of major insulin signaling proteins like Insulin receptor (IR), PI(3)K, pAkt with concomitant reduction in p307 IRS-1.	swertiamarin	17-29	insulin receptor	Homo sapiens	111-127
27490779-6	2016	We observed that swertiamarin significantly increased the expressions of major insulin signaling proteins like Insulin receptor (IR), PI(3)K, pAkt with concomitant reduction in p307 IRS-1.	swertiamarin	17-29	insulin receptor	Homo sapiens	129-131
27900351-4	2016	Further extensive insights into the implications of miRNAs, particularly miR-1271, in HepG2 cells can be found in "MiR-1271 upregulated by saturated fatty acid palmitate provokes impaired insulin signaling by repressing INSR and IRS-1 expression in HepG2 cells" (W.M.	saturated fatty acid palmitate	139-169	insulin receptor	Homo sapiens	220-224
27589886-5	2016	The "insulin receptor signaling", "acute phase response signaling", "Interleukin(IL)-6 signaling", and "prolactin signaling" pathways were significantly enriched in relation to p,p"-DDE.	Dichlorodiphenyl Dichloroethylene	177-185	insulin receptor	Homo sapiens	5-21
27613089-0	2016	MiR-1271 upregulated by saturated fatty acid palmitate provokes impaired insulin signaling by repressing INSR and IRS-1 expression in HepG2 cells.	saturated fatty acid palmitate	24-54	insulin receptor	Homo sapiens	105-109
27613089-3	2016	SFA palmitate provoked an impairment of insulin signaling in HepG2 cells via a reduction in the expression of INSR and IRS-1 protein.	sfa palmitate	0-13	insulin receptor	Homo sapiens	110-114
27613089-6	2016	Furthermore, the overexpression of miR-1271 caused a substantial decrease in INSR and IRS-1 expression, which led to an impairment in insulin signaling and glycogen metabolism.	Glycogen	156-164	insulin receptor	Homo sapiens	77-81
27613089-7	2016	Therefore, these findings suggest that the induction of miR-1271 by SFA palmitate promotes the development of insulin resistance by targeting INSR and IRS-1 in hepatocytes.	sfa palmitate	68-81	insulin receptor	Homo sapiens	142-146
27733843-4	2016	In this study, we assessed alterations in the IR-A and IR-B isoform ratio and associated changes in cell proliferation and migration of PCa cell lines following exposure to altered concentrations of glucose and treatment with IGF-II and insulin.	Glucose	199-206	insulin receptor	Homo sapiens	46-48
27733843-4	2016	In this study, we assessed alterations in the IR-A and IR-B isoform ratio and associated changes in cell proliferation and migration of PCa cell lines following exposure to altered concentrations of glucose and treatment with IGF-II and insulin.	Glucose	199-206	insulin receptor	Homo sapiens	55-57
27648925-5	2016	Isolated by a cell-based SELEX method that allows enrichment for internalizing aptamers, GL56 rapidly internalizes into target cells and is able to discriminate IR from the highly homologous insulin-like growth factor receptor 1.	gl56	89-93	insulin receptor	Homo sapiens	161-163
27648925-7	2016	Given the growing interest in the insulin receptor as target for cancer treatment, GL56 reveals a novel molecule with great translational potential as inhibitor and delivery tool for IR-dependent cancers.	gl56	83-87	insulin receptor	Homo sapiens	34-50
27648925-7	2016	Given the growing interest in the insulin receptor as target for cancer treatment, GL56 reveals a novel molecule with great translational potential as inhibitor and delivery tool for IR-dependent cancers.	gl56	83-87	insulin receptor	Homo sapiens	183-185
27481946-4	2016	We recently reported that the p21-activated kinases (PAKs), which are activated by GTP-bound Ras-related C3 botulinum toxin substrate 1 (Rac1), mediate the phosphorylation of PREX2 after insulin receptor activation.	Guanosine Triphosphate	83-86	insulin receptor	Homo sapiens	187-203
27296149-8	2016	In vitro, we found that INSR was degraded by MMP-8 and this was inhibited by doxycycline and Ilomastat/GM6001.	ilomastat	93-102	insulin receptor	Homo sapiens	24-28
27296149-8	2016	In vitro, we found that INSR was degraded by MMP-8 and this was inhibited by doxycycline and Ilomastat/GM6001.	N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide	103-109	insulin receptor	Homo sapiens	24-28
27296149-10	2016	This INSR cleavage by MMP-8 can be inhibited by synthetic MMP-8 inhibitors such as doxycycline.	Doxycycline	83-94	insulin receptor	Homo sapiens	5-9
26298663-10	2016	Further, STZ also leads to inhibition of Akt/PKB, insulin receptor (IR) signaling molecule, and insulin resistance in brain.	Streptozocin	9-12	insulin receptor	Homo sapiens	50-66
27526875-8	2016	Induction of exon 11 skipping by a splice-site competitive antisense oligonucleotide inhibited the MAPK-ERK signaling pathway downstream of the insulin receptor, sensitizing the pancreatic beta-cell line MIN6 to stress-induced apoptosis and lipotoxicity.	Oligonucleotides	69-84	insulin receptor	Homo sapiens	144-160
26876199-3	2016	We have previously shown that the closely related insulin receptor (InsR) is expressed in tamoxifen-resistant (TamR) breast cancer cells.	Tamoxifen	90-99	insulin receptor	Homo sapiens	50-66
26876199-3	2016	We have previously shown that the closely related insulin receptor (InsR) is expressed in tamoxifen-resistant (TamR) breast cancer cells.	Tamoxifen	90-99	insulin receptor	Homo sapiens	68-72
26298663-10	2016	Further, STZ also leads to inhibition of Akt/PKB, insulin receptor (IR) signaling molecule, and insulin resistance in brain.	Streptozocin	9-12	insulin receptor	Homo sapiens	68-70
27291139-2	2016	Efficient glucose uptake by the endothelium requires insulin receptor activation to deliver GLUT receptors to the cell surface.	Glucose	10-17	insulin receptor	Homo sapiens	53-69
27155325-0	2016	Novel method demonstrates differential ligand activation and phosphatase-mediated deactivation of insulin receptor tyrosine-specific phosphorylation.	Tyrosine	115-123	insulin receptor	Homo sapiens	98-114
27155325-6	2016	We hypothesized that determining differential phosphorylation among individual tyrosine sites activated by ligand binding or dephosphorylation by phosphatases could provide valuable insight into insulin receptor signaling.	Tyrosine	79-87	insulin receptor	Homo sapiens	195-211
27155325-10	2016	Furthermore, we show that insulin receptor deactivation, regulated by tyrosine phosphatases, occurs distinctively across specific tyrosine residues.	Tyrosine	70-78	insulin receptor	Homo sapiens	26-42
27506738-6	2016	RESULTS: The basal autophagy level decreased under the high glucose conditions, which was accompanied by a decrease in the glucose uptake and phosphorylation of the insulin receptor in the human podocytes.	Glucose	60-67	insulin receptor	Homo sapiens	165-181
27506738-7	2016	More interestingly, the glucose uptake and the phosphorylation of the insulin receptor were decreased by 3-MA stimulation and increased by rapamycin, illustrating that the responsiveness of insulin was regulated by autophagy.	3-methyladenine	105-109	insulin receptor	Homo sapiens	70-86
27506738-7	2016	More interestingly, the glucose uptake and the phosphorylation of the insulin receptor were decreased by 3-MA stimulation and increased by rapamycin, illustrating that the responsiveness of insulin was regulated by autophagy.	Sirolimus	139-148	insulin receptor	Homo sapiens	70-86
27281820-3	2016	Further refinement has yielded, in particular, a 36-residue Site 2-Site 1 fusion peptide, S519, that binds the insulin receptor with subnanomolar affinity and exhibits agonist activity in both lipogenesis and glucose uptake assays.	Glucose	209-216	insulin receptor	Homo sapiens	111-127
26831715-2	2016	This study aimed to determine the MTD, safety, pharmacokinetics, pharmacodynamics, and preliminary antitumor activity of linsitinib, a potent oral IGF1R/INSR inhibitor, with EGFR inhibitor erlotinib.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	121-131	insulin receptor	Homo sapiens	153-157
27422524-6	2016	Furthermore, beating-rate in Cor.4U( ) human cardiomyocytes, glucose uptake in HL-1 cells, and prevention from H2O2 induced caspase 3/7 activation in cardiac cells overexpressing the human insulin receptor (H9c2-E2) were analysed.	Glucose	61-68	insulin receptor	Homo sapiens	189-205
27422524-6	2016	Furthermore, beating-rate in Cor.4U( ) human cardiomyocytes, glucose uptake in HL-1 cells, and prevention from H2O2 induced caspase 3/7 activation in cardiac cells overexpressing the human insulin receptor (H9c2-E2) were analysed.	Hydrogen Peroxide	111-115	insulin receptor	Homo sapiens	189-205
27346353-5	2016	Only glycogen synthesis was impaired by both loss of insulin receptor and mTORC1 activation.	Glycogen	5-13	insulin receptor	Homo sapiens	53-69
27178332-7	2016	The selective estrogen receptor degrader, fulvestrant, significantly reduced the anchorage-independent growth of ESR1 mutant-expressing cells, while combination treatments with the mTOR inhibitor everolimus, or an inhibitor blocking IGF1R, and the insulin receptor significantly enhanced anti-proliferative responses.	Fulvestrant	42-53	insulin receptor	Homo sapiens	248-264
26760116-0	2016	Low Oxygen Tension Modulates the Insulin-Like Growth Factor-1 or -2 Signaling via Both Insulin-Like Growth Factor-1 Receptor and Insulin Receptor to Maintain Stem Cell Identity in Placental Mesenchymal Stem Cells.	Oxygen	4-10	insulin receptor	Homo sapiens	129-145
27026683-8	2016	BIL exhibited reduced binding affinity and functional potency as compared with insulin lispro and demonstrated greater selectivity for the human insulin receptor (hIR) as compared with the human insulin-like growth factor 1 receptor.	basal insulin peglispro	0-3	insulin receptor	Homo sapiens	145-161
27200287-6	2016	In June 2009, she was recruited onto the Phase I OSI-906-103 trial of EGFR inhibitor erlotinib with linsitinib, a novel inhibitor of IGF-1R/insulin receptor (INSR).	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	100-110	insulin receptor	Homo sapiens	133-156
26850678-0	2016	Preclinical and first-in-human phase I studies of KW-2450, an oral tyrosine kinase inhibitor with insulin-like growth factor receptor-1/insulin receptor selectivity.	KW-2450	50-57	insulin receptor	Homo sapiens	136-152
26850678-2	2016	We summarize preclinical studies and the first-in-human study of KW-2450, an oral tyrosine kinase inhibitor with IGF-1R and insulin receptor (IR) inhibitory activity.	KW-2450	65-72	insulin receptor	Homo sapiens	124-140
26850678-2	2016	We summarize preclinical studies and the first-in-human study of KW-2450, an oral tyrosine kinase inhibitor with IGF-1R and insulin receptor (IR) inhibitory activity.	KW-2450	65-72	insulin receptor	Homo sapiens	142-144
27107134-2	2016	Activation of dopamine receptor inhibits sodium reabsorption, whereas activation of insulin receptor increases sodium reabsorption in RPTs, and hyperinsulinemic animals and patients have defective renal dopaminergic system.	Sodium	111-117	insulin receptor	Homo sapiens	84-100
26721804-3	2016	To investigate the possible mechanism of this signaling defect at genetic level, single-nucleotide polymorphism (SNP) [His 1085 C/T] at the exon 17 of insulin receptor gene (INSR) was studied in this pilot study.	Histidine	119-122	insulin receptor	Homo sapiens	151-167
26721804-3	2016	To investigate the possible mechanism of this signaling defect at genetic level, single-nucleotide polymorphism (SNP) [His 1085 C/T] at the exon 17 of insulin receptor gene (INSR) was studied in this pilot study.	Histidine	119-122	insulin receptor	Homo sapiens	174-178
26561558-9	2016	Blockade of the InsR/IGF1R pathway synergistically improved sensitivity to gefitinib or dacomitinib.	Gefitinib	75-84	insulin receptor	Homo sapiens	16-20
26561558-9	2016	Blockade of the InsR/IGF1R pathway synergistically improved sensitivity to gefitinib or dacomitinib.	dacomitinib	88-99	insulin receptor	Homo sapiens	16-20
26561558-12	2016	A combination of gefitinib and OSI-906, a dual InsR/IGF1R inhibitor, was more effective than either agent alone to treat subcutaneous glioblastoma xenograft tumors.	Gefitinib	17-26	insulin receptor	Homo sapiens	47-51
26561558-12	2016	A combination of gefitinib and OSI-906, a dual InsR/IGF1R inhibitor, was more effective than either agent alone to treat subcutaneous glioblastoma xenograft tumors.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	31-38	insulin receptor	Homo sapiens	47-51
26485752-2	2016	In skeletal muscle, binding of the insulin to insulin receptor (IR) initiates a signaling cascade that results in the translocation of the insulin-sensitive glucose transporter protein 4 (GLUT4) to the plasma membrane which leads to facilitated diffusion of glucose into the cell.	Glucose	157-164	insulin receptor	Homo sapiens	46-62
26485752-2	2016	In skeletal muscle, binding of the insulin to insulin receptor (IR) initiates a signaling cascade that results in the translocation of the insulin-sensitive glucose transporter protein 4 (GLUT4) to the plasma membrane which leads to facilitated diffusion of glucose into the cell.	Glucose	157-164	insulin receptor	Homo sapiens	64-66
26967923-5	2016	Taken together, anthocyanins, predominantly delphinidin-3-arabinoside, from fermented berry beverages have the potential to modulate DPP-IV and its substrate GLP-1, to increase insulin secretion, and to upregulate expression of mRNA of insulin-receptor associated genes and proteins in pancreatic beta-cells.	Anthocyanins	16-28	insulin receptor	Homo sapiens	236-252
26967923-5	2016	Taken together, anthocyanins, predominantly delphinidin-3-arabinoside, from fermented berry beverages have the potential to modulate DPP-IV and its substrate GLP-1, to increase insulin secretion, and to upregulate expression of mRNA of insulin-receptor associated genes and proteins in pancreatic beta-cells.	delphinidin-3-arabinoside	44-69	insulin receptor	Homo sapiens	236-252
26715336-5	2016	In vitro assays of the isotope labeled [(1-(13) C=(18) O)Phe(B24) ] human insulin showed that it had full insulin receptor binding activity.	Phenylalanine	57-60	insulin receptor	Homo sapiens	106-122
26760116-9	2016	This IGF/low oxygen tension-mediated proliferation was receptor dependent because neutralization of the IGF-1R inhibited PMSC proliferation in the presence of IGF-1 and the IR in presence of IGF-2.	Oxygen	13-19	insulin receptor	Homo sapiens	173-175
26760116-11	2016	We conclude that low-oxygen tension can modify the IGF-1 or IGF-2 signaling via the IGF-1R and IR in PMSCs.	Oxygen	21-27	insulin receptor	Homo sapiens	95-97
26888756-5	2016	Efficient knockdown of either Insr or Irs1/2 was achieved by conditional shRNA expression, severely attenuating insulin-stimulated AKT phosphorylation and glucose uptake.	Glucose	155-162	insulin receptor	Homo sapiens	30-34
26934053-8	2016	Indeed, we found reduced levels of insulin receptor, PI3K, AKT, all important molecules in insulin signaling and glucose uptake by cells.	Glucose	113-120	insulin receptor	Homo sapiens	35-51
27172362-0	2016	Glucosylceramide synthase inhibitors D-PDMP and D-EtDO-P4 decrease the GM3 ganglioside level, differ in their effects on insulin receptor autophosphorylation but increase Akt1 kinase phosphorylation in human hepatoma HepG2 cells.	3',4'-ethylenedioxyphenyl-2-palmitoylamino-3-pyrrolidino-1-propanol	48-57	insulin receptor	Homo sapiens	121-137
27172362-2	2016	It was shown for caveolin-rich adipocytes, that GM3 ganglioside binds to insulin receptor (IR), dissociates its complex with caveolin, and thus lowers IR autophosphorylation following insulin treatment.	G(M3) Ganglioside	48-63	insulin receptor	Homo sapiens	73-89
27172362-2	2016	It was shown for caveolin-rich adipocytes, that GM3 ganglioside binds to insulin receptor (IR), dissociates its complex with caveolin, and thus lowers IR autophosphorylation following insulin treatment.	G(M3) Ganglioside	48-63	insulin receptor	Homo sapiens	91-93
27172362-2	2016	It was shown for caveolin-rich adipocytes, that GM3 ganglioside binds to insulin receptor (IR), dissociates its complex with caveolin, and thus lowers IR autophosphorylation following insulin treatment.	G(M3) Ganglioside	48-63	insulin receptor	Homo sapiens	151-153
27172362-6	2016	The reduction of GM3 obtained with d-PDMP was accompanied by a 185.1% (153.5-423.8%) significant increase in the level of IR autophosphorylation following cell stimulation with 100 nM insulin.	gm3	17-20	insulin receptor	Homo sapiens	122-124
27172362-6	2016	The reduction of GM3 obtained with d-PDMP was accompanied by a 185.1% (153.5-423.8%) significant increase in the level of IR autophosphorylation following cell stimulation with 100 nM insulin.	d-pdmp	35-41	insulin receptor	Homo sapiens	122-124
27172362-7	2016	The effect of d-EtDO-P4 on IR autophosphorylation was smaller amounting to an increase by 134.8% (111.3-167.8%) of the control level and statistically non-significant.	3',4'-ethylenedioxyphenyl-2-palmitoylamino-3-pyrrolidino-1-propanol	14-23	insulin receptor	Homo sapiens	27-29
27172362-11	2016	We assume that glycosphingolipid depletion in HepG2 cells may affect not only IR autophosphorylation but also, independently, the phosphorylation of Akt1, by modifying the membrane microenvironment of this kinase.	Glycosphingolipids	15-32	insulin receptor	Homo sapiens	78-80
26584640-5	2016	Rapamycin induces the tyrosine phosphorylation and activation of IGF-IR/InsR, which is largely dependent on rictor and mTOR.	Tyrosine	22-30	insulin receptor	Homo sapiens	72-76
26467793-2	2016	In insulin-targeted cells, such as hepatocytes, proper glucose utilization requires an elaborate interplay between the insulin receptor, the glucose transporter, and mitochondria that involves the participation of actin microfilaments and microtubules.	Glucose	55-62	insulin receptor	Homo sapiens	119-135
26524290-8	2016	RESULTS: We identified a haplotype in INSR that may contribute to differential topiramate-induced weight loss.	Topiramate	79-89	insulin receptor	Homo sapiens	38-42
26524290-12	2016	CONCLUSION: According to our preliminary findings, genetic variation in the INSR and HNF1A genes may differentially affect weight loss in obese individuals treated with topiramate and genes related to insulin action are implicated in modulating topiramate response.	Topiramate	169-179	insulin receptor	Homo sapiens	76-80
26524290-12	2016	CONCLUSION: According to our preliminary findings, genetic variation in the INSR and HNF1A genes may differentially affect weight loss in obese individuals treated with topiramate and genes related to insulin action are implicated in modulating topiramate response.	Topiramate	245-255	insulin receptor	Homo sapiens	76-80
27397605-0	2016	Molecular Remodeling of the Insulin Receptor Pathway by Thiazolidinediones in Type 2 Diabetes Mellitus: A Brief Review.	Thiazolidinediones	56-74	insulin receptor	Homo sapiens	28-44
27633039-3	2016	Metformin also increases the affinity of the insulin receptor, reduces high insulin levels and improves insulin resistance.	Metformin	0-9	insulin receptor	Homo sapiens	45-61
26696633-6	2016	Moreover, insulin receptor autophosphorylation is dependent on intracellular Mg(2+) concentrations, making Mg(2+) a direct factor in the development of insulin resistance.	magnesium ion	77-83	insulin receptor	Homo sapiens	10-26
26696633-6	2016	Moreover, insulin receptor autophosphorylation is dependent on intracellular Mg(2+) concentrations, making Mg(2+) a direct factor in the development of insulin resistance.	magnesium ion	107-113	insulin receptor	Homo sapiens	10-26
27397605-7	2016	The TZD"s are not only PPARgamma agonists, but substantial insulin sensitizing activity is observed through its direct and indirect targets of the insulin receptor pathway, which contributes to its overall performance.	tzd	4-7	insulin receptor	Homo sapiens	147-163
26569375-5	2015	Several reports have tried to unravel underlying mechanisms concerning the aggregation process taking into account a three aromatic amino acid patch Phe(B24)-Phe(B25)-Tyr(B26) located in the C-terminal part of the B chain, identified as a key site for human insulin-receptor interaction.	Amino Acids, Aromatic	123-142	insulin receptor	Homo sapiens	258-274
26569375-5	2015	Several reports have tried to unravel underlying mechanisms concerning the aggregation process taking into account a three aromatic amino acid patch Phe(B24)-Phe(B25)-Tyr(B26) located in the C-terminal part of the B chain, identified as a key site for human insulin-receptor interaction.	Phenylalanine	149-152	insulin receptor	Homo sapiens	258-274
26569375-5	2015	Several reports have tried to unravel underlying mechanisms concerning the aggregation process taking into account a three aromatic amino acid patch Phe(B24)-Phe(B25)-Tyr(B26) located in the C-terminal part of the B chain, identified as a key site for human insulin-receptor interaction.	Phenylalanine	158-161	insulin receptor	Homo sapiens	258-274
26569375-5	2015	Several reports have tried to unravel underlying mechanisms concerning the aggregation process taking into account a three aromatic amino acid patch Phe(B24)-Phe(B25)-Tyr(B26) located in the C-terminal part of the B chain, identified as a key site for human insulin-receptor interaction.	Tyrosine	167-170	insulin receptor	Homo sapiens	258-274
26438154-0	2015	BI 885578, a Novel IGF1R/INSR Tyrosine Kinase Inhibitor with Pharmacokinetic Properties That Dissociate Antitumor Efficacy and Perturbation of Glucose Homeostasis.	BI 885578	0-9	insulin receptor	Homo sapiens	25-29
26514725-4	2015	By virtue of its ability to directly bind the InsR, IRS1 and PI3K, GIV enhances the InsR-IRS1-Akt-AS160 (RabGAP) signaling cascade and cellular glucose uptake via its GEF function.	Glucose	144-151	insulin receptor	Homo sapiens	46-50
27141540-1	2015	BACKGROUND: Vitamin D and insulin play an important role in susceptibility to polycystic ovary syndrome (PCOS), and therefore vitamin D receptor (VDR), parathyroid hormone (PTH), and insulin receptor (INSR) gene variants might be involved in the pathogenesis of PCOS.	Vitamin D	12-21	insulin receptor	Homo sapiens	201-205
26438154-3	2015	We describe here the profile of the novel compound BI 885578, a potent and selective ATP-competitive IGF1R/INSR tyrosine kinase inhibitor distinguished by rapid intestinal absorption and a short in vivo half-life as a result of rapid metabolic clearance.	BI 885578	51-60	insulin receptor	Homo sapiens	107-111
26438154-3	2015	We describe here the profile of the novel compound BI 885578, a potent and selective ATP-competitive IGF1R/INSR tyrosine kinase inhibitor distinguished by rapid intestinal absorption and a short in vivo half-life as a result of rapid metabolic clearance.	Adenosine Triphosphate	85-88	insulin receptor	Homo sapiens	107-111
26438154-8	2015	We propose that the remarkable therapeutic window observed for BI 885578 is achieved by virtue of the distinctive pharmacokinetic properties of the compound, capitalizing on the physiologic mechanisms of glucose homeostasis and differential levels of IGF1R and INSR expression in tumors and normal tissues.	BI 885578	63-72	insulin receptor	Homo sapiens	261-265
26378251-4	2015	By virtue of its ability to directly bind InsR, IRS1, and phosphoinositide 3-kinase, GIV serves as a key hub in the immediate postreceptor level, which coordinately enhances the metabolic insulin response and glucose uptake in myotubes via its GEF function.	Glucose	209-216	insulin receptor	Homo sapiens	42-46
25476247-0	2015	Resveratrol enhances splicing of insulin receptor exon 11 in myotonic dystrophy type 1 fibroblasts.	Resveratrol	0-11	insulin receptor	Homo sapiens	33-49
26405719-3	2015	Here, we demonstrated, for the first time, the single molecule interaction between insulin and insulin receptor on erythrocytes from a healthy volunteer and a T1-DKA patient using high sensitivity atomic force microscopy (AFM) in PBS solution.	Lead	230-233	insulin receptor	Homo sapiens	95-111
26118462-0	2015	Reduced insulin-receptor mediated modulation of striatal dopamine release by basal insulin as a possible contributing factor to hyperdopaminergia in schizophrenia.	Dopamine	57-65	insulin receptor	Homo sapiens	8-24
26118462-9	2015	Collectively, these data suggest that midbrain insulin receptor functioning may be abnormal in persons with schizophrenia, resulting in reduced insulin-mediated regulation of dopamine transmission in the striatum.	Dopamine	175-183	insulin receptor	Homo sapiens	47-63
26118462-11	2015	We hypothesize that, (i) insulin receptor expression and/or function is reduced in midbrain dopamine neurons in persons with schizophrenia, (ii) basal insulin should reduce dopaminergic transmission in the striatum via these receptors, and (iii) this modulation of dopaminergic transmission by basal insulin is reduced in the brains of persons with schizophrenia.	Dopamine	92-100	insulin receptor	Homo sapiens	25-41
25623440-3	2015	Our analysis revealed that, in response to AP treatment, constructed networks were enriched for different biological processes in patients without EPS (ubiquitination, protein folding and adenosine triphosphate (ATP) metabolism) compared with those presenting EPS (insulin receptor signaling, lipid modification, regulation of autophagy and immune response).	Adenosine Triphosphate	188-210	insulin receptor	Homo sapiens	265-281
25623440-3	2015	Our analysis revealed that, in response to AP treatment, constructed networks were enriched for different biological processes in patients without EPS (ubiquitination, protein folding and adenosine triphosphate (ATP) metabolism) compared with those presenting EPS (insulin receptor signaling, lipid modification, regulation of autophagy and immune response).	Adenosine Triphosphate	212-215	insulin receptor	Homo sapiens	265-281
26276395-2	2015	We previously designed oligopeptides containing the amino-acid sequences surrounding the autophosphorylation sites of the insulin receptor and found that two of them, namely, Ac-DIYET-NH2 and Ac-DYYRK-NH2, suppressed phosphorylation of purified insulin receptors in a non-ATP-competitive manner, whereas Ac-NIYQT-NH2 and Ac-NYYRK-NH2 suppressed in an ATP-competitive manner.	Adenosine Triphosphate	272-275	insulin receptor	Homo sapiens	122-138
26276395-2	2015	We previously designed oligopeptides containing the amino-acid sequences surrounding the autophosphorylation sites of the insulin receptor and found that two of them, namely, Ac-DIYET-NH2 and Ac-DYYRK-NH2, suppressed phosphorylation of purified insulin receptors in a non-ATP-competitive manner, whereas Ac-NIYQT-NH2 and Ac-NYYRK-NH2 suppressed in an ATP-competitive manner.	Adenosine Triphosphate	351-354	insulin receptor	Homo sapiens	122-138
26372847-8	2015	Although in both treatment groups, metformin decreased plasma levels of fasting and post-challenge plasma glucose and improved insulin receptor sensitivity, this effect was more prominent in patients receiving cabergoline.	Metformin	35-44	insulin receptor	Homo sapiens	127-143
26372847-8	2015	Although in both treatment groups, metformin decreased plasma levels of fasting and post-challenge plasma glucose and improved insulin receptor sensitivity, this effect was more prominent in patients receiving cabergoline.	Cabergoline	210-221	insulin receptor	Homo sapiens	127-143
26063811-1	2015	The autophosphorylation of specific tyrosine residues occurs in the cytoplasmic region of the insulin receptor (IR) upon insulin binding, and this in turn initiates signal transduction.	Tyrosine	36-44	insulin receptor	Homo sapiens	94-115
26063811-4	2015	The co-expression of R3 RPTPs with the IR in HEK293T cells suppressed insulin-induced tyrosine phosphorylation of the IR.	Tyrosine	86-94	insulin receptor	Homo sapiens	39-41
26063811-4	2015	The co-expression of R3 RPTPs with the IR in HEK293T cells suppressed insulin-induced tyrosine phosphorylation of the IR.	Tyrosine	86-94	insulin receptor	Homo sapiens	118-120
25808283-2	2015	We have previously characterized an allosteric monoclonal antibody to the human insulin receptor (IR), XMetA, that activated metabolic signaling leading to enhanced glucose transport in cultured cells, and chronically reduced fasting blood glucose levels in mouse models of diabetes mellitus.	Glucose	165-172	insulin receptor	Homo sapiens	80-96
25808283-2	2015	We have previously characterized an allosteric monoclonal antibody to the human insulin receptor (IR), XMetA, that activated metabolic signaling leading to enhanced glucose transport in cultured cells, and chronically reduced fasting blood glucose levels in mouse models of diabetes mellitus.	Glucose	165-172	insulin receptor	Homo sapiens	98-100
25808283-2	2015	We have previously characterized an allosteric monoclonal antibody to the human insulin receptor (IR), XMetA, that activated metabolic signaling leading to enhanced glucose transport in cultured cells, and chronically reduced fasting blood glucose levels in mouse models of diabetes mellitus.	Glucose	240-247	insulin receptor	Homo sapiens	80-96
25808283-2	2015	We have previously characterized an allosteric monoclonal antibody to the human insulin receptor (IR), XMetA, that activated metabolic signaling leading to enhanced glucose transport in cultured cells, and chronically reduced fasting blood glucose levels in mouse models of diabetes mellitus.	Glucose	240-247	insulin receptor	Homo sapiens	98-100
25476247-3	2015	Consequently, the exon 11-deleted IR isoform that is less sensitive to insulin is predominantly produced, leading to glucose intolerance in DM1.	Glucose	117-124	insulin receptor	Homo sapiens	34-36
25476247-6	2015	RESULTS: We revealed that resveratrol (RES) enhanced the percentage of exon 11-containing IR mRNA among the total IR mRNA in HeLa cells.	Resveratrol	26-37	insulin receptor	Homo sapiens	90-92
25476247-6	2015	RESULTS: We revealed that resveratrol (RES) enhanced the percentage of exon 11-containing IR mRNA among the total IR mRNA in HeLa cells.	Resveratrol	26-37	insulin receptor	Homo sapiens	114-116
25476247-6	2015	RESULTS: We revealed that resveratrol (RES) enhanced the percentage of exon 11-containing IR mRNA among the total IR mRNA in HeLa cells.	Resveratrol	0-3	insulin receptor	Homo sapiens	90-92
26021696-0	2015	Oxidovanadium(IV) sulfate-induced glucose uptake in HepG2 cells through IR/Akt pathway and hydroxyl radicals.	oxidovanadium	0-13	insulin receptor	Homo sapiens	72-74
26021696-0	2015	Oxidovanadium(IV) sulfate-induced glucose uptake in HepG2 cells through IR/Akt pathway and hydroxyl radicals.	Sulfates	18-25	insulin receptor	Homo sapiens	72-74
26021696-0	2015	Oxidovanadium(IV) sulfate-induced glucose uptake in HepG2 cells through IR/Akt pathway and hydroxyl radicals.	Glucose	34-41	insulin receptor	Homo sapiens	72-74
26021696-4	2015	Exposure of cells to VOSO4 (5-50 muM) resulted in an increase in glucose uptake, insulin receptor (IR) and protein kinase B (Akt) phosphorylation and intracellular ROS generation.	vanadyl sulfate	21-26	insulin receptor	Homo sapiens	81-102
26021696-5	2015	Using Western blot, we found that catalase and sodium formate, but not superoxide dismutase, prevented the increase of hydroxyl radical ( OH) generation and significantly decreased VOSO4-induced IR and Akt phosphorylation.	formic acid	47-61	insulin receptor	Homo sapiens	195-197
26021696-5	2015	Using Western blot, we found that catalase and sodium formate, but not superoxide dismutase, prevented the increase of hydroxyl radical ( OH) generation and significantly decreased VOSO4-induced IR and Akt phosphorylation.	vanadyl sulfate	181-186	insulin receptor	Homo sapiens	195-197
26021696-6	2015	These results suggest that VOSO4-induced  OH radical, which is a signaling species, promotes glucose uptake via the IR/Akt signaling pathway.	vanadyl sulfate	27-32	insulin receptor	Homo sapiens	116-118
26021696-6	2015	These results suggest that VOSO4-induced  OH radical, which is a signaling species, promotes glucose uptake via the IR/Akt signaling pathway.	oh radical	42-52	insulin receptor	Homo sapiens	116-118
26021696-6	2015	These results suggest that VOSO4-induced  OH radical, which is a signaling species, promotes glucose uptake via the IR/Akt signaling pathway.	Glucose	93-100	insulin receptor	Homo sapiens	116-118
25697343-6	2015	In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types.	Insulin Glargine	28-36	insulin receptor	Homo sapiens	80-96
25864925-0	2015	Tumor vessel up-regulation of INSR revealed by single-cell expression analysis of the tyrosine kinome and phosphatome in human cancers.	Tyrosine	86-94	insulin receptor	Homo sapiens	30-34
26345813-2	2015	Interaction of insulin with the insulin receptor (IR) leads to both its auto-phosphorylation and phosphorylation of tyrosine residues on the IR substrate (IRS) proteins, initiating the activation of intracellular signaling cascades.	Tyrosine	116-124	insulin receptor	Homo sapiens	32-48
26345813-2	2015	Interaction of insulin with the insulin receptor (IR) leads to both its auto-phosphorylation and phosphorylation of tyrosine residues on the IR substrate (IRS) proteins, initiating the activation of intracellular signaling cascades.	Tyrosine	116-124	insulin receptor	Homo sapiens	50-52
26161852-3	2015	Synthesis and release of the neurotransmitter acetylcholine (ACh) is closely linked to the activity of the high-affinity choline transporter protein (CHT), but the impact of insulin receptor signaling and neuronal insulin resistance on these aspects of cholinergic function are unknown.	Acetylcholine	46-59	insulin receptor	Homo sapiens	174-190
26161852-3	2015	Synthesis and release of the neurotransmitter acetylcholine (ACh) is closely linked to the activity of the high-affinity choline transporter protein (CHT), but the impact of insulin receptor signaling and neuronal insulin resistance on these aspects of cholinergic function are unknown.	Acetylcholine	61-64	insulin receptor	Homo sapiens	174-190
25697343-6	2015	In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types.	Insulin Glargine	28-36	insulin receptor	Homo sapiens	98-102
25697343-6	2015	In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types.	Insulin Detemir	41-48	insulin receptor	Homo sapiens	80-96
25697343-6	2015	In addition, we showed that glargine and detemir induced dual activation of the insulin receptor (INSR) and IGF1R in both cell types.	Insulin Detemir	41-48	insulin receptor	Homo sapiens	98-102
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	74-77	insulin receptor	Homo sapiens	26-42
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	74-77	insulin receptor	Homo sapiens	44-46
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	74-77	insulin receptor	Homo sapiens	190-192
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	74-77	insulin receptor	Homo sapiens	190-192
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	85-88	insulin receptor	Homo sapiens	26-42
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	85-88	insulin receptor	Homo sapiens	44-46
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	85-88	insulin receptor	Homo sapiens	190-192
25667086-1	2015	Here, we demonstrate that insulin receptor (IR) tyrosine kinase catalyzes Tyr-19 and Tyr-27 phosphorylation of caveolin-2 (cav-2), leading to stimulation of signaling proteins downstream of IR, and that the catalysis is dependent on fatty acylation status of cav-2, promoting its interaction with IR.	Tyrosine	85-88	insulin receptor	Homo sapiens	190-192
25667086-4	2015	IR interacts with the C-terminal domain of cav-2 containing the cysteines for palmitoylation.	Cysteine	64-73	insulin receptor	Homo sapiens	0-2
25667086-6	2015	Insulin receptor substrate-1 (IRS-1) is recruited to interact with the IR-catalyzed phospho-tyrosine cav-2, which facilitates IRS-1 association with and activation by IR to initiate IRS-1-mediated downstream signaling.	Tyrosine	92-100	insulin receptor	Homo sapiens	30-32
25667086-6	2015	Insulin receptor substrate-1 (IRS-1) is recruited to interact with the IR-catalyzed phospho-tyrosine cav-2, which facilitates IRS-1 association with and activation by IR to initiate IRS-1-mediated downstream signaling.	Tyrosine	92-100	insulin receptor	Homo sapiens	71-73
25627174-8	2015	In addition, our analyses using fluorescent recovery after photobleaching revealed that kinases such as c-Jun N-terminal kinase and IkappaB kinase beta, which phosphorylate serine/threonine residues of IRS and contribute to insulin resistance, altered the interaction kinetics of IRS with insulin receptor.	Serine	173-179	insulin receptor	Homo sapiens	289-305
25927028-8	2015	The frequencies of PmlI (rs1799817) SNPs in the INSR gene were 4(8%), 29(58%), and 17(34%) in cases, also 5(10.64%), 29(61.7%), and 13(27.66%) in controls regarding TT, TC, and CC genotypes, respectively.	Technetium	169-171	insulin receptor	Homo sapiens	48-52
26085948-4	2015	An analysis using the AcalPred program showed that insulin receptor family proteins are divided into two classes: one class with the optimal working pH in the acidic medium (virtually all insulin receptor and insulin-like growth factor receptor orthologs, except for the IGF-IR ortholog from Xenopus laevis) and the second class with the optimal working pH in the alkaline medium (all IRR orthologs).	alkaline	364-372	insulin receptor	Homo sapiens	51-67
25613982-6	2015	The metabolic selectivity of partial IR agonists like XMetA, if recapitulated in vivo, may be a desirable feature of therapeutic agents designed to regulate blood glucose levels while minimizing undesirable outcomes of excessive IR mitogenic activation.	Glucose	163-170	insulin receptor	Homo sapiens	37-39
25795408-2	2015	Linsitinib (OSI-906) is a potent, oral small molecule inhibitor of both IGF-1R and the insulin receptor, which has shown acceptable tolerability and preliminary evidence of anti-tumour activity.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	0-10	insulin receptor	Homo sapiens	87-103
26045896-10	2015	Moreover, we demonstrate that metformin induces GLUT4 expression and inhibits AR expression and blocks insulin receptor/PI3K/Akt/mTOR signaling in the same hyperplasia human tissues.	Metformin	30-39	insulin receptor	Homo sapiens	103-119
25627174-8	2015	In addition, our analyses using fluorescent recovery after photobleaching revealed that kinases such as c-Jun N-terminal kinase and IkappaB kinase beta, which phosphorylate serine/threonine residues of IRS and contribute to insulin resistance, altered the interaction kinetics of IRS with insulin receptor.	Threonine	180-189	insulin receptor	Homo sapiens	289-305
25730798-4	2015	It can strengthened the level of tyrosine phosphorylation of insulin receptor (IR) and extracellular signal-regulated protein kinase (ERK) in HepG2 cells, and then activated the insulin signaling pathway through inhibiting the protein phosphorylation of SHP-1.	Tyrosine	33-41	insulin receptor	Homo sapiens	61-77
25730798-4	2015	It can strengthened the level of tyrosine phosphorylation of insulin receptor (IR) and extracellular signal-regulated protein kinase (ERK) in HepG2 cells, and then activated the insulin signaling pathway through inhibiting the protein phosphorylation of SHP-1.	Tyrosine	33-41	insulin receptor	Homo sapiens	79-81
25848166-1	2015	Normal blood glucose level depends on the availability of insulin and its ability to bind insulin receptor (IR) that regulates the downstream signaling pathway.	Glucose	13-20	insulin receptor	Homo sapiens	90-106
25848166-1	2015	Normal blood glucose level depends on the availability of insulin and its ability to bind insulin receptor (IR) that regulates the downstream signaling pathway.	Glucose	13-20	insulin receptor	Homo sapiens	108-110
26312838-10	2015	However, area under the curve for testosterone was higher in women with INSR mutations after DHEA than in women with PCOS and controls (874 2 [SE 242] vs 425 [136] and 375 2 [109], p&lt;0 001 for both).	Testosterone	34-46	insulin receptor	Homo sapiens	72-76
26312838-10	2015	However, area under the curve for testosterone was higher in women with INSR mutations after DHEA than in women with PCOS and controls (874 2 [SE 242] vs 425 [136] and 375 2 [109], p&lt;0 001 for both).	Dehydroepiandrosterone	93-97	insulin receptor	Homo sapiens	72-76
25212606-1	2015	PURPOSE: OSI-906 is a potent inhibitor of insulin-like growth factor-1 receptor (IGF1R) and insulin receptor (IR).	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	9-16	insulin receptor	Homo sapiens	92-108
25212606-1	2015	PURPOSE: OSI-906 is a potent inhibitor of insulin-like growth factor-1 receptor (IGF1R) and insulin receptor (IR).	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	9-16	insulin receptor	Homo sapiens	110-112
25212606-11	2015	Pharmacodynamic effects on IGF1R and IR phosphorylation were levels observed and correlated with plasma concentrations of OSI-906.	silicon monoxide	122-125	insulin receptor	Homo sapiens	37-39
25670076-2	2015	In this issue of Cancer Cell, Vidal and colleagues identify increased GATA2 and its AR-independent transactivation of IGF2 as a mechanism that can mediate taxane resistance through activation of IGF1/insulin receptor signaling.	taxane	155-161	insulin receptor	Homo sapiens	200-216
25849721-0	2015	Changes in insulin receptor signaling underlie neoadjuvant metformin administration in breast cancer: a prospective window of opportunity neoadjuvant study.	Metformin	59-68	insulin receptor	Homo sapiens	11-27
25687571-2	2015	We performed a bioinformatic screen of Golgi/endosome hepatic protein fractions and found that ATIC, which is a rate-limiting enzyme in the de novo purine biosynthesis pathway, and PTPLAD1 are associated with insulin receptor (IR) internalization.	purine	148-154	insulin receptor	Homo sapiens	209-225
25687571-2	2015	We performed a bioinformatic screen of Golgi/endosome hepatic protein fractions and found that ATIC, which is a rate-limiting enzyme in the de novo purine biosynthesis pathway, and PTPLAD1 are associated with insulin receptor (IR) internalization.	purine	148-154	insulin receptor	Homo sapiens	227-229
25687571-6	2015	Using an in vitro reconstitution system and siRNA-mediated partial knockdown of ATIC and PTPLAD1 in HEK293 cells, we show that both ATIC and PTPLAD1 affect IR tyrosine phosphorylation and endocytosis.	Tyrosine	159-167	insulin receptor	Homo sapiens	156-158
25687571-9	2015	These results suggest the presence of a signaling mechanism that senses adenylate synthesis, ATP levels, and IR activation states and that acts in regulating IR autophosphorylation and endocytosis.	Adenosine Triphosphate	93-96	insulin receptor	Homo sapiens	158-160
25693802-4	2015	Motif analysis using the NetworKIN algorithm revealed that the activity of tyrosine phosphorylation kinases insulin growth factor 1 receptor (IGF1R)/insulin receptor is significantly enriched among the up-regulated phosphorylation substrates during capacitation.	Tyrosine	75-83	insulin receptor	Homo sapiens	149-165
25458098-1	2015	PURPOSE: Insulin/insulin receptor (INSR) signaling plays diverse roles in the central nervous system, including regulation of blood glucose, synaptic plasticity, dendritic growth, modulation of electrophysiological activity, proliferation of astrocytes and neuronal apoptosis.	Glucose	132-139	insulin receptor	Homo sapiens	9-33
25484249-5	2015	Studies have indicated that insulin receptor (IR) and insulin receptor substrate 1 (IRS1) are essential factors involved in the regulation of blood glucose levels.	Blood Glucose	142-155	insulin receptor	Homo sapiens	28-44
25484249-5	2015	Studies have indicated that insulin receptor (IR) and insulin receptor substrate 1 (IRS1) are essential factors involved in the regulation of blood glucose levels.	Blood Glucose	142-155	insulin receptor	Homo sapiens	46-48
25342129-2	2015	Brain tissue studies suggested that insulin resistance is caused by low insulin receptor signaling attributable to its abnormal association with more phospho (P)-serine-type 1 insulin receptor substrate (IRS-1) and less P-tyrosine-IRS-1.	Serine	162-168	insulin receptor	Homo sapiens	72-88
25342129-2	2015	Brain tissue studies suggested that insulin resistance is caused by low insulin receptor signaling attributable to its abnormal association with more phospho (P)-serine-type 1 insulin receptor substrate (IRS-1) and less P-tyrosine-IRS-1.	Tyrosine	222-230	insulin receptor	Homo sapiens	72-88
25458098-1	2015	PURPOSE: Insulin/insulin receptor (INSR) signaling plays diverse roles in the central nervous system, including regulation of blood glucose, synaptic plasticity, dendritic growth, modulation of electrophysiological activity, proliferation of astrocytes and neuronal apoptosis.	Glucose	132-139	insulin receptor	Homo sapiens	35-39
25404012-4	2015	Top canonical pathways that were inhibited upon erlotinib treatment in sensitive cells, but not in the resistant cells include EGFR, insulin receptor, hepatocyte growth factor, mitogen-activated protein kinase, mechanistic target of rapamycin, ribosomal protein S6 kinase beta 1, and Janus kinase/signal transducer and activator of transcription signaling.	Erlotinib Hydrochloride	48-57	insulin receptor	Homo sapiens	133-149
25604425-5	2015	The hybrid receptor specificity is obtained from a combination of two specific antibodies for IGF1R and for an IR tyrosine phosphorylation site.	Tyrosine	114-122	insulin receptor	Homo sapiens	111-113
25281561-8	2015	GO and pathway analyses showed that six fatty acid beta-oxidation-related proteins (HADHB, ECHS1, ACSL4, ACADM, ACSL1 and HADH) were up-regulated in FLL cells, which was consistent with the results obtained from real-time PCR, Western blot and MS, while INSR pathway-related proteins (INSR, IRS1, PI3K and PKC) was low in the ligament of AS as compared with that in healthy controls.	Fatty Acids	40-50	insulin receptor	Homo sapiens	254-258
25281561-8	2015	GO and pathway analyses showed that six fatty acid beta-oxidation-related proteins (HADHB, ECHS1, ACSL4, ACADM, ACSL1 and HADH) were up-regulated in FLL cells, which was consistent with the results obtained from real-time PCR, Western blot and MS, while INSR pathway-related proteins (INSR, IRS1, PI3K and PKC) was low in the ligament of AS as compared with that in healthy controls.	Fatty Acids	40-50	insulin receptor	Homo sapiens	285-289
25281561-9	2015	CONCLUSION: The lower body fat level in AS maybe due to up-regulation of fatty acid beta-oxidation-related enzymes regulated by INSR/PI3K/PKC pathway.	Fatty Acids	73-83	insulin receptor	Homo sapiens	128-132
26491440-6	2015	In males, testosterone works via androgen receptors to increase insulin receptor expression and glycogen synthesis, decrease glucose uptake and lipogenesis, and promote cholesterol storage in the liver.	Testosterone	10-22	insulin receptor	Homo sapiens	64-80
24786779-9	2014	An increased expression of insulin receptor, GLUT-4 and an increased activation of p70S6K1 were observed during treatment with lercanidipine + enalapril but not with lercanidipine + hydrochlorothiazide.	Enalapril	143-152	insulin receptor	Homo sapiens	27-43
25267499-0	2014	The tyrphostin NT157 suppresses insulin receptor substrates and augments therapeutic response of prostate cancer.	Tyrphostins	4-14	insulin receptor	Homo sapiens	32-48
25004245-6	2014	Although phosphorylation at Tyr1146 of the insulin receptor was inhibited by tacrolimus, the phosphorylation and/or protein levels of the insulin signaling proteins IRS1/2, p85-PI3K, PKB, AS160, and mTORC1, as well as GLUT4 and GLUT1, were unchanged by CsA or tacrolimus.	Tacrolimus	77-87	insulin receptor	Homo sapiens	43-59
24786779-9	2014	An increased expression of insulin receptor, GLUT-4 and an increased activation of p70S6K1 were observed during treatment with lercanidipine + enalapril but not with lercanidipine + hydrochlorothiazide.	lercanidipine	127-140	insulin receptor	Homo sapiens	27-43
25241191-1	2014	Although the flavonoid quercetin is known to inhibit activation of insulin receptor signaling, the inhibitory mechanism is largely unknown.	Flavonoids	13-22	insulin receptor	Homo sapiens	67-83
25241191-1	2014	Although the flavonoid quercetin is known to inhibit activation of insulin receptor signaling, the inhibitory mechanism is largely unknown.	Quercetin	23-32	insulin receptor	Homo sapiens	67-83
24277691-12	2014	Moreover, formula-fed children with low expression of SLC27A2, FASN, PPARalpha and INSR presented higher triglyceride levels than subjects with high expression of these genes (77.7 mg dL(-1) vs. 44.8 mg dL(-1) ).	Triglycerides	105-117	insulin receptor	Homo sapiens	83-87
25424739-7	2014	P-DMRs located in INSR and CPT1A have enhancer activity in vitro and differential methylation is associated with birth weight and serum LDL cholesterol.	Cholesterol	140-151	insulin receptor	Homo sapiens	18-22
25240198-3	2014	Furthermore, the ectopic expression of miR-195 suppresses the expression of INSR, thereby impairing the insulin signaling cascade and glycogen synthesis in HepG2 cells.	Glycogen	134-142	insulin receptor	Homo sapiens	76-80
25004245-6	2014	Although phosphorylation at Tyr1146 of the insulin receptor was inhibited by tacrolimus, the phosphorylation and/or protein levels of the insulin signaling proteins IRS1/2, p85-PI3K, PKB, AS160, and mTORC1, as well as GLUT4 and GLUT1, were unchanged by CsA or tacrolimus.	Cyclosporine	253-256	insulin receptor	Homo sapiens	43-59
25004245-6	2014	Although phosphorylation at Tyr1146 of the insulin receptor was inhibited by tacrolimus, the phosphorylation and/or protein levels of the insulin signaling proteins IRS1/2, p85-PI3K, PKB, AS160, and mTORC1, as well as GLUT4 and GLUT1, were unchanged by CsA or tacrolimus.	Tacrolimus	260-270	insulin receptor	Homo sapiens	43-59
25259572-6	2014	Cells chronically exposed to insulin show a diminished the level of IR tyrosine and serine autophosphorylation below that observed after short-term insulin exposure.	Tyrosine	71-79	insulin receptor	Homo sapiens	68-70
24973425-0	2014	Functional genetic approach identifies MET, HER3, IGF1R, INSR pathways as determinants of lapatinib unresponsiveness in HER2-positive gastric cancer.	Lapatinib	90-99	insulin receptor	Homo sapiens	57-61
24973425-9	2014	RESULTS: MET, HER3, insulin-like growth factor (IGF)-1R, and INSR were identified to mediate lapatinib unresponsiveness in HER2+ gastric cancer cells.	Lapatinib	93-102	insulin receptor	Homo sapiens	61-65
24973425-12	2014	CONCLUSIONS: MET, HER3, IGF1R, and INSR pathways activation represent novel mechanism underlying lapatinib unresponsiveness in HER2+ gastric cancer.	Lapatinib	97-106	insulin receptor	Homo sapiens	35-39
25123125-27	2014	The results from these studies demonstrate that the well-established abnormalities in insulin action on glucose uptake and glycogen synthesis are reflected by defects in insulin signaling to these cellular processes in type 2 diabetes, obesity, and PCOS, and as expected also in inherited insulin resistance caused by a mutation in INSR.	Glucose	104-111	insulin receptor	Homo sapiens	332-336
25002580-7	2014	Surprisingly, although [L-Ser(B8)]proinsulin did not fold well under the physiological conditions investigated, once folded the [L-Ser(B8)]proinsulin protein molecule bound to the insulin receptor more effectively than wild-type proinsulin.	Serine	129-134	insulin receptor	Homo sapiens	180-196
25352918-8	2014	Accordingly, aldosterone impairs insulin receptor (IR) signaling by altering the phosphatidylinositol 3-kinase (PI3K)/nitric oxide (NO) pathway and by inducing oxidative stress and crosstalk between the IR and the insulin-like growth factor-1 receptor (IGF-1R).	Nitric Oxide	118-130	insulin receptor	Homo sapiens	33-49
25352918-8	2014	Accordingly, aldosterone impairs insulin receptor (IR) signaling by altering the phosphatidylinositol 3-kinase (PI3K)/nitric oxide (NO) pathway and by inducing oxidative stress and crosstalk between the IR and the insulin-like growth factor-1 receptor (IGF-1R).	Nitric Oxide	118-130	insulin receptor	Homo sapiens	51-53
24703981-1	2014	The hepatic insulin signaling mediated by insulin receptor substrates IRS1 and IRS2 plays a central role in maintaining glucose homeostasis under different physiological conditions.	Glucose	120-127	insulin receptor	Homo sapiens	42-58
24627035-1	2014	OBJECTIVE: To assess the effect of metformin on gene and protein expression of insulin receptor (IR) and IGF-1 (IGF-1R) receptor in human endometrial stromal cells after stimulation with androgen and insulin.	Metformin	35-44	insulin receptor	Homo sapiens	79-95
24627035-1	2014	OBJECTIVE: To assess the effect of metformin on gene and protein expression of insulin receptor (IR) and IGF-1 (IGF-1R) receptor in human endometrial stromal cells after stimulation with androgen and insulin.	Metformin	35-44	insulin receptor	Homo sapiens	97-99
24627035-3	2014	RESULTS: IR gene expression was increased after treatment with insulin (2.9-fold change, p = 0.027) and further after metformin treatment (4.7-fold change, p &lt; 0.001), and in IGF-1R, the group treated with insulin (1.83-fold change) and metformin (1.78-fold change) showed more expression, than control group (p &lt; 0.001).	Metformin	118-127	insulin receptor	Homo sapiens	9-11
24627035-3	2014	RESULTS: IR gene expression was increased after treatment with insulin (2.9-fold change, p = 0.027) and further after metformin treatment (4.7-fold change, p &lt; 0.001), and in IGF-1R, the group treated with insulin (1.83-fold change) and metformin (1.78-fold change) showed more expression, than control group (p &lt; 0.001).	Metformin	240-249	insulin receptor	Homo sapiens	9-11
24627035-4	2014	Similarly, IR protein expression was increased after addition of metformin and insulin (249,869 +- 15,878) in relation to the other groups (p &lt; 0.001).	Metformin	65-74	insulin receptor	Homo sapiens	11-13
24627035-7	2014	CONCLUSION: Metformin in combination with insulin increased IR protein and gene expressions, while it had no influence on the protein expression of IGF-1R in endometrial stromal cells.	Metformin	12-21	insulin receptor	Homo sapiens	60-62
24867955-5	2014	Like insulin-dependent activation, IR-TM requires that IR have a competent ATP-binding site and kinase activation loop.	Adenosine Triphosphate	75-78	insulin receptor	Homo sapiens	35-37
24867955-5	2014	Like insulin-dependent activation, IR-TM requires that IR have a competent ATP-binding site and kinase activation loop.	Adenosine Triphosphate	75-78	insulin receptor	Homo sapiens	55-57
25123125-27	2014	The results from these studies demonstrate that the well-established abnormalities in insulin action on glucose uptake and glycogen synthesis are reflected by defects in insulin signaling to these cellular processes in type 2 diabetes, obesity, and PCOS, and as expected also in inherited insulin resistance caused by a mutation in INSR.	Glycogen	123-131	insulin receptor	Homo sapiens	332-336
24130215-0	2014	Di(2-ethylhexyl)phthalate exposure impairs insulin receptor and glucose transporter 4 gene expression in L6 myotubes.	Diethylhexyl Phthalate	0-25	insulin receptor	Homo sapiens	43-59
25114673-3	2014	OBJECTIVE: To examine whether the exon 17 of INSR gene contributes to genetic susceptibility to PCOS in Iraqi women and its effects on glucose tolerance test and lipid profile.	Glucose	135-142	insulin receptor	Homo sapiens	45-49
25114673-7	2014	RESULTS: The C/T polymorphism at His 1058 in exon 17 of INSR was associated with PCOS (obese and non-obese).	Histidine	33-36	insulin receptor	Homo sapiens	56-60
24568842-0	2014	Human biliverdin reductase-based peptides activate and inhibit glucose uptake through direct interaction with the kinase domain of insulin receptor.	Glucose	63-70	insulin receptor	Homo sapiens	131-147
24535599-8	2014	Grb14-IR binding was also facilitated by replacement of the serines with Ala.	Serine	60-67	insulin receptor	Homo sapiens	6-8
24535599-8	2014	Grb14-IR binding was also facilitated by replacement of the serines with Ala.	Alanine	73-76	insulin receptor	Homo sapiens	6-8
24939305-0	2014	Relationship between tyrosine phosphorylation and protein expression of insulin receptor and insulin resistance in gestational diabetes mellitus.	Tyrosine	21-29	insulin receptor	Homo sapiens	72-88
24939305-1	2014	The relationship between tyrosine phosphorylation (TP) and protein expression of insulin receptor (InsR) and insulin resistance (IR) in patients with gestational diabetes mellitus (GDM) was investigated.	Tyrosine	25-33	insulin receptor	Homo sapiens	81-97
24939305-1	2014	The relationship between tyrosine phosphorylation (TP) and protein expression of insulin receptor (InsR) and insulin resistance (IR) in patients with gestational diabetes mellitus (GDM) was investigated.	Tyrosine	25-33	insulin receptor	Homo sapiens	99-103
24440425-5	2014	The sequence containing residues L962 to Y976 of the TMD of the IR in micelles adopts a well-defined helical structure with a kink formed by glycine and proline residues present at its N-terminus, which might be important for its function.	Glycine	141-148	insulin receptor	Homo sapiens	64-66
24440425-5	2014	The sequence containing residues L962 to Y976 of the TMD of the IR in micelles adopts a well-defined helical structure with a kink formed by glycine and proline residues present at its N-terminus, which might be important for its function.	Proline	153-160	insulin receptor	Homo sapiens	64-66
24341419-6	2014	In contrast, in gestational diabetes, in addition to the decrease in insulin receptor substrate 1 tyrosine phosphorylation, there is an additional decrease in tyrosine phosphorylation of the intracellular portion of the insulin receptor that is not related to the insulin receptor protein content.	Tyrosine	159-167	insulin receptor	Homo sapiens	220-236
24944904-6	2014	Following genetic ablation of InsR, transcriptome profiling of Glut4 neurons demonstrated impairment of the insulin, peptide hormone, and cAMP signaling pathways, with a striking upregulation of anion homeostasis pathway.	Cyclic AMP	138-142	insulin receptor	Homo sapiens	30-34
24651808-6	2014	Through binding to the extracellular domain of the IR, 4548-G05 induces activation of the receptor and initiates the downstream Akt and extracellular signal-related kinase pathways to trigger glucose uptake in C2C12 myotubes.	Glucose	192-199	insulin receptor	Homo sapiens	51-53
24399479-1	2014	We demonstrated the molecular pathogenesis of type 2 diabetes and insulin resistance focusing on the interaction between insulin receptor and GM3 ganglioside in adipocytes and propose a working hypothesis "metabolic disorders, such as type 2 diabetes, are membrane microdomain disorders caused by aberrant expression of gangliosides".	G(M3) Ganglioside	142-157	insulin receptor	Homo sapiens	121-137
24399479-1	2014	We demonstrated the molecular pathogenesis of type 2 diabetes and insulin resistance focusing on the interaction between insulin receptor and GM3 ganglioside in adipocytes and propose a working hypothesis "metabolic disorders, such as type 2 diabetes, are membrane microdomain disorders caused by aberrant expression of gangliosides".	Gangliosides	320-332	insulin receptor	Homo sapiens	121-137
24654916-5	2014	Melatonin acts by regulating GLUT4 expression and/or triggering, via its G-protein-coupled membrane receptors, the phosphorylation of the insulin receptor and its intracellular substrates mobilizing the insulin-signaling pathway.	Melatonin	0-9	insulin receptor	Homo sapiens	138-154
24758840-5	2014	The non-covalently associated dimeric structures are reminiscent of those of the IR family, which has a disulfide-linked dimeric structure.	Disulfides	104-113	insulin receptor	Homo sapiens	81-83
24264858-3	2014	The pathogenesis of insulin resistance involves several inhibitory molecules that interfere with the tyrosine phosphorylation of the insulin receptor and its downstream effectors.	Tyrosine	101-109	insulin receptor	Homo sapiens	133-149
24508798-0	2014	Development of in vitro model of insulin receptor cleavage induced by high glucose in HepG2 cells.	Glucose	75-82	insulin receptor	Homo sapiens	33-49
24196191-2	2014	INSR-A promotes cell growth whereas INSR-B predominantly regulates glucose homeostasis.	Glucose	67-74	insulin receptor	Homo sapiens	36-40
24843827-0	2014	Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription.	Brefeldin A	17-28	insulin receptor	Homo sapiens	60-76
24071517-6	2014	Mechanistic evidence revealed that TMP reduced insulin receptor (InsR) expression and blocked the downstream phosphatidylinositol-3-kinase (PI3K)/AKT and extracellular signal-regulated kinase (ERK) cascades, which was required for TMP attenuation of HSC activation.	tetramethylpyrazine	35-38	insulin receptor	Homo sapiens	47-63
24071517-6	2014	Mechanistic evidence revealed that TMP reduced insulin receptor (InsR) expression and blocked the downstream phosphatidylinositol-3-kinase (PI3K)/AKT and extracellular signal-regulated kinase (ERK) cascades, which was required for TMP attenuation of HSC activation.	tetramethylpyrazine	35-38	insulin receptor	Homo sapiens	65-69
24071517-8	2014	It could be concluded that TMP inhibited Glu/Ins-stimulated HSC activation and ECM production by inhibiting InsR-mediated PI3K/AKT and ERK pathways.	tetramethylpyrazine	27-30	insulin receptor	Homo sapiens	108-112
24071517-8	2014	It could be concluded that TMP inhibited Glu/Ins-stimulated HSC activation and ECM production by inhibiting InsR-mediated PI3K/AKT and ERK pathways.	Glutamic Acid	41-44	insulin receptor	Homo sapiens	108-112
24071517-8	2014	It could be concluded that TMP inhibited Glu/Ins-stimulated HSC activation and ECM production by inhibiting InsR-mediated PI3K/AKT and ERK pathways.	Indium	45-48	insulin receptor	Homo sapiens	108-112
24401367-4	2014	Similarly, Cr enhances the insulin receptor activity on target tissues, especially in muscle cells.	Chromium	11-13	insulin receptor	Homo sapiens	27-43
23969158-2	2014	However, mounting evidence implicates ceramides and their derivatives in various aspects of metabolism via directly impacting the insulin receptor as well as modulating cell survival and proliferation.	Ceramides	38-47	insulin receptor	Homo sapiens	130-146
24843827-0	2014	Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription.	Brefeldin A	17-28	insulin receptor	Homo sapiens	78-80
24843827-0	2014	Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription.	Brefeldin A	30-33	insulin receptor	Homo sapiens	60-76
24843827-0	2014	Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription.	Brefeldin A	30-33	insulin receptor	Homo sapiens	78-80
24843827-5	2014	We report that BFA causes the activation of the insulin receptor (IR), IRS-1, Akt-2, and AS160 components of the insulin pathway.	Brefeldin A	15-18	insulin receptor	Homo sapiens	48-64
24843827-5	2014	We report that BFA causes the activation of the insulin receptor (IR), IRS-1, Akt-2, and AS160 components of the insulin pathway.	Brefeldin A	15-18	insulin receptor	Homo sapiens	66-68
24338270-6	2014	Other drug-discovery approaches are employed to target IGF-1R, and IR includes antisense oligonucleotides and recombinant IGF-binding proteins.	Oligonucleotides	89-105	insulin receptor	Homo sapiens	67-69
24071517-0	2014	Tetramethylpyrazine reduces glucose and insulin-induced activation of hepatic stellate cells by inhibiting insulin receptor-mediated PI3K/AKT and ERK pathways.	tetramethylpyrazine	0-19	insulin receptor	Homo sapiens	107-123
24603137-3	2014	The aim of this study was to evaluate gene and protein expression of an insulin receptor (IR), insulin-like growth factor-1 (IGF1) receptor (IGF1R) and aromatase in granulosa cells treated with metformin and insulin.	Metformin	194-203	insulin receptor	Homo sapiens	72-88
24603137-3	2014	The aim of this study was to evaluate gene and protein expression of an insulin receptor (IR), insulin-like growth factor-1 (IGF1) receptor (IGF1R) and aromatase in granulosa cells treated with metformin and insulin.	Metformin	194-203	insulin receptor	Homo sapiens	90-92
24603137-6	2014	RESULTS: IR and IGF1R mRNA expression was significantly enhanced by metformin but was not affected by insulin.	Metformin	68-77	insulin receptor	Homo sapiens	9-11
24603137-9	2014	CONCLUSION: A direct effect of metformin on the gene expression of IGF1R, IR and aromatase was observed.	Metformin	31-40	insulin receptor	Homo sapiens	74-76
24553405-6	2014	KY-201, but not rosiglitazone inhibited protein tyrosine phosphatase 1B (PTP1B) and increased phosphorylation of the insulin receptor in HepG2 cells.	7-(2-(2-(2-cyclopentylvinyl)-5-methyloxazol-4-yl)-ethoxy)-2-(2,4-hexadienoyl)-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid	0-6	insulin receptor	Homo sapiens	117-133
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Leucine	46-49	insulin receptor	Homo sapiens	125-127
24282611-8	2013	Altogether, these results demonstrate an interplay between E-cadherin and IR/IGF-IR signaling as major networking players in the regulation of bisecting N-glycans expression, with important effects in the modulation of epithelial characteristics and tumor cell invasion.	n-glycans	153-162	insulin receptor	Homo sapiens	74-76
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Glycine	55-58	insulin receptor	Homo sapiens	125-127
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Arginine	64-67	insulin receptor	Homo sapiens	125-127
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Histidine	85-88	insulin receptor	Homo sapiens	125-127
24121506-5	2013	Within L1C domains, five amino acid residues (Leu-135, Gly-188, Arg-244, and vicinal His-318 and Lys-319) were identified as IRR-specific by species conservation analysis of the IR family.	Lysine	97-100	insulin receptor	Homo sapiens	125-127
23969187-0	2013	Metreleptin improves blood glucose in patients with insulin receptor mutations.	Blood Glucose	21-34	insulin receptor	Homo sapiens	52-68
24037759-2	2013	The current model for insulin receptor activation is that two distinct surfaces of insulin monomer engage sequentially with two distinct binding sites on the extracellular surface of the insulin receptor, which is itself a disulfide-linked (alphabeta)2 homodimer.	Disulfides	223-232	insulin receptor	Homo sapiens	22-38
24037759-2	2013	The current model for insulin receptor activation is that two distinct surfaces of insulin monomer engage sequentially with two distinct binding sites on the extracellular surface of the insulin receptor, which is itself a disulfide-linked (alphabeta)2 homodimer.	Disulfides	223-232	insulin receptor	Homo sapiens	187-203
24568043-2	2013	STUDY DESIGN: We ex-amined the frequency of the His 1058 C/T single nucleotide polymorphism (SNP) found in exon 17 of the INSR gene in 61 Japanese PCOS patients and 99 Japanese healthy controls.	Histidine	48-51	insulin receptor	Homo sapiens	122-126
23665048-9	2013	Elevation in status of cav-2 expression rendered the noncaveolar activation of IR signaling in cav-1 down-regulated or/and cholesterol-depleted cells.	Cholesterol	123-134	insulin receptor	Homo sapiens	79-81
24101906-7	2013	STAT3-Ser regulates Hes3, and together they form a convergence point for several signals, including Notch, Tie2, and insulin receptor activation.	Serine	6-9	insulin receptor	Homo sapiens	117-133
24251203-6	2013	Treatment of myoblasts with 10-7 M calcitriol for 24 h showed a significant increase in GLUT1, GLUT4, VDR, and insulin receptor (IR) expression.	Calcitriol	35-45	insulin receptor	Homo sapiens	111-127
24251203-6	2013	Treatment of myoblasts with 10-7 M calcitriol for 24 h showed a significant increase in GLUT1, GLUT4, VDR, and insulin receptor (IR) expression.	Calcitriol	35-45	insulin receptor	Homo sapiens	129-131
23935097-3	2013	Biochemical and structural studies indicate that this class achieves its high selectivity by binding to the ATP-binding pocket of inactive, unphosphorylated IGF-1R/IR and stabilizing the activation loop in a native-like inactive conformation.	Adenosine Triphosphate	108-111	insulin receptor	Homo sapiens	164-166
23603635-3	2013	Different categories of compounds including mono and di substituted benzoquinones, vanadium based compounds and natural products have been reported to cause insulin-like effects either by increasing phosphorylation of insulin receptor (IR) or inhibiting the protein tyrosine phosphatases.	mono and di substituted benzoquinones	44-81	insulin receptor	Homo sapiens	218-234
24251203-7	2013	The results indicate a potential antidiabetic function of vitamin D on GLUT1, GLUT4, VDR, and IR by improving receptor gene expression suggesting a role for vitamin D in regulation of expression of the glucose transporters in muscle cells.	Vitamin D	58-67	insulin receptor	Homo sapiens	94-96
23700321-4	2013	Alternatively, activation of IR increases caveolin-1 phosphorylation on tyrosine-14.	Tyrosine	72-80	insulin receptor	Homo sapiens	29-31
23653049-1	2013	AIMS/HYPOTHESIS: In vitro, insulin glargine (A21Gly,B31Arg,B32Arg human insulin) has an insulin receptor (IR) profile similar to that of human insulin, but a slightly higher affinity for the IGF-1 receptor (IGF1R).	Insulin Glargine	35-43	insulin receptor	Homo sapiens	88-104
23653049-1	2013	AIMS/HYPOTHESIS: In vitro, insulin glargine (A21Gly,B31Arg,B32Arg human insulin) has an insulin receptor (IR) profile similar to that of human insulin, but a slightly higher affinity for the IGF-1 receptor (IGF1R).	Insulin Glargine	35-43	insulin receptor	Homo sapiens	106-108
23653049-6	2013	Glargine treatment resulted in phosphorylation levels of IR and Akt that were comparable with those achieved with human insulin, although delayed in time in some tissues.	Insulin Glargine	0-8	insulin receptor	Homo sapiens	57-59
23700321-8	2013	For cells pretreated with testosterone, higher IR, IRS-1, and caveolin-1 protein levels compared with control conditions were detected.	Testosterone	26-38	insulin receptor	Homo sapiens	47-49
23052216-1	2013	The insulin signaling pathway regulates whole-body glucose homeostasis by transducing extracellular signals from the insulin receptor (IR) to downstream intracellular targets, thus coordinating a multitude of biological functions.	Glucose	51-58	insulin receptor	Homo sapiens	117-133
23052216-1	2013	The insulin signaling pathway regulates whole-body glucose homeostasis by transducing extracellular signals from the insulin receptor (IR) to downstream intracellular targets, thus coordinating a multitude of biological functions.	Glucose	51-58	insulin receptor	Homo sapiens	135-137
23052216-5	2013	Accordingly, our review will focus on roles for IR substrates as they pertain to three primary areas: metabolism/glucose uptake, mitogenesis/growth, and aging/longevity.	Glucose	113-120	insulin receptor	Homo sapiens	48-50
23052216-6	2013	While IR functions in a seemingly pleiotropic manner in many cell types, through these three main roles in fat and skeletal muscle cells, IR multi-tasks to regulate whole-body glucose homeostasis to impact healthspan and lifespan.	Glucose	176-183	insulin receptor	Homo sapiens	6-8
23052216-6	2013	While IR functions in a seemingly pleiotropic manner in many cell types, through these three main roles in fat and skeletal muscle cells, IR multi-tasks to regulate whole-body glucose homeostasis to impact healthspan and lifespan.	Glucose	176-183	insulin receptor	Homo sapiens	138-140
23603635-3	2013	Different categories of compounds including mono and di substituted benzoquinones, vanadium based compounds and natural products have been reported to cause insulin-like effects either by increasing phosphorylation of insulin receptor (IR) or inhibiting the protein tyrosine phosphatases.	mono and di substituted benzoquinones	44-81	insulin receptor	Homo sapiens	236-238
23603635-3	2013	Different categories of compounds including mono and di substituted benzoquinones, vanadium based compounds and natural products have been reported to cause insulin-like effects either by increasing phosphorylation of insulin receptor (IR) or inhibiting the protein tyrosine phosphatases.	Vanadium	83-91	insulin receptor	Homo sapiens	218-234
23603635-3	2013	Different categories of compounds including mono and di substituted benzoquinones, vanadium based compounds and natural products have been reported to cause insulin-like effects either by increasing phosphorylation of insulin receptor (IR) or inhibiting the protein tyrosine phosphatases.	Vanadium	83-91	insulin receptor	Homo sapiens	236-238
23338941-1	2013	The insulin-like growth factor-1 receptor (IGF-1R), like the insulin receptor (IR), plays a significant role in determining bioavailability of the critical signalling molecule nitric oxide (NO) and hence, modulates endothelial cell function, particularly in response to stimulation with insulin.	Nitric Oxide	176-188	insulin receptor	Homo sapiens	61-77
23338941-1	2013	The insulin-like growth factor-1 receptor (IGF-1R), like the insulin receptor (IR), plays a significant role in determining bioavailability of the critical signalling molecule nitric oxide (NO) and hence, modulates endothelial cell function, particularly in response to stimulation with insulin.	Nitric Oxide	176-188	insulin receptor	Homo sapiens	79-81
23875003-4	2013	3xTg-AD mice fed 0.23% w/v lipoic acid in drinking water for 4 weeks showed an insulin mimetic effect that consisted of increased brain glucose uptake, activation of the insulin receptor substrate and of the PI3K/Akt signaling pathway.	Thioctic Acid	27-38	insulin receptor	Homo sapiens	170-186
23875003-4	2013	3xTg-AD mice fed 0.23% w/v lipoic acid in drinking water for 4 weeks showed an insulin mimetic effect that consisted of increased brain glucose uptake, activation of the insulin receptor substrate and of the PI3K/Akt signaling pathway.	Water	51-56	insulin receptor	Homo sapiens	170-186
23425024-2	2013	"Hydrogen sulfide treatment promotes glucose uptake by increasing insulin receptor sensitivity and ameliorates kidney lesions in type 2 diabetes."	Hydrogen Sulfide	1-17	insulin receptor	Homo sapiens	66-82
23425024-2	2013	"Hydrogen sulfide treatment promotes glucose uptake by increasing insulin receptor sensitivity and ameliorates kidney lesions in type 2 diabetes."	Glucose	37-44	insulin receptor	Homo sapiens	66-82
23592917-0	2013	Reduced insulin receptor signaling in retinal Muller cells cultured in high glucose.	Glucose	76-83	insulin receptor	Homo sapiens	8-24
23348915-1	2013	Insulin regulates blood glucose levels in higher organisms by binding to and activating insulin receptor (IR), a constitutively homodimeric glycoprotein of the receptor tyrosine kinase (RTK) superfamily.	Blood Glucose	18-31	insulin receptor	Homo sapiens	88-104
23348915-1	2013	Insulin regulates blood glucose levels in higher organisms by binding to and activating insulin receptor (IR), a constitutively homodimeric glycoprotein of the receptor tyrosine kinase (RTK) superfamily.	Blood Glucose	18-31	insulin receptor	Homo sapiens	106-108
23225242-2	2013	Tyrosine phosphorylation of the insulin receptor (IR) by insulin promotes glucose uptake by activating the PI3K/Akt pathway.	Tyrosine	0-8	insulin receptor	Homo sapiens	32-48
23348423-4	2013	We show here that siRNA knockdown of the insulin receptor enhanced the cytotoxic action of native Pseudomonas exotoxin and enhanced SS1P toxicity on several human cell lines, but did not affect the response to other cytotoxic agents such as TRAIL, etoposide, and cycloheximide.	Etoposide	248-257	insulin receptor	Homo sapiens	41-57
23348423-4	2013	We show here that siRNA knockdown of the insulin receptor enhanced the cytotoxic action of native Pseudomonas exotoxin and enhanced SS1P toxicity on several human cell lines, but did not affect the response to other cytotoxic agents such as TRAIL, etoposide, and cycloheximide.	Cycloheximide	263-276	insulin receptor	Homo sapiens	41-57
23314177-3	2013	Furthermore, Ahsg inhibits InsR autophosphorylation of highly-purified insulin holoreceptors in a cell-free, ATP-dependent system, with an IC50 within the range of single-chain Ahsg concentrations in human serum.	Adenosine Triphosphate	109-112	insulin receptor	Homo sapiens	27-31
23225242-2	2013	Tyrosine phosphorylation of the insulin receptor (IR) by insulin promotes glucose uptake by activating the PI3K/Akt pathway.	Tyrosine	0-8	insulin receptor	Homo sapiens	50-52
23225242-2	2013	Tyrosine phosphorylation of the insulin receptor (IR) by insulin promotes glucose uptake by activating the PI3K/Akt pathway.	Glucose	74-81	insulin receptor	Homo sapiens	32-48
23225242-2	2013	Tyrosine phosphorylation of the insulin receptor (IR) by insulin promotes glucose uptake by activating the PI3K/Akt pathway.	Glucose	74-81	insulin receptor	Homo sapiens	50-52
23363976-1	2013	Binge alcohol exposure impairs hepatic insulin action by blunting insulin receptor signaling in the brain and enables the identification of a therapeutic target that may help treat alcohol-induced insulin resistance (Lindtner et al., this issue).	Alcohols	6-13	insulin receptor	Homo sapiens	66-82
23181759-2	2013	In the present study, in vivo experiments using a non-invasive method of chronic administration of corticosterone in drinking water demonstrated that chronic corticosterone administration led to cognitive impairment in the novel object recognition test and insulin resistance, as shown by significant increases in plasma insulin levels and the homeostatic model assessment index, and decreased insulin receptor phosphorylation.	Corticosterone	99-113	insulin receptor	Homo sapiens	394-410
23181759-2	2013	In the present study, in vivo experiments using a non-invasive method of chronic administration of corticosterone in drinking water demonstrated that chronic corticosterone administration led to cognitive impairment in the novel object recognition test and insulin resistance, as shown by significant increases in plasma insulin levels and the homeostatic model assessment index, and decreased insulin receptor phosphorylation.	Water	126-131	insulin receptor	Homo sapiens	394-410
23181759-2	2013	In the present study, in vivo experiments using a non-invasive method of chronic administration of corticosterone in drinking water demonstrated that chronic corticosterone administration led to cognitive impairment in the novel object recognition test and insulin resistance, as shown by significant increases in plasma insulin levels and the homeostatic model assessment index, and decreased insulin receptor phosphorylation.	Corticosterone	158-172	insulin receptor	Homo sapiens	394-410
23471249-4	2013	The insulin receptor within the central nervous system is widely distributed, reflecting insulin"s diverse range of actions, including acting as an adiposity signal to reduce food intake and increase energy expenditure, regulation of systemic glucose responses, altering sympathetic activity, and involvement in cognitive function.	Glucose	243-250	insulin receptor	Homo sapiens	4-20
23457259-3	2013	As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR"s catalytic activity.	Tyrosine	25-33	insulin receptor	Homo sapiens	81-85
23457259-3	2013	As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR"s catalytic activity.	Tyrosine	25-33	insulin receptor	Homo sapiens	152-156
23457259-3	2013	As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR"s catalytic activity.	Tyrosine	25-33	insulin receptor	Homo sapiens	152-156
23457259-3	2013	As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR"s catalytic activity.	Phosphotyrosine	196-211	insulin receptor	Homo sapiens	81-85
23457259-3	2013	As in prototypical RTKs, tyrosine phosphorylation in the juxtamembrane region of InsR creates recruitment sites for downstream signaling proteins (IRS [InsR substrate] proteins, Shc) containing a phosphotyrosine-binding (PTB) domain, and tyrosine phosphorylation in the kinase activation loop stimulates InsR"s catalytic activity.	Tyrosine	203-211	insulin receptor	Homo sapiens	81-85
23457259-4	2013	For InsR, phosphorylation of the activation loop, which contains three tyrosine residues, also creates docking sites for adaptor proteins (Grb10/14, SH2B2) that possess specialized Src homology-2 (SH2) domains, which are dimeric and engage two phosphotyrosines in the activation loop.	Tyrosine	71-79	insulin receptor	Homo sapiens	4-8
23457259-4	2013	For InsR, phosphorylation of the activation loop, which contains three tyrosine residues, also creates docking sites for adaptor proteins (Grb10/14, SH2B2) that possess specialized Src homology-2 (SH2) domains, which are dimeric and engage two phosphotyrosines in the activation loop.	Phosphotyrosine	244-260	insulin receptor	Homo sapiens	4-8
23628024-6	2013	mRNA level of IGF-IR in CR group was significantly lower than that in newly diagnosed and relapsed groups (P = 0.000 and P = 0.018); mRNA level of IR in newly diagnosed and relapsed groups were significantly lower than that in the normal control group (P = 0.001 and P = 0.018).	Chromium	24-26	insulin receptor	Homo sapiens	18-20
23628024-7	2013	mRNA level of IR in CR group was significantly higher than that in newly diagnosed and relapsed groups (P = 0.000 and P = 0.001); mRNA levels of IGF-IR and IR correlated with the clinical stages of the disease, while they had no association with the sex, age and white blood cell counts at new diagnosis.	Chromium	20-22	insulin receptor	Homo sapiens	14-16
23628024-7	2013	mRNA level of IR in CR group was significantly higher than that in newly diagnosed and relapsed groups (P = 0.000 and P = 0.001); mRNA levels of IGF-IR and IR correlated with the clinical stages of the disease, while they had no association with the sex, age and white blood cell counts at new diagnosis.	Chromium	20-22	insulin receptor	Homo sapiens	149-151
23319492-8	2013	Inhibition of the IGF1R/INSR signalling axis attenuated the effects of IGF2 on steroid hormone synthesis.	Steroids	79-94	insulin receptor	Homo sapiens	24-28
23395167-4	2013	LRP6 mutation carriers exhibited hyperinsulinemia and reduced insulin sensitivity compared to noncarrier relatives in response to oral glucose ingestion, which correlated with a significant decline in tissue expression of the insulin receptor and insulin signaling activity.	Glucose	135-142	insulin receptor	Homo sapiens	226-242
23363976-1	2013	Binge alcohol exposure impairs hepatic insulin action by blunting insulin receptor signaling in the brain and enables the identification of a therapeutic target that may help treat alcohol-induced insulin resistance (Lindtner et al., this issue).	Alcohols	181-188	insulin receptor	Homo sapiens	66-82
23108067-6	2012	Fetuin-A reduced insulin receptor substrate-1 and tyrosine phosphorylated insulin receptor substrate-1 expression in extravillous trophoblast cells that had been treated with insulin-like growth factor.	Tyrosine	50-58	insulin receptor	Homo sapiens	74-90
23844554-11	2013	Inhibition of AKT with AZD5363 resulted in upregulation and activation of RTKs, including IGF-IR and InsR, upregulation of FoxO3a and ERalpha mRNAs as well as FoxO- and ER-dependent transcription of IGF-I and IGF-II ligands.	capivasertib	23-30	insulin receptor	Homo sapiens	101-105
23844554-12	2013	Inhibition of IGF-IR/InsR or PI3K abrogated AKT PH-GFP membrane localization and T308 P-AKT following treatment with AZD5363.	capivasertib	117-124	insulin receptor	Homo sapiens	21-25
23844554-13	2013	Treatment with IGFBP-3 blocked AZD5363-induced P-IGF-IR/InsR and T308 P-AKT, suggesting that receptor phosphorylation was dependent on increased autocrine ligands.	capivasertib	31-38	insulin receptor	Homo sapiens	56-60
23844554-14	2013	Finally, treatment with the dual IGF-IR/InsR inhibitor AZD9362 enhanced the anti-tumor effect of AZD5363 in MCF-7/LTED cells and MCF-7 xenografts in ovariectomized mice devoid of estrogen supplementation.	AZD9362	55-62	insulin receptor	Homo sapiens	40-44
23844554-14	2013	Finally, treatment with the dual IGF-IR/InsR inhibitor AZD9362 enhanced the anti-tumor effect of AZD5363 in MCF-7/LTED cells and MCF-7 xenografts in ovariectomized mice devoid of estrogen supplementation.	capivasertib	97-104	insulin receptor	Homo sapiens	40-44
23073831-6	2013	Here we demonstrate that mature cultures of hippocampal neurons respond to d-chiro-inositol (DCI), pinitol (3-O-methyl DCI), and the inositol glycan INS-2 (pinitol beta-1-4 galactosamine) with increased phosphorylation in key upstream components in the insulin-signaling pathway (insulin receptor, insulin receptor substrate-1, and Akt).	inositol glycan ins-2	133-154	insulin receptor	Homo sapiens	253-326
23569395-8	2013	RESULTS: High Glc indeed led to inactivation of IR, IRS-1, and subsequent Akt in myotubes, indicating an interruption of the signal pathway.	Glucose	14-17	insulin receptor	Homo sapiens	48-50
23705494-9	2013	Mutations of INSR induce insulin resistance, lipodystrophy, other pathology, and suggest an important role of insulin in glucose level regulation and in stimulation of fat accumulation as well.	Glucose	121-128	insulin receptor	Homo sapiens	13-17
24296476-7	2013	Stearic acid (30 muM) significantly increased insulin-induced phosphorylation of insulin receptor at Tyr1185, but insulin-induced phosphorylation of Akt was not significantly enhanced.	stearic acid	0-12	insulin receptor	Homo sapiens	81-97
24296476-9	2013	CONCLUSION: The results of the present study indicate that stearic acid serves as a potent PTP1B inhibitor, possibly causing an enhancement in the insulin receptor signaling to stimulate glucose uptake into adipocytes.	stearic acid	59-71	insulin receptor	Homo sapiens	147-163
24296476-9	2013	CONCLUSION: The results of the present study indicate that stearic acid serves as a potent PTP1B inhibitor, possibly causing an enhancement in the insulin receptor signaling to stimulate glucose uptake into adipocytes.	Glucose	187-194	insulin receptor	Homo sapiens	147-163
23104093-6	2013	The insulin receptor has also been shown to perform an important role in the distal regions of the renal tubules, regulating sodium excretion and blood pressure control here.	Sodium	125-131	insulin receptor	Homo sapiens	4-20
23448488-1	2013	Insulin resistance is associated with the impairment of the response of insulin receptor to insulin, resulting in the reduction of glucose uptake, leading to the alteration of myocardial glucose metabolism, impairment of cardiac electrophysiology, and increased susceptibility to ischemia-induced myocardial injury.	Glucose	131-138	insulin receptor	Homo sapiens	72-88
22972224-8	2013	In the experiments conducted using COS7 cells homozygously transfected with the INSR mutation, T910M INSR failed to process the proreceptor and decreased insulin-stimulated tyrosine phosphorylation.	Tyrosine	173-181	insulin receptor	Homo sapiens	80-84
22972224-8	2013	In the experiments conducted using COS7 cells homozygously transfected with the INSR mutation, T910M INSR failed to process the proreceptor and decreased insulin-stimulated tyrosine phosphorylation.	Tyrosine	173-181	insulin receptor	Homo sapiens	101-105
22972224-9	2013	E1047K INSR resulted in a complete absence of insulin-stimulated tyrosine phosphorylation.	Tyrosine	65-73	insulin receptor	Homo sapiens	7-11
23363253-9	2013	Moreover, hypoxia and glucose or glutamine deprivation are controlled by the expression of insulin receptor and related to insulin signaling genes mostly via ERN1 enzyme signaling.	Glucose	22-29	insulin receptor	Homo sapiens	91-107
23363253-9	2013	Moreover, hypoxia and glucose or glutamine deprivation are controlled by the expression of insulin receptor and related to insulin signaling genes mostly via ERN1 enzyme signaling.	Glutamine	33-42	insulin receptor	Homo sapiens	91-107
23141431-6	2012	Metformin with insulin significantly increased mRNA expressions of INSR, IGF-1R, and IRS-1, while metformin alone had no significant effect.	Metformin	0-9	insulin receptor	Homo sapiens	67-71
23141431-7	2012	And metformin with insulin had the significant effect on the protein activity (activation and phosphorylation) of downstream targets of INSR signaling pathway.	Metformin	4-13	insulin receptor	Homo sapiens	136-140
22974639-3	2012	Moreover, a high extracellular concentration of glucose activated DGKdelta in skeletal muscle cells, which was followed by a reduction in the intracellular diacylglycerol levels and the inactivation of protein kinase Calpha, the enzyme that phosphorylates and inactivates the insulin receptor.	Glucose	48-55	insulin receptor	Homo sapiens	276-292
22992069-2	2012	TrkA autoinhibition closely resembles that seen for the insulin receptor, relying on projection of an activation loop tyrosine residue into the substrate-binding site and occlusion of the ATP-binding site by the activation loop.	Tyrosine	118-126	insulin receptor	Homo sapiens	56-72
22992069-2	2012	TrkA autoinhibition closely resembles that seen for the insulin receptor, relying on projection of an activation loop tyrosine residue into the substrate-binding site and occlusion of the ATP-binding site by the activation loop.	Adenosine Triphosphate	188-191	insulin receptor	Homo sapiens	56-72
23730255-0	2012	H2O2 Signalling Pathway: A Possible Bridge between Insulin Receptor and Mitochondria.	Hydrogen Peroxide	0-4	insulin receptor	Homo sapiens	51-67
23730255-2	2012	Insulin-induced H2O2 promotes insulin receptor activation and the mitochondria act as the insulin-sensitive H2O2 source, providing a direct molecular link between mitochondrial dysfunction and irregular insulin receptor activation.	Hydrogen Peroxide	16-20	insulin receptor	Homo sapiens	30-46
23730255-2	2012	Insulin-induced H2O2 promotes insulin receptor activation and the mitochondria act as the insulin-sensitive H2O2 source, providing a direct molecular link between mitochondrial dysfunction and irregular insulin receptor activation.	Hydrogen Peroxide	16-20	insulin receptor	Homo sapiens	203-219
23730255-2	2012	Insulin-induced H2O2 promotes insulin receptor activation and the mitochondria act as the insulin-sensitive H2O2 source, providing a direct molecular link between mitochondrial dysfunction and irregular insulin receptor activation.	Hydrogen Peroxide	108-112	insulin receptor	Homo sapiens	203-219
23730255-4	2012	Due to the high significance of insulin-induced H2O2 for insulin receptor activation, oxidative stress-induced upregulation of antioxidant enzymes, e.g., in AD brains, may represent another risk factor contributing to the development of insulin resistance.	Hydrogen Peroxide	48-52	insulin receptor	Homo sapiens	57-73
23730255-5	2012	As insulin-induced H2O2 signalling requires fully functional mitochondria, pharmacological strategies based on activating mitochondria biogenesis in the brain are central to the treatment of diseases associated with dysfunctional insulin receptor signalling in this organ.	Hydrogen Peroxide	19-23	insulin receptor	Homo sapiens	230-246
22609131-6	2012	FFA cause insulin resistance by inhibiting insulin signaling through the activation of serin-kinases, i.e. protein kinase C-Theta, and the kinases JNK and IKK, which promote a mechanism of serine phosphorylation of Insulin Receptor Substrates (IRS), leading to interruption of the downstream insulin receptor (IR) signaling.	Serine	189-195	insulin receptor	Homo sapiens	292-308
23053988-2	2012	We found that 1 muM ALA increased IGF-I secretion from hepatocytes at 48 and 72 h. Expression of hepatocytes IGF-I, IGF-II, GH receptor (GHR), insulin receptor (IR), IGF-binding protein 3 (IGFBP3), and IGFBP4 mRNAs was up-regulated by ALA treatment.	alpha-Linolenic Acid	20-23	insulin receptor	Homo sapiens	143-159
23053988-2	2012	We found that 1 muM ALA increased IGF-I secretion from hepatocytes at 48 and 72 h. Expression of hepatocytes IGF-I, IGF-II, GH receptor (GHR), insulin receptor (IR), IGF-binding protein 3 (IGFBP3), and IGFBP4 mRNAs was up-regulated by ALA treatment.	alpha-Linolenic Acid	20-23	insulin receptor	Homo sapiens	161-163
23053988-4	2012	Insulin (1 muM) alone or co-treated with ALA improved IGF-I secretion and the expression of IGFBP3 mRNA, but decreased IGFBP1 mRNA versus appropriate control across ALA. Insulin also up-regulated the expression of GHR, IR, IGFBP3, and IGFBP4 mRNAs, and tended to prevent the transcript levels of IGF-I and IGFBP4 improved by ALA.	alpha-Linolenic Acid	41-44	insulin receptor	Homo sapiens	219-221
23063366-4	2012	Conversion begins by glucocorticoid and cAMP signals raising C/EBPbeta levels above a critical threshold, triggering three consecutive positive feedback loops: from PPARgamma to C/EBPalpha, then to C/EBPbeta, and last to the insulin receptor.	Cyclic AMP	40-44	insulin receptor	Homo sapiens	225-241
22932796-5	2012	In vitro studies with OSI-906, a clinically relevant dual IGF-1R and insulin receptor inhibitor, showed it acted synergistically with bortezomib, and potently resensitized bortezomib-resistant cell lines and patient samples to bortezomib.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	22-29	insulin receptor	Homo sapiens	69-85
23061721-8	2012	The InsR silenced cells also showed increased sensitivity to exogenous IGF-1, and increased PI3K activity was reversed significantly by incubating cells with IGF-1R specific antagonist, AG538.	AG 538	186-191	insulin receptor	Homo sapiens	4-8
23061721-9	2012	PI3K/Akt dependent activation of cAMP responsive element-binding protein (CREB)-1 induced expression of matrix metalloproteinase (MMP)-9 and suppressing MMP activity by doxycycline partially reversed FN accumulation in the InsR silenced cells.	Doxycycline	169-180	insulin receptor	Homo sapiens	223-227
22928576-4	2012	Rodents with tissue-specific knockout of the insulin receptor in the beta-cell (betaIRKO) show reduced first-phase glucose-stimulated insulin secretion (GSIS) and with aging develop glucose intolerance and diabetes, phenotypically similar to the process seen in human T2D.	Glucose	115-122	insulin receptor	Homo sapiens	45-61
23335521-4	2012	The expression of insulin receptor mRNA was detected by RT-PCR, with or without mitogen activated kinase (MAPK) signals blocked by their inhibitors: SP600125, the inhibitor of Jun N-terminal kinase (JNK), and PD98059, the inhibitor of extracellular signal-regulated (ERK1/2).	pyrazolanthrone	149-157	insulin receptor	Homo sapiens	18-34
23335521-4	2012	The expression of insulin receptor mRNA was detected by RT-PCR, with or without mitogen activated kinase (MAPK) signals blocked by their inhibitors: SP600125, the inhibitor of Jun N-terminal kinase (JNK), and PD98059, the inhibitor of extracellular signal-regulated (ERK1/2).	2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one	209-216	insulin receptor	Homo sapiens	18-34
22775461-3	2012	The aim of this work was to investigate the insulin receptor expression in B and T cells under incubation with pathological glucose concentrations, respond hyperglycemia and hypoglycemia.	Glucose	124-131	insulin receptor	Homo sapiens	44-60
22862558-5	2012	EXPERT OPINION: Mechanisms of TCM in treating DM are concluded: i) to promote insulin secretion and increase serum insulin levels; ii) to increase the sensitivity of insulin and improve its resistance; iii) to inhibit glucose absorption; iv) to affect glucose metabolism of insulin receptor; and v) to scavenge radicals and prevent lipid peroxidation.	Glucose	218-225	insulin receptor	Homo sapiens	274-297
23018458-4	2012	We found that GBS-induced, MyD88-dependent chemokine formation of PML was specifically downmodulated by insulin via insulin receptor-mediated induction of PI3K.	gbs	14-17	insulin receptor	Homo sapiens	116-132
22609131-6	2012	FFA cause insulin resistance by inhibiting insulin signaling through the activation of serin-kinases, i.e. protein kinase C-Theta, and the kinases JNK and IKK, which promote a mechanism of serine phosphorylation of Insulin Receptor Substrates (IRS), leading to interruption of the downstream insulin receptor (IR) signaling.	Serine	189-195	insulin receptor	Homo sapiens	244-246
22609131-7	2012	TNF-alpha, secreted by hypertrophic adipocytes and adipose tissue macrophages, also inhibits IR signaling by a double mechanism of serine-phosphorylation and tyrosine-dephosphorylation of IRS-1, causing inactivation and degradation of IRS-1 and a consequent stop of IR signaling.	Serine	131-137	insulin receptor	Homo sapiens	93-95
22609131-7	2012	TNF-alpha, secreted by hypertrophic adipocytes and adipose tissue macrophages, also inhibits IR signaling by a double mechanism of serine-phosphorylation and tyrosine-dephosphorylation of IRS-1, causing inactivation and degradation of IRS-1 and a consequent stop of IR signaling.	Tyrosine	158-166	insulin receptor	Homo sapiens	93-95
22609131-7	2012	TNF-alpha, secreted by hypertrophic adipocytes and adipose tissue macrophages, also inhibits IR signaling by a double mechanism of serine-phosphorylation and tyrosine-dephosphorylation of IRS-1, causing inactivation and degradation of IRS-1 and a consequent stop of IR signaling.	Tyrosine	158-166	insulin receptor	Homo sapiens	188-190
22278734-1	2012	The insulin receptor (IR) and low-density lipoprotein receptor (LDLR) maintain glucose and lipid metabolism, respectively.	Glucose	79-86	insulin receptor	Homo sapiens	4-20
22846360-3	2012	Low levels of magnesium in the venous blood induce the disturbances of auto-phosphylation on the insulin receptor and deteriorate insulin resistance.	Magnesium	14-23	insulin receptor	Homo sapiens	97-113
22775283-3	2012	SUBJECTS AND METHODS: The INSR gene was sequenced in 25 normal glucose-tolerant (NGT) and 25 T2D subjects, and the variant found was genotyped by polymerase chain reaction-restriction fragment length polymorphism in 1,016 NGT and 1,010 T2D subjects, randomly selected from the Chennai Urban Rural Epidemiology Study.	Glucose	63-70	insulin receptor	Homo sapiens	26-30
22573715-6	2012	An IGF1R tyrosine kinase inhibitor, AEW541, with equal potency for the IGF1R and IR, inhibited IGF-I-, IGF-II-, and insulin-stimulated Akt phosphorylation, proliferation, and anchorage-independent growth in parental cells.	NVP-AEW541	36-42	insulin receptor	Homo sapiens	81-83
22573715-10	2012	Inhibition of IR may be necessary to manage tamoxifen-resistant breast cancer.	Tamoxifen	44-53	insulin receptor	Homo sapiens	14-16
22278734-1	2012	The insulin receptor (IR) and low-density lipoprotein receptor (LDLR) maintain glucose and lipid metabolism, respectively.	Glucose	79-86	insulin receptor	Homo sapiens	22-24
22223861-5	2012	These cholesterol-rich microdomains are important, owing to enrichment therein of significant amounts of key transport proteins involved in uptake of cholesterol [SR-B1, ABCA-1, P-glycoprotein (P-gp), sterol carrier binding protein (SCP-2)], FA transport protein (FATP), and glucose transporters 1 and 2 (GLUT1, GLUT2) insulin receptor.	Cholesterol	6-17	insulin receptor	Homo sapiens	319-335
22396018-6	2012	We conclude that catecholamine release is responsible for the ER stress response and impaired insulin receptor signaling after burn injury.	Catecholamines	17-30	insulin receptor	Homo sapiens	94-110
22403294-4	2012	XMetA was found to function as a specific partial agonist of INSR, eliciting tyrosine phosphorylation of INSR but not the IGF-IR.	Tyrosine	77-85	insulin receptor	Homo sapiens	61-65
22403294-4	2012	XMetA was found to function as a specific partial agonist of INSR, eliciting tyrosine phosphorylation of INSR but not the IGF-IR.	Tyrosine	77-85	insulin receptor	Homo sapiens	105-109
22768955-0	2012	"DFG-flip" in the insulin receptor kinase is facilitated by a helical intermediate state of the activation loop.	1,3-Diphenylguanidine	1-4	insulin receptor	Homo sapiens	18-34
22434934-0	2012	Cannabinoids induce pancreatic beta-cell death by directly inhibiting insulin receptor activation.	Cannabinoids	0-12	insulin receptor	Homo sapiens	70-86
22434934-5	2012	Pharmacological blockade or genetic deficiency of CB1 receptors enhanced insulin receptor signaling after injury, leading to reduced blood glucose concentrations and activation of Bad, which increased beta-cell survival.	Glucose	139-146	insulin receptor	Homo sapiens	73-89
21824047-2	2012	This study aimed to correlate polymorphisms of genes involved in the biosynthesis and metabolism of steroids and insulin action (CYP17A1, CYP19A1, AR, ESR1, ESR2, INSR, IGF2 and PAI1) with clinical and biochemical parameters of PCOS.	Steroids	100-108	insulin receptor	Homo sapiens	163-167
22449812-4	2012	Imbalance between muscle and hepatic aPKC activation (and expression of PKC-iota in humans) by insulin results from differential downregulation of insulin receptor substrates that control phosphatidylinositol-3-kinase.	iota	76-80	insulin receptor	Homo sapiens	147-163
23675265-2	2012	Experiments were carried out to determine the role of insulin receptor interaction in the nitric oxide induced maspin synthesis in neutrophils that was effected by estrogen or progesterone.	Nitric Oxide	90-102	insulin receptor	Homo sapiens	54-70
23675265-2	2012	Experiments were carried out to determine the role of insulin receptor interaction in the nitric oxide induced maspin synthesis in neutrophils that was effected by estrogen or progesterone.	Progesterone	176-188	insulin receptor	Homo sapiens	54-70
21979150-3	2012	Many obesity-associated diseases, such as insulin resistance in skeletal muscle, cardiac lipotoxicity, and hepatic steatosis, are thought to be driven by the overflow of fatty acids from adipose stores and the subsequent ectopic accumulation of lipids resulting in apoptosis, ER stress, and inactivation of the insulin receptor signaling cascade.	Fatty Acids	170-181	insulin receptor	Homo sapiens	311-327
21850397-0	2012	Enhancement of doxorubicin cytotoxicity of human cancer cells by tyrosine kinase inhibition of insulin receptor and type I IGF receptor.	Doxorubicin	15-26	insulin receptor	Homo sapiens	95-111
22017372-9	2012	The arginine residue at position 118 is located in the ligand-binding domain of INSR and is highly conserved across species.	Arginine	4-12	insulin receptor	Homo sapiens	80-84
22298784-0	2012	Piceatannol, natural polyphenolic stilbene, inhibits adipogenesis via modulation of mitotic clonal expansion and insulin receptor-dependent insulin signaling in early phase of differentiation.	3,3',4,5'-tetrahydroxystilbene	0-11	insulin receptor	Homo sapiens	113-129
22298784-10	2012	Our kinetics study of IR further identified a K(m) value for ATP of 57.8 mum and a K(i) value for piceatannol of 28.9 mum.	Adenosine Triphosphate	61-64	insulin receptor	Homo sapiens	22-24
22298784-10	2012	Our kinetics study of IR further identified a K(m) value for ATP of 57.8 mum and a K(i) value for piceatannol of 28.9 mum.	3,3',4,5'-tetrahydroxystilbene	98-109	insulin receptor	Homo sapiens	22-24
22298784-11	2012	We also showed that piceatannol directly binds to IR and inhibits IR kinase activity in a mixed noncompetitive manner to ATP, through which piceatannol appears to inhibit adipogenesis.	3,3',4,5'-tetrahydroxystilbene	20-31	insulin receptor	Homo sapiens	50-52
22298784-11	2012	We also showed that piceatannol directly binds to IR and inhibits IR kinase activity in a mixed noncompetitive manner to ATP, through which piceatannol appears to inhibit adipogenesis.	3,3',4,5'-tetrahydroxystilbene	20-31	insulin receptor	Homo sapiens	66-68
22298784-11	2012	We also showed that piceatannol directly binds to IR and inhibits IR kinase activity in a mixed noncompetitive manner to ATP, through which piceatannol appears to inhibit adipogenesis.	Adenosine Triphosphate	121-124	insulin receptor	Homo sapiens	66-68
22298784-11	2012	We also showed that piceatannol directly binds to IR and inhibits IR kinase activity in a mixed noncompetitive manner to ATP, through which piceatannol appears to inhibit adipogenesis.	3,3',4,5'-tetrahydroxystilbene	140-151	insulin receptor	Homo sapiens	50-52
22298784-11	2012	We also showed that piceatannol directly binds to IR and inhibits IR kinase activity in a mixed noncompetitive manner to ATP, through which piceatannol appears to inhibit adipogenesis.	3,3',4,5'-tetrahydroxystilbene	140-151	insulin receptor	Homo sapiens	66-68
22298784-12	2012	Taken together, our study reveals an anti-adipogenic function of piceatannol and highlights IR and its downstream insulin signaling as novel targets for piceatannol in the early phase of adipogenesis.	3,3',4,5'-tetrahydroxystilbene	153-164	insulin receptor	Homo sapiens	92-94
22393939-0	2012	Small-molecule ATP-competitive dual IGF-1R and insulin receptor inhibitors: structural insights, chemical diversity and molecular evolution.	Adenosine Triphosphate	15-18	insulin receptor	Homo sapiens	47-63
22223861-5	2012	These cholesterol-rich microdomains are important, owing to enrichment therein of significant amounts of key transport proteins involved in uptake of cholesterol [SR-B1, ABCA-1, P-glycoprotein (P-gp), sterol carrier binding protein (SCP-2)], FA transport protein (FATP), and glucose transporters 1 and 2 (GLUT1, GLUT2) insulin receptor.	Cholesterol	150-161	insulin receptor	Homo sapiens	319-335
22705438-10	2012	Multivariable logistic regression analysis showed that the NsiI polymorphism of the exon 8 of the INSR was an independent predictor for MS in Han people adjusted for total cholesterol, sex, physical activity, educational level, family income, alcohol intake and smoking (OR=2.55, 95% CI: 1.31-4.94, p=0.006).	Cholesterol	172-183	insulin receptor	Homo sapiens	98-102
22019459-13	2012	Additionally, GGPP treatment of MC3T3-E1 pre-osteoblasts resulted in a decrease in the insulin-induced phosphorylation of the insulin receptor.	geranylgeranyl pyrophosphate	14-18	insulin receptor	Homo sapiens	126-142
22200571-2	2012	Here, we analyzed the interaction between insulin receptor (IR) and GM3 in the plasma membranes using immunoelectron microscopy.	gm3	68-71	insulin receptor	Homo sapiens	42-58
22200571-2	2012	Here, we analyzed the interaction between insulin receptor (IR) and GM3 in the plasma membranes using immunoelectron microscopy.	gm3	68-71	insulin receptor	Homo sapiens	60-62
23251042-5	2012	In this paper we have studied insulin receptor binding of lispro and glargine; the two commonly used recombinant insulins using tools of computational biology.	Insulin Lispro	58-64	insulin receptor	Homo sapiens	30-46
23251042-5	2012	In this paper we have studied insulin receptor binding of lispro and glargine; the two commonly used recombinant insulins using tools of computational biology.	Insulin Glargine	69-77	insulin receptor	Homo sapiens	30-46
23251042-6	2012	We have observed that the binding pattern of insulin receptor (L1-CR-L2 ectodomain) with lispro and glargine is different when compared with human insulin.	Insulin Glargine	100-108	insulin receptor	Homo sapiens	45-61
22705438-10	2012	Multivariable logistic regression analysis showed that the NsiI polymorphism of the exon 8 of the INSR was an independent predictor for MS in Han people adjusted for total cholesterol, sex, physical activity, educational level, family income, alcohol intake and smoking (OR=2.55, 95% CI: 1.31-4.94, p=0.006).	Alcohols	243-250	insulin receptor	Homo sapiens	98-102
23056614-4	2012	But the mechanism integrating insulin receptor signaling to glucose utilization with lipogenesis is unknown.	Glucose	60-67	insulin receptor	Homo sapiens	30-46
21437903-5	2012	Exposure of cells to PA for 12 h increased insulin receptor (IR) and GLUT-4 levels in the plasma membrane.	Palmitic Acid	21-23	insulin receptor	Homo sapiens	43-64
22768670-7	2012	Tyrosine 818 falls in an exquisitely conserved residue of the alphabeta fibronectin domain of the insulin receptor, whose structure and function are much less well understood than other parts of the receptor.	Tyrosine	0-8	insulin receptor	Homo sapiens	98-114
22110065-6	2011	RESULTS: TNF-alpha-only treatments of Muller cells resulted in significant decreases of tyrosine phosphorylation of the insulin receptor and Akt in high-glucose conditions.	Tyrosine	88-96	insulin receptor	Homo sapiens	120-136
22110065-11	2011	By decreasing the levels of TNF-alpha and decreasing the phosphorylation of IRS-1(Ser307) while increasing tyrosine phosphorylation of insulin receptor, these results suggest a possible mechanism by which restoration of beta-adrenergic receptor signaling may protect the retina against diabetes-induced damage.	Tyrosine	107-115	insulin receptor	Homo sapiens	135-151
22110065-6	2011	RESULTS: TNF-alpha-only treatments of Muller cells resulted in significant decreases of tyrosine phosphorylation of the insulin receptor and Akt in high-glucose conditions.	Glucose	153-160	insulin receptor	Homo sapiens	120-136
22110065-7	2011	Salmeterol (10 muM), a beta-2-adrenergic receptor agonist, significantly increased phosphorylation of both insulin receptor and Akt.	Salmeterol Xinafoate	0-10	insulin receptor	Homo sapiens	107-123
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Nitrogen	4-5	insulin receptor	Homo sapiens	65-67
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Nitrogen	4-5	insulin receptor	Homo sapiens	93-95
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Amides	132-137	insulin receptor	Homo sapiens	65-67
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Amides	132-137	insulin receptor	Homo sapiens	93-95
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Hydrogen	138-147	insulin receptor	Homo sapiens	65-67
21880708-4	2011	All N-methylated analogues showed impaired binding affinities to IR, which suggests a direct IR-interacting role for the respective amide hydrogens.	Hydrogen	138-147	insulin receptor	Homo sapiens	93-95
21671008-6	2011	Importantly, alpha-PGG"s ability to elevate p53 was diminished by IR inhibitor and IR-siRNA, suggesting a non-conventional role of IR as being involved in p53 induction.	alphaPGG	13-22	insulin receptor	Homo sapiens	66-68
21841811-7	2011	RESULTS: Tunicamycin-induced chronic ER stress attenuated IR tyrosine phosphorylation in a time-dependent manner, whereas over-expression of ATF6 protected IR from desensitization.	Tunicamycin	9-20	insulin receptor	Homo sapiens	58-60
21841811-7	2011	RESULTS: Tunicamycin-induced chronic ER stress attenuated IR tyrosine phosphorylation in a time-dependent manner, whereas over-expression of ATF6 protected IR from desensitization.	Tyrosine	61-69	insulin receptor	Homo sapiens	58-60
21841811-9	2011	The treatment of the cells with a specific ERK inhibitor U0126 (10 mumol/L) mimicked the effect of ATF6 over-expression and restored the insulin-stimulated IR phosphorylation.	U 0126	57-62	insulin receptor	Homo sapiens	156-158
21671008-0	2011	Insulin receptor signaling activated by penta-O-galloyl-alpha-D: -glucopyranose induces p53 and apoptosis in cancer cells.	penta-o-galloyl-alpha-d	40-63	insulin receptor	Homo sapiens	0-16
21671008-0	2011	Insulin receptor signaling activated by penta-O-galloyl-alpha-D: -glucopyranose induces p53 and apoptosis in cancer cells.	Glucose	66-79	insulin receptor	Homo sapiens	0-16
21904878-4	2011	Pretreatment of beta-cells with HNMPA, an insulin receptor inhibitor, and AG1478, an epidermal growth factor receptor inhibitor, further increased the cAMP level and Erk phosphorylation in the presence of exendin-4 (exe-4), a GLP-1 agonist.	HNMPA	32-37	insulin receptor	Homo sapiens	42-58
21671008-6	2011	Importantly, alpha-PGG"s ability to elevate p53 was diminished by IR inhibitor and IR-siRNA, suggesting a non-conventional role of IR as being involved in p53 induction.	alphaPGG	13-22	insulin receptor	Homo sapiens	83-85
21671008-6	2011	Importantly, alpha-PGG"s ability to elevate p53 was diminished by IR inhibitor and IR-siRNA, suggesting a non-conventional role of IR as being involved in p53 induction.	alphaPGG	13-22	insulin receptor	Homo sapiens	83-85
21671008-7	2011	Further studies revealed that alpha-PGG activated MEK, a downstream signaling factor of IR.	alphaPGG	30-39	insulin receptor	Homo sapiens	88-90
21671008-10	2011	The unique activity of alpha-PGG, a novel IR phosphorylation and apoptosis inducer, may offer a new therapeutic strategy for eliciting apoptotic signal and inhibiting cancer growth.	alphaPGG	23-32	insulin receptor	Homo sapiens	42-44
21671008-4	2011	Specifically, natural compound penta-O-galloyl-alpha-D: -glucopyranose (alpha-PGG), a previously characterized IR signaling activator, induced apoptosis in RKO cells without significantly affecting its normal counterpart FHC cells.	beta-penta-O-galloyl-glucose	31-70	insulin receptor	Homo sapiens	111-113
21555852-5	2011	We found that phosphocreatine recovery after exercise, a measure of skeletal muscle mitochondrial function in vivo, was significantly slowed in patients with INSR mutations compared with that in healthy age-, fitness-, and BMI-matched controls.	Phosphocreatine	14-29	insulin receptor	Homo sapiens	158-162
21671008-4	2011	Specifically, natural compound penta-O-galloyl-alpha-D: -glucopyranose (alpha-PGG), a previously characterized IR signaling activator, induced apoptosis in RKO cells without significantly affecting its normal counterpart FHC cells.	alphaPGG	72-81	insulin receptor	Homo sapiens	111-113
21632854-2	2011	In this study, we describe GTx-134, a novel small-molecule inhibitor of IGF-1R and insulin receptor (IR) and characterized its antitumor activity in preclinical models of MM.	GTx 134	27-34	insulin receptor	Homo sapiens	83-104
21514293-4	2011	Telmisartan treatment dose-dependently increased (from 1 muM) protein expression of PPARgamma-regulated molecules such as fatty acid binding protein 4 (FABP4), insulin receptor, and glucose transporter 4 (GLUT4).	Telmisartan	0-11	insulin receptor	Homo sapiens	160-176
21354844-7	2011	In islets maintained at 5.5 mmol/L of glucose, insulin receptor (IR) expression was reduced by low RHI, while phosphatidylinositol-3 kinase p110-alpha (PI3K) was enhanced by both concentrations of glulisine and aspart, and by high RHI.	Glucose	38-45	insulin receptor	Homo sapiens	47-63
21354844-7	2011	In islets maintained at 5.5 mmol/L of glucose, insulin receptor (IR) expression was reduced by low RHI, while phosphatidylinositol-3 kinase p110-alpha (PI3K) was enhanced by both concentrations of glulisine and aspart, and by high RHI.	Glucose	38-45	insulin receptor	Homo sapiens	65-67
21354844-8	2011	In islets preexposed to high glucose, IR expression was increased by both concentrations of aspart and RHI, but not by glulisine.	Glucose	29-36	insulin receptor	Homo sapiens	38-40
21680660-5	2011	In order to obtain an unbiased evaluation of IR-A substrates differentially involved after IGF-II and insulin stimulation, we performed quantitative proteomics of IR-A substrates recruited to tyrosine-phosphorylated protein complexes using stable isotope labeling with amino acids in cell culture in combination with antiphosphotyrosine antibody pull down and mass spectrometry.	Tyrosine	192-200	insulin receptor	Homo sapiens	45-47
21680660-5	2011	In order to obtain an unbiased evaluation of IR-A substrates differentially involved after IGF-II and insulin stimulation, we performed quantitative proteomics of IR-A substrates recruited to tyrosine-phosphorylated protein complexes using stable isotope labeling with amino acids in cell culture in combination with antiphosphotyrosine antibody pull down and mass spectrometry.	Tyrosine	192-200	insulin receptor	Homo sapiens	163-165
21487008-10	2011	Moreover, we observed that substantial amounts of the uncleaved IR precursor reached the Tris-phosphorylated, fully activated form in an insulin independent fashion.	Tromethamine	89-93	insulin receptor	Homo sapiens	64-66
21597332-4	2011	Understanding how the IR/IGF-1R pathway functions in tumors is increasing in importance as the efficacy of drugs that target metabolic pathways, such as metformin, are investigated in prospective clinical trials.	Metformin	153-162	insulin receptor	Homo sapiens	22-24
21385891-8	2011	However, ganitumab in combination with rapamycin also resulted in a marked increase in INSR expression and activity in the SJSA-1 and A673 models.	Sirolimus	39-48	insulin receptor	Homo sapiens	87-91
21324373-0	2011	Expression and function of the insulin receptor in normal and osteoarthritic human chondrocytes: modulation of anabolic gene expression, glucose transport and GLUT-1 content by insulin.	Glucose	137-144	insulin receptor	Homo sapiens	31-47
21031461-8	2011	Further, the phosphorylation of insulin receptor was attenuated in response to insulin stimulation under high glucose conditions, and PJ34 could reverse this effect.	Glucose	110-117	insulin receptor	Homo sapiens	32-48
21205932-9	2011	Thus, we next investigated a biophysical mechanism by which insulin signaling could be disrupted and found that disruption of lipid microdomains via cholesterol depletion blocks insulin-induced Akt activation and reduces insulin receptor tyrosine phosphorylation.	Cholesterol	149-160	insulin receptor	Homo sapiens	221-237
21205932-9	2011	Thus, we next investigated a biophysical mechanism by which insulin signaling could be disrupted and found that disruption of lipid microdomains via cholesterol depletion blocks insulin-induced Akt activation and reduces insulin receptor tyrosine phosphorylation.	Tyrosine	238-246	insulin receptor	Homo sapiens	221-237
20971625-5	2011	In immortalized C-28/I2 chondrocytes, we showed that increasing concentrations of 17beta-estradiol diminished the 95kDa band of IR.	Estradiol	82-98	insulin receptor	Homo sapiens	128-130
21168390-7	2011	Results of the in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-alpha.	Tyrosine	24-32	insulin receptor	Homo sapiens	107-123
21168390-7	2011	Results of the in vitro tyrosine phosphorylation assay indicated that tyrosine phosphorylation of IRS-1 by insulin receptor was decreased when IRS-1 was contained in IRSomes prepared from 3T3-L1 adipocytes treated with TNF-alpha.	Tyrosine	70-78	insulin receptor	Homo sapiens	107-123
20938636-2	2011	Phosphorylation of TBC1 domain family, member 4 (TBC1D4) is at present the most distal insulin receptor signalling event linked to glucose transport.	Glucose	131-138	insulin receptor	Homo sapiens	87-103
21931226-0	2011	Recurrent hypoglycemia during pregnancies in a woman with multiple autoantibodies including anti-insulin receptor antibody and anti-platelet antibody, whose serum lowered murine blood glucose levels and phosphorylated insulin receptor of CHO-IR cells.	Glucose	184-191	insulin receptor	Homo sapiens	97-113
21411721-5	2011	We have previously shown that in N-nitrosomorpholine-induced hepatocarcinogenesis, insulin receptor substrate (IRS-1) is strongly expressed in GSF and reduced during progression to HCC, thus correlating with the glycogen content.	N-nitrosomorpholine	33-52	insulin receptor	Homo sapiens	83-99
21411721-5	2011	We have previously shown that in N-nitrosomorpholine-induced hepatocarcinogenesis, insulin receptor substrate (IRS-1) is strongly expressed in GSF and reduced during progression to HCC, thus correlating with the glycogen content.	Glycogen	212-220	insulin receptor	Homo sapiens	83-99
20674666-3	2010	In the blocking experiment, we found that Go6976, a kinase inhibitor that potently inhibit PKCmu/protein kinase D 1 (PKD1), effectively and specifically reduced the activity of BBR on InsR.	Go 6976	42-48	insulin receptor	Homo sapiens	184-188
21220496-10	2011	These data suggest that benzimidazole IGF-1R/InsR inhibitors may select for upregulation and be effluxed by the ATP-binding cassette transporter, BCRP, contributing to resistance.	benzimidazole	24-37	insulin receptor	Homo sapiens	45-49
20674666-5	2010	The role of PKD1 in InsR expression was also proved by using another PKD-activator oligomycin.	Oligomycins	83-93	insulin receptor	Homo sapiens	20-24
20674666-10	2010	These results suggest that the PKD family is involved in the transcriptional regulation of the InsR gene; we consider it to be a potential new target to discover drugs for sugar-related disorders in the future.	Sugars	172-177	insulin receptor	Homo sapiens	95-99
20835859-11	2010	Dose-dependency experiments showed that insulin glargine was able to phosphorylate the IGF-IR at fivefold lower doses than those required to activate the insulin receptor.	Insulin Glargine	48-56	insulin receptor	Homo sapiens	154-170
20674666-1	2010	Our previous studies proved that berberine (BBR) up-regulates the insulin receptor (InsR) gene by stimulating its promoter and calphostin C blocks this effect.	Berberine	33-42	insulin receptor	Homo sapiens	66-82
20674666-1	2010	Our previous studies proved that berberine (BBR) up-regulates the insulin receptor (InsR) gene by stimulating its promoter and calphostin C blocks this effect.	Berberine	33-42	insulin receptor	Homo sapiens	84-88
20674666-1	2010	Our previous studies proved that berberine (BBR) up-regulates the insulin receptor (InsR) gene by stimulating its promoter and calphostin C blocks this effect.	Berberine	44-47	insulin receptor	Homo sapiens	66-82
20674666-1	2010	Our previous studies proved that berberine (BBR) up-regulates the insulin receptor (InsR) gene by stimulating its promoter and calphostin C blocks this effect.	Berberine	44-47	insulin receptor	Homo sapiens	84-88
20521171-5	2010	Further analysis revealed her also to be heterozygous for a novel trinucleotide deletion (c.3659 + 1_3659 + 3delGTG) at the end of exon 20 of INSR, encoding the insulin receptor, leading to deletion of Trp1193 in the intracellular tyrosine kinase domain.	trinucleotide	66-79	insulin receptor	Homo sapiens	142-146
20521171-5	2010	Further analysis revealed her also to be heterozygous for a novel trinucleotide deletion (c.3659 + 1_3659 + 3delGTG) at the end of exon 20 of INSR, encoding the insulin receptor, leading to deletion of Trp1193 in the intracellular tyrosine kinase domain.	trinucleotide	66-79	insulin receptor	Homo sapiens	161-177
21063035-3	2010	Ethanol inhibition of insulin signaling is mediated at the insulin receptor (IR) level and caused by both impaired receptor binding and increased activation of phosphatases that reverse IR tyrosine kinase activity.	Ethanol	0-7	insulin receptor	Homo sapiens	59-75
21036152-8	2010	In CHO cells constitutively expressing human insulin receptor (CHO-IR), there was a concentration dependent increase of promoter activity by insulin in the presence of glucose.	Glucose	168-175	insulin receptor	Homo sapiens	45-61
20977462-10	2010	Curcumin suppressed the leptin-induced membrane translocation of GLUT4 by interrupting the insulin receptor substrates/phosphatidyl inositol 3-kinase/AKT signalling pathway.	Curcumin	0-8	insulin receptor	Homo sapiens	91-107
21063035-3	2010	Ethanol inhibition of insulin signaling is mediated at the insulin receptor (IR) level and caused by both impaired receptor binding and increased activation of phosphatases that reverse IR tyrosine kinase activity.	Ethanol	0-7	insulin receptor	Homo sapiens	77-79
20101100-1	2010	BACKGROUND: Protein tyrosine phosphatase (PTP)- 1B, encoded by the PTPN1 gene, negatively regulates insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase activation segment.	Phosphotyrosine	143-158	insulin receptor	Homo sapiens	175-191
20924128-11	2010	In tumor cells with an autocrine IGF-2 loop, both OSI-906 and an anti-IGF-2 antibody reduced phospho-IR/phospho-AKT, whereas MAB391 was ineffective.	silicon monoxide	50-53	insulin receptor	Homo sapiens	101-103
20924128-12	2010	Finally, OSI-906 showed superior efficacy compared with MAB391 in human tumor xenograft models in which both IGF-1R and IR were phosphorylated.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	9-16	insulin receptor	Homo sapiens	120-122
21537430-2	2010	It has been postulated that an increase in the intracellular concentration of fatty acid metabolites activates a serine kinase cascade, which leads to defects in insulin signaling downstream to the insulin receptor.	Fatty Acids	78-88	insulin receptor	Homo sapiens	198-214
24900240-0	2010	Discovery of an Orally Efficacious Imidazo[5,1-f][1,2,4]triazine Dual Inhibitor of IGF-1R and IR.	imidazo[5,1-f][1,2,4]triazine	35-64	insulin receptor	Homo sapiens	94-96
24900240-1	2010	This report describes the investigation of a series of 5,7-disubstituted imidazo[5,1-f][1,2,4]triazine inhibitors of insulin-like growth factor-1 receptor (IGF-1R) and insulin receptor (IR).	5,7-disubstituted imidazo[5,1-f][1,2,4]triazine	55-102	insulin receptor	Homo sapiens	168-184
24900240-1	2010	This report describes the investigation of a series of 5,7-disubstituted imidazo[5,1-f][1,2,4]triazine inhibitors of insulin-like growth factor-1 receptor (IGF-1R) and insulin receptor (IR).	5,7-disubstituted imidazo[5,1-f][1,2,4]triazine	55-102	insulin receptor	Homo sapiens	186-188
20519504-3	2010	We have previously demonstrated that both intron 10 and the alternatively spliced exon 11 contain regulatory sequences that affect insulin receptor splicing both positively and negatively and that these sequences bind the serine/arginine-rich (SR) proteins SRp20 and SF2/ASF and the CELF protein CUG-BP1.	Serine	222-228	insulin receptor	Homo sapiens	131-147
20352052-8	2010	Incubation of adult worms in vitro, both with a specific insulin receptor inhibitor and anti-SjIRs antibodies, resulted in a significant decrease in worm glucose levels, suggesting again the same function for SjIRs in regulating glucose uptake as described for mammalian cells.	Glucose	154-161	insulin receptor	Homo sapiens	57-73
20701717-2	2010	The complex metabolic abnormalities observed in CKD such as vitamin D deficiency, obesity, metabolic acidosis, inflammation, and accumulation of "uremic toxins" are believed to contribute to the etiology of IR and acquired defects in the insulin-receptor signaling pathway in this patient population.	Vitamin D	60-69	insulin receptor	Homo sapiens	238-254
20112420-1	2010	The insulin receptor (IR) is a homo-dimeric, disulfide-linked, membrane-spanning tyrosine kinase.	Disulfides	45-54	insulin receptor	Homo sapiens	4-20
20112420-1	2010	The insulin receptor (IR) is a homo-dimeric, disulfide-linked, membrane-spanning tyrosine kinase.	Disulfides	45-54	insulin receptor	Homo sapiens	22-24
20156067-2	2010	This suggests that either obesity or PCOS is associated with a defect in the coupling of the stimulation of the insulin receptor by insulin to the release of the DCI-IPG mediator.	dci-ipg	162-169	insulin receptor	Homo sapiens	112-128
20352052-8	2010	Incubation of adult worms in vitro, both with a specific insulin receptor inhibitor and anti-SjIRs antibodies, resulted in a significant decrease in worm glucose levels, suggesting again the same function for SjIRs in regulating glucose uptake as described for mammalian cells.	Glucose	229-236	insulin receptor	Homo sapiens	57-73
20209060-3	2010	The aim of this study was to characterize the glargine metabolites in vitro with regard to their insulin receptor (IR) and IGF-1 receptor (IGF1R) binding and signaling properties as well as their metabolic and mitogenic activities.	Insulin Glargine	46-54	insulin receptor	Homo sapiens	97-113
20209060-3	2010	The aim of this study was to characterize the glargine metabolites in vitro with regard to their insulin receptor (IR) and IGF-1 receptor (IGF1R) binding and signaling properties as well as their metabolic and mitogenic activities.	Insulin Glargine	46-54	insulin receptor	Homo sapiens	115-117
20209060-8	2010	CONCLUSIONS: The binding of insulin glargine and its metabolites M1 and M2 to the IR were similar and correlated well with their corresponding autophosphorylation and metabolic activities in vitro.	Insulin Glargine	36-44	insulin receptor	Homo sapiens	82-84
20049867-6	2010	Functional analysis suggested that genistein-regulated protein tyrosine phosphorylation mainly by inhibiting the activity of tyrosine kinase EGFR, PDGFR, insulin receptor, Abl, Fgr, Itk, Fyn and Src.	Tyrosine	63-71	insulin receptor	Homo sapiens	154-170
19862665-10	2010	Long-term (48 h) stimulation of HUVECs with high glucose augmented expression of the insulin receptor and E-selectin, but downregulated COUP-TFII protein expression.	Glucose	49-56	insulin receptor	Homo sapiens	85-101
19800084-0	2010	Berberine lowers blood glucose in type 2 diabetes mellitus patients through increasing insulin receptor expression.	Berberine	0-9	insulin receptor	Homo sapiens	87-103
19800084-0	2010	Berberine lowers blood glucose in type 2 diabetes mellitus patients through increasing insulin receptor expression.	Blood Glucose	17-30	insulin receptor	Homo sapiens	87-103
19879930-8	2010	MCF-7 cells exposed to HCB (0.005 and 0.05 microM) overexpressed IGF-IR and insulin receptor (IR).	Hexachlorobenzene	23-26	insulin receptor	Homo sapiens	76-92
19879930-8	2010	MCF-7 cells exposed to HCB (0.005 and 0.05 microM) overexpressed IGF-IR and insulin receptor (IR).	Hexachlorobenzene	23-26	insulin receptor	Homo sapiens	69-71
19800084-1	2010	Our previous work demonstrated that berberine (BBR) increases insulin receptor (InsR) expression and improves glucose utility both in vitro and in animal models.	Berberine	36-45	insulin receptor	Homo sapiens	62-78
19800084-1	2010	Our previous work demonstrated that berberine (BBR) increases insulin receptor (InsR) expression and improves glucose utility both in vitro and in animal models.	Berberine	36-45	insulin receptor	Homo sapiens	80-84
19800084-1	2010	Our previous work demonstrated that berberine (BBR) increases insulin receptor (InsR) expression and improves glucose utility both in vitro and in animal models.	Berberine	47-50	insulin receptor	Homo sapiens	62-78
19800084-1	2010	Our previous work demonstrated that berberine (BBR) increases insulin receptor (InsR) expression and improves glucose utility both in vitro and in animal models.	Berberine	47-50	insulin receptor	Homo sapiens	80-84
19800084-4	2010	Accordingly, insulin-stimulated phosphorylations of InsR beta-subunit and Akt were increased after BBR treatment in cultured cells.	Berberine	99-102	insulin receptor	Homo sapiens	52-56
19800084-10	2010	Our results confirmed the activity of BBR on InsR in humans and its relationship with the glucose-lowering effect.	Glucose	90-97	insulin receptor	Homo sapiens	45-49
19887566-9	2010	Thus, a sustained elevation of insulin levels diminishes neuronal insulin signaling through mTOR-S6K1-mediated IRS-1 serine phosphorylation, proteasomal degradation of IRS-1 and lysosomal degradation of the IR.	Serine	117-123	insulin receptor	Homo sapiens	111-113
20190490-4	2010	Intravenous boluses of cyclophosphamide (IVCY) with oral prednisolone and cyclosporin A induced remission of SLE, and a subsequent disappearance of anti-insulin receptor autoantibodies, followed by a recovery of glucose intolerance.	Cyclophosphamide	23-39	insulin receptor	Homo sapiens	153-169
19895792-2	2010	An insulin time course revealed that rapidly induced tyrosine phosphorylation of IR was steadily maintained over a 180 min time period.	Tyrosine	53-61	insulin receptor	Homo sapiens	81-83
19887566-0	2010	Central insulin signaling is attenuated by long-term insulin exposure via insulin receptor substrate-1 serine phosphorylation, proteasomal degradation, and lysosomal insulin receptor degradation.	Serine	103-109	insulin receptor	Homo sapiens	74-90
19887566-8	2010	The proteasomal inhibitor epoxomicin and the lysosomal pathway inhibitor 3-methyladenine prevented the degradation of IRS-1 and IR by insulin, respectively, and pretreatment with rapamycin, epoxomicin, or 3-methyladenine prevented attenuation of insulin signaling by long-term insulin exposure.	epoxomicin	26-36	insulin receptor	Homo sapiens	118-120
19887566-8	2010	The proteasomal inhibitor epoxomicin and the lysosomal pathway inhibitor 3-methyladenine prevented the degradation of IRS-1 and IR by insulin, respectively, and pretreatment with rapamycin, epoxomicin, or 3-methyladenine prevented attenuation of insulin signaling by long-term insulin exposure.	3-methyladenine	73-88	insulin receptor	Homo sapiens	118-120
19887566-8	2010	The proteasomal inhibitor epoxomicin and the lysosomal pathway inhibitor 3-methyladenine prevented the degradation of IRS-1 and IR by insulin, respectively, and pretreatment with rapamycin, epoxomicin, or 3-methyladenine prevented attenuation of insulin signaling by long-term insulin exposure.	epoxomicin	190-200	insulin receptor	Homo sapiens	118-120
19887566-8	2010	The proteasomal inhibitor epoxomicin and the lysosomal pathway inhibitor 3-methyladenine prevented the degradation of IRS-1 and IR by insulin, respectively, and pretreatment with rapamycin, epoxomicin, or 3-methyladenine prevented attenuation of insulin signaling by long-term insulin exposure.	3-methyladenine	205-220	insulin receptor	Homo sapiens	118-120
20829623-4	2010	In particular, glucocorticoid excess stimulates the expression of several key enzymes involved in the process of gluconeogenesis, with a consequent increase of glucose production, and induces an impairment of insulin sensitivity either directly by interfering with the insulin receptor signaling pathway or indirectly, through the stimulation of lipolysis and proteolysis and the consequent increase of fatty acids and amino acids, which contribute to the development of insulin resistance.	Fatty Acids	403-414	insulin receptor	Homo sapiens	269-285
20190490-4	2010	Intravenous boluses of cyclophosphamide (IVCY) with oral prednisolone and cyclosporin A induced remission of SLE, and a subsequent disappearance of anti-insulin receptor autoantibodies, followed by a recovery of glucose intolerance.	ivcy	41-45	insulin receptor	Homo sapiens	153-169
20190490-4	2010	Intravenous boluses of cyclophosphamide (IVCY) with oral prednisolone and cyclosporin A induced remission of SLE, and a subsequent disappearance of anti-insulin receptor autoantibodies, followed by a recovery of glucose intolerance.	Prednisolone	57-69	insulin receptor	Homo sapiens	153-169
20190490-4	2010	Intravenous boluses of cyclophosphamide (IVCY) with oral prednisolone and cyclosporin A induced remission of SLE, and a subsequent disappearance of anti-insulin receptor autoantibodies, followed by a recovery of glucose intolerance.	Cyclosporine	74-87	insulin receptor	Homo sapiens	153-169
20137666-4	2009	Furthermore, HUVEC was pretreated with hydroxy-2-naphthalenylmethylphosphonic acid trisacetoxymethyl ester (HNMPA-(AM)3), a specific inhibitor of IR followed by visfatin (100 ng/ml) treatment.	hydroxy-2-naphthalenyl-methyl phosphonic acid trisacetoxymethylester	39-106	insulin receptor	Homo sapiens	146-148
19665448-5	2009	We used a cell-based assay measuring IGF-1R autophosphorylation as an inhibitor screen, and identified a potent purine derivative that is selective compared to IR.	purine	112-118	insulin receptor	Homo sapiens	160-162
19834685-3	2009	RESULTS: While the kinetics of insulin receptor endocytosis after the administration of arginyl-insulins were similar to those observed using human insulin, a more prolonged concentration of endosomal insulin receptor was observed in response to [Arg(A0)]-HI.	Arginine	247-250	insulin receptor	Homo sapiens	201-217
19834685-4	2009	[Arg(A0)]-HI induced a marked increase in the phosphotyrosine content of endosomal insulin receptor, coinciding with a more sustained endosomal association of growth factor receptor-bound protein 14 (GRB14), and a higher and prolonged activation of mitogen-activated protein kinase pathways.	Arginine	1-4	insulin receptor	Homo sapiens	83-99
19834685-4	2009	[Arg(A0)]-HI induced a marked increase in the phosphotyrosine content of endosomal insulin receptor, coinciding with a more sustained endosomal association of growth factor receptor-bound protein 14 (GRB14), and a higher and prolonged activation of mitogen-activated protein kinase pathways.	Histidine	9-12	insulin receptor	Homo sapiens	83-99
19834685-4	2009	[Arg(A0)]-HI induced a marked increase in the phosphotyrosine content of endosomal insulin receptor, coinciding with a more sustained endosomal association of growth factor receptor-bound protein 14 (GRB14), and a higher and prolonged activation of mitogen-activated protein kinase pathways.	Phosphotyrosine	46-61	insulin receptor	Homo sapiens	83-99
19834685-9	2009	The endosomal conversion of [Arg(A0)]-HI into human insulin might extend the insulin receptor signalling at this locus.	arg(a0)	29-36	insulin receptor	Homo sapiens	77-93
19834685-9	2009	The endosomal conversion of [Arg(A0)]-HI into human insulin might extend the insulin receptor signalling at this locus.	Histidine	37-40	insulin receptor	Homo sapiens	77-93
20137666-4	2009	Furthermore, HUVEC was pretreated with hydroxy-2-naphthalenylmethylphosphonic acid trisacetoxymethyl ester (HNMPA-(AM)3), a specific inhibitor of IR followed by visfatin (100 ng/ml) treatment.	hydroxy-2-naphthalenyl-methyl phosphonic acid trisacetoxymethylester	108-119	insulin receptor	Homo sapiens	146-148
19170714-9	2009	RESULTS: Elevated serum insulin and insulin : C-peptide ratios were found in the proband, the father and one of the twin brothers, carried a heterozygous missense mutation of Arginine1174Tryptophan (R1174W) in exon20 of the IR gene.	arginine1174tryptophan	175-197	insulin receptor	Homo sapiens	224-226
19910497-5	2009	LAR reduces tyrosine phosphorylation of the insulin receptor, in turn leading to decreased phosphorylation of the adaptor protein IRS-1 and its downstream molecule Akt (also known as PKB).	Tyrosine	12-20	insulin receptor	Homo sapiens	44-60
19895792-6	2010	As caveolin-2 tyrosine mutants were examined, Y27A-caveolin-2 explicitly impeded the long term IR activation by insulin, enhanced tyrosine dephosphorylation of IR, impaired tyrosine phosphorylation of IRS-1, and exerted the interaction between activated IR and SOCS-3.	Tyrosine	14-22	insulin receptor	Homo sapiens	95-97
19283340-0	2009	Chromium improves glucose uptake and metabolism through upregulating the mRNA levels of IR, GLUT4, GS, and UCP3 in skeletal muscle cells.	Chromium	0-8	insulin receptor	Homo sapiens	88-90
19283340-4	2009	Collectively, results of this study demonstrate that chromium improves glucose uptake and metabolism through upregulating the mRNA levels of IR, GLUT4, GS, and UCP3 in skeletal muscle cells, and CrSP has higher efficacy on glucose uptake and metabolism compared to the forms of CrCl and CrPic.	Chromium	53-61	insulin receptor	Homo sapiens	141-143
19690174-6	2009	This is associated with a decrease in glucose-stimulated phosphorylation of key proteins in the insulin signaling pathway including Akt, AS160, and other Akt substrates, ERK as well as the insulin receptor.	Glucose	38-45	insulin receptor	Homo sapiens	189-205
21099275-0	2009	Insulin receptor signaling for the proliferation of pancreatic beta-cells: involvement of Ca2+ second messengers, IP3, NAADP and cADPR.	Inositol 1,4,5-Trisphosphate	114-117	insulin receptor	Homo sapiens	0-16
21099275-0	2009	Insulin receptor signaling for the proliferation of pancreatic beta-cells: involvement of Ca2+ second messengers, IP3, NAADP and cADPR.	NAADP	119-124	insulin receptor	Homo sapiens	0-16
21099275-2	2009	Herein, we show the insulin receptor signaling pathway underlying CD38/ADPR-cyclase activation for NAADP/cADPR formation to induce Ca2+ rise, ultimately resulting in beta-cell proliferation.	NAADP	99-104	insulin receptor	Homo sapiens	20-36
21099275-8	2009	In conclusion, insulin receptor signaling in beta-cells employs three Ca (2+) signaling messengers, IP3, NAADP, and cADPR through a complex but concerted action of signaling molecules for Ca2+ signaling, which is involved in the proliferation of the islets.	Inositol 1,4,5-Trisphosphate	100-103	insulin receptor	Homo sapiens	15-31
21099275-8	2009	In conclusion, insulin receptor signaling in beta-cells employs three Ca (2+) signaling messengers, IP3, NAADP, and cADPR through a complex but concerted action of signaling molecules for Ca2+ signaling, which is involved in the proliferation of the islets.	NAADP	105-110	insulin receptor	Homo sapiens	15-31
19662499-0	2009	Sphingosine 1-phosphate increases glucose uptake through trans-activation of insulin receptor.	sphingosine 1-phosphate	0-23	insulin receptor	Homo sapiens	77-93
19800225-0	2009	Synthesis and biological evaluation of berberine analogues as novel up-regulators for both low-density-lipoprotein receptor and insulin receptor.	Berberine	39-48	insulin receptor	Homo sapiens	128-144
19800225-1	2009	Berberine (BBR) is a natural compound with up-regulating activity on both low-density-lipoprotein receptor (LDLR) and insulin receptor (InsR).	Berberine	0-9	insulin receptor	Homo sapiens	118-134
19800225-1	2009	Berberine (BBR) is a natural compound with up-regulating activity on both low-density-lipoprotein receptor (LDLR) and insulin receptor (InsR).	Berberine	0-9	insulin receptor	Homo sapiens	136-140
19800225-1	2009	Berberine (BBR) is a natural compound with up-regulating activity on both low-density-lipoprotein receptor (LDLR) and insulin receptor (InsR).	Berberine	11-14	insulin receptor	Homo sapiens	118-134
19800225-1	2009	Berberine (BBR) is a natural compound with up-regulating activity on both low-density-lipoprotein receptor (LDLR) and insulin receptor (InsR).	Berberine	11-14	insulin receptor	Homo sapiens	136-140
19433058-0	2009	Inhibition of cholesterol biosynthesis disrupts lipid raft/caveolae and affects insulin receptor activation in 3T3-L1 preadipocytes.	Cholesterol	14-25	insulin receptor	Homo sapiens	80-96
19662499-0	2009	Sphingosine 1-phosphate increases glucose uptake through trans-activation of insulin receptor.	Glucose	34-41	insulin receptor	Homo sapiens	77-93
21425998-0	2009	Discovery of OSI-906: a selective and orally efficacious dual inhibitor of the IGF-1 receptor and insulin receptor.	3-(8-amino-1-(2-phenylquinolin-7-yl)imidazo(1,5-a)pyrazin-3-yl)-1-methylcyclobutanol	13-20	insulin receptor	Homo sapiens	98-114
21425998-3	2009	RESULTS: Our lead optimization efforts that blended structure-based design and empirical medicinal chemistry led to the discovery of OSI-906, a novel small-molecule dual IGF-1R/insulin receptor (IR) kinase inhibitor.	silicon monoxide	133-136	insulin receptor	Homo sapiens	177-193
19575453-7	2009	In hepatocytes, insulin-stimulated glycogen synthesis and insulin-dependent phosphorylation of Akt-kinase were attenuated synergistically by prior incubation with IL-6 and/or PGE(2) while insulin receptor autophosphorylation was barely affected.	Prostaglandins E	175-178	insulin receptor	Homo sapiens	188-204
19575453-13	2009	Since different molecular mechanisms appear to be employed, PGE(2) may synergize with IL-6, which interrupted the insulin receptor signal chain, principally by an induction of SOCS, namely SOCS3.	Prostaglandins E	60-63	insulin receptor	Homo sapiens	114-130
19679549-0	2009	Metformin disrupts crosstalk between G protein-coupled receptor and insulin receptor signaling systems and inhibits pancreatic cancer growth.	Metformin	0-9	insulin receptor	Homo sapiens	68-84
19679549-4	2009	Here, we determined whether metformin disrupts the crosstalk between insulin receptor and GPCR signaling in pancreatic cancer cells.	Metformin	28-37	insulin receptor	Homo sapiens	69-85
19497338-4	2009	In addition, using active insulin receptor (IR) and synthetic biotinylated PHB peptide (PHB(107-121)) we have shown that IR also phosphorylates Tyr 114 in an in vitro kinase assay.	Tyrosine	144-147	insulin receptor	Homo sapiens	26-42
19763027-3	2009	On 250 Pa polyacrylamide gel (soft gel) laminated with a mixture of collagen type 1 and fibronectin, whose rigidity matches that of adipose tissue, expression of the insulin receptor, IRS-1 and AKT was upregulated and their insulin-stimulated phosphorylation was enhanced.	polyacrylamide	10-24	insulin receptor	Homo sapiens	166-182
19642985-1	2009	Structure and activity relationship of a prenylindole moiety to insulin receptor activation.	prenylindole	41-53	insulin receptor	Homo sapiens	64-80
19642985-5	2009	METHODS: A series of hydroxyfuroic acid compounds were synthesized and tested for their efficacies at activating human insulin receptor.	2-Furancarboxylic acid, 3-hydroxy-	21-39	insulin receptor	Homo sapiens	119-135
19642985-7	2009	RESULT AND CONCLUSION: This study reports a new non-quinone DMAQ B1 derivative, a hydroxyfuroic acid compound (D-410639), which is 128 fold less cytotoxic as DMAQ B1 and as potent as compound 2, a DMAQ B1 synthetic derivative from Merck, at activating human insulin receptor.	quinone	52-59	insulin receptor	Homo sapiens	258-274
19642985-7	2009	RESULT AND CONCLUSION: This study reports a new non-quinone DMAQ B1 derivative, a hydroxyfuroic acid compound (D-410639), which is 128 fold less cytotoxic as DMAQ B1 and as potent as compound 2, a DMAQ B1 synthetic derivative from Merck, at activating human insulin receptor.	dmaq	60-64	insulin receptor	Homo sapiens	258-274
19642985-7	2009	RESULT AND CONCLUSION: This study reports a new non-quinone DMAQ B1 derivative, a hydroxyfuroic acid compound (D-410639), which is 128 fold less cytotoxic as DMAQ B1 and as potent as compound 2, a DMAQ B1 synthetic derivative from Merck, at activating human insulin receptor.	2-Furancarboxylic acid, 3-hydroxy-	82-100	insulin receptor	Homo sapiens	258-274
19642985-9	2009	Structure and activity relationship of the prenylindole moiety to insulin receptor activation is discussed.	prenylindole	43-55	insulin receptor	Homo sapiens	66-82
19497423-4	2009	Similar to insulin, actin also induced autophosphorylation at tyrosines 1158, 1162 and 1163 in the catalytic loop of IR.	Tyrosine	62-71	insulin receptor	Homo sapiens	117-119
19497338-4	2009	In addition, using active insulin receptor (IR) and synthetic biotinylated PHB peptide (PHB(107-121)) we have shown that IR also phosphorylates Tyr 114 in an in vitro kinase assay.	Tyrosine	144-147	insulin receptor	Homo sapiens	121-123
19383820-7	2009	RESULTS: GSK1904529A selectively inhibits IGF-IR and IR with IC(50)s of 27 and 25 nmol/L, respectively.	GSK1904529A	9-20	insulin receptor	Homo sapiens	46-48
19402072-8	2009	Possible mechanisms include the loss of feedback inhibition of insulin receptor substate/PI3K signaling resulting from the inhibition of mTOR complex 1 by rapamycin analogs and the activating phosphorylation of Akt by mTOR complex 2.	Sirolimus	155-164	insulin receptor	Homo sapiens	63-79
19221977-10	2009	Activation of the muscle insulin receptor was increased by 140% with glucose ingestion (Pre 0.62+/-0.12; Post 1.49+/-0.35), but pinitol did not influence this response.	Glucose	69-76	insulin receptor	Homo sapiens	25-41
19277985-0	2009	Insulin receptor kinase-independent signaling via tyrosine phosphorylation of phosphatase PHLPP1.	Tyrosine	50-58	insulin receptor	Homo sapiens	0-16
19293728-9	2009	Fenoldopam also inhibited insulin receptor mRNA and protein expression, which was time dependent and concentration dependent.	Fenoldopam	0-10	insulin receptor	Homo sapiens	26-42
19293728-10	2009	A PKC or MAP kinase inhibitor blocked the inhibitory effect of fenoldopam on insulin receptor expression, indicating that PKC and MAP kinase were involved in the signaling pathway.	Fenoldopam	63-73	insulin receptor	Homo sapiens	77-93
19206072-0	2009	Synthetic pentapeptides inhibiting autophosphorylation of insulin receptor in a non-ATP-competitive mechanism.	Adenosine Triphosphate	84-87	insulin receptor	Homo sapiens	58-74
19384726-6	2009	For example, in a model of metabolic disease with type II diabetes, proteolytic cleavage of the insulin receptor causes the inability of insulin to signal glucose transport across membranes.	Glucose	155-162	insulin receptor	Homo sapiens	96-112
19093871-0	2009	Antibody-mediated targeting of siRNA via the human insulin receptor using avidin-biotin technology.	avidin-biotin	74-87	insulin receptor	Homo sapiens	51-67
19303901-4	2009	More complex glycosphingolipids, so-called gangliosides, block phosphorylation of the insulin receptor and down-stream signaling, possibly by exclusion of the insulin receptor from specific membrane domains.	Glycosphingolipids	13-31	insulin receptor	Homo sapiens	86-102
19303901-4	2009	More complex glycosphingolipids, so-called gangliosides, block phosphorylation of the insulin receptor and down-stream signaling, possibly by exclusion of the insulin receptor from specific membrane domains.	Glycosphingolipids	13-31	insulin receptor	Homo sapiens	159-175
19303901-4	2009	More complex glycosphingolipids, so-called gangliosides, block phosphorylation of the insulin receptor and down-stream signaling, possibly by exclusion of the insulin receptor from specific membrane domains.	Gangliosides	43-55	insulin receptor	Homo sapiens	86-102
19303901-4	2009	More complex glycosphingolipids, so-called gangliosides, block phosphorylation of the insulin receptor and down-stream signaling, possibly by exclusion of the insulin receptor from specific membrane domains.	Gangliosides	43-55	insulin receptor	Homo sapiens	159-175
19150387-4	2009	The molecular mechanisms involved have not been completely identified, but the role of serine/threonine phosphorylation of the IR and IRS-1 proteins in desensitization of insulin action has been well established.	Serine	87-93	insulin receptor	Homo sapiens	127-129
19150387-4	2009	The molecular mechanisms involved have not been completely identified, but the role of serine/threonine phosphorylation of the IR and IRS-1 proteins in desensitization of insulin action has been well established.	Threonine	94-103	insulin receptor	Homo sapiens	127-129
19318401-10	2009	High-dose of corticosteroids, chloroquine and cyclophosphamide therapy had resulted in remission of hypoglycaemia associated with resolution of circulating antibodies to insulin and insulin receptor, and improvement in clinical and laboratory features of SLE.	Chloroquine	30-41	insulin receptor	Homo sapiens	182-198
19318401-10	2009	High-dose of corticosteroids, chloroquine and cyclophosphamide therapy had resulted in remission of hypoglycaemia associated with resolution of circulating antibodies to insulin and insulin receptor, and improvement in clinical and laboratory features of SLE.	Cyclophosphamide	46-62	insulin receptor	Homo sapiens	182-198
19381127-2	2009	Both events inhibit insulin receptor and IRS-1 (insulin receptor substrate) tyrosine phosphorylation.	Tyrosine	76-84	insulin receptor	Homo sapiens	48-64
19164855-4	2009	Here we show that humans with generalized insulin resistance caused by either mutations in the insulin receptor gene or inhibitory antibodies specific for the insulin receptor uniformly exhibited low serum TG and normal HDL cholesterol levels.	Triglycerides	206-208	insulin receptor	Homo sapiens	95-111
19164855-4	2009	Here we show that humans with generalized insulin resistance caused by either mutations in the insulin receptor gene or inhibitory antibodies specific for the insulin receptor uniformly exhibited low serum TG and normal HDL cholesterol levels.	Triglycerides	206-208	insulin receptor	Homo sapiens	159-175
19164855-4	2009	Here we show that humans with generalized insulin resistance caused by either mutations in the insulin receptor gene or inhibitory antibodies specific for the insulin receptor uniformly exhibited low serum TG and normal HDL cholesterol levels.	Cholesterol	224-235	insulin receptor	Homo sapiens	159-175
19251034-1	2009	Binding of insulin to the insulin receptor (IR) leads to a cascade of intracellular signaling events, which regulate multiple biological processes such as glucose and lipid metabolism, gene expression, protein synthesis, and cell growth, division, and survival.	Glucose	155-162	insulin receptor	Homo sapiens	26-42
19079291-8	2009	It also diminished insulin-stimulated tyrosine phosphorylation of IRS-1 and serine phosphorylation of Akt without affecting the phosphorylation of IR, ERK1/2, p38, and JNK.	Tyrosine	38-46	insulin receptor	Homo sapiens	66-68
18834871-1	2009	BACKGROUND: The present study was designed to assess the effect of sex steroids (testosterone and 17beta-estradiol) on insulin receptor expression, insulin binding and glucose oxidation in human liver cell line.	Steroids	71-79	insulin receptor	Homo sapiens	119-135
18834871-1	2009	BACKGROUND: The present study was designed to assess the effect of sex steroids (testosterone and 17beta-estradiol) on insulin receptor expression, insulin binding and glucose oxidation in human liver cell line.	Testosterone	81-93	insulin receptor	Homo sapiens	119-135
18834871-1	2009	BACKGROUND: The present study was designed to assess the effect of sex steroids (testosterone and 17beta-estradiol) on insulin receptor expression, insulin binding and glucose oxidation in human liver cell line.	Estradiol	98-114	insulin receptor	Homo sapiens	119-135
18834871-4	2009	RESULTS: Both testosterone and 17beta-estradiol significantly increased the insulin receptor mRNA expression, cell surface insulin binding and (14)C-glucose oxidation compared to basal, but the increase was not at par with the effect of insulin.	Testosterone	14-26	insulin receptor	Homo sapiens	76-92
18834871-4	2009	RESULTS: Both testosterone and 17beta-estradiol significantly increased the insulin receptor mRNA expression, cell surface insulin binding and (14)C-glucose oxidation compared to basal, but the increase was not at par with the effect of insulin.	Estradiol	31-47	insulin receptor	Homo sapiens	76-92
18834871-6	2009	CONCLUSION: It is concluded from the present study that testosterone and 17beta-estradiol can directly enhance insulin receptor mRNA expression, insulin binding and glucose oxidation in Chang liver cells and thereby glucose metabolism.	Testosterone	56-68	insulin receptor	Homo sapiens	111-127
18834871-6	2009	CONCLUSION: It is concluded from the present study that testosterone and 17beta-estradiol can directly enhance insulin receptor mRNA expression, insulin binding and glucose oxidation in Chang liver cells and thereby glucose metabolism.	Estradiol	73-89	insulin receptor	Homo sapiens	111-127
18984735-6	2009	In 3T3-L1 adipocytes, this inhibition of insulin receptor phosphorylation is followed by a decrease in the phosphorylation state of protein kinase B and AS160, as well as an inhibition of glucose transport in response to insulin.	Glucose	188-195	insulin receptor	Homo sapiens	41-57
18972094-5	2009	RESULTS: Following combined thiazolidinedione-metformin therapy, increases in glucose disposal and increases in sub-maximal and maximal insulin-induced activities of all four muscle signalling factors, IR, IRS-1-dependent PI3K (IRS-1/PI3K), aPKC and PKBbeta, were observed.	2,4-thiazolidinedione	28-45	insulin receptor	Homo sapiens	202-204
18972094-5	2009	RESULTS: Following combined thiazolidinedione-metformin therapy, increases in glucose disposal and increases in sub-maximal and maximal insulin-induced activities of all four muscle signalling factors, IR, IRS-1-dependent PI3K (IRS-1/PI3K), aPKC and PKBbeta, were observed.	Metformin	46-55	insulin receptor	Homo sapiens	202-204
18972094-8	2009	CONCLUSIONS/INTERPRETATION: Combined thiazolidinedione-metformin treatment markedly improves sub-maximal and maximal insulin signalling to IR, IRS-1/PI3K, aPKC and PKBbeta in type 2 diabetic muscle.	2,4-thiazolidinedione	37-54	insulin receptor	Homo sapiens	139-141
18972094-8	2009	CONCLUSIONS/INTERPRETATION: Combined thiazolidinedione-metformin treatment markedly improves sub-maximal and maximal insulin signalling to IR, IRS-1/PI3K, aPKC and PKBbeta in type 2 diabetic muscle.	Metformin	55-64	insulin receptor	Homo sapiens	139-141
19145584-10	2009	Furthermore, glargine induced both insulin receptor (IR) and IGF-IR phosphorylation.	Insulin Glargine	13-21	insulin receptor	Homo sapiens	35-56
18983503-5	2009	Insulin induced Tyr phosphorylation of the insulin receptor (INS-R) and formation of an INS-R - G(i)alpha(2) complex, suggesting interference with LPS-induced cAMP control.	Tyrosine	16-19	insulin receptor	Homo sapiens	43-59
19251034-1	2009	Binding of insulin to the insulin receptor (IR) leads to a cascade of intracellular signaling events, which regulate multiple biological processes such as glucose and lipid metabolism, gene expression, protein synthesis, and cell growth, division, and survival.	Glucose	155-162	insulin receptor	Homo sapiens	44-46
19251044-4	2009	IRS-proteins are insulin receptor substrates that mediate insulin signaling via multiple tyrosyl phosphorylations.	cyclo(tyrosyl-tyrosyl)	89-96	insulin receptor	Homo sapiens	17-33
18925540-1	2008	Tyrosine phosphorylation of the insulin receptor is the initial event following receptor binding to insulin, and it induces further tyrosine phosphorylation of various intracellular molecules.	Tyrosine	0-8	insulin receptor	Homo sapiens	32-48
19251051-4	2009	In this study, we examined the IR signaling in sorbitol-induced hyperosmotic stressed retinas.	Sorbitol	47-55	insulin receptor	Homo sapiens	31-33
19074892-10	2008	Beyond this, P-IGF-IR/IR could be a predictive marker for response to IGF-IR and/or IR-targeted therapies, as these inhibitors may be of benefit in all breast cancer subtypes including those with acquired resistance to tamoxifen.	Tamoxifen	219-228	insulin receptor	Homo sapiens	19-21
19074892-10	2008	Beyond this, P-IGF-IR/IR could be a predictive marker for response to IGF-IR and/or IR-targeted therapies, as these inhibitors may be of benefit in all breast cancer subtypes including those with acquired resistance to tamoxifen.	Tamoxifen	219-228	insulin receptor	Homo sapiens	22-24
19436651-4	2009	There is emerging evidence that early stages of INSR may be characterized by increased basal nitric oxide activity and increased activity of non-NO vasodilators such as endothelial derived hyperpolarization factor (EDHF) which is manifest by reduced arterial stiffness.	Nitric Oxide	93-105	insulin receptor	Homo sapiens	48-52
19436651-4	2009	There is emerging evidence that early stages of INSR may be characterized by increased basal nitric oxide activity and increased activity of non-NO vasodilators such as endothelial derived hyperpolarization factor (EDHF) which is manifest by reduced arterial stiffness.	edhf	215-219	insulin receptor	Homo sapiens	48-52
18925540-1	2008	Tyrosine phosphorylation of the insulin receptor is the initial event following receptor binding to insulin, and it induces further tyrosine phosphorylation of various intracellular molecules.	Tyrosine	132-140	insulin receptor	Homo sapiens	32-48
18500459-4	2008	Her symptoms responded well to the therapy of predonisolone (30 mg/day) and continuous intravenous glucose as anti-insulin receptor antibody became negative.	Glucose	99-106	insulin receptor	Homo sapiens	115-131
18768589-7	2008	A small inhibiting RNA against insulin receptor significantly blocked visfatin-mediated glucose uptake.	Glucose	88-95	insulin receptor	Homo sapiens	31-47
18940392-1	2008	This study assessed the relationships of urinary D-chiro-inositol and myo-inositol excretions to indices of whole-body glucose tolerance and total content and tyrosine phosphorylation of the insulin receptor (activation) in skeletal muscle of older nondiabetic subjects.	Tyrosine	159-167	insulin receptor	Homo sapiens	191-207
18940392-6	2008	Urinary D-chiro-inositol (rho = -0.60, P &lt; or = .05) and myo-inositol (rho = -0.60, P &lt; or = .05) were inversely related to tyrosine phosphorylation of the insulin receptor (phosphotyrosine 1162/1163), but not total content of the insulin receptor during the OGTT.	Inositol	8-24	insulin receptor	Homo sapiens	162-178
18940392-6	2008	Urinary D-chiro-inositol (rho = -0.60, P &lt; or = .05) and myo-inositol (rho = -0.60, P &lt; or = .05) were inversely related to tyrosine phosphorylation of the insulin receptor (phosphotyrosine 1162/1163), but not total content of the insulin receptor during the OGTT.	Inositol	8-24	insulin receptor	Homo sapiens	237-253
18940392-6	2008	Urinary D-chiro-inositol (rho = -0.60, P &lt; or = .05) and myo-inositol (rho = -0.60, P &lt; or = .05) were inversely related to tyrosine phosphorylation of the insulin receptor (phosphotyrosine 1162/1163), but not total content of the insulin receptor during the OGTT.	Inositol	60-72	insulin receptor	Homo sapiens	162-178
18940392-6	2008	Urinary D-chiro-inositol (rho = -0.60, P &lt; or = .05) and myo-inositol (rho = -0.60, P &lt; or = .05) were inversely related to tyrosine phosphorylation of the insulin receptor (phosphotyrosine 1162/1163), but not total content of the insulin receptor during the OGTT.	Inositol	60-72	insulin receptor	Homo sapiens	237-253
18855718-4	2008	At early intracellular level angiotensin II acts on JAK-2/IRS1-IRS2/PI3-kinase, JNK and ERK to phosphorylate serine residues of key elements of insulin signaling pathway therefore inhibiting signaling by the insulin receptor.	Serine	109-115	insulin receptor	Homo sapiens	208-224
18585815-4	2008	Regarding the metabolic signalling, glargine and insulin-induced comparable dose-dependent phosphorylation of insulin receptor, IRS-1, Akt, and GSK3, whereas detemir-induced kinetics were markedly lower in 3T3-L1 adipocytes and L6 myocytes.	Insulin Glargine	36-44	insulin receptor	Homo sapiens	110-126