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Human Insulin Receptor Protein expressed in Human Cells - ABIN2003949
Kan, Kanai, Iida, Jinnouchi, Todaka, Imanaka, Ito, Nishioka, Ohnishi, Kamohara: Frequency of mutations of insulin receptor gene in Japanese patients with NIDDM. in Diabetes 1995
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The gained results are observed not only the unbinding mechanism of IRK (show KCNJ12 Proteins)-PTP1B (show PTPN1 Proteins) complexes came from pulling force profile, number of hydrogen bonds, and interaction energy between IRK (show KCNJ12 Proteins) and PTP1Bs but also described PTP1B's point mutations could variably change its binding affinity towards IRK (show KCNJ12 Proteins).
The data in this paper demonstrate that IR knockdown in primary tumors partially reverses the growth-promoting effects of hyperinsulinemia as well as highlighting the importance of the insulin receptor signaling pathway in cancer progression, and more specifically in epithelial-mesenchymal transition.
INSR rs2252673 and rs3745546 polymorphisms were associated with sensitivity to platinum-based chemotherapy in epithelial ovarian cancer patients and rs2252673 polymorphism may be an independent risk factor for EOC prognosis.
The IGF1R (show IGF1R Proteins) purified in n-dodecyl-beta-D-maltoside showed ligand-stimulated autophosphorylation and kinase activity, suggesting an intact transmembrane signaling mechanism.
Signaling via the insulin (INS (show INS Proteins)) and insulin-like growth factor 1 (IGF1 (show IGF1 Proteins)) receptors (INSR and IGF1R (show IGF1R Proteins)) regulate basal cell (BC) differentiation into ciliated cells.
High INSR expression is associated with drug Resistance in Gastrointestinal Stromal Tumors.
the above data indicate a direct role for IR expression as a determinant of PT-gluconeogenesis. Thus reduced insulin (show INS Proteins) signaling of the proximal tubule may contribute to hyperglycemia in the metabolic syndrome via elevated gluconeogenesis.
Activation of D4 receptor inhibits insulin receptor expression in RPT cells from WKY rats. The aberrant inhibition of D4 receptor on insulin receptor expression and effect might be involved in the pathogenesis of essential hypertension.
The HIR MAb binds the insulin receptor on the BBB.
data indicate that post-receptor signalling abnormalities might contribute to Myotonic dystrophy insulin (show INS Proteins) resistance regardless the alteration of INSR splicing.
long-term hepatic expression of IRA could be a promising therapeutic approach for the treatment of type 2 diabetes mellitus.
the overlap of IR and IGF1R (show IGF1R Proteins) signaling is critical to the regulation of muscle protein turnover, and this regulation depends on suppression of FoxO (show FOXO3 Proteins)-regulated, autophagy-mediated protein degradation
These data reveal a critical pathophysiological role for INSR Thr1160 phosphorylation and provide further mechanistic links between PKCepsilon (show PRKCE Proteins) and INSR in mediating Nonalcoholic fatty liver disease -induced hepatic insulin (show INS Proteins) resistance.
Insr was downregulated in the arcuate nucleus of type 2 diabetic mice.
Mice lacking the insulin receptor in AgRP (show AGRP Proteins) neurons (AgRP (show AGRP Proteins) IR KO) exhibited impaired hepatic insulin (show INS Proteins) action because the ability of insulin (show INS Proteins) to suppress hepatic glucose production (hGP) was reduced, but the ability of insulin (show INS Proteins) to suppress lipolysis was unaltered. To the contrary, in POMC (show POMC Proteins) IR KO mice, insulin (show INS Proteins) lowered hGP but failed to suppress adipose tissue lipolysis.
Intracellular retention of the insulin receptor is caused by elevated amounts of alpha-taxilin (show TXLNA Proteins), a free syntaxin binding protein, in HBV expressing hepatocytes preventing proper targeting of the insulin receptor to the cell surface.
Results found that glioblastoma tumors resistant to PDGFR (show PDGFRB Proteins) inhibition required the expression and activation of the insulin receptor (IR)/insulin (show INS Proteins) growth-like factor receptor (IGF1R (show IGF1R Proteins)) for tumor cell proliferation and survival.
The IR in the intestinal epithelium plays important roles in intestinal gene expression, glucose uptake, and GIP (show GIP Proteins) production, which may contribute to pathophysiological changes in individuals with diabetes, metabolic syndrome, and other insulin (show INS Proteins)-resistant states.
In conclusion, we have identified that ARL15 acts as an insulin (show INS Proteins)-sensitizing effector molecule to upregulate the phosphorylation of members of the canonical IR/IRS1 (show IRS1 Proteins)/PDPK1 (show PDPK1 Proteins)/AKT (show AKT1 Proteins) insulin (show INS Proteins) pathway by interacting with its GAP ASAP2 (show ASAP2 Proteins) and activating PDPK1 (show PDPK1 Proteins). This research may provide new insights into GTPase (show RACGAP1 Proteins)-mediated insulin (show INS Proteins) signalling regulation and facilitate the development of new pharmacotherapeutic targets for insulin (show INS Proteins) sensitizati
it was demonstrated that InR was expressed in follicular cells and that its expression in corpus allatum and follicular cells of Drosophila females was stage-specific, i.e., the expression intensity in young females greatly exceeded that in mature individuals.
INR signaling promotes glial phagocytic clearance of degenerating axons through regulation of Draper.
These results demonstrate that Dock selectively enhances the PTP61Fm-mediated attenuation of InR signalling and underscores the specificity of PTPs and the importance of adaptor proteins in regulating PTP function in vivo.
Mactosylceramide, an early product in GSL (show CTSA Proteins) biosynthesis, prevents inappropriate activation of insulin (show INS Proteins) and fibroblast growth factor receptors in Drosophila glial cells and hypertrophy.
Results show that lifespan and behavioral senescence are independently regulated by the Drosophila insulin receptor.
Study shows that the increase in the dopamine level in D. melanogaster females with the InR gene knockdown in corpus allatum ensures their increased resistance to starvation-induced stress
results indicate that the Drosophila insulin-like peptide system is a crucial regulator of sleep
This study has shown for the first time that suppression of InR expression in VNC leads to a rise in the survival of flies under conditions of toxic stress.
The combined activities of Stit and InR in ectodermal epithelial tissues provide an RTK-mediated, two-tiered reaction threshold to varying nutritional conditions that promote epithelial organ growth even at low levels of InR signaling.
InR, but not Tor, signaling non-autonomously promotes primordial germ cell differentiation.
studied by RT reverse-transcription PCR, whether there are differences in the abundance of mRNA coding for IGF-I (show IGF1 Proteins), IGF-2, IGFBP-2, IGFBP-3 (show IGFBP3 Proteins), IGF-1R (show IGF1R Proteins), IGF-2R, GHR (show GHR Proteins), and InsR in compartmentalized layers of jejunum and ileum of 5-d-old calves fed colostrum
insulin receptor and phosphoinositide 3-kinase localize to detergent-resistant membrane rafts of rod photoreceptor outer segments
FSH (show BRD2 Proteins), but not E2, stimulated the expression of IR and GHR (show GHR Proteins) genes during follicular development.
Data conclude that insulin (show INS Proteins) and IGF-I (show IGF1 Proteins) receptors differentially mediate the production of adhesion molecules by ECs and monocyte adhesion onto the vascular endothelium in response to the hyperinsulinemic state.
After removal of the precursor signal peptide, the insulin receptor precursor is post-translationally cleaved into two chains (alpha and beta) that are covalently linked. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Two transcript variants encoding different isoforms have been found for this gene.
, drosophila insulin receptor
, insulin receptor
, insulin receptor homolog
, insulin receptor homologue
, insulin-like receptor
, insulin receptor tyrosine kinase
, tyrosine kinase
, insulin receptor-like
, insulin receptor, beta-subunit