Role of IRS-2 in insulin and cytokine signalling

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

Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene

Araki, E., Lipes, M. A., Patti, M.-E., Brüning, J. C., Haag III, B., Johnson, R. S., & Kahn, C. R. (1994) · Nature · doi:10.1038/372186a0 · Cited by 1,252

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

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 · Cited by 326

Critical nodes in signalling pathways: insights into insulin action

Taniguchi, C. M., Emanuelli, B., & Kahn, C. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1837 · Cited by 2,760

IRS-1-Mediated Inhibition of Insulin Receptor Tyrosine Kinase Activity in TNF-α- and Obesity-Induced Insulin Resistance

Hotamisligil, G. S., Peraldi, P., Budavari, A., Ellis, R., White, M. F., & Spiegelman, B. M. (1996) · Science · doi:10.1126/science.271.5249.665 · Cited by 2,630

Essential role of Stat6 in IL-4 signalling

Takeda, K., Tanaka, T., Shi, W., Matsumoto, M., Minami, M., Kashiwamura, S.-I., Nakanishi, K., Yoshida, N., Kishimoto, T., & Akira, S. (1996) · Nature · doi:10.1038/380627a0 · Cited by 1,557

The IL-4 receptor: signaling mechanisms and biologic functions

Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.701 · Cited by 1,545

The c-Jun NH2-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser307

Aguirre, V., Uchida, T., Yenush, L., Davis, R., & White, M. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.9047 · Cited by 1,487

Phosphorylation of Ser307 in Insulin Receptor Substrate-1 Blocks Interactions with the Insulin Receptor and Inhibits Insulin Action

Aguirre, V., Werner, E. D., Giraud, J., Lee, Y. H., Shoelson, S. E., & White, M. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m101521200 · Cited by 1,010

Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling

SHEPHERD, P. R., WITHERS, D. J., & SIDDLE, K. (1998) · Biochemical Journal · doi:10.1042/bj3330471 · Cited by 953

Protein–protein interaction in insulin signaling and the molecular mechanisms of insulin resistance

Virkamäki, A., Ueki, K., & Kahn, C. R. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6609 · Cited by 854

Molecular biology of the 3β-hydroxysteroid dehydrogenase/Δ5-Δ4 –isomerase gene family

Simard, J., Ricketts, M.-L., Gingras, S., Soucy, P., Feltus, F. A., & Melner, M. H. (2005) · Endocrine Reviews · doi:10.1210/er.2002-0050 · Cited by 620

Characterization of selective resistance to insulin signaling in the vasculature of obese Zucker (fa/fa) rats

Jiang, Z. Y., Lin, Y.-W., Clemont, A., Feener, E. P., Hein, K. D., Igarashi, M., Yamauchi, T., White, M. F., & King, G. L. (1999) · Journal of Clinical Investigation · doi:10.1172/jci5971 · Cited by 604

-Amyloid Oligomers Induce Phosphorylation of Tau and Inactivation of Insulin Receptor Substrate via c-Jun N-Terminal Kinase Signaling: Suppression by Omega-3 Fatty Acids and Curcumin

Ma, Q.-L., Yang, F., Rosario, E. R., Ubeda, O. J., Beech, W., Gant, D. J., Chen, P. P., Hudspeth, B., Chen, C., Zhao, Y., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1071-09.2009 · Cited by 536

Insulin Receptor Substrate-2 Deficiency Impairs Brain Growth and Promotes Tau Phosphorylation

Schubert, M., Brazil, D. P., Burks, D. J., Kushner, J. A., Ye, J., Flint, C. L., Farhang-Fallah, J., Dikkes, P., Warot, X. M., Rio, C., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-18-07084.2003 · Cited by 488

Current views on type 2 diabetes

Lin, Y., & Sun, Z. (2010) · Journal of Endocrinology · doi:10.1677/joe-09-0260 · Cited by 457

Insulin signaling in health and disease

Saltiel, A. R. (2021) · Journal of Clinical Investigation · doi:10.1172/jci142241 · Cited by 446

Tumor Necrosis Factor (TNF)-α Inhibits Insulin Signaling through Stimulation of the p55 TNF Receptor and Activation of Sphingomyelinase

Peraldi, P., Hotamisligil, G. S., Buurman, W. A., White, M. F., & Spiegelman, B. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13018 · Cited by 412

Increased insulin sensitivity and hypoglycaemia in mice lacking the p85α subunit of phosphoinositide 3–kinase

Terauchi, Y., Tsuji, Y., Satoh, S., Minoura, H., Murakami, K., Okuno, A., Inukai, K., Asano, T., Kaburagi, Y., Ueki, K., et al. (1999) · Nature Genetics · doi:10.1038/6023 · Cited by 399

Disruption of neural signal transducer and activator of transcription 3 causes obesity, diabetes, infertility, and thermal dysregulation

Gao, Q., Wolfgang, M. J., Neschen, S., Morino, K., Horvath, T. L., Shulman, G. I., & Fu, X.-Y. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0303992101 · Cited by 385

Regulation of inflammation by interleukin-4: a review of "alternatives"

Luzina, I. G., Keegan, A. D., Heller, N. M., Rook, G. A. W., Shea-Donohue, T., & Atamas, S. P. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0412214 · Cited by 351

Stat6 Is Necessary and Sufficient for IL-4’s Role in Th2 Differentiation and Cell Expansion

Zhu, J., Guo, L., Watson, C. J., Hu-Li, J., & Paul, W. E. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7276 · Cited by 301

Contrasting Effects of IRS-1 Versus IRS-2 Gene Disruption on Carbohydrate and Lipid Metabolism in Vivo

Previs, S. F., Withers, D. J., Ren, J.-M., White, M. F., & Shulman, G. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006490200 · Cited by 291

Hepatic Selective Insulin Resistance at the Intersection of Insulin Signaling and Metabolic Dysfunction-Associated Steatotic Liver Disease

Bo, T., Gao, L., Yao, Z., Shao, S., Wang, X., Proud, C. G., & Zhao, J. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.04.006 · Cited by 293

Adiponectin Enhances Insulin Sensitivity by Increasing Hepatic IRS-2 Expression via a Macrophage-Derived IL-6-Dependent Pathway

Awazawa, M., Ueki, K., Inabe, K., Yamauchi, T., Kubota, N., Kaneko, K., Kobayashi, M., Iwane, A., Sasako, T., Okazaki, Y., et al. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.02.010 · Cited by 277

Untitled work

(2006) · doi:10.1016/j.tem.2006.01.005 · Cited by 256

Signaling pathways in Th2 development

Mowen, K. A., & Glimcher, L. H. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00209.x · Cited by 255

PDK1, one of the missing links in insulin signal transduction?1

Cohen, P., Alessi, D. R., & Cross, D. A. E. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00490-0 · Cited by 246

Regional differences of insulin action in adipose tissue: insights from in vivo and in vitro studies

Giorgino, F., Laviola, L., & Eriksson, J. W. (2005) · Acta Physiologica Scandinavica · doi:10.1111/j.1365-201x.2004.01385.x · Cited by 230

Insulin action and insulin resistance: diseases involving defects in insulin receptors, signal transduction, and the glucose transport effector system

Hunter, S. J., & Garvey, W. T. (1998) · The American Journal of Medicine · doi:10.1016/s0002-9343(98)00300-3 · Cited by 200

Expression and function of the insulin receptor substrate proteins in cancer

Mardilovich, K., Pankratz, S. L., & Shaw, L. M. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-14 · Cited by 192

Selective impairment of insulin signalling in the hypothalamus of obese Zucker rats

Carvalheira, J. B. C., Ribeiro, E. B., Ara�jo, E. P., Guimar�es, R. B., Telles, M. M., Torsoni, M., Gontijo, J. A. R., Velloso, L. A., & Saad, M. J. A. (2003) · Diabetologia · doi:10.1007/s00125-003-1246-x · Cited by 176

The COOH-terminal Tyrosine Phosphorylation Sites on IRS-1 Bind SHP-2 and Negatively Regulate Insulin Signaling

Myers, M. G., Mendez, R., Shi, P., Pierce, J. H., Rhoads, R., & White, M. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26908 · Cited by 164

The Croonian Lecture 1998. Identification of a protein kinase cascade of major importance in insulin signal transduction

Cohen, P. (1999) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.1999.0399 · Cited by 158

Exercise counteracts the effects of short-term overfeeding and reduced physical activity independent of energy imbalance in healthy young men

Walhin, J., Richardson, J. D., Betts, J. A., & Thompson, D. (2013) · The Journal of Physiology · doi:10.1113/jphysiol.2013.262709 · Cited by 129

Insulin receptor substrate signaling suppresses neonatal autophagy in the heart

Riehle, C., Wende, A. R., Sena, S., Pires, K. M., Pereira, R. O., Zhu, Y., Bugger, H., Frank, D., Bevins, J., Chen, D., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci71171 · Cited by 114

Expression of antioxidant enzymes in rat lungs after inhalation of asbestos or silica.

Janssen, Y. M., Marsh, J. P., Absher, M. P., Hemenway, D., Vacek, P. M., Leslie, K. O., Borm, P. J., & Mossman, B. T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50063-1 · Cited by 113

Differential activation of insulin receptor substrates 1 and 2 by insulin-like growth factor-activated insulin receptors

Denley, A., Carroll, J. M., Brierley, G. V., Cosgrove, L., Wallace, J., Forbes, B., & Roberts, C. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01447-06 · Cited by 103

Specific Increase in p85α Expression in Response to Dexamethasone Is Associated with Inhibition of Insulin-like Growth Factor-I Stimulated Phosphatidylinositol 3-Kinase Activity in Cultured Muscle Cells

Giorgino, F., Pedrini, M. T., Matera, L., & Smith, R. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7455 · Cited by 80

Skeletal muscle and insulin sensitivity: pathophysiological alterations

Ryder, J. (2001) · Frontiers in bioscience · doi:10.2741/ryder · Cited by 73

Insulin Regulation of Hepatic Lipid Homeostasis

Uehara, K., Santoleri, D., Whitlock, A. E. G., & Titchenell, P. M. (2023) · Comprehensive Physiology · doi:10.1002/cphy.c220015 · Cited by 49

FSH stimulates IRS-2 expression in human granulosa cells through cAMP/SP1, an inoperative FSH action in PCOS patients

Anjali, G., Kaur, S., Lakra, R., Taneja, J., Kalsey, G. S., Nagendra, A., Shrivastav, T. G., Gouri Devi, M., Malhotra, N., Kriplani, A., et al. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.09.011 · Cited by 42

B Cell Receptor (BCR) Cross-Talk: IL-4 Creates an Alternate Pathway for BCR-Induced ERK Activation That Is Phosphatidylinositol 3-Kinase Independent

Guo, B., & Rothstein, T. L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.9.5375 · Cited by 31

Regulation of Insulin Receptor Substrate-2 Tyrosine Phosphorylation in Animal Models of Insulin Resistance

Rojas, F. A., Hirata, A. E., & Saad, M. J. A. (2003) · Endocrine · doi:10.1385/endo:21:2:115 · Cited by 30

Dockers at the crossroads

Guy, G. R., Yusoff, P., Bangarusamy, D., Fong, C. W., & Wong, E. S. M. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00227-3 · Cited by 20

Physiological and pathophysiological actions of insulin in the liver

Kubota, N., Kubota, T., & Kadowaki, T. (2025) · Endocrine Journal · doi:10.1507/endocrj.ej24-0192 · Cited by 19

Paradoxical dominant negative activity of an immunodeficiency-associated activating PIK3R1 variant

Tomlinson, P. R., Knox, R. G., Perisic, O., Su, H., Brierley, G. V., Williams, R. L., & Semple, R. K. (2025) · eLife · doi:10.7554/elife.94420.3 · Cited by 2

Untitled work

(2000) · doi:10.1002/1520-7560(2000)9999:9999<::aid-dmrr141>3.0.co;2-x