The DOI matches its Crossref record; 175 of the 176 references it cites were found in a registry or an index.
Protein–protein interaction in insulin signaling and the molecular mechanisms of insulin resistance
Open accessAbstract
Perspective Figure 1 Schematic illustration of major signaling pathways of insulin action.The phosphorylated insulin receptor binds and phosphorylates IRS proteins and Shc, which bind differentially to various downstream signaling proteins.PI3-kinase is critical for metabolic actions of insulin, such as glucose transport, glycogen synthesis, and protein synthesis, whereas Grb-2/SOS complex, which activates the MAP kinase cascade, is critical in mitogenic response.PI3-kinase probably modulates the mitogenic response as well.This series continues from the March 1999, no.6, issue.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Inhibitors of PI3K impair glucose transport and block the activation of glycogen synthase and hexokinase- (HK-) II expression [138–146]”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [143]
In the citing paper
“The phosphorylated tyrosine residues of IRS-1 mediate an association with the 85-kDa regulatory subunit of phosphatidylinositol 3-kinase (PI3K), leading to activation of the enzyme [138–140, 143, 144].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [143]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Positional cloning of the mouse obese gene and its human homologue
Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419
Adipose Expression of Tumor Necrosis Factor-α: Direct Role in Obesity-Linked Insulin Resistance
Hotamisligil, G. S., Shargill, N. S., & Spiegelman, B. M. (1993) · Science · doi:10.1126/science.7678183 · Cited by 7,518
Hotamisligil, G. S., Arner, P., Caro, J. F., Atkinson, R. L., & Spiegelman, B. M. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117936 · Cited by 3,543
Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
Ullrich, A., Bell, J. R., Chen, E. Y., Herrera, R., Petruzzelli, L., Dull, T. J., Gray, A., Coussens, L. M., Liao, Y.-C., Tsubokawa, M., et al. (1985) · Nature · doi:10.1038/313756a0 · Cited by 2,251
Disruption of IRS-2 causes type 2 diabetes in mice
Withers, D. J., Gutierrez, J. S., Towery, H. H., Burks, D. J., Ren, J., Previs, S. F., Zhang, Y., Bernal, D., Pons, S., Shulman, G. I., et al. (1998) · Nature · doi:10.1038/36116 · Cited by 1,775
PPAR-gamma: adipogenic regulator and thiazolidinedione receptor.
Spiegelman, B. M. (1998) · Diabetes · doi:10.2337/diabetes.47.4.507 · Cited by 1,730
Protein Kinase C: Structure, Function, and Regulation
Newton, A. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28495 · Cited by 1,656
The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632
The Structural Basis for 14-3-3:Phosphopeptide Binding Specificity
Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H. C. B., Gamblin, S. J., Smerdon, S. J., & Cantley, L. C. (1997) · Cell · doi:10.1016/s0092-8674(00)80487-0 · Cited by 1,604
The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
Ebina, Y., Ellis, L., Jarnagin, K., Edery, M., Gráf, L., Clauser, É., Ou, J. J., Masiarz, F. R., Kan, Y. W., Goldfine, I. D., et al. (1985) · Cell · doi:10.1016/0092-8674(85)90334-4 · Cited by 1,477
Research works printed but not linked: 9
- Van Horn, 1994, J Biochem, 269, 29
- Liu, 1994, Recent Prog Horm Res, 49, 149
- Cohen, 1997, Growth Regul, 410, 3
- Imai, 1994, J Clin Endocrinol Metab, 79, 1655
- Celi, 1995, J Clin Endocrinol Metab, 80, 2827
- Friedman, 1997, Am J Physiol, 273, E1014
- Ohsaka, 1997, Growth Regul, 402, 246
- Poitout, 1998, Diabetes Metab, 24, 321
- Rossetti, 1995, Clin Invest Med, 18, 255
Cited by
Sorted by citations
Items 601–700 of 854
Mechanisms of insulin signal transduction
Langlais, P. R., Mandarino, L. J., & Garvey, W. T. (2015) · Wiley eBooks · doi:10.1002/9781118387658.ch12 · Cited by 8
Insulin signaling proteins in pancreatic islets of insulin-resistant rats induced by glucocorticoid
Paula, F. M. D., Boschero, A. C., Carneiro, E. M., Bosqueiro, J. R., & Rafacho, A. (2011) · Biological Research · doi:10.4067/s0716-97602011000300006 · Cited by 7
Inhibition of Ganglioside Biosynthesis as a Novel Therapeutic Approach in Insulin Resistance
Inokuchi, J. (2011) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-17214-4_8 · Cited by 7
“Similarities between these cell culture results and the findings in many cases of clinical insulin resistance (Virkamaki et al. 1999) suggest a potential role for microdomains in the pathogenesis of this disorder.”
ResultKim, J., Choi, Y. M., Hong, M. A., Hwang, S.-S., Yoon, S. H., Chae, S. J., Jee, B. C., Ku, S., Kim, J. G., & Moon, S. Y. (2009) · Human Reproduction · doi:10.1093/humrep/dep019 · Cited by 7
Yan, H. M., Meng, J., Zhang, S., Zhuang, H., Song, Y., Xiao, X., Wang, D. W., & Jiang, J. (2018) · Human Gene Therapy · doi:10.1089/hum.2018.140 · Cited by 7
“35 Insulin binds to its receptor, which in turn results in the receptor auto-phosphorylation and the activation of several docking proteins, such as IRS.”
Regulation of Intermediatory Metabolism During Fasting and Feeding
DeFronzo, R. A., & Ferrannini, E. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4160-5583-9.00036-8 · Cited by 7
Apoptosis in the rat brown adipose tissue after insulin treatment
Korać, A., Radovanović, J., Davidović, V., Koko, V., & Nedeljković, M. (1999) · Journal of Thermal Biology · doi:10.1016/s0306-4565(99)00064-9 · Cited by 7
Jakubowicz, D. J., Wainstein, J., & Homburg, R. (2012) · PubMed · Cited by 7
Myoinositol Supplementation on Insulin Resistance in Gestational Diabetes
Corrado, F., & Santamaria, A. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-800093-9.00019-3 · Cited by 7
Proteasome inhibitors regulate tyrosine phosphorylation of IRS-1 and insulin signaling in adipocytes
Rondinone, C. M., & Kramer, D. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02083-1 · Cited by 7
Gene expression in human cells with mutant insulin receptors
Melis, R., Pruett, P. B., Wang, Y., & Longo, N. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01293-2 · Cited by 7
Receptor Modifications in Glycobiology
Inokuchi, J., & Kabayama, K. (2007) · Elsevier eBooks · doi:10.1016/b978-044451967-2/00071-4 · Cited by 7
Insulin actions in vivo : glucose metabolism
Ferrannini, E., & DeFronzo, R. A. (2015) · Wiley eBooks · doi:10.1002/9781118387658.ch14 · Cited by 7
Hirose, M., Inoue, K., Matoba, S., Tatebe, T., Tokita, S., Dodo, Y., Tomishima, T., Hasegawa, A., Honda, A., Ozaki, M., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-67513-9 · Cited by 6
“In mice and humans, the 5 ′ half of the Irs2 gene contains the highly conserved PH-and PTB-encoding sequences that target IRS-2 to the cell membrane and insulin receptor (IR), respectively 25,26 .”
BackgroundNielsen, M. F. (2008) · PubMed · Cited by 6
Chen, T. K., & Bowden, E. F. (2013) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2013.05.023 · Cited by 6
Escharectomy and Allografting During Shock Stage Reduces Insulin Resistance Induced by Major Burn
Chen, X.-L., Xia, Z., & Wei, H. (2011) · Journal of Burn Care & Research · doi:10.1097/bcr.0b013e31820aaf96 · Cited by 6
“It has been proposed that phosphorylation of the serine(307) prevents the association between IRS-1 and the insulin receptor, leading to a decrease in IRS-1 tyrosine phosphorylation.(34) Several stimuli such as TNF- 35 or administration of insulin(36) induce the phosphorylation of serine(307), leading to a reduction i…”
BackgroundIn silico and in vitro approaches allow the identification of the Prosystemin molecular network
Natale, R., Coppola, M., D’Agostino, N., Zhang, Y., Fernie, A. R., Castaldi, V., & Rao, R. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.12.006 · Cited by 6
“PPIs studies have revealed complex networks covering all scien-tific fields from medicine and pharmacology, such as the mechanism of insulin action [3], to the complex metabolic processes that take place in both animal and plant cells [4–5].”
BackgroundNerve growth factor receptor TrkA signaling in streptozotocin-induced type 1 diabetes rat brain
Vines, K., Li, R., Geetha, T., Broderick, T. L., Carroll, C. C., & Babu, J. R. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.162 · Cited by 6
Sp-family of transcription factors regulates human SHIP2 gene expression
Ishida, S., Funakoshi, A., Miyasaka, K., Iguchi, H., & Takiguchi, S. (2005) · Gene · doi:10.1016/j.gene.2004.12.046 · Cited by 6
Effect of obesity on insulin signaling through JAK2 in rat aorta
Zecchin, H. G., de Souza, C. T., Prada, P. O., Carvalheira, J. B. C., Velloso, L. A., & Saad, M. J. A. (2005) · Vascular Pharmacology · doi:10.1016/j.vph.2005.08.019 · Cited by 7
Peptide rescues GLUT4 recruitment, but not GLUT4 activation, in insulin resistance
Funaki, M., Herr, K. B., & Randhawa, P. K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.153 · Cited by 6
The Development of Insulin Resistance in Type 2 Diabetes: Insights from Knockout Studies
Pattaranit, R., van den Berg, H. A., & Spanswick, D. C. (2008) · Science Progress · doi:10.3184/003685008x361343 · Cited by 6
Dietary Calcium and the Metabolic Syndrome
Teegarden, D. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-961-5_26 · Cited by 6
“Insulin acts through the insulin receptor ( 23 ), which is a heterotetramer comprised of twoF -subunits and two G-subunits.”
BackgroundTissue-Specific Targeting of the Insulin Receptor Gene
Kulkarni, R., & Okada, T. (2002) · Endocrine · doi:10.1385/endo:19:3:257 · Cited by 6
Dysregulation of IRS-proteins causes insulin resistance and diabetes
Aguirre, V., & White, M. F. (2000) · Current Opinion in Endocrinology & Diabetes · doi:10.1097/00060793-200002000-00001 · Cited by 6
Furuhata, Y., Yonezawa, T., Takahashi, M., & Nishihara, M. (2002) · Journal of Endocrinology · doi:10.1677/joe.0.1720127 · Cited by 6
“This phenomenon observed in both our transgenic and Zucker rats might be common among obese early stage NIDDM models.”
BackgroundInfluentialTobin, B. W., & Miller, G. D. (2001) · Journal of Nutrition · doi:10.1093/jn/131.2.333s · Cited by 6
Qi, W., Gündoğan, F., Gilligan, J. T., & de la Monte, S. M. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4195657 · Cited by 6
Low Glycaemic Index Cereal Grain Functional Foods
Usman, M. A., Patil, P. J., Patil, D. N., Mehmood, A., Shah, H. A., Zahra, S. M., Ali, Z., & Nasreen, S. (2022) · Springer eBooks · doi:10.1007/978-3-031-05611-6_12 · Cited by 6
Proximity Labeling and Proteomics: Get to Know Neighbors
Kotani, N., Araki, T., Miyagawa‐Yamaguchi, A., Amimoto, T., Nakano, M., & Honke, K. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.07.031 · Cited by 5
Cellular Mechanisms of Insulin Action
Ciaraldi, T. P. (2009) · Springer eBooks · doi:10.1007/978-0-387-09841-8_5 · Cited by 5
Wakayama, S., Haque, A., Koide, N., Kato, Y., Odkhuu, E., Tsolmongyn, B., Naiki, Y., Komatsu, T., Yoshida, T., & Yokochi, T. (2014) · Immunopharmacology and Immunotoxicology · doi:10.3109/08923973.2014.887096 · Cited by 6
“com/ipi ISSN: 0892-3973 (print), 1532-2513 (electronic) Immunopharmacol Immunotoxicol, 2014; 36(2): 145–149”
Family history of PCOS, obesity, low fiber diet, and low physical activity increase the risk of PCOS
Wahyuni, A., Supriyatiningsih, Kusumawati, W., Kirana, K. S., & Mayayustika, C. D. (2022) · Jurnal kedokteran dan kesehatan Indonesia · doi:10.20885/jkki.vol13.iss1.art8 · Cited by 14
Alzheimer’s Disease and Diabetes
Brent, D. A., Gary, L., Aboud, Z., & Gordon, W. (2013) · InTech eBooks · doi:10.5772/54913 · Cited by 6
“Both insulin and IGF-1 receptors are tyrosine kinases [150-152] that, when activated, phosphorylate substrate proteins such as IRS.”
BackgroundInfluentialLes stéatopathies métaboliques : conséquences hépatiques du syndrome métabolique
Anty, R., Gual, P., Huet, P., MARCHAND‐BRUSTEL, Y. L., & Tran, A. (2007) · Gastroentérologie Clinique et Biologique · doi:10.1016/s0399-8320(07)78350-1 · Cited by 5
“La liaison de l’insuline sur son récepteur membranaire active une voie de signalisation complexe qui permet le transport de glucose via des transporteurs membranaires spécifiques, le stockage des acides gras en triglycérides et l’inhibition de la lipolyse [16].”
BackgroundBenzi, L., Cecchetti, P., Ciccarone, A. M., Novelli, S., Paoli, A. A. D., Bertacca, A., Maffei, M., Maggi, D. C., Andraghetti, G., Prato, S. D., et al. (2003) · European Journal of Endocrinology · doi:10.1530/eje.0.1480365 · Cited by 5
“Upon insulin binding with the specific membrane receptor (IR) ( 1 ), the insulin ‐ IR complex is internalized (2, 3). It has been suggested that this process contributes to modulation of insulin action by regulating IR number (4).”
BackgroundEffects of Fluvastatin Treatment on Insulin Sensitivity in Patients with Hyperlipidaemia
Cingözbay, B. Y., Top, C., Terekeci, H., Keskin, Ö. F., & Önde, M. E. (2002) · Journal of International Medical Research · doi:10.1177/147323000203000104 · Cited by 5
Insulin Dependant Gene Expression of Heat Shock Protein 60 in H4IIE Hepatoma Cells.
Franklin, J. L., Keeton, A. B., Bortoff, K. D., & Messina, J. L. (2008) · PubMed Central · Cited by 5
Pathogenesis of Type 2 Diabetes
Cusi, K. J., & DeFronzo, R. A. (2001) · Comprehensive physiology · doi:10.1002/cphy.cp070237 · Cited by 5
Li, J., CHEN, T., Li, K., Yan, H.-T., Li, X., Yang, Y. C., Zhang, Y., Su, B., & Li, F. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3087 · Cited by 4
“Expression of IRS‑1, a key adaptor protein in transmission of signals from insulin receptors to Akt and other kinases (23), did not differ from baseline levels in skeletal muscle from control rats following N14 or N28, but increased significantly in skeletal muscle from the NCPB group compared with…”
Current Dietary Lipids Recommendations: Pros and Cons
Giraudo, S., Montero, J. C., Kaufmann, P., & Grossman, B. (2016) · Journal of Nutrition and Health Sciences · doi:10.15744/2393-9060.3.406 · Cited by 3
Age-Dependent Onset of Insulin Resistance in Insulin-Resistant Mice
Ide, N., Arisawa, K., Ogura, K., Kagawa, Y., & Maeda, T. (2015) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b15-00602 · Cited by 4
Кондро, М. М., Halenova, T., Kuznietsova, M. Y., & Savchuk, О. (2013) · Fìzìologìčnij žurnal · doi:10.15407/fz59.02.059 · Cited by 4
Catalano-Iniesta, L. A., Sánchez‐Robledo, V., Osma, M. D. C. I., García‐Barrado, M. J., Carretero‐Hernández, M., Blanco, E. J., Vicente‐García, T., Burks, D. J., & Carretero, J. (2018) · Journal of Anatomy · doi:10.1111/joa.12917 · Cited by 4
“Insulin and IGFs exert anti-apoptotic effects via a complex network of intracellular signalling pathways (Virkamaki et al. 1999) and are implicated in the performance of gonadotropic hormones; thus, insulin/IGF signalling pathways are involved in proliferative effects on immature testicular follicle-stimulating hormon…”
BackgroundProtein/ Hormone Based Nanoparticles as Carriers for Drugs Targeting Protein-Protein Interactions
Al-Suhaimi, E. A., Ravinayagam, V., Jermy, B. R., Tarhini, M., & Elaı̈ssari, A. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190304152320 · Cited by 4
Mohammed, E. D., Abdel‐Naim, A. B., Jin, K., Jiang, R., Wei, J., & Sun, B. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118615 · Cited by 4
Ola, M. S. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44120410 · Cited by 9
“The reduced tyrosine phosphorylation and increased serine/threonine phosphorylation of IRS-1 due to diabetes or obesity have mostly been considered to be negative regulators of IRS-1 function and are widely regarded as critical players in inhibiting insulin signaling [6,7].”
BackgroundMetabolic Syndrome and Insulin resistance: Etiopathegenesis and influencing factors
Al-Mahmood, A. K., Afrin, S., & Hoque, N. (2013) · Bangladesh Journal of Medical Biochemistry · doi:10.3329/bjmb.v4i2.13773 · Cited by 5
Hupfeld, C. J., & Olefsky, J. M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00040-8 · Cited by 7
The Metabolic Syndrome in Hispanics – The Role of Insulin Resistance and Inflammation
Pablo, I., Jose, M., Escobales, N., Crespo, M., & Hector, L. (2012) · InTech eBooks · doi:10.5772/54620 · Cited by 4
“Phosphorylated IRS proteins serve as multisite docking proteins for various effector molecules possessing src homology 2 (SH2) domains, including phosphatidylinositol 3-kinase (PI 3-kinase) regulatory subunits (p85, p55 p50, p85, and p55PIK), the tyrosine kinases Fyn and Csk, the tyrosine protein phosphatase SHP-2/Syp…”
BackgroundBarrett, K. T., McGrowder, D. A., Brown, P., & Ragoobirsingh, D. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-0387-x · Cited by 4
“Impaired insulin signal transduction and or alterations in traffic and translocation of GLUT 4 to the plasma membrane may be responsible for reduced glucose transport activity in insulin-sensitive tissues in type 2 diabetes [9].”
BackgroundTwo-way learning with one-way supervision for gene expression data
Wong, M. H. T., Mutch, D. M., & McNicholas, P. D. (2017) · BMC Bioinformatics · doi:10.1186/s12859-017-1564-5 · Cited by 4
Ketoacidosis and Hyperosmolar Coma
Foster, D. W., & Esser, V. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4160-5583-9.00046-0 · Cited by 4
Potential Mechanisms Linking Insulin to Cancer
Babichev, Y., Khalid, S., & Fantus, I. G. (2011) · Energy balance and cancer · doi:10.1007/978-1-4419-9911-5_7 · Cited by 4
“This would limit signaling, at least in part, by decreasing insulin sensitivity [ 138 ].”
BackgroundmRNA Translation in Diabetic Nephropathy
Kasinath, B. S., Lee, M. J., Féliers, D., & Sonenberg, N. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-153-6_6 · Cited by 4
“It is probable that there are distinct metabolic factors in type 2 diabetes ( 104 ) that may operate differently from type 1 diabetes that promote a pathogenic role for insulin in the renal tissue in the hyperinsulinemic phase of type 2 diabetes.”
BackgroundNaringenin Ameliorates Palmitic Acid-induced Fatty Acid Stress in Hepatocytes
Maity, S., Chakrabarti, P., & Chakraborti, A. S. (2021) · The Natural Products Journal · doi:10.2174/2210315511666210121154928 · Cited by 3
Criteria for the diagnosis of metabolic syndrome: A review
Ogbu, I. S. I. (2023) · Journal of Medical Laboratory and Diagnosis · doi:10.5897/jmld2022.0174 · Cited by 3
Hupfeld, C. J., Courtney, C. H., & Olefsky, J. M. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4160-5583-9.00041-1 · Cited by 5
Fungal Depsidones Stimulate AKT-Dependent Glucose Uptake in 3T3-L1 Adipocytes
Chantarasakha, K., Yangchum, A., Isaka, M., & Tepaamorndech, S. (2024) · Journal of Natural Products · doi:10.1021/acs.jnatprod.3c01134 · Cited by 3
Type 2 Diabetes Mellitus: Etiology, Pathogenesis and Clinical Manifestations
Kruszynska, Y. T. (2004) · Springer eBooks · doi:10.1007/978-1-4757-6260-0_10 · Cited by 3
Insulin/IGF-1 Signaling Nodes and their Role in Carcinogenesis
Taniguchi, C. M., & Kahn, C. R. (2011) · Energy balance and cancer · doi:10.1007/978-1-4419-9911-5_2 · Cited by 5
“The best studied are adaptor molecules, such as the regulatory subunit of PI 3-kinase or the adaptor molecule Grb2, which associates with SOS to activate the Ras-MAP kinase pathway (reviewed in [51, 52]).”
BackgroundSelf-citationTumor Necrosis Factor-α/Receptor Signaling Through the Akt Kinase
Özeş, O. N., Akça, H., Gustin, J. A., Mayo, L. D., Pincheira, R., Korgaonkar, C. K., & Donner, D. B. (2005) · Humana Press eBooks · doi:10.1007/978-1-59259-909-7_2 · Cited by 3
“Tyrosine phosphorylation of IRS-1 by the activated insulin receptor promotes interaction of IRS-1 with signaling proteins that promote insulin action (19).”
BackgroundNEW INSIGHTS INTO INSULIN RESISTANCE PATHOPHYSIOLOGY: HOW IT AFFECTS GLUCOSE AND LIPID METABOLISM
Col, V. (2001) · Acta Clinica Belgica · doi:10.1179/acb.2001.025 · Cited by 3
“At the cascade end, these in turn activate two main enzymes, which mediate the intracellular effects of insulin (5).”
Background5-Substituted isophthalamides as insulin receptor sensitizers
Robinson, L., Bajjalieh, S., Cairns, N., Lum, R. T., Macsata, R. W., Manchem, V. P., Park, S. J., Rao, S., Schow, S. R., Shi, S., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.05.031 · Cited by 3
Önde, M. E., Top, C., & Öncül, O. (2008) · The Endocrinologist · doi:10.1097/ten.0b013e31817ffea2 · Cited by 3
Saqib, U., & Siddiqi, M. I. (2011) · Journal of Chemical Biology · doi:10.1007/s12154-011-0057-7 · Cited by 3
The interrelationship between insulin resistane and Alzheimer development
Ghareeb, D. A., Mohamed, S. K., & El-Sayed, M. (2013) · Journal of Biomedical Science and Engineering · doi:10.4236/jbise.2013.67093 · Cited by 5
Vedtofte, L., Knop, F. K., & Vilsbøll, T. (2015) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.2015.1029455 · Cited by 3
“The insulin receptor belongs to a family of receptor tyrosine kinases which, upon activation, begin with autophosphorylation of the receptor, lead to phosphorylation of a family of insulin receptor substrate proteins and end with translocation of the insulin-sensitive glucose transporter 4 in muscle and adipose tissue…”
BackgroundTargeting Obesity for the Treatment of Type 2 Diabetes Mellitus
Feng, D. Z. Y. (2014) · Journal of Cytology & Histology · doi:10.4172/2157-7099.1000215 · Cited by 2
“Of importance is the enhanced Glut4 mobilization to cell membrane in peripheral cells for its role in glucose uptake [45].”
BackgroundNonalcoholic Fatty Liver Disease
Stefan, N., & Häring, H. (2005) · Elsevier eBooks · doi:10.1016/b978-84-8174-892-5.50024-3 · Cited by 3
Photoaffinity palladium reagents for capture of protein–protein interactions
Zheng, Q., Pang, Z., Liu, J., Zhou, Y., Sun, Y., Yin, Z., & Lou, Z. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob01048c · Cited by 3
Vaidya, R., Mohan, V., Bai, M. R., & Sudha, V. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-401716-0.00025-8 · Cited by 3
Insulin Resistance and Early Pregnancy Loss in Polycystic Ovary Syndrome
Jakubowicz, D. J., & Sharma, S. T. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-310-3_33 · Cited by 3
Sekar, N., & Veldhuis, J. D. (2004) · Elsevier eBooks · doi:10.1016/b978-012444562-8/50015-x · Cited by 3
Comparison of the interactomic networks of different species in terms of accessibility
Rodrigues, F. A., & Costa, L. D. F. (2009) · Molecular BioSystems · doi:10.1039/b906966f · Cited by 3
Al‐Rasheed, N. M. (2006) · Figshare · Cited by 3
Laychock, S. G. (2003) · Encyclopedia of Hormones · doi:10.1016/b0-12-341103-3/00177-7 · Cited by 3
Wu, X., & Garvey, W. T. (2010) · Wiley eBooks · doi:10.1002/9781444324808.ch7 · Cited by 4
Sun, Y., Chanrasekhar, V., Kessinger, C. W., Tang, P., Gao, Y., Kamli-Salino, S., Nelson, K., Delibegović, M., Abel, E. D., & Kontaridis, M. I. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.19.541546 · Cited by 3
Mechanism of Skeletal Muscle Contraction: Intracellular Signaling in Skeletal Muscle Contraction
Manabe, Y. (2016) · Springer eBooks · doi:10.1007/978-4-431-55720-3_10 · Cited by 2
De, S. K. (2023) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/1871530323666230220123228 · Cited by 2
Chantarasakha, K., Yangchum, A., Isaka, M., & Tepaamorndech, S. (2025) · Natural Products and Bioprospecting · doi:10.1007/s13659-025-00546-3 · Cited by 2
“We also observed an increase in GLUT1 levels, but this is not unexpected, as GLUT4 and GLUT1 are known to colocalize, a phenomenon previously reported in insulin-treated myotubes [32].”
Insulin Action in the Islet β-Cell
Kulkarni, R. (2007) · Springer eBooks · doi:10.1007/978-0-387-72204-7_7 · Cited by 2
Glycaemic control, insulin resistance and obesity
Herter‐Aeberli, I., & Zimmermann, M. B. (2007) · Elsevier eBooks · doi:10.1533/9781845693114.1.43 · Cited by 2
Significance of Organ Crosstalk in Insulin Resistance and Type 2 Diabetes
Bhatt, S., & Kulkarni, R. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-415784-2.00017-8 · Cited by 2
Hoyer, S., & Frölich, L. (2007) · Springer eBooks · doi:10.1007/978-0-387-30377-2_12 · Cited by 2
Bernier, M., He, H., Kwon, Y.-K., & Jang, H.-J. (2004) · Vitamins and hormones · doi:10.1016/s0083-6729(04)69008-x · Cited by 2
Cellular Mechanisms of Insulin Action
Ciaraldi, T. P. (2017) · Springer eBooks · doi:10.1007/978-3-319-18741-9_5 · Cited by 2
Superoxide production by phagocytic leukocytes: the scientific legacy of Bernard Babior
Curnutte, J. T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200423377 · Cited by 2
Syndromes of Extreme Insulin Resistance
Grunberger, G., & Alrefai, H. (2004) · Springer eBooks · doi:10.1007/978-1-4757-6260-0_14 · Cited by 2
Inokuchi, J., Kabayama, K., Sato, T., & Igarashi, Y. (2006) · Springer eBooks · doi:10.1007/4-431-34200-1_21 · Cited by 2
“Insulin resistance, defined as the decreased ability of cells or tissues to respond to physiological levels of insulin, is considered the primary pathophysiological defect of type 2 diabetes (Virkamaki et al., 1999).”
BackgroundProtein Tyrosine Phosphatase Activity in Insulin‐Resistant Rodent Psammomys Obesus
Meyerovitch, J., Balta, Y., Ziv, E., Sack, J., & Shafrir, E. (2002) · Journal of Diabetes Research · doi:10.1080/15604280214273 · Cited by 2
Model and analysis: Diabetes and obesity
Al-Hashmi, S. (2007) · ThinkTech (Texas Tech University) · Cited by 2
The 2-5A Pathway and Signal Transduction
Verhas, M., Verbinnen, T., Meirleir, K. D., Herst, C. V., Frémont, M., & Englebienne, P. (2002) · CRC Press eBooks · doi:10.1201/9781420041002.ch5 · Cited by 2
Types of Diabetes and Their Implications Regarding Heart and Vascular Disease
Lebovitz, H. E. (2002) · CRC Press eBooks · doi:10.1201/b14062-3 · Cited by 2
Insulin Mechanisms/Metabolic Actions
Gallagher, E. J., & LeRoith, D. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00116-x · Cited by 2
Pauli, J. R. (2005) · Americanae (AECID Library) · Cited by 2
Logesh, R., Hari, B., Chidambaram, K., & Das, N. (2024) · Gene · doi:10.1016/j.gene.2024.148216 · Cited by 1
Fetal Programming of Type 2 Diabetes
Piekarz, A., & Ozanne, S. (2009) · KARGER eBooks · doi:10.1159/000221162 · Cited by 5
Metadata
- Authors
- Virkamäki, A., Ueki, K., & Kahn, C. R.
- Affiliations
- Joslin Diabetes Center (US)
- Corresponding author
- Kahn, C. Ronald
- Venue
- Journal of Clinical Investigation
- Published
- 1999-04-01
- Volume
- 103
- Issue
- 7
- Pages
- 931-943
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC408269
- OpenAlex
- W2095252238
- Cited by
- 854
- References
- 176
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 15 · 2023: 8 · 2022: 15 · 2021: 12 · 2020: 13 · 2019: 16 · 2018: 13 · 2017: 21 · 2016: 22 · 2015: 26 · 2014: 24 · 2013: 27 · 2012: 31
- FWCI
- 4.88
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Foundation for the Study of Diabetes
- National Institutes of Health (DK31036)
- National Institute of Diabetes and Digestive and Kidney Diseases (R37DK031036, DK 33201, R01DK031036, DK45935, DK31036, R01DK045935, R01DK033201)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- insulin signaling, insulin resistance, protein-protein interaction, insulin receptor, Shc, PI3-kinase, MAP kinase cascade, glucose transport, glycogen synthesis, mitogen response
- MeSH terms
- Animals, Humans, Insulin, Insulin Resistance, Phosphorylation, Protein Binding, Receptor, Insulin, Signal Transduction, Gene Targeting, src Homology Domains, Phosphatidylinositol 3-Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
