Cited by 326Metabolism, Diabetes, and CancerProtein Kinase Regulation and GTPase SignalingPI3K/AKT/mTOR signaling in cancer

The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.

Expression and function of IRS-1 in insulin signal transmission.

Open access

Sun, X.J., Miralpeix, M, Myers, M G, Glasheen, E.M., Backer, J.M., Kahn, C.R., White, M.F.·1992·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)41723-1

Open this paper in CoChat — free account

Abstract

IRS-1 is a major insulin receptor substrate which may play an important role in insulin signal transmission. The mRNA for IRS-1 in rat cells and tissues is about 9.5 kilobases (kb). Rat liver IRS-1 was stably expressed in Chinese hamster ovary (CHO) cells (CHO/IRS-1). Although its calculated molecular mass is 131 kDa, IRS-1 from quiescent cells migrated between 165 and 170 kDa during sodium dodecyl sulfate-polyacrylamide gel electrophoresis. IRS-1 was phosphorylated strongly on serine residues and weakly on threonine residues before insulin stimulation. Insulin immediately stimulated tyrosine phosphorylation of IRS-1, and after 10-30 min with insulin its apparent molecular mass increased to 175-180 kDa. 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. Purified insulin receptors directly phosphorylated baculovirus-produced IRS-1 exclusively on tyrosine residues. By immunofluorescence, IRS-1 was absent from the nucleus, but otherwise distributed uniformly before and after insulin stimulation. Some IRS-1 associated with the insulin receptor during insulin stimulation. In addition, a phosphatidylinositol 3'-kinase associated with IRS-1 during insulin stimulation, and this association was more sensitive to insulin in CHO cells overexpressing the insulin receptor (CHO/IR cells), more responsive to insulin to CHO/IRS-1 cells, and both sensitive and responsive in CHO/IR/IRS-1 cells. Similarly, insulin-stimulated DNA synthesis was more sensitive to insulin in CHO/IR cells, and more responsive in CHO/IRS-1 cells; however, insulin-stimulated DNA synthesis was sensitive but poorly responsive to insulin in CHO/IR/IRS-1 cells. Together, these results suggest that IRS-1 is a direct physiologic substrate of the insulin receptor and may play an important role in insulin signal transmission.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(18)41723-1

Cites

42 of 42 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
PCR protocols — A guide to methods and applications
U.G. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90252-7 · Cited by 11,751
Signal transduction by receptors with tyrosine kinase activity
Ullrich, A., & Schlessinger, J. (1990) · Cell · doi:10.1016/0092-8674(90)90801-k · Cited by 5,435
A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
Shaw, G. D., & Kamen, R. (1986) · Cell · doi:10.1016/0092-8674(86)90341-7 · Cited by 3,946
Oncogenes and signal transduction
Cantley, L. C., Auger, K. R., Carpenter, C. F., Duckworth, B. C., Graziani, A., Kapeller, R., & Soltoff, S. P. (1991) · Cell · doi:10.1016/0092-8674(91)90639-g · Cited by 2,697
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
Koch, C. A., Anderson, D. H., Moran, M. F., Ellis, C. A., & Pawson, T. J. (1991) · Science · doi:10.1126/science.1708916 · Cited by 1,868
Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction protein
Sun, X. J., Rothenberg, P., Kahn, C. R., Backer, J. M., Araki, E., Wilden, P. A., Cahill, D. A., Goldstein, B. J., & White, M. F. (1991) · Nature · doi:10.1038/352073a0 · Cited by 1,574
Self-citation
Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.
Backer, J., Myers, M. G., Shoelson, S. E., Chin, D. J., Sun, X., Miralpeix, M., Hu, P. J., Margolis, B. L., Skolnik, E. Y., & Schlessinger, J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05426.x · Cited by 1,000
Self-citation
Insulin Resistance — Mechanisms, Syndromes, and Implications
Epstein, F. H., Moller, D. E., & Flier, J. S. (1991) · New England Journal of Medicine · doi:10.1056/nejm199109263251307 · Cited by 807

Show all 42 references

Research works printed but not linked: 2

Summers, 1988, Tex. Agric. Exp. St. Bull., 1555, 1
Escobedo, 1991, Mol. Cell. Biol., 11, 1125

Sorted by citations

Items 101–200 of 321

Association of Insulin Receptor Substrate 1 with Simian Virus 40 Large T Antigen
Fei, Z.-L., D'Ambrosio, C., Li, S., Surmacz, E., & Baserga, R. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4232 · Cited by 82
Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II.
Tanasijevic, M. J., Myers, M. G., Thoma, R. S., Crimmins, D. L., White, M. F., & Sacks, D. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46824-4 · Cited by 81
Self-citation
Activation of Phosphatidylinositol 3-Kinase by Interleukin-13
Wright, K. L., Ward, S. G., Kolios, G. C., & Westwick, J. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12626 · Cited by 80
Insulin-induced activation of phosphatidyl inositol 3-kinase. Demonstration that the p85 subunit binds directly to the COOH terminus of the insulin receptor in intact cells.
Levy-Toledano, R., Taouis, M., Blaettler, D. H., Görden, P., & Taylor, S. I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47406-6 · Cited by 84
Neoplastic Transformation Induced by Insulin Receptor Substrate-1 Overexpression Requires an Interaction with Both Grb2 and Syp Signaling Molecules
Tanaka, S., Ito, T., & Wands, J. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14610 · Cited by 79
Mutational analysis of insulin receptor function
Tavaré, J. M., & Siddle, K. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(93)90106-y · Cited by 80
The early intracellular signaling pathway for the insulin/insulin-like growth factor receptor family in the mammalian central nervous system
Folli, F. B., Ghidella, S., Bonfanti, L., Kahn, C. R., & Merighi, A. (1996) · Molecular Neurobiology · doi:10.1007/bf02740639 · Cited by 79
Self-citation
Insulin signalling: the role of insulin receptor substrate 1
Keller, S. R., & Lienhard, G. E. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90065-5 · Cited by 79
Calmodulin and PI3K Signaling in KRAS Cancers
Nussinov, R., Wang, G., Tsai, C., Jang, H., Lu, S., Banerjee, A., Zhang, J., & Gaponenko, V. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.01.007 · Cited by 78
Alternative splicing, gene localization, and binding of SH2-B to the insulin receptor kinase domain
Nelms, K. A., O’Neill, T. J., Li, S., Hubbard, S. R., Gustafson, T. A., & Paul, W. E. (1999) · Mammalian Genome · doi:10.1007/s003359901183 · Cited by 79
Dephosphorylation of insulin receptor substrate 1 by the tyrosine phosphatase PTP2C.
Kuhné, M. R., Zhao, Z., Rowles, J., Lavan, B. E., Shen, S., Fischer, E. H., & Lienhard, G. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40756-3 · Cited by 78
Alterations in insulin signalling pathway induced by prolonged insulin treatment of 3T3-L1 adipocytes
Ricort, J., Tanti, J., OBBERGHEN, E. V., & MARCHAND‐BRUSTEL, Y. L. (1995) · Diabetologia · doi:10.1007/bf00422363 · Cited by 77
Insulin Receptor Substrates (IRSs) and Breast Tumorigenesis
Chan, B. T.-Y., & Lee, A. V. (2008) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-008-9101-9 · Cited by 76
Insulin Stimulates the Phosphorylation and Activity of Farnesyltransferase via the Ras-Mitogen-Activated Protein Kinase Pathway
Goalstone, M. L., Carel, K. D., Leitner, J. W., & Draznin, B. (1997) · Endocrinology · doi:10.1210/endo.138.12.5621 · Cited by 76
Adapter Function of Protein-tyrosine Phosphatase 1D in Insulin Receptor/Insulin Receptor Substrate-1 Interaction
Kharitonenkov, A., Schnekenburger, J., Chen, Z., Knyazev, P. G., Ali, S., Zwick, E., White, M. F., & Ullrich, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29189 · Cited by 75
Self-citation
Insulin resistance, neuroinflammation, and Alzheimer’s disease
Najem, D., Bamji‐Mirza, M., Chang, N., Liu, Q. Y., & Zhang, W. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0050 · Cited by 76
Improved insulin sensitivity by calorie restriction is associated with reduction of ERK and p70S6K activities in the liver of obese Zucker rats
Zheng, Y., Zhang, W., Pendleton, E., Leng, S.-H., Wu, J., Chen, R., & Sun, X. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0181 · Cited by 74
Self-citation
IRS‐1 Regulation in Health and Disease
Schmitz‐Peiffer, C., & Whitehead, J. P. (2003) · IUBMB Life · doi:10.1080/1521654031000138569 · Cited by 78
Molecular Cloning of an Amphibian Insulin Receptor Substrate 1-Like cDNA and Involvement of Phosphatidylinositol 3-Kinase in Insulin-Induced Xenopus Oocyte Maturation
Liu, X. J., Sorisky, A., Zhu, L., & Pawson, T. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3563 · Cited by 71
Insulin Resistance, Obesity, and Lipotoxicity
Yazıcı, D., Demir, S. Ç., & Sezer, H. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-63657-8_14 · Cited by 85
Insulin-Stimulated Oocyte Maturation Requires Insulin Receptor Substrate 1 and Interaction with the SH2 Domains of Phosphatidylinositol 3-Kinase
Chuang, L., Myers, M. G., Backer, J., Shoelson, S. E., White, M. F., Birnbaum, M. J., & Kahn, C. R. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.6653 · Cited by 70
Self-citation
Association between GRB2/Sos and Insulin Receptor Substrate 1 Is Not Sufficient for Activation of Extracellular Signal-Regulated Kinases by Interleukin-4: Implications for Ras Activation by Insulin
Pruett, W., Yuan, Y. P., Rose, E., Batzer, A., Harada, N., & Skolnik, E. Y. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1778 · Cited by 69
The Role of the IGF-I Receptor in Apoptosis
Baserga, R., Resnicoff, M., D'Ambrosio, C., & Valentinis, B. (1997) · Vitamins and hormones · doi:10.1016/s0083-6729(08)60704-9 · Cited by 69
Signal Transduction in Cell–Matrix Interactions
Guan, J., & Chen, H. (1996) · International review of cytology · doi:10.1016/s0074-7696(08)60883-9 · Cited by 67
1 Cellular insulin action and insulin resistance
Garvey, W. T., & Birnbaum, M. J. (1993) · Baillière s Clinical Endocrinology and Metabolism · doi:10.1016/s0950-351x(05)80237-x · Cited by 67
Polarization of macrophages in the tumor microenvironment is influenced by EGFR signaling within colon cancer cells
Zhang, W., Chen, L., Ma, K., Zhao, Y., Liu, X., Wang, Y., Liu, M., Liang, S., Zhu, H., & Xu, N. (2016) · Oncotarget · doi:10.18632/oncotarget.12207 · Cited by 67
Rapamycin partially prevents insulin resistance induced by chronic insulin treatment
Berg, C. E., Lavan, B. E., & Rondinone, C. M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00333-9 · Cited by 69
PTEN Expression Causes Feedback Upregulation of Insulin Receptor Substrate 2
Simpson, L., Li, J., Liaw, D., Hennessy, I., Oliner, J. D., Christians, F. C., & Parsons, R. E. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.12.3947-3958.2001 · Cited by 68
Association of Csk-homologous Kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in Breast Cancer Cells
Zrihan‐Licht, S., Lim, J., Keydar, I., Sliwkowski, M. X., Groopman, J. E., & Avraham, H. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.3.1856 · Cited by 68
Apolipoprotein A-I enhances insulin-dependent and insulin-independent glucose uptake by skeletal muscle
Tang, S., Tabet, F., Cochran, B. J., Torres, L., Wu, B. J., Barter, P. J., & Rye, K. (2019) · Scientific Reports · doi:10.1038/s41598-018-38014-3 · Cited by 70
Homocysteine thiolactone inhibits insulin-stimulated DNA and protein synthesis: possible role of mitogen-activated protein kinase (MAPK), glycogen synthase kinase-3 (GSK-3) and p70 S6K phosphorylation
Najib, S., & Sánchez‐Margalet, V. (2005) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.01581 · Cited by 68
Localization of the Insulin-like Growth Factor I Receptor Binding Sites for the SH2 Domain Proteins p85, Syp, and GTPase Activating Protein
Seely, B. L., Reichart, D. R., Staubs, P. A., Jhun, B. H., Hsu, D. S., Maegawa, H., Milarski, K. L., Saltiel, A. R., & Olefsky, J. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.19151 · Cited by 64
Immunocytochemical detection of insulin receptor substrate-1 (IRS-1) in rat brain: colocalization with phosphotyrosine
Baskin, D. G., Sipols, A. J., Schwartz, M. W., & White, M. F. (1993) · Regulatory Peptides · doi:10.1016/0167-0115(93)90355-c · Cited by 63
Self-citation
Morphine Induces Desensitization of Insulin Receptor Signaling
Li, Y., Eitan, S., Wu, J., Evans, C. J., Kieffer, B. L., Sun, X., & Polakiewicz, R. D. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.17.6255-6266.2003 · Cited by 63
Self-citation
A Casein Kinase I Activity Is Constitutively Associated with Nck
Lussier, G., & Larose, L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.5.2688 · Cited by 63
Insulin Receptor Substrate-1 as a Signaling Molecule for Focal Adhesion Kinase pp125FAK and pp60
Lebrun, P., Mothe‐Satney, I., Delahaye, L., OBBERGHEN, E. V., & Baron, V. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32244 · Cited by 62
Stimulated Activation of Platelet-Derived Growth Factor Receptor In Vivo in Balloon-Injured Arteries
Abe, J., Deguchi, J., MATSUMOTΟ, T., Takuwa, N., Noda, M., Ohno, M., Makuuchi, M., Kurokawa, K., & Takuwa, Y. (1997) · Circulation · doi:10.1161/01.cir.96.6.1906 · Cited by 62
Two alternatively spliced forms of the human insulin-like growth factor I receptor have distinct biological activities and internalization kinetics.
Condorelli, G., Bueno, R., & Smith, R. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37224-1 · Cited by 62
New frontiers in insulin receptor substrate signaling
Myers, M. G., & White, M. F. (1995) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(95)00092-v · Cited by 60
Self-citation
Defects in insulin signal transduction in liver and muscle of pregnant rats
Saad, M. J. A., Maeda, L., Brenelli, S. L., Carvalho, C. R. D. O., de Paiva, R. S., & Velloso, L. A. (1997) · Diabetologia · doi:10.1007/s001250050660 · Cited by 59
Nuclear IRS‐1 and cancer
Krzysztof Reiss, F., Valle, L. D., Lassak, A., & Trojanek, J. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.24019 · Cited by 60
A novel PTP1B inhibitor extracted from Ganoderma lucidum ameliorates insulin resistance by regulating IRS1-GLUT4 cascades in the insulin signaling pathway
Yang, Z., Wu, F., He, Y., Zhang, Q., Zhang, Y., Zhou, G., Yang, H., & Zhou, P. (2017) · Food & Function · doi:10.1039/c7fo01489a · Cited by 63
IRS‐2 branch of IGF‐1 receptor signaling is essential for appropriate timing of myelination
Freude, S., Leeser, U., Müller, M., Hettich, M. M., Udelhoven, M., Schilbach, K., Tobe, K., Kadowaki, T., Köhler, C. N., Schröder, H., et al. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05631.x · Cited by 59
Sam68 is a docking protein linking GAP and PI3K in insulin receptor signaling
Sánchez‐Margalet, V., & Najib, S. (2001) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(01)00587-1 · Cited by 60
Class IA phosphatidylinositol 3-kinase: from their biologic implication in human cancers to drug discovery
Maira, S.-M., Voliva, C. F., & Garcı́a-Echeverrı́a, C. (2008) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.12.2.223 · Cited by 59
Fault Diagnosis Engineering of Digital Circuits Can Identify Vulnerable Molecules in Complex Cellular Pathways
Abdi, A., Tahoori, M. B., & Emamian, E. S. (2008) · Science Signaling · doi:10.1126/scisignal.2000008 · Cited by 59
Nutritional state regulates insulin receptor and IRS-1 phosphorylation and expression in chicken
Dupont, J., Derouet, M., Simon, J., & Taouis, M. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.274.2.e309 · Cited by 59
Chapter 13 Phosphorylation of IRS Proteins
Sun, X., & Liu, F. (2009) · Vitamins and hormones · doi:10.1016/s0083-6729(08)00613-4 · Cited by 57
Self-citation
The IRS-signalling system in insulin and cytokine action
White, M. F., & Marshall, C. J. (1996) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1996.0015 · Cited by 56
Self-citation
TGF-β1 modulates matrix metalloproteinase-13 expression in hepatic stellate cells by complex mechanisms involving p38MAPK, PI3-kinase, AKT, and p70S6k
Lechuga, C. G., Nazará, Z., Rosales, J.-A. D., Morris, E. R., Rincón‐Sánchez, A. R., Rivas, A., Esteban-Gamboa, A., & Rojkind, M. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00264.2003 · Cited by 54
Insulin-like Growth Factor-1 (IGF-1) Receptor-Insulin Receptor Substrate Complexes in the Uterus
Richards, R. G., Walker, M. P., Sebastian, J., & DiAugustine, R. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.19.11962 · Cited by 52
A Synthetic Mechano Growth Factor E Peptide Enhances Myogenic Precursor Cell Transplantation Success
Mills, P., Dominique, J.-C., Lafreniere, J. F., Bouchentouf, M., & Tremblay, J. P. (2007) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2007.01927.x · Cited by 52
p68 Sam is a substrate of the insulin receptor and associates with the SH2 domains of p85 PI3K
Sánchez‐Margalet, V., & Najib, S. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00887-x · Cited by 51
The insulin-elicited 160 kDa phosphotyrosine protein in mouse adipocytes is an insulin receptor substrate 1: Identification by cloning
Keller, S. R., Aebersold, R. H., Garner, C. W., & Lienhard, G. E. (1993) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(93)90222-y · Cited by 51
Inhibition of apoB secretion from HepG2 cells by insulin is amplified by naringenin, independent of the insulin receptor
Allister, E. M., Mulvihill, E. E., Barrett, P. H. R., Edwards, J. Y., Carter, L. P., & Huff, M. W. (2008) · Journal of Lipid Research · doi:10.1194/jlr.m800297-jlr200 · Cited by 49
Enhancement or Inhibition of Insulin Signaling by Insulin Receptor Substrate 1 Is Cell Context Dependent
Yamauchi, K., & Pessin, J. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.7.4427-4434.1994 · Cited by 50
The insulin-induced down-regulation of IRS-1 in 3T3-L1 adipocytes is mediated by a calcium-dependent thiol protease
Smith, L. K., Rice, K. M., & Garner, C. W. (1996) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(96)03875-0 · Cited by 46
p75, a Member of the Heat Shock Protein Family, Undergoes Tyrosine Phosphorylation in Response to Oxidative Stress
Hadari, Y. R., Häring, H. U., & Zick, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.657 · Cited by 46
Interaction of MAD2 with the Carboxyl Terminus of the Insulin Receptor but Not with the IGFIR EVIDENCE FOR RELEASE FROM THE INSULIN RECEPTOR AFTER ACTIVATION
O’Neill, T. J., Zhu, Y., & Gustafson, T. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.10035 · Cited by 44
PI3K is involved in PDGF-β receptor upregulation post-PDGF-BB treatment in mouse HSC
Lechuga, C. G., Nazará, Z., Hernández, E., Bustamante, M., Desierto, G., Cotty, A., Dharker, N., Choe, M., & Rojkind, M. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00058.2005 · Cited by 43
Substitution of the erbB-2 oncoprotein transmembrane domain activates the insulin receptor and modulates the action of insulin and insulin-receptor substrate 1.
Cheatham, B., Shoelson, S. E., Yamada, K. D., Gonçalves, E., & Kahn, C. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7336 · Cited by 44
Self-citation
Multiple Isoforms of the Regulatory Subunit for Phosphatidylinositol 3-Kinase (PI3-Kinase) Are Expressed in Neurons in the Rat Brain
Shin, B., Suzuki, M., Inukai, K., Anai, M., Asano, T., & Takata, K. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8606 · Cited by 42
HDL-Cholesterol and Triglycerides Dynamics: Essential Players in Metabolic Syndrome
Alcover, S., Ramos-Regalado, L., Girón, G., Muñoz‐García, N., & Vilahur, G. (2025) · Antioxidants · doi:10.3390/antiox14040434 · Cited by 50
Insulin-Like Growth Factor-1 Controls Type 2 T Cell-Independent B Cell Response
Baudler, S., Baumgartl, J., Hampel, B., Buch, T., Waisman, A., Snapper, C. M., Krone, W., & Brüning, J. C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.9.5516 · Cited by 39
Effects of pregnancy on insulin receptor in liver, skeletal muscle and adipose tissue of rats
González, C. G., Alonso, A., Balbı́n, M., Dı́az, F., Fernández, S., & Patterson, A. (2002) · Gynecological Endocrinology · doi:10.1080/gye.16.3.193.205 · Cited by 39
Activation of phosphatidylinositol-3-kinase by platelet-derived growth factor and insulin-like growth factor-1 is inhibited by a transmembrane phosphotyrosine phosphatase.
Way, B. A., & Mooney, R. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74329-4 · Cited by 39
The TORC1-activated Proteins, p70S6K and GRB10, Regulate IL-4 Signaling and M2 Macrophage Polarization by Modulating Phosphorylation of Insulin Receptor Substrate-2
Warren, K. J., Fang, X., Gowda, N. M., Thompson, J. J., & Heller, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.756791 · Cited by 38
Zinc as an insulin replacement in hybridoma cultures
Wong, V. V. T., Nissom, P. M., Sim, S., Yeo, J. H. M., Chuah, S. H., & Yap, M. G. S. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20746 · Cited by 38
Understanding the underlying metabolic abnormalities of polycystic ovary syndrome and their implications
Taylor, A. E. (1998) · American Journal of Obstetrics and Gynecology · doi:10.1016/s0002-9378(98)70239-x · Cited by 35
The insulin receptor substrate-1-related 4PS substrate but not the interleukin-2R gamma chain is involved in interleukin-13-mediated signal transduction
Wang, L., Michieli, P., Lie, W., Liu, F., Lee, C., Minty, A. J., Sun, X., Levine, A., White, M. F., & Pierce, J. (1995) · Blood · doi:10.1182/blood.v86.11.4218.bloodjournal86114218 · Cited by 37
Self-citation
Cyclin-Dependent Kinase 4 Regulates Adult Neural Stem Cell Proliferation and Differentiation in Response to Insulin
Chirivella, L., Kirstein, M., Ferrón, S. R., Domingo-Muelas, A., Durupt, F. C., Umanzor, C. A., Cano‐Jaimez, M., Pérez‐Sánchez, F., Barbacid, M., Ortega, S., et al. (2017) · Stem Cells · doi:10.1002/stem.2694 · Cited by 35
Functional Importance of Amino-terminal Domain of Shc for Interaction with Insulin and Epidermal Growth Factor Receptors in Phosphorylation-independent Manner
Sasaoka, T., Ishihara, H., Sawa, T., Ishiki, M., Morioka, H., Imamura, T., Usui, I., Takata, Y., & Kobayashi, M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.20082 · Cited by 36
Insulin Modulates STAT3 Protein Activation and Gene Transcription in Hepatic Cells*
Campos, S. P., Wang, Y., & Baumann, H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24418 · Cited by 39
A Novel PTP1B Inhibitor-Phosphate of Polymannuronic Acid Ameliorates Insulin Resistance by Regulating IRS-1/Akt Signaling
Li, D., Zhang, S., Yang, C. L., Li, Q., Wang, S., Xu, X., Hao, J., & Li, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312693 · Cited by 35
Dose- and time-dependent effects of 17beta-oestradiol on insulin sensitivity in insulin-dependent tissues of rat: implications of IRS-1
González, C., Alonso, A., Diaz, F., & PATTERSON, A. M. (2003) · Journal of Endocrinology · doi:10.1677/joe.0.1760367 · Cited by 34
FAM13A and POM121C are candidate genes for fasting insulin: functional follow-up analysis of a genome-wide association study
Lundbäck, V., Kulyté, A., Strawbridge, R. J., Rydén, M., Arner, P., Marcus, C., & Dahlman, I. A. (2018) · Diabetologia · doi:10.1007/s00125-018-4572-8 · Cited by 34
Paradoxical effects of overexpression of the type I insulin-like growth factor (IGF) receptor on the responsiveness of human breast cancer cells to IGFs and estradiol
Daws, M. R., Westley, B. R., & May, F. E. B. (1996) · Endocrinology · doi:10.1210/en.137.4.1177 · Cited by 33
Inhibition of Tumor Necrosis Factor Signal Transduction in Endothelial Cells by Dimethylaminopurine
Marino, M. W., Dunbar, J. D., Wu, L., Ngaiza, J. R., Han, H.-M., Guo, D., Matsushita, M., Nairn, A. C., Zhang, Y., Kolesnick, R., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28624 · Cited by 32
Association of Insulin-Like Growth Factor-1 Receptor Polymorphism in Dementia
Garcia, J., Ahmadi, A., Wonnacott, A., Sutcliffe, W., Nägga, K., Söderkvist, P., & Marcusson, J. O. (2006) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000095803 · Cited by 32
Differential response to caloric restriction of retroperitoneal, epididymal, and subcutaneous adipose tissue depots in rats
Narita, T., Kobayashi, M., Itakura, K., Itagawa, R., Kabaya, R., Sudo, Y., Okita, N., & Higami, Y. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.01.016 · Cited by 33
The insulin receptor and type I IGF receptor: Comparison of structure and function
Siddle, K. (1992) · Progress in Growth Factor Research · doi:10.1016/0955-2235(92)90013-8 · Cited by 31
Involvement of Raf-1 kinase and protein kinase C zeta in insulin-like growth factor I-induced brown adipocyte mitogenic signaling cascades: inhibition by cyclic adenosine 3',5'-monophosphate
Valverde, Á. M., Teruel, T., Lorenzo, M., & Benito, M. (1996) · Endocrinology · doi:10.1210/en.137.9.3832 · Cited by 31
Aβ-Induced Insulin Resistance and the Effects of Insulin on the Cholesterol Synthesis Pathway and Aβ Secretion in Neural Cells
Najem, D., Bamji‐Mirza, M., Yang, Z., & Zhang, W. (2016) · Neuroscience Bulletin · doi:10.1007/s12264-016-0034-9 · Cited by 32
LMW-PTP Exerts a Differential Regulation on PDGF- and Insulin-Mediated Signaling
Taddei, L., Chiarugi, P., Cirri, P., Talini, D., Camici, G., Manao, G., Raugei, G., & Ramponi, G. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2456 · Cited by 30
Hormonal regulation of the Grb14 signal modulator and its role in cell cycle progression of MCF‐7 human breast cancer cells
Kairouz, R., Parmar, J., Lyons, R. J., Swarbrick, A., Musgrove, E. A., & Daly, R. J. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20199 · Cited by 30
Phosphatidylinositol 3-Kinase (PI3K) Activity Bound to Insulin-like Growth Factor-I (IGF-I) Receptor, which Is Continuously Sustained by IGF-I Stimulation, Is Required for IGF-I-induced Cell Proliferation
Fukushima, T., Nakamura, Y., Yamanaka, D., Shibano, T., Chida, K., Minami, S., Asano, T., Hakuno, F., & Takahashi, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.393074 · Cited by 29
Bitter Melon Extract Promotes Granulation Tissue Growth and Angiogenesis in the Diabetic Wound
Singh, R., García‐Gómez, I., Gudehithlu, K. P., & Singh, A. K. (2016) · Advances in Skin & Wound Care · doi:10.1097/01.asw.0000504758.86737.76 · Cited by 28
Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and complete sequence of mouse IRS-1
Araki, E., Haag, B. L., & Kahn, C. R. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(94)90261-5 · Cited by 27
Self-citation
Lessons from Immunological, Biochemical, and Molecular Pathways of the Activation Mediated by IL-2 and IL-4
Rebollo, A., Gómez, J., & Martínez‐A, C. (1996) · Advances in immunology · doi:10.1016/s0065-2776(08)60856-1 · Cited by 28
Magnesium Deficiency Modulates the Insulin Signaling Pathway in Liver but Not Muscle of Rats
Reis, M. A. B., Reyes, F. G. R., Saad, M. J. A., & Velloso, L. A. (2000) · The Journal of Nutrition · doi:10.1093/jn/130.2.133 · Cited by 28
C1qTNF-related protein 1 improve insulin resistance by reducing phosphorylation of serine 1101 in insulin receptor substrate 1
Xin, Y., Zhang, D., Fu, Y., Wang, C., Li, Q., Tian, C., Suhe, Z., & Lyu, X. (2017) · Endocrine Journal · doi:10.1507/endocrj.ej17-0128 · Cited by 28
Hypoglycemic mechanism of a novel proteoglycan, extracted from Ganoderma lucidum , in hepatocytes
Yang, Z., Chen, C., Zhao, J., Xu, W., He, Y., Yang, H., & Zhou, P. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.12.020 · Cited by 30
Insulin receptor/IRS-1/PI 3-kinase signaling system in corticosteroid-induced insulin resistance
Folli, F. B., Saad, M. J. A., & Kahn, C. R. (1996) · Acta Diabetologica · doi:10.1007/bf02048541 · Cited by 28
Self-citation
Identification of a Novel Invasion-Promoting Region in Insulin Receptor Substrate 2
Mercado-Matos, J., Janusis, J., Zhu, S., Chen, S. S., & Shaw, L. M. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00590-17 · Cited by 27
Upregulation of miR-497 induces hepatic insulin resistance in E3 rats with HFD-MetS by targeting insulin receptor
Wang, X., Wang, M., Li, H., Lan, X., Liu, L., Li, J., Li, Y., Li, J., Yi, J., Du, X., et al. (2015) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2015.08.021 · Cited by 28
In Vitro Binding and Phosphorylation of Insulin Receptor Substrate 1 by the Insulin Receptor
Backer, J., Wjasow, C., & Zhang, Y. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00091.x · Cited by 29
Self-citation
Insulin Receptor Substrate 1 Rescues Insulin Action in CHO Cells Expressing Mutant Insulin Receptors That Lack a Juxtamembrane NPXY Motif
Chen, D., Horn, D. J. V., White, M. F., & Backer, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.9.4711 · Cited by 28
Self-citation
Insulin-dependent phosphorylation of calmodulin in rat hepatocytes.
Joyal, J. L., & Sacks, D. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43985-3 · Cited by 27
Insulin Receptor Substrate-1 Is Present in Hepatocyte Nuclei from Intact Rats
Boylan, J. M., & Gruppuso, P. A. (2002) · Endocrinology · doi:10.1210/en.2002-220321 · Cited by 25
Alpha-linolenic acid modulates systemic and adipose tissue-specific insulin sensitivity, inflammation, and the endocannabinoid system in dairy cows
Kra, G., Daddam, J. R., Moallem, U., Kamer, H., Mualem, B., Levin, Y., Kočvarová, R., Nemirovski, A., Contreras, A. G., Tam, J., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-32433-7 · Cited by 26

Authors: Sun, X. J., Miralpeix, M., Myers, M. G., Glasheen, E. M., Backer, J. M., Kahn, C. R., & White, M. F.
Affiliations: Joslin Diabetes Center (US)
ORCID: Sun, X.J.
Myers, M G
Backer, J.M.
Kahn, C.R.
White, M.F.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-11
Volume: 267
Issue: 31
Pages: 22662-22672
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)41723-1
OpenAlex: W1524336750
Cited by: 326
References: 42
Citations by year: 2025: 2 · 2024: 1 · 2023: 2 · 2022: 2 · 2021: 4 · 2020: 3 · 2019: 5 · 2018: 8 · 2017: 8 · 2016: 9 · 2015: 4 · 2014: 5 · 2013: 4 · 2012: 11
FWCI: 12.17
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10204 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (DK 33201, DK36836, DK 43808, R01DK033201, R01DK043808, P30DK036836)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: IRS-1, insulin signaling, insulin receptor, tyrosine phosphorylation, serine phosphorylation, phosphatidylinositol 3-kinase, subcellular localization, CHO cell expression
MeSH terms: Amino Acid Sequence, Animals, Cytoplasm, DNA, Cricetinae, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Phosphotransferases, Protein-Tyrosine Kinases, Receptor, Insulin, Recombinant Proteins, RNA, Messenger, Tyrosine, Signal Transduction, Gene Expression, CHO Cells, Phosphotyrosine, Phosphatidylinositol 3-Kinases, Rats, Insulin Receptor Substrate Proteins

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

Expression and function of IRS-1 in insulin signal transmission.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks